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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) (mSiah2)

 SIAH2_MOUSE             Reviewed;         325 AA.
Q06986;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 2.
18-JUL-2018, entry version 154.
RecName: Full=E3 ubiquitin-protein ligase SIAH2;
EC=2.3.2.27 {ECO:0000269|PubMed:26070566};
AltName: Full=RING-type E3 ubiquitin transferase SIAH2 {ECO:0000305};
AltName: Full=Seven in absentia homolog 2;
Short=Siah-2;
Short=mSiah2;
Name=Siah2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=SWR/J;
PubMed=8404535;
Della N.G., Senior P.V., Bowtell D.D.L.;
"Isolation and characterisation of murine homologues of the Drosophila
seven in absentia gene (sina).";
Development 117:1333-1343(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; 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).
[3]
TISSUE SPECIFICITY.
PubMed=7895278; DOI=10.1007/BF00318499;
Della N.G., Bowtell D.D.L., Beck F.;
"Expression of Siah-2, a vertebrate homologue of Drosophila sina, in
germ cells of the mouse ovary and testis.";
Cell Tissue Res. 279:411-419(1995).
[4]
FUNCTION IN DEGRADATION OF NCOR1.
PubMed=9637679; DOI=10.1101/gad.12.12.1775;
Zhang J., Guenther M.G., Carthew R.W., Lazar M.A.;
"Proteasomal regulation of nuclear receptor corepressor-mediated
repression.";
Genes Dev. 12:1775-1780(1998).
[5]
INTERACTION WITH PEG3.
PubMed=10681424; DOI=10.1073/pnas.040378897;
Relaix F., Wei X., Li W., Pan J., Lin Y., Bowtell D.D., Sassoon D.A.,
Wu X.;
"Pw1/Peg3 is a potential cell death mediator and cooperates with
Siah1a in p53-mediated apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 97:2105-2110(2000).
[6]
FUNCTION IN DEGRADATION OF BAG1.
PubMed=11257006;
Sourisseau T., Desbois C., Debure L., Bowtell D.D.L., Cato A.C.B.,
Schneikert J., Moyse E., Michel D.;
"Alteration of the stability of Bag-1 protein in the control of
olfactory neuronal apoptosis.";
J. Cell Sci. 114:1409-1416(2001).
[7]
INDUCTION.
PubMed=12417719; DOI=10.1128/MCB.22.23.8155-8164.2002;
Frew I.J., Dickins R.A., Cuddihy A.R., Del Rosario M., Reinhard C.,
O'Connell M.J., Bowtell D.D.L.;
"Normal p53 function in primary cells deficient for Siah genes.";
Mol. Cell. Biol. 22:8155-8164(2002).
[8]
FUNCTION.
PubMed=14645526; DOI=10.1128/MCB.23.24.9150-9161.2003;
Frew I.J., Hammond V.E., Dickins R.A., Quinn J.M.W., Walkley C.R.,
Sims N.A., Schnall R., Della N.G., Holloway A.J., Digby M.R.,
Janes P.W., Tarlinton D.M., Purton L.E., Gillespie M.T.,
Bowtell D.D.L.;
"Generation and analysis of Siah2 mutant mice.";
Mol. Cell. Biol. 23:9150-9161(2003).
[9]
FUNCTION IN DEGRADATION OF PML.
PubMed=14645235; DOI=10.1074/jbc.M306407200;
Fanelli M., Fantozzi A., De Luca P., Caprodossi S., Matsuzawa S.,
Lazar M.A., Pelicci P.G., Minucci S.;
"The coiled-coil domain is the structural determinant for mammalian
homologues of Drosophila Sina-mediated degradation of promyelocytic
leukemia protein and other tripartite motif proteins by the
proteasome.";
J. Biol. Chem. 279:5374-5379(2004).
[10]
PHOSPHORYLATION AT THR-24 AND SER-29, AND FUNCTION.
PubMed=17003045; DOI=10.1074/jbc.M606568200;
Khurana A., Nakayama K., Williams S., Davis R.J., Mustelin T.,
Ronai Z.;
"Regulation of the ring finger E3 ligase Siah2 by p38 MAPK.";
J. Biol. Chem. 281:35316-35326(2006).
[11]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=26070566; DOI=10.1074/jbc.M115.637660;
Huang J., Cardamone M.D., Johnson H.E., Neault M., Chan M.,
Floyd Z.E., Mallette F.A., Perissi V.;
"Exchange factor TBL1 and arginine methyltransferase PRMT6 cooperate
in protecting G protein pathway suppressor 2 (GPS2) from proteasomal
degradation.";
J. Biol. Chem. 290:19044-19054(2015).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
and subsequent proteasomal degradation of target proteins
(PubMed:11257006, PubMed:14645235, PubMed:14645526,
PubMed:17003045, PubMed:9637679, PubMed:26070566). 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 (PubMed:11257006,
PubMed:14645235, PubMed:14645526, PubMed:17003045, PubMed:9637679,
PubMed:26070566). Mediates E3 ubiquitin ligase activity either
through direct binding to substrates or by functioning as the
essential RING domain subunit of larger E3 complexes. Mediates
ubiquitination and proteasomal degradation of DYRK2 in response to
hypoxia. Promotes monoubiquitination of SNCA (By similarity).
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) (PubMed:11257006,
PubMed:14645235, PubMed:14645526, PubMed:17003045, PubMed:9637679,
PubMed:26070566). 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.
{ECO:0000250|UniProtKB:O43255, ECO:0000269|PubMed:11257006,
ECO:0000269|PubMed:14645235, ECO:0000269|PubMed:14645526,
ECO:0000269|PubMed:17003045, ECO:0000269|PubMed:26070566,
ECO:0000269|PubMed:9637679}.
-!- 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. {ECO:0000269|PubMed:26070566}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homodimer. Interacts with UBE2E2. 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 UBE2I. Interacts with PEG10, which may
inhibit its activity. Interacts with EGLN2 and SNCAIP. Interacts
with DYRK2 (By similarity). Interacts with PEG3.
{ECO:0000250|UniProtKB:O43255, ECO:0000269|PubMed:10681424}.
-!- INTERACTION:
O08715:Akap1; NbExp=6; IntAct=EBI-957413, EBI-7838029;
P10275:AR (xeno); NbExp=6; IntAct=EBI-957413, EBI-608057;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43255}.
Nucleus {ECO:0000250|UniProtKB:O43255}. Note=Predominantly
cytoplasmic. Partially nuclear. {ECO:0000250|UniProtKB:O43255}.
-!- TISSUE SPECIFICITY: Widely expressed at low level in embryos and
adults. Expressed in a specific population of germ cells within
both the mouse ovary and testis. Absent in primordial oocytes but
expressed in all growing oocytes, coincident with their
recruitment from the pool of quiescent cells. Its level of
expression increases as the oocytes mature. Expressed in Graafian
follicles and in fertilized zygotes up until the two cell stage, a
time of extensive maternal transcript degradation and zygotic gene
activation. Expressed in the testis from postmeiotic spermatids.
{ECO:0000269|PubMed:7895278, ECO:0000269|PubMed:8404535}.
-!- INDUCTION: May be induced by p53/TP53, suggesting that it may be
required to modulate p53/TP53 response. The relevance of such
activity in vivo is however unclear and may not exist.
{ECO:0000269|PubMed:12417719}.
-!- 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-29 by DYRK2; this increases the
ubiquitin ligase activity and promotes degradation of EGLN3 (By
similarity). Phosphorylated at Thr-24 and Ser-29 by MAPK14, which
mediates the degradation by the proteasome of EGLN3.
{ECO:0000250|UniProtKB:O43255, ECO:0000269|PubMed:17003045}.
-!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
{ECO:0000305}.
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EMBL; Z19581; CAA79632.1; -; mRNA.
EMBL; BC058400; AAH58400.1; -; mRNA.
CCDS; CCDS17368.1; -.
PIR; I48765; I48765.
RefSeq; NP_033200.2; NM_009174.3.
UniGene; Mm.2847; -.
ProteinModelPortal; Q06986; -.
SMR; Q06986; -.
BioGrid; 203233; 8.
IntAct; Q06986; 5.
MINT; Q06986; -.
