IPP2C_HUMAN
ID IPP2C_HUMAN Reviewed; 202 AA.
AC O14990; Q5H958;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein phosphatase inhibitor 2 family member C {ECO:0000305};
DE AltName: Full=PPP1R2 family member B;
DE AltName: Full=Protein phosphatase 1, regulatory subunit 2 pseudogene 9;
DE AltName: Full=Type-1 protein phosphatase inhibitor 4;
DE Short=I-4;
GN Name=PPP1R2C {ECO:0000312|HGNC:HGNC:16324}; Synonyms=PPP1R2P9;
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], AND FUNCTION.
RX PubMed=11076525; DOI=10.1021/bi001326n;
RA Shirato H., Shima H., Sakashita G., Nakano T., Ito M., Lee Y.E.,
RA Kikuchi K.;
RT "Identification and characterization of a novel protein inhibitor of type 1
RT protein phosphatase.";
RL Biochemistry 39:13848-13855(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=24195737; DOI=10.1186/1471-2148-13-242;
RA Korrodi-Gregorio L., Abrantes J., Muller T., Melo-Ferreira J., Marcus K.,
RA da Cruz e Silva O.A., Fardilha M., Esteves P.J.;
RT "Not so pseudo: the evolutionary history of protein phosphatase 1
RT regulatory subunit 2 and related pseudogenes.";
RL BMC Evol. Biol. 13:242-242(2013).
CC -!- FUNCTION: Functions as a protein phosphatase inhibitor. It inhibits
CC activity of the catalytic subunit of PP1 and weakly inhibits the
CC activity of myosin-associated phosphates.
CC {ECO:0000269|PubMed:11076525}.
CC -!- INTERACTION:
CC O14990; P62136: PPP1CA; NbExp=3; IntAct=EBI-12404293, EBI-357253;
CC O14990; P62140: PPP1CB; NbExp=5; IntAct=EBI-12404293, EBI-352350;
CC O14990; P36873: PPP1CC; NbExp=3; IntAct=EBI-12404293, EBI-356283;
CC -!- TISSUE SPECIFICITY: Detected in sperm (at protein level).
CC {ECO:0000269|PubMed:24195737}.
CC -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 2 family.
CC {ECO:0000305}.
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DR EMBL; AB044137; BAB18974.1; -; mRNA.
DR EMBL; Z94277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056673; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS87739.1; -.
DR AlphaFoldDB; O14990; -.
DR SMR; O14990; -.
DR IntAct; O14990; 3.
DR GlyGen; O14990; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14990; -.
DR PhosphoSitePlus; O14990; -.
DR BioMuta; PPP1R2P9; -.
DR MassIVE; O14990; -.
DR PeptideAtlas; O14990; -.
DR PRIDE; O14990; -.
DR ProteomicsDB; 48362; -.
DR Antibodypedia; 78912; 9 antibodies from 8 providers.
DR Ensembl; ENST00000378131.4; ENSP00000490336.1; ENSG00000102055.7.
DR MANE-Select; ENST00000378131.4; ENSP00000490336.1; NM_025210.2; NP_079486.1.
DR GeneCards; PPP1R2C; -.
DR HGNC; HGNC:16324; PPP1R2C.
DR HPA; ENSG00000102055; Tissue enriched (testis).
DR MIM; 301017; gene.
DR neXtProt; NX_O14990; -.
DR OpenTargets; ENSG00000102055; -.
DR VEuPathDB; HostDB:ENSG00000102055; -.
DR GeneTree; ENSGT00940000164483; -.
DR InParanoid; O14990; -.
DR OMA; MKINEPG; -.
DR PhylomeDB; O14990; -.
DR PathwayCommons; O14990; -.
DR SignaLink; O14990; -.
DR Pharos; O14990; Tdark.
DR PRO; PR:O14990; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O14990; protein.
DR Bgee; ENSG00000102055; Expressed in left testis and 53 other tissues.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR InterPro; IPR007062; PPI-2.
DR PANTHER; PTHR12398; PTHR12398; 1.
DR Pfam; PF04979; IPP-2; 1.
PE 1: Evidence at protein level;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..202
FT /note="Protein phosphatase inhibitor 2 family member C"
FT /id="PRO_0000071485"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 12..17
FT /note="Required for binding PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 43..55
FT /note="Required for binding PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 71..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..147
FT /note="Required for binding PPP1CC catalytic center,
FT displacing metal ions and inhibition of PPP1CC catalytic
FT activity"
FT /evidence="ECO:0000250"
FT REGION 162..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 202 AA; 22660 MW; 007955FFAF01A04B CRC64;
MSASTSSHRP IKGILKNKSS SGSSVATSGQ QSGGTIQDVK RKKSQKWDES SILAAHRATY
RDYDLMKANE PGTSYMSVQD NGEDSVRDVE GEDSVRGVEG KEATDASDHS CEVDEQESSE
AYMRKILLHK QEKKRQFEMR RRLHYNEELN IKLARQLMWK ELQSEDNENE ETPQGTNEEK
TAAEESEEAP LTGGLQTQSC DP
