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E3 ubiquitin-protein ligase SIAH1A (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1A) (Seven in absentia homolog 1a) (Siah-1a) (Siah1a) (mSiah-1a)

 SIA1A_MOUSE             Reviewed;         282 AA.
P61092; Q06984;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 1.
05-DEC-2018, entry version 142.
RecName: Full=E3 ubiquitin-protein ligase SIAH1A;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase SIAH1A {ECO:0000305};
AltName: Full=Seven in absentia homolog 1a;
Short=Siah-1a;
Short=Siah1a;
Short=mSiah-1a;
Name=Siah1a;
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; TISSUE=Eye;
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=Olfactory epithelium;
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]
FUNCTION, AND 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).
[4]
INTERACTION WITH DAB1.
PubMed=12646221; DOI=10.1016/S0006-291X(03)00247-X;
Park T.-J., Hamanaka H., Ohshima T., Watanabe N., Mikoshiba K.,
Nukina N.;
"Inhibition of ubiquitin ligase Siah-1A by disabled-1.";
Biochem. Biophys. Res. Commun. 302:671-678(2003).
[5]
FUNCTION.
PubMed=11884614; DOI=10.1128/MCB.22.7.2294-2303.2002;
Dickins R.A., Frew I.J., House C.M., O'Bryan M.K., Holloway A.J.,
Haviv I., Traficante N., de Kretser D.M., Bowtell D.D.L.;
"The ubiquitin ligase component Siah1a is required for completion of
meiosis I in male mice.";
Mol. Cell. Biol. 22:2294-2303(2002).
[6]
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).
[7]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 93-282 IN COMPLEX WITH ZINC,
HOMODIMERIZATION, AND DOMAIN.
PubMed=11742346; DOI=10.1038/nsb743;
Polekhina G., House C.M., Traficante N., Mackay J.P., Relaix F.,
Sassoon D.A., Parker M.W., Bowtell D.D.L.;
"Siah ubiquitin ligase is structurally related to TRAF and modulates
TNF-alpha signaling.";
Nat. Struct. Biol. 9:68-75(2002).
[8]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 92-282 IN COMPLEX WITH ZINC
AND PEPTIDE SUBSTRATE, FUNCTION, INTERACTION WITH KLF10, AND
MUTAGENESIS OF THR-156; LEU-158; LEU-166 AND MET-180.
PubMed=16615911; DOI=10.1016/j.str.2005.12.013;
House C.M., Hancock N.C., Moller A., Cromer B.A., Fedorov V.,
Bowtell D.D., Parker M.W., Polekhina G.;
"Elucidation of the substrate binding site of Siah ubiquitin ligase.";
Structure 14:695-701(2006).
-!- 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 (ELL2, MYB, POU2AF1, PML and RBBP8), a
cell surface receptor (DCC), the cell-surface receptor-type
tyrosine kinase FLT3, the cytoplasmic signal transduction
molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1),
a microtubule motor protein (KIF22), a protein involved in
synaptic vesicle function in neurons (SYP), a structural protein
(CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2
through proteasomal degradation. It is thereby involved in many
cellular processes such as apoptosis, tumor suppression, cell
cycle, axon guidance, transcription, spermatogenesis and TNF-alpha
signaling. Has some overlapping function with SIAH2. Required for
completion of meiosis I in males. Induces apoptosis in cooperation
with PEG3. Upon nitric oxid (NO) generation that follows apoptotic
stimulation, interacts with S-nitrosylated GAPDH, mediating the
translocation of GAPDH to the nucleus. GAPDH acts as a stabilizer
of SIAH1, facilitating the degradation of nuclear proteins.
{ECO:0000269|PubMed:10681424, ECO:0000269|PubMed:11884614,
ECO:0000269|PubMed:16615911}.
-!- CATALYTIC ACTIVITY:
Reaction=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.; EC=2.3.2.27;
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homodimer. Interacts with group 1 glutamate receptors
GRM1 and GRM5. Interacts with SNCAIP and HIPK2. Interacts with
GAPDH; leading to stabilize SIAH1 (By similarity). Interacts with
UBE2E2. Component of some large E3 complex composed of UBE2D1,
SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with UBE2I.
