PP1B_HUMAN - dbPTM
PP1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP1B_HUMAN
UniProt AC P62140
Protein Name Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Gene Name PPP1CB
Organism Homo sapiens (Human).
Sequence Length 327
Subcellular Localization Cytoplasm . Nucleus . Nucleus, nucleoplasm . Nucleus, nucleolus . 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.
Protein Description 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]
Protein Sequence MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRTANPPKKR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MADGELNVD
------CCCCCCCHH
33.2522223895
10PhosphorylationDGELNVDSLITRLLE
CCCCCHHHHHHHHHH
19.8624719451
13PhosphorylationLNVDSLITRLLEVRG
CCHHHHHHHHHHHCC
22.1324961811
19MethylationITRLLEVRGCRPGKI
HHHHHHHCCCCCCCE
29.17115488403
25AcetylationVRGCRPGKIVQMTEA
HCCCCCCCEEEEEHH
42.2423954790
25UbiquitinationVRGCRPGKIVQMTEA
HCCCCCCCEEEEEHH
42.24-
25MalonylationVRGCRPGKIVQMTEA
HCCCCCCCEEEEEHH
42.2426320211
29SulfoxidationRPGKIVQMTEAEVRG
CCCCEEEEEHHHHHC
2.2421406390
35MethylationQMTEAEVRGLCIKSR
EEEHHHHHCCEECCC
24.70115488395
40UbiquitinationEVRGLCIKSREIFLS
HHHCCEECCCCHHHC
42.33-
41PhosphorylationVRGLCIKSREIFLSQ
HHCCEECCCCHHHCC
18.4228450419
47PhosphorylationKSREIFLSQPILLEL
CCCCHHHCCCEEEEE
24.1428450419
59UbiquitinationLELEAPLKICGDIHG
EEEHHHHHHCCCCCC
34.59-
92PhosphorylationNYLFLGDYVDRGKQS
CEEEHHHHCHHCHHH
11.49-
97UbiquitinationGDYVDRGKQSLETIC
HHHCHHCHHHHHHHH
37.2921890473
112UbiquitinationLLLAYKIKYPENFFL
HHHHHHCCCCCCEEE
51.0721890473
113PhosphorylationLLAYKIKYPENFFLL
HHHHHCCCCCCEEEE
21.1728152594
121MethylationPENFFLLRGNHECAS
CCCEEEECCCCHHHH
46.12-
128PhosphorylationRGNHECASINRIYGF
CCCCHHHHHHHHEEC
31.8630576142
131MethylationHECASINRIYGFYDE
CHHHHHHHHEECHHH
23.10-
133PhosphorylationCASINRIYGFYDECK
HHHHHHHEECHHHHH
9.6528152594
136PhosphorylationINRIYGFYDECKRRF
HHHHEECHHHHHHHH
13.3828152594
140MalonylationYGFYDECKRRFNIKL
EECHHHHHHHHCCCH
44.5626320211
140AcetylationYGFYDECKRRFNIKL
EECHHHHHHHHCCCH
44.5623954790
140UbiquitinationYGFYDECKRRFNIKL
EECHHHHHHHHCCCH
44.5621890473
146UbiquitinationCKRRFNIKLWKTFTD
HHHHHCCCHHHHHHH
49.7721890473
146AcetylationCKRRFNIKLWKTFTD
HHHHHCCCHHHHHHH
49.7723749302
146MalonylationCKRRFNIKLWKTFTD
HHHHHCCCHHHHHHH
49.7726320211
149AcetylationRFNIKLWKTFTDCFN
HHCCCHHHHHHHHCC
44.1726051181
149UbiquitinationRFNIKLWKTFTDCFN
HHCCCHHHHHHHHCC
44.17-
149MalonylationRFNIKLWKTFTDCFN
HHCCCHHHHHHHHCC
44.1726320211
176PhosphorylationFCCHGGLSPDLQSME
EECCCCCCCCHHHHH
21.4630622161
181PhosphorylationGLSPDLQSMEQIRRI
CCCCCHHHHHHHHHH
31.4226437602
210UbiquitinationLLWSDPDKDVQGWGE
HHCCCCCCCCCCCCC
66.25-
233UbiquitinationFGADVVSKFLNRHDL
ECHHHHHHHHCHHCH
42.1121890473
254PhosphorylationHQVVEDGYEFFAKRQ
HHHHHHCHHHHHHCC
23.1428796482
259MalonylationDGYEFFAKRQLVTLF
HCHHHHHHCCEEECC
35.2026320211
259AcetylationDGYEFFAKRQLVTLF
HCHHHHHHCCEEECC
35.2019809617
259UbiquitinationDGYEFFAKRQLVTLF
HCHHHHHHCCEEECC
35.2021890473
298PhosphorylationSFQILKPSEKKAKYQ
EEEECCCCCCCCCCC
61.5326074081
303AcetylationKPSEKKAKYQYGGLN
CCCCCCCCCCCCCCC
41.5923236377
303UbiquitinationKPSEKKAKYQYGGLN
CCCCCCCCCCCCCCC
41.5921890473
304PhosphorylationPSEKKAKYQYGGLNS
CCCCCCCCCCCCCCC
16.3021945579
306PhosphorylationEKKAKYQYGGLNSGR
CCCCCCCCCCCCCCC
15.2921945579
311PhosphorylationYQYGGLNSGRPVTPP
CCCCCCCCCCCCCCC
41.0221945579
316PhosphorylationLNSGRPVTPPRTANP
CCCCCCCCCCCCCCC
30.2025159151
320PhosphorylationRPVTPPRTANPPKKR
CCCCCCCCCCCCCCC
36.2423403867

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PP1B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP1B_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PP1B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP1R7_HUMANPPP1R7physical
17353931
MYPT1_HUMANPPP1R12Aphysical
17353931
IPP2_HUMANPPP1R2physical
17353931
PP1RB_HUMANPPP1R11physical
17353931
PP1R8_HUMANPPP1R8physical
17353931
SH24A_HUMANSH2D4Aphysical
17353931
TMM33_HUMANTMEM33physical
17353931
NUCL_HUMANNCLphysical
12185196
SNF5_HUMANSMARCB1genetic
12016208
BRCA1_HUMANBRCA1physical
17511879
NCOR1_HUMANNCOR1physical
12410313
TIF1B_HUMANTRIM28physical
20424263
HDAC7_HUMANHDAC7physical
17369396
WDR82_HUMANWDR82physical
20516061
TOX4_HUMANTOX4physical
20516061
PP1RA_HUMANPPP1R10physical
20516061
NONO_HUMANNONOphysical
21566083
BCL2_HUMANBCL2physical
17274640
FAK1_HUMANPTK2physical
17274640
LBR_HUMANLBRphysical
17274640
CDN2A_HUMANCDKN2Aphysical
17274640
ARF_HUMANCDKN2Aphysical
17274640
UB2R1_HUMANCDC34physical
17274640
CCNB1_HUMANCCNB1physical
17274640
CCND1_HUMANCCND1physical
17274640
CCND3_HUMANCCND3physical
17274640
HSP74_HUMANHSPA4physical
17274640
MAX_HUMANMAXphysical
17274640
AURKA_HUMANAURKAphysical
11551964
WDR5_HUMANWDR5physical
22939629
MDM4_HUMANMDM4physical
23277204
DHX15_HUMANDHX15physical
22863883
KIME_HUMANMVKphysical
22863883
PPR3C_HUMANPPP1R3Cphysical
25416956
ASPP2_HUMANTP53BP2physical
25416956
SH24A_HUMANSH2D4Aphysical
25416956
CSRN2_HUMANCSRNP2physical
25416956
PP16A_HUMANPPP1R16Aphysical
25416956
AKT1_HUMANAKT1physical
20186153
RORG_HUMANRORCphysical
23555304
CLOCK_HUMANCLOCKphysical
23555304
DAG1_HUMANDAG1physical
26344197
PP1G_HUMANPPP1CCphysical
26344197
IPP2_HUMANPPP1R2physical
26344197
PP1R7_HUMANPPP1R7physical
26344197
SSU72_HUMANSSU72physical
26344197
PP16A_HUMANPPP1R16Aphysical
21516116
ACTS_HUMANACTA1physical
26496610
ACTB_HUMANACTBphysical
26496610
ACTG_HUMANACTG1physical
26496610
ACTN4_HUMANACTN4physical
26496610
ACTN1_HUMANACTN1physical
26496610
AP2A1_HUMANAP2A1physical
26496610
ANXA2_HUMANANXA2physical
26496610
DYST_HUMANDSTphysical
26496610
CALL3_HUMANCALML3physical
26496610
CAZA1_HUMANCAPZA1physical
26496610
CAZA2_HUMANCAPZA2physical
26496610
CAPZB_HUMANCAPZBphysical
26496610
COF1_HUMANCFL1physical
26496610
COF2_HUMANCFL2physical
26496610
CLCA_HUMANCLTAphysical
26496610
CLCB_HUMANCLTBphysical
26496610
DAB2_HUMANDAB2physical
26496610
DAPK3_HUMANDAPK3physical
26496610
DREB_HUMANDBN1physical
26496610
DDX3X_HUMANDDX3Xphysical
26496610
DHX9_HUMANDHX9physical
26496610
SRC8_HUMANCTTNphysical
26496610
EPS15_HUMANEPS15physical
26496610
FLII_HUMANFLIIphysical
26496610
FLNA_HUMANFLNAphysical
26496610
FLNB_HUMANFLNBphysical
26496610
ROA2_HUMANHNRNPA2B1physical
26496610
HNRH3_HUMANHNRNPH3physical
26496610
ILF3_HUMANILF3physical
26496610
ABLM1_HUMANABLIM1physical
26496610
LMO7_HUMANLMO7physical
26496610
MYO1B_HUMANMYO1Bphysical
26496610
MYLK_HUMANMYLKphysical
26496610
MYO1C_HUMANMYO1Cphysical
26496610
MYO1E_HUMANMYO1Ephysical
26496610
MYO5A_HUMANMYO5Aphysical
26496610
MYO5B_HUMANMYO5Bphysical
26496610
MYO6_HUMANMYO6physical
26496610
MYPT1_HUMANPPP1R12Aphysical
26496610
MYPT2_HUMANPPP1R12Bphysical
26496610
P3C2A_HUMANPIK3C2Aphysical
26496610
PLEC_HUMANPLECphysical
26496610
PP1A_HUMANPPP1CAphysical
26496610
PP1R7_HUMANPPP1R7physical
26496610
PP1R8_HUMANPPP1R8physical
26496610
PP1RA_HUMANPPP1R10physical
26496610
TWF1_HUMANTWF1physical
26496610
SAFB1_HUMANSAFBphysical
26496610
SIPA1_HUMANSIPA1physical
26496610
SPTN1_HUMANSPTAN1physical
26496610
SPTB2_HUMANSPTBN1physical
26496610
SPTN2_HUMANSPTBN2physical
26496610
SSFA2_HUMANSSFA2physical
26496610
ST5_HUMANST5physical
26496610
SVIL_HUMANSVILphysical
26496610
PP1RB_HUMANPPP1R11physical
26496610
ZO1_HUMANTJP1physical
26496610
TMOD1_HUMANTMOD1physical
26496610
BACD2_HUMANTNFAIP1physical
26496610
TPM1_HUMANTPM1physical
26496610
TPM2_HUMANTPM2physical
26496610
TPM3_HUMANTPM3physical
26496610
TPM4_HUMANTPM4physical
26496610
YES_HUMANYES1physical
26496610
LUZP1_HUMANLUZP1physical
26496610
RBP56_HUMANTAF15physical
26496610
SRBS2_HUMANSORBS2physical
26496610
RMP_HUMANURI1physical
26496610
IQGA1_HUMANIQGAP1physical
26496610
ABC3B_HUMANAPOBEC3Bphysical
26496610
SAFB2_HUMANSAFB2physical
26496610
EPN4_HUMANCLINT1physical
26496610
RHGBA_HUMANARHGAP11Aphysical
26496610
TOX4_HUMANTOX4physical
26496610
SC16A_HUMANSEC16Aphysical
26496610
WDR1_HUMANWDR1physical
26496610
ARPC4_HUMANARPC4physical
26496610
ARP3_HUMANACTR3physical
26496610
ARP2_HUMANACTR2physical
26496610
ARPC2_HUMANARPC2physical
26496610
RBM6_HUMANRBM6physical
26496610
BASP1_HUMANBASP1physical
26496610
GA2L1_HUMANGAS2L1physical
26496610
KHDR1_HUMANKHDRBS1physical
26496610
TCPQ_HUMANCCT8physical
26496610
IASPP_HUMANPPP1R13Lphysical
26496610
DEST_HUMANDSTNphysical
26496610
TARA_HUMANTRIOBPphysical
26496610
AKAP2_HUMANAKAP2physical
26496610
SYNPO_HUMANSYNPOphysical
26496610
SIR2_HUMANSIRT2physical
26496610
LIMC1_HUMANLIMCH1physical
26496610
SI1L3_HUMANSIPA1L3physical
26496610
MPRIP_HUMANMPRIPphysical
26496610
COBL_HUMANCOBLphysical
26496610
CYTSA_HUMANSPECC1Lphysical
26496610
COR1C_HUMANCORO1Cphysical
26496610
ZDHC5_HUMANZDHHC5physical
26496610
PKHG3_HUMANPLEKHG3physical
26496610
RAI14_HUMANRAI14physical
26496610
TES_HUMANTESphysical
26496610
RBMX_HUMANRBMXphysical
26496610
ZN638_HUMANZNF638physical
26496610
RGAP1_HUMANRACGAP1physical
26496610
TMOD3_HUMANTMOD3physical
26496610
LIMA1_HUMANLIMA1physical
26496610
PP12C_HUMANPPP1R12Cphysical
26496610
PIHD1_HUMANPIH1D1physical
26496610
UACA_HUMANUACAphysical
26496610
RIF1_HUMANRIF1physical
26496610
BMP2K_HUMANBMP2Kphysical
26496610
MYO5C_HUMANMYO5Cphysical
26496610
YLPM1_HUMANYLPM1physical
26496610
COR1B_HUMANCORO1Bphysical
26496610
RHG21_HUMANARHGAP21physical
26496610
NCOA5_HUMANNCOA5physical
26496610
AFAP1_HUMANAFAP1physical
26496610
SH24A_HUMANSH2D4Aphysical
26496610
ZN106_HUMANZNF106physical
26496610
INF2_HUMANINF2physical
26496610
MET17_HUMANMETTL17physical
26496610
MYO19_HUMANMYO19physical
26496610
PDRG1_HUMANPDRG1physical
26496610
NEB2_HUMANPPP1R9Bphysical
26496610
K1671_HUMANKIAA1671physical
26496610
STON2_HUMANSTON2physical
26496610
SSH2_HUMANSSH2physical
26496610
NEXN_HUMANNEXNphysical
26496610
CYTSB_HUMANSPECC1physical
26496610
WDR92_HUMANWDR92physical
26496610
MISP_HUMANMISPphysical
26496610
ACTT1_HUMANACTRT1physical
26496610
KI18B_HUMANKIF18Bphysical
26496610
CDCA2_HUMANCDCA2physical
26496610
UBX2A_HUMANUBXN2Aphysical
26496610
GA2L3_HUMANGAS2L3physical
26496610
ZN326_HUMANZNF326physical
26496610
TPRN_HUMANTPRNphysical
26496610
RB12B_HUMANRBM12Bphysical
26496610
MY18A_HUMANMYO18Aphysical
26496610
RMXL1_HUMANRBMXL1physical
26496610
CC85C_HUMANCCDC85Cphysical
27880917
GSK3A_HUMANGSK3Aphysical
27880917
GSK3B_HUMANGSK3Bphysical
27880917
LRRC1_HUMANLRRC1physical
27880917
PLCL2_HUMANPLCL2physical
27880917
PP1RA_HUMANPPP1R10physical
27880917
PP1RB_HUMANPPP1R11physical
27880917
MYPT2_HUMANPPP1R12Bphysical
27880917
PP12C_HUMANPPP1R12Cphysical
27880917
ASPP1_HUMANPPP1R13Bphysical
27880917
IASPP_HUMANPPP1R13Lphysical
27880917
IPP2_HUMANPPP1R2physical
27880917
PP1R7_HUMANPPP1R7physical
27880917
PP1R8_HUMANPPP1R8physical
27880917
RAI14_HUMANRAI14physical
27880917
SCRIB_HUMANSCRIBphysical
27880917
SH24A_HUMANSH2D4Aphysical
27880917
SHOC2_HUMANSHOC2physical
27880917
TOX4_HUMANTOX4physical
27880917
ASPP2_HUMANTP53BP2physical
27880917
TARA_HUMANTRIOBPphysical
27880917
WDR82_HUMANWDR82physical
27880917
YLPM1_HUMANYLPM1physical
27880917
SFRP2_HUMANSFRP2physical
17123353
SFRP1_HUMANSFRP1physical
17123353
SFRP5_HUMANSFRP5physical
17123353
PP1R7_HUMANPPP1R7physical
27173435
RRP1B_HUMANRRP1Bphysical
27173435
CT027_HUMANC20orf27physical
27173435
PP1RB_HUMANPPP1R11physical
27173435
SH24A_HUMANSH2D4Aphysical
27173435
KI18A_HUMANKIF18Aphysical
27173435
RPAB1_HUMANPOLR2Ephysical
27173435
RMP_HUMANURI1physical
27173435
WBP11_HUMANWBP11physical
27173435
WDR92_HUMANWDR92physical
27173435
MYPT1_HUMANPPP1R12Aphysical
27173435
TLK1_HUMANTLK1physical
27173435
IASPP_HUMANPPP1R13Lphysical
27173435
RIF1_HUMANRIF1physical
27173435
CC85C_HUMANCCDC85Cphysical
27173435
RPAP3_HUMANRPAP3physical
27173435
PACS1_HUMANPACS1physical
27173435
PP1A_HUMANPPP1CAphysical
27173435
INTU_HUMANINTUphysical
27173435
2A5G_HUMANPPP2R5Cphysical
25487150

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PP1B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-316, AND MASS SPECTROMETRY.
"Exploring proteomes and analyzing protein processing by massspectrometric 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).
Cited for: PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT ALA-2.
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-47, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-316, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND MASSSPECTROMETRY.

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