6MSD | pdb_00006msd

Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
S [auth u]SCOP2B SuperfamilyUbiquitin-like 8101457 3000157 SCOP2B (2022-06-29)
T [auth w]SCOP2B SuperfamilyUbiquitin-like 8101457 3000157 SCOP2B (2022-06-29)
JA [auth h]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064014 3000131 SCOP2B (2022-06-29)
V [auth H]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064014 3000131 SCOP2B (2022-06-29)
KA [auth i]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064036 3000131 SCOP2B (2022-06-29)
W [auth I]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064036 3000131 SCOP2B (2022-06-29)
LA [auth j]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064004 3000131 SCOP2B (2022-06-29)
X [auth J]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064004 3000131 SCOP2B (2022-06-29)
MA [auth k]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064022 3000131 SCOP2B (2022-06-29)
Y [auth K]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064022 3000131 SCOP2B (2022-06-29)
Z [auth L]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064060 3000131 SCOP2B (2022-06-29)
NA [auth l]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064060 3000131 SCOP2B (2022-06-29)
OA [auth m]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064054 3000131 SCOP2B (2022-06-29)
AA [auth M]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064054 3000131 SCOP2B (2022-06-29)
BA [auth N]SCOP2B SuperfamilyClass II glutamine amidotransferases 8079175 3000131 SCOP2B (2022-06-29)
PA [auth n]SCOP2B SuperfamilyClass II glutamine amidotransferases 8079175 3000131 SCOP2B (2022-06-29)
CA [auth O]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064074 3000131 SCOP2B (2022-06-29)
QA [auth o]SCOP2B SuperfamilyClass II glutamine amidotransferases 8064074 3000131 SCOP2B (2022-06-29)
FA [auth R]SCOP2B SuperfamilyClass II glutamine amidotransferases 8079492 3000131 SCOP2B (2022-06-29)
TA [auth r]SCOP2B SuperfamilyClass II glutamine amidotransferases 8079492 3000131 SCOP2B (2022-06-29)
D [auth X]SCOP2B SuperfamilyWinged helix DNA-binding domain 8067905 3000034 SCOP2B (2022-06-29)
E [auth Y]SCOP2B SuperfamilyTPR-like 8057045 3001345 SCOP2B (2022-06-29)
E [auth Y]SCOP2B SuperfamilyWinged helix DNA-binding domain 8057047 3000034 SCOP2B (2022-06-29)
F [auth Z]SCOP2B SuperfamilyEIF3 subunit F C-terminal domain-like 8053251 3002167 SCOP2B (2022-06-29)
F [auth Z]SCOP2B SuperfamilyJAB1/MPN domain-like 8053252 3001105 SCOP2B (2022-06-29)
I [auth c]SCOP2B SuperfamilyEIF3 subunit F C-terminal domain-like 8053254 3002167 SCOP2B (2022-06-29)
I [auth c]SCOP2B SuperfamilyJAB1/MPN domain-like 8053255 3001105 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth U]KOG2062_2nde6msdU3 A: beta sandwichesX: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)H: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 C-terminal domainF: KOG2062_2ndECOD (1.6)
A [auth U]KOG2062_1ste6msdU1 A: alpha superhelicesX: Repetitive alpha hairpinsH: 26S proteasome subunit Rpn2 N-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 N-terminal domainF: KOG2062_1stECOD (1.6)
A [auth U]HEAT_2_3e6msdU2 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: HEAT_2_3ECOD (1.6)
J [auth d]CSN8_PSD8_EIF3K_C_2e6msdd2 A: alpha arraysX: HTHH: HTHT: wingedF: CSN8_PSD8_EIF3K_C_2ECOD (1.6)
J [auth d]SAC3_GANP_1ste6msdd1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: SAC3_GANP_1stECOD (1.6)
L [auth f]KOG2005_1ste6msdf3 A: alpha superhelicesX: Repetitive alpha hairpinsH: 26S proteasome subunit Rpn2 N-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 N-terminal domainF: KOG2005_1stECOD (1.6)
L [auth f]KOG1858_2nde6msdf1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: KOG1858_2ndECOD (1.6)
M [auth A]PRK03992e6msdA1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PRK03992ECOD (1.6)
M [auth A]Sigma54_activate6msdA2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: Sigma54_activatECOD (1.6)
P [auth D]26Sp45e6msdD2 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: 26Sp45ECOD (1.6)
P [auth D]PRK03992e6msdD1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PRK03992ECOD (1.6)
P [auth D]Sigma54_activate6msdD3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: Sigma54_activatECOD (1.6)
