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Q15750 (TAB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
Alternative name(s):
Mitogen-activated protein kinase kinase kinase 7-interacting protein 1
TGF-beta-activated kinase 1-binding protein 1
Short name=TAK1-binding protein 1
Gene names
Name:TAB1
Synonyms:MAP3K7IP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be an important signaling intermediate between TGFB receptors and MAP3K7/TAK1. May play an important role in mammalian embryogenesis. Ref.15

Subunit structure

Interacts with XIAP and BIRC7. Interacts with TRAF6 and MAP3K7; during IL-1 signaling. Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2. Ref.1 Ref.7 Ref.8

Tissue specificity

Ubiquitous.

Post-translational modification

Monoubiquitinated. Deubiquitinated by Y.enterocolitica YopP.

Sequence similarities

Contains 1 PP2C-like domain.

Caution

Lacks several key residues involved in metal-binding and catalytic activity, therefore has lost phosphatase activity.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

I-kappaB kinase/NF-kappaB signaling

Traceable author statement. Source: Reactome

JNK cascade

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement. Source: Reactome

activation of MAPKKK activity

Traceable author statement Ref.1. Source: ProtInc

heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

lung development

Inferred from electronic annotation. Source: Ensembl

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement. Source: Reactome

positive regulation of NF-kappaB transcription factor activity

Traceable author statement. Source: Reactome

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

endosome membrane

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncatalytic activity

Inferred from electronic annotation. Source: InterPro

enzyme activator activity

Traceable author statement Ref.1. Source: ProtInc

kinase activator activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.7Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15750-1)

Also known as: TAB1alpha;

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: Q15750-2)

Also known as: TAB1beta;

The sequence of this isoform differs from the canonical sequence as follows:
     436-504: NQSPTLTLQS...HGEQSVVTAP → KDPSRPASDLTAIPQCQLNLLGSLTPG
Note: Does not bind nor activate MAP3K7/TAK1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
PRO_0000057797

Regions

Domain64 – 368305PP2C-like
Compositional bias452 – 4576Poly-Ser

Amino acid modifications

Modified residue71Phosphoserine Ref.10 Ref.11
Modified residue3781Phosphoserine Ref.12
Modified residue4381Phosphoserine Ref.9

Natural variations

Alternative sequence436 – 50469NQSPT…VVTAP → KDPSRPASDLTAIPQCQLNL LGSLTPG in isoform 2.
VSP_042024
Natural variant2241D → E.
Corresponds to variant rs17001096 [ dbSNP | Ensembl ].
VAR_039271

Experimental info

Mutagenesis2131D → A: Loss of interaction with XIAP. Ref.16
Mutagenesis2161F → A: Loss of interaction with XIAP. Ref.16
Mutagenesis4381S → A: Loss of phosphorylation site. Ref.9

Secondary structure

....................................................................... 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TAB1alpha) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A45743288718983A

FASTA50454,644
        10         20         30         40         50         60 
MAAQRRSLLQ SEQQPSWTDD LPLCHLSGVG SASNRSYSAD GKGTESHPPE DSWLKFRSEN 

        70         80         90        100        110        120 
NCFLYGVFNG YDGNRVTNFV AQRLSAELLL GQLNAEHAEA DVRRVLLQAF DVVERSFLES 

       130        140        150        160        170        180 
IDDALAEKAS LQSQLPEGVP QHQLPPQYQK ILERLKTLER EISGGAMAVV AVLLNNKLYV 

       190        200        210        220        230        240 
ANVGTNRALL CKSTVDGLQV TQLNVDHTTE NEDELFRLSQ LGLDAGKIKQ VGIICGQEST 

       250        260        270        280        290        300 
RRIGDYKVKY GYTDIDLLSA AKSKPIIAEP EIHGAQPLDG VTGFLVLMSE GLYKALEAAH 

       310        320        330        340        350        360 
GPGQANQEIA AMIDTEFAKQ TSLDAVAQAV VDRVKRIHSD TFASGGERAR FCPRHEDMTL 

       370        380        390        400        410        420 
LVRNFGYPLG EMSQPTPSPA PAAGGRVYPV SVPYSSAQST SKTSVTLSLV MPSQGQMVNG 

       430        440        450        460        470        480 
AHSASTLDEA TPTLTNQSPT LTLQSTNTHT QSSSSSSDGG LFRSRPAHSL PPGEDGRVEP 

       490        500 
YVDFAEFYRL WSVDHGEQSV VTAP 

« Hide

Isoform 2 (TAB1beta) [UniParc].

Checksum: E26443BBE3BD3404
Show »

FASTA46249,917

References

« Hide 'large scale' references
[1]"TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction."
Shibuya H., Yamaguchi K., Shirakabe K., Tonegawa A., Gotoh Y., Ueno N., Irie K., Nishida E., Matsumoto K.
Science 272:1179-1182(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MAP3K7.
Tissue: Brain.
[2]"TAB1beta (transforming growth factor-beta-activated protein kinase 1-binding protein 1beta), a novel splicing variant of TAB1 that interacts with p38alpha but not TAK1."
Ge B., Xiong X., Jing Q., Mosley J.L., Filose A., Bian D., Huang S., Han J.
J. Biol. Chem. 278:2286-2293(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton 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: PNS.
[7]"The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway."
Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K.
Nature 398:252-256(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF6 AND MAP3K7.
[8]"TAK1 is a ubiquitin-dependent kinase of MKK and IKK."
Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.
Nature 412:346-351(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, IDENTIFICATION IN THE TRIKA2 COMPLEX.
[9]"The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway."
Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K., Autenrieth I., Bohn E., Sakurai H., Niedenthal R., Resch K., Kracht M.
EMBO Rep. 7:838-844(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, PHOSPHORYLATION AT SER-438, MUTAGENESIS OF SER-438, DEUBIQUITINATION BY YOPP.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"TAK1-binding protein 1 is a pseudophosphatase."
Conner S.H., Kular G., Peggie M., Shepherd S., Schuettelkopf A.W., Cohen P., Van Aalten D.M.F.
Biochem. J. 399:427-434(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-401, ABSENCE OF FUNCTION AS A PHOSPHATASE.
[16]"XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization."
Lu M., Lin S.-C., Huang Y., Kang Y.J., Rich R., Lo Y.-C., Myszka D., Han J., Wu H.
Mol. Cell 26:689-702(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1-370 IN COMPLEX WITH XIAP, MUTAGENESIS OF ASP-213 AND PHE-216.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49928 mRNA. Translation: AAC12660.1.
AF425640 mRNA. Translation: AAN32760.1.
DQ314876 Genomic DNA. Translation: ABC40735.1.
AL022312 Genomic DNA. No translation available.
Z83845 Genomic DNA. Translation: CAB55304.1.
Z83845 Genomic DNA. Translation: CAQ07045.1.
CH471095 Genomic DNA. Translation: EAW60326.1.
BC050554 mRNA. Translation: AAH50554.1.
CCDSCCDS13992.1. [Q15750-2]
CCDS13993.1. [Q15750-1]
RefSeqNP_006107.1. NM_006116.2. [Q15750-1]
NP_705717.1. NM_153497.2. [Q15750-2]
UniGeneHs.507681.
Hs.729080.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J4OX-ray2.25A1-401[»]
2POMX-ray2.27A1-370[»]
2POPX-ray3.10A/C1-370[»]
2YDSX-ray2.55T392-398[»]
2YIYX-ray2.49A468-497[»]
4AY5X-ray3.15I/J/K/L389-399[»]
4AY6X-ray3.30E/F/G/H389-401[»]
4GS6X-ray2.20A468-504[»]
4KA3X-ray2.71B395-415[»]
4L3PX-ray2.68A468-504[»]
4L53X-ray2.55A468-496[»]
ProteinModelPortalQ15750.
SMRQ15750. Positions 16-370, 468-496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115717. 81 interactions.
DIPDIP-27524N.
IntActQ15750. 67 interactions.
MINTMINT-88613.

Chemistry

BindingDBQ15750.
ChEMBLCHEMBL5605.

PTM databases

PhosphoSiteQ15750.

Polymorphism databases

DMDM10720303.

Proteomic databases

MaxQBQ15750.
PaxDbQ15750.
PRIDEQ15750.

Protocols and materials databases

DNASU10454.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216160; ENSP00000216160; ENSG00000100324. [Q15750-1]
ENST00000331454; ENSP00000333049; ENSG00000100324. [Q15750-2]
GeneID10454.
KEGGhsa:10454.
UCSCuc003axt.3. human. [Q15750-1]
uc003axu.1. human. [Q15750-2]

Organism-specific databases

CTD10454.
GeneCardsGC22P039796.
HGNCHGNC:18157. TAB1.
HPACAB032328.
HPA039988.
MIM602615. gene.
neXtProtNX_Q15750.
PharmGKBPA30604.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320352.
HOGENOMHOG000044226.
HOVERGENHBG007302.
InParanoidQ15750.
KOK04403.
OMASHPPEDN.
OrthoDBEOG7W41C0.
PhylomeDBQ15750.
TreeFamTF317785.

Enzyme and pathway databases

ReactomeREACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkQ15750.

Gene expression databases

ArrayExpressQ15750.
BgeeQ15750.
CleanExHS_MAP3K7IP1.
GenevestigatorQ15750.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 2 hits.
ProtoNetSearch...

Other

ChiTaRSTAB1. human.
EvolutionaryTraceQ15750.
GeneWikiMAP3K7IP1.
GenomeRNAi10454.
NextBio39627.
PROQ15750.
SOURCESearch...

Entry information

Entry nameTAB1_HUMAN
AccessionPrimary (citable) accession number: Q15750
Secondary accession number(s): Q2PP09, Q8IZW2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 140 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 22

Human chromosome 22: entries, gene names and cross-references to MIM