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RING finger protein 37 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RNF37) (U-box domain-containing protein 5) (UbcM4-interacting protein 5)

 RNF37_MOUSE             Reviewed;         539 AA.
Q925F4;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
12-SEP-2018, entry version 131.
RecName: Full=RING finger protein 37 {ECO:0000305};
EC=2.3.2.27 {ECO:0000269|PubMed:11435423};
AltName: Full=RING-type E3 ubiquitin transferase RNF37 {ECO:0000305};
AltName: Full=U-box domain-containing protein 5 {ECO:0000312|MGI:MGI:2154658};
AltName: Full=UbcM4-interacting protein 5 {ECO:0000303|PubMed:11274149};
Name=Ubox5;
Synonyms=Rnf37 {ECO:0000305}, Uip5 {ECO:0000303|PubMed:11274149};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH UBE2L3, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11274149; DOI=10.1074/jbc.M100192200;
Pringa E., Martinez-Noel G., Muller U., Harbers K.;
"Interaction of the RING finger-related U-box motif of a nuclear dot
protein with ubiquitin-conjugating enzymes.";
J. Biol. Chem. 276:19617-19623(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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).
[3]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, DOMAIN,
AND MUTAGENESIS OF CYS-292 AND PRO-306.
PubMed=11435423; DOI=10.1074/jbc.M102755200;
Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
"U box proteins as a new family of ubiquitin-protein ligases.";
J. Biol. Chem. 276:33111-33120(2001).
[4]
INTERACTION WITH VCP.
PubMed=15189447; DOI=10.1111/j.1356-9597.2004.00742.x;
Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.;
"Interaction of U-box-type ubiquitin-protein ligases (E3s) with
molecular chaperones.";
Genes Cells 9:533-548(2004).
-!- FUNCTION: May have a ubiquitin-protein ligase activity acting as
an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase
promoting elongation of ubiquitin chains on substrates.
{ECO:0000269|PubMed:11435423}.
-!- 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. {ECO:0000269|PubMed:11435423}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:11435423}.
-!- SUBUNIT: Interacts with UBE2L3. Interacts with VCP.
{ECO:0000269|PubMed:11274149, ECO:0000269|PubMed:15189447}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11435423}.
Note=Enriched in nuclear bodies. {ECO:0000250|UniProtKB:O94941}.
-!- TISSUE SPECIFICITY: Expressed in testis and placenta.
{ECO:0000269|PubMed:11274149}.
-!- DEVELOPMENTAL STAGE: Expressed in embryos at 14.5 dpc.
{ECO:0000269|PubMed:11274149}.
-!- DOMAIN: The U-box domain mediates interaction with E2 ubiquitin
ligases and is required for the ubiquitin-protein ligase activity.
{ECO:0000250|UniProtKB:O94941, ECO:0000269|PubMed:11435423}.
-----------------------------------------------------------------------
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EMBL; AF360997; AAK51467.1; -; mRNA.
EMBL; BC025068; AAH25068.1; -; mRNA.
CCDS; CCDS16747.1; -.
RefSeq; NP_001242922.1; NM_001255993.1.
RefSeq; NP_001242923.1; NM_001255994.1.
RefSeq; NP_542129.2; NM_080562.5.
UniGene; Mm.486003; -.
UniGene; Mm.489731; -.
UniGene; Mm.489850; -.
ProteinModelPortal; Q925F4; -.
SMR; Q925F4; -.
BioGrid; 228291; 5.
STRING; 10090.ENSMUSP00000028761; -.
PhosphoSitePlus; Q925F4; -.
MaxQB; Q925F4; -.
PaxDb; Q925F4; -.
PRIDE; Q925F4; -.
Ensembl; ENSMUST00000028761; ENSMUSP00000028761; ENSMUSG00000027300.
GeneID; 140629; -.
KEGG; mmu:140629; -.
UCSC; uc008mji.3; mouse.
CTD; 22888; -.
MGI; MGI:2154658; Ubox5.
eggNOG; KOG2042; Eukaryota.
eggNOG; COG5113; LUCA.
GeneTree; ENSGT00510000049555; -.
HOGENOM; HOG000132931; -.
HOVERGEN; HBG054212; -.
InParanoid; Q925F4; -.
KO; K10600; -.
OMA; YQLPCGH; -.
OrthoDB; EOG091G0L8V; -.
PhylomeDB; Q925F4; -.
TreeFam; TF329105; -.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Ubox5; mouse.
PRO; PR:Q925F4; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027300; Expressed in 257 organ(s), highest expression level in ear.
CleanEx; MM_UBOX5; -.
ExpressionAtlas; Q925F4; baseline and differential.
Genevisible; Q925F4; MM.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR003613; Ubox_domain.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF04564; U-box; 1.
Pfam; PF14634; zf-RING_5; 1.
SMART; SM00504; Ubox; 1.
PROSITE; PS51698; U_BOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Complete proteome; Metal-binding; Nucleus; Reference proteome;
Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 539 RING finger protein 37.
/FTId=PRO_0000056077.
DOMAIN 258 338 U-box.
ZN_FING 481 526 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
MUTAGEN 292 292 C->A: No effect on E3 ubiquitin-protein
ligase activity.
{ECO:0000269|PubMed:11435423}.
MUTAGEN 306 306 P->A: Loss of E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:11435423}.
CONFLICT 75 75 Y -> C (in Ref. 2; AAH25068).
{ECO:0000305}.
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


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