DCC1_HUMAN - dbPTM
DCC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCC1_HUMAN
UniProt AC Q9BVC3
Protein Name Sister chromatid cohesion protein DCC1
Gene Name DSCC1
Organism Homo sapiens (Human).
Sequence Length 393
Subcellular Localization Nucleus.
Protein Description Loads PCNA onto primed templates regulating velocity, spacing and restart activity of replication forks. May couple DNA replication to sister chromatid cohesion through regulation of the acetylation of the cohesin subunit SMC3..
Protein Sequence MKRTRDEVDATLQIAKLNAAELLPAVHCLGFGPGASGAAAGDFCLLELEPTLCQQLEDGHSLVIRGDKDEQAVLCSKDKTYDLKIADTSNMLLFIPGCKTPDQLKKEDSHCNIIHTEIFGFSNNYWELRRRRPKLKKLKKLLMENPYEGPDSQKEKDSNSSKYTTEDLLDQIQASEEEIMTQLQVLNACKIGGYWRILEFDYEMKLLNHVTQLVDSESWSFGKVPLNTCLQELGPLEPEEMIEHCLKCYGKKYVDEGEVYFELDADKICRAAARMLLQNAVKFNLAEFQEVWQQSVPEGMVTSLDQLKGLALVDRHSRPEIIFLLKVDDLPEDNQERFNSLFSLREKWTEEDIAPYIQDLCGEKQTIGALLTKYSHSSMQNGVKVYNSRRPIS
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
68UbiquitinationSLVIRGDKDEQAVLC
EEEECCCCCCCEEEE
67.02-
79UbiquitinationAVLCSKDKTYDLKIA
EEEECCCCCCEEEEE
53.36-
84UbiquitinationKDKTYDLKIADTSNM
CCCCCEEEEECCCCE
32.71-
88PhosphorylationYDLKIADTSNMLLFI
CEEEEECCCCEEEEE
16.9926074081
89PhosphorylationDLKIADTSNMLLFIP
EEEEECCCCEEEEEC
22.3126074081
99UbiquitinationLLFIPGCKTPDQLKK
EEEECCCCCHHHHHC
69.8429967540
100PhosphorylationLFIPGCKTPDQLKKE
EEECCCCCHHHHHCC
35.8522617229
105UbiquitinationCKTPDQLKKEDSHCN
CCCHHHHHCCCCCCC
48.7829967540
140SumoylationPKLKKLKKLLMENPY
HHHHHHHHHHHHCCC
58.24-
140UbiquitinationPKLKKLKKLLMENPY
HHHHHHHHHHHHCCC
58.2429967540
140SumoylationPKLKKLKKLLMENPY
HHHHHHHHHHHHCCC
58.24-
152PhosphorylationNPYEGPDSQKEKDSN
CCCCCCCCCCCCCCC
46.41-
154UbiquitinationYEGPDSQKEKDSNSS
CCCCCCCCCCCCCCC
71.3522817900
156UbiquitinationGPDSQKEKDSNSSKY
CCCCCCCCCCCCCCC
73.7722817900
162UbiquitinationEKDSNSSKYTTEDLL
CCCCCCCCCCHHHHH
46.57-
202UbiquitinationWRILEFDYEMKLLNH
EEEEECCHHHHHHHH
24.2021963094
206UbiquitinationEFDYEMKLLNHVTQL
ECCHHHHHHHHHHHH
5.8222817900
207UbiquitinationFDYEMKLLNHVTQLV
CCHHHHHHHHHHHHH
3.3022817900
223UbiquitinationSESWSFGKVPLNTCL
CCCCCCCCCCHHHHH
38.3729967540
247UbiquitinationEMIEHCLKCYGKKYV
HHHHHHHHHHCCCCC
30.7021963094
251UbiquitinationHCLKCYGKKYVDEGE
HHHHHHCCCCCCCCE
17.9222817900
252UbiquitinationCLKCYGKKYVDEGEV
HHHHHCCCCCCCCEE
46.2522817900
275SulfoxidationICRAAARMLLQNAVK
HHHHHHHHHHHHHHH
3.6221406390
347UbiquitinationSLFSLREKWTEEDIA
HHHHHHHHCCHHHHH
53.6429967540
364UbiquitinationIQDLCGEKQTIGALL
HHHHHCCCCHHHHHH
37.7229967540
374PhosphorylationIGALLTKYSHSSMQN
HHHHHHHCCCCHHHC
13.33-
384UbiquitinationSSMQNGVKVYNSRRP
CHHHCCCEEECCCCC
40.1629967540

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 DCC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCC1_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 DCC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTF18_HUMANCHTF18physical
12766176
DDX11_HUMANDDX11physical
18499658
CTF8_HUMANCHTF8physical
26186194
RFC4_HUMANRFC4physical
26186194
RFC3_HUMANRFC3physical
26186194
RFC5_HUMANRFC5physical
26186194
RFC2_HUMANRFC2physical
26186194
T2FA_HUMANGTF2F1physical
26186194
CTF18_HUMANCHTF18physical
26186194
BBS7_HUMANBBS7physical
26186194
THOC1_HUMANTHOC1physical
26344197
RFC3_HUMANRFC3physical
12766176
RFC4_HUMANRFC4physical
28514442
CTF8_HUMANCHTF8physical
28514442
CTF18_HUMANCHTF18physical
28514442
RFC2_HUMANRFC2physical
28514442
RFC3_HUMANRFC3physical
28514442
T2FA_HUMANGTF2F1physical
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 DCC1_HUMAN

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Related Literatures of Post-Translational Modification

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