Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O15355 (PPM1G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1G

EC=3.1.3.16
Alternative name(s):
Protein phosphatase 1C
Protein phosphatase 2C isoform gamma
Short name=PP2C-gamma
Protein phosphatase magnesium-dependent 1 gamma
Gene names
Name:PPM1G
Synonyms:PPM1C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Subcellular location

Cytoplasm Potential.

Tissue specificity

Widely expressed. Most abundant in testis, skeletal muscle, and heart.

Sequence similarities

Belongs to the PP2C family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

tatP046083EBI-725702,EBI-6164389From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546Protein phosphatase 1G
PRO_0000057750

Regions

Compositional bias258 – 32669Asp/Glu-rich (acidic)
Compositional bias266 – 2727Poly-Glu
Compositional bias306 – 3116Poly-Glu
Compositional bias539 – 5446Poly-Lys

Sites

Metal binding601Manganese 1 By similarity
Metal binding601Manganese 2 By similarity
Metal binding611Manganese 1; via carbonyl oxygen By similarity
Metal binding4411Manganese 2 By similarity
Metal binding4961Manganese 2 By similarity

Amino acid modifications

Modified residue1831Phosphoserine Ref.3
Modified residue3831N6-acetyllysine Ref.6
Modified residue5271Phosphoserine Ref.9

Sequences

Sequence LengthMass (Da)Tools
O15355 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 084C16F8252330D9

FASTA54659,272
        10         20         30         40         50         60 
MGAYLSQPNT VKCSGDGVGA PRLPLPYGFS AMQGWRVSME DAHNCIPELD SETAMFSVYD 

        70         80         90        100        110        120 
GHGGEEVALY CAKYLPDIIK DQKAYKEGKL QKALEDAFLA IDAKLTTEEV IKELAQIAGR 

       130        140        150        160        170        180 
PTEDEDEKEK VADEDDVDNE EAALLHEEAT MTIEELLTRY GQNCHKGPPH SKSGGGTGEE 

       190        200        210        220        230        240 
PGSQGLNGEA GPEDSTRETP SQENGPTAKA YTGFSSNSER GTEAGQVGEP GIPTGEAGPS 

       250        260        270        280        290        300 
CSSASDKLPR VAKSKFFEDS EDESDEAEEE EEDSEECSEE EDGYSSEEAE NEEDEDDTEE 

       310        320        330        340        350        360 
AEEDDEEEEE EMMVPGMEGK EEPGSDSGTT AVVALIRGKQ LIVANAGDSR CVVSEAGKAL 

       370        380        390        400        410        420 
DMSYDHKPED EVELARIKNA GGKVTMDGRV NGGLNLSRAI GDHFYKRNKN LPPEEQMISA 

       430        440        450        460        470        480 
LPDIKVLTLT DDHEFMVIAC DGIWNVMSSQ EVVDFIQSKI SQRDENGELR LLSSIVEELL 

       490        500        510        520        530        540 
DQCLAPDTSG DGTGCDNMTC IIICFKPRNT AELQPESGKR KLEEVLSTEG AEENGNSDKK 


KKAKRD 

« Hide

References

« Hide 'large scale' references
[1]"PP2C gamma: a human protein phosphatase with a unique acidic domain."
Travis S.M., Welsh M.J.
FEBS Lett. 412:415-419(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Skin.
[3]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[4]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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.
[8]"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].
[9]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13936 mRNA. Translation: CAA74245.1.
BC022061 mRNA. Translation: AAH22061.1.
BC000057 mRNA. Translation: AAH00057.1.
CCDSCCDS1752.1.
RefSeqNP_817092.1. NM_177983.2.
UniGeneHs.643951.

3D structure databases

ProteinModelPortalO15355.
SMRO15355. Positions 1-126, 274-506.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111491. 55 interactions.
DIPDIP-29404N.
IntActO15355. 14 interactions.
MINTMINT-5003792.
STRING9606.ENSP00000264714.

PTM databases

PhosphoSiteO15355.

Proteomic databases

MaxQBO15355.
PaxDbO15355.
PeptideAtlasO15355.
PRIDEO15355.

Protocols and materials databases

DNASU5496.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344034; ENSP00000342778; ENSG00000115241.
ENST00000350803; ENSP00000264714; ENSG00000115241.
GeneID5496.
KEGGhsa:5496.
UCSCuc002rkl.4. human.

Organism-specific databases

CTD5496.
GeneCardsGC02M027604.
HGNCHGNC:9278. PPM1G.
HPAHPA035530.
HPA035531.
MIM605119. gene.
neXtProtNX_O15355.
PharmGKBPA33606.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000233896.
HOVERGENHBG053647.
InParanoidO15355.
KOK17499.
OMAMISAMPD.
OrthoDBEOG7034GD.
PhylomeDBO15355.
TreeFamTF354280.

Gene expression databases

ArrayExpressO15355.
BgeeO15355.
CleanExHS_PPM1G.
GenevestigatorO15355.

Family and domain databases

Gene3D3.60.40.10. 2 hits.
InterProIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 2 hits.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 2 hits.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPM1G. human.
GeneWikiPPM1G.
GenomeRNAi5496.
NextBio21262.
PROO15355.
SOURCESearch...

Entry information

Entry namePPM1G_HUMAN
AccessionPrimary (citable) accession number: O15355
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 138 of the entry and version 1 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM