PP14B_HUMAN
ID PP14B_HUMAN Reviewed; 147 AA.
AC Q96C90; Q504S7; Q7KZD7;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 14B;
DE AltName: Full=Phospholipase C-beta-3 neighbouring gene protein;
GN Name=PPP1R14B; Synonyms=PLCB3N, PNG;
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 [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 TISSUE SPECIFICITY.
RX PubMed=8838322; DOI=10.1006/geno.1996.0063;
RA Lagercrantz J., Carson E., Larsson C., Nordenskjoeld M., Weber G.;
RT "Isolation and characterization of a novel gene close to the human
RT phosphoinositide-specific phospholipase C beta 3 gene on chromosomal region
RT 11q13.";
RL Genomics 31:380-384(1996).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; TYR-29 AND SER-32, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Inhibitor of PPP1CA. Has over 50-fold higher inhibitory
CC activity when phosphorylated (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at low levels.
CC {ECO:0000269|PubMed:8838322}.
CC -!- PTM: Phosphorylated primarily on Thr-57 by PKC (in vitro). An unknown
CC Ser is also phosphorylated by PKC (in vitro) (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PP1 inhibitor family. {ECO:0000305}.
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DR EMBL; BT009914; AAP88916.1; -; mRNA.
DR EMBL; BC014522; AAH14522.3; -; mRNA.
DR EMBL; BC094817; AAH94817.1; -; mRNA.
DR CCDS; CCDS31596.1; -.
DR RefSeq; NP_619634.1; NM_138689.2.
DR AlphaFoldDB; Q96C90; -.
DR BioGRID; 117696; 9.
DR IntAct; Q96C90; 5.
DR MINT; Q96C90; -.
DR STRING; 9606.ENSP00000310117; -.
DR GlyGen; Q96C90; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96C90; -.
DR PhosphoSitePlus; Q96C90; -.
DR BioMuta; PPP1R14B; -.
DR DMDM; 55583975; -.
DR EPD; Q96C90; -.
DR jPOST; Q96C90; -.
DR MassIVE; Q96C90; -.
DR MaxQB; Q96C90; -.
DR PaxDb; Q96C90; -.
DR PeptideAtlas; Q96C90; -.
DR PRIDE; Q96C90; -.
DR ProteomicsDB; 76165; -.
DR TopDownProteomics; Q96C90; -.
DR Antibodypedia; 43962; 61 antibodies from 21 providers.
DR DNASU; 26472; -.
DR Ensembl; ENST00000309318.8; ENSP00000310117.3; ENSG00000173457.11.
DR GeneID; 26472; -.
DR KEGG; hsa:26472; -.
DR MANE-Select; ENST00000309318.8; ENSP00000310117.3; NM_138689.3; NP_619634.1.
DR UCSC; uc001nza.4; human.
DR CTD; 26472; -.
DR DisGeNET; 26472; -.
DR GeneCards; PPP1R14B; -.
DR HGNC; HGNC:9057; PPP1R14B.
DR HPA; ENSG00000173457; Low tissue specificity.
DR MIM; 601140; gene.
DR neXtProt; NX_Q96C90; -.
DR OpenTargets; ENSG00000173457; -.
DR PharmGKB; PA33624; -.
DR VEuPathDB; HostDB:ENSG00000173457; -.
DR eggNOG; KOG0824; Eukaryota.
DR GeneTree; ENSGT00950000182985; -.
DR HOGENOM; CLU_114155_1_0_1; -.
DR InParanoid; Q96C90; -.
DR OMA; TQLYDCQ; -.
DR OrthoDB; 1492626at2759; -.
DR PhylomeDB; Q96C90; -.
DR TreeFam; TF105546; -.
DR PathwayCommons; Q96C90; -.
DR SignaLink; Q96C90; -.
DR SIGNOR; Q96C90; -.
DR BioGRID-ORCS; 26472; 119 hits in 1015 CRISPR screens.
DR ChiTaRS; PPP1R14B; human.
DR GeneWiki; PPP1R14B; -.
DR GenomeRNAi; 26472; -.
DR Pharos; Q96C90; Tbio.
DR PRO; PR:Q96C90; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96C90; protein.
DR Bgee; ENSG00000173457; Expressed in cortical plate and 93 other tissues.
DR ExpressionAtlas; Q96C90; baseline and differential.
DR Genevisible; Q96C90; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
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 Acetylation; Coiled coil; Cytoplasm; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..147
FT /note="Protein phosphatase 1 regulatory subunit 14B"
FT /id="PRO_0000071490"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..103
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 29
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62084"
SQ SEQUENCE 147 AA; 15911 MW; 2932A4EA9F312451 CRC64;
MADSGTAGGA ALAAPAPGPG SGGPGPRVYF QSPPGAAGEG PGGADDEGPV RRQGKVTVKY
DRKELRKRLN LEEWILEQLT RLYDCQEEEI PELEIDVDEL LDMESDDARA ARVKELLVDC
YKPTEAFISG LLDKIRGMQK LSTPQKK
