[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1). DOI=10.1016/0167-4781(92)90471-B; PubMed=1311954 [NCBI, ExPASy, EBI, Israel, Japan] Mann D.J., Campbell D.G., McGowan C.H., Cohen P.T.W.; "Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and comparative analysis of amino acid sequences."; Biochim. Biophys. Acta 1130:100-104(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2). DOI=10.1093/emboj/17.16.4744; PubMed=9707433 [NCBI, ExPASy, EBI, Israel, Japan] Takekawa M., Maeda T., Saito H.; "Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways."; EMBO J. 17:4744-4752(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-1). TISSUE=Colon, and Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[5]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). PubMed=9003755 [NCBI, ExPASy, EBI, Israel, Japan] Das A.K., Helps N.R., Cohen P.T.W., Barford D.; "Crystal structure of the protein serine/threonine phosphatase 2C at 2.0-A resolution."; EMBO J. 15:6798-6809(1996).

Comments

FUNCTION: Enzyme with a broad specificity.
CATALYTIC ACTIVITY: A phosphoprotein + H₂O = a protein + phosphate.
COFACTOR: Binds 2 magnesium or manganese ions per subunit.
SUBUNIT: Monomer.
INTERACTION:
P49407:ARRB1; NbExp=1; IntAct=EBI-989143, EBI-743313;
P32121:ARRB2; NbExp=1; IntAct=EBI-989143, EBI-714559;
Q9BS40:LXN; NbExp=1; IntAct=EBI-989143, EBI-1044504;
Q5FBB7:SGOL1; NbExp=1; IntAct=EBI-989143, EBI-989069;
Q562F6:SGOL2; NbExp=1; IntAct=EBI-989143, EBI-989213;

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	Alpha-1
Isoform ID	P35813-1
This is the isoform sequence displayed in this entry.

Name	Alpha-2
Isoform ID	P35813-2
Features which should be applied to build the isoform sequence: VSP_005085, VSP_005086.

SIMILARITY: Belongs to the PP2C family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S87759; AAB21784.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF070670; AAC28354.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026691; AAH26691.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063243; AAH63243.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00020950; -.
IPI00216196; -.

PIR

S22423; S22423.

RefSeq

NP_066283.1; -.
NP_808820.1; -.

UniGene

Hs.130036

3D structure databases

PDB

1A6Q; X-ray; 2.00 A; A=1-382.

[ExPASy / RCSB / EBI]

PDBsum

1A6Q; -.

ModBase

P35813.

Protein-protein interaction databases

IntAct

P35813; 5.

PTM databases

PhosphoSite

P35813; -.

Enzyme and pathway databases

BRENDA

3.1.3.16; 247.

Pathway_Interaction_DB

bmppathway; BMP receptor signaling.
smad2_3pathway; Regulation of cytoplasmic and nuclear SMAD2/3 signaling.

Organism-specific databases

GC14P059782; -.

HIX0011710; -.

HGNC:9275; PPM1A.

606108; gene. [NCBI / EBI]

PharmGKB

PA33603; -.

Gene expression databases

P35813; -.

P35813; -.

HS_PPM1A; -.

ENSG00000100614; Homo sapiens.

Ontologies

GO:0008287;	Cellular component: protein serine/threonine phosphatase complex (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004722;	Molecular function: protein serine/threonine phosphatase activity (inferred from direct assay from UniProtKB).
GO:0004871;	Molecular function: signal transducer activity (inferred from mutant phenotype from UniProtKB).
GO:0043123;	Biological process: positive regulation of I-kappaB kinase/NF-kappaB cascade (inferred from mutant phenotype from UniProtKB).
GO:0045893;	Biological process: positive regulation of transcription, DNA-dependent (inferred from direct assay from UniProtKB).
GO:0030177;	Biological process: positive regulation of Wnt receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0016055;	Biological process: Wnt receptor signaling pathway (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR015655; PP2C.
IPR001932; PP2C-related.
IPR012911; PP2C_C.
IPR000222; PP2C_Mn2_Asp60_BS.
IPR014045; PP2C_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.60.40.10; PP2C-related; 1.
G3DSA:1.10.10.430; PP2C_C; 1.

PANTHER

PTHR13832; PP2C; 1.

Pfam

PF00481; PP2C; 1.
PF07830; PP2C_C; 1.
Pfam graphical view of domain structure.

SMART

SM00331; PP2C_SIG; 1.
SM00332; PP2Cc; 1.
SMART graphical view of domain structure.

PROSITE

PS01032; PP2C; 1.

Proteomic databases

PeptideAtlas

P35813; -.

PRIDE

P35813; -.

Genome annotation databases

Ensembl

ENSG00000100614; Homo sapiens. [Contig view]

GeneID

5494; -.

KEGG

hsa:5494; -.

Phylogenomic databases

HOGENOM

P35813; -.

HOVERGEN

P35813; -.

OMA

P35813; FLQIDEH.

Other

21242; -.

PPM1A; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein; Protein phosphatase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 382`	`382`	`Protein phosphatase 1A.`	`PRO_0000057741`
`METAL`	`60 60`		`Manganese 1.`
`METAL`	`60 60`		`Manganese 2.`
`METAL`	`61 61`		`Manganese 1; via carbonyl oxygen.`
`METAL`	`239 239`		`Manganese 2.`
`METAL`	`282 282`		`Manganese 2.`
`MOD_RES`	`377 377`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`318 324`		`EIIKKQG -> GGSFNKK (in isoform Alpha-2).`	`VSP_005085`
`VAR_SEQ`	`325 382`		`Missing (in isoform Alpha-2).`	`VSP_005086`
`STRAND`	`9 19`	`11`
`STRAND`	`22 31`	`10`
`STRAND`	`33 35`	`3`
`STRAND`	`38 46`	`9`
`TURN`	`47 49`	`3`
`STRAND`	`50 63`	`14`
`HELIX`	`66 80`	`15`
`HELIX`	`83 86`	`4`
`STRAND`	`88 91`	`4`
`HELIX`	`94 118`	`25`
`STRAND`	`129 134`	`6`
`STRAND`	`136 146`	`11`
`STRAND`	`148 153`	`6`
`STRAND`	`156 160`	`5`
`HELIX`	`169 177`	`9`
`TURN`	`188 190`	`3`
`HELIX`	`200 202`	`3`
`HELIX`	`210 212`	`3`
`STRAND`	`213 216`	`4`
`STRAND`	`220 225`	`6`
`TURN`	`228 230`	`3`
`STRAND`	`231 237`	`7`
`HELIX`	`239 242`	`4`
`HELIX`	`247 258`	`12`
`HELIX`	`264 277`	`14`
`STRAND`	`284 290`	`7`
`HELIX`	`299 319`	`21`
`HELIX`	`330 339`	`10`
`TURN`	`347 349`	`3`
`HELIX`	`350 354`	`5`
`HELIX`	`355 365`	`11`

Sequence information

Length: 382 AA [This is the length of the unprocessed precursor]

Molecular weight: 42448 Da [This is the MW of the unprocessed precursor]

CRC64: D48EF508B4A76687 [This is a checksum on the sequence]

        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

P35813 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools