Reviewed, UniProtKB/Swiss-Prot Q8WU17 (RN139_HUMAN)

Names and origin

Protein names

Recommended name:
    RING finger protein 139
Alternative name(s):
    Translocation in renal carcinoma on chromosome 8

Gene names

Name:	RNF139
Synonyms:	TRC8

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	664 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Potential tumor suppressor for renal cell carcinoma. Plays a role in mediating ubiquitination. May function as a signaling receptor. Ref.3 Ref.4 Ref.1
Subunit structure	Interacts with VHL. Ref.4
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Ref.4
Tissue specificity	Highly expressed in testis, placenta and adrenal gland. Moderate expression in heart, brain, liver, skeletal muscle and pancreas, and low expression in lung and kidney. Ref.1
Domain	The RING-type zinc finger domain may be essential for ubiquitin ligase activity. Ref.3
Involvement in disease	Defects in RNF139 are a cause of renal cell carcinoma (RCC) [MIM:144700]. A chromosomal aberration involving RNF139 is found in hereditary RCC. Translocation (3;8)(q14.2;q24.1) with FHIT. The result is RNF139 is found to be fused to FHIT and disrupted within the sterol-sensing domain. In contrast, the FHIT coding region is maintained and expressed. Sporadic RCC, where an acquired mutation in RNF139 results in the duplication of 12 nucleotides in the 5'-UTR, has also been identified. Ref.1
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Chromosomal rearrangement
Domain	Transmembrane Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase Receptor
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of protein ubiquitination Ref.3 Inferred from direct assay. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Ref.4 Traceable author statement. Source: UniProtKB
Molecular function	ligase activity Ref.3 Traceable author statement. Source: UniProtKB protein binding Ref.4 Inferred from physical interaction. Source: UniProtKB receptor activity Ref.1 Traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VHL	P40337	1	EBI-1551681,EBI-301246

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 664	664	RING finger protein 139		PRO_0000056098
Regions
	Transmembrane	51 – 71	21	Potential
	Transmembrane	85 – 105	21	Potential
	Transmembrane	125 – 145	21	Potential
	Transmembrane	154 – 174	21	Potential
	Transmembrane	178 – 198	21	Potential
	Transmembrane	293 – 313	21	Potential
	Transmembrane	323 – 343	21	Potential
	Transmembrane	356 – 376	21	Potential
	Transmembrane	390 – 410	21	Potential
	Transmembrane	420 – 440	21	Potential
	Transmembrane	469 – 489	21	Potential
	Transmembrane	495 – 512	18	Potential
	Zinc finger	547 – 586	40	RING-type; atypical
Amino acid modifications
	Modified residue	625	1	Phosphoserine Ref.7
	Modified residue	634	1	Phosphoserine Ref.7
	Modified residue	635	1	Phosphothreonine Ref.7
	Modified residue	663	1	Phosphothreonine Ref.7 Ref.5 Ref.6
Experimental info
	Sequence conflict	18	1	V → I in AAC39930. Ref.1
	Sequence conflict	18	1	V → I in AAC39931. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8WU17-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 9885F5915F019EF5	FASTA	664	75,994
	10 20 30 40 50 60 MAAVGPPQQQ VRMAHQQVWA ALEVALRVPC LYIIDAIFNS YPDSSQSRFC IVLQIFLRLF 70 80 90 100 110 120 GVFASSIVLI LSQRSLFKFY TYSSAFLLAA TSVLVNYYAS LHIDFYGAYN TSAFGIELLP 130 140 150 160 170 180 RKGPSLWMAL IVLQLTFGIG YVTLLQIHSI YSQLIILDLL VPVIGLITEL PLHIRETLLF 190 200 210 220 230 240 TSSLILTLNT VFVLAVKLKW FYYSTRYVYL LVRHMYRIYG LQLLMEDTWK RIRFPDILRV 250 260 270 280 290 300 FWLTRVTAQA TVLMYILRMA NETDSFFISW DDFWDLICNL IISGCDSTLT VLGMSAVISS 310 320 330 340 350 360 VAHYLGLGIL AFIGSTEEDD RRLGFVAPVL FFILALQTGL SGLRPEERLI RLSRNMCLLL 370 380 390 400 410 420 TAVLHFIHGM TDPVLMSLSA SHVSSFRRHF PVLFVSACLF ILPVLLSYVL WHHYALNTWL 430 440 450 460 470 480 FAVTAFCVEL CLKVIVSLTV YTLFMIDGYY NVLWEKLDDY VYYVRSTGSI IEFIFGVVMF 490 500 510 520 530 540 GNGAYTMMFE SGSKIRAFMM CLHAYFNIYL QAKNGWKTFM NRRTAVKKIN SLPEIKGSRL 550 560 570 580 590 600 QEINDVCAIC YHEFTTSARI TPCNHYFHAL CLRKWLYIQD TCPMCHQKVY IEDDIKDNSN 610 620 630 640 650 660 VSNNNGFIPP NETPEEAVRE AAAESDRELN EDDSTDCDDD VQRERNGVIQ HTGAAAEEFN DDTD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The hereditary renal cell carcinoma 3;8 translocation fuses FHIT to a patched-related gene, TRC8." Gemmill R.M., West J.D., Boldog F., Tanaka N., Robinson L.J., Smith D.I., Li F., Drabkin H.A. Proc. Natl. Acad. Sci. U.S.A. 95:9572-9577(1998) [PubMed: 9689122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60, TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH FHIT.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Pancreas.
[3]	"RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination." Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M. Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999) [PubMed: 10500182] [Abstract] Cited for: FUNCTION.
[4]	"The TRC8 hereditary kidney cancer gene suppresses growth and functions with VHL in a common pathway." Gemmill R.M., Bemis L.T., Lee J.P., Sozen M.A., Baron A., Zeng C., Erickson P.F., Hooper J.E., Drabkin H.A. Oncogene 21:3507-3516(2002) [PubMed: 12032852] [Abstract] Cited for: FUNCTION, INTERACTION WITH VHL, SUBCELLULAR LOCATION.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, MASS SPECTROMETRY.
[7]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; SER-634; THR-635 AND THR-663, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF064800 Genomic DNA. Translation: AAC39931.1. AF064801 mRNA. Translation: AAC39930.1. BC021571 mRNA. Translation: AAH21571.1. BC064636 mRNA. Translation: AAH64636.1.
IPI	IPI00289584.
RefSeq	NP_009149.2.
UniGene	Hs.492751
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8WU17. 1 interaction.
PTM databases
PhosphoSite	Q8WU17.
Proteomic databases
PRIDE	Q8WU17.
Genome annotation databases
Ensembl	ENSG00000170881. Homo sapiens. [Contig view]
GeneID	11236.
KEGG	hsa:11236.
Organism-specific databases
GeneCards	GC08P125556.
H-InvDB	HIX0007773. HIX0038182. HIX0059390.
HGNC	HGNC:17023. RNF139.
HPA	HPA001202.
MIM	144700. phenotype. 603046. gene.
Orphanet	151. Renal cell carcinoma, familial.
PharmGKB	PA134945850.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8WU17.
HOVERGEN	Q8WU17.
OMA	Q8WU17. HMYRIYG.
Gene expression databases
Bgee	Q8WU17.
CleanEx	HS_RNF139.
GermOnline	ENSG00000170881. Homo sapiens.
Family and domain databases
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	42766.
SOURCE	Search...

Entry information

Entry name

RN139_HUMAN

Accession

Primary (citable) accession number: Q8WU17
Secondary accession number(s): O75485, Q7LDL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)