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Q9ULR3 (PPM1H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase 1H

EC=3.1.3.16
Gene names
Name:PPM1H
Synonyms:ARHCL1, KIAA1157, URCC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the PP2C family.

Contains 1 PP2C-like domain.

Caution

A report observed N-glycosylation at Asn-354 (Ref.6). However, as the protein is not predicted to localize in an extracellular compartment of the cell, additional evidences are required to confirm this result.

Ontologies

Keywords
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionphosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Protein phosphatase 1H
PRO_0000286603

Regions

Domain137 – 507371PP2C-like

Amino acid modifications

Modified residue1241Phosphoserine Ref.7 Ref.8
Modified residue2111Phosphoserine Ref.7 Ref.9
Modified residue2211Phosphoserine Ref.7
Modified residue2241Phosphothreonine Ref.7
Modified residue4221Phosphoserine Ref.7

Experimental info

Sequence conflict771A → V in AAI57844. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9ULR3 [UniParc].

Last modified May 15, 2007. Version 2.
Checksum: 9348C6AC3D74D1B7

FASTA51456,448
        10         20         30         40         50         60 
MLTRVKSAVA NFMGGIMAGS SGSEHGGGSC GGSDLPLRFP YGRPEFLGLS QDEVECSADH 

        70         80         90        100        110        120 
IARPILILKE TRRLPWATGY AEVINAGKST HNEDQASCEV LTVKKKAGAV TSTPNRNSSK 

       130        140        150        160        170        180 
RRSSLPNGEG LQLKENSESE GVSCHYWSLF DGHAGSGAAV VASRLLQHHI TEQLQDIVDI 

       190        200        210        220        230        240 
LKNSAVLPPT CLGEEPENTP ANSRTLTRAA SLRGGVGAPG SPSTPPTRFF TEKKIPHECL 

       250        260        270        280        290        300 
VIGALESAFK EMDLQIERER SSYNISGGCT ALIVICLLGK LYVANAGDSR AIIIRNGEII 

       310        320        330        340        350        360 
PMSSEFTPET ERQRLQYLAF MQPHLLGNEF THLEFPRRVQ RKELGKKMLY RDFNMTGWAY 

       370        380        390        400        410        420 
KTIEDEDLKF PLIYGEGKKA RVMATIGVTR GLGDHDLKVH DSNIYIKPFL SSAPEVRIYD 

       430        440        450        460        470        480 
LSKYDHGSDD VLILATDGLW DVLSNEEVAE AITQFLPNCD PDDPHRYTLA AQDLVMRARG 

       490        500        510 
VLKDRGWRIS NDRLGSGDDI SVYVIPLIHG NKLS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of Urcc2, a novel gene up-regulated in colon cancer."
Shimokawa T., Furukawa Y., Nakamura Y.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton 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].
[4]"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].
Tissue: Brain.
[5]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-514.
Tissue: Brain.
[6]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-211; SER-221; THR-224 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB084258 mRNA. Translation: BAG16181.1.
AC023359 Genomic DNA. No translation available.
AC025264 Genomic DNA. No translation available.
AC048341 Genomic DNA. No translation available.
AC078814 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97112.1.
BC157843 mRNA. Translation: AAI57844.1.
AB032983 mRNA. Translation: BAA86471.1.
CCDSCCDS44934.1.
RefSeqNP_065751.1. NM_020700.1.
UniGeneHs.435479.

3D structure databases

ProteinModelPortalQ9ULR3.
SMRQ9ULR3. Positions 248-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121530. 1 interaction.
IntActQ9ULR3. 1 interaction.

PTM databases

PhosphoSiteQ9ULR3.

Polymorphism databases

DMDM147721250.

Proteomic databases

MaxQBQ9ULR3.
PaxDbQ9ULR3.
PRIDEQ9ULR3.

Protocols and materials databases

DNASU57460.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228705; ENSP00000228705; ENSG00000111110.
GeneID57460.
KEGGhsa:57460.
UCSCuc001srk.3. human.

Organism-specific databases

CTD57460.
GeneCardsGC12M063037.
H-InvDBHIX0018169.
HGNCHGNC:18583. PPM1H.
HPACAB020694.
neXtProtNX_Q9ULR3.
PharmGKBPA38354.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000251606.
HOVERGENHBG105802.
InParanoidQ9ULR3.
KOK17503.
OMAERTVYNI.
OrthoDBEOG7F511J.
PhylomeDBQ9ULR3.
TreeFamTF314700.

Gene expression databases

BgeeQ9ULR3.
CleanExHS_PPM1H.
GenevestigatorQ9ULR3.

Family and domain databases

Gene3D3.60.40.10. 4 hits.
InterProIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 2 hits.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 4 hits.
ProtoNetSearch...

Other

ChiTaRSPPM1H. human.
GenomeRNAi57460.
NextBio63648.
PROQ9ULR3.

Entry information

Entry namePPM1H_HUMAN
AccessionPrimary (citable) accession number: Q9ULR3
Secondary accession number(s): B1Q2A9, B2RXG4, Q6PI86
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: July 9, 2014
This is version 94 of the entry and version 2 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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM