CTCF_MOUSE - dbPTM
CTCF_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTCF_MOUSE
UniProt AC Q61164
Protein Name Transcriptional repressor CTCF
Gene Name Ctcf
Organism Mus musculus (Mouse).
Sequence Length 736
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 (By similarity). 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 (By similarity)..
Protein Sequence MEGEAVEAIVEESETFIKGKERKTYQRRREGGQEEDACHLPQNQTDGGEVVQDVNSSVQMVMMEQLDPTLLQMKTEVMEGTVAPEAEAAVDDTQIITLQVVNMEEQPINIGELQLVQVPVPVTVPVATTSVEELQGAYENEVSKEGLAESEPMICHTLPLPEGFQVVKVGANGEVETLEQGELPPQEDSSWQKDPDYQPPAKKTKKTKKSKLRYTEEGKDVDVSVYDFEEEQQEGLLSEVNAEKVVGNMKPPKPTKIKKKGVKKTFQCELCSYTCPRRSNLDRHMKSHTDERPHKCHLCGRAFRTVTLLRNHLNTHTGTRPHKCPDCDMAFVTSGELVRHRRYKHTHEKPFKCSMCDYASVEVSKLKRHIRSHTGERPFQCSLCSYASRDTYKLKRHMRTHSGEKPYECYICHARFTQSGTMKMHILQKHTENVAKFHCPHCDTVIARKSDLGVHLRKQHSYIEQGKKCRYCDAVFHERYALIQHQKSHKNEKRFKCDQCDYACRQERHMIMHKRTHTGEKPYACSHCDKTFRQKQLLDMHFKRYHDPNFVPAAFVCSKCGKTFTRRNTMARHADNCAGPDGVEGENGGETKKSKRGRKRKMRSKKEDSSDSEENAEPDLDDNEEEEEPAVEIEPEPEPQPQPPPPPQPVAPAPPPAKKRRGRPPGRTNQPKQNQPTAIIQVEDQNTGAIENIIVEVKKEPDAEPAEGEEEEAQAATTDAPNGDLTPEMILSMMDR
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-------MEGEAVEA
-------CCCHHHHH		15.66-
20AcetylationSETFIKGKERKTYQR
HHHHHCCCCCHHHHH		49.717959791
45PhosphorylationCHLPQNQTDGGEVVQ
CCCCCCCCCCCCEEE		44.13-
74SumoylationDPTLLQMKTEVMEGT
CHHHHHHCHHHHCCC		28.68-
74SumoylationDPTLLQMKTEVMEGT
CHHHHHHCHHHHCCC		28.68-
150PhosphorylationSKEGLAESEPMICHT
CCCCCCCCCCEEEEE		41.2029514104
272PhosphorylationTFQCELCSYTCPRRS
EEEEEECCCCCCCCC		35.7826745281
273PhosphorylationFQCELCSYTCPRRSN
EEEEECCCCCCCCCC		16.0326745281
274PhosphorylationQCELCSYTCPRRSNL
EEEECCCCCCCCCCH		10.3526745281
279PhosphorylationSYTCPRRSNLDRHMK
CCCCCCCCCHHHHHH		42.9226745281
287PhosphorylationNLDRHMKSHTDERPH
CHHHHHHHCCCCCCH		24.8424719451
289PhosphorylationDRHMKSHTDERPHKC
HHHHHHCCCCCCHHH		46.8027841257
315PhosphorylationLLRNHLNTHTGTRPH
HHHHHHHCCCCCCCC		27.4624719451
317PhosphorylationRNHLNTHTGTRPHKC
HHHHHCCCCCCCCCC		37.9025338131
343PhosphorylationELVRHRRYKHTHEKP
HHHHCCCCCCCCCCC		13.69-
346PhosphorylationRHRRYKHTHEKPFKC
HCCCCCCCCCCCCCC		27.8125266776
364PhosphorylationDYASVEVSKLKRHIR
CCEEEEHHHHHHHHH		20.8223140645
372PhosphorylationKLKRHIRSHTGERPF
HHHHHHHHCCCCCCC		25.4627600695
374PhosphorylationKRHIRSHTGERPFQC
HHHHHHCCCCCCCCC		41.8225266776
400PhosphorylationKLKRHMRTHSGEKPY
HHHHHHHHCCCCCCE		16.9025777480
402PhosphorylationKRHMRTHSGEKPYEC
HHHHHHCCCCCCEEE		48.2925266776
405AcetylationMRTHSGEKPYECYIC
HHHCCCCCCEEEEEE		57.3222826441
407PhosphorylationTHSGEKPYECYICHA
HCCCCCCEEEEEEEE		29.6925777480
410PhosphorylationGEKPYECYICHARFT
CCCCEEEEEEEEEEE		8.4725777480
450PhosphorylationDTVIARKSDLGVHLR
CEEEEEHHHCCCCCH		32.3028066266
461PhosphorylationVHLRKQHSYIEQGKK
CCCHHHCHHHHCCCC		25.8827841257
496AcetylationHKNEKRFKCDQCDYA
HCCCCCCCCCHHHHH		40.7222826441
516PhosphorylationHMIMHKRTHTGEKPY
HEEEECCCCCCCCCC		28.7024719451
518PhosphorylationIMHKRTHTGEKPYAC
EEECCCCCCCCCCCC		46.5628418008
526PhosphorylationGEKPYACSHCDKTFR
CCCCCCCCCCCCCHH		20.9825266776
563PhosphorylationVCSKCGKTFTRRNTM
EECCCCCCCCHHHHH		18.6022817900
565PhosphorylationSKCGKTFTRRNTMAR
CCCCCCCCHHHHHHH		33.6722817900
569PhosphorylationKTFTRRNTMARHADN
CCCCHHHHHHHHCCC		15.4722817900
604PhosphorylationGRKRKMRSKKEDSSD
HHHHHHHCCCCCCCC		44.5824759943
609PhosphorylationMRSKKEDSSDSEENA
HHCCCCCCCCCCHHC		36.8224759943
610PhosphorylationRSKKEDSSDSEENAE
HCCCCCCCCCCHHCC		58.4324759943
612PhosphorylationKKEDSSDSEENAEPD
CCCCCCCCCHHCCCC		49.0824759943
698SumoylationENIIVEVKKEPDAEP
EEEEEEEECCCCCCC		37.60-
698SumoylationENIIVEVKKEPDAEP
EEEEEEEECCCCCCC		37.60-
717PhosphorylationEEEAQAATTDAPNGD
HHHHHHHCCCCCCCC		28.3730635358
718PhosphorylationEEAQAATTDAPNGDL
HHHHHHCCCCCCCCC		25.9930635358
726PhosphorylationDAPNGDLTPEMILSM
CCCCCCCCHHHHHHH		23.1820531401
732PhosphorylationLTPEMILSMMDR---
CCHHHHHHHHCC---		10.9230635358
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
74KSumoylation

19029252
698KSumoylation

19029252
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATRX_MOUSEAtrxphysical
20159591
TYY1_MOUSEYy1physical
17218270
LLPH_HUMANLLPHphysical
20360068
DDX21_HUMANDDX21physical
20360068
UBIM_HUMANFAUphysical
20360068
EBP2_HUMANEBNA1BP2physical
20360068
CTCF_HUMANCTCFphysical
20360068
RL1D1_HUMANRSL1D1physical
20360068
HNRPU_HUMANHNRNPUphysical
20360068
NOP2_HUMANNOP2physical
20360068
ZMYM1_HUMANZMYM1physical
20360068
RPA2_MOUSEPolr1bphysical
21059229
RPA1_MOUSEPolr1aphysical
21059229
RPA34_MOUSECd3eapphysical
21059229
RPA49_MOUSEPolr1ephysical
21059229
WDR5_MOUSEWdr5physical
21059229
KAISO_MOUSEZbtb33physical
16230345
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTCF_MOUSE

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Related Literatures of Post-Translational Modification
Sumoylation
ReferencePubMed
"The CTCF insulator protein is posttranslationally modified by SUMO.";
MacPherson M.J., Beatty L.G., Zhou W., Du M., Sadowski P.D.;
Mol. Cell. Biol. 29:714-725(2009).
Cited for: SUMOYLATION AT LYS-74 AND LYS-698, AND MUTAGENESIS OF LYS-74 ANDLYS-698.

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