SH3R2_RAT
ID SH3R2_RAT Reviewed; 735 AA.
AC Q498M5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=E3 ubiquitin-protein ligase SH3RF2;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8TEC5};
DE AltName: Full=POSH-eliminating RING protein {ECO:0000303|PubMed:22128169};
DE AltName: Full=Protein phosphatase 1 regulatory subunit 39;
DE AltName: Full=RING finger protein 158;
DE AltName: Full=RING-type E3 ubiquitin transferase SH3RF2 {ECO:0000305};
DE AltName: Full=SH3 domain-containing RING finger protein 2;
GN Name=Sh3rf2;
GN Synonyms=Posh3, Posher {ECO:0000303|PubMed:22128169}, Ppp1r39, Rnf158;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH DLK1;
RP MAP3K10; MAPK8IP1; MAPK8IP2; MAPK8IP3; RAC1 AND SH3RF1.
RX PubMed=22128169; DOI=10.1074/jbc.m111.269431;
RA Wilhelm M., Kukekov N.V., Schmit T.L., Biagas K.V., Sproul A.A., Gire S.,
RA Maes M.E., Xu Z., Greene L.A.;
RT "Sh3rf2/POSHER protein promotes cell survival by RING-mediated proteasomal
RT degradation of the c-Jun N-terminal kinase scaffold POSH (Plenty of SH3s)
RT protein.";
RL J. Biol. Chem. 287:2247-2256(2012).
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity. Acts as an anti-
CC apoptotic regulator of the JNK pathway by ubiquitinating and promoting
CC the degradation of SH3RF1, a scaffold protein that is required for pro-
CC apoptotic JNK activation (PubMed:22128169). Facilitates TNF-alpha-
CC mediated recruitment of adapter proteins TRADD and RIPK1 to TNFRSF1A
CC and regulates PAK4 protein stability via inhibition of its ubiquitin-
CC mediated proteasomal degradation. Inhibits PPP1CA phosphatase activity
CC (By similarity). {ECO:0000250|UniProtKB:Q8TEC5,
CC ECO:0000269|PubMed:22128169}.
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:Q8TEC5};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with FASLG and PPP1CA. Interacts with PAK4 and
CC TNFRSF1A (By similarity). Interacts with DLK1, MAP3K10, MAPK8IP1/JIP1,
CC MAPK8IP2/JIP2 and MAPK8IP3/JIP3. Interacts with RAC1 (both active
CC GTP- or inactive GDP-bound forms) (PubMed:22128169).
CC {ECO:0000250|UniProtKB:Q8TEC5, ECO:0000269|PubMed:22128169}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TEC5}.
CC -!- DOMAIN: The RING finger domain is required for ubiquitin ligase
CC activity and autoubiquitination. {ECO:0000250|UniProtKB:Q8TEC5}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q8TEC5}.
CC -!- SIMILARITY: Belongs to the SH3RF family. {ECO:0000305}.
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DR EMBL; BC100155; AAI00156.1; -; mRNA.
DR RefSeq; NP_001029359.1; NM_001034187.1.
DR AlphaFoldDB; Q498M5; -.
DR SMR; Q498M5; -.
DR STRING; 10116.ENSRNOP00000025409; -.
DR iPTMnet; Q498M5; -.
DR PhosphoSitePlus; Q498M5; -.
DR PaxDb; Q498M5; -.
DR Ensembl; ENSRNOT00000025408; ENSRNOP00000025409; ENSRNOG00000018780.
DR GeneID; 307472; -.
DR KEGG; rno:307472; -.
DR UCSC; RGD:1308415; rat.
DR CTD; 153769; -.
DR RGD; 1308415; Sh3rf2.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160067; -.
DR HOGENOM; CLU_015769_2_0_1; -.
DR InParanoid; Q498M5; -.
DR OMA; SVITQHM; -.
DR OrthoDB; 291531at2759; -.
DR PhylomeDB; Q498M5; -.
DR TreeFam; TF105571; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q498M5; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000018780; Expressed in testis and 16 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISS:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd11929; SH3_SH3RF2_1; 1.
DR CDD; cd11932; SH3_SH3RF2_2; 1.
DR CDD; cd11784; SH3_SH3RF2_3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028511; SH3RF2.
DR InterPro; IPR035792; SH3RF2_SH3_1.
DR InterPro; IPR035794; SH3RF2_SH3_2.
DR InterPro; IPR035822; SH3RF2_SH3_3.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14167:SF60; PTHR14167:SF60; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase inhibitor;
KW Reference proteome; Repeat; SH3 domain; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..735
FT /note="E3 ubiquitin-protein ligase SH3RF2"
FT /id="PRO_0000269514"
FT DOMAIN 125..184
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 187..252
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 383..444
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 12..53
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 260..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..466
FT /note="Interaction with PAK4"
FT /evidence="ECO:0000250|UniProtKB:Q8TEC5"
FT REGION 472..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..652
FT /note="Interaction with PPP1CA"
FT /evidence="ECO:0000250"
FT REGION 649..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 735 AA; 79880 MW; D6A1851B2A6046B0 CRC64;
MDDLTLLDLL ECPVCFEKLD VTAKVLPCQH TFCKPCLQRI FKAHKELRCP ECRTLVFCSI
EALPANLLLV RLLDGVRSGH NSWRGGSFRR PRILTLQDNR KAKSSPRSLQ ASPFRLGPTV
RIHMDGVPRA KALCNYRGKN PGDLKFNKGD VILLQRQLDE NWYQGEINGV SGFFPASSVE
VIKQLPQPPP LCRALYNFDL RDKDKSENQD CLTFLKDDVI TVISRVDENW AEGKLGDKVG
IFPILFVEPN LSARHLLEKS KGHQLSRTKH LSLMSSPSRG KATNTSTLRK SPGSRRKGSG
QFAMTTALNT LNRMVHSPEG HQMVEISTPV LISSTSPSML TQHGDRADFP ASSAGQVSTS
HPAPASPGHS TAMVSVPSSQ QHLSTNMFVA LHTYSAQGPE ELDLKKGEGI RVLGKNQDGW
LRGVSLVTGR TGIFPSDYVI PVFSSTARKT SSFPDSRHPT VCTTWALSTS SVSSQGSFSE
GDPRQSGPFR SVFVPTAVNP PRSTSGPGTS GQGSLRKVRS SMRKNGSLQR PVQSGIPTFM
VGSLRCSPAM VIRPQKFQFY QPQGMTPSPT PIMVEIGSKS ISTGEPALTC INRGGKTRTH
SAGNSIIMEG KETPIKSEPP PKPPASAPPS ILVKPENSKN GIEKQVKTVR FQNYSPPPTK
HSASGPTSGK HEQPATLKGS QPEAVSSEGE MTILFAHRSG CHSGQQTDLR RKSAFSKTTP
PVSTASVSQT LFPSK
