RN167_HUMAN
ID RN167_HUMAN Reviewed; 350 AA.
AC Q9H6Y7; D3DTK8; I3L0L6; Q6XYE0; Q8NDC1; Q9Y3V1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=E3 ubiquitin-protein ligase RNF167 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:23353890, ECO:0000269|PubMed:27808481, ECO:0000269|PubMed:33594058, ECO:0000269|PubMed:35114100};
DE AltName: Full=RING finger protein 167 {ECO:0000305};
DE Flags: Precursor;
GN Name=RNF167 {ECO:0000303|PubMed:23353890, ECO:0000312|HGNC:HGNC:24544};
GN Synonyms=RING105 {ECO:0000303|PubMed:16314844}; ORFNames=LP2254;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-232 AND TRP-260,
RP UBIQUITINATION, AND TISSUE SPECIFICITY.
RX PubMed=16314844; DOI=10.1038/sj.onc.1209167;
RA Yamada H.Y., Gorbsky G.J.;
RT "Tumor suppressor candidate TSSC5 is regulated by UbcH6 and a novel
RT ubiquitin ligase RING105.";
RL Oncogene 25:1330-1339(2006).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, GLYCOSYLATION
RP AT ASN-33 AND ASN-79, AND MUTAGENESIS OF ASN-33; ASN-79 AND
RP 250-HIS--HIS-253.
RX PubMed=23129617; DOI=10.1073/pnas.1217477109;
RA Lussier M.P., Herring B.E., Nasu-Nishimura Y., Neutzner A., Karbowski M.,
RA Youle R.J., Nicoll R.A., Roche K.W.;
RT "Ubiquitin ligase RNF167 regulates AMPA receptor-mediated synaptic
RT transmission.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19426-19431(2012).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=23353890; DOI=10.1038/emboj.2013.1;
RA Yamazaki Y., Schoenherr C., Varshney G.K., Dogru M., Hallberg B.,
RA Palmer R.H.;
RT "Goliath family E3 ligases regulate the recycling endosome pathway via
RT VAMP3 ubiquitylation.";
RL EMBO J. 32:524-537(2013).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, VARIANTS GLY-98 AND ARG-268, AND
RP CHARACTERIZATION OF VARIANTS GLY-98 AND ARG-268.
RX PubMed=24387786; DOI=10.1042/bj20131067;
RA van Dijk J.R., Yamazaki Y., Palmer R.H.;
RT "Tumour-associated mutations of PA-TM-RING ubiquitin ligases RNF167/RNF13
RT identify the PA domain as a determinant for endosomal localization.";
RL Biochem. J. 459:27-36(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-233.
RX PubMed=27808481; DOI=10.1111/febs.13947;
RA Deshar R., Moon S., Yoo W., Cho E.B., Yoon S.K., Yoon J.B.;
RT "RNF167 targets Arl8B for degradation to regulate lysosome positioning and
RT endocytic trafficking.";
RL FEBS J. 283:4583-4599(2016).
RN [14]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION
RP (ISOFORMS 1 AND 2), MUTAGENESIS OF CYS-233, VARIANT ASN-97, AND
RP CHARACTERIZATION OF VARIANT ASN-97.
RX PubMed=32409562; DOI=10.1242/jcs.239335;
RA Nair S.V., Narendradev N.D., Nambiar R.P., Kumar R., Srinivasula S.M.;
RT "Naturally occurring and tumor-associated variants of RNF167 promote
RT lysosomal exocytosis and plasma membrane resealing.";
RL J. Cell Sci. 133:0-0(2020).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AUTOUBIQUITINATION, AND MUTAGENESIS
RP OF 250-HIS--HIS-253.
RX PubMed=33650289; DOI=10.1111/febs.15796;
RA Ghilarducci K., Cabana V.C., Desroches C., Chabi K., Bourgault S.,
RA Cappadocia L., Lussier M.P.;
RT "Functional interaction of ubiquitin ligase RNF167 with UBE2D1 and UBE2N
RT promotes ubiquitination of AMPA receptor.";
RL FEBS J. 288:4849-4868(2021).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=33594058; DOI=10.1038/s41467-021-21206-3;
RA Li T., Wang X., Ju E., da Silva S.R., Chen L., Zhang X., Wei S., Gao S.J.;
RT "RNF167 activates mTORC1 and promotes tumorigenesis by targeting CASTOR1
RT for ubiquitination and degradation.";
RL Nat. Commun. 12:1055-1055(2021).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=35114100; DOI=10.1016/j.molcel.2022.01.002;
RA Wang D., Xu C., Yang W., Chen J., Ou Y., Guan Y., Guan J., Liu Y.;
RT "E3 ligase RNF167 and deubiquitinase STAMBPL1 modulate mTOR and cancer
RT progression.";
RL Mol. Cell 82:770-784(2022).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a regulator of the
CC TORC1 signaling pathway (PubMed:35114100, PubMed:33594058). Positively
CC regulates the TORC1 signaling pathway independently of arginine levels:
CC acts by catalyzing 'Lys-29'-polyubiquitination and degradation of
CC CASTOR1, releasing the GATOR2 complex from CASTOR1 (PubMed:33594058).
CC Also negatively regulates the TORC1 signaling pathway in response to
CC leucine deprivation: acts by mediating 'Lys-63'-linked
CC polyubiquitination of SESN2, promoting SESN2-interaction with the
CC GATOR2 complex (PubMed:35114100). Also involved in protein trafficking
CC and localization (PubMed:23129617, PubMed:23353890, PubMed:24387786,
CC PubMed:27808481, PubMed:32409562). Acts as a regulator of synaptic
CC transmission by mediating ubiquitination and degradation of AMPAR
CC receptor GluA2/GRIA2 (PubMed:23129617, PubMed:33650289). Does not
CC catalyze ubiquitination of GluA1/GRIA1 (PubMed:23129617). Also acts as
CC a regulator of the recycling endosome pathway by mediating
CC ubiquitination of VAMP3 (PubMed:23353890). Regulates lysosome
CC positioning by catalyzing ubiquitination and degradation of ARL8B
CC (PubMed:27808481). Plays a role in growth regulation involved in G1/S
CC transition by mediating, possibly by mediating ubiquitination of
CC SLC22A18 (PubMed:16314844). Acts with a limited set of E2 enzymes, such
CC as UBE2D1 and UBE2N (PubMed:33650289). {ECO:0000269|PubMed:16314844,
CC ECO:0000269|PubMed:23129617, ECO:0000269|PubMed:23353890,
CC ECO:0000269|PubMed:24387786, ECO:0000269|PubMed:27808481,
CC ECO:0000269|PubMed:32409562, ECO:0000269|PubMed:33594058,
CC ECO:0000269|PubMed:33650289, ECO:0000269|PubMed:35114100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:23129617,
CC ECO:0000269|PubMed:23353890, ECO:0000269|PubMed:27808481,
CC ECO:0000269|PubMed:33594058, ECO:0000269|PubMed:33650289,
CC ECO:0000269|PubMed:35114100};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23129617, ECO:0000269|PubMed:23353890,
CC ECO:0000269|PubMed:27808481, ECO:0000269|PubMed:33594058,
CC ECO:0000269|PubMed:33650289, ECO:0000269|PubMed:35114100}.
CC -!- INTERACTION:
CC Q9H6Y7; P61086: UBE2K; NbExp=3; IntAct=EBI-1055214, EBI-473850;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16314844,
CC ECO:0000269|PubMed:27808481, ECO:0000269|PubMed:35114100}; Single-pass
CC type I membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000269|PubMed:24387786}; Single-pass type I membrane protein
CC {ECO:0000255}. Endomembrane system {ECO:0000269|PubMed:16314844};
CC Single-pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000269|PubMed:23129617}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Targeted to cytoplasmic membranes; mainly localizes
CC to lysosomal membrane (PubMed:16314844, PubMed:23129617). A
CC subpopulation localizes to the cell membrane of neurons
CC (PubMed:23129617). {ECO:0000269|PubMed:16314844,
CC ECO:0000269|PubMed:23129617}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Lysosome membrane
CC {ECO:0000269|PubMed:32409562}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:32409562}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=RNF167-a {ECO:0000303|PubMed:32409562};
CC IsoId=Q9H6Y7-1; Sequence=Displayed;
CC Name=2; Synonyms=RNF167-b {ECO:0000303|PubMed:32409562};
CC IsoId=Q9H6Y7-2; Sequence=VSP_061564;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:23129617). Strongly
CC expressed in the kidney, pancreas, testis and liver (at protein level)
CC (PubMed:16314844, PubMed:23129617). {ECO:0000269|PubMed:16314844,
CC ECO:0000269|PubMed:23129617}.
CC -!- PTM: Autoubiquitinated in vitro in the presence of UBE2D1 and UBE2E1.
CC {ECO:0000269|PubMed:16314844, ECO:0000269|PubMed:33650289}.
CC -!- SIMILARITY: Belongs to the Godzilla family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP34453.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL050060; CAB43253.1; -; mRNA.
DR EMBL; AL834284; CAD38958.1; -; mRNA.
DR EMBL; AK025329; BAB15113.1; -; mRNA.
DR EMBL; AY203930; AAP34453.1; ALT_FRAME; mRNA.
DR EMBL; CR457340; CAG33621.1; -; mRNA.
DR EMBL; AC004771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90385.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90387.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90388.1; -; Genomic_DNA.
DR EMBL; BC010139; AAH10139.1; -; mRNA.
DR CCDS; CCDS11060.1; -.
DR PIR; T08729; T08729.
DR RefSeq; NP_001307285.1; NM_001320356.1.
DR RefSeq; NP_001307286.1; NM_001320357.1.
DR RefSeq; NP_001307287.1; NM_001320358.1.
DR RefSeq; NP_001307288.1; NM_001320359.1.
DR RefSeq; NP_001307289.1; NM_001320360.1.
DR RefSeq; NP_001307290.1; NM_001320361.1.
DR RefSeq; NP_001307291.1; NM_001320362.1.
DR RefSeq; NP_001307292.1; NM_001320363.1.
DR RefSeq; NP_001307293.1; NM_001320364.1.
DR RefSeq; NP_001307294.1; NM_001320365.1.
DR RefSeq; NP_056343.1; NM_015528.2.
DR RefSeq; XP_016879916.1; XM_017024427.1.
DR AlphaFoldDB; Q9H6Y7; -.
DR SMR; Q9H6Y7; -.
DR BioGRID; 117477; 44.
DR IntAct; Q9H6Y7; 27.
DR MINT; Q9H6Y7; -.
DR STRING; 9606.ENSP00000262482; -.
DR MoonDB; Q9H6Y7; Predicted.
DR GlyGen; Q9H6Y7; 1 site.
DR iPTMnet; Q9H6Y7; -.
DR PhosphoSitePlus; Q9H6Y7; -.
DR SwissPalm; Q9H6Y7; -.
DR BioMuta; RNF167; -.
DR DMDM; 74733620; -.
DR EPD; Q9H6Y7; -.
DR jPOST; Q9H6Y7; -.
DR MassIVE; Q9H6Y7; -.
DR MaxQB; Q9H6Y7; -.
DR PaxDb; Q9H6Y7; -.
DR PeptideAtlas; Q9H6Y7; -.
DR PRIDE; Q9H6Y7; -.
DR ProteomicsDB; 81063; -.
DR Antibodypedia; 23476; 91 antibodies from 20 providers.
DR DNASU; 26001; -.
DR Ensembl; ENST00000262482.11; ENSP00000262482.6; ENSG00000108523.16.
DR Ensembl; ENST00000571816.5; ENSP00000459324.1; ENSG00000108523.16.
DR Ensembl; ENST00000572430.5; ENSP00000458794.1; ENSG00000108523.16.
DR Ensembl; ENST00000575111.5; ENSP00000460190.1; ENSG00000108523.16.
DR GeneID; 26001; -.
DR KEGG; hsa:26001; -.
DR MANE-Select; ENST00000262482.11; ENSP00000262482.6; NM_015528.3; NP_056343.1.
DR UCSC; uc002fzs.4; human.
DR CTD; 26001; -.
DR DisGeNET; 26001; -.
DR GeneCards; RNF167; -.
DR HGNC; HGNC:24544; RNF167.
DR HPA; ENSG00000108523; Low tissue specificity.
DR MIM; 610431; gene.
DR neXtProt; NX_Q9H6Y7; -.
DR OpenTargets; ENSG00000108523; -.
DR PharmGKB; PA134953711; -.
DR VEuPathDB; HostDB:ENSG00000108523; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000159547; -.
DR HOGENOM; CLU_035275_1_1_1; -.
DR InParanoid; Q9H6Y7; -.
