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E3 ubiquitin-protein ligase RNF34 (EC 2.3.2.27) (Caspase regulator CARP1) (Caspases-8 and -10-associated RING finger protein 1) (CARP-1) (FYVE-RING finger protein Momo) (Human RING finger homologous to inhibitor of apoptosis protein) (hRFI) (RING finger protein 34) (RING finger protein RIFF) (RING-type E3 ubiquitin transferase RNF34)

 RNF34_HUMAN             Reviewed;         372 AA.
Q969K3; B7Z933; Q8NG47; Q9H6W8;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
18-JUL-2018, entry version 154.
RecName: Full=E3 ubiquitin-protein ligase RNF34 {ECO:0000305};
EC=2.3.2.27 {ECO:0000269|PubMed:25012219, ECO:0000269|Ref.13};
AltName: Full=Caspase regulator CARP1 {ECO:0000305};
AltName: Full=Caspases-8 and -10-associated RING finger protein 1 {ECO:0000303|PubMed:15069192};
Short=CARP-1 {ECO:0000303|PubMed:15069192};
AltName: Full=FYVE-RING finger protein Momo {ECO:0000250|UniProtKB:Q6AYH3};
AltName: Full=Human RING finger homologous to inhibitor of apoptosis protein {ECO:0000303|PubMed:12118383};
Short=hRFI {ECO:0000303|PubMed:12118383};
AltName: Full=RING finger protein 34 {ECO:0000312|HGNC:HGNC:17297};
AltName: Full=RING finger protein RIFF {ECO:0000303|Ref.2};
AltName: Full=RING-type E3 ubiquitin transferase RNF34 {ECO:0000305};
Name=RNF34 {ECO:0000312|HGNC:HGNC:17297};
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 2), FUNCTION, SUBCELLULAR
LOCATION, CLEAVAGE BY CASPASE-3, AND TISSUE SPECIFICITY.
PubMed=12118383; DOI=10.1038/sj.onc.1205627;
Sasaki S., Nakamura T., Arakawa H., Mori M., Watanabe T., Nagawa H.,
Croce C.M.;
"Isolation and characterization of a novel gene, hRFI, preferentially
expressed in esophageal cancer.";
Oncogene 21:5024-5030(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Olsson P.-A., Lindholm D.;
"Cloning of RIFF, a novel RING finger FYVE finger protein expressed in
human fetal brain.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kanbe D., Araki K., Nawa H.;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
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).
[8]
FUNCTION, INTERACTION WITH CASP8 AND CASP10, MUTAGENESIS OF HIS-342,
PROTEOLYTIC DEGRADATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15069192; DOI=10.1073/pnas.0307459101;
McDonald E.R. III, El-Deiry W.S.;
"Suppression of caspase-8- and -10-associated RING proteins results in
sensitization to death ligands and inhibition of tumor cell growth.";
Proc. Natl. Acad. Sci. U.S.A. 101:6170-6175(2004).
[9]
FUNCTION.
PubMed=15897238; DOI=10.1158/1535-7163.MCT-05-0020;
Konishi T., Sasaki S., Watanabe T., Kitayama J., Nagawa H.;
"Overexpression of hRFI (human RING finger homologous to inhibitor of
apoptosis protein type) inhibits death receptor-mediated apoptosis in
colorectal cancer cells.";
Mol. Cancer Ther. 4:743-750(2005).
[10]
FUNCTION, AND INTERACTION WITH P53/TP53.
PubMed=17121812; DOI=10.1074/jbc.M610793200;
Yang W., Rozan L.M., McDonald E.R. III, Navaraj A., Liu J.J.,
Matthew E.M., Wang W., Dicker D.T., El-Deiry W.S.;
"CARPs are ubiquitin ligases that promote MDM2-independent p53 and
phospho-p53ser20 degradation.";
J. Biol. Chem. 282:3273-3281(2007).
[11]
FUNCTION, AND INTERACTION WITH MDM2 AND P53/TP53.
PubMed=18382127; DOI=10.4161/cc.7.5.5701;
Yang W., Dicker D.T., Chen J., El-Deiry W.S.;
"CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing
MDM2.";
Cell Cycle 7:670-682(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND 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).
[13]
FUNCTION, INTERACTION WITH RIPK1, AND PATHWAY.
DOI=10.1016/j.cub.2008.11.041;
Liao W., Fujita K., Xiao Q., Tchikov V., Yang W., Gunsor M.,
Garfield S., Goldsmith P., El-Deiry W.S., Schuetze S.,
Srinivasula S.M.;
"Response: CARP1 regulates induction of NF-kappaB by TNFalpha.";
Curr. Biol. 19:R17-R19(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
FUNCTION, INTERACTION WITH PPARGC1A, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF CYS-328.
PubMed=22064484; DOI=10.1128/MCB.05674-11;
Wei P., Pan D., Mao C., Wang Y.X.;
"RNF34 is a cold-regulated E3 ubiquitin ligase for PGC-1alpha and
modulates brown fat cell metabolism.";
Mol. Cell. Biol. 32:266-275(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-254, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
FUNCTION, AND INTERACTION WITH NOD1.
PubMed=25012219; DOI=10.1159/000362972;
Zhang R., Zhao J., Song Y., Wang X., Wang L., Xu J., Song C., Liu F.;
"The E3 ligase RNF34 is a novel negative regulator of the NOD1
pathway.";
Cell. Physiol. Biochem. 33:1954-1962(2014).
-!- FUNCTION: E3 ubiquitin-protein ligase that regulates several
biological processes through the ubiquitin-mediated proteasomal
degradation of various target proteins. Ubiquitinates the caspases
CASP8 and CASP10, promoting their proteasomal degradation, to
negatively regulate cell death downstream of death domain
receptors in the extrinsic pathway of apoptosis (PubMed:15069192).
May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its
subsequent proteasomal degradation thereby indirectly regulating
the tumor necrosis factor-mediated signaling pathway (Ref.13).
Negatively regulates p53/TP53 through its direct ubiquitination
and targeting to proteasomal degradation (PubMed:17121812).
Indirectly, may also negatively regulate p53/TP53 through
ubiquitination and degradation of SFN (PubMed:18382127). Mediates
PPARGC1A proteasomal degradation probably through ubiquitination
thereby indirectly regulating the metabolism of brown fat cells
(PubMed:22064484). Possibly involved in innate immunity, through
'Lys-48'-linked polyubiquitination of NOD1 and its subsequent
proteasomal degradation (PubMed:25012219).
{ECO:0000269|PubMed:12118383, ECO:0000269|PubMed:15069192,
ECO:0000269|PubMed:15897238, ECO:0000269|PubMed:17121812,
ECO:0000269|PubMed:22064484, ECO:0000269|PubMed:25012219,
ECO:0000269|Ref.13, ECO:0000303|PubMed:18382127}.
-!- 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:25012219,
ECO:0000269|Ref.13}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|Ref.13}.
-!- SUBUNIT: Interacts with CASP8 and CASP10. Interacts (via RING-type
zinc finger) with PPARGC1A. Interacts with NOD1. Interacts with
p53/TP53; involved in p53/TP53 ubiquitination. Interacts (via
RING-type zinc finger) with MDM2; the interaction stabilizes MDM2.
{ECO:0000269|PubMed:12118383, ECO:0000269|PubMed:15069192,
ECO:0000269|PubMed:17121812, ECO:0000269|PubMed:18382127,
ECO:0000269|PubMed:22064484, ECO:0000269|PubMed:25012219,
ECO:0000305}.
-!- INTERACTION:
Q92624:APPBP2; NbExp=3; IntAct=EBI-2340642, EBI-743771;
Q14790:CASP8; NbExp=3; IntAct=EBI-2340642, EBI-78060;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15069192};
Peripheral membrane protein {ECO:0000305}. Endomembrane system
{ECO:0000250|UniProtKB:Q6AYH3}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q6AYH3}. Nucleus
{ECO:0000269|PubMed:22064484}. Nucleus speckle
{ECO:0000269|PubMed:12118383}. Cytoplasm, cytosol
{ECO:0000269|PubMed:15069192}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q969K3-1; Sequence=Displayed;
Name=2;
IsoId=Q969K3-2; Sequence=VSP_038341;
-!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, liver,
skeletal muscle, kidney, pancreas, spleen, thymus, prostate,
testis, ovary, colon and leukocytes. {ECO:0000269|PubMed:12118383,
ECO:0000269|PubMed:15069192}.
-!- DOMAIN: The RING-type zinc finger is required for the
ubiquitination of target proteins. {ECO:0000303|PubMed:25012219}.
-!- DOMAIN: The FYVE-type zinc finger domain is required for
localization and may confer affinity for cellular compartments
enriched in phosphatidylinositol 5-phosphate and
phosphatidylinositol 3-phosphate phospholipids.
{ECO:0000303|PubMed:15069192}.
-!- PTM: Autoubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q6AYH3}.
-!- PTM: Proteolytically cleaved by caspases upon induction of
apoptosis by TNF. {ECO:0000269|PubMed:12118383}.
-!- SEQUENCE CAUTION:
Sequence=BAH14169.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AB084914; BAC11802.1; -; mRNA.
EMBL; AF306709; AAK51328.1; -; mRNA.
EMBL; AY098934; AAM29180.1; -; mRNA.
EMBL; AK304366; BAH14169.1; ALT_SEQ; mRNA.
EMBL; AK025439; BAB15132.1; -; mRNA.
EMBL; BT007283; AAP35947.1; -; mRNA.
EMBL; CR457342; CAG33623.1; -; mRNA.
EMBL; BC007826; AAH07826.1; -; mRNA.
CCDS; CCDS31915.1; -. [Q969K3-1]
CCDS; CCDS9221.1; -. [Q969K3-2]
RefSeq; NP_001243787.1; NM_001256858.1.
RefSeq; NP_079402.2; NM_025126.3. [Q969K3-1]
RefSeq; NP_919247.1; NM_194271.2. [Q969K3-2]
UniGene; Hs.292804; -.
ProteinModelPortal; Q969K3; -.
SMR; Q969K3; -.
BioGrid; 123169; 30.
IntAct; Q969K3; 10.
STRING; 9606.ENSP00000376258; -.
iPTMnet; Q969K3; -.
PhosphoSitePlus; Q969K3; -.
BioMuta; RNF34; -.
DMDM; 74760679; -.
EPD; Q969K3; -.
MaxQB; Q969K3; -.
PaxDb; Q969K3; -.
PeptideAtlas; Q969K3; -.
PRIDE; Q969K3; -.
ProteomicsDB; 75779; -.
ProteomicsDB; 75780; -. [Q969K3-2]
DNASU; 80196; -.
Ensembl; ENST00000361234; ENSP00000355137; ENSG00000170633. [Q969K3-1]
Ensembl; ENST00000392465; ENSP00000376258; ENSG00000170633. [Q969K3-2]
GeneID; 80196; -.
KEGG; hsa:80196; -.
UCSC; uc001uak.3; human. [Q969K3-1]
CTD; 80196; -.
DisGeNET; 80196; -.
EuPathDB; HostDB:ENSG00000170633.16; -.
GeneCards; RNF34; -.
HGNC; HGNC:17297; RNF34.
HPA; HPA074151; -.
MIM; 608299; gene.
neXtProt; NX_Q969K3; -.
OpenTargets; ENSG00000170633; -.
PharmGKB; PA34436; -.
eggNOG; ENOG410IMEF; Eukaryota.
eggNOG; ENOG410Y1GP; LUCA.
GeneTree; ENSGT00390000012719; -.
HOGENOM; HOG000068080; -.
HOVERGEN; HBG055079; -.
InParanoid; Q969K3; -.
KO; K20804; -.
PhylomeDB; Q969K3; -.
TreeFam; TF325195; -.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q969K3; -.
UniPathway; UPA00143; -.
ChiTaRS; RNF34; human.
GeneWiki; RNF34; -.
GenomeRNAi; 80196; -.
PRO; PR:Q969K3; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000170633; -.
CleanEx; HS_RNF34; -.
ExpressionAtlas; Q969K3; baseline and differential.
