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Protein

Tubulin alpha-1A chain

Gene

TUBA1A

Organism
Homo sapiens (Human)
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei451 – 4511Involved in polymerizationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. structural constituent of cytoskeleton Source: InterPro
  4. structural molecule activity Source: BHF-UCL

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: Reactome
  2. cell division Source: BHF-UCL
  3. cellular protein metabolic process Source: Reactome
  4. cytoskeleton-dependent intracellular transport Source: BHF-UCL
  5. G2/M transition of mitotic cell cycle Source: Reactome
  6. microtubule-based process Source: BHF-UCL
  7. mitotic cell cycle Source: Reactome
  8. organelle organization Source: Reactome
  9. protein folding Source: Reactome
  10. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_267965. Anchoring of the basal body to the plasma membrane.
REACT_268024. Intraflagellar transport.
REACT_268265. Assembly of the primary cilium.
REACT_268323. Hedgehog 'off' state.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1A chain
Alternative name(s):
Alpha-tubulin 3
Tubulin B-alpha-1
Tubulin alpha-3 chain
Gene namesi
Name:TUBA1A
Synonyms:TUBA3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:20766. TUBA1A.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic microtubule Source: Ensembl
  2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. microtubule Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. recycling endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Lissencephaly 3 (LIS3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA classic type lissencephaly associated with psychomotor retardation and seizures. Features include agyria or pachygyria or laminar heterotopia, severe mental retardation, motor delay, variable presence of seizures, and abnormalities of corpus callosum, hippocampus, cerebellar vermis and brainstem.

See also OMIM:611603
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti188 – 1881I → L in LIS3. 1 Publication
VAR_039332
Natural varianti263 – 2631P → T in LIS3. 1 Publication
VAR_039333
Natural varianti264 – 2641R → C in LIS3. 1 Publication
VAR_039334
Natural varianti286 – 2861L → F in LIS3. 1 Publication
VAR_039335
Natural varianti402 – 4021R → C in LIS3. 1 Publication
VAR_039336
Natural varianti402 – 4021R → H in LIS3. 1 Publication
VAR_039337
Natural varianti419 – 4191S → L in LIS3. 1 Publication
VAR_039338

Keywords - Diseasei

Disease mutation, Lissencephaly

Organism-specific databases

MIMi611603. phenotype.
Orphaneti171680. Lissencephaly due to TUBA1A mutation.
PharmGKBiPA162407319.

Chemistry

DrugBankiDB00518. Albendazole.
DB00643. Mebendazole.
DB00570. Vinblastine.

Polymorphism and mutation databases

BioMutaiTUBA1A.
DMDMi55977864.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Tubulin alpha-1A chainPRO_0000048111Add
BLAST

Post-translational modificationi

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
Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation 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 glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable).1 Publication
Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ71U36.
PaxDbiQ71U36.
PRIDEiQ71U36.

PTM databases

PhosphoSiteiQ71U36.

Miscellaneous databases

PMAP-CutDBQ71U36.

Expressioni

Tissue specificityi

Expressed at a high level in fetal brain.1 Publication

Gene expression databases

BgeeiQ71U36.
CleanExiHS_TUBA1A.
ExpressionAtlasiQ71U36. baseline and differential.
GenevestigatoriQ71U36.

Organism-specific databases

HPAiCAB008686.
HPA039247.
HPA043684.
HPA063394.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
CYLDQ9NQC76EBI-302552,EBI-2117940
EGFRP005333EBI-302552,EBI-297353

Protein-protein interaction databases

BioGridi113603. 193 interactions.
DIPiDIP-32773N.
IntActiQ71U36. 80 interactions.
MINTiMINT-156132.
STRINGi9606.ENSP00000301071.

Structurei

3D structure databases

ProteinModelPortaliQ71U36.
SMRiQ71U36. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ71U36.
KOiK07374.
OMAiGSKRECI.
OrthoDBiEOG7TBC1W.
PhylomeDBiQ71U36.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q71U36-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 IGQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT 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):50,136
Last modified:July 5, 2004 - v1
Checksum:i00F8429A4A10E5FE
GO
Isoform 2 (identifier: Q71U36-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Note: No experimental confirmation available.

Show »
Length:416
Mass (Da):46,297
Checksum:iBF1E2C9AC0754A68
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311G → R in CAA25855 (PubMed:3839072).Curated
Sequence conflicti131 – 1311G → R in AAA91575 (PubMed:6646120).Curated
Sequence conflicti290 – 2901E → D in AAA91575 (PubMed:6646120).Curated
Sequence conflicti308 – 3081R → G in CAA25855 (PubMed:3839072).Curated
Sequence conflicti308 – 3081R → G in AAA91575 (PubMed:6646120).Curated
Sequence conflicti438 – 4381D → H in CAA25855 (PubMed:3839072).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti188 – 1881I → L in LIS3. 1 Publication
VAR_039332
Natural varianti263 – 2631P → T in LIS3. 1 Publication
VAR_039333
Natural varianti264 – 2641R → C in LIS3. 1 Publication
VAR_039334
Natural varianti286 – 2861L → F in LIS3. 1 Publication
VAR_039335
Natural varianti402 – 4021R → C in LIS3. 1 Publication
VAR_039336
Natural varianti402 – 4021R → H in LIS3. 1 Publication
VAR_039337
Natural varianti419 – 4191S → L in LIS3. 1 Publication
VAR_039338
Natural varianti447 – 4471E → K.
Corresponds to variant rs1065730 [ dbSNP | Ensembl ].
VAR_034540

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3535Missing in isoform 2. CuratedVSP_046782Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01703 Genomic DNA. Translation: CAA25855.1.
AF141347 mRNA. Translation: AAD33871.1.
AK289483 mRNA. Translation: BAF82172.1.
AC010173 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58052.1.
CH471111 Genomic DNA. Translation: EAW58054.1.
CH471111 Genomic DNA. Translation: EAW58055.1.
BC006468 mRNA. Translation: AAH06468.1.
BC050637 mRNA. Translation: AAH50637.1.
K00557 mRNA. Translation: AAA91575.1.
CCDSiCCDS58226.1. [Q71U36-2]
CCDS58227.1. [Q71U36-1]
CCDS8781.1. [Q71U36-1]
RefSeqiNP_001257328.1. NM_001270399.1. [Q71U36-1]
NP_001257329.1. NM_001270400.1. [Q71U36-2]
NP_006000.2. NM_006009.3. [Q71U36-1]
UniGeneiHs.654422.