Q [auth E]26Sp45e6msdE1 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: 26Sp45ECOD (1.6)
Q [auth E]KOG0652_2nde6msdE2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: KOG0652_2ndECOD (1.6)
Q [auth E]Sigma54_activate6msdE3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: Sigma54_activatECOD (1.6)
S [auth u]ubiquitin_1e6msdu1 A: a+b two layersX: beta-GraspH: Ubiquitin-relatedT: Ubiquitin-likeF: ubiquitin_1ECOD (1.6)
T [auth w]ubiquitin_1e6msdw1 A: a+b two layersX: beta-GraspH: Ubiquitin-relatedT: Ubiquitin-likeF: ubiquitin_1ECOD (1.6)
B [auth V]PCIe6msdV3 A: alpha arraysX: HTHH: HTHT: wingedF: PCIECOD (1.6)
B [auth V]KOG2581e6msdV1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: KOG2581ECOD (1.6)
B [auth V]Rpn3_Ce6msdV2 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN3 C-terminal helixF: Rpn3_CECOD (1.6)
IA [auth g]Proteasomee6msdg1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
U [auth G]Proteasomee6msdG1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
JA [auth h]Proteasomee6msdh1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
V [auth H]Proteasomee6msdH1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
KA [auth i]Proteasomee6msdi1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
W [auth I]Proteasomee6msdI1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
LA [auth j]Proteasomee6msdj1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
X [auth J]Proteasomee6msdJ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
MA [auth k]Proteasomee6msdk1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
Y [auth K]Proteasomee6msdK1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
Z [auth L]Proteasomee6msdL1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
NA [auth l]Proteasomee6msdl1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
OA [auth m]Proteasomee6msdm1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
AA [auth M]Proteasomee6msdM1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
BA [auth N]Proteasomee6msdN1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
PA [auth n]Proteasomee6msdn1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
CA [auth O]Proteasomee6msdO1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
QA [auth o]Proteasomee6msdo1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
DA [auth P]Proteasomee6msdP1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
RA [auth p]Proteasomee6msdp1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
C [auth W]PCIe6msdW3 A: alpha arraysX: HTHH: HTHT: wingedF: PCIECOD (1.6)
C [auth W]RPN7_1e6msdW2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: RPN7_1ECOD (1.6)
C [auth W]KOG1498e6msdW1 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN5 C-terminal helixF: KOG1498ECOD (1.6)
EA [auth Q]Proteasomee6msdQ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
SA [auth q]Proteasomee6msdq1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
FA [auth R]Proteasomee6msdR1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
TA [auth r]Proteasomee6msdr1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
UA [auth s]Proteasomee6msds1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
GA [auth S]Proteasomee6msdS1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
VA [auth t]Proteasomee6msdt1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
HA [auth T]Proteasomee6msdT1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
D [auth X]PCIe6msdX3 A: alpha arraysX: HTHH: HTHT: wingedF: PCIECOD (1.6)
D [auth X]KOG1463e6msdX1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: KOG1463ECOD (1.6)
D [auth X]RPN6_likee6msdX2 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN6 C-termial helix (From Topology)T: 26S proteasome regulatory subunit RPN6 C-termial helixF: RPN6_likeECOD (1.6)
E [auth Y]PCI_1e6msdY1 A: alpha arraysX: HTHH: HTHT: wingedF: PCI_1ECOD (1.6)
E [auth Y]RPN7e6msdY2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: RPN7ECOD (1.6)
E [auth Y]KOG0687e6msdY3 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN7 C-terminal helixF: KOG0687ECOD (1.6)
F [auth Z]JABe6msdZ1 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: JABECOD (1.6)
F [auth Z]MitMem_rege6msdZ2 A: extended segmentsX: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domainF: MitMem_regECOD (1.6)
G [auth a]PCI_1e6msda3 A: alpha arraysX: HTHH: HTHT: wingedF: PCI_1ECOD (1.6)
G [auth a]KOG2908_Ne6msda2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: KOG2908_NECOD (1.6)
G [auth a]KOG2908_Ce6msda1 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN9 C-terminal helixF: KOG2908_CECOD (1.6)
H [auth b]VWAe6msdb1 A: a/b three-layered sandwichesX: HAD domain-likeH: HAD domain-relatedT: vWA-likeF: VWAECOD (1.6)
I [auth c]JABe6msdc2 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: JABECOD (1.6)
I [auth c]EUF08560e6msdc1 A: extended segmentsX: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domainF: EUF08560ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth U]PF13646HEAT repeats (HEAT_2)HEAT repeats- Repeat
A [auth U]PF1800426S proteasome regulatory subunit RPN2 C-terminal domain (RPN2_C)26S proteasome regulatory subunit RPN2 C-terminal domainThis is the C-terminal domain found in S. cerevisiae Rpn2 (26S proteasome regulatory subunit RPN2) as well as other eukaryotic species. A study revealed that the C-terminal 52 residues of the Rpn2 C-terminal domain are responsible for mediating inter ...This is the C-terminal domain found in S. cerevisiae Rpn2 (26S proteasome regulatory subunit RPN2) as well as other eukaryotic species. A study revealed that the C-terminal 52 residues of the Rpn2 C-terminal domain are responsible for mediating interactions with the ubiquitin-binding subunit Rpn13. Futhermore, the extreme C-terminal 20 or 21 residues of Rpn2 (926-945 or 925-945) of S. cerevisiae, were shown to be equally effective at binding Rpn13. Multiple sequence alignments indicate that Rpn2 orthologs are highly conserved in this C-terminal region and share characteristic acidic, aromatic, and proline residues, suggesting a common function. In the structure of Rpn2 from S. cerevisiae , this region is exposed and disordered, and is thus accessible for associating with Rpn13. The Rpn2 binding surface of human Rpn13 has been mapped by nuclear magnetic resonance titration to one surface of its Pru domain [1].
Domain
A [auth U]PF00240Ubiquitin family (ubiquitin)Ubiquitin familyThis family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry ...This family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites [5].
Domain
A [auth U]PF01851Proteasome/cyclosome repeat (PC_rep)Proteasome/cyclosome repeat- Repeat
M [auth A]PF22037PSD13 N-terminal repeats (PSD13_N)PSD13 N-terminal repeats- Repeat
M [auth A]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. Domain
M [auth A]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1]. Domain
M [auth A]PF2123626S proteasome regulatory subunit 7, OB domain (PRS7_OB)26S proteasome regulatory subunit 7, OB domainThis is the OB domain from 26S proteasome regulatory subunit 7 (PRS7, also known as PSMC2, Rpt1 or MSS1), a component of the 19S proteasome cap [1-5]. These are one of six ATPases of the regulatory particle that form a heterohexameric ring. This doma ...This is the OB domain from 26S proteasome regulatory subunit 7 (PRS7, also known as PSMC2, Rpt1 or MSS1), a component of the 19S proteasome cap [1-5]. These are one of six ATPases of the regulatory particle that form a heterohexameric ring. This domain mediates interactions with USP14 or Ubp6 [2,4].
Domain
M [auth A]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. Domain
N [auth B]PF13519von Willebrand factor type A domain (VWA_2)von Willebrand factor type A domainDomain
N [auth B]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] Domain
N [auth B]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. Domain
N [auth B]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. Domain
O [auth C]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] Domain
O [auth C]PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin proteaseProteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or J ...Proteins with this domain are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This domain is known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or JAMM domain [7]. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes [7]. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archaeal protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [8,9].
