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CHERP_MOUSE
ID   CHERP_MOUSE             Reviewed;         936 AA.
AC   Q8CGZ0; Q8K291; Q8VCD2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Calcium homeostasis endoplasmic reticulum protein;
DE   AltName: Full=SR-related CTD-associated factor 6;
GN   Name=Cherp {ECO:0000312|MGI:MGI:106417};
GN   Synonyms=Scaf6 {ECO:0000312|EMBL:AAN77182.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAN77182.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sampson N.D., Hewitt J.E.;
RT   "Functional characterization of the novel SR-related CTD associated factor,
RT   SCAF6.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-723, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824; SER-826 AND THR-828, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-822; SER-824; SER-826 AND
RP   THR-828, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in calcium homeostasis, growth and proliferation.
CC       {ECO:0000250|UniProtKB:Q8IWX8}.
CC   -!- INTERACTION:
CC       Q8CGZ0; Q15637: SF1; Xeno; NbExp=3; IntAct=EBI-2366446, EBI-744603;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IWX8}.
CC       Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWX8}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IWX8}. Note=Distributed
CC       throughout the cytoplasm and also localizes to the perinuclear region.
CC       Colocalizes with ITPR1 (By similarity). {ECO:0000250|UniProtKB:Q8IWX8}.
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DR   EMBL; AF536541; AAN77182.1; -; mRNA.
DR   EMBL; BC020488; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_613051.3; NM_138585.3.
DR   AlphaFoldDB; Q8CGZ0; -.
DR   SMR; Q8CGZ0; -.
DR   BioGRID; 205695; 4.
DR   IntAct; Q8CGZ0; 3.
DR   MINT; Q8CGZ0; -.
DR   STRING; 10090.ENSMUSP00000078469; -.
DR   iPTMnet; Q8CGZ0; -.
DR   PhosphoSitePlus; Q8CGZ0; -.
DR   EPD; Q8CGZ0; -.
DR   jPOST; Q8CGZ0; -.
DR   MaxQB; Q8CGZ0; -.
DR   PaxDb; Q8CGZ0; -.
DR   PRIDE; Q8CGZ0; -.
DR   ProteomicsDB; 281612; -.
DR   DNASU; 27967; -.
DR   GeneID; 27967; -.
DR   KEGG; mmu:27967; -.
DR   UCSC; uc009mgb.1; mouse.
DR   CTD; 10523; -.
DR   MGI; MGI:106417; Cherp.
DR   eggNOG; KOG4368; Eukaryota.
DR   InParanoid; Q8CGZ0; -.
DR   PhylomeDB; Q8CGZ0; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 27967; 21 hits in 72 CRISPR screens.
DR   ChiTaRS; Cherp; mouse.
DR   PRO; PR:Q8CGZ0; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8CGZ0; protein.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:MGI.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:MGI.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 1.10.10.790; -; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR039037; CHERP.
DR   InterPro; IPR006569; CID_dom.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR000061; Surp.
DR   InterPro; IPR035967; SWAP/Surp_sf.
DR   PANTHER; PTHR12323; PTHR12323; 3.
DR   Pfam; PF04818; CID; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF01805; Surp; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00648; SWAP; 1.
DR   SUPFAM; SSF109905; SSF109905; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   PROSITE; PS51391; CID; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50128; SURP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Endoplasmic reticulum; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..936
FT                   /note="Calcium homeostasis endoplasmic reticulum protein"
FT                   /id="PRO_0000299493"
FT   REPEAT          15..57
FT                   /note="SURP motif"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          149..289
FT                   /note="CID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT   DOMAIN          850..900
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          77..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..93
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..388
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..459
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..544
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..630
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..825
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT   MOD_RES         18
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT   MOD_RES         723
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         822
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         824
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         826
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         828
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         837
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT   MOD_RES         864
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT   MOD_RES         866
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT   MOD_RES         888
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT   MOD_RES         913
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT   CROSSLNK        853
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT   CROSSLNK        881
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT   CONFLICT        348..349
FT                   /note="Missing (in Ref. 2; BC020488)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   936 AA;  106169 MW;  8C29DF0822CA9EB3 CRC64;
     MEMPMPPDDQ ELRNVIDKLA QFVARNGPEF EKMTMEKQKD NPKFSFLFGG EFYSYYKCKL
     ALEQQQLICK QQAPELEPTS AMPPLPQPPL APTASLTPAQ GTPSMDELIQ QSQWSLQQQE
     QHLLALRQEQ VTTAVAHAVE QQMQKLLEET QLDMSEFDNL LQPIIDTCTK DAISAGKNWM
     FSNAKSPPHC ELMAGHLRNR ITADGAHFEL RLHLIYLIND VLHHCQRKQA RELLAALQKV
     VVPIYCTSFL AVEEDKQQKI ARLLQLWEKN GYFDDSIIQQ LQSPALGLGQ YQATLINEYS
     SVVQPVQLAF QQQIQSLKTQ HEEFVSSLAQ QQQQQQQQQQ QQPQPQPQPQ IQLPQMEADV
     KATPPPPAPP PASAPAPTIP PTTQPDDNKP PIQMPGSSEY DTSAGVQDPA AAGPRGPGPH
     EQIPPNKPPW FDQPHPVAPW GQQQPPEQPP YPHHQGGPPH CPPWNNSHEG MWGEQRGDPG
     WNGQRDAPWN NQPDPNWNNQ FEGPWNNQHE PPPWGGAQRE PPFRMQRPPH FRGPFPPHQQ
     HPQFNQPPHP HNFNRFPPRF MQDDFPPRHP FERPPYPHRF DYPQGDFPAD MGPPHHHPGH
     RMPHPGINEH PPWAGPQHPD FGPPPHGFNG QPPHMRRQGP PHINHDDPSL VPNVPYFDLP
     AGLMAPLVKL EDHEYKPLDP KDIRLPPPMP PSERLLAAVE AFYSPPSHDR PRNSEGWEQN
     GLYEFFRAKM RARRRKGQEK RNSGPSRSRS RSKSRGRSSS RSSSRSSKSS RSSSRSHSRS
     RSRSSSRSRS RSRSRSRSSR SRSRSRSRSR SKSYSPGRRR RSRSRSPTPP SAAGLGSNSA
     PPIPDSRLGE ENKGHQMLVK MGWSGSGGLG AKEQGIQDPI KGGDVRDKWD QYKGVGVALD
     DPYENYRRNK SYSFIARMKA RDEFSTFGTR KEEKED
 
 
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