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Q86TM6 (SYVN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
E3 ubiquitin-protein ligase synoviolin

EC=6.3.2.-
Alternative name(s):
Synovial apoptosis inhibitor 1
Gene names
Name:SYVN1
Synonyms:HRD1, KIAA1810
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis. Ref.1 Ref.2 Ref.3 Ref.4 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.22

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer. Interacts with p53/TP53 and HTT. Interacts with VCP, HERPUD1 and DERL1. Part of a complex containing SYVN1, HERPUD1, VIMP and DERL1; which probably transfer misfolded proteins from the ER to VCP. Part of a complex containing SYVN1, SEL1L and DERL2. Interacts with UBXN6. Interacts with SEL1L; recruits ERLEC1 and OS9. May form a complex with ERLEC1; HSPA5; OS9 AND SEL1L. Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1 Ref.2 Ref.4 Ref.9.

Tissue specificity

Ubiquitously expressed, with highest levels in liver and kidney (at protein level). Up-regulated in synovial tissues from patients with rheumatoid arthritis (at protein level). Ref.1 Ref.2 Ref.3

Induction

By endoplasmic reticulum stress-inducing agents such as thapsigargin, tunicamycin or brefeldin A, but not by heat shock. Ref.1 Ref.4

Domain

The RING-type zinc finger is required for E3 ligase activity.

Post-translational modification

Not N-glycosylated. Ref.4

Auto-ubiquitinated.

Sequence similarities

Belongs to the HRD1 family.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence BAB47439.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processStress response
Ubl conjugation pathway
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from electronic annotation. Source: Ensembl

protein N-linked glycosylation via asparagine

Inferred from mutant phenotype Ref.22. Source: UniProtKB

protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.1. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionacid-amino acid ligase activity

Inferred from direct assay Ref.1. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86TM6-1)

Also known as: b; long;

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: Q86TM6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     127-177: Missing.
     411-411: Missing.
Isoform 3 (identifier: Q86TM6-3)

Also known as: a; short;

The sequence of this isoform differs from the canonical sequence as follows:
     411-411: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 617595E3 ubiquitin-protein ligase synoviolin
PRO_0000280548

Regions

Topological domain23 – 4119Lumenal Potential
Transmembrane42 – 6221Helical; Potential
Topological domain63 – 9836Cytoplasmic Potential
Transmembrane99 – 11921Helical; Potential
Topological domain120 – 14021Lumenal Potential
Transmembrane141 – 16121Helical; Potential
Topological domain162 – 1698Cytoplasmic Potential
Transmembrane170 – 19021Helical; Potential
Topological domain191 – 22434Lumenal Potential
Transmembrane225 – 24521Helical; Potential
Topological domain246 – 617372Cytoplasmic Potential
Zinc finger291 – 33040RING-type; atypical
Region236 – 27035Interaction with p53/TP53
Compositional bias339 – 478140Pro-rich

Amino acid modifications

Modified residue6131Phosphoserine Ref.17 Ref.20

Natural variations

Alternative sequence127 – 17751Missing in isoform 2.
VSP_023777
Alternative sequence4111Missing in isoform 2 and isoform 3.
VSP_023778

Experimental info

Mutagenesis3291C → S: Abolishes E3 ligase activity. Ref.1
Sequence conflict1451M → I in BAC24801. Ref.1
Sequence conflict1451M → I in AAL26903. Ref.4
Sequence conflict5451E → G in BAC57449. Ref.3

Sequences

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

Last modified March 20, 2007. Version 2.
Checksum: B8A6BACBAF9673C1

FASTA61767,685
        10         20         30         40         50         60 
MFRTAVMMAA SLALTGAVVA HAYYLKHQFY PTVVYLTKSS PSMAVLYIQA FVLVFLLGKV 

        70         80         90        100        110        120 
MGKVFFGQLR AAEMEHLLER SWYAVTETCL AFTVFRDDFS PRFVALFTLL LFLKCFHWLA 

       130        140        150        160        170        180 
EDRVDFMERS PNISWLFHCR IVSLMFLLGI LDFLFVSHAY HSILTRGASV QLVFGFEYAI 

       190        200        210        220        230        240 
LMTMVLTIFI KYVLHSVDLQ SENPWDNKAV YMLYTELFTG FIKVLLYMAF MTIMIKVHTF 

       250        260        270        280        290        300 
PLFAIRPMYL AMRQFKKAVT DAIMSRRAIR NMNTLYPDAT PEELQAMDNV CIICREEMVT 

       310        320        330        340        350        360 
GAKRLPCNHI FHTSCLRSWF QRQQTCPTCR MDVLRASLPA QSPPPPEPAD QGPPPAPHPP 

       370        380        390        400        410        420 
PLLPQPPNFP QGLLPPFPPG MFPLWPPMGP FPPVPPPPSS GEAVAPPSTS AAALSRPSGA 

       430        440        450        460        470        480 
ATTTAAGTSA TAASATASGP GSGSAPEAGP APGFPFPPPW MGMPLPPPFA FPPMPVPPAG 

       490        500        510        520        530        540 
FAGLTPEELR ALEGHERQHL EARLQSLRNI HTLLDAAMLQ INQYLTVLAS LGPPRPATSV 

       550        560        570        580        590        600 
NSTEETATTV VAAASSTSIP SSEATTPTPG ASPPAPEMER PPAPESVGTE EMPEDGEPDA 

       610 
AELRRRRLQK LESPVAH 

« Hide

Isoform 2 [UniParc].

Checksum: 8C2226662D099D15
Show »

FASTA56561,732
Isoform 3 (a) (short) [UniParc].

Checksum: 3D035485BDF67376
Show »

FASTA61667,614

References

« Hide 'large scale' references
[1]"Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation."
Kaneko M., Ishiguro M., Niinuma Y., Uesugi M., Nomura Y.
FEBS Lett. 532:147-152(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-329, INDUCTION BY ER STRESS, AUTOUBIQUITINATION.
[2]"A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1."
Nadav E., Shmueli A., Barr H., Gonen H., Ciechanover A., Reiss Y.
Biochem. Biophys. Res. Commun. 303:91-97(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AUTOUBIQUITINATION.
[3]"Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy."
Amano T., Yamasaki S., Yagishita N., Tsuchimochi K., Shin H., Kawahara K., Aratani S., Fujita H., Zhang L., Ikeda R., Fujii R., Miura N., Komiya S., Nishioka K., Maruyama I., Fukamizu A., Nakajima T.
Genes Dev. 17:2436-2449(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AUTOUBIQUITINATION.
Tissue: Articular cartilage.
[4]"Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum."
Kikkert M., Doolman R., Dai M., Avner R., Hassink G., van Voorden S., Thanedar S., Roitelman J., Chau V., Wiertz E.
J. Biol. Chem. 279:3525-3534(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INDUCTION BY ER STRESS, LACK OF GLYCOSYLATION, SUBCELLULAR LOCATION, TOPOLOGY.
[5]"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Amygdala.
[7]"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: Blood.
[8]"The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway."
Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E., Koning F., Kloetzel P.-M., Seeger M.
J. Mol. Biol. 354:1021-1027(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH VCP; HERPUD1 AND DERL1, IDENTIFICATION IN A COMPLEX WITH HERPUD1; VIMP AND DERL1.
[9]"Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane."
Ye Y., Shibata Y., Kikkert M., van Voorden S., Wiertz E., Rapoport T.A.
Proc. Natl. Acad. Sci. U.S.A. 102:14132-14138(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VCP, SUBCELLULAR LOCATION.
[10]"Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane."
Lilley B.N., Ploegh H.L.
Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH DERL2 AND SEL1L, INTERACTION WITH SEL1L.
[11]"A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin."
Omura T., Kaneko M., Okuma Y., Orba Y., Nagashima K., Takahashi R., Fujitani N., Matsumura S., Hata A., Kubota K., Murahashi K., Uehara T., Nomura Y.
J. Neurochem. 99:1456-1469(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery."
Arteaga M.F., Wang L., Ravid T., Hochstrasser M., Canessa C.M.
Proc. Natl. Acad. Sci. U.S.A. 103:11178-11183(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'."
Yamasaki S., Yagishita N., Sasaki T., Nakazawa M., Kato Y., Yamadera T., Bae E., Toriyama S., Ikeda R., Zhang L., Fujitani K., Yoo E., Tsuchimochi K., Ohta T., Araya N., Fujita H., Aratani S., Eguchi K. expand/collapse author list , Komiya S., Maruyama I., Higashi N., Sato M., Senoo H., Ochi T., Yokoyama S., Amano T., Kim J., Gay S., Fukamizu A., Nishioka K., Tanaka K., Nakajima T.
EMBO J. 26:113-122(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53.
[14]"Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin."
Yang H., Zhong X., Ballar P., Luo S., Shen Y., Rubinsztein D.C., Monteiro M.J., Fang S.
Exp. Cell Res. 313:538-550(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HTT.
[15]"Ubxd1 is a novel co-factor of the human p97 ATPase."
Madsen L., Andersen K.M., Prag S., Moos T., Semple C.A., Seeger M., Hartmann-Petersen R.
Int. J. Biochem. Cell Biol. 40:2927-2942(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBXN6.
[16]"Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP."
Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.
J. Biol. Chem. 283:20914-20924(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERLEC1; HSPA5; OS9 AND SEL1L.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD."
Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.
Nat. Cell Biol. 10:272-282(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERLEC1; OS9 AND SEL1L.
[19]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
[22]"STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein."
Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H., Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T., Morino-Koga S., Wada I., Kai H.
Mol. Cell 47:99-110(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ERAD PATHWAY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB085847 mRNA. Translation: BAC24801.1.
AB024690 mRNA. Translation: BAC57449.1.
AF317634 mRNA. Translation: AAL26903.1.
AB058713 mRNA. Translation: BAB47439.1. Different initiation.
AL834262 mRNA. Translation: CAD38937.1.
BC030530 mRNA. Translation: AAH30530.1.
RefSeqNP_115807.1. NM_032431.2.
NP_757385.1. NM_172230.2.
UniGeneHs.75859.

3D structure databases

ProteinModelPortalQ86TM6.
SMRQ86TM6. Positions 291-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124085. 51 interactions.
IntActQ86TM6. 17 interactions.
MINTMINT-4052103.
STRING9606.ENSP00000366395.

PTM databases

PhosphoSiteQ86TM6.

Polymorphism databases

DMDM134035039.

Proteomic databases

PaxDbQ86TM6.
PRIDEQ86TM6.

Protocols and materials databases

DNASU84447.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294256; ENSP00000294256; ENSG00000162298. [Q86TM6-3]
ENST00000307289; ENSP00000302035; ENSG00000162298. [Q86TM6-2]
ENST00000377190; ENSP00000366395; ENSG00000162298. [Q86TM6-1]
ENST00000526060; ENSP00000436984; ENSG00000162298. [Q86TM6-3]
GeneID84447.
KEGGhsa:84447.
UCSCuc001odb.3. human. [Q86TM6-1]
uc001odc.3. human. [Q86TM6-3]
uc009yqc.3. human. [Q86TM6-2]

Organism-specific databases

CTD84447.
GeneCardsGC11M064894.
HGNCHGNC:20738. SYVN1.
HPAHPA005480.
HPA024300.
MIM608046. gene.
neXtProtNX_Q86TM6.
PharmGKBPA128394735.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5243.
HOGENOMHOG000294196.
HOVERGENHBG094015.
InParanoidQ86TM6.
KOK10601.
OMAHHYLSTV.
OrthoDBEOG7V766G.
PhylomeDBQ86TM6.
TreeFamTF318635.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ86TM6.
BgeeQ86TM6.
CleanExHS_SYVN1.
GenevestigatorQ86TM6.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSYVN1. human.
GeneWikiSYVN1.
GenomeRNAi84447.
NextBio74217.
PROQ86TM6.
SOURCESearch...

Entry information

Entry nameSYVN1_HUMAN
AccessionPrimary (citable) accession number: Q86TM6
Secondary accession number(s): Q8N3K3 expand/collapse secondary AC list , Q8N6E8, Q96JL5, Q96PK3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 110 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM