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P35813 (PPM1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase 1A

EC=3.1.3.16
Alternative name(s):
Protein phosphatase 2C isoform alpha
Short name=PP2C-alpha
Protein phosphatase IA
Gene names
Name:PPM1A
Synonyms:PPPM1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. Ref.8 Ref.9

Catalytic activity

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

Cofactor

Binds 2 magnesium or manganese ions per subunit.

Subunit structure

Monomer. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling. Interacts with the phosphorylated form of IKBKB/IKKB. Ref.8 Ref.9

Subcellular location

Nucleus. Cytoplasmcytosol. Membrane By similarity. Note: Weakly associates at the membrane and N-myristoylation mediates the membrane localization By similarity. Ref.8 Ref.13

Post-translational modification

N-myristoylation is essential for the recognition of its substrates for dephosphorylation By similarity.

Sequence similarities

Belongs to the PP2C family.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal protein myristoylation

Inferred from sequence or structural similarity. Source: UniProtKB

Wnt signaling pathway

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

cell cycle arrest

Traceable author statement. Source: Reactome

dephosphorylation

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.9. Source: UniProtKB

negative regulation of NF-kappaB import into nucleus

Inferred from mutant phenotype Ref.9. Source: UniProtKB

negative regulation of SMAD protein complex assembly

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

peptidyl-threonine dephosphorylation

Inferred from direct assay PubMed 11559703PubMed 20801214. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

positive regulation of Wnt signaling pathway

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

protein dephosphorylation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

voltage-gated calcium channel complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionR-SMAD binding

Inferred from physical interaction Ref.8. Source: UniProtKB

calmodulin-dependent protein phosphatase activity

Inferred from direct assay PubMed 11559703. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

manganese ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.8Ref.9. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from direct assay PubMed 10644691PubMed 11559703PubMed 20801214. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha-1 (identifier: P35813-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Alpha-2 (identifier: P35813-2)

The sequence of this isoform differs from the canonical sequence as follows:
     318-324: EIIKKQG → GGSFNKK
     325-382: Missing.
Isoform 3 (identifier: P35813-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MFCSGRKWVAEATICTKLMKREKRRMGKRRAKKAKREEKKKGGERRRNEKRGNQMKRMCERKKYETDLEDQDIM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 382381Protein phosphatase 1A
PRO_0000057741

Sites

Metal binding601Manganese 1
Metal binding601Manganese 2
Metal binding611Manganese 1; via carbonyl oxygen
Metal binding2391Manganese 2
Metal binding2821Manganese 2

Amino acid modifications

Modified residue3751Phosphoserine Ref.10
Lipidation21N-myristoyl glycine Ref.11

Natural variations

Alternative sequence11M → MFCSGRKWVAEATICTKLMK REKRRMGKRRAKKAKREEKK KGGERRRNEKRGNQMKRMCE RKKYETDLEDQDIM in isoform 3.
VSP_045687
Alternative sequence318 – 3247EIIKKQG → GGSFNKK in isoform Alpha-2.
VSP_005085
Alternative sequence325 – 38258Missing in isoform Alpha-2.
VSP_005086

Experimental info

Mutagenesis2391D → N: No effect on binding SMAD2. Ref.8
Sequence conflict3421I → T in AK097843. Ref.3
Isoform 3:
Sequence conflict541Q → R in AK097843. Ref.3

Secondary structure

......................................................... 382
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: D48EF508B4A76687

FASTA38242,448
        10         20         30         40         50         60 
MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL ESWSFFAVYD 

        70         80         90        100        110        120 
GHAGSQVAKY CCEHLLDHIT NNQDFKGSAG APSVENVKNG IRTGFLEIDE HMRVMSEKKH 

       130        140        150        160        170        180 
GADRSGSTAV GVLISPQHTY FINCGDSRGL LCRNRKVHFF TQDHKPSNPL EKERIQNAGG 

       190        200        210        220        230        240 
SVMIQRVNGS LAVSRALGDF DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG 

       250        260        270        280        290        300 
IWDVMGNEEL CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPNAPKVSPE 

       310        320        330        340        350        360 
AVKKEAELDK YLECRVEEII KKQGEGVPDL VHVMRTLASE NIPSLPPGGE LASKRNVIEA 

       370        380 
VYNRLNPYKN DDTDSTSTDD MW 

« Hide

Isoform Alpha-2 [UniParc].

Checksum: ED58E203BB26CE00
Show »

FASTA32435,958
Isoform 3 [UniParc].

Checksum: CBC6E3F350D6FDBD
Show »

FASTA45551,366

References

« Hide 'large scale' references
[1]"Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and comparative analysis of amino acid sequences."
Mann D.J., Campbell D.G., McGowan C.H., Cohen P.T.W.
Biochim. Biophys. Acta 1130:100-104(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
[2]"Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways."
Takekawa M., Maeda T., Saito H.
EMBO J. 17:4744-4752(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
[3]"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] (ISOFORM 3).
Tissue: Testis.
[4]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-1).
[5]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM ALPHA-1).
Tissue: Colon and Lung.
[8]"PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling."
Lin X., Duan X., Liang Y.Y., Su Y., Wrighton K.H., Long J., Hu M., Davis C.M., Wang J., Brunicardi F.C., Shi Y., Chen Y.G., Meng A., Feng X.H.
Cell 125:915-928(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMAD2 AND SMAD3, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-239.
[9]"PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation."
Sun W., Yu Y., Dotti G., Shen T., Tan X., Savoldo B., Pass A.K., Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.
Cell. Signal. 21:95-102(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IKBKB.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[12]"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].
[13]"Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Crystal structure of the protein serine/threonine phosphatase 2C at 2.0-A resolution."
Das A.K., Helps N.R., Cohen P.T.W., Barford D.
EMBO J. 15:6798-6809(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S87759 mRNA. Translation: AAB21784.1.
AF070670 mRNA. Translation: AAC28354.1.
AK097843 mRNA. No translation available.
AB451247 mRNA. Translation: BAG70061.1.
AL132778 Genomic DNA. No translation available.
AL157756 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80774.1.
BC026691 mRNA. Translation: AAH26691.1.
BC063243 mRNA. Translation: AAH63243.1.
CCDSCCDS45120.1. [P35813-3]
CCDS9744.1. [P35813-1]
CCDS9745.1. [P35813-2]
PIRS22423.
RefSeqNP_066283.1. NM_021003.4. [P35813-1]
NP_808820.1. NM_177951.2. [P35813-2]
NP_808821.2. NM_177952.2. [P35813-3]
XP_005267834.1. XM_005267777.1. [P35813-1]
XP_005267835.1. XM_005267778.1. [P35813-1]
XP_005267836.1. XM_005267779.1. [P35813-1]
XP_005267837.1. XM_005267780.1. [P35813-1]
XP_005267838.1. XM_005267781.1. [P35813-1]
XP_006720242.1. XM_006720179.1. [P35813-1]
XP_006720243.1. XM_006720180.1. [P35813-1]
UniGeneHs.130036.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6QX-ray2.00A1-382[»]
3FXJX-ray2.50A1-382[»]
3FXKX-ray2.10A1-382[»]
3FXLX-ray2.30A1-382[»]
3FXMX-ray2.50A1-382[»]
3FXOX-ray2.50A1-382[»]
ProteinModelPortalP35813.
SMRP35813. Positions 2-368.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111489. 12 interactions.
IntActP35813. 20 interactions.
MINTMINT-2802996.
STRING9606.ENSP00000327255.

Chemistry

BindingDBP35813.
ChEMBLCHEMBL2437.

PTM databases

PhosphoSiteP35813.

Polymorphism databases

DMDM548442.

Proteomic databases

MaxQBP35813.
PaxDbP35813.
PeptideAtlasP35813.
PRIDEP35813.

Protocols and materials databases

DNASU5494.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325642; ENSP00000327255; ENSG00000100614. [P35813-3]
ENST00000325658; ENSP00000314850; ENSG00000100614. [P35813-2]
ENST00000395076; ENSP00000378514; ENSG00000100614. [P35813-1]
ENST00000529574; ENSP00000432966; ENSG00000100614. [P35813-1]
GeneID5494.
KEGGhsa:5494.
UCSCuc001xex.4. human. [P35813-2]
uc001xey.4. human. [P35813-1]

Organism-specific databases

CTD5494.
GeneCardsGC14P060712.
HGNCHGNC:9275. PPM1A.
HPAHPA029209.
MIM606108. gene.
neXtProtNX_P35813.
PharmGKBPA33603.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000233895.
HOVERGENHBG053647.
InParanoidP35813.
KOK04457.
OMAEVYAIER.
OrthoDBEOG7WMCJH.
PhylomeDBP35813.
TreeFamTF313590.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_71. Gene Expression.
SignaLinkP35813.

Gene expression databases

ArrayExpressP35813.
BgeeP35813.
CleanExHS_PPM1A.
GenevestigatorP35813.

Family and domain databases

Gene3D1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPM1A. human.
EvolutionaryTraceP35813.
GeneWikiPPM1A.
GenomeRNAi5494.
NextBio21242.
PROP35813.
SOURCESearch...

Entry information

Entry namePPM1A_HUMAN
AccessionPrimary (citable) accession number: P35813
Secondary accession number(s): B5BU11, J3KNM0, O75551
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 151 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM