PCGF1_HUMAN - dbPTM
PCGF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCGF1_HUMAN
UniProt AC Q9BSM1
Protein Name Polycomb group RING finger protein 1
Gene Name PCGF1
Organism Homo sapiens (Human).
Sequence Length 259
Subcellular Localization Nucleus .
Protein Description Component of the Polycomb group (PcG) multiprotein BCOR complex, a complex required to maintain the transcriptionally repressive state of some genes, such as BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. Transcriptional repressor that may be targeted to the DNA by BCL6; this transcription repressor activity may be related to PKC signaling pathway. Represses CDKN1A expression by binding to its promoter, and this repression is dependent on the retinoic acid response element (RARE element). Promotes cell cycle progression and enhances cell proliferation as well. May have a positive role in tumor cell growth by down-regulating CDKN1A. 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 MASPQGGQIAIAMRLRNQLQSVYKMDPLRNEEEVRVKIKDLNEHIVCCLCAGYFVDATTITECLHTFCKSCIVKYLQTSKYCPMCNIKIHETQPLLNLKLDRVMQDIVYKLVPGLQDSEEKRIREFYQSRGLDRVTQPTGEEPALSNLGLPFSSFDHSKAHYYRYDEQLNLCLERLSSGKDKNKSVLQNKYVRCSVRAEVRHLRRVLCHRLMLNPQHVQLLFDNEVLPDHMTMKQIWLSRWFGKPSPLLLQYSVKEKRR
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------MASPQGGQI
------CCCCCHHHH
29.8920068231
3Phosphorylation-----MASPQGGQIA
-----CCCCCHHHHH
19.2323401153
21PhosphorylationRLRNQLQSVYKMDPL
HHHHHHHHHHCCCCC
35.6928555341
24SumoylationNQLQSVYKMDPLRNE
HHHHHHHCCCCCCCH
34.3728112733
69UbiquitinationECLHTFCKSCIVKYL
HHHHHHHHHHHHHHH
44.1422817900
70PhosphorylationCLHTFCKSCIVKYLQ
HHHHHHHHHHHHHHH
15.4024719451
74 (in isoform 1)Ubiquitination-21.9721890473
74UbiquitinationFCKSCIVKYLQTSKY
HHHHHHHHHHHHCCC
21.9721890473
76 (in isoform 3)Ubiquitination-3.5721890473
87 (in isoform 3)Ubiquitination-3.6421890473
88SumoylationYCPMCNIKIHETQPL
CCCCCCCEEEECCHH
24.8228112733
99UbiquitinationTQPLLNLKLDRVMQD
CCHHHHCCHHHHHHH
47.4721906983
99 (in isoform 1)Ubiquitination-47.4721890473
109PhosphorylationRVMQDIVYKLVPGLQ
HHHHHHHHHHCCCCC
10.0315620699
118PhosphorylationLVPGLQDSEEKRIRE
HCCCCCCCHHHHHHH
34.3921815630
121UbiquitinationGLQDSEEKRIREFYQ
CCCCCHHHHHHHHHH
49.4227667366
146PhosphorylationTGEEPALSNLGLPFS
CCCCCCHHHCCCCCC
31.92-
158PhosphorylationPFSSFDHSKAHYYRY
CCCCCCCCHHHHHCH
33.1220068231
159UbiquitinationFSSFDHSKAHYYRYD
CCCCCCCHHHHHCHH
35.4421890473
159 (in isoform 1)Ubiquitination-35.4421890473
184UbiquitinationSSGKDKNKSVLQNKY
HCCCCCCHHHHCCCC
47.9127667366
190UbiquitinationNKSVLQNKYVRCSVR
CHHHHCCCCCHHHHH
31.9622817900
190 (in isoform 1)Ubiquitination-31.9621890473
195PhosphorylationQNKYVRCSVRAEVRH
CCCCCHHHHHHHHHH
12.2222817900

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 PCGF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCGF1_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 PCGF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCOR_HUMANBCORphysical
16943429
KDM2B_HUMANKDM2Bphysical
16943429
HSP74_HUMANHSPA4physical
16943429
RING1_HUMANRING1physical
16943429
RING2_HUMANRNF2physical
16943429
RYBP_HUMANRYBPphysical
16943429
SKP1_HUMANSKP1physical
16943429
RING2_HUMANRNF2physical
22325352
RING1_HUMANRING1physical
22325352
RYBP_HUMANRYBPphysical
22325352
YAF2_HUMANYAF2physical
22325352
SKP1_HUMANSKP1physical
22325352
BCOR_HUMANBCORphysical
22325352
BCORL_HUMANBCORL1physical
22325352
KDM2B_HUMANKDM2Bphysical
22325352
UBP7_HUMANUSP7physical
22325352
BCOR_HUMANBCORphysical
23523425
BCORL_HUMANBCORL1physical
23523425
RING1_HUMANRING1physical
22493164
RING2_HUMANRNF2physical
22493164
PCGF5_HUMANPCGF5physical
22493164
TRI55_HUMANTRIM55physical
22493164
RN125_HUMANRNF125physical
22493164
RING2_HUMANRNF2physical
26151332
PCGF1_HUMANPCGF1physical
26151332
UB2D3_HUMANUBE2D3physical
26151332
RYBP_HUMANRYBPphysical
26687479
IBTK_HUMANIBTKphysical
26687479
LTMD1_HUMANLETMD1physical
26687479
DIDO1_HUMANDIDO1physical
26687479
PCGF1_HUMANPCGF1physical
26687479
PCMD2_HUMANPCMTD2physical
26687479
NSF_HUMANNSFphysical
26687479
ERCC8_HUMANERCC8physical
26687479
NAA50_HUMANNAA50physical
26687479
UBP42_HUMANUSP42physical
26687479
SAS6_HUMANSASS6physical
26687479
FABP5_HUMANFABP5physical
26687479
ERBB3_HUMANERBB3physical
26687479
GPTC8_HUMANGPATCH8physical
26687479
DPPA4_HUMANDPPA4physical
26687479
ZN157_HUMANZNF157physical
26687479
RING2_HUMANRNF2physical
26687479
ATG13_HUMANATG13physical
26687479
USP9X_HUMANUSP9Xphysical
26687479
DPPA2_HUMANDPPA2physical
26687479
THIO_HUMANTXNphysical
26687479
CYTSB_HUMANSPECC1physical
26687479
SI1L2_HUMANSIPA1L2physical
26687479
SMRC2_HUMANSMARCC2physical
26687479
TOR3A_HUMANTOR3Aphysical
26687479
CLIP1_HUMANCLIP1physical
26687479
ATGA1_HUMANATG101physical
26687479
PGAM1_HUMANPGAM1physical
26687479
BCOR_HUMANBCORphysical
26687479
HMGA2_HUMANHMGA2physical
26687479
ING4_HUMANING4physical
26687479
ACACB_HUMANACACBphysical
26687479
MRE11_HUMANMRE11Aphysical
26687479
KDM2B_HUMANKDM2Bphysical
26687479
ELOC_HUMANTCEB1physical
26687479
PHC2_HUMANPHC2physical
26687479
HMGA1_HUMANHMGA1physical
26687479
SKP1_HUMANSKP1physical
26687479
CHM4B_HUMANCHMP4Bphysical
26687479
CCAR1_HUMANCCAR1physical
26687479
PRAM_HUMANPRAM1physical
26687479
ELP3_HUMANELP3physical
26687479
SUZ12_HUMANSUZ12physical
26687479
PATZ1_HUMANPATZ1physical
26687479
HRG_HUMANHRGphysical
26687479
DDB1_HUMANDDB1physical
26687479
RING1_HUMANRING1physical
26687479
CDK12_HUMANCDK12physical
26687479
RAB13_HUMANRAB13physical
26687479
ZGPAT_HUMANZGPATphysical
26687479
PIMT_HUMANPCMT1physical
26687479
SATB2_HUMANSATB2physical
26687479
DPOE2_HUMANPOLE2physical
26687479
TP53B_HUMANTP53BP1physical
26687479
RENT1_HUMANUPF1physical
26687479
COE1_HUMANEBF1physical
26687479
UBP7_HUMANUSP7physical
26687479
PDCD7_HUMANPDCD7physical
26687479
SSBP3_HUMANSSBP3physical
26687479
PPP6_HUMANPPP6Cphysical
26687479
RB6I2_HUMANERC1physical
26687479
PQBP1_HUMANPQBP1physical
26687479
SAP18_HUMANSAP18physical
26687479
P2R3A_HUMANPPP2R3Aphysical
26687479
TIAR_HUMANTIAL1physical
26687479
TCRG1_HUMANTCERG1physical
26687479
UBP34_HUMANUSP34physical
26687479
MDC1_HUMANMDC1physical
26687479
AKAP9_HUMANAKAP9physical
26687479
CDAN1_HUMANCDAN1physical
26687479
CRBN_HUMANCRBNphysical
26687479
GCP2_HUMANTUBGCP2physical
26687479
SRRT_HUMANSRRTphysical
26687479
ITPR3_HUMANITPR3physical
26687479
ARI1B_HUMANARID1Bphysical
26687479
BCORL_HUMANBCORL1physical
26687479
CAR14_HUMANCARD14physical
26687479
H2A1_HUMANHIST1H2AIphysical
26687479
NANOG_HUMANNANOGphysical
26687479
BMI1_HUMANBMI1physical
26687479
CBX8_HUMANCBX8physical
26687479
EZH2_HUMANEZH2physical
26687479

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 PCGF1_HUMAN

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Related Literatures of Post-Translational Modification

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