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Protein

Protein phosphatase 1A

Gene

PPM1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Mg2+, Mn2+Note: Binds 2 magnesium or manganese ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Manganese 1
Metal bindingi60 – 601Manganese 2
Metal bindingi61 – 611Manganese 1; via carbonyl oxygen
Metal bindingi239 – 2391Manganese 2
Metal bindingi282 – 2821Manganese 2

GO - Molecular functioni

  • calmodulin-dependent protein phosphatase activity Source: UniProtKB
  • magnesium ion binding Source: InterPro
  • manganese ion binding Source: InterPro
  • protein serine/threonine phosphatase activity Source: UniProtKB
  • R-SMAD binding Source: UniProtKB
  • signal transducer activity Source: UniProtKB

GO - Biological processi

  • cell cycle arrest Source: Reactome
  • dephosphorylation Source: BHF-UCL
  • gene expression Source: Reactome
  • insulin receptor signaling pathway Source: Reactome
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of NF-kappaB import into nucleus Source: UniProtKB
  • negative regulation of SMAD protein complex assembly Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • N-terminal protein myristoylation Source: UniProtKB
  • peptidyl-threonine dephosphorylation Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of Wnt signaling pathway Source: BHF-UCL
  • protein dephosphorylation Source: UniProtKB
  • transcription, DNA-templated Source: Reactome
  • transcription initiation from RNA polymerase II promoter Source: Reactome
  • transforming growth factor beta receptor signaling pathway Source: Reactome
  • Wnt signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.16. 2681.
ReactomeiREACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_21285. Regulation of AMPK activity via LKB1.
SignaLinkiP35813.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PPM1A
Synonyms:PPPM1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9275. PPM1A.

Subcellular locationi

  • Nucleus
  • Cytoplasmcytosol
  • Membrane By similarity

  • Note: Weakly associates at the membrane and N-myristoylation mediates the membrane localization.By similarity

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
  • neuron projection Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • voltage-gated calcium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi239 – 2391D → N: No effect on binding SMAD2. 1 Publication

Organism-specific databases

PharmGKBiPA33603.

Polymorphism and mutation databases

BioMutaiPPM1A.
DMDMi548442.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 382381Protein phosphatase 1APRO_0000057741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei375 – 3751Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiP35813.
PaxDbiP35813.
PeptideAtlasiP35813.
PRIDEiP35813.

PTM databases

DEPODiP35813.
PhosphoSiteiP35813.

Expressioni

Gene expression databases

BgeeiP35813.
CleanExiHS_PPM1A.
ExpressionAtlasiP35813. baseline and differential.
GenevisibleiP35813. HS.

Organism-specific databases

HPAiHPA029209.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB1P494074EBI-989143,EBI-743313
ARRB2P321213EBI-989143,EBI-714559
AXIN1O151692EBI-989143,EBI-710484
MAPK1P2848219EBI-989143,EBI-959949
MAPK14Q165392EBI-989143,EBI-73946
RANBP3Q9H6Z44EBI-989143,EBI-992681
SMAD2Q157962EBI-989143,EBI-1040141

Protein-protein interaction databases

BioGridi111489. 27 interactions.
IntActiP35813. 23 interactions.
MINTiMINT-2802996.
STRINGi9606.ENSP00000327255.

Structurei

Secondary structure

1
382
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 1911Combined sources
Beta strandi22 – 3110Combined sources
Beta strandi33 – 353Combined sources
Beta strandi38 – 469Combined sources
Turni47 – 493Combined sources
Beta strandi50 – 6314Combined sources
Helixi66 – 8015Combined sources
Helixi83 – 864Combined sources
Beta strandi88 – 914Combined sources
Helixi94 – 11825Combined sources
Beta strandi129 – 1346Combined sources
Beta strandi136 – 14611Combined sources
Beta strandi148 – 1536Combined sources
Beta strandi156 – 1605Combined sources
Helixi169 – 1779Combined sources
Turni188 – 1903Combined sources
Helixi200 – 2023Combined sources
Helixi210 – 2123Combined sources
Beta strandi213 – 2164Combined sources
Beta strandi220 – 2256Combined sources
Turni228 – 2303Combined sources
Beta strandi231 – 2377Combined sources
Helixi239 – 2424Combined sources
Helixi247 – 25812Combined sources
Helixi264 – 27714Combined sources
Beta strandi284 – 2907Combined sources
Helixi299 – 31921Combined sources
Helixi330 – 33910Combined sources
Turni347 – 3493Combined sources
Helixi350 – 3545Combined sources
Helixi355 – 36511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4RA2X-ray1.94A2-368[»]
ProteinModelPortaliP35813.
SMRiP35813. Positions 2-368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35813.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 291269PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000115384.
HOGENOMiHOG000233895.
HOVERGENiHBG053647.
InParanoidiP35813.
KOiK04457.
OMAiEVYAIER.
OrthoDBiEOG7WMCJH.
PhylomeDBiP35813.
TreeFamiTF313590.

Family and domain databases

Gene3Di1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR012911. PP2C_C.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha-1 (identifier: P35813-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL
60 70 80 90 100
ESWSFFAVYD GHAGSQVAKY CCEHLLDHIT NNQDFKGSAG APSVENVKNG
110 120 130 140 150
IRTGFLEIDE HMRVMSEKKH GADRSGSTAV GVLISPQHTY FINCGDSRGL
160 170 180 190 200
LCRNRKVHFF TQDHKPSNPL EKERIQNAGG SVMIQRVNGS LAVSRALGDF
210 220 230 240 250
DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG IWDVMGNEEL
260 270 280 290 300
CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPNAPKVSPE
310 320 330 340 350
AVKKEAELDK YLECRVEEII KKQGEGVPDL VHVMRTLASE NIPSLPPGGE
360 370 380
LASKRNVIEA VYNRLNPYKN DDTDSTSTDD MW
Length:382
Mass (Da):42,448
Last modified:June 1, 1994 - v1
Checksum:iD48EF508B4A76687
GO
Isoform Alpha-2 (identifier: P35813-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     318-324: EIIKKQG → GGSFNKK
     325-382: Missing.

Show »
Length:324
Mass (Da):35,958
Checksum:iED58E203BB26CE00
GO
Isoform 3 (identifier: P35813-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MFCSGRKWVAEATICTKLMKREKRRMGKRRAKKAKREEKKKGGERRRNEKRGNQMKRMCERKKYETDLEDQDIM

Note: No experimental confirmation available.Curated
Show »
Length:455
Mass (Da):51,366
Checksum:iCBC6E3F350D6FDBD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti342 – 3421I → T in AK097843 (PubMed:14702039).Curated
Isoform 3 (identifier: P35813-3)
Sequence conflicti54 – 541Q → R in AK097843 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MFCSGRKWVAEATICTKLMK REKRRMGKRRAKKAKREEKK KGGERRRNEKRGNQMKRMCE RKKYETDLEDQDIM in isoform 3. 1 PublicationVSP_045687
Alternative sequencei318 – 3247EIIKKQG → GGSFNKK in isoform Alpha-2. 1 PublicationVSP_005085
Alternative sequencei325 – 38258Missing in isoform Alpha-2. 1 PublicationVSP_005086Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS45120.1. [P35813-3]
CCDS9744.1. [P35813-1]
CCDS9745.1. [P35813-2]
PIRiS22423.
RefSeqiNP_066283.1. NM_021003.4. [P35813-1]
NP_808820.1. NM_177951.2. [P35813-2]
NP_808821.2. NM_177952.2. [P35813-3]
XP_005267836.1. XM_005267779.1. [P35813-1]
XP_005267838.1. XM_005267781.1. [P35813-1]
XP_006720242.1. XM_006720179.1. [P35813-1]
UniGeneiHs.130036.

Genome annotation databases

EnsembliENST00000325642; ENSP00000327255; ENSG00000100614. [P35813-3]
ENST00000325658; ENSP00000314850; ENSG00000100614. [P35813-2]
ENST00000395076; ENSP00000378514; ENSG00000100614. [P35813-1]
GeneIDi5494.
KEGGihsa:5494.
UCSCiuc001xex.4. human. [P35813-2]
uc001xey.4. human. [P35813-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS45120.1. [P35813-3]
CCDS9744.1. [P35813-1]
CCDS9745.1. [P35813-2]
PIRiS22423.
RefSeqiNP_066283.1. NM_021003.4. [P35813-1]
NP_808820.1. NM_177951.2. [P35813-2]
NP_808821.2. NM_177952.2. [P35813-3]
XP_005267836.1. XM_005267779.1. [P35813-1]
XP_005267838.1. XM_005267781.1. [P35813-1]
XP_006720242.1. XM_006720179.1. [P35813-1]
UniGeneiHs.130036.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4RA2X-ray1.94A2-368[»]
ProteinModelPortaliP35813.
SMRiP35813. Positions 2-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111489. 27 interactions.
IntActiP35813. 23 interactions.
MINTiMINT-2802996.
STRINGi9606.ENSP00000327255.

Chemistry

BindingDBiP35813.
ChEMBLiCHEMBL2437.

PTM databases

DEPODiP35813.
PhosphoSiteiP35813.

Polymorphism and mutation databases

BioMutaiPPM1A.
DMDMi548442.

Proteomic databases

MaxQBiP35813.
PaxDbiP35813.
PeptideAtlasiP35813.
PRIDEiP35813.

Protocols and materials databases

DNASUi5494.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325642; ENSP00000327255; ENSG00000100614. [P35813-3]
ENST00000325658; ENSP00000314850; ENSG00000100614. [P35813-2]
ENST00000395076; ENSP00000378514; ENSG00000100614. [P35813-1]
GeneIDi5494.
KEGGihsa:5494.
UCSCiuc001xex.4. human. [P35813-2]
uc001xey.4. human. [P35813-1]

Organism-specific databases

CTDi5494.
GeneCardsiGC14P060712.
HGNCiHGNC:9275. PPM1A.
HPAiHPA029209.
MIMi606108. gene.
neXtProtiNX_P35813.
PharmGKBiPA33603.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000115384.
HOGENOMiHOG000233895.
HOVERGENiHBG053647.
InParanoidiP35813.
KOiK04457.
OMAiEVYAIER.
OrthoDBiEOG7WMCJH.
PhylomeDBiP35813.
TreeFamiTF313590.

Enzyme and pathway databases

BRENDAi3.1.3.16. 2681.
ReactomeiREACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_21285. Regulation of AMPK activity via LKB1.
SignaLinkiP35813.

Miscellaneous databases

ChiTaRSiPPM1A. human.
EvolutionaryTraceiP35813.
GeneWikiiPPM1A.
GenomeRNAii5494.
NextBioi21242.
PROiP35813.
SOURCEiSearch...

Gene expression databases

BgeeiP35813.
CleanExiHS_PPM1A.
ExpressionAtlasiP35813. baseline and differential.
GenevisibleiP35813. HS.

Family and domain databases

Gene3Di1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR012911. PP2C_C.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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).

Entry informationi

Entry nameiPPM1A_HUMAN
AccessioniPrimary (citable) accession number: P35813
Secondary accession number(s): B5BU11, J3KNM0, O75551
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 24, 2015
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.