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Protein

Protein phosphatase methylesterase 1

Gene

PPME1

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

Functioni

Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme.1 Publication

Catalytic activityi

[Phosphatase 2A protein]-leucine methyl ester + H2O = [phosphatase 2A protein]-leucine + methanol.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei156 – 15611 Publication
Active sitei181 – 18111 Publication
Active sitei349 – 34911 Publication

GO - Molecular functioni

  • protein C-terminal methylesterase activity Source: HGNC
  • protein phosphatase 2A binding Source: HGNC
  • protein phosphatase binding Source: HGNC
  • protein phosphatase inhibitor activity Source: ProtInc
  • protein phosphatase type 2A regulator activity Source: HGNC

GO - Biological processi

  • negative regulation of catalytic activity Source: GOC
  • protein demethylation Source: HGNC
  • regulation of protein phosphatase type 2A activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16514.
BRENDAi3.1.1.89. 2681.

Protein family/group databases

ESTHERihuman-PPME1. PPase_methylesterase_euk.
MEROPSiS33.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase methylesterase 1 (EC:3.1.1.89)
Short name:
PME-1
Gene namesi
Name:PPME1
Synonyms:PME1
ORF Names:PP2593, PRO0750
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:30178. PPME1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671152.

Chemistry

ChEMBLiCHEMBL1293320.
GuidetoPHARMACOLOGYi2875.

Polymorphism and mutation databases

DMDMi47606055.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 386385Protein phosphatase methylesterase 1PRO_0000090390Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by SIK1 following increases in intracellular sodium, leading to dissociation from the protein phosphatase 2A (PP2A) complex and subsequent dephosphorylation of sodium/potassium-transporting ATPase ATP1A1.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y570.
MaxQBiQ9Y570.
PaxDbiQ9Y570.
PRIDEiQ9Y570.

2D gel databases

REPRODUCTION-2DPAGEIPI00007694.

PTM databases

iPTMnetiQ9Y570.
PhosphoSiteiQ9Y570.

Expressioni

Gene expression databases

BgeeiQ9Y570.
CleanExiHS_PPME1.
ExpressionAtlasiQ9Y570. baseline and differential.
GenevisibleiQ9Y570. HS.

Organism-specific databases

HPAiCAB004541.
HPA043900.

Interactioni

Subunit structurei

Binds PPP2CA and PPP2CB.1 Publication

GO - Molecular functioni

  • protein phosphatase 2A binding Source: HGNC
  • protein phosphatase binding Source: HGNC

Protein-protein interaction databases

BioGridi119524. 96 interactions.
IntActiQ9Y570. 7 interactions.
STRINGi9606.ENSP00000329867.

Chemistry

BindingDBiQ9Y570.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 483Combined sources
Beta strandi51 – 6010Combined sources
Beta strandi63 – 7210Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 825Combined sources
Helixi89 – 924Combined sources
Helixi93 – 1008Combined sources
Beta strandi106 – 1105Combined sources
Helixi128 – 14316Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi150 – 1556Combined sources
Helixi157 – 16711Combined sources
Beta strandi174 – 1818Combined sources
Helixi184 – 20017Combined sources
Beta strandi205 – 2073Combined sources
Helixi208 – 21710Combined sources
Helixi224 – 23411Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi285 – 2884Combined sources
Helixi291 – 2944Combined sources
Helixi295 – 3028Combined sources
Helixi305 – 3117Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi316 – 3227Combined sources
Helixi323 – 3253Combined sources
Helixi328 – 3358Combined sources
Beta strandi339 – 3435Combined sources
Helixi351 – 3544Combined sources
Helixi356 – 36914Combined sources
Beta strandi372 – 3754Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C5VX-ray2.00A39-386[»]
3C5WX-ray2.80P284-386[»]
P39-238[»]
ProteinModelPortaliQ9Y570.
SMRiQ9Y570. Positions 39-376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y570.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi256 – 2638Poly-Glu

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Phylogenomic databases

eggNOGiKOG2564. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00390000004396.
HOGENOMiHOG000116699.
HOVERGENiHBG053622.
InParanoidiQ9Y570.
KOiK13617.
OMAiLYTWRIE.
OrthoDBiEOG741Z2K.
PhylomeDBiQ9Y570.
TreeFamiTF314697.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR016812. PPase_methylesterase_euk.
[Graphical view]
PANTHERiPTHR14189. PTHR14189. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF022950. PPase_methylesterase_euk. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y570-1) [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
MSALEKSMHL GRLPSRPPLP GSGGSQSGAK MRMGPGRKRD FSPVPWSQYF
60 70 80 90 100
ESMEDVEVEN ETGKDTFRVY KSGSEGPVLL LLHGGGHSAL SWAVFTAAII
110 120 130 140 150
SRVQCRIVAL DLRSHGETKV KNPEDLSAET MAKDVGNVVE AMYGDLPPPI
160 170 180 190 200
MLIGHSMGGA IAVHTASSNL VPSLLGLCMI DVVEGTAMDA LNSMQNFLRG
210 220 230 240 250
RPKTFKSLEN AIEWSVKSGQ IRNLESARVS MVGQVKQCEG ITSPEGSKSI
260 270 280 290 300
VEGIIEEEEE DEEGSESISK RKKEDDMETK KDHPYTWRIE LAKTEKYWDG
310 320 330 340 350
WFRGLSNLFL SCPIPKLLLL AGVDRLDKDL TIGQMQGKFQ MQVLPQCGHA
360 370 380
VHEDAPDKVA EAVATFLIRH RFAEPIGGFQ CVFPGC
Length:386
Mass (Da):42,315
Last modified:January 23, 2007 - v3
Checksum:i37B25324583E8578
GO
Isoform 2 (identifier: Q9Y570-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-187: Missing.

Note: No experimental confirmation available.
Show »
Length:199
Mass (Da):22,462
Checksum:iF39B21A7AD5C5115
GO
Isoform 3 (identifier: Q9Y570-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-276: Missing.
     360-386: AEAVATFLIRHRFAEPIGGFQCVFPGC → SLVLSDCKRT...LCYFIPGPCG

Note: No experimental confirmation available.
Show »
Length:161
Mass (Da):18,214
Checksum:i53E51B3B7916DBFB
GO
Isoform 4 (identifier: Q9Y570-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-278: E → EGLPSETQNLLLFLQ

Note: Gene prediction based on EST data.
Show »
Length:400
Mass (Da):43,870
Checksum:i0F9F02DDFABA6C3B
GO

Sequence cautioni

The sequence AAG22477.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3091F → S in BAA91661 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 276276Missing in isoform 3. 1 PublicationVSP_010335Add
BLAST
Alternative sequencei1 – 187187Missing in isoform 2. 1 PublicationVSP_010336Add
BLAST
Alternative sequencei278 – 2781E → EGLPSETQNLLLFLQ in isoform 4. CuratedVSP_054818
Alternative sequencei360 – 38627AEAVA…VFPGC → SLVLSDCKRTTVRITLDVTE DKSLSLSLHCLQQLLWSLCR CSSTSSPTSPWQLLMVLVLC ICAEELLTLCYFIPGPCG in isoform 3. 1 PublicationVSP_010337Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157028 mRNA. Translation: AAD44976.1.
AF111853 mRNA. Translation: AAF16692.1.
AK001381 mRNA. Translation: BAA91661.1.
AK022725 mRNA. Translation: BAG51108.1.
AK123288 mRNA. Translation: BAC85574.1.
AP000577 Genomic DNA. No translation available.
AP002392 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74932.1.
BC003046 mRNA. Translation: AAH03046.1.
BC050705 mRNA. Translation: AAH50705.1.
AF193049 mRNA. Translation: AAG22477.1. Sequence problems.
CCDSiCCDS44678.1. [Q9Y570-1]
CCDS60891.1. [Q9Y570-4]
RefSeqiNP_001258522.1. NM_001271593.1. [Q9Y570-4]
NP_057231.1. NM_016147.2. [Q9Y570-1]
UniGeneiHs.503251.

