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 24-JAN-2024, entry version 164. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 28. 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; 9606-ENSP00000310117; -. DR PeptideAtlas; Q96C90; -. DR ProteomicsDB; 76165; -. DR Pumba; Q96C90; -. DR TopDownProteomics; Q96C90; -. DR Antibodypedia; 43962; 74 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 AGR; HGNC:9057; -. 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; DMDSDEH; -. DR OrthoDB; 5321897at2759; -. DR PhylomeDB; Q96C90; -. DR TreeFam; TF105546; -. DR PathwayCommons; Q96C90; -. DR SignaLink; Q96C90; -. DR SIGNOR; Q96C90; -. DR BioGRID-ORCS; 26472; 122 hits in 1093 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 95 other cell types or tissues. DR ExpressionAtlas; Q96C90; baseline and differential. 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; CPI-17; 1. DR InterPro; IPR008025; CPI-17. DR InterPro; IPR036658; CPI-17_sf. DR PANTHER; PTHR16188; PROTEIN PHOSPHATASE 1 INHIBITOR POTENTIATED BY PROTEIN KINASE C; 1. DR PANTHER; PTHR16188:SF5; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 14B; 1. DR Pfam; PF05361; PP1_inhibitor; 1. DR SUPFAM; SSF81790; Myosin phosphatase inhibitor 17kDa protein, CPI-17; 1. DR Genevisible; Q96C90; HS. 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 //