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Q9H0M0 (WWP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NEDD4-like E3 ubiquitin-protein ligase WWP1

EC=6.3.2.-
Alternative name(s):
Atrophin-1-interacting protein 5
Short name=AIP5
TGIF-interacting ubiquitin ligase 1
Short name=Tiul1
WW domain-containing protein 1
Gene names
Name:WWP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length922 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF. Ref.3 Ref.9 Ref.14

Enzyme regulation

Activated by NDFIP1- and NDFIP2-binding.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Binds KLF2 AND HIVEP3 By similarity. Binds SCNN1A, SCNN1B, SCNN1G, WBP1, WBP2, DRPLA and adenovirus type 2 PIII. Interacts with RNF11 By similarity. Interacts with SPG20. Interacts with ERBB4 isoforms JM-B CYT-1 and JM-A CYT-1. Interacts with SMAD1, SMAD2, SMAD3, SMAD5, SMAD6, SMAD7, TGFBR1 AND TGFBR2. Associates with the TGFBR1:TGFBR2 receptor complex in presence of SMAD7. Interacts with SKIL isoform 1. Interacts with TP63 isoform 1 and isoform 2. Interacts with STAMBP and RNF11. Interacts with NDFIP1 and NDFIP2 Probable; this interaction activates the E3 ubiquitin-protein ligase. Interacts with TGIF. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13

Subcellular location

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity. Nucleus By similarity.

Tissue specificity

Detected in heart, placenta, pancreas, kidney, liver, skeletal muscle, bone marrow, fetal brain, and at much lower levels in adult brain and lung. Isoform 1 and isoform 5 predominate in all tissues tested, except in testis and bone marrow, where isoform 5 is expressed at much higher levels than isoform 1. Ref.2 Ref.7

Post-translational modification

Auto-ubiquitinated and ubiquitinated by RNF11.

Sequence similarities

Contains 1 C2 domain.

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.

Contains 4 WW domains.

Ontologies

Keywords
   Biological processHost-virus interaction
Ubl conjugation pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionLigase
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcentral nervous system development

Non-traceable author statement Ref.7. Source: UniProtKB

ion transmembrane transport

Traceable author statement. Source: Reactome

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Traceable author statement Ref.14. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transduction

Non-traceable author statement Ref.6. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

viral entry into host cell

Traceable author statement Ref.8. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

ubiquitin ligase complex

Non-traceable author statement Ref.6. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.11Ref.7. Source: UniProtKB

ubiquitin-protein transferase activity

Traceable author statement Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CPSF6Q166303EBI-742157,EBI-358410

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9H0M0-1)

Also known as: A;

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: Q9H0M0-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     112-120: LERVKEQLK → CWLLKARME
     121-922: Missing.
Isoform 3 (identifier: Q9H0M0-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     112-242: LERVKEQLKL...LASEPADDTV → F
Isoform 4 (identifier: Q9H0M0-4)

Also known as: D;

The sequence of this isoform is not available.
Isoform 5 (identifier: Q9H0M0-5)

Also known as: E;

The sequence of this isoform is not available.
Isoform 6 (identifier: Q9H0M0-6)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     23-240: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 922922NEDD4-like E3 ubiquitin-protein ligase WWP1
PRO_0000120336

Regions

Domain5 – 9894C2
Domain349 – 38234WW 1
Domain381 – 41434WW 2
Domain456 – 48934WW 3
Domain496 – 52934WW 4
Domain588 – 922335HECT

Sites

Active site8901Glycyl thioester intermediate By similarity
Site8901Required for ubiquitin-thioester formation By similarity

Natural variations

Alternative sequence23 – 240218Missing in isoform 6.
VSP_007600
Alternative sequence112 – 242131LERVK…ADDTV → F in isoform 3.
VSP_007602
Alternative sequence112 – 1209LERVKEQLK → CWLLKARME in isoform 2.
VSP_007601
Alternative sequence121 – 922802Missing in isoform 2.
VSP_007603
Natural variant8521G → V.
Corresponds to variant rs1059901 [ dbSNP | Ensembl ].
VAR_052960

Experimental info

Mutagenesis6141E → A: Reduces ubiquitin transfer. Ref.14
Mutagenesis6211H → A: Strongly reduces ubiquitin transfer. Ref.14
Mutagenesis6751D → A: Reduces ubiquitin transfer. Ref.14
Mutagenesis7981E → A: Reduces ubiquitin transfer. Strongly reduces ubiquitin transfer; when associated with A-845. Ref.14
Mutagenesis8041M → P: Strongly reduces ubiquitin transfer; when associated with P-806. Ref.14
Mutagenesis8061E → P: Strongly reduces ubiquitin transfer; when associated with P-804. Ref.14
Mutagenesis8451R → A: No effect. Ref.14
Mutagenesis8481Q → A: Abolishes ubiquitin transfer; when associated with A-855. Ref.14
Mutagenesis8551R → A: Abolishes ubiquitin transfer; when associated with A-848. Ref.14

Secondary structure

......................................................................... 922
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 35B6E1C03A3147DA

FASTA922105,202
        10         20         30         40         50         60 
MATASPRSDT SNNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVVVDGEI TKTAKSSSSS 

        70         80         90        100        110        120 
NPKWDEQLTV NVTPQTTLEF QVWSHRTLKA DALLGKATID LKQALLIHNR KLERVKEQLK 

       130        140        150        160        170        180 
LSLENKNGIA QTGELTVVLD GLVIEQENIT NCSSSPTIEI QENGDALHEN GEPSARTTAR 

       190        200        210        220        230        240 
LAVEGTNGID NHVPTSTLVQ NSCCSYVVNG DNTPSSPSQV AARPKNTPAP KPLASEPADD 

       250        260        270        280        290        300 
TVNGESSSFA PTDNASVTGT PVVSEENALS PNCTSTTVED PPVQEILTSS ENNECIPSTS 

       310        320        330        340        350        360 
AELESEARSI LEPDTSNSRS SSAFEAAKSR QPDGCMDPVR QQSGNANTET LPSGWEQRKD 

       370        380        390        400        410        420 
PHGRTYYVDH NTRTTTWERP QPLPPGWERR VDDRRRVYYV DHNTRTTTWQ RPTMESVRNF 

       430        440        450        460        470        480 
EQWQSQRNQL QGAMQQFNQR YLYSASMLAA ENDPYGPLPP GWEKRVDSTD RVYFVNHNTK 

       490        500        510        520        530        540 
TTQWEDPRTQ GLQNEEPLPE GWEIRYTREG VRYFVDHNTR TTTFKDPRNG KSSVTKGGPQ 

       550        560        570        580        590        600 
IAYERGFRWK LAHFRYLCQS NALPSHVKIN VSRQTLFEDS FQQIMALKPY DLRRRLYVIF 

       610        620        630        640        650        660 
RGEEGLDYGG LAREWFFLLS HEVLNPMYCL FEYAGKNNYC LQINPASTIN PDHLSYFCFI 

       670        680        690        700        710        720 
GRFIAMALFH GKFIDTGFSL PFYKRMLSKK LTIKDLESID TEFYNSLIWI RDNNIEECGL 

       730        740        750        760        770        780 
EMYFSVDMEI LGKVTSHDLK LGGSNILVTE ENKDEYIGLM TEWRFSRGVQ EQTKAFLDGF 

       790        800        810        820        830        840 
NEVVPLQWLQ YFDEKELEVM LCGMQEVDLA DWQRNTVYRH YTRNSKQIIW FWQFVKETDN 

       850        860        870        880        890        900 
EVRMRLLQFV TGTCRLPLGG FAELMGSNGP QKFCIEKVGK DTWLPRSHTC FNRLDLPPYK 

       910        920 
SYEQLKEKLL FAIEETEGFG QE 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 952B6A78C5D4B93D
Show »

FASTA12013,453
Isoform 3 (C) [UniParc].

Checksum: 833D351CC08D9998
Show »

FASTA79291,548
Isoform 4 (D) (Sequence not available).
Isoform 5 (E) (Sequence not available).
Isoform 6 (F) [UniParc].

Checksum: B39DCB6841290CF0
Show »

FASTA70481,649

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[2]"Alternative splicing determines the domain structure of WWP1, a Nedd4 family protein."
Flasza M., Gorman P., Roylance R., Canfield A.E., Baron M.
Biochem. Biophys. Res. Commun. 290:431-437(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), TISSUE SPECIFICITY.
Tissue: Mammary cancer.
[3]"The novel E3 ubiquitin ligase Tiul1 associates with TGIF to target Smad2 for degradation."
Seo S.R., Lallemand F., Ferrand N., Pessah M., L'Hoste S., Camonis J., Atfi A.
EMBO J. 23:3780-3792(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, UBIQUITINATION OF SMAD2 AND TGFBR1, INTERACTION WITH SMAD7 AND TGIF.
[4]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Lung and Testis.
[6]"Identification of novel human WW domain-containing proteins by cloning of ligand targets."
Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B., Kay B.K., Fowlkes D.M.
J. Biol. Chem. 272:14611-14616(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 191-870, INTERACTION WITH WBP1; WBP2; SCNN1A; SCNN1B AND SCNN1G.
Tissue: Bone marrow and Brain.
[7]"Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins."
Wood J.D., Yuan J., Margolis R.L., Colomer V., Duan K., Kushi J., Kaminsky Z., Kleiderlein J.J. Jr., Sharp A.H., Ross C.A.
Mol. Cell. Neurosci. 11:149-160(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DRPLA, TISSUE SPECIFICITY.
[8]"Adenovirus protein involved in virus internalization recruits ubiquitin-protein ligases."
Galinier R., Gout E., Lortat-Jacob H., Wood J., Chroboczek J.
Biochemistry 41:14299-14305(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIII.
[9]"Negative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1)."
Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K., Miyazawa K.
Oncogene 23:6914-6923(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF TGFBR1; SMAD6 AND SMAD7, INTERACTION WITH SMAD1; SMAD2; SMAD3; SMAD5; SMAD6; SMAD7; TGFBR1; TGFBR2 AND SKIL.
[10]"The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11."
Chen C., Zhou Z., Liu R., Li Y., Azmi P.B., Seth A.K.
Oncogene 27:6845-6855(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOUBIQUITINATION.
[11]"Endogenous spartin (SPG20) is recruited to endosomes and lipid droplets and interacts with the ubiquitin E3 ligases AIP4 and AIP5."
Edwards T.L., Clowes V.E., Tsang H.T., Connell J.W., Sanderson C.M., Luzio J.P., Reid E.
Biochem. J. 423:31-39(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPG20.
[12]"Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins."
Mund T., Pelham H.R.
EMBO Rep. 10:501-507(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION BY NDFIP1 AND NDFIP2, AUTOUBIQUITINATION.
[13]"WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer."
Li Y., Zhou Z., Alimandi M., Chen C.
Oncogene 28:2948-2958(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4.
[14]"Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase."
Verdecia M.A., Joazeiro C.A.P., Wells N.J., Ferrer J.-L., Bowman M.E., Hunter T., Noel J.P.
Mol. Cell 11:249-259(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 546-917, MUTAGENESIS OF GLU-614; HIS-621; ASP-675; GLU-798; MET-804; GLU-806; ARG-845; GLN-848 AND ARG-855, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL136739 mRNA. Translation: CAB66673.1.
AY043361 mRNA. Translation: AAK94668.1.
AY345857 mRNA. Translation: AAQ22764.1.
AC083845 Genomic DNA. No translation available.
AC103817 Genomic DNA. No translation available.
BC015380 mRNA. Translation: AAH15380.2.
BC036065 mRNA. Translation: AAH36065.1.
U96113 mRNA. Translation: AAC51324.1.
CCDSCCDS6242.1. [Q9H0M0-1]
RefSeqNP_008944.1. NM_007013.3. [Q9H0M0-1]
XP_005250817.1. XM_005250760.2. [Q9H0M0-1]
UniGeneHs.655189.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ND7X-ray2.10A546-917[»]
2OP7NMR-A494-532[»]
ProteinModelPortalQ9H0M0.
SMRQ9H0M0. Positions 19-145, 351-919.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116243. 57 interactions.
IntActQ9H0M0. 22 interactions.
MINTMINT-199541.
STRING9606.ENSP00000265428.

PTM databases

PhosphoSiteQ9H0M0.

Polymorphism databases

DMDM32171908.

Proteomic databases

MaxQBQ9H0M0.
PaxDbQ9H0M0.
PRIDEQ9H0M0.

Protocols and materials databases

DNASU11059.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265428; ENSP00000265428; ENSG00000123124. [Q9H0M0-1]
ENST00000341922; ENSP00000340564; ENSG00000123124. [Q9H0M0-3]
ENST00000349423; ENSP00000342665; ENSG00000123124. [Q9H0M0-6]
ENST00000517970; ENSP00000427793; ENSG00000123124. [Q9H0M0-1]
GeneID11059.
KEGGhsa:11059.
UCSCuc003ydt.3. human. [Q9H0M0-1]

Organism-specific databases

CTD11059.
GeneCardsGC08P087424.
HGNCHGNC:17004. WWP1.
HPAHPA023180.
MIM602307. gene.
neXtProtNX_Q9H0M0.
PharmGKBPA134960138.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5021.
HOGENOMHOG000208453.
HOVERGENHBG004134.
InParanoidQ9H0M0.
KOK05633.
OMAKNGIVQT.
OrthoDBEOG7RFTGT.
PhylomeDBQ9H0M0.
TreeFamTF323658.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_15518. Transmembrane transport of small molecules.
REACT_6900. Immune System.
SignaLinkQ9H0M0.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9H0M0.
BgeeQ9H0M0.
CleanExHS_WWP1.
GenevestigatorQ9H0M0.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view]
PIRSFPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 4 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 4 hits.
SSF56204. SSF56204. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWWP1. human.
EvolutionaryTraceQ9H0M0.
GeneWikiWWP1.
GenomeRNAi11059.
NextBio42019.
PROQ9H0M0.
SOURCESearch...

Entry information

Entry nameWWP1_HUMAN
AccessionPrimary (citable) accession number: Q9H0M0
Secondary accession number(s): O00307, Q5YLC1, Q96BP4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 133 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 8

Human chromosome 8: entries, gene names and cross-references to MIM