Interacts with alpha-tubulin. Interacts with PEG10, which may
inhibit its activity (By similarity). Interacts with DAB1, which
may inhibit its activity. Interacts with PEG3 and KLF10.
{ECO:0000250, ECO:0000269|PubMed:10681424,
ECO:0000269|PubMed:11742346, ECO:0000269|PubMed:12646221,
ECO:0000269|PubMed:16615911}.
-!- INTERACTION:
P97318:Dab1; NbExp=3; IntAct=EBI-446761, EBI-81680;
Q27934:phyl (xeno); NbExp=2; IntAct=EBI-446761, EBI-77033;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
cytoplasmic. Partially nuclear.
-!- TISSUE SPECIFICITY: Widely expressed at low level in embryos and
adults. Expressed at higher level in testis. Due to the high
similarity between SIAH1A and SIAH1B, it is difficult to
distinguish its own tissue specificity.
{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:0000269|PubMed:11742346}.
-!- PTM: Phosphorylated on Ser-19 by ATM and ATR. This phosphorylation
disrupts SIAH1 interaction with HIPK2, and subsequent proteasomal
degradation of HIPK2 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
{ECO:0000305}.
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EMBL; Z19579; CAA79630.1; -; mRNA.
EMBL; BC046317; AAH46317.1; -; mRNA.
CCDS; CCDS22504.1; -.
PIR; I48763; I48763.
RefSeq; NP_033198.1; NM_009172.2.
RefSeq; XP_006530847.2; XM_006530784.3.
UniGene; Mm.324553; -.
UniGene; Mm.474080; -.
PDB; 1K2F; X-ray; 2.60 A; A/B=93-282.
PDB; 2AN6; X-ray; 3.00 A; A/B/C/D=92-282.
PDBsum; 1K2F; -.
PDBsum; 2AN6; -.
ProteinModelPortal; P61092; -.
SMR; P61092; -.
BioGrid; 203231; 8.
DIP; DIP-29100N; -.
IntAct; P61092; 4.
STRING; 10090.ENSMUSP00000044123; -.
PhosphoSitePlus; P61092; -.
MaxQB; P61092; -.
PaxDb; P61092; -.
PRIDE; P61092; -.
Ensembl; ENSMUST00000045296; ENSMUSP00000044123; ENSMUSG00000036840.
GeneID; 20437; -.
KEGG; mmu:20437; -.
UCSC; uc009mqn.2; mouse.
CTD; 20437; -.
MGI; MGI:108064; Siah1a.
eggNOG; KOG3002; Eukaryota.
eggNOG; ENOG410XVP0; LUCA.
GeneTree; ENSGT00940000154837; -.
HOGENOM; HOG000231487; -.
HOVERGEN; HBG055701; -.
InParanoid; P61092; -.
KO; K04506; -.
OMA; EACEFRP; -.
OrthoDB; EOG091G0BPY; -.
PhylomeDB; P61092; -.
TreeFam; TF312976; -.
BRENDA; 6.3.2.19; 3474.
Reactome; R-MMU-373752; Netrin-1 signaling.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Siah1a; mouse.
EvolutionaryTrace; P61092; -.
PRO; PR:P61092; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000036840; Expressed in 270 organ(s), highest expression level in ureter smooth muscle.
CleanEx; MM_SIAH1A; -.
Genevisible; P61092; MM.
GO; GO:0030877; C:beta-catenin destruction complex; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IMP:CAFA.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007141; P:male meiosis I; IMP:MGI.
GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0030163; P:protein catabolic process; ISO:MGI.
GO; GO:0031648; P:protein destabilization; ISO:MGI.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
Gene3D; 2.60.210.10; -; 1.
Gene3D; 3.30.40.10; -; 2.
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;
Developmental protein; Differentiation; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Spermatogenesis; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 282 E3 ubiquitin-protein ligase SIAH1A.
/FTId=PRO_0000056164.
ZN_FING 41 76 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 93 153 SIAH-type. {ECO:0000255|PROSITE-
ProRule:PRU00455}.
