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E3 ubiquitin-protein ligase SIAH1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1) (Seven in absentia homolog 1) (Siah-1) (Siah-1a)

 SIAH1_HUMAN             Reviewed;         282 AA.
Q8IUQ4; A0FKF3; O43269; Q49A58; Q92880;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 2.
25-OCT-2017, entry version 160.
RecName: Full=E3 ubiquitin-protein ligase SIAH1;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase SIAH1 {ECO:0000305};
AltName: Full=Seven in absentia homolog 1;
Short=Siah-1;
AltName: Full=Siah-1a;
Name=SIAH1; Synonyms=HUMSIAH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Intestinal epithelium;
PubMed=8799150; DOI=10.1073/pnas.93.17.9039;
Nemani M., Linares-Cruz G., Bruzzoni-Giovanelli H., Roperch J.-P.,
Tuynder M., Bougueleret L., Cherif D., Medhioub M., Pasturaud P.,
Alvaro V., Der Sarkissan H., Cazes L., Le Paslier D., Le Gall I.,
Israeli D., Dausset J., Sigaux F., Chumakov I., Oren M., Calvo F.,
Amson R.B., Cohen D., Telerman A.;
"Activation of the human homologue of the Drosophila sina gene in
apoptosis and tumor suppression.";
Proc. Natl. Acad. Sci. U.S.A. 93:9039-9042(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Fetal brain;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10956387;
DOI=10.1002/1097-0215(20000915)87:6<794::AID-IJC5>3.0.CO;2-B;
Medhioub M., Vaury C., Hamelin R., Thomas G.;
"Lack of somatic mutation in the coding sequence of SIAH1 in tumors
hemizygous for this candidate tumor suppressor gene.";
Int. J. Cancer 87:794-797(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=17420721; DOI=10.1038/sj.onc.1210449;
Mei Y., Xie C., Xie W., Wu Z., Wu M.;
"Siah-1S, a novel splice variant of Siah-1 (seven in absentia
homolog), counteracts Siah-1-mediated downregulation of beta-
catenin.";
Oncogene 26:6319-6331(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Pancreas, and Testis;
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).
[7]
FUNCTION IN DEGRADATION OF DCC, SUBCELLULAR LOCATION, 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).
[8]
INTERACTION WITH BAG1, AND SUBCELLULAR LOCATION.
PubMed=9582267; DOI=10.1093/emboj/17.10.2736;
Matsuzawa S., Takayama S., Froesch B.A., Zapata J.M., Reed J.C.;
"p53-inducible human homologue of Drosophila seven in absentia (Siah)
inhibits cell growth: suppression by BAG-1.";
EMBO J. 17:2736-2747(1998).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-40; CYS-41;
CYS-44; CYS-55; HIS-59; ARG-66; LYS-68; ARG-76; HIS-152; HIS-202 AND
LEU-211.
PubMed=9858595; DOI=10.1128/MCB.19.1.724;
Hu G., Fearon E.R.;
"Siah-1 N-terminal RING domain is required for proteolysis function,
and C-terminal sequences regulate oligomerization and binding to
target proteins.";
Mol. Cell. Biol. 19:724-732(1999).
[10]
FUNCTION IN DEGRADATION OF KIF22, AND INTERACTION WITH ALPHA-TUBULIN.
PubMed=11146551; DOI=10.1038/sj.onc.1204002;
Germani A., Bruzzoni-Giovanelli H., Fellous A., Gisselbrecht S.,
Varin-Blank N., Calvo F.;
"SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by
the proteasome pathway during mitosis.";
Oncogene 19:5997-6006(2000).
[11]
FUNCTION IN DEGRADATION OF MYB.
PubMed=10747903; DOI=10.1074/jbc.M000372200;
Tanikawa J., Ichikawa-Iwata E., Kanei-Ishii C., Nakai A.,
Matsuzawa S., Reed J.C., Ishii S.;
"p53 suppresses the c-Myb-induced activation of heat shock
transcription factor 3.";
J. Biol. Chem. 275:15578-15585(2000).
[12]
FUNCTION IN DEGRADATION OF CTNNB1, AND SUBUNIT OF A COMPLEX WITH
UBE2D1; CACYBP; SKP1; APC AND TBL1X.
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).
[13]
FUNCTION IN DEGRADATION OF CTNNB1.
PubMed=11389840; DOI=10.1016/S1097-2765(01)00241-6;
Liu J., Stevens J., Rote C.A., Yost H.J., Hu Y., Neufeld K.L.,
White R.L., Matsunami N.;
"Siah-1 mediates a novel beta-catenin degradation pathway linking p53
to the adenomatous polyposis coli protein.";
Mol. Cell 7:927-936(2001).
[14]
FUNCTION IN DEGRADATION OF POU2AF1, AND SUBCELLULAR LOCATION.
PubMed=11483517; DOI=10.1093/emboj/20.15.4143;
Tiedt R., Bartholdy B.A., Matthias G., Newell J.W., Matthias P.;
"The RING finger protein Siah-1 regulates the level of the
transcriptional coactivator OBF-1.";
EMBO J. 20:4143-4152(2001).
[15]
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).
[16]
FUNCTION IN DEGRADATION OF NUMB.
PubMed=11752454; DOI=10.1073/pnas.261571998;
Susini L., Passer B.J., Amzallag-Elbaz N., Juven-Gershon T.,
Prieur S., Privat N., Tuynder M., Gendron M.-C., Israeel A., Amson R.,
Oren M., Telerman A.;
"Siah-1 binds and regulates the function of Numb.";
Proc. Natl. Acad. Sci. U.S.A. 98:15067-15072(2001).
[17]
FUNCTION IN DEGRADATION OF KLF10.
PubMed=12072443; DOI=10.1074/jbc.M204812200;
Johnsen S.A., Subramaniam M., Monroe D.G., Janknecht R.,
Spelsberg T.C.;
"Modulation of transforming growth factor beta (TGFbeta)/Smad
transcriptional responses through targeted degradation of TGFbeta-
inducible early gene-1 by human seven in absentia homologue.";
J. Biol. Chem. 277:30754-30759(2002).
[18]
FUNCTION IN DEGRADATION OF SNCAIP, AND SUBCELLULAR LOCATION.
PubMed=14506261; DOI=10.1074/jbc.M306347200;
Nagano Y., Yamashita H., Takahashi T., Kishida S., Nakamura T.,
Iseki E., Hattori N., Mizuno Y., Kikuchi A., Matsumoto M.;
"Siah-1 facilitates ubiquitination and degradation of synphilin-1.";
J. Biol. Chem. 278:51504-51514(2003).
[19]
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).
[20]
TISSUE SPECIFICITY.
PubMed=12557228; DOI=10.1002/gcc.10170;
Matsuo K., Satoh S., Okabe H., Nomura A., Maeda T., Yamaoka Y.,
Ikai I.;
"SIAH1 inactivation correlates with tumor progression in
hepatocellular carcinomas.";
Genes Chromosomes Cancer 36:283-291(2003).
[21]
FUNCTION IN DEGRADATION OF RBBP8.
PubMed=14654780; DOI=10.1038/sj.onc.1206994;
Germani A., Prabel A., Mourah S., Podgorniak M.-P., Di Carlo A.,
Ehrlich R., Gisselbrecht S., Varin-Blank N., Calvo F.,
Bruzzoni-Giovanelli H.;
"SIAH-1 interacts with CtIP and promotes its degradation by the
proteasome pathway.";
Oncogene 22:8845-8851(2003).
[22]
INTERACTION WITH CACYBP, AND MUTANTS A; B; C; D AND E.
PubMed=12421809; DOI=10.1074/jbc.M210263200;
Matsuzawa S., Li C., Ni C.-Z., Takayama S., Reed J.C., Ely K.R.;
"Structural analysis of Siah1 and its interactions with Siah-
interacting protein (SIP).";
J. Biol. Chem. 278:1837-1840(2003).
[23]
INTERACTION WITH KHDRBS3.
PubMed=15163637; DOI=10.1093/hmg/ddh165;
Venables J.P., Dalgliesh C., Paronetto M.P., Skitt L., Thornton J.K.,
Saunders P.T., Sette C., Jones K.T., Elliott D.J.;
"SIAH1 targets the alternative splicing factor T-STAR for degradation
by the proteasome.";
Hum. Mol. Genet. 13:1525-1534(2004).
[24]
FUNCTION IN DEGRADATION OF PML, AND MUTANTS A AND D.
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).
[25]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNCAIP AND SNCA, AND
MUTAGENESIS OF CYS-55; HIS-59 AND CYS-72.
PubMed=15064394; DOI=10.1073/pnas.0401081101;
Liani E., Eyal A., Avraham E., Shemer R., Szargel R., Berg D.,
Bornemann A., Riess O., Ross C.A., Rott R., Engelender S.;
"Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
presence in cellular inclusions and Lewy bodies imply a role in
Parkinson's disease.";
Proc. Natl. Acad. Sci. U.S.A. 101:5500-5505(2004).
[26]
FUNCTION, MUTAGENESIS OF SER-19 AND CYS-44, INTERACTION WITH HIPK2,
AND PHOSPHORYLATION AT SER-19 BY ATM AND ATR.
PubMed=18536714; DOI=10.1038/ncb1743;
Winter M., Sombroek D., Dauth I., Moehlenbrink J., Scheuermann K.,
Crone J., Hofmann T.G.;
"Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint
kinases ATM and ATR.";
Nat. Cell Biol. 10:812-824(2008).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[28]
INTERACTION WITH SNCAIP, ENZYME REGULATION, AND FUNCTION.
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).
[29]
FUNCTION IN UBIQUITINATION OF FLT3.
PubMed=20508617; DOI=10.1038/leu.2010.114;
Buchwald M., Pietschmann K., Muller J.P., Bohmer F.D., Heinzel T.,
Kramer O.H.;
"Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3
for proteasomal degradation.";
Leukemia 24:1412-1421(2010).
[30]
FUNCTION.
PubMed=22483617; DOI=10.1016/j.molcel.2012.03.007;
Liu M., Hsu J., Chan C., Li Z., Zhou Q.;
"The ubiquitin ligase Siah1 controls ELL2 stability and formation of
super elongation complexes to modulate gene transcription.";
Mol. Cell 46:325-334(2012).
[31]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 90-282 IN COMPLEX WITH ZINC
IONS AND CACYBP, FUNCTION, MUTAGENESIS OF 198-LYS--ASP-200 AND
MET-252, AND INTERACTION WITH CACYBP.
PubMed=16085652; DOI=10.1074/jbc.M506707200;
Santelli E., Leone M., Li C., Fukushima T., Preece N.E., Olson A.J.,
Ely K.R., Reed J.C., Pellecchia M., Liddington R.C., Matsuzawa S.;
"Structural analysis of Siah1-Siah-interacting protein interactions
and insights into the assembly of an E3 ligase multiprotein complex.";
J. Biol. Chem. 280:34278-34287(2005).
-!- 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 regulation, spermatogenesis
and TNF-alpha signaling. Has some overlapping function with SIAH2.
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:10747903,
ECO:0000269|PubMed:11146551, ECO:0000269|PubMed:11389839,
ECO:0000269|PubMed:11389840, ECO:0000269|PubMed:11483517,
ECO:0000269|PubMed:11483518, ECO:0000269|PubMed:11752454,
ECO:0000269|PubMed:12072443, ECO:0000269|PubMed:14506261,
ECO:0000269|PubMed:14645235, ECO:0000269|PubMed:14654780,
ECO:0000269|PubMed:15064394, ECO:0000269|PubMed:16085652,
ECO:0000269|PubMed:18536714, ECO:0000269|PubMed:19224863,
ECO:0000269|PubMed:20508617, ECO:0000269|PubMed:22483617,
ECO:0000269|PubMed:9334332, ECO:0000269|PubMed:9858595}.
-!- 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.
-!- ENZYME 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 group 1 glutamate receptors
GRM1 and GRM5. Interacts with DAB1, which may inhibit its
activity. Interacts with UBE2E2. Interacts with PEG3. Interacts
with GAPDH; leading to stabilize SIAH1 (By similarity). 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.
Interacts with KHDRBS3. Interacts with SNCAIP and HIPK2.
{ECO:0000250, ECO:0000269|PubMed:11146551,
ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:12421809,
ECO:0000269|PubMed:12810624, ECO:0000269|PubMed:15064394,
ECO:0000269|PubMed:15163637, ECO:0000269|PubMed:16085652,
ECO:0000269|PubMed:18536714, ECO:0000269|PubMed:19224863,
ECO:0000269|PubMed:9334332, ECO:0000269|PubMed:9582267}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-747107, EBI-747107;
Q59GP6:-; NbExp=3; IntAct=EBI-747107, EBI-10243413;
Q9NRN7:AASDHPPT; NbExp=3; IntAct=EBI-747107, EBI-740884;
Q9UHB7:AFF4; NbExp=5; IntAct=EBI-747107, EBI-395282;
Q9UHB7-2:AFF4; NbExp=5; IntAct=EBI-747107, EBI-10261324;
P29972:AQP1; NbExp=3; IntAct=EBI-747107, EBI-745213;
Q7Z3E5-2:ARMC9; NbExp=3; IntAct=EBI-747107, EBI-10256990;
O15265:ATXN7; NbExp=2; IntAct=EBI-747107, EBI-708350;
P41182:BCL6; NbExp=3; IntAct=EBI-747107, EBI-765407;
Q9NVL8:C14orf105; NbExp=3; IntAct=EBI-747107, EBI-10238351;
P40121:CAPG; NbExp=3; IntAct=EBI-747107, EBI-4291044;
Q9UJX2:CDC23; NbExp=3; IntAct=EBI-747107, EBI-396137;
P49427:CDC34; NbExp=3; IntAct=EBI-747107, EBI-975634;
Q8N619:CDK5R1; NbExp=3; IntAct=EBI-747107, EBI-10266998;
Q8TAM4:CDK5R1; NbExp=3; IntAct=EBI-747107, EBI-10271838;
Q9UJV9:DDX41; NbExp=3; IntAct=EBI-747107, EBI-1046350;
Q9Y5T4:DNAJC15; NbExp=3; IntAct=EBI-747107, EBI-10329228;
O14645:DNALI1; NbExp=3; IntAct=EBI-747107, EBI-395638;
P29692:EEF1D; NbExp=4; IntAct=EBI-747107, EBI-358607;
Q8N2X6:EXOC3-AS1; NbExp=3; IntAct=EBI-747107, EBI-749333;
Q86YD7:FAM90A1; NbExp=3; IntAct=EBI-747107, EBI-6658203;
Q01543:FLI1; NbExp=3; IntAct=EBI-747107, EBI-2271018;
Q8TAN2:FZD9; NbExp=3; IntAct=EBI-747107, EBI-741016;
Q8WTR4:GDPD5; NbExp=3; IntAct=EBI-747107, EBI-2833203;
P62805:HIST2H4B; NbExp=3; IntAct=EBI-747107, EBI-302023;
P05111:INHA; NbExp=3; IntAct=EBI-747107, EBI-10194422;
Q9BW62:KATNAL1; NbExp=3; IntAct=EBI-747107, EBI-743591;
P78508:KCNJ10; NbExp=3; IntAct=EBI-747107, EBI-9117877;
Q8IZA0:KIAA0319L; NbExp=3; IntAct=EBI-747107, EBI-5240269;
Q5T5P2-6:KIAA1217; NbExp=3; IntAct=EBI-747107, EBI-10188326;
Q9H0B3:KIAA1683; NbExp=3; IntAct=EBI-747107, EBI-745878;
O60333:KIF1B; NbExp=3; IntAct=EBI-747107, EBI-465633;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-747107, EBI-2125614;
Q53H82:LACTB2; NbExp=3; IntAct=EBI-747107, EBI-3943430;
Q13394:MAB21L1; NbExp=3; IntAct=EBI-747107, EBI-10229059;
P53778:MAPK12; NbExp=3; IntAct=EBI-747107, EBI-602406;
O60336:MAPKBP1; NbExp=3; IntAct=EBI-747107, EBI-947402;
Q70IA8:MOB3C; NbExp=3; IntAct=EBI-747107, EBI-9679267;
Q9H2K0:MTIF3; NbExp=3; IntAct=EBI-747107, EBI-3923617;
P20591:MX1; NbExp=3; IntAct=EBI-747107, EBI-929476;
Q99836:MYD88; NbExp=3; IntAct=EBI-747107, EBI-447677;
Q92692:NECTIN2; NbExp=3; IntAct=EBI-747107, EBI-718419;
Q9H3P2:NELFA; NbExp=3; IntAct=EBI-747107, EBI-5461341;
Q9H6R4-4:NOL6; NbExp=3; IntAct=EBI-747107, EBI-10307896;
P35372:OPRM1; NbExp=4; IntAct=EBI-747107, EBI-2624570;
Q96DC9:OTUB2; NbExp=3; IntAct=EBI-747107, EBI-746259;
Q86TG7:PEG10; NbExp=3; IntAct=EBI-747107, EBI-2858265;
P08237:PFKM; NbExp=3; IntAct=EBI-747107, EBI-514788;
Q8IXK0:PHC2; NbExp=5; IntAct=EBI-747107, EBI-713786;
Q16633:POU2AF1; NbExp=2; IntAct=EBI-747107, EBI-943588;
Q64693:Pou2af1 (xeno); NbExp=5; IntAct=EBI-747107, EBI-943530;
Q8WWY3:PRPF31; NbExp=3; IntAct=EBI-747107, EBI-1567797;
P86479:PRR20C; NbExp=5; IntAct=EBI-747107, EBI-10172814;
Q8WUK0:PTPMT1; NbExp=3; IntAct=EBI-747107, EBI-7199479;
Q9UHX1:PUF60; NbExp=7; IntAct=EBI-747107, EBI-1053259;
P11216:PYGB; NbExp=3; IntAct=EBI-747107, EBI-1047231;
Q2TAL8:QRICH1; NbExp=3; IntAct=EBI-747107, EBI-2798044;
Q14088:RAB33A; NbExp=3; IntAct=EBI-747107, EBI-744685;
Q96B01:RAD51AP1; NbExp=3; IntAct=EBI-747107, EBI-1178724;
Q96B01-2:RAD51AP1; NbExp=3; IntAct=EBI-747107, EBI-1178743;
Q9Y4B4:RAD54L2; NbExp=3; IntAct=EBI-747107, EBI-948156;
Q86WX3:RPS19BP1; NbExp=3; IntAct=EBI-747107, EBI-4479407;
O00560:SDCBP; NbExp=3; IntAct=EBI-747107, EBI-727004;
O43236-6:SEPT4; NbExp=2; IntAct=EBI-747107, EBI-4372019;
Q69ZI1:Sh3rf1 (xeno); NbExp=5; IntAct=EBI-747107, EBI-957380;
Q8NEY3:SPATA4; NbExp=3; IntAct=EBI-747107, EBI-7067221;
Q9H0A9:SPATC1L; NbExp=3; IntAct=EBI-747107, EBI-372911;
O43581:SYT7; NbExp=3; IntAct=EBI-747107, EBI-10184345;
Q9NU19:TBC1D22B; NbExp=3; IntAct=EBI-747107, EBI-8787464;
Q9BTV4:TMEM43; NbExp=3; IntAct=EBI-747107, EBI-721293;
Q6FIE9:TOLLIP; NbExp=3; IntAct=EBI-747107, EBI-10249783;
Q13625-3:TP53BP2; NbExp=3; IntAct=EBI-747107, EBI-10175039;
P36406:TRIM23; NbExp=3; IntAct=EBI-747107, EBI-740098;
P14373:TRIM27; NbExp=3; IntAct=EBI-747107, EBI-719493;
Q9C029:TRIM7; NbExp=3; IntAct=EBI-747107, EBI-2813981;
P61086:UBE2K; NbExp=4; IntAct=EBI-747107, EBI-473850;
O95045:UPP2; NbExp=3; IntAct=EBI-747107, EBI-10191025;
Q9UBK9:UXT; NbExp=3; IntAct=EBI-747107, EBI-357355;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-747107, EBI-741158;
P69713:X (xeno); NbExp=4; IntAct=EBI-747107, EBI-7088789;
P98170:XIAP; NbExp=3; IntAct=EBI-747107, EBI-517127;
A2RRL9:ZBP1; NbExp=3; IntAct=EBI-747107, EBI-10173066;
Q8TBK6:ZCCHC10; NbExp=3; IntAct=EBI-747107, EBI-597063;
Q8WW36:ZCCHC13; NbExp=3; IntAct=EBI-747107, EBI-954111;
Q9BQ24:ZFYVE21; NbExp=3; IntAct=EBI-747107, EBI-2849569;
Q9HA38:ZMAT3; NbExp=3; IntAct=EBI-747107, EBI-2548480;
Q9UQR1:ZNF148; NbExp=3; IntAct=EBI-747107, EBI-2688184;
Q96KM6:ZNF512B; NbExp=3; IntAct=EBI-747107, EBI-1049952;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
cytoplasmic. Partially nuclear.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8IUQ4-1; Sequence=Displayed;
Name=2;
IsoId=Q8IUQ4-2; Sequence=VSP_010166;
Name=3; Synonyms=Siah-1S;
IsoId=Q8IUQ4-3; Sequence=VSP_029210, VSP_029211;
-!- TISSUE SPECIFICITY: Widely expressed at a low level. Down-
regulated in advanced hepatocellular carcinomas.
{ECO:0000269|PubMed:12557228, ECO:0000269|PubMed:9403064}.
-!- 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.
-!- 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}.
-!- PTM: Phosphorylated on Ser-19 by ATM and ATR. This phosphorylation
disrupts SIAH1 interaction with HIPK2, and subsequent proteasomal
degradation of HIPK2. {ECO:0000269|PubMed:18536714}.
-!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U63295; AAC12950.1; -; mRNA.
EMBL; U76247; AAC51907.1; -; mRNA.
EMBL; AJ400626; CAC35542.1; -; Genomic_DNA.
EMBL; EF026094; ABK15529.1; -; mRNA.
EMBL; BX647064; CAE46191.1; -; mRNA.
EMBL; BC035562; AAH35562.1; -; mRNA.
EMBL; BC042550; AAH42550.1; -; mRNA.
EMBL; BC044920; AAH44920.1; -; mRNA.
CCDS; CCDS10735.1; -. [Q8IUQ4-1]
CCDS; CCDS32444.1; -. [Q8IUQ4-2]
RefSeq; NP_001006611.1; NM_001006610.1. [Q8IUQ4-2]
RefSeq; NP_003022.3; NM_003031.3. [Q8IUQ4-1]
RefSeq; XP_006721309.1; XM_006721246.1. [Q8IUQ4-1]
RefSeq; XP_011521581.1; XM_011523279.1. [Q8IUQ4-1]
UniGene; Hs.706828; -.
PDB; 2A25; X-ray; 2.20 A; A=90-282.
PDB; 4C9Z; X-ray; 1.95 A; A/B=91-282.
PDB; 4CA1; X-ray; 1.58 A; A/B=91-282.
PDB; 4I7B; X-ray; 3.00 A; A/C=90-282.
PDB; 4I7C; X-ray; 2.80 A; A/C=90-282.
PDB; 4I7D; X-ray; 2.40 A; A/C=90-282.
PDB; 4X3G; X-ray; 2.34 A; A/B=91-282.
PDB; 5WZZ; X-ray; 2.10 A; A/B/C/D=93-282.
PDBsum; 2A25; -.
PDBsum; 4C9Z; -.
PDBsum; 4CA1; -.
PDBsum; 4I7B; -.
PDBsum; 4I7C; -.
PDBsum; 4I7D; -.
PDBsum; 4X3G; -.
PDBsum; 5WZZ; -.
ProteinModelPortal; Q8IUQ4; -.
SMR; Q8IUQ4; -.
BioGrid; 112372; 164.
CORUM; Q8IUQ4; -.
DIP; DIP-35684N; -.
IntAct; Q8IUQ4; 126.
MINT; MINT-156060; -.
STRING; 9606.ENSP00000349156; -.
iPTMnet; Q8IUQ4; -.
PhosphoSitePlus; Q8IUQ4; -.
BioMuta; SIAH1; -.
DMDM; 46577493; -.
EPD; Q8IUQ4; -.
MaxQB; Q8IUQ4; -.
PaxDb; Q8IUQ4; -.
PeptideAtlas; Q8IUQ4; -.
PRIDE; Q8IUQ4; -.
DNASU; 6477; -.
Ensembl; ENST00000356721; ENSP00000349156; ENSG00000196470. [Q8IUQ4-2]
Ensembl; ENST00000380006; ENSP00000369343; ENSG00000196470. [Q8IUQ4-1]
Ensembl; ENST00000394725; ENSP00000378214; ENSG00000196470. [Q8IUQ4-1]
Ensembl; ENST00000568007; ENSP00000456421; ENSG00000196470. [Q8IUQ4-1]
GeneID; 6477; -.
KEGG; hsa:6477; -.
UCSC; uc002efl.4; human. [Q8IUQ4-1]
CTD; 6477; -.
DisGeNET; 6477; -.
EuPathDB; HostDB:ENSG00000196470.11; -.
GeneCards; SIAH1; -.
HGNC; HGNC:10857; SIAH1.
HPA; CAB018724; -.
MIM; 602212; gene.
neXtProt; NX_Q8IUQ4; -.
OpenTargets; ENSG00000196470; -.
PharmGKB; PA35759; -.
eggNOG; KOG3002; Eukaryota.
eggNOG; ENOG410XVP0; LUCA.
GeneTree; ENSGT00390000005434; -.
HOGENOM; HOG000231487; -.
HOVERGEN; HBG055701; -.
InParanoid; Q8IUQ4; -.
KO; K04506; -.
OMA; EACEFRP; -.
OrthoDB; EOG091G0BPY; -.
PhylomeDB; Q8IUQ4; -.
TreeFam; TF312976; -.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-373752; Netrin-1 signaling.
Reactome; R-HSA-977225; Amyloid fiber formation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q8IUQ4; -.
UniPathway; UPA00143; -.
ChiTaRS; SIAH1; human.
EvolutionaryTrace; Q8IUQ4; -.
GeneWiki; SIAH1; -.
GenomeRNAi; 6477; -.
PRO; PR:Q8IUQ4; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000196470; -.
CleanEx; HS_SIAH1; -.
ExpressionAtlas; Q8IUQ4; baseline and differential.
Genevisible; Q8IUQ4; HS.
GO; GO:0030877; C:beta-catenin destruction complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0030163; P:protein catabolic process; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
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; Alternative splicing; 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 SIAH1.
/FTId=PRO_0000056163.
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.
METAL 98 98 Zinc 1. {ECO:0000250}.
METAL 105 105 Zinc 1. {ECO:0000250}.
METAL 117 117 Zinc 1. {ECO:0000250}.
METAL 121 121 Zinc 1. {ECO:0000250}.
METAL 128 128 Zinc 2.
METAL 135 135 Zinc 2.
METAL 147 147 Zinc 2.
METAL 152 152 Zinc 2.
MOD_RES 19 19 Phosphoserine; by ATM and ATR.
{ECO:0000269|PubMed:18536714}.
VAR_SEQ 1 1 M -> MTGKATPPSLYSWRGVLFTCLPAARTRKRKEM (in
isoform 2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_010166.
VAR_SEQ 193 195 LEK -> DLS (in isoform 3).
{ECO:0000303|PubMed:17420721}.
/FTId=VSP_029210.
VAR_SEQ 196 282 Missing (in isoform 3).
{ECO:0000303|PubMed:17420721}.
/FTId=VSP_029211.
MUTAGEN 19 19 S->A: Impaired ATM mediated
phosphorylation, but normal interaction
with HIPK2 and HIPK2 subsequent
proteasomal degradation.
{ECO:0000269|PubMed:18536714}.
MUTAGEN 19 19 S->D: Reduced interaction with HIPK2 and
HIPK2 subsequent proteasomal degradation.
{ECO:0000269|PubMed:18536714}.
MUTAGEN 40 40 E->R: Loss of function.
{ECO:0000269|PubMed:9858595}.
MUTAGEN 41 41 C->S: Loss of function; when associated
with S-44. {ECO:0000269|PubMed:9858595}.
MUTAGEN 44 44 C->S: Loss of function.
{ECO:0000269|PubMed:18536714,
ECO:0000269|PubMed:9858595}.
MUTAGEN 55 55 C->A: Loss of function; when associated
with A-59 and S-72.
{ECO:0000269|PubMed:15064394,
ECO:0000269|PubMed:9858595}.
MUTAGEN 55 55 C->S: Loss of function; when associated
with Y-59. {ECO:0000269|PubMed:15064394,
ECO:0000269|PubMed:9858595}.
MUTAGEN 59 59 H->A: Loss of function; when associated
with A-55 and S-72.
{ECO:0000269|PubMed:15064394,
ECO:0000269|PubMed:9858595}.
MUTAGEN 59 59 H->Y: Loss of function.
{ECO:0000269|PubMed:15064394,
ECO:0000269|PubMed:9858595}.
MUTAGEN 66 66 R->L: Decreased activity; when associated
with T-68. {ECO:0000269|PubMed:9858595}.
MUTAGEN 68 68 K->T: Decreased activity; when associated
with L-66. {ECO:0000269|PubMed:9858595}.
MUTAGEN 72 72 C->S: Loss of function; when associated
with A-55 and A-59.
{ECO:0000269|PubMed:15064394}.
MUTAGEN 76 76 R->E: Decreased activity.
{ECO:0000269|PubMed:9858595}.
MUTAGEN 124 124 R->A: In D; does not impair its ability
to interact with CACYBP and degrade
CTNNB1 and PML; when associated with A-
214; A-215; A-231 and A-232.
MUTAGEN 142 142 D->A: In E; does not impair its ability
to interact with CACYBP and degrade
CTNNB1; when associated with A-151.
MUTAGEN 151 151 Q->A: In E; does not impair its ability
to interact with CACYBP and degrade
CTNNB1; when associated with A-142.
MUTAGEN 152 152 H->Y: Abolishes ability to degrade DCC.
{ECO:0000269|PubMed:9858595}.
MUTAGEN 161 162 ED->AA: In A; does not impair its ability
to degrade PML while it abolishes its
ability to interact with CACYBP and
degrade CTNNB1; when associated with A-
226 and A-237.
MUTAGEN 198 200 KYD->GDG: Impairs CTNNB1 degradation.
{ECO:0000269|PubMed:16085652}.
MUTAGEN 202 202 H->Y: No effect.
{ECO:0000269|PubMed:9858595}.
MUTAGEN 211 211 L->R: Abolishes ability to degrade DCC.
{ECO:0000269|PubMed:9858595}.
MUTAGEN 214 215 TR->AA: In D; does not impair its ability
to interact with CACYBP and degrade
CTNNB1 and PML; when associated with A-
124; A-231 and A-232.
MUTAGEN 224 224 R->A: In C; does not impair its ability
to interact with CACYBP and degrade
CTNNB1; when associated with A-233.
MUTAGEN 226 226 E->A: In A; does not impair its ability
to degrade PML while it abolishes its
ability to interact with CACYBP and
degrade CTNNB1; when associated with A-
161; A-162 and A-237.
MUTAGEN 231 232 RR->AA: In D; does not impair its ability
to interact with CACYBP and degrade
CTNNB1 and PML; when associated with A-
124; A-214 and A-215.
MUTAGEN 233 233 R->A: In C; does not impair its ability
to interact with CACYBP and degrade
CTNNB1; when associated with A-233.
MUTAGEN 237 237 E->A: In A; does not impair its ability
to degrade PML while it abolishes its
ability to interact with CACYBP and
degrade CTNNB1; when associated with A-
161; A-162 and A-226.
MUTAGEN 252 252 M->D,K: Impairs CTNNB1 degradation.
{ECO:0000269|PubMed:16085652}.
MUTAGEN 253 253 N->A: In B; does not impair its ability
to interact with CACYBP and degrade
CTNNB1; when associated with A-265.
MUTAGEN 265 265 Q->A: In B; does not impair its ability
to interact with CACYBP and degrade
CTNNB1; when associated with A-253.
CONFLICT 173 173 P -> S (in Ref. 5; CAE46191).
{ECO:0000305}.
CONFLICT 245 245 E -> G (in Ref. 5; CAE46191).
{ECO:0000305}.
STRAND 95 97 {ECO:0000244|PDB:4X3G}.
HELIX 101 103 {ECO:0000244|PDB:4CA1}.
STRAND 108 110 {ECO:0000244|PDB:4X3G}.
HELIX 111 120 {ECO:0000244|PDB:4CA1}.
STRAND 122 124 {ECO:0000244|PDB:4I7B}.
STRAND 130 134 {ECO:0000244|PDB:4CA1}.
HELIX 141 143 {ECO:0000244|PDB:4CA1}.
HELIX 144 151 {ECO:0000244|PDB:4CA1}.
STRAND 156 167 {ECO:0000244|PDB:4CA1}.
STRAND 172 184 {ECO:0000244|PDB:4CA1}.
STRAND 187 197 {ECO:0000244|PDB:4CA1}.
STRAND 203 213 {ECO:0000244|PDB:4CA1}.
HELIX 215 218 {ECO:0000244|PDB:4CA1}.
STRAND 221 229 {ECO:0000244|PDB:4CA1}.
STRAND 232 238 {ECO:0000244|PDB:4CA1}.
TURN 243 245 {ECO:0000244|PDB:4CA1}.
HELIX 248 252 {ECO:0000244|PDB:4CA1}.
STRAND 256 260 {ECO:0000244|PDB:4CA1}.
HELIX 261 267 {ECO:0000244|PDB:4CA1}.
STRAND 272 281 {ECO:0000244|PDB:4CA1}.
SEQUENCE 282 AA; 31123 MW; FA0698D0DC1B0A15 CRC64;
MSRQTATALP TGTSKCPPSQ RVPALTGTTA SNNDLASLFE CPVCFDYVLP PILQCQSGHL
VCSNCRPKLT CCPTCRGPLG SIRNLAMEKV ANSVLFPCKY ASSGCEITLP HTEKADHEEL
CEFRPYSCPC PGASCKWQGS LDAVMPHLMH QHKSITTLQG EDIVFLATDI NLPGAVDWVM
MQSCFGFHFM LVLEKQEKYD GHQQFFAIVQ LIGTRKQAEN FAYRLELNGH RRRLTWEATP
RSIHEGIATA IMNSDCLVFD TSIAQLFAEN GNLGINVTIS MC


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