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 P07437


[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 TBB5_HUMAN
Primary accession number P07437
Secondary accession numbers P05218 Q8WUC1 Q9CY33
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on December 21, 2004 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 114)
Name and origin of the protein
Protein name Tubulin beta chain
Synonym Tubulin beta-5 chain
Gene name
Name: TUBB
Synonyms: TUBB5
ORFNames: OK/SW-cl.56
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 [GENOMIC DNA].
DOI=10.1016/0092-8674(83)90429-4; PubMed=6688039 [NCBI, ExPASy, EBI, Israel, Japan]
Lee M.G.-S., Lewis S.A., Wilde C.D., Cowan N.J.;
"Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes.";
Cell 33:477-487(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6865944 [NCBI, ExPASy, EBI, Israel, Japan]
Hall J.L., Dudley L., Dobner P.R., Lewis S.A., Cowan N.J.;
"Identification of two human beta-tubulin isotypes.";
Mol. Cell. Biol. 3:854-862(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Retina;
DOI=10.1016/S0968-0896(01)00103-1; PubMed=11504633 [NCBI, ExPASy, EBI, Israel, Japan]
Crabtree D.V., Ojima I., Geng X., Adler A.J.;
"Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site.";
Bioorg. Med. Chem. 9:1967-1976(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Yu W., Gibbs R.A.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
"Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, Lung, Muscle, and Placenta;
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).
[9]
PROTEIN SEQUENCE OF 3-19; 47-58; 63-77; 104-121; 163-174; 242-251; 253-276; 283-297; 310-318; 325-336 AND 381-390, AND MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[11]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-324, AND MASS SPECTROMETRY.
DOI=10.1021/pr800468j; PubMed=18781797 [NCBI, ExPASy, EBI, Israel, Japan]
Meierhofer D., Wang X., Huang L., Kaiser P.;
"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.";
J. Proteome Res. 7:4566-4576(2008).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
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
J00314; AAB59507.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF141349; AAD33873.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF070561; AAC28642.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF070593; AAC28650.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF070600; AAC28654.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000025; BAB63321.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB088100; BAC54932.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB062393; BAB93480.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001938; AAH01938.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002347; AAH02347.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005838; AAH05838.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007605; AAH07605.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013374; AAH13374.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019924; AAH19924.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020946; AAH20946.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021909; AAH21909.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070326; AAH70326.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00011654; -.
PIR A26561; A26561.
RefSeq NP_821133.1; -.
UniGene Hs.636480
3D structure databases
HSSP P02554; 1FFX. [HSSP ENTRY / PDB]
SMR P07437; 2-427.
ModBase P07437.
Protein-protein interaction databases
IntAct P07437; 41.
PTM databases
PhosphoSite P07437; -.
2D gel databases
SWISS-2DPAGE P07437; -.
Cornea-2DPAGE P07437; -.
OGP P07437; -.
REPRODUCTION-2DPAGE P07437; -.
Organism-specific databases
GeneCards GC06P030797; -.
GC13M040856; -.
H-InvDB HIX0005701; -.
HIX0057935; -.
HIX0058104; -.
HGNC HGNC:20778; TUBB.
GenAtlas TUBB.
HPA CAB005417; -.
CAB012406; -.
MIM 191130; gene. [NCBI / EBI]
PharmGKB PA358; -.
Gene expression databases
ArrayExpress P07437; -.
Bgee P07437; -.
CleanEx HS_TUBB; -.
GermOnline ENSG00000196230; Homo sapiens.
Ontologies
GO
GO:0005874; Cellular component: microtubule (inferred from electronic annotation from UniProtKB-KW).
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:0042288; Molecular function: MHC class I protein binding (inferred from direct assay from UniProtKB).
GO:0006928; Biological process: cell motion (traceable author statement from UniProtKB).
GO:0007018; Biological process: microtubule-based movement (inferred from electronic annotation from InterPro).
GO:0042267; Biological process: natural killer cell mediated cytotoxicity (non-traceable author statement from UniProtKB).
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 P07437; -.
Genome annotation databases
Ensembl ENSG00000137379; Homo sapiens. [Contig view]
ENSG00000183311; Homo sapiens. [Contig view]
ENSG00000196230; Homo sapiens. [Contig view]
GeneID 203068; -.
KEGG hsa:203068; -.
Phylogenomic databases
HOVERGEN P07437; -.
OMA P07437; DQLARIN.
Other
DrugBank DB01394; Colchicine.
DB00570; Vinblastine.
DB00541; Vincristine.
DB00361; Vinorelbine.
NextBio 90324; -.
SOURCE TUBB; Homo sapiens.
ProtoNet P07437.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; GTP-binding; Isopeptide bond; Microtubule; Nucleotide-binding; Phosphoprotein; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   444  444     Tubulin beta chain. PRO_0000048243
NP_BIND   140   146  7     GTP (Potential). 
MOD_RES   36    36        Phosphotyrosine. 
MOD_RES   340   340        Phosphotyrosine (By similarity). 
CROSSLNK   58    58        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   324   324        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CONFLICT   216   216        K -> R (in Ref. 1 and 2). 
CONFLICT   231   231        A -> G (in Ref. 1 and 2). 
CONFLICT   234   235        SG -> EC (in Ref. 1 and 2). 
CONFLICT   288   288        E -> D (in Ref. 1 and 2). 
CONFLICT   298   298        N -> D (in Ref. 8; AAH20946). 
Sequence information
Length: 444 AA [This is the length of the unprocessed precursor] Molecular weight: 49671 Da [This is the MW of the unprocessed precursor] CRC64: 1E6CD0A36773A103 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY YNEATGGKYV 

        70         80         90        100        110        120 
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 

       130        140        150        160        170        180 
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV 

       190        200        210        220        230        240 
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL 

       250        260        270        280        290        300 
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM 

       310        320        330        340        350        360 
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG 

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

       430        440 
EYQQYQDATA EEEEDFGEEA EEEA 

P07437 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!