CTF18_HUMAN - dbPTM
CTF18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTF18_HUMAN
UniProt AC Q8WVB6
Protein Name Chromosome transmission fidelity protein 18 homolog
Gene Name CHTF18
Organism Homo sapiens (Human).
Sequence Length 975
Subcellular Localization Nucleus . Associates with chromatin during S phase.
Protein Description Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs and has weak ATPase activity that is stimulated by the presence of primed DNA, replication protein A (RPA) and by proliferating cell nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-dependent loading of PCNA onto primed and gapped DNA. It also interacts with and stimulates DNA polymerase POLH..
Protein Sequence MEDYEQELCGVEDDFHNQFAAELEVLAELEGASTPSPSGVPLFTAGRPPRTFEEALARGDAASSPAPAASVGSSQGGARKRQVDADLQPAGSLPHAPRIKRPRLQVVKRLNFRSEEMEEPPPPDSSPTDITPPPSPEDLAELWGHGVSEAAADVGLTRASPAARNPVLRRPPILEDYVHVTSTEGVRAYLVLRADPMAPGVQGSLLHVPWRGGGQLDLLGVSLASLKKQVDGERRERLLQEAQKLSDTLHSLRSGEEEAAQPLGAPEEEPTDGQDASSHCLWVDEFAPRHYTELLSDDFTNRCLLKWLKLWDLVVFGHERPSRKPRPSVEPARVSKEATAPGKWKSHEQVLEEMLEAGLDPSQRPKQKVALLCGPPGLGKTTLAHVIARHAGYSVVEMNASDDRSPEVFRTRIEAATQMESVLGAGGKPNCLVIDEIDGAPVAAINVLLSILNRKGPQEVGPQGPAVPSGGGRRRRAEGGLLMRPIICICNDQFAPSLRQLKQQAFLLHFPPTLPSRLVQRLQEVSLRQGMRADPGVLAALCEKTDNDIRACINTLQFLYSRGQRELSVRDVQATRVGLKDQRRGLFSVWQEVFQLPRAQRRRVGQDPALPADTLLLGDGDAGSLTSASQRFYRVLHAAASAGEHEKVVQGLFDNFLRLRLRDSSLGAVCVALDWLAFDDLLAGAAHHSQSFQLLRYPPFLPVAFHVLFASSHTPRITFPSSQQEAQNRMSQMRNLIQTLVSGIAPATRSRATPQALLLDALCLLLDILAPKLRPVSTQLYSTREKQQLASLVGTMLAYSLTYRQERTPDGQYIYRLEPNVEELCRFPELPARKPLTYQTKQLIAREIEVEKMRRAEASARVENSPQVDGSPPGLEGLLGGIGEKGVHRPAPRNHEQRLEHIMRRAAREEQPEKDFFGRVVVRSTAVPSAGDTAPEQDSVERRMGTAVGRSEVWFRFNEGVSNAVRRSLYIRDLL
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
33PhosphorylationLAELEGASTPSPSGV
HHHHCCCCCCCCCCC		52.2726074081
34PhosphorylationAELEGASTPSPSGVP
HHHCCCCCCCCCCCC		27.5326074081
36PhosphorylationLEGASTPSPSGVPLF
HCCCCCCCCCCCCCE		31.6126074081
37 (in isoform 3)Ubiquitination-35.9821906983
37UbiquitinationEGASTPSPSGVPLFT
CCCCCCCCCCCCCEE		35.9822817900
38PhosphorylationGASTPSPSGVPLFTA
CCCCCCCCCCCCEEC		57.6826074081
44PhosphorylationPSGVPLFTAGRPPRT
CCCCCCEECCCCCCC		35.5726074081
51PhosphorylationTAGRPPRTFEEALAR
ECCCCCCCHHHHHHC		40.9730266825
63PhosphorylationLARGDAASSPAPAAS
HHCCCCCCCCCCCCH		38.2829255136
64PhosphorylationARGDAASSPAPAASV
HCCCCCCCCCCCCHH		21.9829255136
70PhosphorylationSSPAPAASVGSSQGG
CCCCCCCHHCCCCCC		29.1730266825
73PhosphorylationAPAASVGSSQGGARK
CCCCHHCCCCCCHHC		19.8229255136
74PhosphorylationPAASVGSSQGGARKR
CCCHHCCCCCCHHCC		27.2417525332
92PhosphorylationADLQPAGSLPHAPRI
CCCCCCCCCCCCCCC		40.6130576142
108AcetylationRPRLQVVKRLNFRSE
CCHHHHHHHHCCCCH		52.927338451
115 (in isoform 2)Phosphorylation-58.0420068231
117 (in isoform 2)Phosphorylation-6.5820068231
121 (in isoform 2)Phosphorylation-57.2325849741
125PhosphorylationEEPPPPDSSPTDITP
CCCCCCCCCCCCCCC		43.9526029660
126PhosphorylationEPPPPDSSPTDITPP
CCCCCCCCCCCCCCC		38.9226029660
128PhosphorylationPPPDSSPTDITPPPS
CCCCCCCCCCCCCCC		41.8225921289
131PhosphorylationDSSPTDITPPPSPED
CCCCCCCCCCCCHHH		32.3325921289
135PhosphorylationTDITPPPSPEDLAEL
CCCCCCCCHHHHHHH		46.8526029660
157PhosphorylationAAADVGLTRASPAAR
HHHHHCCCCCCHHHC		20.4726074081
160PhosphorylationDVGLTRASPAARNPV
HHCCCCCCHHHCCCC		16.2826074081
204PhosphorylationMAPGVQGSLLHVPWR
CCCCCCCEEEECCCC		15.6328555341
222PhosphorylationQLDLLGVSLASLKKQ
CHHHHCEEHHHHHHH		19.2030266825
225PhosphorylationLLGVSLASLKKQVDG
HHCEEHHHHHHHCCH		46.1229255136
244UbiquitinationRLLQEAQKLSDTLHS
HHHHHHHHHHHHHHH		57.9429967540
246PhosphorylationLQEAQKLSDTLHSLR
HHHHHHHHHHHHHHH		35.2728674419
248PhosphorylationEAQKLSDTLHSLRSG
HHHHHHHHHHHHHCC		24.0120873877
251PhosphorylationKLSDTLHSLRSGEEE
HHHHHHHHHHCCCCH		28.7028555341
256 (in isoform 2)Ubiquitination-54.64-
272 (in isoform 2)Ubiquitination-64.57-
306AcetylationFTNRCLLKWLKLWDL
CHHHHHHHHHHHHHH		37.2225953088
324UbiquitinationGHERPSRKPRPSVEP
CCCCCCCCCCCCCCC		50.11-
328PhosphorylationPSRKPRPSVEPARVS
CCCCCCCCCCCCCCC		40.1528555341
335PhosphorylationSVEPARVSKEATAPG
CCCCCCCCCCCCCCC		21.1620068231
339UbiquitinationARVSKEATAPGKWKS
CCCCCCCCCCCCCCC		34.1822817900
343AcetylationKEATAPGKWKSHEQV
CCCCCCCCCCCHHHH		50.8425953088
343UbiquitinationKEATAPGKWKSHEQV
CCCCCCCCCCCHHHH		50.8429967540
345UbiquitinationATAPGKWKSHEQVLE
CCCCCCCCCHHHHHH		45.4829967540
366UbiquitinationLDPSQRPKQKVALLC
CCHHHCCCCEEEEEC		66.0129967540
368UbiquitinationPSQRPKQKVALLCGP
HHHCCCCEEEEECCC		35.2829967540
381PhosphorylationGPPGLGKTTLAHVIA
CCCCCCHHHHHHHHH		25.8320068231
382PhosphorylationPPGLGKTTLAHVIAR
CCCCCHHHHHHHHHH		25.9820068231
396 (in isoform 2)Ubiquitination-4.80-
405PhosphorylationMNASDDRSPEVFRTR
CCCCCCCCHHHHHHH		32.1923403867
423UbiquitinationATQMESVLGAGGKPN
HHHHHHHHCCCCCCC		5.6121963094
434UbiquitinationGKPNCLVIDEIDGAP
CCCCEEEEEECCCCC		2.2522817900
455UbiquitinationLLSILNRKGPQEVGP
HHHHHHCCCCCCCCC		74.0822817900
455 (in isoform 1)Ubiquitination-74.0821906983
456UbiquitinationLSILNRKGPQEVGPQ
HHHHHCCCCCCCCCC		26.3622817900
469PhosphorylationPQGPAVPSGGGRRRR
CCCCCCCCCCCCCCC		43.3921712546
483UbiquitinationRAEGGLLMRPIICIC
CCCCCCCCEEEEEEE		6.0322817900
483 (in isoform 2)Ubiquitination-6.0321906983
544UbiquitinationVLAALCEKTDNDIRA
HHHHHHHCCCHHHHH		61.25-
561PhosphorylationNTLQFLYSRGQRELS
HHHHHHHHCCCCEEE		31.8924719451
572 (in isoform 2)Ubiquitination-2.67-
575PhosphorylationSVRDVQATRVGLKDQ
EHHHHHHHCCCCHHH		14.5920068231
725UbiquitinationTFPSSQQEAQNRMSQ
CCCHHHHHHHHHHHH		44.5821963094
742PhosphorylationNLIQTLVSGIAPATR
