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E3 ubiquitin-protein ligase SIAH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH2) (Seven in absentia homolog 2) (Siah-2) (hSiah2)

 SIAH2_HUMAN             Reviewed;         324 AA.
O43255; O43270;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 167.
RecName: Full=E3 ubiquitin-protein ligase SIAH2;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase SIAH2 {ECO:0000305};
AltName: Full=Seven in absentia homolog 2;
Short=Siah-2;
Short=hSiah2;
Name=SIAH2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=9403064; DOI=10.1006/geno.1997.4997;
Hu G., Chung Y.-L., Glover T., Valentine V., Look A.T., Fearon E.R.;
"Characterization of human homologs of the Drosophila seven in
absentia (sina) gene.";
Genomics 46:103-111(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH VAV1.
PubMed=10207103; DOI=10.1128/MCB.19.5.3798;
Germani A., Romero F., Houlard M., Camonis J., Gisselbrecht S.,
Fischer S., Varin-Blank N.;
"hSiah2 is a new Vav binding protein which inhibits Vav-mediated
signaling pathways.";
Mol. Cell. Biol. 19:3798-3807(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION IN DEGRADATION OF DCC, AND INTERACTION WITH UBE2I.
PubMed=9334332; DOI=10.1101/gad.11.20.2701;
Hu G., Zhang S., Vidal M., Baer J.L., Xu T., Fearon E.R.;
"Mammalian homologs of seven in absentia regulate DCC via the
ubiquitin-proteasome pathway.";
Genes Dev. 11:2701-2714(1997).
[5]
FUNCTION IN DEGRADATION OF POU2AF1.
PubMed=11483518; DOI=10.1093/emboj/20.15.4153;
Boehm J., He Y., Greiner A., Staudt L., Wirth T.;
"Regulation of BOB.1/OBF.1 stability by SIAH.";
EMBO J. 20:4153-4162(2001).
[6]
INTERACTION WITH CACYBP.
PubMed=11389839; DOI=10.1016/S1097-2765(01)00242-8;
Matsuzawa S., Reed J.C.;
"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin
degradation linked to p53 responses.";
Mol. Cell 7:915-926(2001).
[7]
FUNCTION IN DEGRADATION OF TRAF2.
PubMed=12411493; DOI=10.1093/emboj/cdf576;
Habelhah H., Frew I.J., Laine A., Janes P.W., Relaix F., Sassoon D.,
Bowtell D.D.L., Ronai Z.;
"Stress-induced decrease in TRAF2 stability is mediated by Siah2.";
EMBO J. 21:5756-5765(2002).
[8]
INTERACTION WITH PEG10.
PubMed=12810624;
Okabe H., Satoh S., Furukawa Y., Kato T., Hasegawa S., Nakajima Y.,
Yamaoka Y., Nakamura Y.;
"Involvement of PEG10 in human hepatocellular carcinogenesis through
interaction with SIAH1.";
Cancer Res. 63:3043-3048(2003).
[9]
INTERACTION WITH EGLN2.
PubMed=16509823; DOI=10.1042/BJ20051996;
Tian Y.M., Mole D.R., Ratcliffe P.J., Gleadle J.M.;
"Characterization of different isoforms of the HIF prolyl hydroxylase
PHD1 generated by alternative initiation.";
Biochem. J. 397:179-186(2006).
[10]
FUNCTION, INTERACTION WITH SNCAIP, SUBCELLULAR LOCATION, AND ACTIVITY
REGULATION.
PubMed=19224863; DOI=10.1074/jbc.M805990200;
Szargel R., Rott R., Eyal A., Haskin J., Shani V., Balan L.,
Wolosker H., Engelender S.;
"Synphilin-1A inhibits seven in absentia homolog (SIAH) and modulates
alpha-synuclein monoubiquitylation and inclusion formation.";
