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Q9ULR3

- PPM1H_HUMAN

UniProt

Q9ULR3 - PPM1H_HUMAN

Protein

Protein phosphatase 1H

Gene

PPM1H

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (15 May 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. phosphoprotein phosphatase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 1H (EC:3.1.3.16)
    Gene namesi
    Name:PPM1H
    Synonyms:ARHCL1, KIAA1157, URCC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18583. PPM1H.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38354.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 514514Protein phosphatase 1HPRO_0000286603Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei124 – 1241Phosphoserine2 Publications
    Modified residuei211 – 2111Phosphoserine2 Publications
    Modified residuei221 – 2211Phosphoserine1 Publication
    Modified residuei224 – 2241Phosphothreonine1 Publication
    Modified residuei422 – 4221Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9ULR3.
    PaxDbiQ9ULR3.
    PRIDEiQ9ULR3.

    PTM databases

    PhosphoSiteiQ9ULR3.

    Expressioni

    Gene expression databases

    BgeeiQ9ULR3.
    CleanExiHS_PPM1H.
    GenevestigatoriQ9ULR3.

    Organism-specific databases

    HPAiCAB020694.

    Interactioni

    Protein-protein interaction databases

    BioGridi121530. 2 interactions.
    IntActiQ9ULR3. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ULR3.
    SMRiQ9ULR3. Positions 248-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini137 – 507371PP2C-likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PP2C family.Curated
    Contains 1 PP2C-like domain.Curated

    Phylogenomic databases

    eggNOGiCOG0631.
    HOGENOMiHOG000251606.
    HOVERGENiHBG105802.
    InParanoidiQ9ULR3.
    KOiK17503.
    OMAiERTVYNI.
    OrthoDBiEOG7F511J.
    PhylomeDBiQ9ULR3.
    TreeFamiTF314700.

    Family and domain databases

    Gene3Di3.60.40.10. 4 hits.
    InterProiIPR001932. PP2C-like_dom.
    IPR015655. Protein_Pase_2C.
    [Graphical view]
    PANTHERiPTHR13832. PTHR13832. 1 hit.
    PfamiPF00481. PP2C. 2 hits.
    [Graphical view]
    SMARTiSM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81606. SSF81606. 4 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9ULR3-1 [UniParc]FASTAAdd to Basket

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    MLTRVKSAVA NFMGGIMAGS SGSEHGGGSC GGSDLPLRFP YGRPEFLGLS    50
    QDEVECSADH IARPILILKE TRRLPWATGY AEVINAGKST HNEDQASCEV 100
    LTVKKKAGAV TSTPNRNSSK RRSSLPNGEG LQLKENSESE GVSCHYWSLF 150
    DGHAGSGAAV VASRLLQHHI TEQLQDIVDI LKNSAVLPPT CLGEEPENTP 200
    ANSRTLTRAA SLRGGVGAPG SPSTPPTRFF TEKKIPHECL VIGALESAFK 250
    EMDLQIERER SSYNISGGCT ALIVICLLGK LYVANAGDSR AIIIRNGEII 300
    PMSSEFTPET ERQRLQYLAF MQPHLLGNEF THLEFPRRVQ RKELGKKMLY 350
    RDFNMTGWAY KTIEDEDLKF PLIYGEGKKA RVMATIGVTR GLGDHDLKVH 400
    DSNIYIKPFL SSAPEVRIYD LSKYDHGSDD VLILATDGLW DVLSNEEVAE 450
    AITQFLPNCD PDDPHRYTLA AQDLVMRARG VLKDRGWRIS NDRLGSGDDI 500
    SVYVIPLIHG NKLS 514
    Length:514
    Mass (Da):56,448
    Last modified:May 15, 2007 - v2
    Checksum:i9348C6AC3D74D1B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771A → V in AAI57844. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS44934.1.
    RefSeqiNP_065751.1. NM_020700.1.
    UniGeneiHs.435479.

    Genome annotation databases

    EnsembliENST00000228705; ENSP00000228705; ENSG00000111110.
    GeneIDi57460.
    KEGGihsa:57460.
    UCSCiuc001srk.3. human.

    Polymorphism databases

    DMDMi147721250.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS44934.1.
    RefSeqi NP_065751.1. NM_020700.1.
    UniGenei Hs.435479.

    3D structure databases

    ProteinModelPortali Q9ULR3.
    SMRi Q9ULR3. Positions 248-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121530. 2 interactions.
    IntActi Q9ULR3. 1 interaction.

    PTM databases

    PhosphoSitei Q9ULR3.

    Polymorphism databases

    DMDMi 147721250.

    Proteomic databases

    MaxQBi Q9ULR3.
    PaxDbi Q9ULR3.
    PRIDEi Q9ULR3.

    Protocols and materials databases

    DNASUi 57460.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228705 ; ENSP00000228705 ; ENSG00000111110 .
    GeneIDi 57460.
    KEGGi hsa:57460.
    UCSCi uc001srk.3. human.

    Organism-specific databases

    CTDi 57460.
    GeneCardsi GC12M063037.
    H-InvDB HIX0018169.
    HGNCi HGNC:18583. PPM1H.
    HPAi CAB020694.
    neXtProti NX_Q9ULR3.
    PharmGKBi PA38354.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0631.
    HOGENOMi HOG000251606.
    HOVERGENi HBG105802.
    InParanoidi Q9ULR3.
    KOi K17503.
    OMAi ERTVYNI.
    OrthoDBi EOG7F511J.
    PhylomeDBi Q9ULR3.
    TreeFami TF314700.

    Miscellaneous databases

    ChiTaRSi PPM1H. human.
    GenomeRNAii 57460.
    NextBioi 63648.
    PROi Q9ULR3.

    Gene expression databases

    Bgeei Q9ULR3.
    CleanExi HS_PPM1H.
    Genevestigatori Q9ULR3.

    Family and domain databases

    Gene3Di 3.60.40.10. 4 hits.
    InterProi IPR001932. PP2C-like_dom.
    IPR015655. Protein_Pase_2C.
    [Graphical view ]
    PANTHERi PTHR13832. PTHR13832. 1 hit.
    Pfami PF00481. PP2C. 2 hits.
    [Graphical view ]
    SMARTi SM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81606. SSF81606. 4 hits.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: IDENTIFICATION.
    7. 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].

    Entry informationi

    Entry nameiPPM1H_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULR3
    Secondary accession number(s): B1Q2A9, B2RXG4, Q6PI86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 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

    Caution

    A report observed N-glycosylation at Asn-354 (PubMed:19139490). However, as the protein is not predicted to localize in an extracellular compartment of the cell, additional evidences are required to confirm this result.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3