STRING; 10090.ENSMUSP00000067496; -.
iPTMnet; Q06986; -.
PhosphoSitePlus; Q06986; -.
PaxDb; Q06986; -.
PeptideAtlas; Q06986; -.
PRIDE; Q06986; -.
Ensembl; ENSMUST00000070368; ENSMUSP00000067496; ENSMUSG00000036432.
GeneID; 20439; -.
KEGG; mmu:20439; -.
UCSC; uc008pia.1; mouse.
CTD; 6478; -.
MGI; MGI:108062; Siah2.
eggNOG; KOG3002; Eukaryota.
eggNOG; ENOG410XVP0; LUCA.
GeneTree; ENSGT00390000005434; -.
HOGENOM; HOG000231487; -.
HOVERGEN; HBG055701; -.
InParanoid; Q06986; -.
KO; K08742; -.
OMA; IDPPQNE; -.
OrthoDB; EOG091G0BPY; -.
TreeFam; TF312976; -.
Reactome; R-MMU-373752; Netrin-1 signaling.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:Q06986; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000036432; -.
CleanEx; MM_SIAH2; -.
ExpressionAtlas; Q06986; baseline and differential.
Genevisible; Q06986; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
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; ISO:MGI.
GO; GO:0007275; P:multicellular organism development; IEA:InterPro.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA: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;
Apoptosis; Cell cycle; Complete proteome; Cytoplasm; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 325 E3 ubiquitin-protein ligase SIAH2.
/FTId=PRO_0000056169.
ZN_FING 81 116 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 134 194 SIAH-type. {ECO:0000255|PROSITE-
ProRule:PRU00455}.
REGION 131 323 SBD. {ECO:0000250|UniProtKB:P61092}.
METAL 139 139 Zinc 1. {ECO:0000250|UniProtKB:P61092}.
METAL 146 146 Zinc 1. {ECO:0000250|UniProtKB:P61092}.
METAL 158 158 Zinc 1. {ECO:0000250|UniProtKB:P61092}.
METAL 162 162 Zinc 1. {ECO:0000250|UniProtKB:P61092}.
METAL 169 169 Zinc 2. {ECO:0000250|UniProtKB:P61092}.
METAL 176 176 Zinc 2. {ECO:0000250|UniProtKB:P61092}.
METAL 188 188 Zinc 2. {ECO:0000250|UniProtKB:P61092}.
METAL 193 193 Zinc 2. {ECO:0000250|UniProtKB:P61092}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000250|UniProtKB:O43255}.
MOD_RES 16 16 Phosphoserine; by DYRK2.
{ECO:0000250|UniProtKB:O43255}.
MOD_RES 24 24 Phosphothreonine; by MAPK14.
{ECO:0000269|PubMed:17003045}.
MOD_RES 29 29 Phosphoserine; by DYRK2 and MAPK14.
{ECO:0000269|PubMed:17003045}.
MOD_RES 69 69 Phosphoserine; by DYRK2.
{ECO:0000250|UniProtKB:O43255}.
MOD_RES 120 120 Phosphothreonine; by DYRK2.
{ECO:0000250|UniProtKB:O43255}.
CONFLICT 203 204 DI -> ET (in Ref. 1; CAA79632).
{ECO:0000305}.
SEQUENCE 325 AA; 34758 MW; 1CB73AD3B4C9982F CRC64;
MSRPSSTGPS ANKPCSKQPP PPQTPHAPSP AAPPAAATIS AAGPGSSAVP AAAAVISGPG
AGGGADPVSP QHHELTSLFE CPVCFDYVLP PILQCQAGHL VCNQCRQKLS CCPTCRGALT
PSIRNLAMEK VASAVLFPCK YATTGCSLTL HHTEKPEHED ICEYRPYSCP CPGASCKWQG
SLEAVMSHLM HAHKSITTLQ GEDIVFLATD INLPGAVDWV MMQSCFGHHF MLVLEKQEKY
EGHQQFFAIV LLIGTRKQAE NFAYRLELNG NRRRLTWEAT PRSIHDGVAA AIMNSDCLVF
DTAIAHLFAD NGNLGINVTI STCCQ


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