Reviewed, UniProtKB/Swiss-Prot P49593 (PPM1F_HUMAN)

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
      Short name=hFEM-2

Gene names

Name:	PPM1F
Synonyms:	KIAA0015, POPX2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.

Ontologies

Keywords
Biological process	Apoptosis
Coding sequence diversity	Polymorphism
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	protein serine/threonine phosphatase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
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: dbSNP rs9610645.		VAR_050620
	Natural variant	296	1	R → Q in a colorectal cancer sample; somatic mutation. Ref.6		VAR_036520
	Natural variant	417	1	Q → K in a breast cancer sample; somatic mutation. Ref.6		VAR_036521
	Natural variant	420	1	L → R: dbSNP rs2070507. Ref.4		VAR_024580
Experimental info
	Sequence conflict	202	1	G → D in AAL15579. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49593-1 [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: 11559703] [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: 11864573] [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: 7584026] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-420. Tissue: Placenta.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"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: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-296 AND LYS-417.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Hs.112728
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P49593. 2 interactions.
2-D gel databases
OGP	P49593.
Proteomic databases
PeptideAtlas	P49593.
PRIDE	P49593.
Genome annotation databases
Ensembl	ENSG00000100034. Homo sapiens. [Contig view]
GeneID	9647.
KEGG	hsa:9647.
NMPDR	fig|9606.3.peg.21329.
Organism-specific databases
GeneCards	GC22M020598.
H-InvDB	HIX0016282. HIX0027933.
HGNC	HGNC:19388. PPM1F.
PharmGKB	PA134935566.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P49593.
HOVERGEN	P49593.
OMA	P49593. VHAIRNT.
Enzyme and pathway databases
BRENDA	3.1.3.16. 247.
Gene expression databases
ArrayExpress	P49593.
Bgee	P49593.
CleanEx	HS_PPM1F.
GermOnline	ENSG00000100034. Homo sapiens.
Family and domain databases
InterPro	IPR015655. PP2C. IPR001932. PP2C-related. IPR000222. PP2C_Mn2_Asp60_BS. IPR014045. PP2C_N. [Graphical view]
Gene3D	G3DSA:3.60.40.10. PP2C-related. 1 hit.
PANTHER	PTHR13832. PP2C. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)