J. Biol. Chem. 284:11706-11716(2009).
[11]
FUNCTION, INTERACTION WITH DYRK2, SUBCELLULAR LOCATION,
PHOSPHORYLATION AT SER-16; THR-26; SER-28; SER-68 AND THR-119,
MUTAGENESIS OF SER-16; THR-26; SER-28; SER-68 AND THR-119, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22878263; DOI=10.1093/jmcb/mjs047;
Perez M., Garcia-Limones C., Zapico I., Marina A., Schmitz M.L.,
Munoz E., Calzado M.A.;
"Mutual regulation between SIAH2 and DYRK2 controls hypoxic and
genotoxic signaling pathways.";
J. Mol. Cell Biol. 4:316-330(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
and subsequent proteasomal degradation of target proteins. E3
ubiquitin ligases accept ubiquitin from an E2 ubiquitin-
conjugating enzyme in the form of a thioester and then directly
transfers the ubiquitin to targeted substrates. Mediates E3
ubiquitin ligase activity either through direct binding to
substrates or by functioning as the essential RING domain subunit
of larger E3 complexes. Triggers the ubiquitin-mediated
degradation of many substrates, including proteins involved in
transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell
surface receptor (DCC), an antiapoptotic protein (BAG1), and a
protein involved in synaptic vesicle function in neurons (SYP).
Mediates ubiquitination and proteasomal degradation of DYRK2 in
response to hypoxia. It is thereby involved in apoptosis, tumor
suppression, cell cycle, transcription and signaling processes.
Has some overlapping function with SIAH1. Triggers the ubiquitin-
mediated degradation of TRAF2, whereas SIAH1 does not. Promotes
monoubiquitination of SNCA. {ECO:0000269|PubMed:11483518,
ECO:0000269|PubMed:12411493, ECO:0000269|PubMed:19224863,
ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:9334332}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- ACTIVITY REGULATION: Inhibited by interaction with SNCAIP (isoform
2, but not isoform 1). May be inhibited by interaction with PEG10.
{ECO:0000269|PubMed:19224863}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homodimer. Interacts with UBE2E2. Interacts with PEG3 (By
similarity). Interacts with VAV1, without mediating its ubiquitin-
mediated degradation. Interacts with CACYBP/SIP. Probable
component of some large E3 complex possibly composed of UBE2D1,
SIAH2, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with PEG10,
which may inhibit its activity. Interacts with EGLN2 and SNCAIP.
Interacts with DYRK2. {ECO:0000250|UniProtKB:Q06986,
ECO:0000269|PubMed:10207103, ECO:0000269|PubMed:11389839,
ECO:0000269|PubMed:12810624, ECO:0000269|PubMed:16509823,
ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:22878263,
ECO:0000269|PubMed:9334332}.
-!- INTERACTION:
O95835:LATS1; NbExp=2; IntAct=EBI-948141, EBI-444209;
Q9NRM7:LATS2; NbExp=6; IntAct=EBI-948141, EBI-3506895;
P35372:OPRM1; NbExp=3; IntAct=EBI-948141, EBI-2624570;
Q7Z6J0:SH3RF1; NbExp=3; IntAct=EBI-948141, EBI-311339;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19224863,
ECO:0000269|PubMed:22878263}. Nucleus
{ECO:0000269|PubMed:22878263}. Note=Predominantly cytoplasmic.
Partially nuclear. {ECO:0000269|PubMed:22878263}.
-!- TISSUE SPECIFICITY: Widely expressed at low level.
{ECO:0000269|PubMed:9403064}.
-!- DOMAIN: The RING-type zinc finger domain is essential for
ubiquitin ligase activity.
-!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
homodimerization and the interaction with substrate proteins. It
is related to the TRAF family. {ECO:0000250|UniProtKB:P61092}.
-!- PTM: Phosphorylated at Ser-28 by MAPK14, which mediates the
degradation by the proteasome of EGLN3 (By similarity).
Phosphorylated at Ser-28 by DYRK2; this increases the ubiquitin
ligase activity and promotes degradation of EGLN3.
{ECO:0000250|UniProtKB:Q06986, ECO:0000269|PubMed:22878263}.
-!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SIAH2ID46199ch3q25.html";
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EMBL; U76248; AAC51908.1; -; mRNA.
EMBL; Y15268; CAA75557.1; -; mRNA.
EMBL; BC013082; AAH13082.1; -; mRNA.
CCDS; CCDS3152.1; -.
RefSeq; NP_005058.3; NM_005067.5.
UniGene; Hs.477959; -.
UniGene; Hs.692394; -.
PDB; 5H9M; X-ray; 1.76 A; A/B=131-321.
PDBsum; 5H9M; -.
ProteinModelPortal; O43255; -.
SMR; O43255; -.
BioGrid; 112373; 71.
DIP; DIP-41874N; -.
IntAct; O43255; 22.
MINT; O43255; -.
STRING; 9606.ENSP00000322457; -.
iPTMnet; O43255; -.
PhosphoSitePlus; O43255; -.
BioMuta; SIAH2; -.
MaxQB; O43255; -.
PaxDb; O43255; -.
PeptideAtlas; O43255; -.
PRIDE; O43255; -.
ProteomicsDB; 48838; -.
Ensembl; ENST00000312960; ENSP00000322457; ENSG00000181788.
GeneID; 6478; -.
KEGG; hsa:6478; -.
UCSC; uc003eyi.4; human.
CTD; 6478; -.
DisGeNET; 6478; -.
EuPathDB; HostDB:ENSG00000181788.3; -.
GeneCards; SIAH2; -.
H-InvDB; HIX0163461; -.
HGNC; HGNC:10858; SIAH2.
HPA; CAB069930; -.
HPA; HPA061293; -.
MIM; 602213; gene.
neXtProt; NX_O43255; -.
OpenTargets; ENSG00000181788; -.
PharmGKB; PA35760; -.
eggNOG; KOG3002; Eukaryota.
eggNOG; ENOG410XVP0; LUCA.
GeneTree; ENSGT00390000005434; -.
HOGENOM; HOG000231487; -.
HOVERGEN; HBG055701; -.
InParanoid; O43255; -.
KO; K08742; -.
OMA; IDPPQNE; -.
OrthoDB; EOG091G0BPY; -.
PhylomeDB; O43255; -.
TreeFam; TF312976; -.
Reactome; R-HSA-373752; Netrin-1 signaling.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-977225; Amyloid fiber formation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; O43255; -.
UniPathway; UPA00143; -.
ChiTaRS; SIAH2; human.
GeneWiki; SIAH2; -.
GenomeRNAi; 6478; -.
PRO; PR:O43255; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000181788; Expressed in 217 organ(s), highest expression level in adrenal tissue.
CleanEx; HS_SIAH2; -.
ExpressionAtlas; O43255; baseline and differential.
Genevisible; O43255; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:Ensembl.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0044257; P:cellular protein catabolic process; IGI:MGI.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0007275; P:multicellular organism development; IEA:InterPro.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:1902842; P:negative regulation of netrin-activated signaling pathway; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0031396; P:regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
Gene3D; 2.60.210.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
InterPro; IPR004162; SINA-like.
InterPro; IPR008974; TRAF-like.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR013010; Znf_SIAH.
PANTHER; PTHR10315; PTHR10315; 1.
Pfam; PF03145; Sina; 1.
SUPFAM; SSF49599; SSF49599; 1.
PROSITE; PS50089; ZF_RING_2; 1.
PROSITE; PS51081; ZF_SIAH; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Cell cycle; Complete proteome; Cytoplasm;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 324 E3 ubiquitin-protein ligase SIAH2.
/FTId=PRO_0000056168.
ZN_FING 80 115 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 133 193 SIAH-type. {ECO:0000255|PROSITE-
ProRule:PRU00455}.
REGION 130 322 SBD. {ECO:0000250|UniProtKB:P61092}.
METAL 138 138 Zinc 1. {ECO:0000250|UniProtKB:P61092}.
METAL 145 145 Zinc 1. {ECO:0000250|UniProtKB:P61092}.
METAL 157 157 Zinc 1. {ECO:0000250|UniProtKB:P61092}.
METAL 161 161 Zinc 1. {ECO:0000250|UniProtKB:P61092}.
METAL 168 168 Zinc 2. {ECO:0000250|UniProtKB:P61092}.
METAL 175 175 Zinc 2. {ECO:0000250|UniProtKB:P61092}.
METAL 187 187 Zinc 2. {ECO:0000250|UniProtKB:P61092}.
