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 24-JAN-2024, entry version 188. 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 GN {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; 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=6; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 25. DR IntAct; O94941; 18. 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; 9606-ENSP00000217173; -. DR PeptideAtlas; O94941; -. DR ProteomicsDB; 50570; -. [O94941-1] DR ProteomicsDB; 50571; -. [O94941-2] DR Pumba; O94941; -. DR Antibodypedia; 23444; 243 antibodies from 21 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 AGR; HGNC:17777; -. 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; NTSWRPG; -. DR OrthoDB; 2908152at2759; -. DR PhylomeDB; O94941; -. DR TreeFam; TF329105; -. DR PathwayCommons; O94941; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; O94941; -. DR SIGNOR; O94941; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 22888; 20 hits in 1196 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 primordial germ cell in gonad and 167 other cell types or tissues. DR ExpressionAtlas; O94941; baseline and differential. 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; cd16537; RING-HC_RNF37; 1. DR CDD; cd16660; RING-Ubox_RNF37; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; RING FINGER PROTEIN 37; 1. DR PANTHER; PTHR13492:SF2; RING FINGER PROTEIN 37; 1. DR Pfam; PF19318; DUF5918; 1. DR Pfam; PF04564; U-box; 1. DR Pfam; PF14634; zf-RING_5; 1. DR SMART; SM00504; Ubox; 1. DR SUPFAM; SSF57850; RING/U-box; 2. DR PROSITE; PS51698; U_BOX; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; O94941; HS. 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 //