RAD1_HUMAN - dbPTM
RAD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAD1_HUMAN
UniProt AC O60671
Protein Name Cell cycle checkpoint protein RAD1
Gene Name RAD1
Organism Homo sapiens (Human).
Sequence Length 282
Subcellular Localization Nucleus .
Protein Description Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. [PubMed: 10846170]
Protein Sequence MPLLTQQIQDEDDQYSLVASLDNVRNLSTILKAIHFREHATCFATKNGIKVTVENAKCVQANAFIQAGIFQEFKVQEESVTFRINLTVLLDCLSIFGSSPMPGTLTALRMCYQGYGYPLMLFLEEGGVVTVCKINTQEPEETLDFDFCSTNVINKIILQSEGLREAFSELDMTSEVLQITMSPDKPYFRLSTFGNAGSSHLDYPKDSDLMEAFHCNQTQVNRYKISLLKPSTKALVLSCKVSIRTDNRGFLSLQYMIRNEDGQICFVEYYCCPDEEVPESES
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
5Phosphorylation---MPLLTQQIQDED
---CCCCCCCCCCCC
26.5529523821
15PhosphorylationIQDEDDQYSLVASLD
CCCCCCCEEEEEEHH
15.8027642862
16PhosphorylationQDEDDQYSLVASLDN
CCCCCCEEEEEEHHH
15.6728122231
20PhosphorylationDQYSLVASLDNVRNL
CCEEEEEEHHHHHCH
28.8620873877
32UbiquitinationRNLSTILKAIHFREH
HCHHHHHHHHHHHHC
41.25-
46UbiquitinationHATCFATKNGIKVTV
CCEEEEECCCEEEEE
50.15-
50UbiquitinationFATKNGIKVTVENAK
EEECCCEEEEEECCE
33.00-
57UbiquitinationKVTVENAKCVQANAF
EEEEECCEEEECCHH
46.66-
106PhosphorylationSPMPGTLTALRMCYQ
CCCCCHHHHHHHHHC
24.3924719451
205UbiquitinationSSHLDYPKDSDLMEA
CCCCCCCCCCCHHHH
64.73-
224UbiquitinationQTQVNRYKISLLKPS
CHHCCEEEEEEECCC
23.68-
226PhosphorylationQVNRYKISLLKPSTK
HCCEEEEEEECCCCE
24.4024719451
229UbiquitinationRYKISLLKPSTKALV
EEEEEEECCCCEEEE
42.06-
233UbiquitinationSLLKPSTKALVLSCK
EEECCCCEEEEEEEE
44.02-
240UbiquitinationKALVLSCKVSIRTDN
EEEEEEEEEEEECCC
35.32-
280PhosphorylationPDEEVPESES-----
CCCCCCCCCC-----
36.7520545769
282PhosphorylationEEVPESES-------
CCCCCCCC-------
55.5920545769

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
280SPhosphorylationKinaseCSNK2A1P68400
GPS
282SPhosphorylationKinaseCSNK2A1P68400
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAD1_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 RAD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HUS1_HUMANHUS1physical
9872989
RAD9A_HUMANRAD9Aphysical
9872989
HUS1B_HUMANHUS1Bphysical
11944979
RAD9A_HUMANRAD9Aphysical
11994305
RAD17_HUMANRAD17physical
11418864
RFA1_HUMANRPA1physical
15897895
RFA2_HUMANRPA2physical
15897895
HUS1_HUMANHUS1physical
20847938
CSN5_HUMANCOPS5physical
17583730
MSH2_HUMANMSH2physical
20188637
MSH6_HUMANMSH6physical
20188637
MSH3_HUMANMSH3physical
20188637
FEN1_HUMANFEN1physical
15556996
ZBT14_HUMANZBTB14physical
26186194
RAD9A_HUMANRAD9Aphysical
26186194
ZBT14_HUMANZBTB14physical
28514442
RAD9A_HUMANRAD9Aphysical
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 RAD1_HUMAN

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Related Literatures of Post-Translational Modification

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