Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P62140 (PP1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Short name=PP-1B
Short name=PPP1CD
EC=3.1.3.16
EC=3.1.3.53
Gene names
Name:PPP1CB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Ref.20 Ref.24

Catalytic activity

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

[Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Enzyme regulation

Inhibited by the toxins okadaic acid, tautomycin and microcystin Leu-Arg By similarity. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress. Ref.16

Subunit structure

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. The targeting or regulatory subunits determine the substrate specificity of PP1. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Part of a complex containing PPP1R15B, PP1 and NCK1/2 By similarity. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7 and PPP1R12C. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with TRIM28; the interaction is weak. Interacts with PPP1R12A and NUAK1; the interaction is direct. Ref.12 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22

Subcellular location

Cytoplasm. Nucleus. Nucleusnucleoplasm. Nucleusnucleolus. Note: Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. Ref.13

Sequence similarities

Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
   Biological processBiological rhythms
Carbohydrate metabolism
Cell cycle
Cell division
Glycogen metabolism
   Cellular componentCytoplasm
Nucleus
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

entrainment of circadian clock by photoperiod

Inferred from sequence or structural similarity. Source: UniProtKB

glycogen metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell adhesion

Inferred from direct assay Ref.21. Source: UniProtKB

regulation of circadian rhythm

Inferred from mutant phenotype Ref.24. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

triglyceride catabolic process

Traceable author statement. Source: Reactome

   Cellular_componentMLL5-L complex

Inferred from direct assay Ref.19. Source: UniProtKB

PTW/PP1 phosphatase complex

Inferred from direct assay Ref.21Ref.20. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

myosin-light-chain-phosphatase activity

Inferred from direct assay Ref.21. Source: UniProtKB

phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17Ref.22Ref.20. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.21. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BRCA1P383983EBI-352350,EBI-349905
ClockO087852EBI-352350,EBI-79859From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 327326Serine/threonine-protein phosphatase PP1-beta catalytic subunit
PRO_0000058779

Sites

Active site1241Proton donor By similarity
Metal binding631Manganese 1 By similarity
Metal binding651Manganese 1 By similarity
Metal binding911Manganese 1 By similarity
Metal binding911Manganese 2 By similarity
Metal binding1231Manganese 2 By similarity
Metal binding1721Manganese 2 By similarity
Metal binding2471Manganese 2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.11 Ref.25 Ref.26
Modified residue3161Phosphothreonine Ref.18

Experimental info

Sequence conflict511L → P in AAV38549. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P62140 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E8356022E9B94ECD

FASTA32737,187
        10         20         30         40         50         60 
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI 

        70         80         90        100        110        120 
CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL 

       130        140        150        160        170        180 
RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ 

       190        200        210        220        230        240 
SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL 

       250        260        270        280        290        300 
DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK 