Genome annotation databases

EnsembliENST00000328257; ENSP00000329867; ENSG00000214517. [Q9Y570-1]
ENST00000398427; ENSP00000381461; ENSG00000214517. [Q9Y570-4]
GeneIDi51400.
KEGGihsa:51400.
UCSCiuc001ouw.5. human. [Q9Y570-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157028 mRNA. Translation: AAD44976.1.
AF111853 mRNA. Translation: AAF16692.1.
AK001381 mRNA. Translation: BAA91661.1.
AK022725 mRNA. Translation: BAG51108.1.
AK123288 mRNA. Translation: BAC85574.1.
AP000577 Genomic DNA. No translation available.
AP002392 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74932.1.
BC003046 mRNA. Translation: AAH03046.1.
BC050705 mRNA. Translation: AAH50705.1.
AF193049 mRNA. Translation: AAG22477.1. Sequence problems.
CCDSiCCDS44678.1. [Q9Y570-1]
CCDS60891.1. [Q9Y570-4]
RefSeqiNP_001258522.1. NM_001271593.1. [Q9Y570-4]
NP_057231.1. NM_016147.2. [Q9Y570-1]
UniGeneiHs.503251.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C5VX-ray2.00A39-386[»]
3C5WX-ray2.80P284-386[»]
P39-238[»]
ProteinModelPortaliQ9Y570.
SMRiQ9Y570. Positions 39-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119524. 96 interactions.
IntActiQ9Y570. 7 interactions.
STRINGi9606.ENSP00000329867.

Chemistry

BindingDBiQ9Y570.
ChEMBLiCHEMBL1293320.
GuidetoPHARMACOLOGYi2875.

Protein family/group databases

ESTHERihuman-PPME1. PPase_methylesterase_euk.
MEROPSiS33.984.

PTM databases

iPTMnetiQ9Y570.
PhosphoSiteiQ9Y570.

Polymorphism and mutation databases

DMDMi47606055.

2D gel databases

REPRODUCTION-2DPAGEIPI00007694.

Proteomic databases

EPDiQ9Y570.
MaxQBiQ9Y570.
PaxDbiQ9Y570.
PRIDEiQ9Y570.

Protocols and materials databases

DNASUi51400.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328257; ENSP00000329867; ENSG00000214517. [Q9Y570-1]
ENST00000398427; ENSP00000381461; ENSG00000214517. [Q9Y570-4]
GeneIDi51400.
KEGGihsa:51400.
UCSCiuc001ouw.5. human. [Q9Y570-1]

Organism-specific databases

CTDi51400.
GeneCardsiPPME1.
HGNCiHGNC:30178. PPME1.
HPAiCAB004541.
HPA043900.
MIMi611117. gene.
neXtProtiNX_Q9Y570.
PharmGKBiPA142671152.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2564. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00390000004396.
HOGENOMiHOG000116699.
HOVERGENiHBG053622.
InParanoidiQ9Y570.
KOiK13617.
OMAiLYTWRIE.
OrthoDBiEOG741Z2K.
PhylomeDBiQ9Y570.
TreeFamiTF314697.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16514.
BRENDAi3.1.1.89. 2681.

Miscellaneous databases

ChiTaRSiPPME1. human.
EvolutionaryTraceiQ9Y570.
GenomeRNAii51400.
NextBioi35537428.
PROiQ9Y570.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y570.
CleanExiHS_PPME1.
ExpressionAtlasiQ9Y570. baseline and differential.
GenevisibleiQ9Y570. HS.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR016812. PPase_methylesterase_euk.
[Graphical view]
PANTHERiPTHR14189. PTHR14189. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF022950. PPase_methylesterase_euk. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A."
    Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., Pallas D.C.
    J. Biol. Chem. 274:14382-14391(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PPP2CB.
    Tissue: Cervix carcinoma.
  2. "Functional prediction of the coding sequences of 9 new genes deduced by analysis of cDNA clones from human fetal liver."
    Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhang Y., Liu M., He F.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal liver.
  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] (ISOFORMS 1 AND 3).
    Tissue: Amygdala.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 1).
    Tissue: Lung and Skin.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Tissue: Platelet.
  8. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-386 (ISOFORM 1).
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Structural mechanism of demethylation and inactivation of protein phosphatase 2A."
    Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y.
    Cell 133:154-163(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 39-386 ALONE AND IN COMPLEX WITH PPP2CA AND PPP2R1A, ACTIVE SITE, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiPPME1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y570
Secondary accession number(s): B3KMU6
, B5MEE7, J3QT22, Q8WYG8, Q9NVT5, Q9UI18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 140 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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 one 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.