P49593 (PPM1F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase 1F
EC=3.1.3.16

Alternative name(s):
Ca(2+)/calmodulin-dependent protein kinase phosphatase
Short name=CaM-kinase phosphatase
Short name=CaMKPase
Partner of PIX 2
Protein fem-2 homolog
Short name=hFem-2

Gene names

Name:	PPM1F
Synonyms:	KIAA0015, POPX2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Subunit structure	Associates with FEM1B.
Sequence similarities	Belongs to the PP2C family.
Sequence caution	The sequence BAA02803.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis
Coding sequence diversity	Polymorphism
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to drug Inferred from direct assay PubMed 20801214. Source: UniProtKB intrinsic apoptotic signaling pathway Inferred from direct assay Ref.1. Source: UniProtKB negative regulation of peptidyl-serine phosphorylation Inferred from direct assay PubMed 15140879. Source: UniProtKB negative regulation of protein kinase activity by regulation of protein phosphorylation Inferred from direct assay PubMed 15140879. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 20016286. Source: UniProtKB peptidyl-threonine dephosphorylation Inferred from direct assay Ref.1Ref.2PubMed 15140879PubMed 20801214. Source: UniProtKB positive regulation of chemotaxis Inferred from mutant phenotype PubMed 20016286. Source: UniProtKB positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of epithelial cell migration Inferred from mutant phenotype PubMed 20016286. Source: UniProtKB positive regulation of focal adhesion assembly Inferred from mutant phenotype PubMed 20016286. Source: UniProtKB positive regulation of gene expression Inferred from mutant phenotype PubMed 20016286. Source: UniProtKB positive regulation of growth Inferred from mutant phenotype PubMed 20016286. Source: UniProtKB positive regulation of stress fiber assembly Inferred from direct assay Ref.2. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay Ref.1. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara protein complex Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	calmodulin-dependent protein phosphatase activity Inferred from direct assay Ref.1PubMed 15140879. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 454	454	Protein phosphatase 1F		PRO_0000057758
Regions
	Compositional bias	101 – 107	7	Poly-Glu
Sites
	Metal binding	198	1	Manganese 1 By similarity
	Metal binding	198	1	Manganese 2 By similarity
	Metal binding	199	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	360	1	Manganese 2 By similarity
	Metal binding	404	1	Manganese 2 By similarity
Natural variations
	Natural variant	132	1	R → C. Corresponds to variant rs9610645 [ dbSNP | Ensembl ].		VAR_050620
	Natural variant	296	1	R → Q in a colorectal cancer sample; somatic mutation. Ref.7		VAR_036520
	Natural variant	417	1	Q → K in a breast cancer sample; somatic mutation. Ref.7		VAR_036521
	Natural variant	420	1	L → R. Ref.4 Corresponds to variant rs2070507 [ dbSNP | Ensembl ].		VAR_024580
Experimental info
	Sequence conflict	202	1	G → D in AAL15579. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49593 [UniParc]. Last modified November 1, 2002. Version 3. Checksum: 2B49262333D4C9CF	FASTA	454	49,831
	10 20 30 40 50 60 MSSGAPQKSS PMASGAEETP GFLDTLLQDF PALLNPEDPL PWKAPGTVLS QEEVEGELAE 70 80 90 100 110 120 LAMGFLGSRK APPPLAAALA HEAVSQLLQT DLSEFRKLPR EEEEEEEDDD EEEKAPVTLL 130 140 150 160 170 180 DAQSLAQSFF NRLWEVAGQW QKQVPLAARA SQRQWLVSIH AIRNTRRKME DRHVSLPSFN 190 200 210 220 230 240 QLFGLSDPVN RAYFAVFDGH GGVDAARYAA VHVHTNAARQ PELPTDPEGA LREAFRRTDQ 250 260 270 280 290 300 MFLRKAKRER LQSGTTGVCA LIAGATLHVA WLGDSQVILV QQGQVVKLME PHRPERQDEK 310 320 330 340 350 360 ARIEALGGFV SHMDCWRVNG TLAVSRAIGD VFQKPYVSGE ADAASRALTG SEDYLLLACD 370 380 390 400 410 420 GFFDVVPHQE VVGLVQSHLT RQQGSGLRVA EELVAAARER GSHDNITVMV VFLRDPQELL 430 440 450 EGGNQGEGDP QAEGRRQDLP SSLPEPETQA PPRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Caenorhabditis elegans sex-determining protein fem-2 and its human homologue, hFEM-2, are Ca2+/calmodulin-dependent protein kinase phosphatases that promote apoptosis." Tan K.M.L., Chan S.-L., Tan K.O., Yu V.C. J. Biol. Chem. 276:44193-44202(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FEM1B.
[2]	"The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family." Koh C.-G., Tan E.-J., Manser E., Lim L. Curr. Biol. 12:317-321(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1." Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S. DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-420. Tissue: Placenta.
[5]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-296 AND LYS-417.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF305840 mRNA. Translation: AAL15579.1. AF520615 mRNA. Translation: AAM76059.1. D13640 mRNA. Translation: BAA02803.2. Different initiation. AK291628 mRNA. Translation: BAF84317.1.
IPI	IPI00291412.
RefSeq	NP_055449.1. NM_014634.3.
UniGene	Hs.112728.
3D structure databases
ProteinModelPortal	P49593.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49593. 2 interactions.
MINT	MINT-1397077.
STRING	9606.ENSP00000263212.
PTM databases
PhosphoSite	P49593.
Polymorphism databases
DMDM	24638458.
2D gel databases
OGP	P49593.
Proteomic databases
PaxDb	P49593.
PeptideAtlas	P49593.
PRIDE	P49593.
Protocols and materials databases
DNASU	9647.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263212; ENSP00000263212; ENSG00000100034.
GeneID	9647.
KEGG	hsa:9647.
UCSC	uc002zvp.2. human.
Organism-specific databases
CTD	9647.
GeneCards	GC22M022273.
H-InvDB	HIX0027933.
HGNC	HGNC:19388. PPM1F.
HPA	HPA030989. HPA030990.
neXtProt	NX_P49593.
PharmGKB	PA134935566.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0631.
HOGENOM	HOG000232094.
HOVERGEN	HBG053656.
InParanoid	P49593.
KO	K01090.
OMA	GDVFQKP.
OrthoDB	EOG4JM7PR.
PhylomeDB	P49593.
Gene expression databases
ArrayExpress	P49593.
Bgee	P49593.
CleanEx	HS_PPM1F.
Genevestigator	P49593.
GermOnline	ENSG00000100034. Homo sapiens.
Family and domain databases
Gene3D	3.60.40.10. 1 hit.
InterPro	IPR001932. PP2C-like. IPR000222. PP2C_Mn2_Asp60_BS. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PPM1F. human.
GenomeRNAi	9647.
NextBio	36211.

Entry information

Entry name

PPM1F_HUMAN

Accession

Primary (citable) accession number: P49593
Secondary accession number(s): A8K6G3, Q96PM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	November 1, 2002
Last modified:	May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.