       310        320 
KAKYQYGGLN SGRPVTPPRT ANPPKKR 

« Hide

References

« Hide 'large scale' references
[1]"Three genes for protein phosphatase 1 map to different human chromosomes: sequence, expression and gene localisation of protein serine/threonine phosphatase 1 beta (PPP1CB)."
Barker H.M., Brewis N.D., Street A.J., Spurr N.K., Cohen P.T.W.
Biochim. Biophys. Acta 1220:212-218(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular and linkage analysis of type-1 protein phosphatase catalytic beta-subunit gene: lack of evidence for its major role in insulin resistance in Pima Indians."
Prochazka M., Mochizuki H., Baier L.J., Cohen P.T.W., Bogardus C.
Diabetologia 38:461-466(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Characterization of the protein phosphatase 1 catalytic subunit in endothelium: involvement in contractile responses."
Verin A.D., Csortos C., Durbin S.D., Aydanyan A., Wang P., Patterson C.E., Garcia J.G.
J. Cell. Biochem. 79:113-125(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Umbilical vein.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"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. expand/collapse author list , 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].
Tissue: Cerebellum.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Endometrium.
[8]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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: Uterus.
[11]"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 2-14, ACETYLATION AT ALA-2.
Tissue: Platelet.
[12]"Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton."
Tan I., Ng C.H., Lim L., Leung T.
J. Biol. Chem. 276:21209-21216(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R12C.
[13]"Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1."
Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.
Mol. Cell. Biol. 21:6841-6850(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R15A.
[15]"Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1."
Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W., Bollen M.
J. Biol. Chem. 277:47331-47337(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R7.
[16]"A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress."
Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.
Science 307:935-939(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[17]"TIMAP is a positive regulator of pulmonary endothelial barrier function."
Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C., Olah G., Verin A.D.
Am. J. Physiol. 295:L440-L450(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R16B.
[18]"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 THR-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
[20]"Identification and characterization of a novel human PP1 phosphatase complex."
Lee J.H., You J., Dobrota E., Skalnik D.G.
J. Biol. Chem. 285:24466-24476(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, INTERACTION WITH PPP1R8.
[21]"New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion."
Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M., Aizawa S., Prescott A.R., Alessi D.R.
Sci. Signal. 3:RA25-RA25(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUAK1 AND PPP1R12A.
[22]"SUMOylation of the transcriptional co-repressor KAP1 is regulated by the serine and threonine phosphatase PP1."
Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.
Sci. Signal. 3:RA32-RA32(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM28.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock."
Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.
PLoS ONE 6:E21325-E21325(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CIRCADIAN CLOCK.
[25]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80910 mRNA. Translation: CAA56870.1.
U11005 expand/collapse EMBL AC list , U10998, U10999, U11000, U11001, U11002, U11003, U11004 Genomic DNA. Translation: AAA85093.1.
AF092905 mRNA. Translation: AAF01137.1.
CR542263 mRNA. Translation: CAG47059.1.
CR542285 mRNA. Translation: CAG47080.1.
BT019744 mRNA. Translation: AAV38549.1.
AK312329 mRNA. Translation: BAG35251.1.
BX647970 mRNA. No translation available.
AC097724 Genomic DNA. Translation: AAY24124.1.
CH471053 Genomic DNA. Translation: EAX00527.1.
CH471053 Genomic DNA. Translation: EAX00528.1.
CH471053 Genomic DNA. Translation: EAX00529.1.
CH471053 Genomic DNA. Translation: EAX00530.1.
BC002697 mRNA. Translation: AAH02697.1.
BC012045 mRNA. Translation: AAH12045.1.
CCDSCCDS33169.1.
PIRS41052.
RefSeqNP_002700.1. NM_002709.2.
NP_996759.1. NM_206876.1.
UniGeneHs.702907.

3D structure databases

ProteinModelPortalP62140.
SMRP62140. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111494. 59 interactions.
IntActP62140. 35 interactions.
MINTMINT-208135.
STRING9606.ENSP00000296122.

Chemistry

BindingDBP62140.

PTM databases

PhosphoSiteP62140.

Polymorphism databases

DMDM49065814.

2D gel databases

OGPP37140.

Proteomic databases

MaxQBP62140.
PaxDbP62140.
PRIDEP62140.

Protocols and materials databases

DNASU5500.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296122; ENSP00000296122; ENSG00000213639.
ENST00000358506; ENSP00000351298; ENSG00000213639.
ENST00000395366; ENSP00000378769; ENSG00000213639.
GeneID5500.
KEGGhsa:5500.
UCSCuc002rmg.3. human.

Organism-specific databases

CTD5500.
GeneCardsGC02P028974.
HGNCHGNC:9282. PPP1CB.
HPACAB022558.
MIM600590. gene.
neXtProtNX_P62140.
PharmGKBPA33610.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172697.
HOVERGENHBG000216.
InParanoidP62140.
KOK06269.
OMAPDLQGME.
PhylomeDBP62140.
TreeFamTF354243.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP62140.
BgeeP62140.
CleanExHS_PPP1CB.
GenevestigatorP62140.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP1CB. human.
GeneWikiPPP1CB.
GenomeRNAi5500.
NextBio21280.
PROP62140.
SOURCESearch...

Entry information

Entry namePP1B_HUMAN
AccessionPrimary (citable) accession number: P62140
Secondary accession number(s): B2R5V4 expand/collapse secondary AC list , D6W565, P37140, Q5U087, Q6FG45
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 125 of the entry and version 3 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM