Q86TM6 (SYVN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase synoviolin
EC=6.3.2.-

Alternative name(s):
Synovial apoptosis inhibitor 1

Gene names

Name:	SYVN1
Synonyms:	HRD1, KIAA1810

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	617 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Stress response Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated 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 in utero embryonic development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara protein N-linked glycosylation via asparagine Inferred from mutant phenotype Ref.22. Source: UniProtKB protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA
Molecular_function	acid-amino acid ligase activity Inferred from direct assay Ref.1. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 617	595	E3 ubiquitin-protein ligase synoviolin		PRO_0000280548
Regions
	Topological domain	23 – 41	19	Lumenal Potential
	Transmembrane	42 – 62	21	Helical; Potential
	Topological domain	63 – 98	36	Cytoplasmic Potential
	Transmembrane	99 – 119	21	Helical; Potential
	Topological domain	120 – 140	21	Lumenal Potential
	Transmembrane	141 – 161	21	Helical; Potential
	Topological domain	162 – 169	8	Cytoplasmic Potential
	Transmembrane	170 – 190	21	Helical; Potential
	Topological domain	191 – 224	34	Lumenal Potential
	Transmembrane	225 – 245	21	Helical; Potential
	Topological domain	246 – 617	372	Cytoplasmic Potential
	Zinc finger	291 – 330	40	RING-type; atypical
	Region	236 – 270	35	Interaction with p53/TP53
	Compositional bias	339 – 478	140	Pro-rich
Amino acid modifications
	Modified residue	613	1	Phosphoserine Ref.17 Ref.20
Natural variations
	Alternative sequence	127 – 177	51	Missing in isoform 2.		VSP_023777
	Alternative sequence	411	1	Missing in isoform 2 and isoform 3.		VSP_023778
Experimental info
	Mutagenesis	329	1	C → S: Abolishes E3 ligase activity. Ref.1
	Sequence conflict	145	1	M → I in BAC24801. Ref.1
	Sequence conflict	145	1	M → I in AAL26903. Ref.4
	Sequence conflict	545	1	E → G in BAC57449. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (b) (long) [UniParc]. Last modified March 20, 2007. Version 2. Checksum: B8A6BACBAF9673C1	FASTA	617	67,685
	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
	Isoform 2 [UniParc]. Checksum: 8C2226662D099D15	FASTA	565	61,732
	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 EDRVDFYAIL MTMVLTIFIK YVLHSVDLQS ENPWDNKAVY MLYTELFTGF IKVLLYMAFM 190 200 210 220 230 240 TIMIKVHTFP LFAIRPMYLA MRQFKKAVTD AIMSRRAIRN MNTLYPDATP EELQAMDNVC 250 260 270 280 290 300 IICREEMVTG AKRLPCNHIF HTSCLRSWFQ RQQTCPTCRM DVLRASLPAQ SPPPPEPADQ 310 320 330 340 350 360 GPPPAPHPPP LLPQPPNFPQ GLLPPFPPGM FPLWPPMGPF PPVPPPPSSG EAVAPPSTSA 370 380 390 400 410 420 ALSRPSGAAT TTAAGTSATA ASATASGPGS GSAPEAGPAP GFPFPPPWMG MPLPPPFAFP 430 440 450 460 470 480 PMPVPPAGFA GLTPEELRAL EGHERQHLEA RLQSLRNIHT LLDAAMLQIN QYLTVLASLG 490 500 510 520 530 540 PPRPATSVNS TEETATTVVA AASSTSIPSS EATTPTPGAS PPAPEMERPP APESVGTEEM 550 560 PEDGEPDAAE LRRRRLQKLE SPVAH
	Isoform 3 (a) (short) [UniParc]. Checksum: 3D035485BDF67376	FASTA	616	67,614
	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 AALSRPSGAA 430 440 450 460 470 480 TTTAAGTSAT AASATASGPG SGSAPEAGPA PGFPFPPPWM GMPLPPPFAF PPMPVPPAGF 490 500 510 520 530 540 AGLTPEELRA LEGHERQHLE ARLQSLRNIH TLLDAAMLQI NQYLTVLASL GPPRPATSVN 550 560 570 580 590 600 STEETATTVV AAASSTSIPS SEATTPTPGA SPPAPEMERP PAPESVGTEE MPEDGEPDAA 610 ELRRRRLQKL ESPVAH

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
IPI	IPI00166996. IPI00172510. IPI00396584.
RefSeq	NP_115807.1. NM_032431.2. NP_757385.1. NM_172230.2.
UniGene	Hs.75859.
3D structure databases
HSSP	HSSP built from PDB template 1IYM based on UniProtKB Q9LRB7.
ProteinModelPortal	Q86TM6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86TM6. 14 interactions.
MINT	MINT-4052103.
STRING	9606.ENSP00000366395.
PTM databases
PhosphoSite	Q86TM6.
Polymorphism databases
DMDM	134035039.
Proteomic databases
PaxDb	Q86TM6.
PRIDE	Q86TM6.
Protocols and materials databases
DNASU	84447.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000294256; ENSP00000294256; ENSG00000162298. ENST00000307289; ENSP00000302035; ENSG00000162298. ENST00000377190; ENSP00000366395; ENSG00000162298. ENST00000526060; ENSP00000436984; ENSG00000162298.
GeneID	84447.
KEGG	hsa:84447.
UCSC	uc001odb.3. human. uc001odc.3. human. uc009yqc.3. human.
Organism-specific databases
CTD	84447.
GeneCards	GC11M064894.
HGNC	HGNC:20738. SYVN1.
HPA	HPA005480. HPA024300.
MIM	608046. gene.
neXtProt	NX_Q86TM6.
PharmGKB	PA128394735.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5243.
HOGENOM	HOG000294196.
HOVERGEN	HBG094015.
InParanoid	Q86TM6.
KO	K10601.
Enzyme and pathway databases
Reactome	REACT_116125. Disease.
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q86TM6.
Bgee	Q86TM6.
CleanEx	HS_SYVN1.
Genevestigator	Q86TM6.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF13639. zf-RING_2. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SYVN1. human.
GenomeRNAi	84447.
NextBio	74217.
SOURCE	Search...

Entry information

Entry name

SYVN1_HUMAN

Accession

Primary (citable) accession number: Q86TM6
Secondary accession number(s): Q8N3K3 , Q8N6E8, Q96JL5, Q96PK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	March 20, 2007
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.