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E3 ubiquitin-protein ligase RNF5 (EC 2.3.2.27) (Protein G16) (RING finger protein 5) (RING-type E3 ubiquitin transferase RNF5) (Ram1 homolog) (HsRma1)

 RNF5_HUMAN              Reviewed;         180 AA.
Q99942; A2BFI6; B2R4K3; Q0VDB7; Q9UMQ2;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
25-OCT-2017, entry version 164.
RecName: Full=E3 ubiquitin-protein ligase RNF5;
EC=2.3.2.27;
AltName: Full=Protein G16;
AltName: Full=RING finger protein 5;
AltName: Full=RING-type E3 ubiquitin transferase RNF5 {ECO:0000305};
AltName: Full=Ram1 homolog;
Short=HsRma1;
Name=RNF5; Synonyms=G16, NG2, RMA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=9533025;
Kyushiki H., Kuga Y., Suzuki M., Takahashi E., Horie M.;
"Cloning, expression and mapping of a novel RING-finger gene (RNF5), a
human homologue of a putative zinc-finger gene from Caenorhabditis
elegans.";
Cytogenet. Cell Genet. 79:114-117(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF CYS-42.
PubMed=11329381;
Matsuda N., Suzuki T., Tanaka K., Nakano A.;
"Rma1, a novel type of RING finger protein conserved from Arabidopsis
to human, is a membrane-bound ubiquitin ligase.";
J. Cell Sci. 114:1949-1957(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Khanna A., Campbell R.D.;
"Characterisation of a novel gene, G16, in the class III region of the
human major histocompatibility complex.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PXN.
PubMed=12861019; DOI=10.1128/MCB.23.15.5331-5345.2003;
Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S.,
Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H.,
Ronai Z.;
"RNF5, a RING finger protein that regulates cell motility by targeting
paxillin ubiquitination and altered localization.";
Mol. Cell. Biol. 23:5331-5345(2003).
[10]
FUNCTION.
PubMed=16176924; DOI=10.1074/jbc.M506309200;
Zhang Y., Higashide W., Dai S., Sherman D.M., Zhou D.;
"Recognition and ubiquitination of Salmonella type III effector SopA
by a ubiquitin E3 ligase, HsRMA1.";
J. Biol. Chem. 280:38682-38688(2005).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
FUNCTION IN UBIQUITINATION OF TMEM173, INTERACTION WITH TMEM173, AND
SUBCELLULAR LOCATION.
PubMed=19285439; DOI=10.1016/j.immuni.2009.01.008;
Zhong B., Zhang L., Lei C., Li Y., Mao A.P., Yang Y., Wang Y.Y.,
Zhang X.L., Shu H.B.;
"The ubiquitin ligase RNF5 regulates antiviral responses by mediating
degradation of the adaptor protein MITA.";
Immunity 30:397-407(2009).
[13]
FUNCTION IN UBIQUITINATION OF JKAMP, AND INTERACTION WITH JKAMP.
PubMed=19269966; DOI=10.1074/jbc.M808222200;
Tcherpakov M., Delaunay A., Toth J., Kadoya T., Petroski M.D.,
Ronai Z.A.;
"Regulation of endoplasmic reticulum-associated degradation by RNF5-
dependent ubiquitination of JNK-associated membrane protein (JAMP).";
J. Biol. Chem. 284:12099-12109(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; THR-94 AND SER-107,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
PubMed=25489052; DOI=10.1093/hmg/ddu611;
Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K.,
Arnesen T.;
"Biochemical and cellular analysis of Ogden syndrome reveals
downstream Nt-acetylation defects.";
Hum. Mol. Genet. 24:1956-1976(2015).
-!- FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity.
May function together with E2 ubiquitin-conjugating enzymes
UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of
PXN/paxillin and Salmonella type III secreted protein sopA. May be
involved in regulation of cell motility and localization of
PXN/paxillin. Mediates the 'Lys-63'-linked polyubiquitination of
JKAMP thereby regulating JKAMP function by decreasing its
association with components of the proteasome and ERAD; the
ubiquitination appears to involve E2 ubiquitin-conjugating enzyme
UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of TMEM173
at 'Lys-150' leading to its proteasomal degradation; the
ubiquitination occurs in mitochondria after viral transfection and
regulates antiviral responses. {ECO:0000269|PubMed:11329381,
ECO:0000269|PubMed:12861019, ECO:0000269|PubMed:16176924,
ECO:0000269|PubMed:19269966, ECO:0000269|PubMed:19285439}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with PXN. Interacts with Salmonella typhimurium
sopA. Interacts with JKAMP. Interacts with TMEM173; the
interaction of endogenous proteins is dependent on viral
infection. {ECO:0000269|PubMed:12861019,
ECO:0000269|PubMed:19269966, ECO:0000269|PubMed:19285439}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-348482, EBI-348482;
O95870:ABHD16A; NbExp=6; IntAct=EBI-348482, EBI-348517;
P13569:CFTR; NbExp=3; IntAct=EBI-348482, EBI-349854;
P49447:CYB561; NbExp=3; IntAct=EBI-348482, EBI-8646596;
Q8NBI2:CYB561A3; NbExp=5; IntAct=EBI-348482, EBI-10269179;
Q9Y5U4:INSIG2; NbExp=5; IntAct=EBI-348482, EBI-8503746;
O95214:LEPROTL1; NbExp=4; IntAct=EBI-348482, EBI-750776;
Q04941:PLP2; NbExp=4; IntAct=EBI-348482, EBI-608347;
P49023:PXN; NbExp=6; IntAct=EBI-348482, EBI-702209;
Q96GF1:RNF185; NbExp=3; IntAct=EBI-348482, EBI-2340249;
Q96IW7:SEC22A; NbExp=3; IntAct=EBI-348482, EBI-8652744;
P43005:SLC1A1; NbExp=5; IntAct=EBI-348482, EBI-745376;
Q15758:SLC1A5; NbExp=4; IntAct=EBI-348482, EBI-356576;
Q96QD8:SLC38A2; NbExp=3; IntAct=EBI-348482, EBI-723083;
Q9NVC3:SLC38A7; NbExp=3; IntAct=EBI-348482, EBI-10314552;
Q9NWH2:TMEM242; NbExp=3; IntAct=EBI-348482, EBI-10315004;
P51668:UBE2D1; NbExp=7; IntAct=EBI-348482, EBI-743540;
P62837:UBE2D2; NbExp=6; IntAct=EBI-348482, EBI-347677;
P61077:UBE2D3; NbExp=8; IntAct=EBI-348482, EBI-348268;
Q9Y2X8:UBE2D4; NbExp=6; IntAct=EBI-348482, EBI-745527;
Q96LR5:UBE2E2; NbExp=7; IntAct=EBI-348482, EBI-2129763;
Q969T4:UBE2E3; NbExp=7; IntAct=EBI-348482, EBI-348496;
P61086:UBE2K; NbExp=5; IntAct=EBI-348482, EBI-473850;
Q96B02:UBE2W; NbExp=4; IntAct=EBI-348482, EBI-716589;
Q96FI0:UBE2W; NbExp=3; IntAct=EBI-348482, EBI-10285774;
Q9BWQ6:YIPF2; NbExp=7; IntAct=EBI-348482, EBI-751204;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
Mitochondrion membrane. Endoplasmic reticulum membrane.
Note=Predominantly located in the plasma membrane, with some
localization occurring within cytoplasmic organelles.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9533025}.
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EMBL; AB056869; BAB39359.1; -; mRNA.
EMBL; AJ243936; CAB51286.1; -; mRNA.
EMBL; AK311859; BAG34800.1; -; mRNA.
EMBL; BT007105; AAP35769.1; -; mRNA.
EMBL; U89336; AAB47492.1; -; Genomic_DNA.
EMBL; AL845464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX284686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX927239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR812478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR933878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004155; AAH04155.1; -; mRNA.
EMBL; BC111392; AAI11393.1; -; mRNA.
EMBL; BC119741; AAI19742.1; -; mRNA.
EMBL; BC119742; AAI19743.1; -; mRNA.
EMBL; BC127651; AAI27652.1; -; mRNA.
EMBL; BC127652; AAI27653.1; -; mRNA.
EMBL; BC148255; AAI48256.1; -; mRNA.
CCDS; CCDS4745.1; -.
RefSeq; NP_008844.1; NM_006913.3.
UniGene; Hs.731774; -.
ProteinModelPortal; Q99942; -.
SMR; Q99942; -.
BioGrid; 111975; 59.
DIP; DIP-29268N; -.
IntAct; Q99942; 63.
MINT; MINT-1032027; -.
STRING; 9606.ENSP00000364235; -.
iPTMnet; Q99942; -.
PhosphoSitePlus; Q99942; -.
BioMuta; RNF5; -.
DMDM; 74762702; -.
EPD; Q99942; -.
MaxQB; Q99942; -.
PaxDb; Q99942; -.
PeptideAtlas; Q99942; -.
PRIDE; Q99942; -.
TopDownProteomics; Q99942; -.
DNASU; 6048; -.
Ensembl; ENST00000375094; ENSP00000364235; ENSG00000204308.
Ensembl; ENST00000413786; ENSP00000387879; ENSG00000225452.
Ensembl; ENST00000432616; ENSP00000413131; ENSG00000183574.
Ensembl; ENST00000445885; ENSP00000401172; ENSG00000227277.
Ensembl; ENST00000449794; ENSP00000415784; ENSG00000223767.
Ensembl; ENST00000453473; ENSP00000415127; ENSG00000228907.
Ensembl; ENST00000456167; ENSP00000388795; ENSG00000228405.
GeneID; 6048; -.
KEGG; hsa:6048; -.
UCSC; uc003oaj.5; human.
CTD; 6048; -.
DisGeNET; 6048; -.
EuPathDB; HostDB:ENSG00000204308.7; -.
GeneCards; RNF5; -.
H-InvDB; HIX0034363; -.
HGNC; HGNC:10068; RNF5.
HPA; CAB034107; -.
HPA; HPA065032; -.
MIM; 602677; gene.
neXtProt; NX_Q99942; -.
OpenTargets; ENSG00000204308; -.
PharmGKB; PA34442; -.
eggNOG; KOG0823; Eukaryota.
eggNOG; ENOG4111IHV; LUCA.
GeneTree; ENSGT00390000014107; -.
HOGENOM; HOG000238304; -.
HOVERGEN; HBG054495; -.
InParanoid; Q99942; -.
KO; K10666; -.
OMA; TVFNTND; -.
OrthoDB; EOG091G0W2I; -.
PhylomeDB; Q99942; -.
TreeFam; TF317334; -.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
UniPathway; UPA00143; -.
GeneWiki; RNF5; -.
GenomeRNAi; 6048; -.
PRO; PR:Q99942; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204308; -.
CleanEx; HS_RNF5; -.
ExpressionAtlas; Q99942; baseline and differential.
Genevisible; Q99942; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:1904264; F:ubiquitin protein ligase activity involved in ERAD pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0044257; P:cellular protein catabolic process; IMP:UniProtKB.
GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:UniProtKB.
GO; GO:0036503; P:ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:2000785; P:regulation of autophagosome assembly; IEA:Ensembl.
GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Endoplasmic reticulum; Membrane;
Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome;
Transferase; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:25489052}.
CHAIN 2 180 E3 ubiquitin-protein ligase RNF5.
/FTId=PRO_0000240393.
TRANSMEM 118 138 Helical. {ECO:0000255}.
TRANSMEM 160 180 Helical. {ECO:0000255}.
ZN_FING 27 68 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:25489052}.
MOD_RES 84 84 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 94 94 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MUTAGEN 42 42 C->S: Loss of E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:11329381}.
CONFLICT 22 22 G -> S (in Ref. 3; CAB51286).
{ECO:0000305}.
CONFLICT 60 60 E -> D (in Ref. 3; CAB51286).
{ECO:0000305}.
CONFLICT 117 117 T -> A (in Ref. 3; CAB51286).
{ECO:0000305}.
CONFLICT 148 148 T -> A (in Ref. 3; CAB51286).
{ECO:0000305}.
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


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