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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
 
 
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