Genome annotation databases

EnsembliENST00000295766; ENSP00000439020; ENSG00000167552. [Q71U36-1]
ENST00000301071; ENSP00000301071; ENSG00000167552. [Q71U36-1]
ENST00000550767; ENSP00000446637; ENSG00000167552. [Q71U36-2]
GeneIDi7846.
KEGGihsa:7846.
UCSCiuc001rtp.4. human. [Q71U36-1]

Polymorphism and mutation databases

BioMutaiTUBA1A.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01703 Genomic DNA. Translation: CAA25855.1.
AF141347 mRNA. Translation: AAD33871.1.
AK289483 mRNA. Translation: BAF82172.1.
AC010173 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58052.1.
CH471111 Genomic DNA. Translation: EAW58054.1.
CH471111 Genomic DNA. Translation: EAW58055.1.
BC006468 mRNA. Translation: AAH06468.1.
BC050637 mRNA. Translation: AAH50637.1.
K00557 mRNA. Translation: AAA91575.1.
CCDSiCCDS58226.1. [Q71U36-2]
CCDS58227.1. [Q71U36-1]
CCDS8781.1. [Q71U36-1]
RefSeqiNP_001257328.1. NM_001270399.1. [Q71U36-1]
NP_001257329.1. NM_001270400.1. [Q71U36-2]
NP_006000.2. NM_006009.3. [Q71U36-1]
UniGeneiHs.654422.

3D structure databases

ProteinModelPortaliQ71U36.
SMRiQ71U36. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113603. 193 interactions.
DIPiDIP-32773N.
IntActiQ71U36. 80 interactions.
MINTiMINT-156132.
STRINGi9606.ENSP00000301071.

Chemistry

BindingDBiQ71U36.
ChEMBLiCHEMBL2095182.
DrugBankiDB00518. Albendazole.
DB00643. Mebendazole.
DB00570. Vinblastine.

PTM databases

PhosphoSiteiQ71U36.

Polymorphism and mutation databases

BioMutaiTUBA1A.
DMDMi55977864.

Proteomic databases

MaxQBiQ71U36.
PaxDbiQ71U36.
PRIDEiQ71U36.

Protocols and materials databases

DNASUi7846.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295766; ENSP00000439020; ENSG00000167552. [Q71U36-1]
ENST00000301071; ENSP00000301071; ENSG00000167552. [Q71U36-1]
ENST00000550767; ENSP00000446637; ENSG00000167552. [Q71U36-2]
GeneIDi7846.
KEGGihsa:7846.
UCSCiuc001rtp.4. human. [Q71U36-1]

Organism-specific databases

CTDi7846.
GeneCardsiGC12M049578.
HGNCiHGNC:20766. TUBA1A.
HPAiCAB008686.
HPA039247.
HPA043684.
HPA063394.
MIMi602529. gene.
611603. phenotype.
neXtProtiNX_Q71U36.
Orphaneti171680. Lissencephaly due to TUBA1A mutation.
PharmGKBiPA162407319.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ71U36.
KOiK07374.
OMAiGSKRECI.
OrthoDBiEOG7TBC1W.
PhylomeDBiQ71U36.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_267965. Anchoring of the basal body to the plasma membrane.
REACT_268024. Intraflagellar transport.
REACT_268265. Assembly of the primary cilium.
REACT_268323. Hedgehog 'off' state.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Miscellaneous databases

ChiTaRSiTUBA1A. human.
GeneWikiiTUBA1A.
GenomeRNAii7846.
NextBioi30260.
PMAP-CutDBQ71U36.
PROiQ71U36.
SOURCEiSearch...

Gene expression databases

BgeeiQ71U36.
CleanExiHS_TUBA1A.
ExpressionAtlasiQ71U36. baseline and differential.
GenevestigatoriQ71U36.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Structural features and restricted expression of a human alpha-tubulin gene."
    Hall J.L., Cowan N.J.
    Nucleic Acids Res. 13:207-223(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site."
    Crabtree D.V., Ojima I., Geng X., Adler A.J.
    Bioorg. Med. Chem. 9:1967-1976(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cerebellum.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle and Skin.
  7. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-105; 113-121; 157-163; 216-304; 312-320; 327-336; 340-352; 374-390; 395-401 AND 403-430, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  8. "Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions."
    Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W.
    Mol. Cell. Biol. 3:1738-1745(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-451.
    Tissue: Fetal brain.
  9. Cited for: TISSUE SPECIFICITY, VARIANTS LIS3 LEU-188; THR-263; CYS-264; PHE-286; HIS-402; CYS-402 AND LEU-419.
  10. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
    Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
    Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCYLATION.

Entry informationi

Entry nameiTBA1A_HUMAN
AccessioniPrimary (citable) accession number: Q71U36
Secondary accession number(s): A8K0B8
, G3V1U9, P04687, P05209
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 5, 2004
Last modified: April 29, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.