Genevisible; Q969K3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0070417; P:cellular response to cold; IEA:Ensembl.
GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:UniProtKB.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:2000374; P:regulation of oxygen metabolic process; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR036361; SAP_dom_sf.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
SMART; SM00184; RING; 1.
SUPFAM; SSF57903; SSF57903; 1.
SUPFAM; SSF68906; SSF68906; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Cell membrane; Complete proteome;
Cytoplasm; Membrane; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 372 E3 ubiquitin-protein ligase RNF34.
/FTId=PRO_0000056072.
DOMAIN 115 134 SAP 1.
DOMAIN 264 278 SAP 2.
ZN_FING 56 107 FYVE-type.
ZN_FING 325 360 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COMPBIAS 223 234 Asp-rich.
SITE 232 233 Cleavage; by caspase-3.
{ECO:0000269|PubMed:12118383}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000250|UniProtKB:Q99KR6}.
VAR_SEQ 1 1 M -> MR (in isoform 2).
{ECO:0000303|PubMed:12118383,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_038341.
MUTAGEN 328 328 C->A: Loss of E3 ubiquitin protein ligase
activity. {ECO:0000303|PubMed:22064484}.
MUTAGEN 342 342 H->A: Loss of E3 ubiquitin protein ligase
activity. {ECO:0000269|PubMed:15069192}.
CONFLICT 183 183 Y -> C (in Ref. 4; BAB15132).
{ECO:0000305}.
CONFLICT 238 238 N -> D (in Ref. 4; BAB15132).
{ECO:0000305}.
CONFLICT 333 333 I -> V (in Ref. 4; BAB15132).
{ECO:0000305}.
SEQUENCE 372 AA; 41641 MW; C044B83BD8591FFA CRC64;
MKAGATSMWA SCCGLLNEVM GTGAVRGQQS AFAGATGPFR FTPNPEFSTY PPAATEGPNI
VCKACGLSFS VFRKKHVCCD CKKDFCSVCS VLQENLRRCS TCHLLQETAF QRPQLMRLKV
KDLRQYLILR NIPIDTCREK EDLVDLVLCH HGLGSEDDMD TSSLNSSRSQ TSSFFTRSFF
SNYTAPSATM SSFQGELMDG DQTSRSGVPA QVQSEITSAN TEDDDDDDDE DDDDEEENAE
DRNPGLSKER VRASLSDLSS LDDVEGMSVR QLKEILARNF VNYSGCCEKW ELVEKVNRLY
KENEENQKSY GERLQLQDEE DDSLCRICMD AVIDCVLLEC GHMVTCTKCG KRMSECPICR
QYVVRAVHVF KS


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EIAAB35573 E3 ubiquitin-protein ligase RNF34,Mouse,Mus musculus,Phafin-1,RING finger protein 34,RING finger protein RIFF,Rnf34
EIAAB35572 E3 ubiquitin-protein ligase RNF34,Rat,Rattus norvegicus,RING finger protein 34,RING finger protein MOMO,Rnf34
EIAAB45299 E3 ubiquitin-protein ligase UHRF2,Homo sapiens,Human,NIRF,Np95_ICBP90-like RING finger protein,Np95-like RING finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,RING finger protein 107
EIAAB43947 E3 ubiquitin-protein ligase TRIM63,Homo sapiens,Human,IRF,Iris RING finger protein,MuRF1,MURF1,MuRF-1,Muscle-specific RING finger protein 1,RING finger protein 28,RNF28,SMRZ,Striated muscle RING zinc
EIAAB35413 E3 ubiquitin-protein ligase RNF138,hNARF,Homo sapiens,HSD4,HSD-4,Human,NARF,Nemo-like kinase-associated RING finger protein,NLK-associated RING finger protein,RING finger protein 138,RNF138
EIAAB35549 E3 ubiquitin-protein ligase RLIM,Homo sapiens,Human,LIM domain-interacting RING finger protein,Renal carcinoma antigen NY-REN-43,RING finger LIM domain-binding protein,RING finger protein 12,RLIM,R-LI
