CTC1_HUMAN - dbPTM
CTC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTC1_HUMAN
UniProt AC Q2NKJ3
Protein Name CST complex subunit CTC1
Gene Name CTC1
Organism Homo sapiens (Human).
Sequence Length 1217
Subcellular Localization Nucleus . Chromosome, telomere . A transmembrane region is predicted by sequence analysis tools (ESKW, MEMSAT and Phobius)
however, given the telomeric localization of the protein, the relevance of the transmembrane region is unsure in vivo.
Protein Description Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation. [PubMed: 19854130 However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha]
Protein Sequence MAAGRAQVPSSEQAWLEDAQVFIQKTLCPAVKEPNVQLTPLVIDCVKTVWLSQGRNQGSTLPLSYSFVSVQDLKTHQRLPCCSHLSWSSSAYQAWAQEAGPNGNPLPREQLLLLGTLTDLSADLEQECRNGSLYVRDNTGVLSCELIDLDLSWLGHLFLFPRWSYLPPARWNSSGEGHLELWDAPVPVFPLTISPGPVTPIPVLYPESASCLLRLRNKLRGVQRNLAGSLVRLSALVKSKQKAYFILSLGRSHPAVTHVSIIVQVPAQLVWHRALRPGTAYVLTELRVSKIRGQRQHVWMTSQSSRLLLLKPECVQELELELEGPLLEADPKPLPMPSNSEDKKDPESLVRYSRLLSYSGAVTGVLNEPAGLYELDGQLGLCLAYQQFRGLRRVMRPGVCLQLQDVHLLQSVGGGTRRPVLAPCLRGAVLLQSFSRQKPGAHSSRQAYGASLYEQLVWERQLGLPLYLWATKALEELACKLCPHVLRHHQFLQHSSPGSPSLGLQLLAPTLDLLAPPGSPVRNAHNEILEEPHHCPLQKYTRLQTPSSFPTLATLKEEGQRKAWASFDPKALLPLPEASYLPSCQLNRRLAWSWLCLLPSAFCPAQVLLGVLVASSHKGCLQLRDQSGSLPCLLLAKHSQPLSDPRLIGCLVRAERFQLIVERDVRSSFPSWKELSMPGFIQKQQARVYVQFFLADALILPVPRPCLHSATPSTPQTDPTGPEGPHLGQSRLFLLCHKEALMKRNFCVPPGASPEVPKPALSFYVLGSWLGGTQRKEGTGWGLPEPQGNDDNDQKVHLIFFGSSVRWFEFLHPGQVYRLIAPGPATPMLFEKDGSSCISRRPLELAGCASCLTVQDNWTLELESSQDIQDVLDANKSLPESSLTDLLSDNFTDSLVSFSAEILSRTLCEPLVASLWMKLGNTGAMRRCVKLTVALETAECEFPPHLDVYIEDPHLPPSLGLLPGARVHFSQLEKRVSRSHNVYCCFRSSTYVQVLSFPPETTISIPLPHIYLAELLQGGQSPFQATASCHIVSVFSLQLFWVCAYCTSICRQGKCTRLGSTCPTQTAISQAIIRLLVEDGTAEAVVTCRNHHVAAALGLCPREWASLLDFVQVPGRVVLQFAGPGAQLESSARVDEPMTMFLWTLCTSPSVLRPIVLSFELERKPSKIVPLEPPRLQRFQCGELPFLTHVNPRLRLSCLSIRESEYSSSLGILASSC
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
25UbiquitinationDAQVFIQKTLCPAVK
HHHHHHHHHCCHHHC
38.3529967540
32UbiquitinationKTLCPAVKEPNVQLT
HHCCHHHCCCCCCCC
70.3429967540
47UbiquitinationPLVIDCVKTVWLSQG
HHHHHHHEEEEECCC
43.63-
74 (in isoform 2)Ubiquitination-52.8521906983
74 (in isoform 1)Ubiquitination-52.8521906983
74UbiquitinationFVSVQDLKTHQRLPC
EEEHHHCCCCCCCCC
52.8521906983
132PhosphorylationEQECRNGSLYVRDNT
HHHHHCCCEEEECCC
21.7824719451
238UbiquitinationVRLSALVKSKQKAYF
HHHHHHHHCCCCEEE
53.4321906983
238 (in isoform 1)Ubiquitination-53.4321906983
240UbiquitinationLSALVKSKQKAYFIL
HHHHHHCCCCEEEEE
50.5322817900
242UbiquitinationALVKSKQKAYFILSL
HHHHCCCCEEEEEEC
49.1122817900
257UbiquitinationGRSHPAVTHVSIIVQ
CCCCCCCCEEEEEEE
20.7522817900
374UbiquitinationNEPAGLYELDGQLGL
CCCCCEEEECCHHHH
45.4822817900
477UbiquitinationATKALEELACKLCPH
HHHHHHHHHHHHCHH
5.0422817900
480UbiquitinationALEELACKLCPHVLR
HHHHHHHHHCHHHHH
47.7429967540
496UbiquitinationHQFLQHSSPGSPSLG
HHHHCCCCCCCCCHH
31.0222817900
513UbiquitinationLLAPTLDLLAPPGSP
HHHHHHHHHCCCCCC
5.0322817900
519PhosphorylationDLLAPPGSPVRNAHN
HHHCCCCCCCCCCCH
26.4626329039
521UbiquitinationLAPPGSPVRNAHNEI
HCCCCCCCCCCCHHH
8.6922817900
521 (in isoform 2)Ubiquitination-8.6921906983
539UbiquitinationPHHCPLQKYTRLQTP
CCCCCCHHCCCCCCC
57.1629967540
540PhosphorylationHHCPLQKYTRLQTPS