REGION 90 282 SBD. {ECO:0000269|PubMed:11742346}.
METAL 98 98 Zinc 1. {ECO:0000269|PubMed:11742346,
ECO:0000269|PubMed:16615911}.
METAL 105 105 Zinc 1. {ECO:0000269|PubMed:11742346,
ECO:0000269|PubMed:16615911}.
METAL 117 117 Zinc 1. {ECO:0000269|PubMed:11742346,
ECO:0000269|PubMed:16615911}.
METAL 121 121 Zinc 1. {ECO:0000269|PubMed:11742346,
ECO:0000269|PubMed:16615911}.
METAL 128 128 Zinc 2. {ECO:0000269|PubMed:11742346,
ECO:0000269|PubMed:16615911}.
METAL 135 135 Zinc 2. {ECO:0000269|PubMed:11742346,
ECO:0000269|PubMed:16615911}.
METAL 147 147 Zinc 2. {ECO:0000269|PubMed:11742346,
ECO:0000269|PubMed:16615911}.
METAL 152 152 Zinc 2. {ECO:0000269|PubMed:11742346,
ECO:0000269|PubMed:16615911}.
MOD_RES 19 19 Phosphoserine; by ATM and ATR.
{ECO:0000250}.
MUTAGEN 156 156 T->E: Strongly reduced binding and
degradation of target proteins; when
associated with D-158.
{ECO:0000269|PubMed:16615911}.
MUTAGEN 158 158 L->D,K: Strongly reduced binding of
target proteins. Strongly reduced
degradation of target proteins.
{ECO:0000269|PubMed:16615911}.
MUTAGEN 166 166 L->K: Minor effect on binding and
degradation of target proteins.
{ECO:0000269|PubMed:16615911}.
MUTAGEN 180 180 M->K: Strongly reduced binding of target
proteins. Strongly reduced degradation of
target proteins.
{ECO:0000269|PubMed:16615911}.
HELIX 101 103 {ECO:0000244|PDB:1K2F}.
HELIX 111 113 {ECO:0000244|PDB:1K2F}.
HELIX 114 119 {ECO:0000244|PDB:1K2F}.
STRAND 130 132 {ECO:0000244|PDB:1K2F}.
HELIX 141 143 {ECO:0000244|PDB:1K2F}.
HELIX 144 150 {ECO:0000244|PDB:1K2F}.
STRAND 156 167 {ECO:0000244|PDB:1K2F}.
STRAND 177 184 {ECO:0000244|PDB:1K2F}.
STRAND 187 198 {ECO:0000244|PDB:1K2F}.
TURN 199 201 {ECO:0000244|PDB:1K2F}.
STRAND 202 213 {ECO:0000244|PDB:1K2F}.
HELIX 215 218 {ECO:0000244|PDB:1K2F}.
STRAND 221 229 {ECO:0000244|PDB:1K2F}.
STRAND 232 238 {ECO:0000244|PDB:1K2F}.
TURN 243 245 {ECO:0000244|PDB:1K2F}.
HELIX 248 252 {ECO:0000244|PDB:1K2F}.
STRAND 256 260 {ECO:0000244|PDB:1K2F}.
HELIX 261 267 {ECO:0000244|PDB:1K2F}.
STRAND 272 281 {ECO:0000244|PDB:1K2F}.
SEQUENCE 282 AA; 31137 MW; 852EADC5DD4A4FFA CRC64;
MSRQTATALP TGTSKCPPSQ RVPALTGTTA SNNDLASLFE CPVCFDYVLP PILQCQSGHL
VCSNCRPKLT CCPTCRGPLG SIRNLAMEKV ANSVLFPCKY ASSGCEITLP HTEKAEHEEL
CEFRPYSCPC PGASCKWQGS LDAVMPHLMH QHKSITTLQG EDIVFLATDI NLPGAVDWVM
MQSCFGFHFM LVLEKQEKYD GHQQFFAIVQ LIGTRKQAEN FAYRLELNGH RRRLTWEATP
RSIHEGIATA IMNSDCLVFD TSIAQLFAEN GNLGINVTIS MC


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