Annotations: 3JAR

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth F]	SCOP2B Superfamily	Tubulin C-terminal domain-like	8036011	3001732	SCOP2B (2022-06-29)
B [auth F]	SCOP2B Superfamily	Tubulin nucleotide-binding domain-like	8044258	3001758	SCOP2B (2022-06-29)
E [auth G]	SCOP2B Superfamily	Tubulin nucleotide-binding domain-like	8044258	3001758	SCOP2B (2022-06-29)
E [auth G]	SCOP2B Superfamily	Tubulin C-terminal domain-like	8036011	3001732	SCOP2B (2022-06-29)
G [auth D]	SCOP2B Superfamily	Tubulin C-terminal domain-like	8036011	3001732	SCOP2B (2022-06-29)
G [auth D]	SCOP2B Superfamily	Tubulin nucleotide-binding domain-like	8044258	3001758	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Tubulin C-terminal domain-like	8036011	3001732	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Tubulin nucleotide-binding domain-like	8044258	3001758	SCOP2B (2022-06-29)
K [auth B]	SCOP2B Superfamily	Tubulin C-terminal domain-like	8036011	3001732	SCOP2B (2022-06-29)
K [auth B]	SCOP2B Superfamily	Tubulin nucleotide-binding domain-like	8044258	3001758	SCOP2B (2022-06-29)
N [auth H]	SCOP2B Superfamily	Tubulin C-terminal domain-like	8036011	3001732	SCOP2B (2022-06-29)
N [auth H]	SCOP2B Superfamily	Tubulin nucleotide-binding domain-like	8044258	3001758	SCOP2B (2022-06-29)
C [auth N]	SCOP2B Superfamily	Calponin-homology domain, CH-domain	8051974	3000264	SCOP2B (2022-06-29)
L [auth M]	SCOP2B Superfamily	Calponin-homology domain, CH-domain	8051974	3000264	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth E]	Tubulin_C	e3jarE2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
A [auth E]	Tubulin	e3jarE1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
D [auth J]	Tubulin_C	e3jarJ2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
D [auth J]	Tubulin	e3jarJ1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
F [auth C]	Tubulin_C	e3jarC1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
F [auth C]	Tubulin	e3jarC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
H [auth L]	Tubulin_C	e3jarL2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
H [auth L]	Tubulin	e3jarL1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
J [auth A]	Tubulin_C	e3jarA1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
J [auth A]	Tubulin	e3jarA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
M [auth K]	Tubulin_C	e3jarK1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
M [auth K]	Tubulin	e3jarK2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
B [auth F]	Tubulin_C	e3jarF1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
B [auth F]	Tubulin	e3jarF2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
E [auth G]	Tubulin_C	e3jarG1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
E [auth G]	Tubulin	e3jarG2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
G [auth D]	Tubulin_C	e3jarD1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
G [auth D]	Tubulin	e3jarD2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
I	Tubulin_C	e3jarI1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
I	Tubulin	e3jarI2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
K [auth B]	Tubulin_C	e3jarB2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
K [auth B]	Tubulin	e3jarB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
N [auth H]	Tubulin_C	e3jarH2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
N [auth H]	Tubulin	e3jarH1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
C [auth N]	CH	e3jarN1	A: alpha bundles	X: CH domain-like	H: Calponin-homology domain-like (From Topology)	T: Calponin-homology domain-like	F: CH	ECOD (1.6)
L [auth M]	CH	e3jarM1	A: alpha bundles	X: CH domain-like	H: Calponin-homology domain-like (From Topology)	T: Calponin-homology domain-like	F: CH	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth E]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
A [auth E]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
A [auth E]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
D [auth J]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
D [auth J]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
D [auth J]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
F [auth C]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
F [auth C]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
F [auth C]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
H [auth L]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
H [auth L]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
H [auth L]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
J [auth A]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
J [auth A]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
J [auth A]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
M [auth K]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
M [auth K]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
M [auth K]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
B [auth F]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
B [auth F]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
B [auth F]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
E [auth G]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
E [auth G]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
E [auth G]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
G [auth D]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
G [auth D]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
G [auth D]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
I	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
I	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
I	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
K [auth B]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
K [auth B]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
K [auth B]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
N [auth H]	3.40.50.1440	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Tubulin/FtsZ, GTPase domain	CATH (4.3.0)
N [auth H]	3.30.1330.20	Alpha Beta	2-Layer Sandwich	60s Ribosomal Protein L30	Chain: A	CATH (4.3.0)
N [auth H]	1.10.287.600	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
C [auth N]	1.10.418.10	Mainly Alpha	Orthogonal Bundle	Actin-binding Protein, T-fimbrin	domain 1	CATH (4.3.0)
L [auth M]	1.10.418.10	Mainly Alpha	Orthogonal Bundle	Actin-binding Protein, T-fimbrin	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	PF00091	Tubulin/FtsZ family, GTPase domain (Tubulin)	Tubulin/FtsZ family, GTPase domain	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ...	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.	Domain
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	PF03953	Tubulin C-terminal domain (Tubulin_C)	Tubulin C-terminal domain	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tub ...	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules. (The FtsZ GTPases have been split into their won family).	Domain
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	PF00091	Tubulin/FtsZ family, GTPase domain (Tubulin)	Tubulin/FtsZ family, GTPase domain	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ...	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.	Domain
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	PF03953	Tubulin C-terminal domain (Tubulin_C)	Tubulin C-terminal domain	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tub ...	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules. (The FtsZ GTPases have been split into their won family).	Domain
C [auth N], L [auth M]	PF00307	Calponin homology (CH) domain (CH)	Calponin homology (CH) domain	The CH domain is found in both cytoskeletal proteins and signal transduction proteins [1]. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its ac ...	The CH domain is found in both cytoskeletal proteins and signal transduction proteins [1]. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity [4]. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin and Swiss:P15498 have only a single copy.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	Tubulin alpha-1B chain	structural constituent of cytoskeleton structural molecule activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding structural constituent of cytoskeleton structural molecule activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding cation binding metal ion binding pyrophosphatase activity GTPase activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity	cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cellular component organization or biogenesis cytoskeleton organization	cellular anatomical structure intracellular anatomical structure cytoplasm polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cytoskeleton organelle membraneless organelle supramolecular fiber microtubule supramolecular polymer supramolecular complex microtubule cytoskeleton
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	Tubulin beta chain	structural constituent of cytoskeleton structural molecule activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding structural constituent of cytoskeleton structural molecule activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding cation binding metal ion binding pyrophosphatase activity GTPase activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity	cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cellular component organization or biogenesis cytoskeleton organization	cellular anatomical structure intracellular anatomical structure cytoplasm polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cytoskeleton organelle membraneless organelle supramolecular fiber microtubule supramolecular polymer supramolecular complex microtubule cytoskeleton
C [auth N], L [auth M]	Microtubule-associated protein RP/EB family member 3	cytoskeletal protein binding microtubule binding protein binding binding tubulin binding kinase binding enzyme binding protein kinase binding microtubule plus-end binding identical protein binding	protein localization localization cellular localization cellular macromolecule localization macromolecule localization cellular process cell division regulation of cellular process positive regulation of phosphorylation regulation of catalytic activity regulation of cyclin-dependent protein kinase activity regulation of transferase activity positive regulation of phosphate metabolic process regulation of primary metabolic process protein localization localization cellular localization cellular macromolecule localization macromolecule localization cellular process cell division regulation of cellular process positive regulation of phosphorylation regulation of catalytic activity regulation of cyclin-dependent protein kinase activity regulation of transferase activity positive regulation of phosphate metabolic process regulation of primary metabolic process positive regulation of metabolic process positive regulation of protein serine/threonine kinase activity positive regulation of cyclin-dependent protein serine/threonine kinase activity regulation of phosphate metabolic process regulation of cyclin-dependent protein serine/threonine kinase activity phosphate-containing compound metabolic process positive regulation of macromolecule metabolic process cell cycle phosphorus metabolic process protein modification process positive regulation of protein phosphorylation regulation of biological process protein phosphorylation positive regulation of phosphorus metabolic process phosphorylation regulation of protein metabolic process primary metabolic process regulation of molecular function positive regulation of kinase activity regulation of kinase activity macromolecule modification regulation of protein serine/threonine kinase activity regulation of phosphorus metabolic process metabolic process macromolecule metabolic process regulation of metabolic process regulation of protein modification process regulation of protein phosphorylation positive regulation of protein metabolic process positive regulation of biological process positive regulation of cyclin-dependent protein kinase activity positive regulation of molecular function positive regulation of protein modification process protein metabolic process positive regulation of protein kinase activity regulation of cell cycle positive regulation of cellular process positive regulation of transferase activity biological regulation positive regulation of catalytic activity regulation of protein kinase activity regulation of macromolecule metabolic process positive regulation of cell cycle regulation of phosphorylation organelle assembly microtubule cytoskeleton organization membraneless organelle assembly spindle assembly cellular component organization cellular component biogenesis organelle organization cellular component assembly microtubule-based process cellular component organization or biogenesis cytoskeleton organization chromosome segregation spindle organization cell cycle process regulation of cytoskeleton organization regulation of microtubule polymerization or depolymerization regulation of cellular component organization regulation of protein-containing complex assembly microtubule polymerization or depolymerization protein-containing complex assembly protein polymerization protein-containing complex organization regulation of microtubule-based process microtubule polymerization regulation of cellular component biogenesis regulation of organelle organization regulation of microtubule polymerization regulation of protein polymerization regulation of supramolecular fiber organization supramolecular fiber organization regulation of microtubule cytoskeleton organization protein localization to microtubule cytoskeleton protein localization to microtubule protein localization to cytoskeleton protein localization to organelle positive regulation of DNA-templated transcription RNA metabolic process positive regulation of macromolecule biosynthetic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process DNA-templated transcription regulation of RNA metabolic process positive regulation of biosynthetic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process positive regulation of nucleobase-containing compound metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process positive regulation of RNA metabolic process regulation of gene expression biosynthetic process positive regulation of RNA biosynthetic process regulation of macromolecule biosynthetic process regulation of DNA-templated transcription	midbody cellular anatomical structure intracellular organelle intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle midzone microtubule cytoskeleton polymeric cytoskeletal fiber mitotic spindle aster midbody cellular anatomical structure intracellular organelle intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle midzone microtubule cytoskeleton polymeric cytoskeletal fiber mitotic spindle aster spindle microtubule cytoplasmic microtubule mitotic spindle astral microtubule end supramolecular polymer supramolecular complex microtubule end mitotic spindle astral microtubule astral microtubule supramolecular fiber cytoplasm microtubule microtubule plus-end microtubule organizing center perinuclear region of cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	IPR003008	Tubulin/FtsZ, GTPase domain	Domain
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	IPR008280	Tubulin/FtsZ, C-terminal	Homologous Superfamily
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	IPR037103	Tubulin/FtsZ-like, C-terminal domain	Homologous Superfamily
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	IPR017975	Tubulin, conserved site	Conserved Site
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	IPR002452	Alpha tubulin	Family
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	IPR000217	Tubulin	Family
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	IPR023123	Tubulin, C-terminal	Homologous Superfamily
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain	Domain
A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], A [auth E], D [auth J], F [auth C], H [auth L], J [auth A], M [auth K]	IPR036525	Tubulin/FtsZ, GTPase domain superfamily	Homologous Superfamily
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR003008	Tubulin/FtsZ, GTPase domain	Domain
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR008280	Tubulin/FtsZ, C-terminal	Homologous Superfamily
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR037103	Tubulin/FtsZ-like, C-terminal domain	Homologous Superfamily
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR017975	Tubulin, conserved site	Conserved Site
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR000217	Tubulin	Family
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR023123	Tubulin, C-terminal	Homologous Superfamily
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR002453	Beta tubulin	Family
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR013838	Beta tubulin, autoregulation binding site	Binding Site
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain	Domain
B [auth F], E [auth G], G [auth D], I, K [auth B], B [auth F], E [auth G], G [auth D], I, K [auth B], N [auth H]	IPR036525	Tubulin/FtsZ, GTPase domain superfamily	Homologous Superfamily
C [auth N], L [auth M]	IPR001715	Calponin homology domain	Domain
C [auth N], L [auth M]	IPR004953	EB1, C-terminal	Domain
C [auth N], L [auth M]	IPR027328	Microtubule-associated protein RP/EB	Family
C [auth N], L [auth M]	IPR036133	EB1, C-terminal domain superfamily	Homologous Superfamily
C [auth N], L [auth M]	IPR036872	CH domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
C [auth N], L [auth M]	Pharos: Q9UPY8	polycystic ovary syndrome Abortion, Spontaneous atypical teratoid rhabdoid tumor glioblastoma malignant glioma ovarian cancer Crohn disease large cell medulloblastoma medulloblastoma Pick disease psoriasis subependymal giant cell astrocytoma astrocytic tumor dermatomyositis lung carcinoma polycystic ovary syndrome Abortion, Spontaneous atypical teratoid rhabdoid tumor glioblastoma malignant glioma ovarian cancer Crohn disease large cell medulloblastoma medulloblastoma Pick disease psoriasis subependymal giant cell astrocytoma astrocytic tumor dermatomyositis lung carcinoma oligodendroglioma pilocytic astrocytoma