CCCCCHHCCCCCCCC
5.5522468782
545PhosphorylationQKYTRLQTPSSFPTL
HHCCCCCCCCCCCCH
29.7222468782
556 (in isoform 1)Ubiquitination-49.7321906983
556UbiquitinationFPTLATLKEEGQRKA
CCCHHHHHHHCCCCH
49.7321906983
562UbiquitinationLKEEGQRKAWASFDP
HHHHCCCCHHHCCCH
40.1529967540
580PhosphorylationLPLPEASYLPSCQLN
CCCCCHHHCCCCHHH
29.6718452278
583PhosphorylationPEASYLPSCQLNRRL
CCHHHCCCCHHHHHH
16.3518452278
630UbiquitinationLRDQSGSLPCLLLAK
HHCCCCCCCEEEEEC
3.8622817900
637UbiquitinationLPCLLLAKHSQPLSD
CCEEEEECCCCCCCC
43.70-
638UbiquitinationPCLLLAKHSQPLSDP
CEEEEECCCCCCCCH
26.5122817900
638 (in isoform 2)Ubiquitination-26.5121906983
673UbiquitinationRSSFPSWKELSMPGF
HHCCCCHHHHCCCCC
53.7922817900
673 (in isoform 1)Ubiquitination-53.7921906983
675UbiquitinationSFPSWKELSMPGFIQ
CCCCHHHHCCCCCCH
4.7622817900
683UbiquitinationSMPGFIQKQQARVYV
CCCCCCHHHHHHHHH
39.29-
689PhosphorylationQKQQARVYVQFFLAD
HHHHHHHHHHHHHCC
5.2928348404
709PhosphorylationVPRPCLHSATPSTPQ
CCCCCCCCCCCCCCC
22.3823312004
711PhosphorylationRPCLHSATPSTPQTD
CCCCCCCCCCCCCCC
22.3123312004
713PhosphorylationCLHSATPSTPQTDPT
CCCCCCCCCCCCCCC
48.6523312004
714PhosphorylationLHSATPSTPQTDPTG
CCCCCCCCCCCCCCC
22.1823312004
717PhosphorylationATPSTPQTDPTGPEG
CCCCCCCCCCCCCCC
45.1923312004
733UbiquitinationHLGQSRLFLLCHKEA
CCCHHHHHHHHHHHH
4.8122817900
741 (in isoform 2)Ubiquitination-4.3321906983
741UbiquitinationLLCHKEALMKRNFCV
HHHHHHHHHHCCCCC
4.3322817900
752UbiquitinationNFCVPPGASPEVPKP
CCCCCCCCCCCCCCC
27.9022817900
753PhosphorylationFCVPPGASPEVPKPA
CCCCCCCCCCCCCCC
27.7525159151
760UbiquitinationSPEVPKPALSFYVLG
CCCCCCCCEEEEEEE
23.2022817900
760 (in isoform 2)Ubiquitination-23.2021906983
776UbiquitinationWLGGTQRKEGTGWGL
HHCCCCCCCCCCCCC
51.1621906983
776 (in isoform 1)Ubiquitination-51.1621906983
795UbiquitinationGNDDNDQKVHLIFFG
CCCCCCCEEEEEEEC
34.1922817900
795 (in isoform 1)Ubiquitination-34.1921906983
835PhosphorylationMLFEKDGSSCISRRP
EEEECCCCCCCCCCC
31.9729262532
836PhosphorylationLFEKDGSSCISRRPL
EEECCCCCCCCCCCH
22.4729262532
839PhosphorylationKDGSSCISRRPLELA
CCCCCCCCCCCHHHC
26.9429262532
904PhosphorylationSFSAEILSRTLCEPL
HHCHHHHHHHCCHHH
28.9624719451
918UbiquitinationLVASLWMKLGNTGAM
HHHHHHHHHCCCHHH
41.48-
931UbiquitinationAMRRCVKLTVALETA
HHHHHHHHEEEEEEE
2.0222817900
939UbiquitinationTVALETAECEFPPHL
EEEEEEEECCCCCCE
41.8422817900
939 (in isoform 2)Ubiquitination-41.8421906983
974 (in isoform 1)Ubiquitination-67.6921906983
974UbiquitinationVHFSQLEKRVSRSHN
EEHHHHHHHHHHCCC
67.6927667366
1060PhosphorylationGKCTRLGSTCPTQTA
CCCCCCCCCCCCHHH
31.28-
1064PhosphorylationRLGSTCPTQTAISQA
CCCCCCCCHHHHHHH
40.47-
1066PhosphorylationGSTCPTQTAISQAII
CCCCCCHHHHHHHHH
28.56-

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 CTC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTC1_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 CTC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CTC1_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612199Cerebroretinal microangiopathy with calcifications and cysts (CRMCC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTC1_HUMAN

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Related Literatures of Post-Translational Modification

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