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Q71U36 (TBA1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin alpha-1A chain
Alternative name(s):
Alpha-tubulin 3
Tubulin B-alpha-1
Tubulin alpha-3 chain
Gene names
Name:TUBA1A
Synonyms:TUBA3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Expressed at a high level in fetal brain. Ref.9

Post-translational modification

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.

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.

Involvement in disease

Lissencephaly 3 (LIS3) [MIM:611603]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the tubulin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Lissencephaly
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Nitration
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' posttranslational protein folding

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cell division

Traceable author statement PubMed 12090300. Source: BHF-UCL

cellular protein metabolic process

Traceable author statement. Source: Reactome

cytoskeleton-dependent intracellular transport

Traceable author statement PubMed 12090300. Source: BHF-UCL

microtubule-based process

Traceable author statement PubMed 12090300. Source: BHF-UCL

mitotic cell cycle

Traceable author statement. Source: Reactome

protein folding

Traceable author statement. Source: Reactome

protein polymerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasmic microtubule

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Traceable author statement PubMed 12090300. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CYLDQ9NQC76EBI-302552,EBI-2117940

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q71U36-1)

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.
Isoform 2 (identifier: Q71U36-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Tubulin alpha-1A chain
PRO_0000048111

Regions

Nucleotide binding142 – 1487GTP Potential

Sites

Site4511Involved in polymerization By similarity

Amino acid modifications

Modified residue481Phosphoserine By similarity
Modified residue831Nitrated tyrosine By similarity
Modified residue2821Nitrated tyrosine By similarity
Modified residue4321Phosphotyrosine By similarity
Modified residue4391Phosphoserine By similarity

Natural variations

Alternative sequence1 – 3535Missing in isoform 2.
VSP_046782
Natural variant1881I → L in LIS3. Ref.9
VAR_039332
Natural variant2631P → T in LIS3. Ref.9
VAR_039333
Natural variant2641R → C in LIS3. Ref.9
VAR_039334
Natural variant2861L → F in LIS3. Ref.9
VAR_039335
Natural variant4021R → C in LIS3. Ref.9
VAR_039336
Natural variant4021R → H in LIS3. Ref.9
VAR_039337
Natural variant4191S → L in LIS3. Ref.9
VAR_039338
Natural variant4471E → K.
Corresponds to variant rs1065730 [ dbSNP | Ensembl ].
VAR_034540

Experimental info

Sequence conflict1311G → R in CAA25855. Ref.1
Sequence conflict1311G → R in AAA91575. Ref.8
Sequence conflict2901E → D in AAA91575. Ref.8
Sequence conflict3081R → G in CAA25855. Ref.1
Sequence conflict3081R → G in AAA91575. Ref.8
Sequence conflict4381D → H in CAA25855. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 00F8429A4A10E5FE

FASTA45150,136
        10         20         30         40         50         60 
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 

        70         80         90        100        110        120 
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD 

       130        140        150        160        170        180 
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA 

       190        200        210        220        230        240 
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA 

       250        260        270        280        290        300 
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 

       310        320        330        340        350        360 
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP 

       370        380        390        400        410        420 
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 

       430        440        450 
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y 

« Hide

Isoform 2 [UniParc].

Checksum: BF1E2C9AC0754A68
Show »

FASTA41646,297

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Large spectrum of lissencephaly and pachygyria phenotypes resulting from de novo missense mutations in tubulin alpha 1A (TUBA1A)."
Poirier K., Keays D.A., Francis F., Saillour Y., Bahi N., Manouvrier S., Fallet-Bianco C., Pasquier L., Toutain A., Tuy F.P., Bienvenu T., Joriot S., Odent S., Ville D., Desguerre I., Goldenberg A., Moutard M.L., Fryns J.-P. expand/collapse author list , van Esch H., Harvey R.J., Siebold C., Flint J., Beldjord C., Chelly J.
Hum. Mutat. 28:1055-1064(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001257328.1. NM_001270399.1.
NP_001257329.1. NM_001270400.1.
NP_006000.2. NM_006009.3.
UniGeneHs.654422.

3D structure databases

ProteinModelPortalQ71U36.
SMRQ71U36. Positions 1-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113603. 131 interactions.
IntActQ71U36. 69 interactions.
MINTMINT-156132.
STRING9606.ENSP00000301071.

Chemistry

BindingDBQ71U36.
ChEMBLCHEMBL2095182.

PTM databases

PhosphoSiteQ71U36.

Polymorphism databases

DMDM55977864.

Proteomic databases

PaxDbQ71U36.
PRIDEQ71U36.

Protocols and materials databases

DNASU7846.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295766; ENSP00000439020; ENSG00000167552. [Q71U36-1]
ENST00000301071; ENSP00000301071; ENSG00000167552. [Q71U36-1]
ENST00000550767; ENSP00000446637; ENSG00000167552. [Q71U36-2]
GeneID7846.
KEGGhsa:7846.
UCSCuc001rtp.4. human. [Q71U36-1]

Organism-specific databases

CTD7846.
GeneCardsGC12M049578.
HGNCHGNC:20766. TUBA1A.
HPACAB008686.
HPA039247.
HPA043684.
MIM602529. gene.
611603. phenotype.
neXtProtNX_Q71U36.
Orphanet171680. Lissencephaly due to TUBA1A mutation.
PharmGKBPA162407319.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5023.
HOGENOMHOG000165711.
HOVERGENHBG000089.
InParanoidQ71U36.
KOK07374.
OMAASRSLCM.
OrthoDBEOG7TBC1W.
PhylomeDBQ71U36.
TreeFamTF300314.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.
REACT_17015. Metabolism of proteins.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ71U36.
BgeeQ71U36.
CleanExHS_TUBA1A.
GenevestigatorQ71U36.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR002452. 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]
PANTHERPTHR11588. PTHR11588. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTUBA1A. human.
GeneWikiTUBA1A.
GenomeRNAi7846.
NextBio30260.
PMAP-CutDBQ71U36.
PROQ71U36.
SOURCESearch...

Entry information

Entry nameTBA1A_HUMAN
AccessionPrimary (citable) accession number: Q71U36
Secondary accession number(s): A8K0B8 expand/collapse secondary AC list , G3V1U9, P04687, P05209
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM