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Protein

E3 ubiquitin-protein ligase synoviolin

Gene

SYVN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.10 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri291 – 33040RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: UniProtKB
  2. ubiquitin protein ligase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. endoplasmic reticulum unfolded protein response Source: Reactome
  4. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  5. in utero embryonic development Source: Ensembl
  6. negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
  7. protein N-linked glycosylation via asparagine Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Stress response, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
REACT_263883. Hh ligand biogenesis disease.
REACT_264605. Hedgehog ligand biogenesis.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase synoviolin (EC:6.3.2.-)
Alternative name(s):
Synovial apoptosis inhibitor 1
Gene namesi
Name:SYVN1
Synonyms:HRD1, KIAA1810
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:20738. SYVN1.

Subcellular locationi

  1. Endoplasmic reticulum membrane 4 Publications; Multi-pass membrane protein 4 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 4119LumenalSequence AnalysisAdd
BLAST
Transmembranei42 – 6221HelicalSequence AnalysisAdd
BLAST
Topological domaini63 – 9836CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei99 – 11921HelicalSequence AnalysisAdd
BLAST
Topological domaini120 – 14021LumenalSequence AnalysisAdd
BLAST
Transmembranei141 – 16121HelicalSequence AnalysisAdd
BLAST
Topological domaini162 – 1698CytoplasmicSequence Analysis
Transmembranei170 – 19021HelicalSequence AnalysisAdd
BLAST
Topological domaini191 – 22434LumenalSequence AnalysisAdd
BLAST
Transmembranei225 – 24521HelicalSequence AnalysisAdd
BLAST
Topological domaini246 – 617372CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi329 – 3291C → S: Abolishes E3 ligase activity. 1 Publication

Organism-specific databases

PharmGKBiPA128394735.

Polymorphism and mutation databases

BioMutaiSYVN1.
DMDMi134035039.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 617595E3 ubiquitin-protein ligase synoviolinPRO_0000280548Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei613 – 6131Phosphoserine2 Publications

Post-translational modificationi

Not N-glycosylated.
Auto-ubiquitinated.3 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ86TM6.
PaxDbiQ86TM6.
PRIDEiQ86TM6.

PTM databases

PhosphoSiteiQ86TM6.

Expressioni

Tissue specificityi

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).3 Publications

Inductioni

By endoplasmic reticulum stress-inducing agents such as thapsigargin, tunicamycin or brefeldin A, but not by heat shock.2 Publications

Gene expression databases

BgeeiQ86TM6.
CleanExiHS_SYVN1.
ExpressionAtlasiQ86TM6. baseline and differential.
GenevestigatoriQ86TM6.

Organism-specific databases

HPAiCAB037030.
HPA005480.
HPA024300.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERN1O754602EBI-947849,EBI-371750
TP53P046375EBI-947849,EBI-366083

Protein-protein interaction databases

BioGridi124085. 82 interactions.
IntActiQ86TM6. 17 interactions.
MINTiMINT-4052103.
STRINGi9606.ENSP00000366395.

Structurei

3D structure databases

ProteinModelPortaliQ86TM6.
SMRiQ86TM6. Positions 291-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 27035Interaction with p53/TP53Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi339 – 478140Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the HRD1 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri291 – 33040RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiCOG5243.
GeneTreeiENSGT00530000062938.
HOGENOMiHOG000294196.
HOVERGENiHBG094015.
InParanoidiQ86TM6.
KOiK10601.
OMAiMLNIHHY.
OrthoDBiEOG7V766G.
PhylomeDBiQ86TM6.
TreeFamiTF318635.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86TM6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MFRTAVMMAA SLALTGAVVA HAYYLKHQFY PTVVYLTKSS PSMAVLYIQA
60 70 80 90 100
FVLVFLLGKV MGKVFFGQLR AAEMEHLLER SWYAVTETCL AFTVFRDDFS
110 120 130 140 150
PRFVALFTLL LFLKCFHWLA EDRVDFMERS PNISWLFHCR IVSLMFLLGI
160 170 180 190 200
LDFLFVSHAY HSILTRGASV QLVFGFEYAI LMTMVLTIFI KYVLHSVDLQ
210 220 230 240 250
SENPWDNKAV YMLYTELFTG FIKVLLYMAF MTIMIKVHTF PLFAIRPMYL
260 270 280 290 300
AMRQFKKAVT DAIMSRRAIR NMNTLYPDAT PEELQAMDNV CIICREEMVT
310 320 330 340 350
GAKRLPCNHI FHTSCLRSWF QRQQTCPTCR MDVLRASLPA QSPPPPEPAD
360 370 380 390 400
QGPPPAPHPP PLLPQPPNFP QGLLPPFPPG MFPLWPPMGP FPPVPPPPSS
410 420 430 440 450
GEAVAPPSTS AAALSRPSGA ATTTAAGTSA TAASATASGP GSGSAPEAGP
460 470 480 490 500
APGFPFPPPW MGMPLPPPFA FPPMPVPPAG FAGLTPEELR ALEGHERQHL
510 520 530 540 550
EARLQSLRNI HTLLDAAMLQ INQYLTVLAS LGPPRPATSV NSTEETATTV
560 570 580 590 600
VAAASSTSIP SSEATTPTPG ASPPAPEMER PPAPESVGTE EMPEDGEPDA
610
AELRRRRLQK LESPVAH
Length:617
Mass (Da):67,685
Last modified:March 20, 2007 - v2
Checksum:iB8A6BACBAF9673C1
GO
Isoform 2 (identifier: Q86TM6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-177: Missing.
     411-411: Missing.

Show »
Length:565
Mass (Da):61,732
Checksum:i8C2226662D099D15
GO
Isoform 3 (identifier: Q86TM6-3) [UniParc]FASTAAdd to basket

Also known as: a, short

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

Show »
Length:616
Mass (Da):67,614
Checksum:i3D035485BDF67376
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451M → I in BAC24801 (PubMed:12459480).Curated
Sequence conflicti145 – 1451M → I in AAL26903 (PubMed:14593114).Curated
Sequence conflicti545 – 5451E → G in BAC57449 (PubMed:12975321).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei127 – 17751Missing in isoform 2. 1 PublicationVSP_023777Add
BLAST
Alternative sequencei411 – 4111Missing in isoform 2 and isoform 3. 4 PublicationsVSP_023778

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31605.1. [Q86TM6-1]
CCDS8097.1. [Q86TM6-3]
RefSeqiNP_115807.1. NM_032431.2. [Q86TM6-3]
NP_757385.1. NM_172230.2. [Q86TM6-1]
UniGeneiHs.75859.

Genome annotation databases

EnsembliENST00000294256; ENSP00000294256; ENSG00000162298. [Q86TM6-3]
ENST00000307289; ENSP00000302035; ENSG00000162298. [Q86TM6-2]
ENST00000377190; ENSP00000366395; ENSG00000162298. [Q86TM6-1]
ENST00000526060; ENSP00000436984; ENSG00000162298. [Q86TM6-3]
GeneIDi84447.
KEGGihsa:84447.
UCSCiuc001odb.3. human. [Q86TM6-1]
uc001odc.3. human. [Q86TM6-3]
uc009yqc.3. human. [Q86TM6-2]

Polymorphism and mutation databases

BioMutaiSYVN1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31605.1. [Q86TM6-1]
CCDS8097.1. [Q86TM6-3]
RefSeqiNP_115807.1. NM_032431.2. [Q86TM6-3]
NP_757385.1. NM_172230.2. [Q86TM6-1]
UniGeneiHs.75859.

3D structure databases

ProteinModelPortaliQ86TM6.
SMRiQ86TM6. Positions 291-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124085. 82 interactions.
IntActiQ86TM6. 17 interactions.
MINTiMINT-4052103.
STRINGi9606.ENSP00000366395.

PTM databases

PhosphoSiteiQ86TM6.

Polymorphism and mutation databases

BioMutaiSYVN1.
DMDMi134035039.

Proteomic databases

MaxQBiQ86TM6.
PaxDbiQ86TM6.
PRIDEiQ86TM6.

Protocols and materials databases

DNASUi84447.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294256; ENSP00000294256; ENSG00000162298. [Q86TM6-3]
ENST00000307289; ENSP00000302035; ENSG00000162298. [Q86TM6-2]
ENST00000377190; ENSP00000366395; ENSG00000162298. [Q86TM6-1]
ENST00000526060; ENSP00000436984; ENSG00000162298. [Q86TM6-3]
GeneIDi84447.
KEGGihsa:84447.
UCSCiuc001odb.3. human. [Q86TM6-1]
uc001odc.3. human. [Q86TM6-3]
uc009yqc.3. human. [Q86TM6-2]

Organism-specific databases

CTDi84447.
GeneCardsiGC11M064894.
HGNCiHGNC:20738. SYVN1.
HPAiCAB037030.
HPA005480.
HPA024300.
MIMi608046. gene.
neXtProtiNX_Q86TM6.
PharmGKBiPA128394735.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5243.
GeneTreeiENSGT00530000062938.
HOGENOMiHOG000294196.
HOVERGENiHBG094015.
InParanoidiQ86TM6.
KOiK10601.
OMAiMLNIHHY.
OrthoDBiEOG7V766G.
PhylomeDBiQ86TM6.
TreeFamiTF318635.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
REACT_263883. Hh ligand biogenesis disease.
REACT_264605. Hedgehog ligand biogenesis.

Miscellaneous databases

ChiTaRSiSYVN1. human.
GeneWikiiSYVN1.
GenomeRNAii84447.
NextBioi74217.
PROiQ86TM6.
SOURCEiSearch...

Gene expression databases

BgeeiQ86TM6.
CleanExiHS_SYVN1.
ExpressionAtlasiQ86TM6. baseline and differential.
GenevestigatoriQ86TM6.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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. 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.
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSYVN1_HUMAN
AccessioniPrimary (citable) accession number: Q86TM6
Secondary accession number(s): Q8N3K3
, Q8N6E8, Q96JL5, Q96PK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: April 29, 2015
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.