PCGF3_HUMAN - dbPTM
PCGF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCGF3_HUMAN
UniProt AC Q3KNV8
Protein Name Polycomb group RING finger protein 3
Gene Name PCGF3
Organism Homo sapiens (Human).
Sequence Length 242
Subcellular Localization Nucleus . Nucleus, nucleoplasm . Recruited by the non-coding RNA Xist to specific nuclear foci that probably correspond to the inactivated X chromosome.
Protein Description 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. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity. [PubMed: 26151332 Plays a redundant role with PCGF5 as part of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females (By similarity]
Protein Sequence MLTRKIKLWDINAHITCRLCSGYLIDATTVTECLHTFCRSCLVKYLEENNTCPTCRIVIHQSHPLQYIGHDRTMQDIVYKLVPGLQEAEMRKQREFYHKLGMEVPGDIKGETCSAKQHLDSHRNGETKADDSSNKEAAEEKPEEDNDYHRSDEQVSICLECNSSKLRGLKRKWIRCSAQATVLHLKKFIAKKLNLSSFNELDILCNEEILGKDHTLKFVVVTRWRFKKAPLLLHYRPKMDLL
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
40PhosphorylationCLHTFCRSCLVKYLE
HHHHHHHHHHHHHHH
17.0024719451
73PhosphorylationQYIGHDRTMQDIVYK
HHCCCCCCHHHHHHH
25.8225690035
79PhosphorylationRTMQDIVYKLVPGLQ
CCHHHHHHHHCCCHH
10.0322817900
99UbiquitinationKQREFYHKLGMEVPG
HHHHHHHHCCCCCCC
35.04-
104 (in isoform 2)Ubiquitination-4.82-
116AcetylationKGETCSAKQHLDSHR
CCCCCCCHHHHHHCC
23.207670035
116UbiquitinationKGETCSAKQHLDSHR
CCCCCCCHHHHHHCC
23.20-
132PhosphorylationGETKADDSSNKEAAE
CCCCCCCCCCHHHHH
36.0424260401
148PhosphorylationKPEEDNDYHRSDEQV
CCCCCCCCCCCHHHE
12.8522817900
165UbiquitinationCLECNSSKLRGLKRK
EEECCCHHHCCCCHH
41.86-
212UbiquitinationCNEEILGKDHTLKFV
CCHHHCCCCCEEEEE
42.78-

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 PCGF3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCGF3_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 PCGF3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RING2_HUMANRNF2physical
22325352
RING1_HUMANRING1physical
22325352
RYBP_HUMANRYBPphysical
22325352
YAF2_HUMANYAF2physical
22325352
CBX4_HUMANCBX4physical
22325352
MGAP_HUMANMGAphysical
22325352
BCORL_HUMANBCORL1physical
22325352
KDM2B_HUMANKDM2Bphysical
22325352
UBP7_HUMANUSP7physical
22325352
AUTS2_HUMANAUTS2physical
22325352
FBRS_HUMANFBRSphysical
22325352
FBSL_HUMANFBRSL1physical
22325352
CSK21_HUMANCSNK2A1physical
22325352
CSK22_HUMANCSNK2A2physical
22325352
CSK2B_HUMANCSNK2Bphysical
22325352
BCOR_HUMANBCORphysical
23523425
BCORL_HUMANBCORL1physical
23523425
RING2_HUMANRNF2physical
22493164
BMI1_HUMANBMI1physical
22493164
RING1_HUMANRING1physical
22493164
BCOR_HUMANBCORphysical
25416956
RING2_HUMANRNF2physical
26151332
PCGF3_HUMANPCGF3physical
26151332
UB2D3_HUMANUBE2D3physical
26151332
NISCH_HUMANNISCHphysical
27173435

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 PCGF3_HUMAN

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Related Literatures of Post-Translational Modification

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