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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-SEP-2019, entry version 161.
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:
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;
Evidence={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=