ID RNF5_HUMAN Reviewed; 180 AA.
AC Q99942; A2BFI6; B2R4K3; Q0VDB7; Q9UMQ2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 204.
DE RecName: Full=E3 ubiquitin-protein ligase RNF5 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:19269966, ECO:0000269|PubMed:19285439, ECO:0000269|PubMed:23093945};
DE AltName: Full=RING finger protein 5 {ECO:0000303|PubMed:9533025};
DE AltName: Full=Ram1 homolog {ECO:0000303|PubMed:16176924};
DE Short=HsRma1 {ECO:0000303|PubMed:16176924};
GN Name=RNF5 {ECO:0000303|PubMed:9533025, ECO:0000312|HGNC:HGNC:10068};
GN Synonyms=G16 {ECO:0000303|Ref.3}, NG2, RMA1 {ECO:0000303|PubMed:11329381};
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9533025; DOI=10.1159/000134695;
RA Kyushiki H., Kuga Y., Suzuki M., Takahashi E., Horie M.;
RT "Cloning, expression and mapping of a novel RING-finger gene (RNF5), a
RT human homologue of a putative zinc-finger gene from Caenorhabditis
RT elegans.";
RL Cytogenet. Cell Genet. 79:114-117(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF CYS-42.
RX PubMed=11329381; DOI=10.1242/jcs.114.10.1949;
RA Matsuda N., Suzuki T., Tanaka K., Nakano A.;
RT "Rma1, a novel type of RING finger protein conserved from Arabidopsis to
RT human, is a membrane-bound ubiquitin ligase.";
RL J. Cell Sci. 114:1949-1957(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Khanna A., Campbell R.D.;
RT "Characterisation of a novel gene, G16, in the class III region of the
RT human major histocompatibility complex.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PXN.
RX PubMed=12861019; DOI=10.1128/mcb.23.15.5331-5345.2003;
RA Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., Nakayama K.,
RA Thomas S.M., Turner C.E., Henderson S., Sabe H., Ronai Z.;
RT "RNF5, a RING finger protein that regulates cell motility by targeting
RT paxillin ubiquitination and altered localization.";
RL Mol. Cell. Biol. 23:5331-5345(2003).
RN [10]
RP FUNCTION.
RX PubMed=16176924; DOI=10.1074/jbc.m506309200;
RA Zhang Y., Higashide W., Dai S., Sherman D.M., Zhou D.;
RT "Recognition and ubiquitination of Salmonella type III effector SopA by a
RT ubiquitin E3 ligase, HsRMA1.";
RL J. Biol. Chem. 280:38682-38688(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP FUNCTION IN UBIQUITINATION OF STING1, INTERACTION WITH STING1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19285439; DOI=10.1016/j.immuni.2009.01.008;
RA Zhong B., Zhang L., Lei C., Li Y., Mao A.P., Yang Y., Wang Y.Y.,
RA Zhang X.L., Shu H.B.;
RT "The ubiquitin ligase RNF5 regulates antiviral responses by mediating
RT degradation of the adaptor protein MITA.";
RL Immunity 30:397-407(2009).
RN [13]
RP FUNCTION IN UBIQUITINATION OF JKAMP, AND INTERACTION WITH JKAMP.
RX PubMed=19269966; DOI=10.1074/jbc.m808222200;
RA Tcherpakov M., Delaunay A., Toth J., Kadoya T., Petroski M.D., Ronai Z.A.;
RT "Regulation of endoplasmic reticulum-associated degradation by RNF5-
RT dependent ubiquitination of JNK-associated membrane protein (JAMP).";
RL J. Biol. Chem. 284:12099-12109(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=23093945; DOI=10.1371/journal.pgen.1003007;
RA Kuang E., Okumura C.Y., Sheffy-Levin S., Varsano T., Shu V.C., Qi J.,
RA Niesman I.R., Yang H.J., Lopez-Otin C., Yang W.Y., Reed J.C., Broday L.,
RA Nizet V., Ronai Z.A.;
RT "Regulation of ATG4B stability by RNF5 limits basal levels of autophagy and
RT influences susceptibility to bacterial infection.";
RL PLoS Genet. 8:e1003007-e1003007(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; THR-94 AND SER-107, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
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 [19]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
CC -!- FUNCTION: Membrane-bound E3 ubiquitin-protein ligase that mediates
CC ubiquitination of target proteins (PubMed:11329381, PubMed:12861019,
CC PubMed:16176924, PubMed:19285439, PubMed:19269966). May function
CC together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and
CC UBE2D2/UBC4 (PubMed:11329381). Mediates ubiquitination of
CC PXN/paxillin,thereby regulating cell motility and localization of
CC PXN/paxillin (PubMed:12861019). Catalyzes ubiquitination of Salmonella
CC type III secreted protein sopA (PubMed:16176924). Mediates the 'Lys-
CC 63'-linked polyubiquitination of JKAMP thereby regulating JKAMP
CC function by decreasing its association with components of the
CC proteasome and ERAD; the ubiquitination appears to involve E2
CC ubiquitin-conjugating enzyme UBE2N (PubMed:19269966). Mediates the
CC 'Lys-48'-linked polyubiquitination of STING1 at 'Lys-150' leading to
CC its proteasomal degradation; the ubiquitination occurs in mitochondria
CC after viral transfection and regulates antiviral responses
CC (PubMed:19285439). Catalyzes ubiquitination and subsequent degradation
CC of ATG4B, thereby inhibiting autophagy (PubMed:23093945).
CC {ECO:0000269|PubMed:11329381, ECO:0000269|PubMed:12861019,
CC ECO:0000269|PubMed:16176924, ECO:0000269|PubMed:19269966,
CC ECO:0000269|PubMed:19285439, ECO:0000269|PubMed:23093945}.
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:19269966,
CC ECO:0000269|PubMed:19285439, ECO:0000269|PubMed:23093945};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:19269966, ECO:0000269|PubMed:19285439,
CC ECO:0000269|PubMed:23093945}.
CC -!- SUBUNIT: Interacts with PXN (PubMed:12861019). Interacts with
CC Salmonella typhimurium sopA (PubMed:12861019). Interacts with JKAMP
CC (PubMed:19269966). Interacts with STING1; the interaction of endogenous
CC proteins is dependent on viral infection (PubMed:19285439).
CC {ECO:0000269|PubMed:12861019, ECO:0000269|PubMed:19269966,
CC ECO:0000269|PubMed:19285439}.
CC -!- INTERACTION:
CC Q99942; O95870: ABHD16A; NbExp=9; IntAct=EBI-348482, EBI-348517;
CC Q99942; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-348482, EBI-714543;
CC Q99942; P13569: CFTR; NbExp=8; IntAct=EBI-348482, EBI-349854;
CC Q99942; P49447: CYB561; NbExp=3; IntAct=EBI-348482, EBI-8646596;
CC Q99942; Q8NBI2: CYB561A3; NbExp=6; IntAct=EBI-348482, EBI-10269179;
CC Q99942; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-348482, EBI-12831978;
CC Q99942; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-348482, EBI-12118888;
CC Q99942; Q9Y5U4: INSIG2; NbExp=6; IntAct=EBI-348482, EBI-8503746;
CC Q99942; O95214: LEPROTL1; NbExp=3; IntAct=EBI-348482, EBI-750776;
CC Q99942; P11836: MS4A1; NbExp=3; IntAct=EBI-348482, EBI-2808234;
CC Q99942; Q96CV9: OPTN; NbExp=3; IntAct=EBI-348482, EBI-748974;
CC Q99942; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-348482, EBI-1054848;
CC Q99942; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-348482, EBI-721750;
CC Q99942; Q04941: PLP2; NbExp=3; IntAct=EBI-348482, EBI-608347;
CC Q99942; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-348482, EBI-11721828;
CC Q99942; O60831: PRAF2; NbExp=3; IntAct=EBI-348482, EBI-2506064;
CC Q99942; P49023: PXN; NbExp=6; IntAct=EBI-348482, EBI-702209;
CC Q99942; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-348482, EBI-712367;
CC Q99942; Q8TEB9: RHBDD1; NbExp=3; IntAct=EBI-348482, EBI-9916444;
CC Q99942; Q96GF1: RNF185; NbExp=3; IntAct=EBI-348482, EBI-2340249;
CC Q99942; Q99942: RNF5; NbExp=4; IntAct=EBI-348482, EBI-348482;
CC Q99942; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-348482, EBI-8636004;
CC Q99942; O00767: SCD; NbExp=3; IntAct=EBI-348482, EBI-2684237;
CC Q99942; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-348482, EBI-8652744;
CC Q99942; P43005: SLC1A1; NbExp=6; IntAct=EBI-348482, EBI-745376;
CC Q99942; Q15758: SLC1A5; NbExp=4; IntAct=EBI-348482, EBI-356576;
CC Q99942; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-348482, EBI-13389236;
CC Q99942; Q96QD8: SLC38A2; NbExp=3; IntAct=EBI-348482, EBI-723083;
CC Q99942; Q9NVC3: SLC38A7; NbExp=8; IntAct=EBI-348482, EBI-10314552;
CC Q99942; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-348482, EBI-10171534;
CC Q99942; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-348482, EBI-10315004;
CC Q99942; P51668: UBE2D1; NbExp=10; IntAct=EBI-348482, EBI-743540;
CC Q99942; P62837: UBE2D2; NbExp=9; IntAct=EBI-348482, EBI-347677;
CC Q99942; P61077: UBE2D3; NbExp=11; IntAct=EBI-348482, EBI-348268;
CC Q99942; Q9Y2X8: UBE2D4; NbExp=7; IntAct=EBI-348482, EBI-745527;
CC Q99942; Q96LR5: UBE2E2; NbExp=10; IntAct=EBI-348482, EBI-2129763;
CC Q99942; Q969T4: UBE2E3; NbExp=11; IntAct=EBI-348482, EBI-348496;
CC Q99942; P61086: UBE2K; NbExp=11; IntAct=EBI-348482, EBI-473850;
CC Q99942; Q96B02: UBE2W; NbExp=4; IntAct=EBI-348482, EBI-716589;
CC Q99942; Q96FI0: UBE2W; NbExp=3; IntAct=EBI-348482, EBI-10285774;
CC Q99942; Q9HAC8: UBTD1; NbExp=5; IntAct=EBI-348482, EBI-745871;
CC Q99942; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-348482, EBI-7850136;
CC Q99942; Q9BWQ6: YIPF2; NbExp=6; IntAct=EBI-348482, EBI-751204;
CC Q99942; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-348482, EBI-751253;
CC Q99942; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-348482, EBI-2510804;
CC Q99942; Q6UX98: ZDHHC24; NbExp=3; IntAct=EBI-348482, EBI-10254561;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9533025};
CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000269|PubMed:19285439}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19285439}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Predominantly located in the plasma membrane, with
CC some localization occurring within cytoplasmic organelles.
CC {ECO:0000269|PubMed:9533025}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9533025}.
CC -!- SIMILARITY: Belongs to the RNF5 family. {ECO:0000305}.
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DR EMBL; AB056869; BAB39359.1; -; mRNA.
DR EMBL; AJ243936; CAB51286.1; -; mRNA.
DR EMBL; AK311859; BAG34800.1; -; mRNA.
DR EMBL; BT007105; AAP35769.1; -; mRNA.
DR EMBL; U89336; AAB47492.1; -; Genomic_DNA.
DR EMBL; AL845464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX284686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR812478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004155; AAH04155.1; -; mRNA.
DR EMBL; BC111392; AAI11393.1; -; mRNA.
DR EMBL; BC119741; AAI19742.1; -; mRNA.
DR EMBL; BC119742; AAI19743.1; -; mRNA.
DR EMBL; BC127651; AAI27652.1; -; mRNA.
DR EMBL; BC127652; AAI27653.1; -; mRNA.
DR EMBL; BC148255; AAI48256.1; -; mRNA.
DR CCDS; CCDS4745.1; -.
DR RefSeq; NP_008844.1; NM_006913.3.
DR AlphaFoldDB; Q99942; -.
DR SMR; Q99942; -.
DR BioGRID; 111975; 162.
DR DIP; DIP-29268N; -.
DR IntAct; Q99942; 76.
DR MINT; Q99942; -.
DR STRING; 9606.ENSP00000364235; -.
DR iPTMnet; Q99942; -.
DR PhosphoSitePlus; Q99942; -.
DR BioMuta; RNF5; -.
DR DMDM; 74762702; -.
DR EPD; Q99942; -.
DR jPOST; Q99942; -.
DR MassIVE; Q99942; -.
DR MaxQB; Q99942; -.
DR PaxDb; 9606-ENSP00000364235; -.
DR PeptideAtlas; Q99942; -.
DR ProteomicsDB; 78533; -.
DR Pumba; Q99942; -.
DR TopDownProteomics; Q99942; -.
DR Antibodypedia; 28471; 271 antibodies from 29 providers.
DR DNASU; 6048; -.
DR Ensembl; ENST00000375094.4; ENSP00000364235.3; ENSG00000204308.8.
DR Ensembl; ENST00000413786.2; ENSP00000387879.2; ENSG00000225452.5.
DR Ensembl; ENST00000432616.2; ENSP00000413131.2; ENSG00000183574.12.
DR Ensembl; ENST00000445885.6; ENSP00000401172.2; ENSG00000227277.9.
DR Ensembl; ENST00000449794.2; ENSP00000415784.2; ENSG00000223767.5.
DR Ensembl; ENST00000453473.2; ENSP00000415127.2; ENSG00000228907.5.
DR Ensembl; ENST00000456167.2; ENSP00000388795.2; ENSG00000228405.5.
DR GeneID; 6048; -.
DR KEGG; hsa:6048; -.
DR MANE-Select; ENST00000375094.4; ENSP00000364235.3; NM_006913.4; NP_008844.1.
DR UCSC; uc003oaj.5; human.
DR AGR; HGNC:10068; -.
DR CTD; 6048; -.
DR DisGeNET; 6048; -.
DR GeneCards; RNF5; -.
DR HGNC; HGNC:10068; RNF5.
DR HPA; ENSG00000204308; Low tissue specificity.
DR MIM; 602677; gene.
DR neXtProt; NX_Q99942; -.
DR OpenTargets; ENSG00000204308; -.
DR PharmGKB; PA34442; -.
DR VEuPathDB; HostDB:ENSG00000204308; -.
DR eggNOG; KOG0823; Eukaryota.
DR GeneTree; ENSGT00390000014107; -.
DR HOGENOM; CLU_055198_2_1_1; -.
DR InParanoid; Q99942; -.
DR OMA; ETSRQQC; -.
DR OrthoDB; 276791at2759; -.
DR PhylomeDB; Q99942; -.
DR TreeFam; TF317334; -.
DR PathwayCommons; Q99942; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR SignaLink; Q99942; -.
DR SIGNOR; Q99942; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 6048; 104 hits in 1191 CRISPR screens.
DR GeneWiki; RNF5; -.
DR GenomeRNAi; 6048; -.
DR Pharos; Q99942; Tbio.
DR PRO; PR:Q99942; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q99942; Protein.
DR Bgee; ENSG00000204308; Expressed in ganglionic eminence and 103 other cell types or tissues.
DR ExpressionAtlas; Q99942; baseline and differential.
DR Genevisible; Q99942; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:UniProtKB.
DR GO; GO:0036503; P:ERAD pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:ParkinsonsUK-UCL.
DR CDD; cd16743; RING-HC_RNF5; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12313:SF4; E3 UBIQUITIN-PROTEIN LIGASE RNF5; 1.
DR PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Endoplasmic reticulum; Membrane; Metal-binding;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..180
FT /note="E3 ubiquitin-protein ligase RNF5"
FT /id="PRO_0000240393"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 27..68
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 79..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 42
FT /note="C->S: Loss of E3 ubiquitin-protein ligase activity."
FT /evidence="ECO:0000269|PubMed:11329381"
FT CONFLICT 22
FT /note="G -> S (in Ref. 3; CAB51286)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="E -> D (in Ref. 3; CAB51286)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="T -> A (in Ref. 3; CAB51286)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="T -> A (in Ref. 3; CAB51286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 19881 MW; E5AFA4DE6DE85942 CRC64;
MAAAEEEDGG PEGPNRERGG AGATFECNIC LETAREAVVS VCGHLYCWPC LHQWLETRPE
RQECPVCKAG ISREKVVPLY GRGSQKPQDP RLKTPPRPQG QRPAPESRGG FQPFGDTGGF
HFSFGVGAFP FGFFTTVFNA HEPFRRGTGV DLGQGHPASS WQDSLFLFLA IFFFFWLLSI
//
