RNF37_MOUSE
ID RNF37_MOUSE Reviewed; 539 AA.
AC Q925F4;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=RING finger protein 37 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:11435423};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF37 {ECO:0000305};
DE AltName: Full=U-box domain-containing protein 5 {ECO:0000312|MGI:MGI:2154658};
DE AltName: Full=UbcM4-interacting protein 5 {ECO:0000303|PubMed:11274149};
GN Name=Ubox5;
GN Synonyms=Rnf37 {ECO:0000305}, Uip5 {ECO:0000303|PubMed:11274149};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH UBE2L3, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF CYS-292 AND PRO-306.
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 [4]
RP INTERACTION WITH VCP.
RX PubMed=15189447; DOI=10.1111/j.1356-9597.2004.00742.x;
RA Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.;
RT "Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular
RT chaperones.";
RL Genes Cells 9:533-548(2004).
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:0000269|PubMed:11435423}.
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:11435423};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:11435423}.
CC -!- SUBUNIT: Interacts with UBE2L3. Interacts with VCP.
CC {ECO:0000269|PubMed:11274149, ECO:0000269|PubMed:15189447}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11435423}.
CC Note=Enriched in nuclear bodies. {ECO:0000250|UniProtKB:O94941}.
CC -!- TISSUE SPECIFICITY: Expressed in testis and placenta.
CC {ECO:0000269|PubMed:11274149}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos at 14.5 dpc.
CC {ECO:0000269|PubMed:11274149}.
CC -!- DOMAIN: The U-box domain mediates interaction with E2 ubiquitin ligases
CC and is required for the ubiquitin-protein ligase activity.
CC {ECO:0000250|UniProtKB:O94941, ECO:0000269|PubMed:11435423}.
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DR EMBL; AF360997; AAK51467.1; -; mRNA.
DR EMBL; BC025068; AAH25068.1; -; mRNA.
DR CCDS; CCDS16747.1; -.
DR RefSeq; NP_001242922.1; NM_001255993.1.
DR RefSeq; NP_001242923.1; NM_001255994.1.
DR RefSeq; NP_542129.2; NM_080562.5.
DR AlphaFoldDB; Q925F4; -.
DR SMR; Q925F4; -.
DR BioGRID; 228291; 7.
DR STRING; 10090.ENSMUSP00000028761; -.
DR PhosphoSitePlus; Q925F4; -.
DR MaxQB; Q925F4; -.
DR PaxDb; Q925F4; -.
DR PRIDE; Q925F4; -.
DR ProteomicsDB; 300501; -.
DR Antibodypedia; 23444; 206 antibodies from 20 providers.
DR DNASU; 140629; -.
DR Ensembl; ENSMUST00000028761; ENSMUSP00000028761; ENSMUSG00000027300.
DR GeneID; 140629; -.
DR KEGG; mmu:140629; -.
DR UCSC; uc008mji.3; mouse.
DR CTD; 22888; -.
DR MGI; MGI:2154658; Ubox5.
DR VEuPathDB; HostDB:ENSMUSG00000027300; -.
DR eggNOG; KOG2042; Eukaryota.
DR GeneTree; ENSGT00510000049555; -.
DR HOGENOM; CLU_038691_0_0_1; -.
DR InParanoid; Q925F4; -.
DR OMA; MDCSTDP; -.
DR OrthoDB; 725845at2759; -.
DR PhylomeDB; Q925F4; -.
DR TreeFam; TF329105; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 140629; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ubox5; mouse.
DR PRO; PR:Q925F4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q925F4; protein.
DR Bgee; ENSMUSG00000027300; Expressed in ureteric bud trunk and 231 other tissues.
DR ExpressionAtlas; Q925F4; baseline and differential.
DR Genevisible; Q925F4; MM.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
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 Pfam; PF14634; zf-RING_5; 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 Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..539
FT /note="RING finger protein 37"
FT /id="PRO_0000056077"
FT DOMAIN 258..338
FT /note="U-box"
FT ZN_FING 481..526
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 226..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 292
FT /note="C->A: No effect on E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:11435423"
FT MUTAGEN 306
FT /note="P->A: Loss of E3 ubiquitin-protein ligase activity."
FT /evidence="ECO:0000269|PubMed:11435423"
FT CONFLICT 75
FT /note="Y -> C (in Ref. 2; AAH25068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 58732 MW; 93F7372A9F888814 CRC64;
MVVNLCLPQF RPRIHCNKVS ADGYEVENLI SEDLIKRSHG FRTEYFIRPP IYVTVSFPFN
VEICRVNIDL TTGGYQNVSG LELYTSALSS RVSQDAQDCW TTGPVETSVP DKEAFTLVGK
VLLKNQNHVV FSHRGFKARP PFSPMEVTLL SPAVVAQELW NKGALSLSHV AHLKIGITHV
TGSGISCIKR LEVWGQPART CSQEVINSVL LIASESLPQD LDLHAPALPM ESDCDPGGQS
ESQHSPCTLQ DMSEVESDVP EEFLDPITLE IMPCPMLLPS GKVIDQSTLE KCNLSEAAWG
RVPSDPFTGL AFTPQSQPLP HPSLKARIDR FLLQHSISGC RLLGRAQTPS AMTPSVITLP
SRKRKTEQAE HSSHYSLGMS ASSSATSPLF SPTTSEPTAK KMKATSELGL TDMDCSAGPV
SHEQKLAQSL EIALTSTLGS MPSFTARLTK GQLQLGTRGS SACRRPASSS EHPRSVSGPE
CASCKQAFSS YSTNEPVYQL PCGHLLCRPC LSEKQRSQPM MCTACRQPVT SQDVLRVHF
