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PP1R7_RAT
ID   PP1R7_RAT               Reviewed;         360 AA.
AC   Q5HZV9;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 7;
DE   AltName: Full=Protein phosphatase 1 regulatory subunit 22;
GN   Name=Ppp1r7; Synonyms=Sds22;
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=Brain;
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   PROTEIN SEQUENCE OF 276-285, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=7498485; DOI=10.1016/0014-5793(95)01180-m;
RA   Renouf S., Beullens M., Wera S., Van Eynde A., Sikela J., Stalmans W.,
RA   Bollen M.;
RT   "Molecular cloning of a human polypeptide related to yeast sds22, a
RT   regulator of protein phosphatase-1.";
RL   FEBS Lett. 375:75-78(1995).
RN   [4]
RP   ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver;
RX   PubMed=12555814; DOI=10.1139/o02-155;
RA   Tran H.T., Bridges D., Ulke A., Moorhead G.B.;
RT   "Detection of multiple splice variants of the nuclear protein phosphatase 1
RT   regulator sds22 in rat liver nuclei.";
RL   Biochem. Cell Biol. 80:811-815(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-24; SER-27; SER-44;
RP   SER-47 AND SER-322, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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: Regulatory subunit of protein phosphatase 1. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12555814,
CC       ECO:0000269|PubMed:7498485}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.;
CC       Name=1;
CC         IsoId=Q5HZV9-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the SDS22 family. {ECO:0000305}.
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DR   EMBL; BC088868; AAH88868.1; -; mRNA.
DR   RefSeq; NP_001009825.1; NM_001009825.1. [Q5HZV9-1]
DR   AlphaFoldDB; Q5HZV9; -.
DR   SMR; Q5HZV9; -.
DR   BioGRID; 257021; 1.
DR   IntAct; Q5HZV9; 1.
DR   STRING; 10116.ENSRNOP00000022854; -.
DR   iPTMnet; Q5HZV9; -.
DR   PhosphoSitePlus; Q5HZV9; -.
DR   jPOST; Q5HZV9; -.
DR   PaxDb; Q5HZV9; -.
DR   PRIDE; Q5HZV9; -.
DR   Ensembl; ENSRNOT00000095497; ENSRNOP00000081944; ENSRNOG00000016974. [Q5HZV9-1]
DR   GeneID; 301618; -.
DR   KEGG; rno:301618; -.
DR   UCSC; RGD:1308169; rat. [Q5HZV9-1]
DR   CTD; 5510; -.
DR   RGD; 1308169; Ppp1r7.
DR   eggNOG; KOG0531; Eukaryota.
DR   GeneTree; ENSGT00940000158551; -.
DR   InParanoid; Q5HZV9; -.
DR   OrthoDB; 968788at2759; -.
DR   PhylomeDB; Q5HZV9; -.
DR   TreeFam; TF105538; -.
DR   PRO; PR:Q5HZV9; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   GO; GO:0005694; C:chromosome; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; ISO:RGD.
DR   GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:RGD.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR   Pfam; PF12799; LRR_4; 2.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00446; LRRcap; 1.
DR   PROSITE; PS51450; LRR; 12.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15435"
FT   CHAIN           2..360
FT                   /note="Protein phosphatase 1 regulatory subunit 7"
FT                   /id="PRO_0000239616"
FT   REPEAT          77..98
FT                   /note="LRR 1"
FT   REPEAT          99..120
FT                   /note="LRR 2"
FT   REPEAT          121..142
FT                   /note="LRR 3"
FT   REPEAT          143..164
FT                   /note="LRR 4"
FT   REPEAT          165..186
FT                   /note="LRR 5"
FT   REPEAT          187..208
FT                   /note="LRR 6"
FT   REPEAT          209..230
FT                   /note="LRR 7"
FT   REPEAT          231..252
FT                   /note="LRR 8"
FT   REPEAT          253..274
FT                   /note="LRR 9"
FT   REPEAT          275..296
FT                   /note="LRR 10"
FT   REPEAT          297..318
FT                   /note="LRR 11"
FT   DOMAIN          331..360
FT                   /note="LRRCT"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15435"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   360 AA;  41297 MW;  1CDA9FB2ACC02400 CRC64;
     MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKHGGGIV ADLSQQSLKD GVERGAEDPE
     EEHELAVDME TISLDRDAED VDLNHYRIGK IEGFEVLKKV KSLCLRQNLI KCIENLDELQ
     SLRELDLYDN QIKKIENLEA LTELEVLDIS FNLLRNIEGI DKLTQLKKLF LVNNKINKIE
     NISTLQQLQM LELGSNRIRA IENIDTLTNL ESLFLGKNKI TKLQNLDALS NLTVLSMQSN
     RLTKIEGLQN LVNLRELYLS HNGIEVIEGL ENNNKLTMLD IASNRIKKIE NISHLTELQE
     FWMNDNLLES WSDLDELKGA RSLETVYLER NPLQKDPQYR RKVMLALPSV RQIDATFVRF
 
 
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