METAL 192 192 Zinc 2. {ECO:0000250|UniProtKB:P61092}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 16 16 Phosphoserine; by DYRK2.
{ECO:0000269|PubMed:22878263}.
MOD_RES 26 26 Phosphothreonine; by DYRK2.
{ECO:0000269|PubMed:22878263}.
MOD_RES 28 28 Phosphoserine; by DYRK2 and MAPK14.
{ECO:0000269|PubMed:22878263}.
MOD_RES 68 68 Phosphoserine; by DYRK2.
{ECO:0000269|PubMed:22878263}.
MOD_RES 119 119 Phosphothreonine; by DYRK2.
{ECO:0000269|PubMed:22878263}.
MUTAGEN 16 16 S->A: Strongly reduced phosphorylation by
DYRK2; when associated with A-26; A-28;
A-68 and A-119.
{ECO:0000269|PubMed:22878263}.
MUTAGEN 26 26 T->A: Strongly reduced phosphorylation by
DYRK2; when associated with A-16; A-28;
A-68 and A-119.
{ECO:0000269|PubMed:22878263}.
MUTAGEN 28 28 S->A: Strongly reduced phosphorylation by
DYRK2; when associated with A-16; A-26;
A-68 and A-119.
{ECO:0000269|PubMed:22878263}.
MUTAGEN 68 68 S->A: Strongly reduced phosphorylation by
DYRK2; when associated with A-16; A-26;
A-28 and A-119.
{ECO:0000269|PubMed:22878263}.
MUTAGEN 119 119 T->A: Strongly reduced phosphorylation by
DYRK2; when associated with A-16; A-26;
A-28 and A-68.
{ECO:0000269|PubMed:22878263}.
CONFLICT 200 200 G -> E (in Ref. 1; AAC51908).
{ECO:0000305}.
STRAND 135 137 {ECO:0000244|PDB:5H9M}.
HELIX 141 143 {ECO:0000244|PDB:5H9M}.
STRAND 148 150 {ECO:0000244|PDB:5H9M}.
TURN 151 153 {ECO:0000244|PDB:5H9M}.
HELIX 154 160 {ECO:0000244|PDB:5H9M}.
HELIX 181 183 {ECO:0000244|PDB:5H9M}.
HELIX 184 191 {ECO:0000244|PDB:5H9M}.
STRAND 196 207 {ECO:0000244|PDB:5H9M}.
STRAND 217 224 {ECO:0000244|PDB:5H9M}.
STRAND 227 239 {ECO:0000244|PDB:5H9M}.
STRAND 242 253 {ECO:0000244|PDB:5H9M}.
HELIX 255 258 {ECO:0000244|PDB:5H9M}.
STRAND 262 269 {ECO:0000244|PDB:5H9M}.
STRAND 272 278 {ECO:0000244|PDB:5H9M}.
HELIX 283 285 {ECO:0000244|PDB:5H9M}.
HELIX 288 292 {ECO:0000244|PDB:5H9M}.
STRAND 296 300 {ECO:0000244|PDB:5H9M}.
HELIX 301 307 {ECO:0000244|PDB:5H9M}.
STRAND 312 320 {ECO:0000244|PDB:5H9M}.
SEQUENCE 324 AA; 34615 MW; 2D5DD845666EC924 CRC64;
MSRPSSTGPS ANKPCSKQPP PQPQHTPSPA APPAAATISA AGPGSSAVPA AAAVISGPGG
GGGAGPVSPQ HHELTSLFEC PVCFDYVLPP ILQCQAGHLV CNQCRQKLSC CPTCRGALTP
SIRNLAMEKV ASAVLFPCKY ATTGCSLTLH HTEKPEHEDI CEYRPYSCPC PGASCKWQGS
LEAVMSHLMH AHKSITTLQG EDIVFLATDI NLPGAVDWVM MQSCFGHHFM LVLEKQEKYE
GHQQFFAIVL LIGTRKQAEN FAYRLELNGN RRRLTWEATP RSIHDGVAAA IMNSDCLVFD
TAIAHLFADN GNLGINVTIS TCCP


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