UniProtKB - P81947 (TBA1B_BOVIN)
Tubulin alpha-1B chain
Functioni
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 451 | Involved in polymerizationBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 142 – 148 | GTPSequence analysis | 7 |
GO - Molecular functioni
- GTPase activity Source: InterPro
- GTP binding Source: GO_Central
- structural constituent of cytoskeleton Source: GO_Central
GO - Biological processi
- microtubule-based process Source: GO_Central
- microtubule cytoskeleton organization Source: GO_Central
- mitotic cell cycle Source: GO_Central
Keywordsi
Ligand | GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-BTA-190840, Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane R-BTA-2467813, Separation of Sister Chromatids R-BTA-2500257, Resolution of Sister Chromatid Cohesion R-BTA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) R-BTA-380320, Recruitment of NuMA to mitotic centrosomes R-BTA-5610787, Hedgehog 'off' state R-BTA-5617833, Cilium Assembly R-BTA-5620924, Intraflagellar transport R-BTA-5626467, RHO GTPases activate IQGAPs R-BTA-5663220, RHO GTPases Activate Formins R-BTA-6807878, COPI-mediated anterograde transport R-BTA-6811434, COPI-dependent Golgi-to-ER retrograde traffic R-BTA-68877, Mitotic Prometaphase R-BTA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint R-BTA-8955332, Carboxyterminal post-translational modifications of tubulin R-BTA-9646399, Aggrephagy R-BTA-9648025, EML4 and NUDC in mitotic spindle formation R-BTA-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III R-BTA-983189, Kinesins |
Names & Taxonomyi
Protein namesi | Recommended name: Tubulin alpha-1B chainAlternative name(s): Alpha-tubulin ubiquitous Tubulin K-alpha-1 Tubulin alpha-ubiquitous chain Cleaved into the following chain: |
Organismi | Bos taurus (Bovine)Curated |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Cytoskeleton
Cytoskeleton
- microtubule Source: GO_Central
Cytosol
- cytosol Source: Reactome
Other locations
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, MicrotubulePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000048114 | 1 – 451 | Tubulin alpha-1B chainAdd BLAST | 451 | |
ChainiPRO_0000437397 | 1 – 450 | Detyrosinated tubulin alpha-1B chainBy similarityAdd BLAST | 450 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 40 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 40 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 48 | PhosphoserineBy similarity | 1 | |
Modified residuei | 232 | PhosphoserineBy similarity | 1 | |
Modified residuei | 282 | 3'-nitrotyrosineBy similarity | 1 | |
Cross-linki | 326 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 339 | Omega-N-methylarginineBy similarity | 1 | |
Cross-linki | 370 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 439 | PhosphoserineBy similarity | 1 | |
Modified residuei | 445 | 5-glutamyl polyglutamateBy similarity | 1 | |
Modified residuei | 451 | 3'-nitrotyrosineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P81947 |
PeptideAtlasi | P81947 |
PRIDEi | P81947 |
PTM databases
iPTMneti | P81947 |
SwissPalmi | P81947 |
Expressioni
Gene expression databases
Bgeei | ENSBTAG00000012244, Expressed in prefrontal cortex and 18 other tissues |
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
DIPi | DIP-41283N |
IntActi | P81947, 1 interactor |
MINTi | P81947 |
STRINGi | 9913.ENSBTAP00000016242 |
Structurei
Secondary structure
3D structure databases
SASBDBi | P81947 |
SMRi | P81947 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P81947 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1376, Eukaryota |
HOGENOMi | CLU_015718_0_0_1 |
InParanoidi | P81947 |
OMAi | VDNEACY |
OrthoDBi | 514396at2759 |
TreeFami | TF300314 |
Family and domain databases
Gene3Di | 1.10.287.600, 1 hit 3.30.1330.20, 1 hit 3.40.50.1440, 1 hit |
InterProi | View protein in InterPro IPR002452, Alpha_tubulin IPR008280, Tub_FtsZ_C IPR000217, Tubulin IPR018316, Tubulin/FtsZ_2-layer-sand-dom IPR037103, Tubulin/FtsZ_C_sf IPR036525, Tubulin/FtsZ_GTPase_sf IPR023123, Tubulin_C IPR017975, Tubulin_CS IPR003008, Tubulin_FtsZ_GTPase |
PANTHERi | PTHR11588, PTHR11588, 1 hit |
Pfami | View protein in Pfam PF00091, Tubulin, 1 hit PF03953, Tubulin_C, 1 hit |
PRINTSi | PR01162, ALPHATUBULIN PR01161, TUBULIN |
SMARTi | View protein in SMART SM00864, Tubulin, 1 hit SM00865, Tubulin_C, 1 hit |
SUPFAMi | SSF52490, SSF52490, 1 hit SSF55307, SSF55307, 1 hit |
PROSITEi | View protein in PROSITE PS00227, TUBULIN, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC146060 mRNA Translation: AAI46061.1 |
RefSeqi | NP_001108328.1, NM_001114856.1 |
Genome annotation databases
GeneIDi | 539882 |
KEGGi | bta:539882 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC146060 mRNA Translation: AAI46061.1 |
RefSeqi | NP_001108328.1, NM_001114856.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3DCO | electron microscopy | 1.90 | A | 1-451 | [»] | |
3EDL | electron microscopy | 28.00 | A/F | 1-451 | [»] | |
3IZ0 | electron microscopy | 8.60 | A | 1-451 | [»] | |
3J1T | electron microscopy | 9.70 | B | 1-451 | [»] | |
3J1U | electron microscopy | 9.70 | B | 1-451 | [»] | |
3J2U | electron microscopy | 10.80 | A/C | 1-451 | [»] | |
4I4T | X-ray | 1.80 | A/C | 1-450 | [»] | |
4I50 | X-ray | 2.30 | A/C | 1-451 | [»] | |
4I55 | X-ray | 2.20 | A/C | 1-450 | [»] | |
4IHJ | X-ray | 2.00 | A/C | 1-450 | [»] | |
4IIJ | X-ray | 2.60 | A/C | 1-451 | [»] | |
4O2A | X-ray | 2.50 | A/C | 1-451 | [»] | |
4O2B | X-ray | 2.30 | A/C | 1-451 | [»] | |
4O4H | X-ray | 2.10 | A/C | 1-451 | [»] | |
4O4I | X-ray | 2.40 | A/C | 1-451 | [»] | |
4O4J | X-ray | 2.20 | A/C | 1-451 | [»] | |
4O4L | X-ray | 2.20 | A/C | 1-451 | [»] | |
4TUY | X-ray | 2.10 | A/C | 1-451 | [»] | |
4TV8 | X-ray | 2.10 | A/C | 1-451 | [»] | |
4TV9 | X-ray | 2.00 | A/C | 1-451 | [»] | |
4UXO | electron microscopy | 6.30 | A | 1-451 | [»] | |
4UXP | electron microscopy | 6.30 | A | 1-451 | [»] | |
4UXR | electron microscopy | 7.00 | A | 1-451 | [»] | |
4UXS | electron microscopy | 7.00 | A | 1-451 | [»] | |
4UXT | electron microscopy | 7.40 | A | 1-451 | [»] | |
4UXY | electron microscopy | 6.50 | A | 1-451 | [»] | |
4UY0 | electron microscopy | 7.70 | A | 1-451 | [»] | |
4YJ2 | X-ray | 2.60 | A/C | 1-451 | [»] | |
4YJ3 | X-ray | 3.75 | A/C | 1-451 | [»] | |
5BMV | X-ray | 2.50 | A/C | 1-451 | [»] | |
5EIB | X-ray | 2.10 | C | 1-451 | [»] | |
5GON | X-ray | 2.48 | A/C | 1-440 | [»] | |
5HNW | electron microscopy | 6.60 | A | 2-451 | [»] | |
5HNX | electron microscopy | 6.60 | A | 1-451 | [»] | |
5HNY | electron microscopy | 6.30 | A | 2-439 | [»] | |
5HNZ | electron microscopy | 5.80 | A | 1-451 | [»] | |
5ITZ | X-ray | 2.20 | A | 1-451 | [»] | |
5IYZ | X-ray | 1.80 | A/C | 1-451 | [»] | |
5J2T | X-ray | 2.20 | A/C | 1-451 | [»] | |
5J2U | X-ray | 2.50 | A/C | 1-451 | [»] | |
5JH7 | X-ray | 2.25 | A/C | 1-450 | [»] | |
5JVD | X-ray | 2.39 | A/C | 1-451 | [»] | |
5LA6 | X-ray | 2.10 | A/C | 1-451 | [»] | |
5LOV | X-ray | 2.40 | A/C | 1-451 | [»] | |
5LP6 | X-ray | 2.90 | A | 1-439 | [»] | |
C | 1-440 | [»] | ||||
5LXS | X-ray | 2.20 | A/C | 1-451 | [»] | |
5LXT | X-ray | 1.90 | A/C | 1-451 | [»] | |
5LYJ | X-ray | 2.40 | A/C | 1-451 | [»] | |
5M50 | electron microscopy | 5.30 | A/D | 1-439 | [»] | |
5M54 | electron microscopy | 8.00 | A/D | 2-439 | [»] | |
5M5C | electron microscopy | 4.80 | A/D | 2-439 | [»] | |
5M7E | X-ray | 2.05 | A/C | 1-451 | [»] | |
5M7G | X-ray | 2.25 | A/C | 1-451 | [»] | |
5M8D | X-ray | 2.25 | A/C | 1-451 | [»] | |
5M8G | X-ray | 2.15 | A/C | 1-451 | [»] | |
5MF4 | X-ray | 2.30 | A/C | 1-451 | [»] | |
5MIO | X-ray | 3.19 | A | 1-451 | [»] | |
5ND2 | electron microscopy | 5.80 | A | 1-451 | [»] | |
5ND3 | electron microscopy | 6.10 | A | 1-451 | [»] | |
5ND4 | electron microscopy | 4.40 | A | 2-439 | [»] | |
5ND7 | electron microscopy | 7.90 | A | 1-451 | [»] | |
5NFZ | X-ray | 2.10 | A/C | 1-451 | [»] | |
5NG1 | X-ray | 2.20 | A/C | 1-451 | [»] | |
5NJH | X-ray | 2.39 | A/C | 1-450 | [»] | |
5NM5 | X-ray | 2.05 | A | 1-451 | [»] | |
5NQT | X-ray | 2.15 | A | 1-451 | [»] | |
5NQU | X-ray | 1.80 | A | 1-451 | [»] | |
5O7A | X-ray | 2.50 | A/C | 1-451 | [»] | |
5OAM | electron microscopy | 5.50 | A | 1-451 | [»] | |
5OCU | electron microscopy | 5.20 | A | 1-451 | [»] | |
5OGC | electron microscopy | 4.80 | A | 1-451 | [»] | |
5OSK | X-ray | 2.11 | A/C | 1-451 | [»] | |
5OV7 | X-ray | 2.40 | A/C | 1-451 | [»] | |
5XAF | X-ray | 2.55 | A/C | 1-451 | [»] | |
5XAG | X-ray | 2.56 | A/C | 1-451 | [»] | |
5XLT | X-ray | 2.81 | A/C | 1-450 | [»] | |
5XLZ | X-ray | 2.30 | A/C | 1-450 | [»] | |
5YZ3 | X-ray | 2.54 | A/C | 1-450 | [»] | |
5Z4P | X-ray | 2.50 | A | 1-438 | [»] | |
C | 1-440 | [»] | ||||
6BBN | X-ray | 3.51 | A/C | 1-451 | [»] | |
6F7C | X-ray | 2.00 | A/C | 1-451 | [»] | |
6FII | X-ray | 2.40 | A/C | 1-451 | [»] | |
6FJF | X-ray | 2.40 | A/C | 1-451 | [»] | |
6FJM | X-ray | 2.10 | A/C | 1-451 | [»] | |
6FKJ | X-ray | 2.15 | A/C | 1-451 | [»] | |
6FKL | X-ray | 2.10 | A/C | 1-451 | [»] | |
6GF3 | X-ray | 2.40 | A/C | 1-451 | [»] | |
6GJ4 | X-ray | 2.40 | A/C | 1-451 | [»] | |
6GZE | X-ray | 2.49 | A/C | 1-440 | [»] | |
6HX8 | X-ray | 2.40 | A/C | 1-451 | [»] | |
6I5C | X-ray | 2.95 | A/C | 1-451 | [»] | |
6K9V | X-ray | 2.54 | A/C | 1-450 | [»] | |
6KNZ | X-ray | 2.48 | A/C | 1-450 | [»] | |
6OJQ | electron microscopy | 3.67 | A | 1-437 | [»] | |
6QQN | X-ray | 2.30 | A/C | 1-451 | [»] | |
6QTN | X-ray | 1.90 | A/C | 1-451 | [»] | |
6REV | electron microscopy | 3.80 | A/a | 1-441 | [»] | |
6RF2 | electron microscopy | 4.20 | A/a | 1-441 | [»] | |
6RF8 | electron microscopy | 3.80 | A/a | 1-441 | [»] | |
6RFD | electron microscopy | 3.90 | A/a | 1-441 | [»] | |
6S8K | X-ray | 1.52 | A | 1-437 | [»] | |
6S9E | X-ray | 2.25 | A/C | 1-440 | [»] | |
6SES | X-ray | 2.00 | A/C | 1-451 | [»] | |
6WVL | electron microscopy | 3.20 | A/C | 1-451 | [»] | |
6WVM | electron microscopy | 3.30 | A/C | 1-451 | [»] | |
6WVR | electron microscopy | 2.90 | A/C | 1-451 | [»] | |
6Y6D | X-ray | 2.20 | A/C | 1-451 | [»] | |
SASBDBi | P81947 | |||||
SMRi | P81947 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-41283N |
IntActi | P81947, 1 interactor |
MINTi | P81947 |
STRINGi | 9913.ENSBTAP00000016242 |
PTM databases
iPTMneti | P81947 |
SwissPalmi | P81947 |
Proteomic databases
PaxDbi | P81947 |
PeptideAtlasi | P81947 |
PRIDEi | P81947 |
Genome annotation databases
GeneIDi | 539882 |
KEGGi | bta:539882 |
Organism-specific databases
CTDi | 10376 |
Phylogenomic databases
eggNOGi | KOG1376, Eukaryota |
HOGENOMi | CLU_015718_0_0_1 |
InParanoidi | P81947 |
OMAi | VDNEACY |
OrthoDBi | 514396at2759 |
TreeFami | TF300314 |
Enzyme and pathway databases
Reactomei | R-BTA-190840, Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane R-BTA-2467813, Separation of Sister Chromatids R-BTA-2500257, Resolution of Sister Chromatid Cohesion R-BTA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) R-BTA-380320, Recruitment of NuMA to mitotic centrosomes R-BTA-5610787, Hedgehog 'off' state R-BTA-5617833, Cilium Assembly R-BTA-5620924, Intraflagellar transport R-BTA-5626467, RHO GTPases activate IQGAPs R-BTA-5663220, RHO GTPases Activate Formins R-BTA-6807878, COPI-mediated anterograde transport R-BTA-6811434, COPI-dependent Golgi-to-ER retrograde traffic R-BTA-68877, Mitotic Prometaphase R-BTA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint R-BTA-8955332, Carboxyterminal post-translational modifications of tubulin R-BTA-9646399, Aggrephagy R-BTA-9648025, EML4 and NUDC in mitotic spindle formation R-BTA-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III R-BTA-983189, Kinesins |
Miscellaneous databases
EvolutionaryTracei | P81947 |
Gene expression databases
Bgeei | ENSBTAG00000012244, Expressed in prefrontal cortex and 18 other tissues |
Family and domain databases
Gene3Di | 1.10.287.600, 1 hit 3.30.1330.20, 1 hit 3.40.50.1440, 1 hit |
InterProi | View protein in InterPro IPR002452, Alpha_tubulin IPR008280, Tub_FtsZ_C IPR000217, Tubulin IPR018316, Tubulin/FtsZ_2-layer-sand-dom IPR037103, Tubulin/FtsZ_C_sf IPR036525, Tubulin/FtsZ_GTPase_sf IPR023123, Tubulin_C IPR017975, Tubulin_CS IPR003008, Tubulin_FtsZ_GTPase |
PANTHERi | PTHR11588, PTHR11588, 1 hit |
Pfami | View protein in Pfam PF00091, Tubulin, 1 hit PF03953, Tubulin_C, 1 hit |
PRINTSi | PR01162, ALPHATUBULIN PR01161, TUBULIN |
SMARTi | View protein in SMART SM00864, Tubulin, 1 hit SM00865, Tubulin_C, 1 hit |
SUPFAMi | SSF52490, SSF52490, 1 hit SSF55307, SSF55307, 1 hit |
PROSITEi | View protein in PROSITE PS00227, TUBULIN, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TBA1B_BOVIN | |
Accessioni | P81947Primary (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: | December 2, 2020 | |
This is version 144 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families