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Q8WU17

- RN139_HUMAN

UniProt

Q8WU17 - RN139_HUMAN

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Protein

E3 ubiquitin-protein ligase RNF139

Gene

RNF139

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

Functioni

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.6 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri547 – 58640RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB
  2. receptor activity Source: UniProtKB
  3. small conjugating protein ligase activity Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. negative regulation of cell proliferation Source: UniProtKB
  2. negative regulation of translation Source: UniProtKB
  3. protein ubiquitination Source: UniProtKB
  4. regulation of ER to Golgi vesicle-mediated transport Source: UniProtKB
  5. regulation of protein processing Source: UniProtKB
  6. regulation of protein ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Receptor

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RNF139Imported
Synonyms:TRC8Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:17023. RNF139.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi547 – 58640Missing: Increases proliferation. Rescues MHC class I to the cell surface. Fails to down-regulate SREBF1 and SREBF2. 4 PublicationsAdd
BLAST
Mutagenesisi547 – 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. 4 Publications
Mutagenesisi557 – 5593SAR → AAA: Retaines about 30% of ubiquitination activity. 1 Publication
Mutagenesisi572 – 5743LRK → AAA: Abolishes ubiquitination activity. Increases proliferation. 1 Publication
Mutagenesisi582 – 5854CPMC → APMA: Abolishes ubiquitination activity. Increases proliferation. 1 Publication

Organism-specific databases

MIMi144700. phenotype.
Orphaneti151. Familial renal cell carcinoma.
PharmGKBiPA134945850.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 664663E3 ubiquitin-protein ligase RNF139PRO_0000056098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei663 – 6631Phosphothreonine6 Publications

Post-translational modificationi

Autoubiquitinated. Ubiquitination is induced by sterol and leads to ist degradation via the ubiquitin-proteasome pathway.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8WU17.
PaxDbiQ8WU17.
PRIDEiQ8WU17.

PTM databases

PhosphoSiteiQ8WU17.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

Down-regulated by sterols (at protein level).1 Publication

Gene expression databases

BgeeiQ8WU17.
CleanExiHS_RNF139.
ExpressionAtlasiQ8WU17. baseline and differential.
GenevestigatoriQ8WU17.

Organism-specific databases

HPAiHPA001202.

Interactioni

Subunit structurei

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-terminal 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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VHLP403372EBI-1551681,EBI-301246

Protein-protein interaction databases

BioGridi116401. 19 interactions.
IntActiQ8WU17. 4 interactions.
STRINGi9606.ENSP00000304051.

Structurei

3D structure databases

ProteinModelPortaliQ8WU17.
SMRiQ8WU17. Positions 544-591.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei51 – 7121HelicalSequence AnalysisAdd
BLAST
Transmembranei85 – 10521HelicalSequence AnalysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence AnalysisAdd
BLAST
Transmembranei154 – 17421HelicalSequence AnalysisAdd
BLAST
Transmembranei178 – 19821HelicalSequence AnalysisAdd
BLAST
Transmembranei293 – 31321HelicalSequence AnalysisAdd
BLAST
Transmembranei323 – 34321HelicalSequence AnalysisAdd
BLAST
Transmembranei356 – 37621HelicalSequence AnalysisAdd
BLAST
Transmembranei390 – 41021HelicalSequence AnalysisAdd
BLAST
Transmembranei420 – 44021HelicalSequence AnalysisAdd
BLAST
Transmembranei469 – 48921HelicalSequence AnalysisAdd
BLAST
Transmembranei495 – 51218HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domaini

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

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri547 – 58640RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG246550.
GeneTreeiENSGT00530000062938.
HOGENOMiHOG000267029.
HOVERGENiHBG053146.
InParanoidiQ8WU17.
KOiK15703.
OMAiRIRFPDI.
OrthoDBiEOG77M8N3.
PhylomeDBiQ8WU17.
TreeFamiTF318635.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR025754. TRC8_N_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13705. TRC8_N. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8WU17-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVGPPQQQ VRMAHQQVWA ALEVALRVPC LYIIDAIFNS YPDSSQSRFC
60 70 80 90 100
IVLQIFLRLF GVFASSIVLI LSQRSLFKFY TYSSAFLLAA TSVLVNYYAS
110 120 130 140 150
LHIDFYGAYN TSAFGIELLP RKGPSLWMAL IVLQLTFGIG YVTLLQIHSI
160 170 180 190 200
YSQLIILDLL VPVIGLITEL PLHIRETLLF TSSLILTLNT VFVLAVKLKW
210 220 230 240 250
FYYSTRYVYL LVRHMYRIYG LQLLMEDTWK RIRFPDILRV FWLTRVTAQA
260 270 280 290 300
TVLMYILRMA NETDSFFISW DDFWDLICNL IISGCDSTLT VLGMSAVISS
310 320 330 340 350
VAHYLGLGIL AFIGSTEEDD RRLGFVAPVL FFILALQTGL SGLRPEERLI
360 370 380 390 400
RLSRNMCLLL TAVLHFIHGM TDPVLMSLSA SHVSSFRRHF PVLFVSACLF
410 420 430 440 450
ILPVLLSYVL WHHYALNTWL FAVTAFCVEL CLKVIVSLTV YTLFMIDGYY
460 470 480 490 500
NVLWEKLDDY VYYVRSTGSI IEFIFGVVMF GNGAYTMMFE SGSKIRAFMM
510 520 530 540 550
CLHAYFNIYL QAKNGWKTFM NRRTAVKKIN SLPEIKGSRL QEINDVCAIC
560 570 580 590 600
YHEFTTSARI TPCNHYFHAL CLRKWLYIQD TCPMCHQKVY IEDDIKDNSN
610 620 630 640 650
VSNNNGFIPP NETPEEAVRE AAAESDRELN EDDSTDCDDD VQRERNGVIQ
660
HTGAAAEEFN DDTD
Length:664
Mass (Da):75,994
Last modified:March 1, 2002 - v1
Checksum:i9885F5915F019EF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181V → I in AAC39930. (PubMed:9689122)Curated
Sequence conflicti18 – 181V → I in AAC39931. (PubMed:9689122)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6350.1.
RefSeqiNP_009149.2. NM_007218.3.
UniGeneiHs.744151.

Genome annotation databases

EnsembliENST00000303545; ENSP00000304051; ENSG00000170881.
GeneIDi11236.
KEGGihsa:11236.
UCSCiuc003yrc.3. human.

Polymorphism databases

DMDMi74760542.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6350.1.
RefSeqi NP_009149.2. NM_007218.3.
UniGenei Hs.744151.

3D structure databases

ProteinModelPortali Q8WU17.
SMRi Q8WU17. Positions 544-591.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116401. 19 interactions.
IntActi Q8WU17. 4 interactions.
STRINGi 9606.ENSP00000304051.

PTM databases

PhosphoSitei Q8WU17.

Polymorphism databases

DMDMi 74760542.

Proteomic databases

MaxQBi Q8WU17.
PaxDbi Q8WU17.
PRIDEi Q8WU17.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303545 ; ENSP00000304051 ; ENSG00000170881 .
GeneIDi 11236.
KEGGi hsa:11236.
UCSCi uc003yrc.3. human.

Organism-specific databases

CTDi 11236.
GeneCardsi GC08P125487.
HGNCi HGNC:17023. RNF139.
HPAi HPA001202.
MIMi 144700. phenotype.
603046. gene.
neXtProti NX_Q8WU17.
Orphaneti 151. Familial renal cell carcinoma.
PharmGKBi PA134945850.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG246550.
GeneTreei ENSGT00530000062938.
HOGENOMi HOG000267029.
HOVERGENi HBG053146.
InParanoidi Q8WU17.
KOi K15703.
OMAi RIRFPDI.
OrthoDBi EOG77M8N3.
PhylomeDBi Q8WU17.
TreeFami TF318635.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

GeneWikii RNF139.
GenomeRNAii 11236.
NextBioi 42766.
PROi Q8WU17.
SOURCEi Search...

Gene expression databases

Bgeei Q8WU17.
CleanExi HS_RNF139.
ExpressionAtlasi Q8WU17. baseline and differential.
Genevestigatori Q8WU17.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR025754. TRC8_N_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF13705. TRC8_N. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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: LungImported and PancreasImported.
  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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRN139_HUMAN
AccessioniPrimary (citable) accession number: Q8WU17
Secondary accession number(s): B3KMD5, O75485, Q7LDL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 120 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 8
    Human chromosome 8: 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