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SH3R1_RAT
ID   SH3R1_RAT               Reviewed;         894 AA.
AC   Q71F54;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=E3 ubiquitin-protein ligase SH3RF1;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q7Z6J0};
DE   AltName: Full=Plenty of SH3s;
DE            Short=Protein POSH;
DE   AltName: Full=RING-type E3 ubiquitin transferase SH3RF1 {ECO:0000305};
DE   AltName: Full=SH3 domain-containing RING finger protein 1;
DE   AltName: Full=SH3 multiple domains protein 2;
GN   Name=Sh3rf1; Synonyms=Posh, Posh1 {ECO:0000250|UniProtKB:Q7Z6J0}, Sh3md2;
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 [MRNA], INTERACTION WITH MAP3K10; MAP3K11; DLK1;
RP   MAP2K4; MAP2K7; MAPK8 AND MAPK9, UBIQUITINATION, AND FUNCTION.
RC   STRAIN=New England Deaconess Hospital;
RX   PubMed=12514131; DOI=10.1093/emboj/cdg021;
RA   Xu Z., Kukekov N.V., Greene L.A.;
RT   "POSH acts as a scaffold for a multiprotein complex that mediates JNK
RT   activation in apoptosis.";
RL   EMBO J. 22:252-261(2003).
RN   [2]
RP   INTERACTION WITH SIAH1.
RX   PubMed=16230351; DOI=10.1074/jbc.m509060200;
RA   Xu Z., Sproul A., Wang W., Kukekov N., Greene L.A.;
RT   "Siah1 interacts with the scaffold protein POSH to promote JNK activation
RT   and apoptosis.";
RL   J. Biol. Chem. 281:303-312(2006).
RN   [3]
RP   INTERACTION WITH MAPK8IP, AND SUBCELLULAR LOCATION.
RX   PubMed=16571722; DOI=10.1074/jbc.m601056200;
RA   Kukekov N.V., Xu Z., Greene L.A.;
RT   "Direct interaction of the molecular scaffolds POSH and JIP is required for
RT   apoptotic activation of JNKs.";
RL   J. Biol. Chem. 281:15517-15524(2006).
RN   [4]
RP   INTERACTION WITH SH3RF2, UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
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).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743, 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).
CC   -!- FUNCTION: Has E3 ubiquitin-protein ligase activity. In the absence of
CC       an external substrate, it can catalyze self-ubiquitination. Stimulates
CC       ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-
CC       dependent and clathrin-independent endocytosis (By similarity). Acts as
CC       a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing
CC       different components of the JNK pathway, including RAC1 or RAC2,
CC       MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2
CC       into a functional multiprotein complex to ensure the effective
CC       activation of the JNK signaling pathway (PubMed:12514131). Regulates
CC       the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper
CC       1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1
CC       and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in
CC       CD8(+) T-cells. Plays a crucial role in the migration of neocortical
CC       neurons in the developing brain. Controls proper cortical neuronal
CC       migration and the formation of proximal cytoplasmic dilation in the
CC       leading process (PCDLP) in migratory neocortical neurons by regulating
CC       the proper localization of activated RAC1 and F-actin assembly (By
CC       similarity). {ECO:0000250|UniProtKB:Q69ZI1,
CC       ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:12514131}.
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:Q7Z6J0};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with HERP1. Interacts with RAC1; in a GTP-dependent
CC       manner (By similarity). Interacts with MAP3K10/MLK2 and MAP3K11/MLK3.
CC       Interacts with MAPK8IP; this interaction leads to the PJAC complex
CC       (POSH-JIP or SH3RF1/MAPK8IP apoptotic complex) with a 1:1 ratio.
CC       Interacts with SIAH1. Probably part of a signaling complex that may
CC       contain SH3RF1, MAPK8IP, DLK1, MAP2K4/MKK4, MAP2K7/MKK7, MAPK8/JNK1,
CC       MAPK9/JNK2, AKT1 and AKT2 (PubMed:12514131, PubMed:16230351,
CC       PubMed:16571722). Found in a complex with RAC2, MAP3K7/TAK1,
CC       MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2. Found in a
CC       complex with RAC1, MAP3K11/MLK3, MAP2K7/MKK7, MAPK8IP1/JIP1 and
CC       MAPK8/JNK1 (By similarity). Interacts with SH3RF2 (PubMed:22128169).
CC       {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0,
CC       ECO:0000269|PubMed:12514131, ECO:0000269|PubMed:16230351,
CC       ECO:0000269|PubMed:16571722, ECO:0000269|PubMed:22128169}.
CC   -!- INTERACTION:
CC       Q71F54; Q920M9: Siah1; NbExp=2; IntAct=EBI-957526, EBI-957514;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:16571722}. Cell projection, lamellipodium
CC       {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in
CC       lamellipodia. Colocalizes, with HERP1, in trans-Golgi network.
CC       {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
CC   -!- DOMAIN: The RING finger domain is required for ubiquitin ligase
CC       activity and autoubiquitination. {ECO:0000250|UniProtKB:Q7Z6J0}.
CC   -!- PTM: Phosphorylated at Ser-305 by AKT1 and AKT2. When phosphorylated,
CC       it has reduced ability to bind Rac. {ECO:0000250|UniProtKB:Q7Z6J0}.
CC   -!- PTM: Autoubiquitinated. Ubiquitinated by SH3RF2, leading to proteasome-
CC       mediated degradation. {ECO:0000269|PubMed:12514131,
CC       ECO:0000269|PubMed:22128169}.
CC   -!- SIMILARITY: Belongs to the SH3RF family. {ECO:0000305}.
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DR   EMBL; AF515735; AAQ08184.1; -; mRNA.
DR   RefSeq; NP_942059.1; NM_198764.1.
DR   RefSeq; XP_017455595.1; XM_017600106.1.
DR   AlphaFoldDB; Q71F54; -.
DR   SMR; Q71F54; -.
DR   IntAct; Q71F54; 1.
DR   STRING; 10116.ENSRNOP00000013815; -.
DR   iPTMnet; Q71F54; -.
DR   PhosphoSitePlus; Q71F54; -.
DR   PaxDb; Q71F54; -.
DR   PRIDE; Q71F54; -.
DR   Ensembl; ENSRNOT00000013816; ENSRNOP00000013815; ENSRNOG00000010358.
DR   GeneID; 306417; -.
DR   KEGG; rno:306417; -.
DR   UCSC; RGD:735154; rat.
DR   CTD; 57630; -.
DR   RGD; 735154; Sh3rf1.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000155875; -.
DR   HOGENOM; CLU_015769_1_0_1; -.
DR   InParanoid; Q71F54; -.
DR   OMA; LVCERYR; -.
DR   OrthoDB; 291531at2759; -.
DR   PhylomeDB; Q71F54; -.
DR   TreeFam; TF105571; -.
DR   Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q71F54; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000010358; Expressed in duodenum and 18 other tissues.
DR   Genevisible; Q71F54; RN.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005078; F:MAP-kinase scaffold activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR   GO; GO:0001764; P:neuron 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; IBA:GO_Central.
DR   GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0043370; P:regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR   GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; ISS:UniProtKB.
DR   CDD; cd11930; SH3_SH3RF1_2; 1.
DR   CDD; cd11785; SH3_SH3RF_C; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035816; SH3RF1/SH3RF3_SH3_4.
DR   InterPro; IPR035795; SH3RF1_SH3_2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF14604; SH3_9; 3.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00326; SH3; 4.
DR   SUPFAM; SSF50044; SSF50044; 4.
DR   PROSITE; PS50002; SH3; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cytoplasm; Golgi apparatus; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; SH3 domain; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..894
FT                   /note="E3 ubiquitin-protein ligase SH3RF1"
FT                   /id="PRO_0000334154"
FT   DOMAIN          134..193
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          196..259
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          453..514
FT                   /note="SH3 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          835..894
FT                   /note="SH3 4"
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          274..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..363
FT                   /note="Interaction with RAC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6J0"
FT   REGION          448..551
FT                   /note="Interaction with AKT2"
FT                   /evidence="ECO:0000250"
FT   REGION          526..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6J0"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6J0"
FT   MOD_RES         743
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   894 AA;  93879 MW;  E7CB1B7E6330C62D CRC64;
     MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV
     DELPSNILLV RLLDGIKQRP WKPGPGGGGS TTCTNVLRAQ GSTVVNCGSK DLQSPQCGQQ
     PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IILRRQVDEN WYHGEVNGVH
     GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG
     MLADKIGIFP ISYVEFNSAA KQLIEWDKPP VPGVDTAECP SATAAQSSSA SKHSDTKKNT
     RKRHSFTSLT MANKSSQASQ NRHSMEISPP VLISSSNPTA AARISELSGL SCSAPSQVHI
     STTGLIVTPP PSSPVTTGPS FTFPTDVPYQ AALGTMNPPL PPPPLLATTV LASTPSGATA
     AAVAAAAAAV AAGVGPRPAV GSTEQIAHLR PQTRPSVYVA IYPYTPRKED ELELRKGEMF
     LVFERCQDGW YKGTSMHTSK IGVFPGNYVA PVTRAVTNAS QAKVPMSTAG QASRGVTMVS
     PSTAGGPAQK PQGNGVAGNP SVVPTAVVSA AHIQTSPQAK VLLHMTGQMT VNQARNAVRT
     VAAHNQERPT AAVTPIQVQN AACIGPASVG LPHHSLASQP LPPMVGPAAH IAAVNINRTS
     VPLACAAGAS SLASPNMTTA ALETEPSGRT VTILPGLPTS PESAASACGN SSAVKPDKDS
     KKEKKGLLKL LSGASTKRKP RVSPPASPTL DVELGSGEVP LQGAVGPELP LGGVHGRVGS
     CPTDGDGPVA AGTAALAQDA FHRKTSSLDS AVPIAPPPRQ ACSSLGPVMN EARPVVCERH
     RVVVSYPPQS EAELELKEGD IVFVHKKRED GWFKGTLQRN GKTGLFPGSF VENI
 
 
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