18-003-42502 Ubiquitin ligase protein RING2 - EC 6.3.2.-; RING finger protein 2; RING finger protein 1B; RING1b; RING finger protein BAP-1; DinG protein; Huntingtin-interacting protein 2-interacting protein 3; HIP 0.1 mg Protein A
18-003-42501 Ubiquitin ligase protein RING2 - EC 6.3.2.-; RING finger protein 2; RING finger protein 1B; RING1b; RING finger protein BAP-1; DinG protein; Huntingtin-interacting protein 2-interacting protein 3; HIP 0.05 mg Aff Pur
EIAAB34369 E3 ubiquitin-protein ligase rififylin,FYVE-RING finger protein Sakura,Rat,Rattus norvegicus,Rffl,RING finger and FYVE-like domain-containing protein 1
EIAAB24906 Homo sapiens,Human,Makorin RING finger protein pseudogene 4,Makorin RING finger protein pseudogene 5,MKRN4,MKRN4P,MKRNP5,Putative E3 ubiquitin-protein ligase makorin-4,RING finger protein 64,RNF64,Zin
EIAAB43990 BERP,Brain-expressed RING finger protein,Homo sapiens,Human,RING finger protein 22,RING finger protein 97,RNF22,RNF97,TRIM3,Tripartite motif-containing protein 3
EIAAB35550 E3 ubiquitin-protein ligase RLIM,LIM domain-interacting RING finger protein,Mouse,Mus musculus,RING finger LIM domain-binding protein,RING finger protein 12,Rlim,R-LIM,Rnf12
EIAAB43957 Mouse,Mus musculus,RING finger B-box coiled-coil transcription factor,RING finger protein 36,Rnf36,Testis-specific RING finger protein,Trif,Trim69,Tripartite motif-containing protein 69
EIAAB30145 Homo sapiens,Human,MBLR,Mel18 and Bmi1-like RING finger,PCGF6,Polycomb group RING finger protein 6,RING finger protein 134,RNF134
EIAAB30144 Mblr,Mel18 and Bmi1-like RING finger,Mouse,Mus musculus,Pcgf6,Polycomb group RING finger protein 6,RING finger protein 134,Rnf134
EIAAB38244 E3 ubiquitin-protein ligase SH3RF1,Homo sapiens,Human,KIAA1494,Plenty of SH3s,POSH,Protein POSH,RING finger protein 142,RNF142,SH3 domain-containing RING finger protein 1,SH3 multiple domains protein
EIAAB38246 Heart protein phosphatase 1-binding protein,HEPP1,Homo sapiens,Human,Putative E3 ubiquitin-protein ligase SH3RF2,RING finger protein 158,RNF158,SH3 domain-containing RING finger protein 2,SH3RF2
EIAAB45298 E3 ubiquitin-protein ligase UHRF2,Mouse,Mus musculus,NIRF,Nirf,Np95-like ring finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,Ubiquitin-like PHD and RING finger domain-containing pr
EIAAB43998 GERP,Glioblastoma-expressed RING finger protein,Homo sapiens,Human,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,RNF27,TRIM8,Tripartite motif-containing protein 8
EIAAB34424 Constitutive photomorphogenesis protein 1 homolog,COP1,E3 ubiquitin-protein ligase RFWD2,hCOP1,Homo sapiens,Human,RFWD2,RING finger and WD repeat domain protein 2,RING finger protein 200,RNF200
EIAAB43861 E3 ubiquitin-protein ligase TRIM17,Homo sapiens,Human,RBCC,RING finger protein 16,RNF16,TERF,Testis RING finger protein,TRIM17,Tripartite motif-containing protein 17
EIAAB33374 E3 ubiquitin-protein ligase RNF144B,Homo sapiens,Human,IBR domain-containing protein 2,IBRDC2,p53-inducible RING finger protein,P53RFP,RING finger protein 144B,RNF144B
EIAAB35482 Dorfin,Double ring-finger protein,E3 ubiquitin-protein ligase RNF19A,Gametogenesis-expressed protein GEG-154,Geg-154,Mouse,Mus musculus,RING finger protein 19A,Rnf19,Rnf19a,UBCM4-interacting protein 1


 

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