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Protein

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Gene

PPP1CB

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

Functioni

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. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208).3 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
[Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

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.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Manganese 1By similarity
Metal bindingi65 – 651Manganese 1By similarity
Metal bindingi91 – 911Manganese 1By similarity
Metal bindingi91 – 911Manganese 2By similarity
Metal bindingi123 – 1231Manganese 2By similarity
Active sitei124 – 1241Proton donorBy similarity
Metal bindingi172 – 1721Manganese 2By similarity
Metal bindingi247 – 2471Manganese 2By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • myosin-light-chain-phosphatase activity Source: UniProtKB
  • myosin phosphatase activity Source: UniProtKB
  • phosphatase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_24941. Circadian Clock.
REACT_355192. RHO GTPases Activate ROCKs.
REACT_355347. RHO GTPases activate PAKs.
REACT_355542. RHO GTPases activate PKNs.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-beta catalytic subunit (EC:3.1.3.16, EC:3.1.3.53)
Short name:
PP-1B
Short name:
PPP1CD
Gene namesi
Name:PPP1CB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9282. PPP1CB.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication
  • Nucleusnucleoplasm 1 Publication
  • Nucleusnucleolus 1 Publication

  • 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.

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • glycogen granule Source: Ensembl
  • MLL5-L complex Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein phosphatase type 1 complex Source: Ensembl
  • PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33610.

Polymorphism and mutation databases

BioMutaiPPP1CB.
DMDMi49065814.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 327326Serine/threonine-protein phosphatase PP1-beta catalytic subunitPRO_0000058779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei316 – 3161Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP62140.
PRIDEiP62140.

2D gel databases

OGPiP37140.

PTM databases

DEPODiP62140.
PhosphoSiteiP62140.

Expressioni

Inductioni

Up-regulated in synovial fluid mononuclear cells and peripheral blood mononuclear cells from patients with rheumatoid arthritis.1 Publication

Gene expression databases

BgeeiP62140.
CleanExiHS_PPP1CB.
ExpressionAtlasiP62140. baseline and differential.
GenevestigatoriP62140.

Organism-specific databases

HPAiCAB022558.
CAB069426.

Interactioni

Subunit structurei

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. Interacts with FOXP3.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA1P383983EBI-352350,EBI-349905
ClockO087852EBI-352350,EBI-79859From a different organism.
CSRNP2Q9H1753EBI-352350,EBI-5235958
PPP1R16AQ96I344EBI-352350,EBI-710402
PPP1R2P3Q6NXS13EBI-352350,EBI-10251630
PPP1R3CQ9UQK13EBI-352350,EBI-2506727
SH2D4AQ9H7885EBI-352350,EBI-747035
TP53BP2Q13625-33EBI-352350,EBI-10175039

Protein-protein interaction databases

BioGridi111494. 68 interactions.
IntActiP62140. 41 interactions.
MINTiMINT-208135.
STRINGi9606.ENSP00000296122.

Structurei

3D structure databases

ProteinModelPortaliP62140.
SMRiP62140. Positions 1-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP62140.
KOiK06269.
OMAiRSCRTGK.
PhylomeDBiP62140.
TreeFamiTF354243.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62140-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI
60 70 80 90 100
LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL
110 120 130 140 150
ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT
160 170 180 190 200
FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL
210 220 230 240 250
CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV
260 270 280 290 300
EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
310 320
KAKYQYGGLN SGRPVTPPRT ANPPKKR
Length:327
Mass (Da):37,187
Last modified:January 23, 2007 - v3
Checksum:iE8356022E9B94ECD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511L → P in AAV38549 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80910 mRNA. Translation: CAA56870.1.
U11005
, 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.
CCDSiCCDS33169.1.
PIRiS41052.
RefSeqiNP_002700.1. NM_002709.2.
NP_996759.1. NM_206876.1.
UniGeneiHs.702907.

Genome annotation databases

EnsembliENST00000296122; ENSP00000296122; ENSG00000213639.
ENST00000358506; ENSP00000351298; ENSG00000213639.
ENST00000395366; ENSP00000378769; ENSG00000213639.
GeneIDi5500.
KEGGihsa:5500.
UCSCiuc002rmg.3. human.

Cross-referencesi

Web resourcesi

Protein Spotlight

The things we forget - Issue 32 of March 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80910 mRNA. Translation: CAA56870.1.
U11005
, 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.
CCDSiCCDS33169.1.
PIRiS41052.
RefSeqiNP_002700.1. NM_002709.2.
NP_996759.1. NM_206876.1.
UniGeneiHs.702907.

3D structure databases

ProteinModelPortaliP62140.
SMRiP62140. Positions 1-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111494. 68 interactions.
IntActiP62140. 41 interactions.
MINTiMINT-208135.
STRINGi9606.ENSP00000296122.

PTM databases

DEPODiP62140.
PhosphoSiteiP62140.

Polymorphism and mutation databases

BioMutaiPPP1CB.
DMDMi49065814.

2D gel databases

OGPiP37140.

Proteomic databases

PaxDbiP62140.
PRIDEiP62140.

Protocols and materials databases

DNASUi5500.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296122; ENSP00000296122; ENSG00000213639.
ENST00000358506; ENSP00000351298; ENSG00000213639.
ENST00000395366; ENSP00000378769; ENSG00000213639.
GeneIDi5500.
KEGGihsa:5500.
UCSCiuc002rmg.3. human.

Organism-specific databases

CTDi5500.
GeneCardsiGC02P028974.
HGNCiHGNC:9282. PPP1CB.
HPAiCAB022558.
CAB069426.
MIMi600590. gene.
neXtProtiNX_P62140.
PharmGKBiPA33610.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP62140.
KOiK06269.
OMAiRSCRTGK.
PhylomeDBiP62140.
TreeFamiTF354243.

Enzyme and pathway databases

ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_24941. Circadian Clock.
REACT_355192. RHO GTPases Activate ROCKs.
REACT_355347. RHO GTPases activate PAKs.
REACT_355542. RHO GTPases activate PKNs.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

ChiTaRSiPPP1CB. human.
GeneWikiiPPP1CB.
GenomeRNAii5500.
NextBioi21280.
PROiP62140.
SOURCEiSearch...

Gene expression databases

BgeeiP62140.
CleanExiHS_PPP1CB.
ExpressionAtlasiP62140. baseline and differential.
GenevestigatoriP62140.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. 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. 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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  26. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  27. "Phosphorylation of FOXP3 controls regulatory T cell function and is inhibited by TNF-alpha in rheumatoid arthritis."
    Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L., Chen X., Wan B., Chin Y.E., Zhang J.Z.
    Nat. Med. 19:322-328(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FOXP3, INDUCTION.

Entry informationi

Entry nameiPP1B_HUMAN
AccessioniPrimary (citable) accession number: P62140
Secondary accession number(s): B2R5V4
, D6W565, P37140, Q5U087, Q6FG45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 135 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. 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.