PCGF6_HUMAN - dbPTM
PCGF6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCGF6_HUMAN
UniProt AC Q9BYE7
Protein Name Polycomb group RING finger protein 6
Gene Name PCGF6
Organism Homo sapiens (Human).
Sequence Length 350
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor. [PubMed: 12167161 May modulate the levels of histone H3K4Me3 by activating KDM5D histone demethylase]
Protein Sequence MEGVAVVTAGSVGAAKTEGAAALPPPPPVSPPALTPAPAAGEEGPAPLSETGAPGCSGSRPPELEPERSLGRFRGRFEDEDEELEEEEELEEEEEEEEEDMSHFSLRLEGGRQDSEDEEERLINLSELTPYILCSICKGYLIDATTITECLHTFCKSCIVRHFYYSNRCPKCNIVVHQTQPLYNIRLDRQLQDIVYKLVINLEEREKKQMHDFYKERGLEVPKPAVPQPVPSSKGRSKKVLESVFRIPPELDMSLLLEFIGANEGTGHFKPLEKKFVRVSGEATIGHVEKFLRRKMGLDPACQVDIICGDHLLEQYQTLREIRRAIGDAAMQDGLLVLHYGLVVSPLKIT
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
8PhosphorylationMEGVAVVTAGSVGAA
CCCEEEEEECCCCCC
20.78-
30PhosphorylationLPPPPPVSPPALTPA
CCCCCCCCCCCCCCC
30.8226074081
30 (in isoform 3)Phosphorylation-30.82-
35PhosphorylationPVSPPALTPAPAAGE
CCCCCCCCCCCCCCC
21.3622210691
102PhosphorylationEEEEEDMSHFSLRLE
HHHHHHHCCHHEEEC
33.43-
105PhosphorylationEEDMSHFSLRLEGGR
HHHHCCHHEEECCCC
13.73-
115PhosphorylationLEGGRQDSEDEEERL
ECCCCCCCCCHHHHH
38.3129255136
115 (in isoform 3)Phosphorylation-38.31-
126PhosphorylationEERLINLSELTPYIL
HHHHHCHHHHHHHHH
26.5222210691
129PhosphorylationLINLSELTPYILCSI
HHCHHHHHHHHHHHH
15.2521406692
131PhosphorylationNLSELTPYILCSICK
CHHHHHHHHHHHHHC
10.9921406692
135PhosphorylationLTPYILCSICKGYLI
HHHHHHHHHHCCCCC
27.8121406692
145PhosphorylationKGYLIDATTITECLH
CCCCCCCHHHHHHHH
18.2527251275
146PhosphorylationGYLIDATTITECLHT
CCCCCCHHHHHHHHH
27.8527251275
148PhosphorylationLIDATTITECLHTFC
CCCCHHHHHHHHHHH
20.6727251275
153PhosphorylationTITECLHTFCKSCIV
HHHHHHHHHHHHHHH
20.1327251275
164PhosphorylationSCIVRHFYYSNRCPK
HHHHHHHHCCCCCCC
10.40-
205 (in isoform 3)Phosphorylation-52.22-
208UbiquitinationNLEEREKKQMHDFYK
CHHHHHHHHHHHHHH
48.3727667366
209 (in isoform 3)Phosphorylation-45.57-
214PhosphorylationKKQMHDFYKERGLEV
HHHHHHHHHHCCCCC
20.2826074081
215 (in isoform 3)Ubiquitination-40.7121890473
215UbiquitinationKQMHDFYKERGLEVP
HHHHHHHHHCCCCCC
40.7123000965
220UbiquitinationFYKERGLEVPKPAVP
HHHHCCCCCCCCCCC
60.6523000965
223SumoylationERGLEVPKPAVPQPV
HCCCCCCCCCCCCCC
51.2728112733
232PhosphorylationAVPQPVPSSKGRSKK
CCCCCCCCCCCCCHH
44.9425159151
233PhosphorylationVPQPVPSSKGRSKKV
CCCCCCCCCCCCHHH
32.8125159151
234UbiquitinationPQPVPSSKGRSKKVL
CCCCCCCCCCCHHHH
63.7827667366
234SumoylationPQPVPSSKGRSKKVL
CCCCCCCCCCCHHHH
63.7828112733
237PhosphorylationVPSSKGRSKKVLESV
CCCCCCCCHHHHHHH
45.5626074081
239UbiquitinationSSKGRSKKVLESVFR
CCCCCCHHHHHHHHC
53.9821890473
241 (in isoform 1)Ubiquitination-5.8021890473
280PhosphorylationEKKFVRVSGEATIGH
CCCEEEEECCEEHHH
21.9820068231
284PhosphorylationVRVSGEATIGHVEKF
EEEECCEEHHHHHHH
24.1620068231
290UbiquitinationATIGHVEKFLRRKMG
EEHHHHHHHHHHHCC
48.9223000965
292 (in isoform 1)Ubiquitination-8.4121890473
295UbiquitinationVEKFLRRKMGLDPAC
HHHHHHHHCCCCCCC
30.7723000965
345PhosphorylationLHYGLVVSPLKIT--
EEEEEEEECCCCC--
19.6226074081

