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Q8WU17 (RN139_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase RNF139

EC=6.3.2.-
Alternative name(s):
RING finger protein 139
Translocation in renal carcinoma on chromosome 8 protein
Gene names
Name:RNF139
Synonyms:TRC8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3-ubiquitin ligase; acts as a negative regulator of the cell proliferation through mechanisms involving G2/M arrest and cell death. Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER). Affects SREBP processing by hindering the SREBP/SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression. Required for INSIG1 ubiquitination. May be required for EIF3 complex ubiquitination. May function as a signaling receptor. Ref.5 Ref.6 Ref.8 Ref.12 Ref.13 Ref.15

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with VHL. Interacts with MHC class I and HM13. Component of SCAP/SREBP complex composed of SREBF2, SCAP and RNF139; the complex hampers the interaction between SCAP and SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts with SREBF2 (via C-terminus domain). Interacts with SCAP; the interaction inhibits the interaction of SCAP with SEC24B and hampering the ER to Golgi transport of the SCAP/SREBP complex. Interacts with SEC24B. Interacts with INSIG1 and INSIG2. Interacts with EIF3F and EIF3H; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner. Ref.6 Ref.12 Ref.13 Ref.15

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.6.

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

Induction

Down-regulated by sterols (at protein level). Ref.15

Domain

The RING-type zinc finger domain mediates ubiquitin ligase activity.

Post-translational modification

Autoubiquitinated. Ubiquitination is induced by sterol and leads to ist degradation via the ubiquitin-proteasome pathway.

Involvement in disease

Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype.
Note: The disease may be caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving RNF139 has been found in a lymphoblastoid cell line established from a family with renal cell carcinoma and thyroid carcinoma. Translocation (3;8)(q14.2;q24.1) with FHIT. 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 cases of renal carcinoma, where an acquired mutation in RNF139 results in the duplication of 12 nucleotides in the 5'-UTR, has also been identified.

Sequence similarities

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityChromosomal rearrangement
   DomainTransmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
Receptor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of cell proliferation

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of translation

Inferred from direct assay Ref.15. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of ER to Golgi vesicle-mediated transport

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of protein processing

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of protein ubiquitination

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.6. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Traceable author statement Ref.6. Source: UniProtKB

   Molecular_functionligase activity

Traceable author statement Ref.5. Source: UniProtKB

receptor activity

Traceable author statement Ref.1. Source: UniProtKB

small conjugating protein ligase activity

Inferred from direct assay Ref.8. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.8. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VHLP403372EBI-1551681,EBI-301246

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 664663E3 ubiquitin-protein ligase RNF139
PRO_0000056098

Regions

Transmembrane51 – 7121Helical; Potential
Transmembrane85 – 10521Helical; Potential
Transmembrane125 – 14521Helical; Potential
Transmembrane154 – 17421Helical; Potential
Transmembrane178 – 19821Helical; Potential
Transmembrane293 – 31321Helical; Potential
Transmembrane323 – 34321Helical; Potential
Transmembrane356 – 37621Helical; Potential
Transmembrane390 – 41021Helical; Potential
Transmembrane420 – 44021Helical; Potential
Transmembrane469 – 48921Helical; Potential
Transmembrane495 – 51218Helical; Potential
Zinc finger547 – 58640RING-type; atypical

Amino acid modifications

Modified residue21N-acetylalanine Ref.18
Modified residue6631Phosphothreonine Ref.7 Ref.9 Ref.10 Ref.14 Ref.16 Ref.17

Experimental info

Mutagenesis547 – 58640Missing: Increases proliferation. Rescues MHC class I to the cell surface. Fails to down-regulate SREBF1 and SREBF2. Ref.12 Ref.13 Ref.15
Mutagenesis547 – 5504CAIC → SAIS: Abolishes ubiquitination activity. Increases proliferation. Does not phosphorylates CHEK2 on T-68. Does not phosphorylates ATM on S-1981. Rescues MHC class I to the cell surface. Suppresses SREBF2 processing in the presence or absence of sterols. Fails to down-regulate SREBF1 and SREBF2. Decreases INSIG1 ubiquitination. Ref.12 Ref.13 Ref.15
Mutagenesis557 – 5593SAR → AAA: Retaines about 30% of ubiquitination activity.
Mutagenesis572 – 5743LRK → AAA: Abolishes ubiquitination activity. Increases proliferation. Ref.8
Mutagenesis582 – 5854CPMC → APMA: Abolishes ubiquitination activity. Increases proliferation. Ref.8
Sequence conflict181V → I in AAC39930. Ref.1
Sequence conflict181V → I in AAC39931. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8WU17 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 9885F5915F019EF5

FASTA66475,994
        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 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60, TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH FHIT.
[2]"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. expand/collapse author list , 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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Lung and Pancreas.
[5]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VHL, SUBCELLULAR LOCATION.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"RING-dependent tumor suppression and G2/M arrest induced by the TRC8 hereditary kidney cancer gene."
Brauweiler A., Lorick K.L., Lee J.P., Tsai Y.C., Chan D., Weissman A.M., Drabkin H.A., Gemmill R.M.
Oncogene 26:2263-2271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 547-CYS--CYS-550; 547-CYS--HIS-586; 557-SER--ARG-559; 572-LEU--LYS-574 AND 582-CYS--CYS-585.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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 THR-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage."
Irisawa M., Inoue J., Ozawa N., Mori K., Sato R.
J. Biol. Chem. 284:28995-29004(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SREBF2; SCAP AND SEC24B, UBIQUITINATION, MUTAGENESIS OF 547-CYS--CYS-550 AND 547-CYS--HIS-586.
[13]"The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ER."
Stagg H.R., Thomas M., van den Boomen D., Wiertz E.J., Drabkin H.A., Gemmill R.M., Lehner P.J.
J. Cell Biol. 186:685-692(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MHC CLASS I AND HM13, MUTAGENESIS OF 547-CYS--CYS-550 AND 547-CYS--HIS-586.
[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 THR-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways."
Lee J.P., Brauweiler A., Rudolph M., Hooper J.E., Drabkin H.A., Gemmill R.M.
Mol. Cancer Res. 8:93-106(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH INSIG1; INSIG2; EIF3F AND EIF3H, INDUCTION, MUTAGENESIS OF 547-CYS--CYS-550 AND 547-CYS--HIS-586.
[16]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064800 Genomic DNA. Translation: AAC39931.1.
AF064801 mRNA. Translation: AAC39930.1.
AK001602 mRNA. Translation: BAG50947.1.
CH471060 Genomic DNA. Translation: EAW92064.1.
BC021571 mRNA. Translation: AAH21571.1.
BC064636 mRNA. Translation: AAH64636.1.
RefSeqNP_009149.2. NM_007218.3.
UniGeneHs.744151.

3D structure databases

ProteinModelPortalQ8WU17.
SMRQ8WU17. Positions 544-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116401. 17 interactions.
IntActQ8WU17. 4 interactions.
STRING9606.ENSP00000304051.

PTM databases

PhosphoSiteQ8WU17.

Polymorphism databases

DMDM74760542.

Proteomic databases

PaxDbQ8WU17.
PRIDEQ8WU17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303545; ENSP00000304051; ENSG00000170881.
GeneID11236.
KEGGhsa:11236.
UCSCuc003yrc.3. human.

Organism-specific databases

CTD11236.
GeneCardsGC08P125487.
HGNCHGNC:17023. RNF139.
HPAHPA001202.
MIM144700. phenotype.
603046. gene.
neXtProtNX_Q8WU17.
Orphanet151. Familial renal cell carcinoma.
PharmGKBPA134945850.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246550.
HOGENOMHOG000267029.
HOVERGENHBG053146.
InParanoidQ8WU17.
KOK15703.
OMARIRFPDI.
OrthoDBEOG77M8N3.
PhylomeDBQ8WU17.
TreeFamTF318635.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ8WU17.
BgeeQ8WU17.
CleanExHS_RNF139.
GenevestigatorQ8WU17.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR025754. TRC8_N_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF13705. TRC8_N. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRNF139.
GenomeRNAi11236.
NextBio42766.
PROQ8WU17.
SOURCESearch...

Entry information

Entry nameRN139_HUMAN
AccessionPrimary (citable) accession number: Q8WU17
Secondary accession number(s): B3KMD5, O75485, Q7LDL3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM