RNF37_HUMAN
ID RNF37_HUMAN Reviewed; 541 AA.
AC O94941; Q6IAR5; Q86X87; Q9H4J2;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=RING finger protein 37 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q925F4};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF37 {ECO:0000305};
DE AltName: Full=U-box domain-containing protein 5 {ECO:0000312|HGNC:HGNC:17777};
DE AltName: Full=UbcM4-interacting protein 5 {ECO:0000303|PubMed:10431818};
DE Short=hUIP5 {ECO:0000303|PubMed:11274149};
DE AltName: Full=Ubiquitin-conjugating enzyme 7-interacting protein 5 {ECO:0000312|EMBL:CAG33370.1};
GN Name=UBOX5 {ECO:0000312|HGNC:HGNC:17777};
GN Synonyms=KIAA0860 {ECO:0000312|EMBL:BAA74883.2}, RNF37 {ECO:0000305},
GN UBCE7IP5 {ECO:0000312|EMBL:CAG33370.1}, UIP5 {ECO:0000303|PubMed:10431818};
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Lymph;
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 [7]
RP IDENTIFICATION.
RX PubMed=10431818; DOI=10.1016/s0014-5793(99)00823-6;
RA Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.;
RT "A family of structurally related RING finger proteins interacts
RT specifically with the ubiquitin-conjugating enzyme UbcM4.";
RL FEBS Lett. 454:257-261(1999).
RN [8]
RP INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=11274149; DOI=10.1074/jbc.m100192200;
RA Pringa E., Martinez-Noel G., Muller U., Harbers K.;
RT "Interaction of the RING finger-related U-box motif of a nuclear dot
RT protein with ubiquitin-conjugating enzymes.";
RL J. Biol. Chem. 276:19617-19623(2001).
RN [9]
RP TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=11435423; DOI=10.1074/jbc.m102755200;
RA Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
RT "U box proteins as a new family of ubiquitin-protein ligases.";
RL J. Biol. Chem. 276:33111-33120(2001).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-451, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May have a ubiquitin-protein ligase activity acting as an E3
CC ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting
CC elongation of ubiquitin chains on substrates.
CC {ECO:0000250|UniProtKB:Q925F4}.
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:0000250|UniProtKB:Q925F4};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q925F4}.
CC -!- SUBUNIT: Interacts with UBE2L3. Interacts with VCP.
CC {ECO:0000250|UniProtKB:Q925F4, ECO:0000269|PubMed:11274149}.
CC -!- INTERACTION:
CC O94941; P54253: ATXN1; NbExp=6; IntAct=EBI-751901, EBI-930964;
CC O94941; V9HW80: HEL-S-70; NbExp=3; IntAct=EBI-751901, EBI-10175326;
CC O94941; P40692: MLH1; NbExp=7; IntAct=EBI-751901, EBI-744248;
CC O94941; Q13148: TARDBP; NbExp=3; IntAct=EBI-751901, EBI-372899;
CC O94941; P55072: VCP; NbExp=3; IntAct=EBI-751901, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11274149,
CC ECO:0000269|PubMed:11435423}. Note=Enriched in nuclear bodies.
CC {ECO:0000269|PubMed:11274149}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94941-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94941-2; Sequence=VSP_042899;
CC -!- TISSUE SPECIFICITY: Expressed in liver, heart, brain, kidney and
CC testis. {ECO:0000269|PubMed:11435423}.
CC -!- DOMAIN: The U-box domain mediates interaction with E2 ubiquitin ligases
CC and is required for the ubiquitin-protein ligase activity.
CC {ECO:0000269|PubMed:11435423, ECO:0000303|PubMed:11274149}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74883.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB020667; BAA74883.2; ALT_INIT; mRNA.
DR EMBL; AK022444; BAG51073.1; -; mRNA.
DR EMBL; CR457089; CAG33370.1; -; mRNA.
DR EMBL; AL121891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10550.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10551.1; -; Genomic_DNA.
DR EMBL; BC000515; AAH00515.1; -; mRNA.
DR EMBL; BC046122; AAH46122.1; -; mRNA.
DR CCDS; CCDS13046.1; -. [O94941-1]
DR CCDS; CCDS13047.1; -. [O94941-2]
DR RefSeq; NP_055763.1; NM_014948.3. [O94941-1]
DR RefSeq; NP_955447.1; NM_199415.2. [O94941-2]
DR AlphaFoldDB; O94941; -.
DR SMR; O94941; -.
DR BioGRID; 116554; 24.
DR IntAct; O94941; 19.
DR STRING; 9606.ENSP00000217173; -.
DR iPTMnet; O94941; -.
DR PhosphoSitePlus; O94941; -.
DR BioMuta; UBOX5; -.
DR EPD; O94941; -.
DR jPOST; O94941; -.
DR MassIVE; O94941; -.
DR MaxQB; O94941; -.
DR PaxDb; O94941; -.
DR PeptideAtlas; O94941; -.
DR PRIDE; O94941; -.
DR ProteomicsDB; 50570; -. [O94941-1]
DR ProteomicsDB; 50571; -. [O94941-2]
DR Antibodypedia; 23444; 206 antibodies from 20 providers.
DR DNASU; 22888; -.
DR Ensembl; ENST00000217173.7; ENSP00000217173.2; ENSG00000185019.17. [O94941-1]
DR Ensembl; ENST00000348031.6; ENSP00000311726.3; ENSG00000185019.17. [O94941-2]
DR GeneID; 22888; -.
DR KEGG; hsa:22888; -.
DR MANE-Select; ENST00000217173.7; ENSP00000217173.2; NM_014948.4; NP_055763.1.
DR UCSC; uc002whw.5; human. [O94941-1]
DR CTD; 22888; -.
DR DisGeNET; 22888; -.
DR GeneCards; UBOX5; -.
DR HGNC; HGNC:17777; UBOX5.
DR HPA; ENSG00000185019; Low tissue specificity.
DR MIM; 619675; gene.
DR neXtProt; NX_O94941; -.
DR OpenTargets; ENSG00000185019; -.
DR PharmGKB; PA134991794; -.
DR VEuPathDB; HostDB:ENSG00000185019; -.
DR eggNOG; KOG2042; Eukaryota.
DR GeneTree; ENSGT00510000049555; -.
DR HOGENOM; CLU_038691_0_0_1; -.
DR InParanoid; O94941; -.
DR OMA; MDCSTDP; -.
DR OrthoDB; 725845at2759; -.
DR PhylomeDB; O94941; -.
DR TreeFam; TF329105; -.
DR PathwayCommons; O94941; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O94941; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22888; 17 hits in 1117 CRISPR screens.
DR ChiTaRS; UBOX5; human.
DR GeneWiki; UBOX5; -.
DR GenomeRNAi; 22888; -.
DR Pharos; O94941; Tbio.
DR PRO; PR:O94941; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O94941; protein.
DR Bgee; ENSG00000185019; Expressed in parotid gland and 166 other tissues.
DR ExpressionAtlas; O94941; baseline and differential.
DR Genevisible; O94941; HS.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR CDD; cd16660; RING-Ubox_RNF37; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR039925; RNF37_RING-Ubox.
DR InterPro; IPR039847; Ubox5.
DR InterPro; IPR045696; Ubox5_N.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13492; PTHR13492; 1.
DR Pfam; PF19318; DUF5918; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00504; Ubox; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Methylation; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..541
FT /note="RING finger protein 37"
FT /id="PRO_0000056076"
FT DOMAIN 258..338
FT /note="U-box"
FT ZN_FING 483..528
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 451
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 419..472
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_042899"
FT VARIANT 96
FT /note="T -> M (in dbSNP:rs999409)"
FT /id="VAR_046402"
FT VARIANT 479
FT /note="L -> P (in dbSNP:rs34205880)"
FT /id="VAR_046403"
SQ SEQUENCE 541 AA; 58966 MW; 4AF1A0C5115FAF7B CRC64;
MVINLCLPQF RPRIHCNKIS ADGYEVENLI SEDLTKRSHG FRTEYFIKPP VYVTVSFPFN
VEICRINIDL TAGGGQNVTG LEMYTSASSS RVSWNTPQCR TLGPAEPSVP DKEAFTLVGK
VLLKNQSQVV FSHRGFKARP PFGAMEATLP SPAVVAQELW NKGALSLSHV AHLRICITHV
TGGGIPCIKR LEVWGQPAKT CSQEVIDSIL LVTSENLPQD VALQAPALPM ESDCDPGDQP
ESQQAPSSLQ KLAEIIQDVP EEFLDPITLE IMPCPMLLPS GKVIDQSTLE KCNRSEATWG
RVPSDPFTGV AFTPHSQPLP HPSLKARIDH FLLQHSIPGC HLLGRAQTAL AVIPSSIVLP
SQKRKIEQAE HVPDSNFGVN ASCFSATSPL VLPTTSEHTA KKMKATNEPS LTHMDCSTGP
LSHEQKLSQS LEIALASTLG SMPSFTARLT RGQLQHLGTR GSNTSWRPGT GSEQPGSILG
PECASCKRVF SPYFKKEPVY QLPCGHLLCR PCLGEKQRSL PMTCTACQRP VASQDVLRVH
F
