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PPR1A_MOUSE
ID   PPR1A_MOUSE             Reviewed;         171 AA.
AC   Q9ERT9;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 1A;
DE   AltName: Full=Protein phosphatase inhibitor 1;
DE            Short=I-1;
DE            Short=IPP-1;
GN   Name=Ppp1r1a;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=10960791; DOI=10.1016/s0925-4773(00)00388-9;
RA   McLaren L., Boyle S., Mason J.O., Bard J.B.L.;
RT   "Expression and genomic characterization of protein phosphatase inhibitor-
RT   1: a novel marker for mesothelium in the mouse.";
RL   Mech. Dev. 96:237-241(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 THR-35; SER-43; SER-46 AND
RP   SER-47, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Lung;
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: Inhibitor of protein-phosphatase 1. This protein may be
CC       important in hormonal control of glycogen metabolism. Hormones that
CC       elevate intracellular cAMP increase I-1 activity in many tissues. I-1
CC       activation may impose cAMP control over proteins that are not directly
CC       phosphorylated by PKA. Following a rise in intracellular calcium, I-1
CC       is inactivated by calcineurin (or PP2B). Does not inhibit type-2
CC       phosphatases.
CC   -!- SUBUNIT: Interacts with PPP1R15A. {ECO:0000250}.
CC   -!- PTM: Phosphorylation of Thr-35 is required for activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF281676; AAG15192.1; -; mRNA.
DR   EMBL; BC025123; AAH25123.1; -; mRNA.
DR   CCDS; CCDS37237.1; -.
DR   RefSeq; NP_067366.1; NM_021391.3.
DR   AlphaFoldDB; Q9ERT9; -.
DR   BioGRID; 208385; 1.
DR   STRING; 10090.ENSMUSP00000023133; -.
DR   iPTMnet; Q9ERT9; -.
DR   PhosphoSitePlus; Q9ERT9; -.
DR   jPOST; Q9ERT9; -.
DR   MaxQB; Q9ERT9; -.
DR   PaxDb; Q9ERT9; -.
DR   PeptideAtlas; Q9ERT9; -.
DR   PRIDE; Q9ERT9; -.
DR   ProteomicsDB; 291721; -.
DR   Antibodypedia; 27544; 87 antibodies from 30 providers.
DR   DNASU; 58200; -.
DR   Ensembl; ENSMUST00000023133; ENSMUSP00000023133; ENSMUSG00000022490.
DR   GeneID; 58200; -.
DR   KEGG; mmu:58200; -.
DR   UCSC; uc007xyj.1; mouse.
DR   CTD; 5502; -.
DR   MGI; MGI:1889595; Ppp1r1a.
DR   VEuPathDB; HostDB:ENSMUSG00000022490; -.
DR   eggNOG; ENOG502S1WG; Eukaryota.
DR   GeneTree; ENSGT00940000161232; -.
DR   HOGENOM; CLU_092269_1_0_1; -.
DR   InParanoid; Q9ERT9; -.
DR   OMA; PKTQERC; -.
DR   OrthoDB; 1571652at2759; -.
DR   PhylomeDB; Q9ERT9; -.
DR   TreeFam; TF332576; -.
DR   BioGRID-ORCS; 58200; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Ppp1r1a; mouse.
DR   PRO; PR:Q9ERT9; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9ERT9; protein.
DR   Bgee; ENSMUSG00000022490; Expressed in right kidney and 213 other tissues.
DR   Genevisible; Q9ERT9; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   InterPro; IPR008466; PPP1R1A/B/C.
DR   PANTHER; PTHR15417; PTHR15417; 1.
DR   Pfam; PF05395; DARPP-32; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW   Protein phosphatase inhibitor; Reference proteome.
FT   CHAIN           1..171
FT                   /note="Protein phosphatase 1 regulatory subunit 1A"
FT                   /id="PRO_0000071478"
FT   REGION          1..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          9..12
FT                   /note="Essential for activity"
FT   REGION          42..54
FT                   /note="Essential for activity"
FT                   /evidence="ECO:0000305"
FT   REGION          143..171
FT                   /note="Interaction with PPP1R15A"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        58..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P01099"
FT   MOD_RES         35
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13522"
SQ   SEQUENCE   171 AA;  18718 MW;  F6981C75CA163F8D CRC64;
     MEPDNSPRKI QFTVPLLEPH LDPEAAEQIR RRRPTPATLV LTSDQSSPEI DEDRIPNSLL
     KSTLSMSPRQ RKKMTRTTPT MKELQTMVEH HLGQQKQGEE PEGATESTGN QESCPPGIPD
     TGSASRPDTP GTAQKSAESN PKTQEQCGVE PRTEDSSAHM LPLDSQGASL V
 
 
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