Full text data of PPM1F
PPM1F
(KIAA0015, POPX2)
[Confidence: low (only semi-automatic identification from reviews)]
Protein phosphatase 1F; 3.1.3.16 (Ca(2+)/calmodulin-dependent protein kinase phosphatase; CaM-kinase phosphatase; CaMKPase; Partner of PIX 2; Protein fem-2 homolog; hFem-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein phosphatase 1F; 3.1.3.16 (Ca(2+)/calmodulin-dependent protein kinase phosphatase; CaM-kinase phosphatase; CaMKPase; Partner of PIX 2; Protein fem-2 homolog; hFem-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P49593
ID PPM1F_HUMAN Reviewed; 454 AA.
AC P49593; A8K6G3; Q96PM2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-2002, sequence version 3.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Protein phosphatase 1F;
DE EC=3.1.3.16;
DE AltName: Full=Ca(2+)/calmodulin-dependent protein kinase phosphatase;
DE Short=CaM-kinase phosphatase;
DE Short=CaMKPase;
DE AltName: Full=Partner of PIX 2;
DE AltName: Full=Protein fem-2 homolog;
DE Short=hFem-2;
GN Name=PPM1F; Synonyms=KIAA0015, POPX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH FEM1B.
RX PubMed=11559703; DOI=10.1074/jbc.M105880200;
RA Tan K.M.L., Chan S.-L., Tan K.O., Yu V.C.;
RT "The Caenorhabditis elegans sex-determining protein fem-2 and its
RT human homologue, hFEM-2, are Ca2+/calmodulin-dependent protein kinase
RT phosphatases that promote apoptosis.";
RL J. Biol. Chem. 276:44193-44202(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11864573; DOI=10.1016/S0960-9822(02)00652-8;
RA Koh C.-G., Tan E.-J., Manser E., Lim L.;
RT "The p21-activated kinase PAK is negatively regulated by POPX1 and
RT POPX2, a pair of serine/threonine phosphatases of the PP2C family.";
RL Curr. Biol. 12:317-321(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
RA Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I.
RT The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
RT analysis of randomly sampled cDNA clones from human immature myeloid
RT cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-420.
RC TISSUE=Placenta;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP IDENTIFICATION BY 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
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.,
RA Buerckstuemmer T., 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 [7]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-296 AND LYS-417.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Dephosphorylates and concomitantly deactivates CaM-
CC kinase II activated upon autophosphorylation, and CaM-kinases IV
CC and I activated upon phosphorylation by CaM-kinase kinase.
CC Promotes apoptosis.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- SUBUNIT: Associates with FEM1B.
CC -!- INTERACTION:
CC Q8C078:Camkk2 (xeno); NbExp=3; IntAct=EBI-719945, EBI-937199;
CC O60610:DIAPH1; NbExp=3; IntAct=EBI-719945, EBI-3959709;
CC Q9UK73:FEM1B; NbExp=2; IntAct=EBI-719945, EBI-310482;
CC -!- SIMILARITY: Belongs to the PP2C family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02803.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF305840; AAL15579.1; -; mRNA.
DR EMBL; AF520615; AAM76059.1; -; mRNA.
DR EMBL; D13640; BAA02803.2; ALT_INIT; mRNA.
DR EMBL; AK291628; BAF84317.1; -; mRNA.
DR RefSeq; NP_055449.1; NM_014634.3.
DR UniGene; Hs.112728; -.
DR ProteinModelPortal; P49593; -.
DR SMR; P49593; 84-445.
DR IntAct; P49593; 10.
DR MINT; MINT-1397077; -.
DR STRING; 9606.ENSP00000263212; -.
DR PhosphoSite; P49593; -.
DR DMDM; 24638458; -.
DR OGP; P49593; -.
DR PaxDb; P49593; -.
DR PeptideAtlas; P49593; -.
DR PRIDE; P49593; -.
DR DNASU; 9647; -.
DR Ensembl; ENST00000263212; ENSP00000263212; ENSG00000100034.
DR GeneID; 9647; -.
DR KEGG; hsa:9647; -.
DR UCSC; uc002zvp.2; human.
DR CTD; 9647; -.
DR GeneCards; GC22M022273; -.
DR H-InvDB; HIX0027933; -.
DR HGNC; HGNC:19388; PPM1F.
DR HPA; HPA030989; -.
DR HPA; HPA030990; -.
DR neXtProt; NX_P49593; -.
DR PharmGKB; PA134935566; -.
DR eggNOG; COG0631; -.
DR HOGENOM; HOG000232094; -.
DR HOVERGEN; HBG053656; -.
DR InParanoid; P49593; -.
DR KO; K17502; -.
DR OMA; GDVFQKP; -.
DR OrthoDB; EOG7D2FDH; -.
DR PhylomeDB; P49593; -.
DR ChiTaRS; PPM1F; human.
DR GeneWiki; PPM1F; -.
DR GenomeRNAi; 9647; -.
DR NextBio; 36211; -.
DR PRO; PR:P49593; -.
DR ArrayExpress; P49593; -.
DR Bgee; P49593; -.
DR CleanEx; HS_PPM1F; -.
DR Genevestigator; P49593; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045927; P:positive regulation of growth; IMP:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR001932; PP2C-like_dom.
DR InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR InterPro; IPR015655; Protein_Pase_2C.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PP2C; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Complete proteome; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Polymorphism; Protein phosphatase; Reference proteome.
FT CHAIN 1 454 Protein phosphatase 1F.
FT /FTId=PRO_0000057758.
FT COMPBIAS 101 107 Poly-Glu.
FT METAL 198 198 Manganese 1 (By similarity).
FT METAL 198 198 Manganese 2 (By similarity).
FT METAL 199 199 Manganese 1; via carbonyl oxygen (By
FT similarity).
FT METAL 360 360 Manganese 2 (By similarity).
FT METAL 404 404 Manganese 2 (By similarity).
FT VARIANT 132 132 R -> C (in dbSNP:rs9610645).
FT /FTId=VAR_050620.
FT VARIANT 296 296 R -> Q (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036520.
FT VARIANT 417 417 Q -> K (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036521.
FT VARIANT 420 420 L -> R (in dbSNP:rs2070507).
FT /FTId=VAR_024580.
FT CONFLICT 202 202 G -> D (in Ref. 1; AAL15579).
SQ SEQUENCE 454 AA; 49831 MW; 2B49262333D4C9CF CRC64;
MSSGAPQKSS PMASGAEETP GFLDTLLQDF PALLNPEDPL PWKAPGTVLS QEEVEGELAE
LAMGFLGSRK APPPLAAALA HEAVSQLLQT DLSEFRKLPR EEEEEEEDDD EEEKAPVTLL
DAQSLAQSFF NRLWEVAGQW QKQVPLAARA SQRQWLVSIH AIRNTRRKME DRHVSLPSFN
QLFGLSDPVN RAYFAVFDGH GGVDAARYAA VHVHTNAARQ PELPTDPEGA LREAFRRTDQ
MFLRKAKRER LQSGTTGVCA LIAGATLHVA WLGDSQVILV QQGQVVKLME PHRPERQDEK
ARIEALGGFV SHMDCWRVNG TLAVSRAIGD VFQKPYVSGE ADAASRALTG SEDYLLLACD
GFFDVVPHQE VVGLVQSHLT RQQGSGLRVA EELVAAARER GSHDNITVMV VFLRDPQELL
EGGNQGEGDP QAEGRRQDLP SSLPEPETQA PPRS
//
ID PPM1F_HUMAN Reviewed; 454 AA.
AC P49593; A8K6G3; Q96PM2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-2002, sequence version 3.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Protein phosphatase 1F;
DE EC=3.1.3.16;
DE AltName: Full=Ca(2+)/calmodulin-dependent protein kinase phosphatase;
DE Short=CaM-kinase phosphatase;
DE Short=CaMKPase;
DE AltName: Full=Partner of PIX 2;
DE AltName: Full=Protein fem-2 homolog;
DE Short=hFem-2;
GN Name=PPM1F; Synonyms=KIAA0015, POPX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH FEM1B.
RX PubMed=11559703; DOI=10.1074/jbc.M105880200;
RA Tan K.M.L., Chan S.-L., Tan K.O., Yu V.C.;
RT "The Caenorhabditis elegans sex-determining protein fem-2 and its
RT human homologue, hFEM-2, are Ca2+/calmodulin-dependent protein kinase
RT phosphatases that promote apoptosis.";
RL J. Biol. Chem. 276:44193-44202(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11864573; DOI=10.1016/S0960-9822(02)00652-8;
RA Koh C.-G., Tan E.-J., Manser E., Lim L.;
RT "The p21-activated kinase PAK is negatively regulated by POPX1 and
RT POPX2, a pair of serine/threonine phosphatases of the PP2C family.";
RL Curr. Biol. 12:317-321(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
RA Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I.
RT The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
RT analysis of randomly sampled cDNA clones from human immature myeloid
RT cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-420.
RC TISSUE=Placenta;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP IDENTIFICATION BY 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
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.,
RA Buerckstuemmer T., 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 [7]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-296 AND LYS-417.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Dephosphorylates and concomitantly deactivates CaM-
CC kinase II activated upon autophosphorylation, and CaM-kinases IV
CC and I activated upon phosphorylation by CaM-kinase kinase.
CC Promotes apoptosis.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- SUBUNIT: Associates with FEM1B.
CC -!- INTERACTION:
CC Q8C078:Camkk2 (xeno); NbExp=3; IntAct=EBI-719945, EBI-937199;
CC O60610:DIAPH1; NbExp=3; IntAct=EBI-719945, EBI-3959709;
CC Q9UK73:FEM1B; NbExp=2; IntAct=EBI-719945, EBI-310482;
CC -!- SIMILARITY: Belongs to the PP2C family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02803.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF305840; AAL15579.1; -; mRNA.
DR EMBL; AF520615; AAM76059.1; -; mRNA.
DR EMBL; D13640; BAA02803.2; ALT_INIT; mRNA.
DR EMBL; AK291628; BAF84317.1; -; mRNA.
DR RefSeq; NP_055449.1; NM_014634.3.
DR UniGene; Hs.112728; -.
DR ProteinModelPortal; P49593; -.
DR SMR; P49593; 84-445.
DR IntAct; P49593; 10.
DR MINT; MINT-1397077; -.
DR STRING; 9606.ENSP00000263212; -.
DR PhosphoSite; P49593; -.
DR DMDM; 24638458; -.
DR OGP; P49593; -.
DR PaxDb; P49593; -.
DR PeptideAtlas; P49593; -.
DR PRIDE; P49593; -.
DR DNASU; 9647; -.
DR Ensembl; ENST00000263212; ENSP00000263212; ENSG00000100034.
DR GeneID; 9647; -.
DR KEGG; hsa:9647; -.
DR UCSC; uc002zvp.2; human.
DR CTD; 9647; -.
DR GeneCards; GC22M022273; -.
DR H-InvDB; HIX0027933; -.
DR HGNC; HGNC:19388; PPM1F.
DR HPA; HPA030989; -.
DR HPA; HPA030990; -.
DR neXtProt; NX_P49593; -.
DR PharmGKB; PA134935566; -.
DR eggNOG; COG0631; -.
DR HOGENOM; HOG000232094; -.
DR HOVERGEN; HBG053656; -.
DR InParanoid; P49593; -.
DR KO; K17502; -.
DR OMA; GDVFQKP; -.
DR OrthoDB; EOG7D2FDH; -.
DR PhylomeDB; P49593; -.
DR ChiTaRS; PPM1F; human.
DR GeneWiki; PPM1F; -.
DR GenomeRNAi; 9647; -.
DR NextBio; 36211; -.
DR PRO; PR:P49593; -.
DR ArrayExpress; P49593; -.
DR Bgee; P49593; -.
DR CleanEx; HS_PPM1F; -.
DR Genevestigator; P49593; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045927; P:positive regulation of growth; IMP:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR001932; PP2C-like_dom.
DR InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR InterPro; IPR015655; Protein_Pase_2C.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PP2C; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Complete proteome; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Polymorphism; Protein phosphatase; Reference proteome.
FT CHAIN 1 454 Protein phosphatase 1F.
FT /FTId=PRO_0000057758.
FT COMPBIAS 101 107 Poly-Glu.
FT METAL 198 198 Manganese 1 (By similarity).
FT METAL 198 198 Manganese 2 (By similarity).
FT METAL 199 199 Manganese 1; via carbonyl oxygen (By
FT similarity).
FT METAL 360 360 Manganese 2 (By similarity).
FT METAL 404 404 Manganese 2 (By similarity).
FT VARIANT 132 132 R -> C (in dbSNP:rs9610645).
FT /FTId=VAR_050620.
FT VARIANT 296 296 R -> Q (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036520.
FT VARIANT 417 417 Q -> K (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036521.
FT VARIANT 420 420 L -> R (in dbSNP:rs2070507).
FT /FTId=VAR_024580.
FT CONFLICT 202 202 G -> D (in Ref. 1; AAL15579).
SQ SEQUENCE 454 AA; 49831 MW; 2B49262333D4C9CF CRC64;
MSSGAPQKSS PMASGAEETP GFLDTLLQDF PALLNPEDPL PWKAPGTVLS QEEVEGELAE
LAMGFLGSRK APPPLAAALA HEAVSQLLQT DLSEFRKLPR EEEEEEEDDD EEEKAPVTLL
DAQSLAQSFF NRLWEVAGQW QKQVPLAARA SQRQWLVSIH AIRNTRRKME DRHVSLPSFN
QLFGLSDPVN RAYFAVFDGH GGVDAARYAA VHVHTNAARQ PELPTDPEGA LREAFRRTDQ
MFLRKAKRER LQSGTTGVCA LIAGATLHVA WLGDSQVILV QQGQVVKLME PHRPERQDEK
ARIEALGGFV SHMDCWRVNG TLAVSRAIGD VFQKPYVSGE ADAASRALTG SEDYLLLACD
GFFDVVPHQE VVGLVQSHLT RQQGSGLRVA EELVAAARER GSHDNITVMV VFLRDPQELL
EGGNQGEGDP QAEGRRQDLP SSLPEPETQA PPRS
//