Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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_RAT               Reviewed;         282 AA.
Q920M9; Q06984;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 2.
05-DEC-2018, entry version 140.
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=Siah1a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN DEGRADATION OF SYP,
SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2E2.
STRAIN=Sprague-Dawley;
PubMed=11786535; DOI=10.1074/jbc.M107857200;
Wheeler T.C., Chin L.-S., Li Y., Roudabush F.L., Li L.;
"Regulation of synaptophysin degradation by mammalian homologues of
Seven in Absentia.";
J. Biol. Chem. 277:10273-10282(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Yamaguchi A., Hori O., Tohyama M.;
"Rat Siah1A.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH GRM1 AND GRM5.
PubMed=10469171; DOI=10.1046/j.1365-2443.1999.00269.x;
Ishikawa K., Nash S.R., Nishimune A., Neki A., Kaneko S.,
Nakanishi S.;
"Competitive interaction of seven in absentia homolog-1A and
Ca2+/calmodulin with the cytoplasmic tail of group 1 metabotropic
glutamate receptors.";
Genes Cells 4:381-390(1999).
[4]
INTERACTION WITH SNCAIP.
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).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GAPDH.
PubMed=15951807; DOI=10.1038/ncb1268;
Hara M.R., Agrawal N., Kim S.F., Cascio M.B., Fujimuro M., Ozeki Y.,
Takahashi M., Cheah J.H., Tankou S.K., Hester L.D., Ferris C.D.,
Hayward S.D., Snyder S.H., Sawa A.;
"S-nitrosylated GAPDH initiates apoptotic cell death by nuclear
translocation following Siah1 binding.";
Nat. Cell Biol. 7:665-674(2005).
[6]
INTERACTION WITH SNCAIP, AND SUBCELLULAR LOCATION.
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).
-!- 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), 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. Induces
apoptosis in cooperation with PEG3 (By similarity). 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:0000250,
ECO:0000269|PubMed:11786535, ECO:0000269|PubMed:15951807}.
-!- 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. 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 PEG3 and HIPK2 (By
similarity). Interacts with group 1 glutamate receptors GRM1 and
GRM5. Interacts with DAB1, which may inhibit its activity.
Interacts with UBE2E2. Interacts with SNCAIP. Interacts with
GAPDH; leading to stabilize SIAH1. {ECO:0000250,
ECO:0000269|PubMed:10469171, ECO:0000269|PubMed:11786535,
ECO:0000269|PubMed:15064394, ECO:0000269|PubMed:15951807,
ECO:0000269|PubMed:19224863}.
-!- INTERACTION:
O88778:Bsn; NbExp=3; IntAct=EBI-957514, EBI-2271660;
Q9JKS6:Pclo; NbExp=2; IntAct=EBI-957514, EBI-2271602;
Q71F54:Sh3rf1; NbExp=2; IntAct=EBI-957514, EBI-957526;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
cytoplasmic. Partially nuclear.
-!- DOMAIN: The RING-type zinc finger domain is essential for
ubiquitin ligase activity. {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB70753.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF389476; AAL91362.1; -; mRNA.
EMBL; AB067814; BAB70753.1; ALT_INIT; mRNA.
RefSeq; NP_543181.2; NM_080905.2.
RefSeq; XP_008770567.1; XM_008772345.2.
UniGene; Rn.73937; -.
ProteinModelPortal; Q920M9; -.
SMR; Q920M9; -.
BioGrid; 250875; 7.
DIP; DIP-35686N; -.
IntAct; Q920M9; 4.
MINT; Q920M9; -.
STRING; 10116.ENSRNOP00000020329; -.
PaxDb; Q920M9; -.
PRIDE; Q920M9; -.
Ensembl; ENSRNOT00000020329; ENSRNOP00000020329; ENSRNOG00000015143.
GeneID; 140941; -.
KEGG; rno:140941; -.
CTD; 6477; -.
RGD; 620449; Siah1.
eggNOG; KOG3002; Eukaryota.
eggNOG; ENOG410XVP0; LUCA.
GeneTree; ENSGT00940000154837; -.
HOGENOM; HOG000231487; -.
HOVERGEN; HBG055701; -.
InParanoid; Q920M9; -.
KO; K04506; -.
OMA; EACEFRP; -.
OrthoDB; EOG091G0BPY; -.
PhylomeDB; Q920M9; -.
TreeFam; TF312976; -.
Reactome; R-RNO-373752; Netrin-1 signaling.
Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:Q920M9; -.
Proteomes; UP000002494; Chromosome 19.
Bgee; ENSRNOG00000015143; Expressed in 10 organ(s), highest expression level in lung.
ExpressionAtlas; Q920M9; baseline and differential.
Genevisible; Q920M9; RN.
GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:RGD.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IMP:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0031648; P:protein destabilization; IMP:RGD.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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;
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_0000056166.
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. {ECO:0000250}.
METAL 135 135 Zinc 2. {ECO:0000250}.
METAL 147 147 Zinc 2. {ECO:0000250}.
METAL 152 152 Zinc 2. {ECO:0000250}.
MOD_RES 19 19 Phosphoserine; by ATM and ATR.
{ECO:0000250|UniProtKB:Q8IUQ4}.
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


Related products :

Catalog number Product name Quantity
EIAAB38421 E3 ubiquitin-protein ligase SIAH1,Rat,Rattus norvegicus,Seven in absentia homolog 1,Siah1,Siah-1,Siah1a,Siah-1a
EIAAB38420 E3 ubiquitin-protein ligase SIAH1,Homo sapiens,Human,HUMSIAH,Seven in absentia homolog 1,SIAH1,Siah-1,Siah-1a
18-003-43198 E3 ubiquitin-protein ligase SIAH1 - EC 6.3.2.-; Seven in absentia homolog 1; Siah-1; Siah-1a Polyclonal 0.1 mg Protein A
28-017 SIAH1 is a protein that is a member of the seven in absentia homolog (SIAH) family. The protein is an E3 ligase and is involved in ubiquitination and proteasome-mediated degradation of specific protei 0.1 mg
28-820 SIAH1 is a protein that is a member of the seven in absentia homolog (SIAH) family. The protein is an E3 ligase and is involved in ubiquitination and proteasome-mediated degradation of specific protei 0.1 mg
18-783-78616 GOAT ANTI HUMAN SIAH-1 - EC 6.3.2.-; Seven in absentia homolog 1; Siah-1; Siah-1a Polyclonal 0.1 mg
EIAAB38424 E3 ubiquitin-protein ligase SIAH2,Rat,Rattus norvegicus,Seven in absentia homolog 2,Siah2,Siah-2
EIAAB38422 E3 ubiquitin-protein ligase SIAH2,Mouse,mSiah2,Mus musculus,Seven in absentia homolog 2,Siah2,Siah-2
EIAAB38423 E3 ubiquitin-protein ligase SIAH2,Homo sapiens,hSiah2,Human,Seven in absentia homolog 2,SIAH2,Siah-2
EIAAB38375 E3 ubiquitin-protein ligase SIAH1B,Mouse,Mus musculus,Seven in absentia homolog 1b,Siah1b,Siah1b,Siah-1b
EIAAB38374 E3 ubiquitin-protein ligase SIAH1A,Mouse,mSiah-1a,Mus musculus,Seven in absentia homolog 1a,Siah1a,Siah1a,Siah-1a
CSB-EL021287HU Human E3 ubiquitin-protein ligase SIAH1(SIAH1) ELISA kit SpeciesHuman 96T
CSB-EL021287HU Human E3 ubiquitin-protein ligase SIAH1(SIAH1) ELISA kit 96T
CSB-EL021287RA Rat E3 ubiquitin-protein ligase SIAH1(SIAH1) ELISA kit SpeciesRat 96T
CSB-EL021287RA Rat E3 ubiquitin-protein ligase SIAH1(SIAH1) ELISA kit 96T
ARP34163_T200 Anti-Ubiquitin ligase SIAH1 (SIAH1) Species_Reactivity: Human
enz-640 Recombinant Human Siah E3 Ubiquitin Protein Ligase 1 1mg
enz-640 Recombinant Human Siah E3 Ubiquitin Protein Ligase 1 2
REN-640 Recombinant Human Siah E3 Ubiquitin Protein Ligase 1 2
enz-640 Recombinant Human Siah E3 Ubiquitin Protein Ligase 1 10
SIAH1 SIAH1 Gene seven in absentia homolog 1 (Drosophila)
enz-640 Recombinant Human Siah E3 Ubiquitin Protein Ligase 1 ENZYMES 10
enz-640 Recombinant Human Siah E3 Ubiquitin Protein Ligase 1 ENZYMES 2
enz-640 Recombinant Human Siah E3 Ubiquitin Protein Ligase 1 ENZYMES 1mg
X1854B SIAH1, E3 Ubiquitin Ligase type: Blocking Peptide 50


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur