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Protein

Protein phosphatase 1H

Gene

PPM1H

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

Functioni

Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  • phosphoprotein phosphatase activity Source: UniProtKB

GO - Biological processi

  • dephosphorylation Source: GOC
Complete GO annotation...

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 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18583. PPM1H.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi153 – 1531H → L: Decreased enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA38354.

Polymorphism and mutation databases

BioMutaiPPM1H.
DMDMi147721250.

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

DEPODiQ9ULR3.
PhosphoSiteiQ9ULR3.

Expressioni

Gene expression databases

BgeeiQ9ULR3.
CleanExiHS_PPM1H.
GenevisibleiQ9ULR3. HS.

Organism-specific databases

HPAiCAB020694.
HPA044244.
HPA058777.

Interactioni

Protein-protein interaction databases

BioGridi121530. 3 interactions.
IntActiQ9ULR3. 1 interaction.
STRINGi9606.ENSP00000228705.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 507431PPM-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.
GeneTreeiENSGT00530000063231.
HOGENOMiHOG000251606.
HOVERGENiHBG105802.
InParanoidiQ9ULR3.
KOiK17503.
OMAiDLPYTYF.
OrthoDBiEOG7F511J.
PhylomeDBiQ9ULR3.
TreeFamiTF314700.

Family and domain databases

Gene3Di3.60.40.10. 4 hits.
InterProiIPR015655. PP2C.
IPR001932. PPM-type_phosphatase_dom.
[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.
PROSITEiPS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ULR3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTRVKSAVA NFMGGIMAGS SGSEHGGGSC GGSDLPLRFP YGRPEFLGLS
60 70 80 90 100
QDEVECSADH IARPILILKE TRRLPWATGY AEVINAGKST HNEDQASCEV
110 120 130 140 150
LTVKKKAGAV TSTPNRNSSK RRSSLPNGEG LQLKENSESE GVSCHYWSLF
160 170 180 190 200
DGHAGSGAAV VASRLLQHHI TEQLQDIVDI LKNSAVLPPT CLGEEPENTP
210 220 230 240 250
ANSRTLTRAA SLRGGVGAPG SPSTPPTRFF TEKKIPHECL VIGALESAFK
260 270 280 290 300
EMDLQIERER SSYNISGGCT ALIVICLLGK LYVANAGDSR AIIIRNGEII
310 320 330 340 350
PMSSEFTPET ERQRLQYLAF MQPHLLGNEF THLEFPRRVQ RKELGKKMLY
360 370 380 390 400
RDFNMTGWAY KTIEDEDLKF PLIYGEGKKA RVMATIGVTR GLGDHDLKVH
410 420 430 440 450
DSNIYIKPFL SSAPEVRIYD LSKYDHGSDD VLILATDGLW DVLSNEEVAE
460 470 480 490 500
AITQFLPNCD PDDPHRYTLA AQDLVMRARG VLKDRGWRIS NDRLGSGDDI
510
SVYVIPLIHG NKLS
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:
EMBLi
GenBanki
DDBJi
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi121530. 3 interactions.
IntActiQ9ULR3. 1 interaction.
STRINGi9606.ENSP00000228705.

PTM databases

DEPODiQ9ULR3.
PhosphoSiteiQ9ULR3.

Polymorphism and mutation databases

BioMutaiPPM1H.
DMDMi147721250.

Proteomic databases

MaxQBiQ9ULR3.
PaxDbiQ9ULR3.
PRIDEiQ9ULR3.

Protocols and materials databases

DNASUi57460.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi57460.
GeneCardsiGC12M063037.
H-InvDBHIX0018169.
HGNCiHGNC:18583. PPM1H.
HPAiCAB020694.
HPA044244.
HPA058777.
MIMi616016. gene.
neXtProtiNX_Q9ULR3.
PharmGKBiPA38354.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00530000063231.
HOGENOMiHOG000251606.
HOVERGENiHBG105802.
InParanoidiQ9ULR3.
KOiK17503.
OMAiDLPYTYF.
OrthoDBiEOG7F511J.
PhylomeDBiQ9ULR3.
TreeFamiTF314700.

Miscellaneous databases

ChiTaRSiPPM1H. human.
GenomeRNAii57460.
NextBioi63648.
PROiQ9ULR3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULR3.
CleanExiHS_PPM1H.
GenevisibleiQ9ULR3. HS.

Family and domain databases

Gene3Di3.60.40.10. 4 hits.
InterProiIPR015655. PP2C.
IPR001932. PPM-type_phosphatase_dom.
[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.
PROSITEiPS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF HIS-153.
  10. "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: July 22, 2015
This is version 103 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

Miscellaneous

May act as a suppressor of trastuzumab resistance.1 Publication

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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.