Q969K3 (RNF34_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase RNF34
EC=6.3.2.-

Alternative name(s):
Caspase regulator CARP1
Caspases-8 and -10-associated RING finger protein 1
Short name=CARP-1
FYVE-RING finger protein Momo
Human RING finger homologous to inhibitor of apoptosis protein
Short name=hRFI
RING finger protein 34
RING finger protein RIFF

Gene names

Name:

RNF34

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has E3 ubiquitin-protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Protects cells against apoptosis induced by TNF. Binds phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate. Ref.1 Ref.8 Ref.9
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with DNAJA3 Potential. Interacts with CASP8 and CASP10. Ref.1 Ref.8
Subcellular location	Nucleus speckle. Endomembrane system; Peripheral membrane protein Ref.1 Ref.8.
Tissue specificity	Ubiquitous. Detected in heart, brain, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, colon and leukocytes. Ref.1 Ref.8
Post-translational modification	Auto-ubiquitinated (in vitro) By similarity. Proteolytically cleaved by caspases upon induction of apoptosis by TNF. Ref.1
Sequence similarities	Contains 1 FYVE-type zinc finger. Contains 1 RING-type zinc finger. Contains 2 SAP domains.
Caution	Was isolated as potential interaction partner of the mitochondrial protein DNAJA3, but the 2 proteins are not in the same cellular compartments.
Sequence caution	The sequence BAH14169.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Biological process	Apoptosis Ubl conjugation pathway
Cellular component	Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q969K3-1)

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.

Isoform 2 (identifier: Q969K3-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 372	372	E3 ubiquitin-protein ligase RNF34		PRO_0000056072
Regions
	Domain	115 – 134	20	SAP 1
	Domain	264 – 278	15	SAP 2
	Zinc finger	56 – 107	52	FYVE-type
	Zinc finger	325 – 360	36	RING-type
	Compositional bias	223 – 234	12	Asp-rich
Sites
	Site	232 – 233	2	Cleavage; by caspase-3
Amino acid modifications
	Modified residue	254	1	Phosphoserine Ref.10 Ref.11
	Modified residue	256	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1	1	M → MR in isoform 2.		VSP_038341
Experimental info
	Mutagenesis	342	1	H → A: Loss of E3 ubiquitin protein ligase activity. Ref.8
	Sequence conflict	183	1	Y → C in BAB15132. Ref.4
	Sequence conflict	238	1	N → D in BAB15132. Ref.4
	Sequence conflict	333	1	I → V in BAB15132. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: C044B83BD8591FFA	FASTA	372	41,641
	10 20 30 40 50 60 MKAGATSMWA SCCGLLNEVM GTGAVRGQQS AFAGATGPFR FTPNPEFSTY PPAATEGPNI 70 80 90 100 110 120 VCKACGLSFS VFRKKHVCCD CKKDFCSVCS VLQENLRRCS TCHLLQETAF QRPQLMRLKV 130 140 150 160 170 180 KDLRQYLILR NIPIDTCREK EDLVDLVLCH HGLGSEDDMD TSSLNSSRSQ TSSFFTRSFF 190 200 210 220 230 240 SNYTAPSATM SSFQGELMDG DQTSRSGVPA QVQSEITSAN TEDDDDDDDE DDDDEEENAE 250 260 270 280 290 300 DRNPGLSKER VRASLSDLSS LDDVEGMSVR QLKEILARNF VNYSGCCEKW ELVEKVNRLY 310 320 330 340 350 360 KENEENQKSY GERLQLQDEE DDSLCRICMD AVIDCVLLEC GHMVTCTKCG KRMSECPICR 370 QYVVRAVHVF KS
	Isoform 2 [UniParc]. Checksum: 0177B2F0FACD62FF	FASTA	373	41,797
	10 20 30 40 50 60 MRKAGATSMW ASCCGLLNEV MGTGAVRGQQ SAFAGATGPF RFTPNPEFST YPPAATEGPN 70 80 90 100 110 120 IVCKACGLSF SVFRKKHVCC DCKKDFCSVC SVLQENLRRC STCHLLQETA FQRPQLMRLK 130 140 150 160 170 180 VKDLRQYLIL RNIPIDTCRE KEDLVDLVLC HHGLGSEDDM DTSSLNSSRS QTSSFFTRSF 190 200 210 220 230 240 FSNYTAPSAT MSSFQGELMD GDQTSRSGVP AQVQSEITSA NTEDDDDDDD EDDDDEEENA 250 260 270 280 290 300 EDRNPGLSKE RVRASLSDLS SLDDVEGMSV RQLKEILARN FVNYSGCCEK WELVEKVNRL 310 320 330 340 350 360 YKENEENQKS YGERLQLQDE EDDSLCRICM DAVIDCVLLE CGHMVTCTKC GKRMSECPIC 370 RQYVVRAVHV FKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, INTERACTION WITH DNAJA3, 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00100010. IPI00375563.
RefSeq	NP_001243787.1. NM_001256858.1. NP_079402.2. NM_025126.3. NP_919247.1. NM_194271.2.
UniGene	Hs.292804.
3D structure databases
ProteinModelPortal	Q969K3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q969K3. 4 interactions.
STRING	9606.ENSP00000346850.
PTM databases
PhosphoSite	Q969K3.
Polymorphism databases
DMDM	74760679.
Proteomic databases
PaxDb	Q969K3.
PRIDE	Q969K3.
Protocols and materials databases
DNASU	80196.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361234; ENSP00000355137; ENSG00000170633. ENST00000392465; ENSP00000376258; ENSG00000170633.
GeneID	80196.
KEGG	hsa:80196.
UCSC	uc001uak.1. human. uc001ual.1. human.
Organism-specific databases
CTD	80196.
GeneCards	GC12P121837.
HGNC	HGNC:17297. RNF34.
MIM	608299. gene.
neXtProt	NX_Q969K3.
PharmGKB	PA34436.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG121302.
HOGENOM	HOG000068080.
HOVERGEN	HBG055079.
OrthoDB	EOG4HX51R.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q969K3.
Bgee	Q969K3.
CleanEx	HS_RNF34.
Genevestigator	Q969K3.
GermOnline	ENSG00000170633. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR011011. Znf_FYVE_PHD. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS50800. SAP. False negative. PS50178. ZF_FYVE. False negative. PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	80196.
NextBio	70550.
SOURCE	Search...

Entry information

Entry name

RNF34_HUMAN

Accession

Primary (citable) accession number: Q969K3
Secondary accession number(s): B7Z933, Q8NG47, Q9H6W8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.