PP14D_HUMAN
ID PP14D_HUMAN Reviewed; 145 AA.
AC Q9NXH3; Q4V773;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 14D;
DE AltName: Full=Gastrointestinal and brain-specific PP1-inhibitory protein 1;
DE Short=GBPI-1;
GN Name=PPP1R14D; Synonyms=GBPI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION AT THR-58,
RP MUTAGENESIS OF 21-LYS-LYS-22; TRP-25 AND THR-58, AND TISSUE SPECIFICITY.
RX PubMed=12974676; DOI=10.1042/bj20030128;
RA Liu Q.-R., Zhang P.-W., Lin Z., Li Q.-F., Woods A.S., Troncoso J.,
RA Uhl G.R.;
RT "GBPI, a novel gastrointestinal- and brain-specific PP1-inhibitory protein,
RT is activated by PKC and inactivated by PKA.";
RL Biochem. J. 377:171-181(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon mucosa;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
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).
CC -!- FUNCTION: Inhibitor of PPP1CA. Has inhibitory activity only when
CC phosphorylated, creating a molecular switch for regulating the
CC phosphorylation status of PPP1CA substrates and smooth muscle
CC contraction. {ECO:0000269|PubMed:12974676}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in colon, intestine, kidney and brain
CC cortex. {ECO:0000269|PubMed:12974676}.
CC -!- PTM: Phosphorylated on several residues. {ECO:0000269|PubMed:12974676}.
CC -!- SIMILARITY: Belongs to the PP1 inhibitor family. {ECO:0000305}.
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DR EMBL; AY050671; AAL25829.1; -; mRNA.
DR EMBL; AK000258; BAA91037.1; -; mRNA.
DR EMBL; BC096716; AAH96716.1; -; mRNA.
DR EMBL; BC098124; AAH98124.1; -; mRNA.
DR CCDS; CCDS10066.1; -.
DR RefSeq; NP_060196.1; NM_017726.7.
DR AlphaFoldDB; Q9NXH3; -.
DR BioGRID; 120215; 4.
DR STRING; 9606.ENSP00000398342; -.
DR iPTMnet; Q9NXH3; -.
DR PhosphoSitePlus; Q9NXH3; -.
DR BioMuta; PPP1R14D; -.
DR DMDM; 55583999; -.
DR jPOST; Q9NXH3; -.
DR MassIVE; Q9NXH3; -.
DR PaxDb; Q9NXH3; -.
DR PeptideAtlas; Q9NXH3; -.
DR PRIDE; Q9NXH3; -.
DR ProteomicsDB; 83098; -.
DR Antibodypedia; 49878; 65 antibodies from 23 providers.
DR DNASU; 54866; -.
DR Ensembl; ENST00000299174.10; ENSP00000299174.6; ENSG00000166143.10.
DR GeneID; 54866; -.
DR KEGG; hsa:54866; -.
DR MANE-Select; ENST00000299174.10; ENSP00000299174.6; NM_017726.8; NP_060196.1.
DR UCSC; uc001zmy.3; human.
DR CTD; 54866; -.
DR GeneCards; PPP1R14D; -.
DR HGNC; HGNC:14953; PPP1R14D.
DR HPA; ENSG00000166143; Tissue enriched (intestine).
DR MIM; 613256; gene.
DR neXtProt; NX_Q9NXH3; -.
DR OpenTargets; ENSG00000166143; -.
DR PharmGKB; PA33631; -.
DR VEuPathDB; HostDB:ENSG00000166143; -.
DR eggNOG; ENOG502TKY0; Eukaryota.
DR GeneTree; ENSGT00950000182985; -.
DR HOGENOM; CLU_114155_0_0_1; -.
DR InParanoid; Q9NXH3; -.
DR OMA; PDEGQRT; -.
DR PhylomeDB; Q9NXH3; -.
DR PathwayCommons; Q9NXH3; -.
DR BioGRID-ORCS; 54866; 11 hits in 1070 CRISPR screens.
DR GenomeRNAi; 54866; -.
DR Pharos; Q9NXH3; Tbio.
DR PRO; PR:Q9NXH3; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9NXH3; protein.
DR Bgee; ENSG00000166143; Expressed in mucosa of transverse colon and 87 other tissues.
DR ExpressionAtlas; Q9NXH3; baseline and differential.
DR Genevisible; Q9NXH3; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:UniProtKB.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:1905184; P:positive regulation of protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0042325; P:regulation of phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.150.220; -; 1.
DR InterPro; IPR008025; CPI-17.
DR InterPro; IPR036658; CPI-17_sf.
DR PANTHER; PTHR16188; PTHR16188; 1.
DR Pfam; PF05361; PP1_inhibitor; 1.
DR SUPFAM; SSF81790; SSF81790; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Protein phosphatase inhibitor;
KW Reference proteome.
FT CHAIN 1..145
FT /note="Protein phosphatase 1 regulatory subunit 14D"
FT /id="PRO_0000071497"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..25
FT /note="Interaction with protein phosphatase 1"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:12974676"
FT MUTAGEN 21..22
FT /note="KK->EE: Reduces inhibitory activity by 57%."
FT /evidence="ECO:0000269|PubMed:12974676"
FT MUTAGEN 25
FT /note="W->A: Reduces inhibitory activity by 13%."
FT /evidence="ECO:0000269|PubMed:12974676"
FT MUTAGEN 58
FT /note="T->E: Reduces inhibitory activity by 16%. Reduces
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:12974676"
SQ SEQUENCE 145 AA; 16508 MW; 012899C72C5760A4 CRC64;
MLSSSPASCT SPSPDGENPC KKVHWASGRR RTSSTDSESK SHPDSSKIPR SRRPSRLTVK
YDRGQLQRWL EMEQWVDAQV QELFQDQATP SEPEIDLEAL MDLSTEEQKT QLEAILGNCP
RPTEAFISEL LSQLKKLRRL SRPQK
