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P49593 (PPM1F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 114. 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·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)
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 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

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.6
VAR_036520
Natural variant4171Q → K in a breast cancer sample; somatic mutation. Ref.6
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: 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. 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-420.
Tissue: Placenta.
[5]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. 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: 16959974] [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.
IPIIPI00291412.
RefSeqNP_055449.1. NM_014634.3.
UniGeneHs.112728.

3D structure databases

ProteinModelPortalP49593.
SMRP49593. Positions 156-415.
ModBaseSearch...

Protein-protein interaction databases

IntActP49593. 2 interactions.
MINTMINT-1397077.
STRINGP49593.

Polymorphism databases

DMDM24638458.

2D gel databases

OGPP49593.

Proteomic databases

PeptideAtlasP49593.
PRIDEP49593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263212; ENSP00000263212; ENSG00000100034.
ENST00000406981; ENSP00000384715; ENSG00000100034.
GeneID9647.
KEGGhsa:9647.
NMPDRfig|9606.3.peg.21329.
UCSCuc002zvp.1. human.

Organism-specific databases

CTD9647.
GeneCardsGC22M022273.
H-InvDBHIX0016282.
HGNCHGNC:19388. PPM1F.
HPAHPA030989.
HPA030990.
neXtProtNX_P49593.
PharmGKBPA134935566.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG715807.
HOVERGENHBG053656.
InParanoidP49593.
OMAYMDCWRV.
OrthoDBEOG4JM7PR.
PhylomeDBP49593.

Gene expression databases

BgeeP49593.
CleanExHS_PPM1F.
GenevestigatorP49593.
GermOnlineENSG00000100034. Homo sapiens.

Family and domain databases

InterProIPR001932. PP2C-like.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
Gene3DG3DSA:3.60.40.10. PP2C-related. 1 hit.
KOK01090.
PANTHERPTHR13832. PP2C. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. PP2C-related. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio36211.

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: January 25, 2012
This is version 114 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.

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