CTCF_HUMAN - dbPTM
CTCF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTCF_HUMAN
UniProt AC P49711
Protein Name Transcriptional repressor CTCF
Gene Name CTCF
Organism Homo sapiens (Human).
Sequence Length 727
Subcellular Localization Nucleus, nucleoplasm . Chromosome . Chromosome, centromere . May translocate to the nucleolus upon cell differentiation. Associates with both centromeres and chromosomal arms during metaphase. Associates with the H19 ICR in mitotic chromosomes. May b
Protein Description Chromatin binding factor that binds to DNA sequence specific sites. Involved in transcriptional regulation by binding to chromatin insulators and preventing interaction between promoter and nearby enhancers and silencers. Acts as transcriptional repressor binding to promoters of vertebrate MYC gene and BAG1 gene. Also binds to the PLK and PIM1 promoters. Acts as a transcriptional activator of APP. Regulates APOA1/C3/A4/A5 gene cluster and controls MHC class II gene expression. Plays an essential role in oocyte and preimplantation embryo development by activating or repressing transcription. Seems to act as tumor suppressor. Plays a critical role in the epigenetic regulation. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, binding within the H19 imprinting control region (ICR) mediates maternally inherited higher-order chromatin conformation to restrict enhancer access to IGF2. Plays a critical role in gene silencing over considerable distances in the genome. Preferentially interacts with unmethylated DNA, preventing spreading of CpG methylation and maintaining methylation-free zones. Inversely, binding to target sites is prevented by CpG methylation. Plays a important role in chromatin remodeling. Can dimerize when it is bound to different DNA sequences, mediating long-range chromatin looping. Mediates interchromosomal association between IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a common transcription factory. Causes local loss of histone acetylation and gain of histone methylation in the beta-globin locus, without affecting transcription. When bound to chromatin, it provides an anchor point for nucleosomes positioning. Seems to be essential for homologous X-chromosome pairing. May participate with Tsix in establishing a regulatable epigenetic switch for X chromosome inactivation. May play a role in preventing the propagation of stable methylation at the escape genes from X- inactivation. Involved in sister chromatid cohesion. Associates with both centromeres and chromosomal arms during metaphase and required for cohesin localization to CTCF sites. Regulates asynchronous replication of IGF2/H19. Plays a role in the recruitment of CENPE to the pericentromeric/centromeric regions of the chromosome during mitosis. [PubMed: 26321640]
Protein Sequence MEGDAVEAIVEESETFIKGKERKTYQRRREGGQEEDACHLPQNQTDGGEVVQDVNSSVQMVMMEQLDPTLLQMKTEVMEGTVAPEAEAAVDDTQIITLQVVNMEEQPINIGELQLVQVPVPVTVPVATTSVEELQGAYENEVSKEGLAESEPMICHTLPLPEGFQVVKVGANGEVETLEQGELPPQEDPSWQKDPDYQPPAKKTKKTKKSKLRYTEEGKDVDVSVYDFEEEQQEGLLSEVNAEKVVGNMKPPKPTKIKKKGVKKTFQCELCSYTCPRRSNLDRHMKSHTDERPHKCHLCGRAFRTVTLLRNHLNTHTGTRPHKCPDCDMAFVTSGELVRHRRYKHTHEKPFKCSMCDYASVEVSKLKRHIRSHTGERPFQCSLCSYASRDTYKLKRHMRTHSGEKPYECYICHARFTQSGTMKMHILQKHTENVAKFHCPHCDTVIARKSDLGVHLRKQHSYIEQGKKCRYCDAVFHERYALIQHQKSHKNEKRFKCDQCDYACRQERHMIMHKRTHTGEKPYACSHCDKTFRQKQLLDMHFKRYHDPNFVPAAFVCSKCGKTFTRRNTMARHADNCAGPDGVEGENGGETKKSKRGRKRKMRSKKEDSSDSENAEPDLDDNEDEEEPAVEIEPEPEPQPVTPAPPPAKKRRGRPPGRTNQPKQNQPTAIIQVEDQNTGAIENIIVEVKKEPDAEPAEGEEEEAQPAATDAPNGDLTPEMILSMMDR
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
1Acetylation-------MEGDAVEA
-------CCCCHHHH		13.5022814378
13PhosphorylationVEAIVEESETFIKGK
HHHHHHHHHHHHCCC		28.5620860994
15PhosphorylationAIVEESETFIKGKER
HHHHHHHHHHCCCCC		39.6821955146
18AcetylationEESETFIKGKERKTY
HHHHHHHCCCCCHHH		60.7919608861
18SumoylationEESETFIKGKERKTY
HHHHHHHCCCCCHHH		60.7928112733
20AcetylationSETFIKGKERKTYQR
HHHHHCCCCCHHHHH		49.717959783
74SumoylationDPTLLQMKTEVMEGT
CHHHHHHCHHHHCCC		28.68-
74SumoylationDPTLLQMKTEVMEGT
CHHHHHHCHHHHCCC		28.68-
138PhosphorylationVEELQGAYENEVSKE
HHHHHHHHHCCCCCC		26.5526074081
143PhosphorylationGAYENEVSKEGLAES
HHHHCCCCCCCCCCC		20.8626074081
150PhosphorylationSKEGLAESEPMICHT
CCCCCCCCCCEEEEE		41.2027050516
157PhosphorylationSEPMICHTLPLPEGF
CCCEEEEECCCCCCC		26.1728348404
177PhosphorylationGANGEVETLEQGELP
CCCCEEEEECCCCCC		40.5526714015
197PhosphorylationSWQKDPDYQPPAKKT
CCCCCCCCCCCCCCC		28.4525159151
214PhosphorylationTKKSKLRYTEEGKDV
CCCCCCCCCCCCCEE		29.0128122231
215PhosphorylationKKSKLRYTEEGKDVD
CCCCCCCCCCCCEEE		22.5628122231
215UbiquitinationKKSKLRYTEEGKDVD
CCCCCCCCCCCCEEE		22.5621890473
219SumoylationLRYTEEGKDVDVSVY
CCCCCCCCEEEEEEE		58.8328112733
219AcetylationLRYTEEGKDVDVSVY
CCCCCCCCEEEEEEE		58.8326051181
224PhosphorylationEGKDVDVSVYDFEEE
CCCEEEEEEEECHHH		15.5330576142
226PhosphorylationKDVDVSVYDFEEEQQ
CEEEEEEEECHHHHH		13.8629523821
259UbiquitinationPKPTKIKKKGVKKTF
CCCCCCCCCCCCCEE		59.2321890473
272PhosphorylationTFQCELCSYTCPRRS
EEEEEECCCCCCCCC		35.7828152594
273PhosphorylationFQCELCSYTCPRRSN
EEEEECCCCCCCCCC		16.0328152594
274PhosphorylationQCELCSYTCPRRSNL
EEEECCCCCCCCCCH		10.3528152594
279PhosphorylationSYTCPRRSNLDRHMK
CCCCCCCCCHHHHHH		42.9221955146
287PhosphorylationNLDRHMKSHTDERPH
CHHHHHHHCCCCCCH		24.8420068231
289PhosphorylationDRHMKSHTDERPHKC
HHHHHHCCCCCCHHH		46.8030576142
305PhosphorylationLCGRAFRTVTLLRNH
CCCCHHHHHHHHHHH		16.05-
307PhosphorylationGRAFRTVTLLRNHLN
CCHHHHHHHHHHHHH		21.33-
315PhosphorylationLLRNHLNTHTGTRPH
HHHHHHHCCCCCCCC		27.4627732954
317PhosphorylationRNHLNTHTGTRPHKC
HHHHHCCCCCCCCCC		37.9020068231
319PhosphorylationHLNTHTGTRPHKCPD
HHHCCCCCCCCCCCC		42.0327732954
333PhosphorylationDCDMAFVTSGELVRH
CCCEEEEECCHHHHC		25.2620068231
334PhosphorylationCDMAFVTSGELVRHR
CCEEEEECCHHHHCC		25.6020068231
343PhosphorylationELVRHRRYKHTHEKP
HHHHCCCCCCCCCCC		13.6928152594
346PhosphorylationRHRRYKHTHEKPFKC
HCCCCCCCCCCCCCC		27.8128152594
349AcetylationRYKHTHEKPFKCSMC
CCCCCCCCCCCCCCC		48.4226051181
352MethylationHTHEKPFKCSMCDYA
CCCCCCCCCCCCCCE		33.65-
372PhosphorylationKLKRHIRSHTGERPF
HHHHHHHHCCCCCCC		25.4628152594
374PhosphorylationKRHIRSHTGERPFQC
HHHHHHCCCCCCCCC		41.8225159151
382PhosphorylationGERPFQCSLCSYASR
CCCCCCCCCCCCCCC		22.9422817900
400PhosphorylationKLKRHMRTHSGEKPY
HHHHHHHHCCCCCCE		16.9020068231
402PhosphorylationKRHMRTHSGEKPYEC
HHHHHHCCCCCCEEE		48.2920201521
407PhosphorylationTHSGEKPYECYICHA
HCCCCCCEEEEEEEE		29.6928152594
410PhosphorylationGEKPYECYICHARFT
CCCCEEEEEEEEEEE		8.4728152594
417PhosphorylationYICHARFTQSGTMKM
EEEEEEEECCCCEEE		19.1030576142
419PhosphorylationCHARFTQSGTMKMHI
EEEEEECCCCEEEEE		32.9227732954
421PhosphorylationARFTQSGTMKMHILQ
EEEECCCCEEEEEHH		20.9027732954
423UbiquitinationFTQSGTMKMHILQKH
EECCCCEEEEEHHHH		27.45-
429UbiquitinationMKMHILQKHTENVAK
EEEEEHHHHHCCCHH		49.39-
431PhosphorylationMHILQKHTENVAKFH
EEEHHHHHCCCHHHC		35.9720068231
436AcetylationKHTENVAKFHCPHCD
HHHCCCHHHCCCCCC		31.2126051181
436UbiquitinationKHTENVAKFHCPHCD
HHHCCCHHHCCCCCC		31.21-
449UbiquitinationCDTVIARKSDLGVHL
CCEEEEEHHHCCCCC		39.02-
450PhosphorylationDTVIARKSDLGVHLR
CEEEEEHHHCCCCCH		32.3025159151
458UbiquitinationDLGVHLRKQHSYIEQ
HCCCCCHHHCHHHHC		59.74-
461PhosphorylationVHLRKQHSYIEQGKK
CCCHHHCHHHHCCCC		25.8829496963
462PhosphorylationHLRKQHSYIEQGKKC
CCHHHCHHHHCCCCC		13.3225159151
480PhosphorylationDAVFHERYALIQHQK
CHHHHHHHHHHHHHH		11.6328152594
487UbiquitinationYALIQHQKSHKNEKR
HHHHHHHHHHCCCCC		53.02-
496UbiquitinationHKNEKRFKCDQCDYA
HCCCCCCCCCHHHHH		40.72-
516PhosphorylationHMIMHKRTHTGEKPY
HEEEECCCCCCCCCC		28.7029083192
518PhosphorylationIMHKRTHTGEKPYAC
EEECCCCCCCCCCCC		46.5629496963
521AcetylationKRTHTGEKPYACSHC
CCCCCCCCCCCCCCC		44.6826051181
523PhosphorylationTHTGEKPYACSHCDK
CCCCCCCCCCCCCCC		31.1628111955
526PhosphorylationGEKPYACSHCDKTFR
CCCCCCCCCCCCCHH		20.9822067460
543UbiquitinationQLLDMHFKRYHDPNF
HHHHHHHHHHCCCCC		37.0521890473
545PhosphorylationLDMHFKRYHDPNFVP
HHHHHHHHCCCCCCC		15.92-
558PhosphorylationVPAAFVCSKCGKTFT
CCHHHEECCCCCCCC		26.1920068231
559AcetylationPAAFVCSKCGKTFTR
CHHHEECCCCCCCCH		41.7125953088
592AcetylationGENGGETKKSKRGRK
CCCCCCCCCCHHHHH		51.2326051181
604PhosphorylationGRKRKMRSKKEDSSD
HHHHHHHCCCCCCCC		44.5823927012
609PhosphorylationMRSKKEDSSDSENAE
HHCCCCCCCCCCCCC		36.8223927012
610PhosphorylationRSKKEDSSDSENAEP
HCCCCCCCCCCCCCC		58.4323927012
612PhosphorylationKKEDSSDSENAEPDL
CCCCCCCCCCCCCCC		34.4023927012
642PhosphorylationEPEPQPVTPAPPPAK
CCCCCCCCCCCCCCC		22.0323927012
689SumoylationENIIVEVKKEPDAEP
EEEEEEEECCCCCCC		37.6028112733
689SumoylationENIIVEVKKEPDAEP
EEEEEEEECCCCCCC		37.60-
709PhosphorylationEEAQPAATDAPNGDL
HHHCCCCCCCCCCCC		34.5030108239
717PhosphorylationDAPNGDLTPEMILSM
CCCCCCCCHHHHHHH		23.1825159151
723PhosphorylationLTPEMILSMMDR---
CCHHHHHHHHCC---		10.9230108239
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 CTCF_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
74KSumoylation

-
689KSumoylation

25218447
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 CTCF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YBOX1_HUMANYBX1physical
10906122
CHD8_HUMANCHD8physical
16949368
SUZ12_HUMANSUZ12physical
18662993
RPB1_HUMANPOLR2Aphysical
17210645
SIN3A_HUMANSIN3Aphysical
10734189
SMAD3_HUMANSMAD3physical
20427289
RXRA_HUMANRXRAphysical
20404925
PARP1_HUMANPARP1physical
20038529
NPM_HUMANNPM1physical
14759373
TOP2A_HUMANTOP2Aphysical
14759373
PARP1_HUMANPARP1physical
14759373
LMNA_HUMANLMNAphysical
14759373
IMA3_HUMANKPNA4physical
14759373
IMA1_HUMANKPNA2physical
14759373
H2A2C_HUMANHIST2H2ACphysical
14759373
H2AZ_HUMANH2AFZphysical
14759373
SUZ12_HUMANSUZ12physical
21536749
ZMYM2_HUMANZMYM2physical
22939629
KANL1_HUMANKANSL1physical
22939629
TOP2B_HUMANTOP2Bphysical
19450526
NPM_HUMANNPM1physical
19450526
PARP1_HUMANPARP1physical
19450526
NUCL_HUMANNCLphysical
19450526
SET_HUMANSETphysical
14759373
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615502Mental retardation, autosomal dominant 21 (MRD21)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTCF_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-374; SER-402; SER-609;SER-610 AND SER-612, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609; SER-610 ANDSER-612, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-374, AND MASSSPECTROMETRY.

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