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
30SPhosphorylationKinaseCDK7P50613
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
30SPhosphorylation

12167161

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 PCGF6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
E2F6_HUMANE2F6physical
11171983
LMBL2_HUMANL3MBTL2physical
21596310
RING2_HUMANRNF2physical
22325352
RING1_HUMANRING1physical
22325352
RYBP_HUMANRYBPphysical
22325352
YAF2_HUMANYAF2physical
22325352
LMBL2_HUMANL3MBTL2physical
22325352
CBX3_HUMANCBX3physical
22325352
E2F6_HUMANE2F6physical
22325352
TFDP1_HUMANTFDP1physical
22325352
WDR5_HUMANWDR5physical
22325352
MAX_HUMANMAXphysical
22325352
MGAP_HUMANMGAphysical
22325352
HDAC1_HUMANHDAC1physical
22325352
BMI1_HUMANBMI1physical
12167161
RING1_HUMANRING1physical
12167161
RING2_HUMANRNF2physical
12167161
RING2_HUMANRNF2physical
22493164
RING1_HUMANRING1physical
22493164
PEX10_HUMANPEX10physical
22493164
C170B_HUMANCEP170Bphysical
26186194
WDR76_HUMANWDR76physical
26186194
ZKSC1_HUMANZKSCAN1physical
26186194
CEP78_HUMANCEP78physical
26186194
RICTR_HUMANRICTORphysical
26186194
EFL1_HUMANEFTUD1physical
26186194
APBB1_HUMANAPBB1physical
26186194
MGAP_HUMANMGAphysical
26186194
KAISO_HUMANZBTB33physical
26186194
MSD2_HUMANMSANTD2physical
26186194
WDR5_HUMANWDR5physical
26186194
ELP3_HUMANELP3physical
26186194
DDX51_HUMANDDX51physical
26186194
RPP38_HUMANRPP38physical
26186194
EI2BB_HUMANEIF2B2physical
21516116
PNMA1_HUMANPNMA1physical
21516116
RING2_HUMANRNF2physical
26151332
PCGF6_HUMANPCGF6physical
26151332
UB2D3_HUMANUBE2D3physical
26151332
LMBL2_HUMANL3MBTL2physical
28514442
RYBP_HUMANRYBPphysical
28514442
BCORL_HUMANBCORL1physical
28514442
MGAP_HUMANMGAphysical
28514442
TFDP1_HUMANTFDP1physical
28514442
TFDP2_HUMANTFDP2physical
28514442
FBRS_HUMANFBRSphysical
28514442
RING2_HUMANRNF2physical
28514442
RING1_HUMANRING1physical
28514442
UBP33_HUMANUSP33physical
28514442
HDAC1_HUMANHDAC1physical
28514442
CBX4_HUMANCBX4physical
28514442
CBX8_HUMANCBX8physical
28514442
ZN644_HUMANZNF644physical
28514442
AUTS2_HUMANAUTS2physical
28514442
CSK22_HUMANCSNK2A2physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
CBX1_HUMANCBX1physical
28514442
UBP7_HUMANUSP7physical
28514442
HDAC2_HUMANHDAC2physical
28514442
CSK2B_HUMANCSNK2Bphysical
28514442
CBX3_HUMANCBX3physical
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 PCGF6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"MBLR, a new RING finger protein resembling mammalian Polycomb geneproducts, is regulated by cell cycle-dependent phosphorylation.";
Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., Koga H.;
Genes Cells 7:835-850(2002).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSCRIPTIONALREPRESSION, INTERACTION WITH BMI1; RING1 AND RNF2, PHOSPHORYLATION ATSER-30, MUTAGENESIS OF SER-30; SER-57; SER-59 AND SER-69, VARIANTPRO-PRO-23 INS, AND SUBCELLULAR LOCATION.

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