SIA1B_MOUSE
ID SIA1B_MOUSE Reviewed; 282 AA.
AC Q06985; Q7TPV6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase SIAH1B;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8IUQ4};
DE AltName: Full=RING-type E3 ubiquitin transferase SIAH1B {ECO:0000305};
DE AltName: Full=Seven in absentia homolog 1b;
DE Short=Siah-1b;
DE Short=Siah1b;
GN Name=Siah1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=SWR/J;
RX PubMed=8404535; DOI=10.1242/dev.117.4.1333;
RA Della N.G., Senior P.V., Bowtell D.D.L.;
RT "Isolation and characterisation of murine homologues of the Drosophila
RT seven in absentia gene (sina).";
RL Development 117:1333-1343(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INDUCTION.
RX PubMed=8632996; DOI=10.1073/pnas.93.9.3953;
RA Amson R.B., Nemani M., Roperch J.-P., Israeli D., Bougueleret L.,
RA Le Gall I., Medhioub M., Linares-Cruz G., Lethrosne F., Pasturaud P.,
RA Piouffre L., Prieur S., Susini L., Alvaro V., Millasseau P., Guidicelli C.,
RA Bui H., Massart C., Cazes L., Dufour F., Bruzzoni-Giovanelli H., Owadi H.,
RA Hennion C., Charpak G., Dausset J., Calvo F., Oren M., Cohen D.,
RA Telerman A.;
RT "Isolation of 10 differentially expressed cDNAs in p53-induced apoptosis:
RT activation of the vertebrate homologue of the Drosophila seven in absentia
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3953-3957(1996).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12842817; DOI=10.1152/ajpheart.00983.2002;
RA Favre C.J., Mancuso M., Maas K., McLean J.W., Baluk P., McDonald D.M.;
RT "Expression of genes involved in vascular development and angiogenesis in
RT endothelial cells of adult lung.";
RL Am. J. Physiol. 285:H1917-H1938(2003).
RN [5]
RP INDUCTION.
RX PubMed=14985507; DOI=10.1073/pnas.0400177101;
RA Fiucci G., Beaucourt S., Duflaut D., Lespagnol A., Stumptner-Cuvelette P.,
RA Geant A., Buchwalter G., Tuynder M., Susini L., Lassalle J.-M., Wasylyk C.,
RA Wasylyk B., Oren M., Amson R., Telerman A.;
RT "Siah-1b is a direct transcriptional target of p53: identification of the
RT functional p53 responsive element in the siah-1b promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3510-3515(2004).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. Mediates E3 ubiquitin ligase activity either
CC through direct binding to substrates or by functioning as the essential
CC RING domain subunit of larger E3 complexes.
CC {ECO:0000250|UniProtKB:Q8IUQ4, ECO:0000250|UniProtKB:Q920M9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8IUQ4};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8IUQ4}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P61092}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed at low level in embryos and
CC adults. Due to the high similarity between SIAH1A and SIAH1B, it is
CC difficult to distinguish its own tissue specificity. Overexpressed in
CC endothelial cells of adult lung. {ECO:0000269|PubMed:12842817,
CC ECO:0000269|PubMed:8404535}.
CC -!- INDUCTION: Induced by p53/TP53, suggesting that it may be required to
CC modulate p53/TP53 response. {ECO:0000269|PubMed:14985507,
CC ECO:0000269|PubMed:8632996}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity.
CC -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC homodimerization and the interaction with substrate proteins. It is
CC related to the TRAF family. {ECO:0000250|UniProtKB:P61092}.
CC -!- PTM: Phosphorylated on Ser-19 by ATM and ATR.
CC {ECO:0000250|UniProtKB:Q8IUQ4}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
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DR EMBL; Z19580; CAA79631.1; -; mRNA.
DR EMBL; BC052887; AAH52887.1; -; mRNA.
DR CCDS; CCDS30516.1; -.
DR PIR; I48764; S35754.
DR RefSeq; NP_001295314.1; NM_001308385.1.
DR RefSeq; NP_001295315.1; NM_001308386.1.
DR RefSeq; NP_033199.1; NM_009173.2.
DR AlphaFoldDB; Q06985; -.
DR SMR; Q06985; -.
DR IntAct; Q06985; 1.
DR STRING; 10090.ENSMUSP00000043215; -.
DR MaxQB; Q06985; -.
DR PaxDb; Q06985; -.
DR PRIDE; Q06985; -.
DR ProteomicsDB; 261230; -.
DR DNASU; 20438; -.
DR GeneID; 20438; -.
DR KEGG; mmu:20438; -.
DR CTD; 20438; -.
DR MGI; MGI:108063; Siah1b.
DR eggNOG; KOG3002; Eukaryota.
DR InParanoid; Q06985; -.
DR OrthoDB; 780610at2759; -.
DR PhylomeDB; Q06985; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 20438; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Siah1b; mouse.
DR PRO; PR:Q06985; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q06985; protein.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR004162; SINA-like_animal.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR45877; PTHR45877; 1.
DR Pfam; PF03145; Sina; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..282
FT /note="E3 ubiquitin-protein ligase SIAH1B"
FT /id="PRO_0000056165"
FT ZN_FING 41..76
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 93..153
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..282
FT /note="SBD"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT MOD_RES 19
FT /note="Phosphoserine; by ATM and ATR"
FT /evidence="ECO:0000250|UniProtKB:Q8IUQ4"
FT CONFLICT 87
FT /note="V -> M (in Ref. 1; CAA79631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 31122 MW; A09F5D3DEEB39AC2 CRC64;
MSRQAATALS TGTSKCPPSQ RVPALTDTTA SNNDLASLFE CPVCFDYVLP PILQCQSGHL
VCSNCRPKLT CCPTCRGPLG SIRNLAVEKV ANSVLFPCKY SASGCEITLP HTKKAEHEEL
CEFRPYSCPC PGASCKWQGS LDAVMPHLMH QHKSITTLQG EDIVFLATDI NLPGAVDWVM
MQSCFGFHFM LVLEKQEKYD GHQQFFAIVQ LIGTRKQAEN FAYRLELNGH RRRLTWEATP
RSIHEGIATA IMNSDCLVFD TSIAQLFAEN GNLGINVTIS MC