DR OMA; RIPTHKF; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q9H6Y7; -.
DR TreeFam; TF317486; -.
DR PathwayCommons; Q9H6Y7; -.
DR SignaLink; Q9H6Y7; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26001; 8 hits in 1124 CRISPR screens.
DR ChiTaRS; RNF167; human.
DR GenomeRNAi; 26001; -.
DR Pharos; Q9H6Y7; Tbio.
DR PRO; PR:Q9H6Y7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9H6Y7; protein.
DR Bgee; ENSG00000108523; Expressed in granulocyte and 199 other tissues.
DR ExpressionAtlas; Q9H6Y7; baseline and differential.
DR Genevisible; Q9H6Y7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0036020; C:endolysosome membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990253; P:cellular response to leucine starvation; IDA:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; IDA:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IDA:UniProtKB.
DR GO; GO:0051640; P:organelle localization; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd02123; PA_C_RZF_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Endosome; Glycoprotein;
KW Lysosome; Membrane; Metal-binding; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..350
FT /note="E3 ubiquitin-protein ligase RNF167"
FT /id="PRO_0000245593"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 49..152
FT /note="PA"
FT /evidence="ECO:0000255"
FT ZN_FING 230..272
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 271..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23129617"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23129617"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /id="VSP_061564"
FT VARIANT 97
FT /note="K -> N (found in a tumor sample; unknown
FT pathological significance; impaired localization to
FT lysosomes and ability to regulate lysosome positioning)"
FT /evidence="ECO:0000269|PubMed:32409562"
FT /id="VAR_086371"
FT VARIANT 98
FT /note="V -> G (found in a tumor sample; unknown
FT pathological significance; impaired localization to
FT endosomes)"
FT /evidence="ECO:0000269|PubMed:24387786"
FT /id="VAR_086372"
FT VARIANT 121
FT /note="N -> K (in dbSNP:rs1127356)"
FT /id="VAR_026996"
FT VARIANT 268
FT /note="C -> R (found in a tumor sample; unknown
FT pathological significance; abolished ability to regulate
FT protein trafficking and localization)"
FT /evidence="ECO:0000269|PubMed:24387786"
FT /id="VAR_086373"
FT MUTAGEN 33
FT /note="N->Q: Reduced N-glycosylation. Abolished N-
FT glycosylation; when associated with Q-79."
FT /evidence="ECO:0000269|PubMed:23129617"
FT MUTAGEN 79
FT /note="N->Q: Reduced N-glycosylation. Abolished N-
FT glycosylation; when associated with Q-33."
FT /evidence="ECO:0000269|PubMed:23129617"
FT MUTAGEN 232
FT /note="I->A: Drastically increased stability; reduction in
FT auto-ubiquitination activity; loss of cell delay/arrest in
FT G1."
FT /evidence="ECO:0000269|PubMed:16314844"
FT MUTAGEN 233
FT /note="C->S: Abolished E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:27808481,
FT ECO:0000269|PubMed:32409562"
FT MUTAGEN 250..253
FT /note="HAYH->WAYW: Abolished E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:23129617,
FT ECO:0000269|PubMed:33650289"
FT MUTAGEN 260
FT /note="W->A: Drastically increased stability; reduction in
FT auto-ubiquitination activity; loss of cell delay/arrest in
FT G1."
FT /evidence="ECO:0000269|PubMed:16314844"
FT CONFLICT 224
FT /note="Missing (in Ref. 1; CAD38958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38299 MW; D87493CE24C2A418 CRC64;
MHPAAFPLPV VVAAVLWGAA PTRGLIRATS DHNASMDFAD LPALFGATLS QEGLQGFLVE
AHPDNACSPI APPPPAPVNG SVFIALLRRF DCNFDLKVLN AQKAGYGAAV VHNVNSNELL
NMVWNSEEIQ QQIWIPSVFI GERSSEYLRA LFVYEKGARV LLVPDNTFPL GYYLIPFTGI
VGLLVLAMGA VMIARCIQHR KRLQRNRLTK EQLKQIPTHD YQKGDQYDVC AICLDEYEDG
DKLRVLPCAH AYHSRCVDPW LTQTRKTCPI CKQPVHRGPG DEDQEEETQG QEEGDEGEPR
DHPASERTPL LGSSPTLPTS FGSLAPAPLV FPGPSTDPPL SPPSSPVILV
