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P49593 (PPM1F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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 processApoptosis
   Coding sequence diversityPolymorphism
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to drug

Inferred from direct assay PubMed 20801214. Source: UniProtKB

histone dephosphorylation

Inferred from electronic annotation. Source: Ensembl

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

Inferred from direct assay Ref.2. 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-templated

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 cell-substrate adhesion

Inferred from mutant phenotype PubMed 20016286. 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_componentcytosol

Inferred from direct assay Ref.1. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functioncalmodulin-dependent protein phosphatase activity

Inferred from direct assay Ref.1PubMed 15140879. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatase activity

Inferred from direct assay PubMed 15140879. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from direct assay Ref.1Ref.2PubMed 20801214. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Camkk2Q8C0783EBI-719945,EBI-937199From a different organism.
DIAPH1O606103EBI-719945,EBI-3959709
FEM1BQ9UK732EBI-719945,EBI-310482

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Protein phosphatase 1F
PRO_0000057758

Regions

Compositional bias101 – 1077Poly-Glu

Sites

Metal binding1981Manganese 1 By similarity
Metal binding1981Manganese 2 By similarity
Metal binding1991Manganese 1; via carbonyl oxygen By similarity
Metal binding3601Manganese 2 By similarity
Metal binding4041Manganese 2 By similarity

Natural variations

Natural variant1321R → C.
Corresponds to variant rs9610645 [ dbSNP | Ensembl ].
VAR_050620
Natural variant2961R → Q in a colorectal cancer sample; somatic mutation. Ref.7
VAR_036520
Natural variant4171Q → K in a breast cancer sample; somatic mutation. Ref.7
VAR_036521
Natural variant4201L → R. Ref.4
Corresponds to variant rs2070507 [ dbSNP | Ensembl ].
VAR_024580

Experimental info

Sequence conflict2021G → D in AAL15579. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49593 [UniParc].

Last modified November 1, 2002. Version 3.
Checksum: 2B49262333D4C9CF

FASTA45449,831
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_055449.1. NM_014634.3.
UniGeneHs.112728.

3D structure databases

ProteinModelPortalP49593.
SMRP49593. Positions 84-445.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115005. 11 interactions.
IntActP49593. 10 interactions.
MINTMINT-1397077.
STRING9606.ENSP00000263212.

PTM databases

PhosphoSiteP49593.

Polymorphism databases

DMDM24638458.

2D gel databases

OGPP49593.

Proteomic databases

PaxDbP49593.
PeptideAtlasP49593.
PRIDEP49593.

Protocols and materials databases

DNASU9647.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263212; ENSP00000263212; ENSG00000100034.
GeneID9647.
KEGGhsa:9647.
UCSCuc002zvp.2. human.

Organism-specific databases

CTD9647.
GeneCardsGC22M022273.
H-InvDBHIX0027933.
HGNCHGNC:19388. PPM1F.
HPAHPA030989.
HPA030990.
neXtProtNX_P49593.
PharmGKBPA134935566.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000232094.
HOVERGENHBG053656.
InParanoidP49593.
KOK17502.
OMAGDVFQKP.
OrthoDBEOG7D2FDH.
PhylomeDBP49593.
TreeFamTF317617.

Gene expression databases

ArrayExpressP49593.
BgeeP49593.
CleanExHS_PPM1F.
GenevestigatorP49593.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPM1F. human.
GeneWikiPPM1F.
GenomeRNAi9647.
NextBio36211.
PROP49593.

Entry information

Entry namePPM1F_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM