PCGF2_HUMAN - dbPTM
PCGF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCGF2_HUMAN
UniProt AC P35227
Protein Name Polycomb group RING finger protein 2
Gene Name PCGF2
Organism Homo sapiens (Human).
Sequence Length 344
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor. Binds specifically to the DNA sequence 5'-GACTNGACT-3'. Has tumor suppressor activity. May play a role in control of cell proliferation and/or neural cell development. Regulates proliferation of early T progenitor cells by maintaining expression of HES1. Also plays a role in antero-posterior specification of the axial skeleton and negative regulation of the self-renewal activity of hematopoietic stem cells (By similarity). Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. [PubMed: 26151332 Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity]
Protein Sequence MHRTTRIKITELNPHLMCALCGGYFIDATTIVECLHSFCKTCIVRYLETNKYCPMCDVQVHKTRPLLSIRSDKTLQDIVYKLVPGLFKDEMKRRRDFYAAYPLTEVPNGSNEDRGEVLEQEKGALSDDEIVSLSIEFYEGARDRDEKKGPLENGDGDKEKTGVRFLRCPAAMTVMHLAKFLRNKMDVPSKYKVEVLYEDEPLKEYYTLMDIAYIYPWRRNGPLPLKYRVQPACKRLTLATVPTPSEGTNTSGASECESVSDKAPSPATLPATSSSLPSPATPSHGSPSSHGPPATHPTSPTPPSTASGATTAANGGSLNCLQTPSSTSRGRKMTVNGAPVPPLT
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
51SumoylationVRYLETNKYCPMCDV
HHHHHHCCCCCCCCE		56.5028112733
73UbiquitinationLLSIRSDKTLQDIVY
CEECCCCCCHHHHHH		53.0021890473
81UbiquitinationTLQDIVYKLVPGLFK
CHHHHHHHHCCCCCH		31.92-
88SumoylationKLVPGLFKDEMKRRR
HHCCCCCHHHHHHHH		58.8028112733
197PhosphorylationKYKVEVLYEDEPLKE
CCEEEEEECCCCHHH		26.8926552605
205PhosphorylationEDEPLKEYYTLMDIA
CCCCHHHHEEEHHHH		10.5226552605
206PhosphorylationDEPLKEYYTLMDIAY
CCCHHHHEEEHHHHH		8.4226552605
207PhosphorylationEPLKEYYTLMDIAYI
CCHHHHEEEHHHHHH		18.0726552605
213PhosphorylationYTLMDIAYIYPWRRN
EEEHHHHHHCCCCCC		11.0026552605
215PhosphorylationLMDIAYIYPWRRNGP
EHHHHHHCCCCCCCC		5.5326552605
226UbiquitinationRNGPLPLKYRVQPAC
CCCCCCCCEECCCCC		29.13-
251PhosphorylationPSEGTNTSGASECES
CCCCCCCCCCCCCEE		34.1428985074
334PhosphorylationTSRGRKMTVNGAPVP
CCCCCEEEECCCCCC		17.5428985074
344PhosphorylationGAPVPPLT-------
CCCCCCCC-------		42.1925159151
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 PCGF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCGF2_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 PCGF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RING1_HUMANRING1physical
17936708
CBX8_HUMANCBX8physical
17936708
RING2_HUMANRNF2physical
17936708
PHC1_HUMANPHC1physical
19636380
PHC3_HUMANPHC3physical
19636380
PHC2_HUMANPHC2physical
19636380
RING2_HUMANRNF2physical
19636380
CBX4_HUMANCBX4physical
19636380
CBX2_HUMANCBX2physical
19636380
RING1_HUMANRING1physical
19636380
CBX8_HUMANCBX8physical
19636380
SPDEF_HUMANSPDEFphysical
20211142
UBP7_HUMANUSP7physical
20601937
UBP11_HUMANUSP11physical
20601937
RING2_HUMANRNF2physical
22325352
RING1_HUMANRING1physical
22325352
RYBP_HUMANRYBPphysical
22325352
YAF2_HUMANYAF2physical
22325352
PHC1_HUMANPHC1physical
22325352
PHC2_HUMANPHC2physical
22325352
PHC3_HUMANPHC3physical
22325352
CBX2_HUMANCBX2physical
22325352
CBX4_HUMANCBX4physical
22325352
CBX8_HUMANCBX8physical
22325352
SCMH1_HUMANSCMH1physical
22325352
SCML1_HUMANSCML1physical
22325352
UBC9_HUMANUBE2Iphysical
18211895
RAGP1_HUMANRANGAP1physical
18706886
LMNA_HUMANLMNAphysical
16248985
CCND2_HUMANCCND2physical
16182291
PCGF2_HUMANPCGF2physical
19727227
PCBP1_HUMANPCBP1physical
19727227
VHL_HUMANVHLphysical
21602890
HIF1A_HUMANHIF1Aphysical
21602890
TYY1_HUMANYY1physical
16624538
PHC1_HUMANPHC1physical
23523425
RING1_HUMANRING1physical
22493164
RING2_HUMANRNF2physical
22493164
RING2_HUMANRNF2physical
26151332
PCGF2_HUMANPCGF2physical
26151332
UB2D3_HUMANUBE2D3physical
26151332
UBC9_HUMANUBE2Iphysical
27030546
PHC1_HUMANPHC1physical
28514442
RYBP_HUMANRYBPphysical
28514442
CBX8_HUMANCBX8physical
28514442
CBX2_HUMANCBX2physical
28514442
SCMH1_HUMANSCMH1physical
28514442
PHC3_HUMANPHC3physical
28514442
PHC2_HUMANPHC2physical
28514442
CBX4_HUMANCBX4physical
28514442
BMI1_HUMANBMI1physical
28514442
BCORL_HUMANBCORL1physical
28514442
KLH25_HUMANKLHL25physical
28514442
RING2_HUMANRNF2physical
28514442
RING1_HUMANRING1physical
28514442
CBX7_HUMANCBX7physical
28514442
CBX6_HUMANCBX6physical
28514442
TPM2_HUMANTPM2physical
28514442
NFS1_HUMANNFS1physical
28514442
GOPC_HUMANGOPCphysical
28514442
PDP1_HUMANPDP1physical
28514442
LTV1_HUMANLTV1physical
28514442
LANC2_HUMANLANCL2physical
28514442
NUCG_HUMANENDOGphysical
28514442
SCML1_HUMANSCML1physical
28514442
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 PCGF2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-344, AND MASSSPECTROMETRY.

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