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Protein

Protein phosphatase 1G

Gene

Ppm1g

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Manganese 1By similarity
Metal bindingi60 – 601Manganese 2By similarity
Metal bindingi61 – 611Manganese 1; via carbonyl oxygenBy similarity
Metal bindingi438 – 4381Manganese 2By similarity
Metal bindingi493 – 4931Manganese 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1GCurated (EC:3.1.3.16)
Alternative name(s):
Protein phosphatase magnesium-dependent 1 gammaCurated
Gene namesi
Name:Ppm1gImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628676. Ppm1g.

Subcellular locationi

  • Cytoplasm Curated
  • Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 542541Protein phosphatase 1GPRO_0000432429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei122 – 1221PhosphothreonineBy similarity
Modified residuei380 – 3801N6-acetyllysineBy similarity
Modified residuei524 – 5241PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiF1LNI5.
PeptideAtlasiF1LNI5.

Expressioni

Gene expression databases

GenevisibleiF1LNI5. RN.

Interactioni

Subunit structurei

Interacts with NOL3; may dephosphorylate NOL3.1 Publication1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000029414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 502477PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi258 – 31962Glu-richPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0699. Eukaryota.
COG0631. LUCA.
InParanoidiF1LNI5.
OMAiHNCILNF.
OrthoDBiEOG7034GD.

Family and domain databases

Gene3Di3.60.40.10. 2 hits.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 2 hits.
PfamiPF00481. PP2C. 2 hits.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 2 hits.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

F1LNI5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAYLSQPNT VKCSGDGVGA PRLPLPYGFS AMQGWRVSME DAHNCIPELD
60 70 80 90 100
NETAMFSVYD GHGGEEVALY CAKYLPDIIK DQKAYKEGKL QKALQDAFLA
110 120 130 140 150
IDAKLTTDEV IKELAQIAGR PTEDEDDKEK VADEDDVDNE EAALLHEEAT
160 170 180 190 200
MTIEELLTRY GQNCQKGPPH TKSGTGIGDE PEPQGLNGEA GPEDPSRETP
210 220 230 240 250
SQENGPTAKG HTGPSSNSDH GTEAGQIGEP GTATGEAGPS CSSASDKLPR
260 270 280 290 300
VAKSKFFEDS EDESDEVEEE EDDIEECSED EDGYSSEEAE NEEDEDDTEE
310 320 330 340 350
AEEDDDEEMM VPGMEGKEEP GSDSGTTAVV ALIRGKQLIV ANAGDSRCVV
360 370 380 390 400
SEAGKALDMS YDHKPEDEVE LARIKNAGGK VTMDGRVNGG LNLSRAIGDH
410 420 430 440 450
FYKRNKNLPP QEQMISALPD IKVLTLTDDH EFMVIACDGI WNVMSSQEVV
460 470 480 490 500
DFIQSKISQR DENGELRLLS SIVEELLDQC LAPDTSGDGT GCDNMTCIII
510 520 530 540
CFKPRNTVEL QPESGKRKLE EALSTEGAEE NGNSDKKKAK RD
Length:542
Mass (Da):58,743
Last modified:April 3, 2013 - v2
Checksum:i189AB14A1E596F9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06042433 Genomic DNA. No translation available.
AABR06042434 Genomic DNA. No translation available.
AABR06042435 Genomic DNA. No translation available.
UniGeneiRn.16969.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06042433 Genomic DNA. No translation available.
AABR06042434 Genomic DNA. No translation available.
AABR06042435 Genomic DNA. No translation available.
UniGeneiRn.16969.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000029414.

Proteomic databases

PaxDbiF1LNI5.
PeptideAtlasiF1LNI5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi628676. Ppm1g.

Phylogenomic databases

eggNOGiKOG0699. Eukaryota.
COG0631. LUCA.
InParanoidiF1LNI5.
OMAiHNCILNF.
OrthoDBiEOG7034GD.

Miscellaneous databases

PROiF1LNI5.

Gene expression databases

GenevisibleiF1LNI5. RN.

Family and domain databases

Gene3Di3.60.40.10. 2 hits.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 2 hits.
PfamiPF00481. PP2C. 2 hits.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 2 hits.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "ARC protects rat cardiomyocytes against oxidative stress through inhibition of caspase-2 mediated mitochondrial pathway."
    Zhang Y.Q., Herman B.
    J. Cell. Biochem. 99:575-588(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOL3.

Entry informationi

Entry nameiPPM1G_RAT
AccessioniPrimary (citable) accession number: F1LNI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 2015
Last sequence update: April 3, 2013
Last modified: July 6, 2016
This is version 47 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.