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Protein

Tubulin alpha-1B chain

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei451Involved in polymerizationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1B chain
Alternative name(s):
Alpha-tubulin ubiquitous
Tubulin K-alpha-1
Tubulin alpha-ubiquitous chain
Cleaved into the following chain:
OrganismiBos taurus (Bovine)Curated
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000481141 – 451Tubulin alpha-1B chainAdd BLAST451
ChainiPRO_00004373971 – 450Detyrosinated tubulin alpha-1B chainBy similarityAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-acetyllysineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei232PhosphoserineBy similarity1
Modified residuei282Nitrated tyrosineBy similarity1
Cross-linki326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei339Omega-N-methylarginineBy similarity1
Cross-linki370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei439PhosphoserineBy similarity1
Modified residuei4455-glutamyl polyglutamateBy similarity1
Modified residuei4513'-nitrotyrosineBy similarity1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.By similarity
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity).By similarity
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.By similarity
Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.By similarity
Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.By similarity
Tubulin alpha-1B chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).By similarity
Detyrosinated tubulin alpha-1B chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP81947.
PeptideAtlasiP81947.
PRIDEiP81947.

PTM databases

iPTMnetiP81947.

Expressioni

Gene expression databases

BgeeiENSBTAG00000012244.

Interactioni

Subunit structurei

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Protein-protein interaction databases

DIPiDIP-41283N.
MINTiMINT-235448.
STRINGi9913.ENSBTAP00000016242.

Structurei

Secondary structure

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi10 – 28Combined sources19
Beta strandi41 – 43Combined sources3
Helixi48 – 51Combined sources4
Beta strandi53 – 55Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi61 – 63Combined sources3
Beta strandi65 – 72Combined sources8
Helixi73 – 80Combined sources8
Helixi84 – 86Combined sources3
Helixi89 – 91Combined sources3
Beta strandi92 – 94Combined sources3
Helixi103 – 107Combined sources5
Turni108 – 110Combined sources3
Helixi111 – 126Combined sources16
Beta strandi134 – 143Combined sources10
Helixi144 – 160Combined sources17
Turni161 – 163Combined sources3
Beta strandi164 – 172Combined sources9
Turni175 – 177Combined sources3
Helixi183 – 194Combined sources12
Helixi195 – 197Combined sources3
Beta strandi199 – 205Combined sources7
Helixi206 – 216Combined sources11
Helixi224 – 243Combined sources20
Beta strandi247 – 249Combined sources3
Helixi252 – 259Combined sources8
Beta strandi261 – 264Combined sources4
Beta strandi269 – 273Combined sources5
Beta strandi277 – 279Combined sources3
Beta strandi280 – 282Combined sources3
Helixi288 – 293Combined sources6
Helixi294 – 296Combined sources3
Helixi298 – 300Combined sources3
Beta strandi301 – 303Combined sources3
Helixi307 – 309Combined sources3
Beta strandi312 – 322Combined sources11
Helixi325 – 336Combined sources12
Beta strandi349 – 358Combined sources10
Beta strandi366 – 368Combined sources3
Beta strandi372 – 381Combined sources10
Helixi382 – 384Combined sources3
Helixi385 – 399Combined sources15
Turni400 – 404Combined sources5
Helixi405 – 409Combined sources5
Turni410 – 412Combined sources3
Helixi415 – 436Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DCOelectron microscopy1.90A1-451[»]
3EDLelectron microscopy28.00A/F1-451[»]
3IZ0electron microscopy8.60A1-451[»]
3J1Telectron microscopy9.70B1-451[»]
3J1Uelectron microscopy9.70B1-451[»]
3J2Uelectron microscopy10.80A/C1-451[»]
4I4TX-ray1.80A/C1-450[»]
4I50X-ray2.30A/C1-451[»]
4I55X-ray2.20A/C1-450[»]
4IHJX-ray2.00A/C1-450[»]
4IIJX-ray2.60A/C1-451[»]
4O2AX-ray2.50A/C1-451[»]
4O2BX-ray2.30A/C1-451[»]
4O4HX-ray2.10A/C1-451[»]
4O4IX-ray2.40A/C1-451[»]
4O4JX-ray2.20A/C1-451[»]
4O4LX-ray2.20A/C1-451[»]
4TUYX-ray2.10A/C1-451[»]
4TV8X-ray2.10A/C1-451[»]
4TV9X-ray2.00A/C1-451[»]
4UXOelectron microscopy6.30A1-451[»]
4UXPelectron microscopy6.30A1-451[»]
4UXRelectron microscopy7.00A1-451[»]
4UXSelectron microscopy7.00A1-451[»]
4UXTelectron microscopy7.40A1-451[»]
4UXYelectron microscopy6.50A1-451[»]
4UY0electron microscopy7.70A1-451[»]
4WBNX-ray2.30A/C1-451[»]
4YJ2X-ray2.60A/C1-451[»]
4YJ3X-ray3.75A/C1-451[»]
5BMVX-ray2.50A/C1-451[»]
5HNWelectron microscopy6.60A2-451[»]
5HNXelectron microscopy6.60A1-451[»]
5HNYelectron microscopy6.30A2-439[»]
5HNZelectron microscopy5.80A1-451[»]
5ITZX-ray2.20A1-451[»]
5IYZX-ray1.80A/C1-451[»]
5J2TX-ray2.20A/C1-451[»]
5J2UX-ray2.50A/C1-451[»]
5JH7X-ray2.25A/C1-450[»]
5JVDX-ray2.39A/C1-451[»]
5LA6X-ray2.10A/C1-451[»]
5LP6X-ray2.90A1-439[»]
C1-440[»]
ProteinModelPortaliP81947.
SMRiP81947.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81947.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP81947.
KOiK07374.
OMAiWARTRNT.
OrthoDBiEOG091G0736.
TreeFamiTF300314.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P81947-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE

Y
Length:451
Mass (Da):50,152
Last modified:February 10, 2009 - v2
Checksum:i94355B4EC2086429
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC146060 mRNA. Translation: AAI46061.1.
RefSeqiNP_001108328.1. NM_001114856.1.
UniGeneiBt.106995.
Bt.109492.

Genome annotation databases

EnsembliENSBTAT00000016242; ENSBTAP00000016242; ENSBTAG00000012244.
GeneIDi539882.
KEGGibta:539882.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC146060 mRNA. Translation: AAI46061.1.
RefSeqiNP_001108328.1. NM_001114856.1.
UniGeneiBt.106995.
Bt.109492.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DCOelectron microscopy1.90A1-451[»]
3EDLelectron microscopy28.00A/F1-451[»]
3IZ0electron microscopy8.60A1-451[»]
3J1Telectron microscopy9.70B1-451[»]
3J1Uelectron microscopy9.70B1-451[»]
3J2Uelectron microscopy10.80A/C1-451[»]
4I4TX-ray1.80A/C1-450[»]
4I50X-ray2.30A/C1-451[»]
4I55X-ray2.20A/C1-450[»]
4IHJX-ray2.00A/C1-450[»]
4IIJX-ray2.60A/C1-451[»]
4O2AX-ray2.50A/C1-451[»]
4O2BX-ray2.30A/C1-451[»]
4O4HX-ray2.10A/C1-451[»]
4O4IX-ray2.40A/C1-451[»]
4O4JX-ray2.20A/C1-451[»]
4O4LX-ray2.20A/C1-451[»]
4TUYX-ray2.10A/C1-451[»]
4TV8X-ray2.10A/C1-451[»]
4TV9X-ray2.00A/C1-451[»]
4UXOelectron microscopy6.30A1-451[»]
4UXPelectron microscopy6.30A1-451[»]
4UXRelectron microscopy7.00A1-451[»]
4UXSelectron microscopy7.00A1-451[»]
4UXTelectron microscopy7.40A1-451[»]
4UXYelectron microscopy6.50A1-451[»]
4UY0electron microscopy7.70A1-451[»]
4WBNX-ray2.30A/C1-451[»]
4YJ2X-ray2.60A/C1-451[»]
4YJ3X-ray3.75A/C1-451[»]
5BMVX-ray2.50A/C1-451[»]
5HNWelectron microscopy6.60A2-451[»]
5HNXelectron microscopy6.60A1-451[»]
5HNYelectron microscopy6.30A2-439[»]
5HNZelectron microscopy5.80A1-451[»]
5ITZX-ray2.20A1-451[»]
5IYZX-ray1.80A/C1-451[»]
5J2TX-ray2.20A/C1-451[»]
5J2UX-ray2.50A/C1-451[»]
5JH7X-ray2.25A/C1-450[»]
5JVDX-ray2.39A/C1-451[»]
5LA6X-ray2.10A/C1-451[»]
5LP6X-ray2.90A1-439[»]
C1-440[»]
ProteinModelPortaliP81947.
SMRiP81947.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-41283N.
MINTiMINT-235448.
STRINGi9913.ENSBTAP00000016242.

PTM databases

iPTMnetiP81947.

Proteomic databases

PaxDbiP81947.
PeptideAtlasiP81947.
PRIDEiP81947.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000016242; ENSBTAP00000016242; ENSBTAG00000012244.
GeneIDi539882.
KEGGibta:539882.

Organism-specific databases

CTDi10376.

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP81947.
KOiK07374.
OMAiWARTRNT.
OrthoDBiEOG091G0736.
TreeFamiTF300314.

Miscellaneous databases

EvolutionaryTraceiP81947.

Gene expression databases

BgeeiENSBTAG00000012244.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTBA1B_BOVIN
AccessioniPrimary (citable) accession number: P81947
Secondary accession number(s): A6H700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 10, 2009
Last modified: November 30, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.