HHHHHHHHCCCHHCC		27.8218491316
767UbiquitinationDALCLLLDILAPKLR
HHHHHHHHHHCHHCC		33.5521963094
777PhosphorylationAPKLRPVSTQLYSTR
CHHCCCCCHHHCCHH		17.0820860994
778PhosphorylationPKLRPVSTQLYSTRE
HHCCCCCHHHCCHHH		23.8720860994
783PhosphorylationVSTQLYSTREKQQLA
CCHHHCCHHHHHHHH		29.3220860994
791PhosphorylationREKQQLASLVGTMLA
HHHHHHHHHHHHHHH		31.9824043423
795PhosphorylationQLASLVGTMLAYSLT
HHHHHHHHHHHHHHH		11.0924043423
799PhosphorylationLVGTMLAYSLTYRQE
HHHHHHHHHHHCCEE		10.5524043423
800PhosphorylationVGTMLAYSLTYRQER
HHHHHHHHHHCCEEC		14.5024043423
802PhosphorylationTMLAYSLTYRQERTP
HHHHHHHHCCEECCC		15.6624043423
803PhosphorylationMLAYSLTYRQERTPD
HHHHHHHCCEECCCC		18.6524043423
820UbiquitinationYIYRLEPNVEELCRF
EEEEECCCHHHHHCC		44.4421963094
834UbiquitinationFPELPARKPLTYQTK
CCCCCCCCCCCHHHH		46.6229967540
841UbiquitinationKPLTYQTKQLIAREI
CCCCHHHHHHHHHHH		27.8121963094
842UbiquitinationPLTYQTKQLIAREIE
CCCHHHHHHHHHHHH		41.3021963094
852UbiquitinationAREIEVEKMRRAEAS
HHHHHHHHHHHHHHH		42.7729967540
865PhosphorylationASARVENSPQVDGSP
HHHHHCCCCCCCCCC		11.8225463755
869 (in isoform 2)Ubiquitination-46.75-
869UbiquitinationVENSPQVDGSPPGLE
HCCCCCCCCCCCCHH		46.7521963094
871PhosphorylationNSPQVDGSPPGLEGL
CCCCCCCCCCCHHHH		24.3719664994
880 (in isoform 2)Ubiquitination-30.62-
885UbiquitinationLLGGIGEKGVHRPAP
HHCCCCCCCCCCCCC		62.1029967540
929PhosphorylationVRSTAVPSAGDTAPE
EECCCCCCCCCCCCC		37.9824114839
939PhosphorylationDTAPEQDSVERRMGT
CCCCCCCHHHHHHCC		26.1028674419
968PhosphorylationVSNAVRRSLYIRDLL
HCHHHHHHHHHHHHC		18.2422199227
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
74SPhosphorylationKinaseATRQ13535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTF18_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 CTF18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
12930902
HSP74_HUMANHSPA4physical
12930902
RFC2_HUMANRFC2physical
12930902
RFC3_HUMANRFC3physical
12930902
RFC4_HUMANRFC4physical
12930902
RFC5_HUMANRFC5physical
12930902
DCC1_HUMANDSCC1physical
12930902
SMC1A_HUMANSMC1Aphysical
12930902
RAD21_HUMANRAD21physical
12930902
DCC1_HUMANDSCC1physical
12766176
DDX11_HUMANDDX11physical
18499658
DCC1_HUMANDSCC1physical
22939629
RFC2_HUMANRFC2physical
22939629
RFC3_HUMANRFC3physical
12766176
PCNA_HUMANPCNAphysical
12766176
FANCA_HUMANFANCAphysical
28215707
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 CTF18_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-64 AND SER-871, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-64; SER-73;SER-74 AND SER-871, AND MASS SPECTROMETRY.
"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 SER-225; SER-865 ANDSER-871, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871, AND MASSSPECTROMETRY.

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