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PPR1B_PIG
ID   PPR1B_PIG               Reviewed;         137 AA.
AC   Q29277;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 1B;
DE   AltName: Full=DARPP-32;
DE   AltName: Full=Dopamine- and cAMP-regulated neuronal phosphoprotein;
DE   Flags: Fragment;
GN   Name=PPP1R1B;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RX   PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA library:
RT   analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
CC   -!- FUNCTION: Inhibitor of protein-phosphatase 1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Phosphorylation of Thr-33 is required for activity. {ECO:0000250}.
CC   -!- PTM: Dopamine- and cyclic AMP-regulated neuronal phosphoprotein.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; F14627; CAA23161.1; -; mRNA.
DR   STRING; 9823.ENSSSCP00000018546; -.
DR   PaxDb; Q29277; -.
DR   PeptideAtlas; Q29277; -.
DR   eggNOG; ENOG502S19Z; Eukaryota.
DR   InParanoid; Q29277; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   InterPro; IPR015670; DARPP-32.
DR   InterPro; IPR008466; PPP1R1A/B/C.
DR   PANTHER; PTHR15417; PTHR15417; 1.
DR   PANTHER; PTHR15417:SF2; PTHR15417:SF2; 1.
DR   Pfam; PF05395; DARPP-32; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Protein phosphatase inhibitor;
KW   Reference proteome.
FT   CHAIN           <1..>137
FT                   /note="Protein phosphatase 1 regulatory subunit 1B"
FT                   /id="PRO_0000071475"
FT   REGION          1..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..137
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         33
FT                   /note="Phosphothreonine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P07516"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60829"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60829"
FT   MOD_RES         74
FT                   /note="Phosphothreonine; by CDK5"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UD71"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60829"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6J4I0"
FT   NON_TER         1
FT   NON_TER         137
SQ   SEQUENCE   137 AA;  15802 MW;  43EE03018D41F52D CRC64;
     DPKDRKKIQF SXPAPPSQLD PRQLEMIRRR RPTPAMLFRL XEHSSPEEEA SPHQRAAGEG
     HHLKSKRPNP CAYTPPSLKA VQRIAESHLQ SISNLGENQA SEEEDELGEL RELGYPREEE
     EEEEEDDEEE EEEEDSQ
 
 
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