P35813 (PPM1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.8
Catalytic activity	A phosphoprotein + H2O = a protein + 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. Ref.8
Subcellular location	Nucleus Ref.8.
Sequence similarities	Belongs to the PP2C family.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from direct assay PubMed 10644691. Source: BHF-UCL cell cycle arrest Traceable author statement. Source: Reactome insulin receptor signaling pathway Traceable author statement. Source: Reactome 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 cascade Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB positive regulation of Wnt receptor signaling pathway Inferred from direct assay PubMed 10644691. Source: BHF-UCL positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 10644691. Source: BHF-UCL transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	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 signal transducer activity Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	4	EBI-989143,EBI-743313
ARRB2	P32121	3	EBI-989143,EBI-714559

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 382

382

Protein phosphatase 1A

PRO_0000057741

Sites

Metal binding

60

1

Manganese 1

Metal binding

60

1

Manganese 2

Metal binding

61

1

Manganese 1; via carbonyl oxygen

Metal binding

239

1

Manganese 2

Metal binding

282

1

Manganese 2

Amino acid modifications

Modified residue

375

1

Phosphoserine Ref.9

Modified residue

377

1

Phosphoserine By similarity

Lipidation

2

1

N-myristoyl glycine Ref.10

Natural variations

Alternative sequence

1

1

M → MFCSGRKWVAEATICTKLMK REKRRMGKRRAKKAKREEKK KGGERRRNEKRGNQMKRMCE RKKYETDLEDQDIM in isoform 3.

VSP_045687

Alternative sequence

318 – 324

7

EIIKKQG → GGSFNKK in isoform Alpha-2.

VSP_005085

Alternative sequence

325 – 382

58

Missing in isoform Alpha-2.

VSP_005086

Experimental info

Mutagenesis

239

1

D → N: No effect on binding SMAD2. Ref.8

Sequence conflict

342

1

I → T in AK097843. Ref.3

Isoform 3:

Sequence conflict

54

1

Q → R in AK097843. Ref.3

Secondary structure

1

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382

Helix Strand Turn

Details...

Beta strand

9 – 19

11

Beta strand

22 – 31

10

Beta strand

33 – 35

3

Beta strand

38 – 46

9

Turn

47 – 49

3

Beta strand

50 – 63

14

Helix

66 – 80

15

Helix

83 – 86

4

Beta strand

88 – 91

4

Helix

94 – 118

25

Beta strand

129 – 134

6

Beta strand

136 – 146

11

Beta strand

148 – 153

6

Beta strand

156 – 160

5

Helix

169 – 177

9

Turn

188 – 190

3

Helix

200 – 202

3

Helix

210 – 212

3

Beta strand

213 – 216

4

Beta strand

220 – 225

6

Turn

228 – 230

3

Beta strand

231 – 237

7

Helix

239 – 242

4

Helix

247 – 258

12

Helix

264 – 277

14

Beta strand

284 – 290

7

Helix

299 – 319

21

Helix

330 – 339

10

Turn

347 – 349

3

Helix

350 – 354

5

Helix

355 – 365

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: D48EF508B4A76687	FASTA	382	42,448
	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
	Isoform Alpha-2 [UniParc]. Checksum: ED58E203BB26CE00	FASTA	324	35,958
	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 AVKKEAELDK YLECRVEGGS FNKK
	Isoform 3 [UniParc]. Checksum: CBC6E3F350D6FDBD	FASTA	455	51,366
	10 20 30 40 50 60 MFCSGRKWVA EATICTKLMK REKRRMGKRR AKKAKREEKK KGGERRRNEK RGNQMKRMCE 70 80 90 100 110 120 RKKYETDLED QDIMGAFLDK PKMEKHNAQG QGNGLRYGLS SMQGWRVEME DAHTAVIGLP 130 140 150 160 170 180 SGLESWSFFA VYDGHAGSQV AKYCCEHLLD HITNNQDFKG SAGAPSVENV KNGIRTGFLE 190 200 210 220 230 240 IDEHMRVMSE KKHGADRSGS TAVGVLISPQ HTYFINCGDS RGLLCRNRKV HFFTQDHKPS 250 260 270 280 290 300 NPLEKERIQN AGGSVMIQRV NGSLAVSRAL GDFDYKCVHG KGPTEQLVSP EPEVHDIERS 310 320 330 340 350 360 EEDDQFIILA CDGIWDVMGN EELCDFVRSR LEVTDDLEKV CNEVVDTCLY KGSRDNMSVI 370 380 390 400 410 420 LICFPNAPKV SPEAVKKEAE LDKYLECRVE EIIKKQGEGV PDLVHVMRTL ASENIPSLPP 430 440 450 GGELASKRNV IEAVYNRLNP YKNDDTDSTS TDDMW

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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.
[11]	"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].
[12]	"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.

IPI

IPI00020950.
IPI00216196.

PIR

S22423.

RefSeq

NP_066283.1. NM_021003.4.
NP_808820.1. NM_177951.2.
NP_808821.2. NM_177952.2.

UniGene

Hs.130036.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A6Q	X-ray	2.00	A	1-382	[»]
3FXJ	X-ray	2.50	A	1-382	[»]
3FXK	X-ray	2.10	A	1-382	[»]
3FXL	X-ray	2.30	A	1-382	[»]
3FXM	X-ray	2.50	A	1-382	[»]
3FXO	X-ray	2.50	A	1-382	[»]

ProteinModelPortal

P35813.

ModBase

Search...

Protein-protein interaction databases

IntAct

P35813. 9 interactions.

STRING

9606.ENSP00000327255.

PTM databases

PhosphoSite

P35813.

Polymorphism databases

DMDM

548442.

Proteomic databases

PaxDb

P35813.

PeptideAtlas

P35813.

PRIDE

P35813.

Protocols and materials databases

DNASU

5494.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325642; ENSP00000327255; ENSG00000100614.
ENST00000325658; ENSP00000314850; ENSG00000100614.
ENST00000395076; ENSP00000378514; ENSG00000100614.
ENST00000529574; ENSP00000432966; ENSG00000100614.

GeneID

5494.

KEGG

hsa:5494.

UCSC

uc001xew.4. human.
uc001xex.4. human.

Organism-specific databases

CTD

5494.

GeneCards

GC14P060712.

HGNC

HGNC:9275. PPM1A.

HPA

HPA029209.

MIM

606108. gene.

neXtProt

NX_P35813.

PharmGKB

PA33603.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0631.

HOGENOM

HOG000233895.

HOVERGEN

HBG053647.

InParanoid

P35813.

KO

K04457.

OrthoDB

EOG4GMTX1.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_111102. Signal Transduction.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P35813.

Bgee

P35813.

CleanEx

HS_PPM1A.

Genevestigator

P35813.

GermOnline

ENSG00000100614. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.430. 1 hit.
3.60.40.10. 1 hit.

InterPro

IPR001932. PP2C-like.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]

PANTHER

PTHR13832. PTHR13832. 1 hit.

Pfam

PF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]

SMART

SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]

SUPFAM

SSF81606. PP2C-related. 1 hit.
SSF81601. PP2C_C. 1 hit.

PROSITE

PS01032. PP2C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P35813.

ChEMBL

CHEMBL2437.

ChiTaRS

PPM1A. human.

EvolutionaryTrace

P35813.

GenomeRNAi

5494.

NextBio

21242.

SOURCE

Search...

Entry information

Entry name

PPM1A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.