Domain
O [auth C]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. Domain
O [auth C]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. Domain
P [auth D]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] Domain
P [auth D]PF10075CSN8/PSMD8/EIF3K family (CSN8_PSD8_EIF3K)CSN8/PSMD8/EIF3K family- Family
P [auth D]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. Domain
P [auth D]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. Domain
Q [auth E]PF05160DSS1/SEM1 family (DSS1_SEM1)DSS1/SEM1 family- Family
Q [auth E]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] Domain
Q [auth E]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. Domain
Q [auth E]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. Domain
R [auth F]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] Domain
R [auth F]PF17781RPN1 N-terminal domain (RPN1_RPN2_N)RPN1 N-terminal domain- Repeat
R [auth F]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. Domain
R [auth F]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. Domain
B [auth V]PF08375Proteasome regulatory subunit C-terminal (Rpn3_C)Proteasome regulatory subunit C-terminal- Family
B [auth V]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1]. Domain
IA [auth g],
U [auth G]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
IA [auth g],
U [auth G]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
JA [auth h],
V [auth H]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
JA [auth h],
V [auth H]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
KA [auth i],
W [auth I]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
KA [auth i],
W [auth I]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
LA [auth j],
X [auth J]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
LA [auth j],
X [auth J]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
MA [auth k],
Y [auth K]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
MA [auth k],
Y [auth K]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
NA [auth l],
Z [auth L]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
NA [auth l],
Z [auth L]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
AA [auth M],
OA [auth m]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
AA [auth M],
OA [auth m]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
CA [auth O],
QA [auth o]
PF12465Proteasome beta subunits C terminal (Pr_beta_C)Proteasome beta subunits C terminal- Family
DA [auth P],
RA [auth p]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
C [auth W]PF1809826S proteasome regulatory subunit RPN5 C-terminal domain (RPN5_C)26S proteasome regulatory subunit RPN5 C-terminal domainThis is the C-terminal domain of the 26S proteasome regulatory subunit RPN5 proteins.This helical domain can be found adjacent to Pfam:PF01399. The 26S proteasome is the major ATP-dependent protease in eukaryotes. Three subcomplexes form this degrada ...This is the C-terminal domain of the 26S proteasome regulatory subunit RPN5 proteins.This helical domain can be found adjacent to Pfam:PF01399. The 26S proteasome is the major ATP-dependent protease in eukaryotes. Three subcomplexes form this degradation machine: the lid, the base, and the core. The helices found at the C terminus of each lid subunit form a helical bundle that directs the ordered self-assembly of the lid subcomplex. This domain which comprises the tail of RPN5 along with the tail of Rpn9, are important for Rpn12 binding to the lid [1].
Domain
C [auth W]PF22241PSMD12/CSN4, N-terminal (PSMD12-CSN4_N)PSMD12/CSN4, N-terminal- Repeat
C [auth W]PF00240Ubiquitin family (ubiquitin)Ubiquitin familyThis family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry ...This family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites [5].
Domain
C [auth W]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1]. Domain
EA [auth Q],
SA [auth q]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
GA [auth S],
UA [auth s]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
HA [auth T],
VA [auth t]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
D [auth X]PF1850326S proteasome subunit RPN6 C-terminal helix domain (RPN6_C_helix)26S proteasome subunit RPN6 C-terminal helix domainThis is the C-terminal helix domain found in RPN6, a component of the 26S proteasome. The C-terminal helices are essential for lid assembly [1, 2]. Domain
D [auth X]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1]. Domain
E [auth Y]PF2115426S proteasome regulatory subunit RPN7/PSMD6 C-terminal helix (RPN7_PSMD6_C)26S proteasome regulatory subunit RPN7/PSMD6 C-terminal helixRPN7/PSDM6 are regulatory subunits from the 26S proteasome. This entry represents the C-terminal helix. Domain
E [auth Y]PF1060226S proteasome subunit RPN7 (RPN7)26S proteasome subunit RPN7- Repeat
E [auth Y]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1]. Domain
F [auth Z]PF13012Maintenance of mitochondrial structure and function (MitMem_reg)Maintenance of mitochondrial structure and function- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth U]26S proteasome non-ATPase regulatory subunit 1
J [auth d]26S proteasome non-ATPase regulatory subunit 8-
K [auth e]26S proteasome complex subunit SEM1-
L [auth f]26S proteasome non-ATPase regulatory subunit 2
M [auth A]26S proteasome regulatory subunit 7
N [auth B]26S proteasome regulatory subunit 4
O [auth C]26S proteasome regulatory subunit 8
P [auth D]26S proteasome regulatory subunit 6B
Q [auth E]26S proteasome regulatory subunit 10B
R [auth F]26S proteasome regulatory subunit 6A
S [auth u],
T [auth w]
Ubiquitin
B [auth V]26S proteasome non-ATPase regulatory subunit 3
IA [auth g],
U [auth G]
Proteasome subunit alpha type-6
JA [auth h],
V [auth H]
Proteasome subunit alpha type-2-
KA [auth i],
W [auth I]
Proteasome subunit alpha type-4-
LA [auth j],
X [auth J]
Proteasome subunit alpha type-7
MA [auth k],
Y [auth K]
Proteasome subunit alpha type-5-
NA [auth l],
Z [auth L]
Proteasome subunit alpha type-1
AA [auth M],
OA [auth m]
Proteasome subunit alpha type-3
BA [auth N],
PA [auth n]
Proteasome subunit beta type-6
CA [auth O],
QA [auth o]
Proteasome subunit beta type-7
DA [auth P],
RA [auth p]
Proteasome subunit beta type-3-
C [auth W]26S proteasome non-ATPase regulatory subunit 12-
EA [auth Q],
SA [auth q]
Proteasome subunit beta type-2-
FA [auth R],
TA [auth r]
Proteasome subunit beta type-5
GA [auth S],
UA [auth s]
Proteasome subunit beta type-1-
HA [auth T],
VA [auth t]
Proteasome subunit beta type-4
D [auth X]26S proteasome non-ATPase regulatory subunit 11
E [auth Y]26S proteasome non-ATPase regulatory subunit 6-
F [auth Z]26S proteasome non-ATPase regulatory subunit 7
G [auth a]26S proteasome non-ATPase regulatory subunit 13
H [auth b]26S proteasome non-ATPase regulatory subunit 4
I [auth c]26S proteasome non-ATPase regulatory subunit 14

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A [auth U]IPR04062326S proteasome regulatory subunit RPN2, C-terminalDomain
A [auth U]IPR016024Armadillo-type foldHomologous Superfamily
A [auth U]IPR002015Proteasome/cyclosome repeatRepeat
A [auth U]IPR011989Armadillo-like helicalHomologous Superfamily
A [auth U]IPR04857026S proteasome non-ATPase regulatory subunit 1/RPN2, N-terminal domainDomain
A [auth U]IPR01664226S proteasome regulatory complex, non-ATPase subcomplex, Rpn2/Psmd1 subunitFamily
J [auth d]IPR000717Proteasome component (PCI) domainDomain
J [auth d]IPR00674626S proteasome non-ATPase regulatory subunit Rpn12Family
J [auth d]IPR033464CSN8/PSMD8/EIF3KDomain
K [auth e]IPR007834DSS1/SEM1Family
L [auth f]IPR04143326S proteasome non-ATPase regulatory subunit RPN1, C-terminalDomain
L [auth f]IPR016024Armadillo-type foldHomologous Superfamily
L [auth f]IPR002015Proteasome/cyclosome repeatRepeat
L [auth f]IPR01664326S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 subunitFamily
L [auth f]IPR011989Armadillo-like helicalHomologous Superfamily
L [auth f]IPR040892RPN1, N-terminalDomain
M [auth A]IPR05022126S Proteasome Regulatory ATPaseFamily
M [auth A]IPR003593AAA+ ATPase domainDomain
M [auth A]IPR003959ATPase, AAA-type, coreDomain
M [auth A]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
M [auth A]IPR04872326S proteasome regulatory subunit 7-like, OB domainDomain
M [auth A]IPR041569AAA ATPase, AAA+ lid domainDomain
M [auth A]IPR003960ATPase, AAA-type, conserved siteConserved Site
M [auth A]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
N [auth B]IPR05022126S Proteasome Regulatory ATPaseFamily
N [auth B]IPR041569AAA ATPase, AAA+ lid domainDomain
N [auth B]IPR032501Proteasomal ATPase, second OB domainDomain
N [auth B]IPR003960ATPase, AAA-type, conserved siteConserved Site
N [auth B]IPR003593AAA+ ATPase domainDomain
N [auth B]IPR003959ATPase, AAA-type, coreDomain
N [auth B]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
N [auth B]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
O [auth C]IPR05022126S Proteasome Regulatory ATPaseFamily
O [auth C]IPR003593AAA+ ATPase domainDomain
O [auth C]IPR003959ATPase, AAA-type, coreDomain
O [auth C]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
O [auth C]IPR041569AAA ATPase, AAA+ lid domainDomain
O [auth C]IPR032501Proteasomal ATPase, second OB domainDomain
O [auth C]IPR003960ATPase, AAA-type, conserved siteConserved Site
O [auth C]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
P [auth D]IPR05022126S Proteasome Regulatory ATPaseFamily
P [auth D]IPR041569AAA ATPase, AAA+ lid domainDomain
P [auth D]IPR032501Proteasomal ATPase, second OB domainDomain
P [auth D]IPR003960ATPase, AAA-type, conserved siteConserved Site
P [auth D]IPR003593AAA+ ATPase domainDomain
P [auth D]IPR003959ATPase, AAA-type, coreDomain
P [auth D]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
P [auth D]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
Q [auth E]IPR05022126S Proteasome Regulatory ATPaseFamily
Q [auth E]IPR003593AAA+ ATPase domainDomain
Q [auth E]IPR003959ATPase, AAA-type, coreDomain
Q [auth E]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
Q [auth E]IPR041569AAA ATPase, AAA+ lid domainDomain
Q [auth E]IPR032501Proteasomal ATPase, second OB domainDomain
Q [auth E]IPR003960ATPase, AAA-type, conserved siteConserved Site
Q [auth E]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
R [auth F]IPR05022126S Proteasome Regulatory ATPaseFamily
R [auth F]IPR003593AAA+ ATPase domainDomain
R [auth F]IPR003959ATPase, AAA-type, coreDomain
R [auth F]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
R [auth F]IPR041569AAA ATPase, AAA+ lid domainDomain
R [auth F]IPR032501Proteasomal ATPase, second OB domainDomain
R [auth F]IPR003960ATPase, AAA-type, conserved siteConserved Site
R [auth F]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
S [auth u],
T [auth w]
IPR019954Ubiquitin conserved siteConserved Site
S [auth u],
T [auth w]
IPR050158Ubiquitin and ubiquitin-likeFamily
S [auth u],
T [auth w]
IPR000626Ubiquitin-like domainDomain
S [auth u],
T [auth w]
IPR019956Ubiquitin domainDomain
S [auth u],
T [auth w]
IPR029071Ubiquitin-like domain superfamilyHomologous Superfamily
B [auth V]IPR01358626S proteasome regulatory subunit, C-terminalDomain
B [auth V]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
B [auth V]IPR050756COP9 signalosome complex subunit 3Family
B [auth V]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
B [auth V]IPR000717Proteasome component (PCI) domainDomain
IA [auth g],
U [auth G]
IPR034642Proteasome subunit alpha6Family
IA [auth g],
U [auth G]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
IA [auth g],
U [auth G]
IPR050115Proteasome subunit alphaFamily
IA [auth g],
U [auth G]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
IA [auth g],
U [auth G]
IPR023332Proteasome alpha-type subunitFamily
IA [auth g],
U [auth G]
IPR001353Proteasome, subunit alpha/betaFamily
JA [auth h],
V [auth H]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
JA [auth h],
V [auth H]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
JA [auth h],
V [auth H]
IPR050115Proteasome subunit alphaFamily
JA [auth h],
V [auth H]
IPR023332Proteasome alpha-type subunitFamily
JA [auth h],
V [auth H]
IPR001353Proteasome, subunit alpha/betaFamily
KA [auth i],
W [auth I]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
KA [auth i],
W [auth I]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
KA [auth i],
W [auth I]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
KA [auth i],
W [auth I]
IPR050115Proteasome subunit alphaFamily
KA [auth i],
W [auth I]
IPR023332Proteasome alpha-type subunitFamily
KA [auth i],
W [auth I]
IPR001353Proteasome, subunit alpha/betaFamily
LA [auth j],
X [auth J]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
LA [auth j],
X [auth J]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
LA [auth j],
X [auth J]
IPR050115Proteasome subunit alphaFamily
LA [auth j],
X [auth J]
IPR023332Proteasome alpha-type subunitFamily
LA [auth j],
X [auth J]
IPR001353Proteasome, subunit alpha/betaFamily
MA [auth k],
Y [auth K]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
MA [auth k],
Y [auth K]
IPR033812Proteasome subunit alpha5Family
MA [auth k],
Y [auth K]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
MA [auth k],
Y [auth K]
IPR050115Proteasome subunit alphaFamily
MA [auth k],
Y [auth K]
IPR023332Proteasome alpha-type subunitFamily
MA [auth k],
Y [auth K]
IPR001353Proteasome, subunit alpha/betaFamily
NA [auth l],
Z [auth L]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
NA [auth l],
Z [auth L]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
NA [auth l],
Z [auth L]
IPR050115Proteasome subunit alphaFamily
NA [auth l],
Z [auth L]
IPR035144Proteasome subunit alpha 1Family
NA [auth l],
Z [auth L]
IPR023332Proteasome alpha-type subunitFamily
NA [auth l],
Z [auth L]
IPR001353Proteasome, subunit alpha/betaFamily
AA [auth M],
OA [auth m]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
AA [auth M],
OA [auth m]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
AA [auth M],
OA [auth m]
IPR050115Proteasome subunit alphaFamily
AA [auth M],
OA [auth m]
IPR023332Proteasome alpha-type subunitFamily
AA [auth M],
OA [auth m]
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth N],
PA [auth n]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
BA [auth N],
PA [auth n]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
BA [auth N],
PA [auth n]
IPR023333Proteasome B-type subunitFamily
BA [auth N],
PA [auth n]
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth N],
PA [auth n]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
CA [auth O],
QA [auth o]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
CA [auth O],
QA [auth o]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
CA [auth O],
QA [auth o]
IPR024689Proteasome beta subunit, C-terminalDomain
CA [auth O],
QA [auth o]
IPR023333Proteasome B-type subunitFamily
CA [auth O],
QA [auth o]
IPR001353Proteasome, subunit alpha/betaFamily
CA [auth O],
QA [auth o]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
DA [auth P],
RA [auth p]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
DA [auth P],
RA [auth p]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
DA [auth P],
RA [auth p]
IPR023333Proteasome B-type subunitFamily
DA [auth P],
RA [auth p]
IPR001353Proteasome, subunit alpha/betaFamily
DA [auth P],
RA [auth p]
IPR033811Proteasome beta 3 subunitFamily
C [auth W]IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
C [auth W]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
C [auth W]IPR000717Proteasome component (PCI) domainDomain
C [auth W]IPR04089626S proteasome regulatory subunit RPN5, C-terminal domainDomain
C [auth W]IPR04013426S Proteasome non-ATPase regulatory subunit 12/COP9 signalosome complex subunit 4Family
C [auth W]IPR054559PSMD12/CSN4-like, N-terminalDomain
EA [auth Q],
SA [auth q]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
EA [auth Q],
SA [auth q]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
EA [auth Q],
SA [auth q]
IPR023333Proteasome B-type subunitFamily
EA [auth Q],
SA [auth q]
IPR001353Proteasome, subunit alpha/betaFamily
EA [auth Q],
SA [auth q]
IPR035206Proteasome subunit beta 2Family
FA [auth R],
TA [auth r]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
FA [auth R],
TA [auth r]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
FA [auth R],
TA [auth r]
IPR023333Proteasome B-type subunitFamily
FA [auth R],
TA [auth r]
IPR001353Proteasome, subunit alpha/betaFamily
FA [auth R],
TA [auth r]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
GA [auth S],
UA [auth s]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
GA [auth S],
UA [auth s]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
GA [auth S],
UA [auth s]
IPR023333Proteasome B-type subunitFamily
GA [auth S],
UA [auth s]
IPR001353Proteasome, subunit alpha/betaFamily
HA [auth T],
VA [auth t]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
HA [auth T],
VA [auth t]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
HA [auth T],
VA [auth t]
IPR023333Proteasome B-type subunitFamily
HA [auth T],
VA [auth t]
IPR016295Proteasome subunit beta 4Family
HA [auth T],
VA [auth t]
IPR001353Proteasome, subunit alpha/betaFamily
D [auth X]IPR05087126S Proteasome and COP9 Signalosome ComponentsFamily
D [auth X]IPR0407806S proteasome subunit Rpn6, C-terminal helix domainDomain
D [auth X]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
D [auth X]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
D [auth X]IPR04077326S proteasome regulatory subunit Rpn6, N-terminalDomain
D [auth X]IPR000717Proteasome component (PCI) domainDomain
E [auth Y]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
E [auth Y]IPR01958526S proteasome regulatory subunit Rpn7/COP9 signalosome complex subunit 1Family
E [auth Y]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
E [auth Y]IPR04954926S proteasome regulatory subunit RPN7/PSMD6, C-terminal helixDomain
E [auth Y]IPR000717Proteasome component (PCI) domainDomain
E [auth Y]IPR04513526S proteasome regulatory subunit Rpn7, N-terminalDomain
F [auth Z]IPR03385826S Proteasome non-ATPase regulatory subunit 7/8Family
F [auth Z]IPR024969EIF3F/CSN6-like, C-terminalDomain
F [auth Z]IPR037518MPN domainDomain
F [auth Z]IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
G [auth a]IPR054179PSD13, N-terminalDomain
G [auth a]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
G [auth a]IPR03529826S Proteasome non-ATPase regulatory subunit 13Family
G [auth a]IPR000717Proteasome component (PCI) domainDomain
H [auth b]IPR036465von Willebrand factor A-like domain superfamilyHomologous Superfamily
H [auth b]IPR02704026S proteasome non-ATPase regulatory subunit 4Family
H [auth b]IPR002035von Willebrand factor, type ADomain
H [auth b]IPR003903Ubiquitin interacting motifConserved Site
H [auth b]IPR049590PSMD4, RAZUL domainDomain
I [auth c]IPR05626326S proteasome regulatory subunit RPN11, C-terminal domainDomain
I [auth c]IPR050242JAMM/MPN+ metalloenzymes, peptidase M67AFamily
I [auth c]IPR037518MPN domainDomain
I [auth c]IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A [auth U]PharosQ99460
J [auth d]PharosP48556
K [auth e]PharosP60896
L [auth f]PharosQ13200
M [auth A]PharosP35998
O [auth C]PharosP62195
P [auth D]PharosP43686
R [auth F]PharosP17980
S [auth u],
T [auth w]
PharosP0CG47
B [auth V]PharosO43242
IA [auth g],
U [auth G]
PharosP60900
JA [auth h],
V [auth H]
PharosP25787
KA [auth i],
W [auth I]
PharosP25789
LA [auth j],
X [auth J]
PharosO14818
MA [auth k],
Y [auth K]
PharosP28066
NA [auth l],
Z [auth L]
PharosP25786
AA [auth M],
OA [auth m]
PharosP25788
BA [auth N],
PA [auth n]
PharosP28072
CA [auth O],
QA [auth o]
PharosQ99436
DA [auth P],
RA [auth p]
PharosP49720
C [auth W]PharosO00232
EA [auth Q],
SA [auth q]
PharosP49721
FA [auth R],
TA [auth r]
PharosP28074
GA [auth S],
UA [auth s]
PharosP20618
HA [auth T],
VA [auth t]
PharosP28070
D [auth X]PharosO00231
E [auth Y]PharosQ15008
F [auth Z]PharosP51665
G [auth a]PharosQ9UNM6
H [auth b]PharosP55036
I [auth c]PharosO00487
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