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Q969K3

- RNF34_HUMAN

UniProt

Q969K3 - RNF34_HUMAN

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Protein

E3 ubiquitin-protein ligase RNF34

Gene

RNF34

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (PubMed:19690332). 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).7 Publications1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei232 – 2332Cleavage; by caspase-31 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri56 – 10752FYVE-typeAdd
BLAST
Zinc fingeri325 – 36036RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. p53 binding Source: UniProtKB
  3. phosphatidylinositol phosphate binding Source: UniProtKB
  4. ubiquitin protein ligase activity Source: UniProtKB
  5. ubiquitin protein ligase binding Source: UniProtKB
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: UniProtKB
  2. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
  3. negative regulation of signal transduction by p53 class mediator Source: UniProtKB
  4. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: UniProtKB
  5. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  6. protein K48-linked ubiquitination Source: UniProtKB
  7. protein ubiquitination Source: UniProtKB
  8. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  9. regulation of oxygen metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF34Curated (EC:6.3.2.-2 Publications)
Alternative name(s):
Caspase regulator CARP1Curated
Caspases-8 and -10-associated RING finger protein 11 Publication
Short name:
CARP-11 Publication
FYVE-RING finger protein MomoBy similarity
Human RING finger homologous to inhibitor of apoptosis protein1 Publication
Short name:
hRFI1 Publication
RING finger protein 34Imported
RING finger protein RIFF1 Publication
Gene namesi
Name:RNF34Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:17297. RNF34.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein Curated. Endomembrane system By similarity; Peripheral membrane protein By similarity. Nucleus 1 Publication. Nucleus speckle 1 Publication. Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi328 – 3281C → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication
Mutagenesisi342 – 3421H → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication

Organism-specific databases

PharmGKBiPA34436.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372E3 ubiquitin-protein ligase RNF34PRO_0000056072Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei254 – 2541Phosphoserine2 Publications

Post-translational modificationi

Autoubiquitinated (in vitro).By similarity
Proteolytically cleaved by caspases upon induction of apoptosis by TNF.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ969K3.
PaxDbiQ969K3.
PRIDEiQ969K3.

PTM databases

PhosphoSiteiQ969K3.

Expressioni

Tissue specificityi

Ubiquitous. Detected in heart, brain, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, colon and leukocytes.2 Publications

Gene expression databases

BgeeiQ969K3.
CleanExiHS_RNF34.
ExpressionAtlasiQ969K3. baseline and differential.
GenevestigatoriQ969K3.

Interactioni

Subunit structurei

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 MDM2.6 PublicationsCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP8Q147903EBI-2340642,EBI-78060

Protein-protein interaction databases

BioGridi123169. 19 interactions.
IntActiQ969K3. 6 interactions.
STRINGi9606.ENSP00000346850.

Structurei

3D structure databases

ProteinModelPortaliQ969K3.
SMRiQ969K3. Positions 62-148, 315-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini115 – 13420SAP 1Add
BLAST
Domaini264 – 27815SAP 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi223 – 23412Asp-richAdd
BLAST

Domaini

The RING-type zinc finger is required for the ubiquitination of target proteins.1 Publication
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.1 Publication

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 2 SAP domains.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri56 – 10752FYVE-typeAdd
BLAST
Zinc fingeri325 – 36036RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG121302.
GeneTreeiENSGT00390000012719.
HOGENOMiHOG000068080.
HOVERGENiHBG055079.
InParanoidiQ969K3.
PhylomeDBiQ969K3.
TreeFamiTF325195.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q969K3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKAGATSMWA SCCGLLNEVM GTGAVRGQQS AFAGATGPFR FTPNPEFSTY
60 70 80 90 100
PPAATEGPNI VCKACGLSFS VFRKKHVCCD CKKDFCSVCS VLQENLRRCS
110 120 130 140 150
TCHLLQETAF QRPQLMRLKV KDLRQYLILR NIPIDTCREK EDLVDLVLCH
160 170 180 190 200
HGLGSEDDMD TSSLNSSRSQ TSSFFTRSFF SNYTAPSATM SSFQGELMDG
210 220 230 240 250
DQTSRSGVPA QVQSEITSAN TEDDDDDDDE DDDDEEENAE DRNPGLSKER
260 270 280 290 300
VRASLSDLSS LDDVEGMSVR QLKEILARNF VNYSGCCEKW ELVEKVNRLY
310 320 330 340 350
KENEENQKSY GERLQLQDEE DDSLCRICMD AVIDCVLLEC GHMVTCTKCG
360 370
KRMSECPICR QYVVRAVHVF KS
Length:372
Mass (Da):41,641
Last modified:December 1, 2001 - v1
Checksum:iC044B83BD8591FFA
GO
Isoform 2 (identifier: Q969K3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MR

Show »
Length:373
Mass (Da):41,797
Checksum:i0177B2F0FACD62FF
GO

Sequence cautioni

The sequence BAH14169.1 differs from that shown. Reason: Intron retention.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831Y → C in BAB15132. (PubMed:14702039)Curated
Sequence conflicti238 – 2381N → D in BAB15132. (PubMed:14702039)Curated
Sequence conflicti333 – 3331I → V in BAB15132. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MR in isoform 2. 2 PublicationsVSP_038341

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB084914 mRNA. Translation: BAC11802.1.
AF306709 mRNA. Translation: AAK51328.1.
AY098934 mRNA. Translation: AAM29180.1.
AK304366 mRNA. Translation: BAH14169.1. Sequence problems.
AK025439 mRNA. Translation: BAB15132.1.
BT007283 mRNA. Translation: AAP35947.1.
CR457342 mRNA. Translation: CAG33623.1.
BC007826 mRNA. Translation: AAH07826.1.
CCDSiCCDS31915.1. [Q969K3-1]
CCDS9221.1. [Q969K3-2]
RefSeqiNP_001243787.1. NM_001256858.1.
NP_079402.2. NM_025126.3. [Q969K3-1]
NP_919247.1. NM_194271.2. [Q969K3-2]
UniGeneiHs.292804.

Genome annotation databases

EnsembliENST00000361234; ENSP00000355137; ENSG00000170633. [Q969K3-1]
ENST00000392465; ENSP00000376258; ENSG00000170633. [Q969K3-2]
GeneIDi80196.
KEGGihsa:80196.
UCSCiuc001uak.2. human. [Q969K3-2]
uc001ual.2. human. [Q969K3-1]

Polymorphism databases

DMDMi74760679.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB084914 mRNA. Translation: BAC11802.1 .
AF306709 mRNA. Translation: AAK51328.1 .
AY098934 mRNA. Translation: AAM29180.1 .
AK304366 mRNA. Translation: BAH14169.1 . Sequence problems.
AK025439 mRNA. Translation: BAB15132.1 .
BT007283 mRNA. Translation: AAP35947.1 .
CR457342 mRNA. Translation: CAG33623.1 .
BC007826 mRNA. Translation: AAH07826.1 .
CCDSi CCDS31915.1. [Q969K3-1 ]
CCDS9221.1. [Q969K3-2 ]
RefSeqi NP_001243787.1. NM_001256858.1.
NP_079402.2. NM_025126.3. [Q969K3-1 ]
NP_919247.1. NM_194271.2. [Q969K3-2 ]
UniGenei Hs.292804.

3D structure databases

ProteinModelPortali Q969K3.
SMRi Q969K3. Positions 62-148, 315-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123169. 19 interactions.
IntActi Q969K3. 6 interactions.
STRINGi 9606.ENSP00000346850.

PTM databases

PhosphoSitei Q969K3.

Polymorphism databases

DMDMi 74760679.

Proteomic databases

MaxQBi Q969K3.
PaxDbi Q969K3.
PRIDEi Q969K3.

Protocols and materials databases

DNASUi 80196.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361234 ; ENSP00000355137 ; ENSG00000170633 . [Q969K3-1 ]
ENST00000392465 ; ENSP00000376258 ; ENSG00000170633 . [Q969K3-2 ]
GeneIDi 80196.
KEGGi hsa:80196.
UCSCi uc001uak.2. human. [Q969K3-2 ]
uc001ual.2. human. [Q969K3-1 ]

Organism-specific databases

CTDi 80196.
GeneCardsi GC12P121837.
HGNCi HGNC:17297. RNF34.
MIMi 608299. gene.
neXtProti NX_Q969K3.
PharmGKBi PA34436.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG121302.
GeneTreei ENSGT00390000012719.
HOGENOMi HOG000068080.
HOVERGENi HBG055079.
InParanoidi Q969K3.
PhylomeDBi Q969K3.
TreeFami TF325195.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GeneWikii RNF34.
GenomeRNAii 80196.
NextBioi 70550.
PROi Q969K3.
SOURCEi Search...

Gene expression databases

Bgeei Q969K3.
CleanExi HS_RNF34.
ExpressionAtlasi Q969K3. baseline and differential.
Genevestigatori Q969K3.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a novel gene, hRFI, preferentially expressed in esophageal cancer."
    Sasaki S., Nakamura T., Arakawa H., Mori M., Watanabe T., Nagawa H., Croce C.M.
    Oncogene 21:5024-5030(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE BY CASPASE-3, TISSUE SPECIFICITY.
  2. "Cloning of RIFF, a novel RING finger FYVE finger protein expressed in human fetal brain."
    Olsson P.-A., Lindholm D.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. Kanbe D., Araki K., Nawa H.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Trachea.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    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.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  8. "Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth."
    McDonald E.R. III, El-Deiry W.S.
    Proc. Natl. Acad. Sci. U.S.A. 101:6170-6175(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CASP8 AND CASP10, MUTAGENESIS OF HIS-342, PROTEOLYTIC DEGRADATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Overexpression of hRFI (human RING finger homologous to inhibitor of apoptosis protein type) inhibits death receptor-mediated apoptosis in colorectal cancer cells."
    Konishi T., Sasaki S., Watanabe T., Kitayama J., Nagawa H.
    Mol. Cancer Ther. 4:743-750(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-p53ser20 degradation."
    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.
    J. Biol. Chem. 282:3273-3281(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH P53/TP53.
  11. "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2."
    Yang W., Dicker D.T., Chen J., El-Deiry W.S.
    Cell Cycle 7:670-682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MDM2 AND P53/TP53.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: FUNCTION, INTERACTION WITH RIPK1, PATHWAY.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "RNF34 is a cold-regulated E3 ubiquitin ligase for PGC-1alpha and modulates brown fat cell metabolism."
    Wei P., Pan D., Mao C., Wang Y.X.
    Mol. Cell. Biol. 32:266-275(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPARGC1A, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-328.
  17. "The E3 ligase RNF34 is a novel negative regulator of the NOD1 pathway."
    Zhang R., Zhao J., Song Y., Wang X., Wang L., Xu J., Song C., Liu F.
    Cell. Physiol. Biochem. 33:1954-1962(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOD1.

Entry informationi

Entry nameiRNF34_HUMAN
AccessioniPrimary (citable) accession number: Q969K3
Secondary accession number(s): B7Z933, Q8NG47, Q9H6W8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3