ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q13509

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TBB3_HUMAN
Primary accession number Q13509
Secondary accession numbers Q9BTZ0 Q9BW10
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on May 2, 2002 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 86)
Name and origin of the protein
Protein name Tubulin beta-3 chain
Synonyms Tubulin beta-III
Tubulin beta-4
Gene name
Name: TUBB3
Synonyms: TUBB4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0167-4781(97)00168-1; PubMed=9473684 [NCBI, ExPASy, EBI, Israel, Japan]
Ranganathan S., Dexter D.W., Benetatos C.A., Hudes G.R.;
"Cloning and sequencing of human betaIII-tubulin cDNA: induction of betaIII isotype in human prostate carcinoma cells by acute exposure to antimicrotubule agents.";
Biochim. Biophys. Acta 1395:237-245(1998).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary cancer;
Banerjee A.;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
 PROTEIN SEQUENCE OF 63-77; 104-121; 242-251; 163-174 AND 381-390, AND MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[5]
 IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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: Dimer of alpha and beta chains.
  • DOMAIN: The highly acidic C-terminal region may bind cations such as calcium.
  • SIMILARITY: Belongs to the tubulin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U47634; AAC52035.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF427491; AAL28094.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000748; AAH00748.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003021; AAH03021.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00013683; -.
RefSeq NP_006077.2; -.
UniGene Hs.511743
3D structure databases
HSSP P02554; 1FFX. [HSSP ENTRY / PDB]
SMR Q13509; 2-427.
ModBase Q13509.
Protein-protein interaction databases
IntAct Q13509; 4.
PTM databases
PhosphoSite Q13509; -.
2D gel databases
OGP Q13509; -.
Organism-specific databases
GeneCards GC16P088514; -.
HGNC HGNC:20772; TUBB3.
GenAtlas TUBB3.
HPA CAB011512; -.
MIM 602661; gene. [NCBI / EBI]
PharmGKB PA134953867; -.
Gene expression databases
ArrayExpress Q13509; -.
Bgee Q13509; -.
CleanEx HS_TUBB3; -.
HS_TUBB4; -.
GermOnline ENSG00000198211; Homo sapiens.
Ontologies
GO
GO:0005874; Cellular component: microtubule (inferred from electronic annotation from UniProtKB-KW).
GO:0043234; Cellular component: protein complex (inferred from electronic annotation from InterPro).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003924; Molecular function: GTPase activity (inferred from electronic annotation from InterPro).
GO:0005198; Molecular function: structural molecule activity (inferred from electronic annotation from InterPro).
GO:0007018; Biological process: microtubule-based movement (inferred from electronic annotation from InterPro).
GO:0051258; Biological process: protein polymerization (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013838; Beta-tubulin_BS.
IPR002453; Beta_tubulin.
IPR000217; Tubulin.
IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
IPR017975; Tubulin_CS.
IPR003008; Tubulin_FtsZ_GTPase.
Graphical view of domain structure.
Gene3D G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
PANTHER PTHR11588:SF9; Beta_tubulin; 1.
PTHR11588; Tubulin; 1.
Pfam PF00091; Tubulin; 1.
PF03953; Tubulin_C; 1.
Pfam graphical view of domain structure.
PRINTS PR01163; BETATUBULIN.
PR01161; TUBULIN.
PROSITE PS00227; TUBULIN; 1.
PS00228; TUBULIN_B_AUTOREG; 1.
Proteomic databases
PRIDE Q13509; -.
Genome annotation databases
Ensembl ENSG00000198211; Homo sapiens. [Contig view]
GeneID 10381; -.
KEGG hsa:10381; -.
Phylogenomic databases
HOVERGEN Q13509; -.
Other
NextBio 39327; -.
SOURCE TUBB3; Homo sapiens.
ProtoNet Q13509.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; GTP-binding; Microtubule; Nucleotide-binding.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   450  450     Tubulin beta-3 chain. PRO_0000048250
NP_BIND   140   146  7     GTP (Potential). 
CONFLICT   275   275        A -> R (in Ref. 1; AAC52035). 
Sequence information
Length: 450 AA [This is the length of the unprocessed precursor] Molecular weight: 50433 Da [This is the MW of the unprocessed precursor] CRC64: 4B9CDE7DBA102949 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV 

        70         80         90        100        110        120 
PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 

       130        140        150        160        170        180 
RKECENCDCL QGFQLTHSLG GGTGSGMGTL LISKVREEYP DRIMNTFSVV PSPKVSDTVV 

       190        200        210        220        230        240 
EPYNATLSIH QLVENTDETY CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL 

       250        260        270        280        290        300 
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM 

       310        320        330        340        350        360 
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG 

       370        380        390        400        410        420 
LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 

       430        440        450 
EYQQYQDATA EEEGEMYEDD EEESEAQGPK
Q13509 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!