EXO5_HUMAN - dbPTM
EXO5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXO5_HUMAN
UniProt AC Q9H790
Protein Name Exonuclease V
Gene Name EXO5
Organism Homo sapiens (Human).
Sequence Length 373
Subcellular Localization Nucleus . Cytoplasm, cytosol . Localizes to repair foci in response to DNA damage.
Protein Description Single-stranded DNA (ssDNA) bidirectional exonuclease involved in DNA repair. Probably involved in DNA repair following ultraviolet (UV) irradiation and interstrand cross-links (ICLs) damage. Has both 5'-3' and 3'-5' exonuclease activities with a strong preference for 5'-ends. Acts as a sliding exonuclease that loads at ssDNA ends and then slides along the ssDNA prior to cutting; however the sliding and the 3'-5' exonuclease activities are abolished upon binding to the replication protein A (RPA) complex that enforces 5'-directionality activity..
Protein Sequence MAETREEETVSAEASGFSDLSDSEFLEFLDLEDAQESKALVNMPGPSSESLGKDDKPISLQNWKRGLDILSPMERFHLKYLYVTDLATQNWCELQTAYGKELPGFLAPEKAAVLDTGASIHLARELELHDLVTVPVTTKEDAWAIKFLNILLLIPTLQSEGHIREFPVFGEGEGVLLVGVIDELHYTAKGELELAELKTRRRPMLPLEAQKKKDCFQVSLYKYIFDAMVQGKVTPASLIHHTKLCLEKPLGPSVLRHAQQGGFSVKSLGDLMELVFLSLTLSDLPVIDILKIEYIHQETATVLGTEIVAFKEKEVRAKVQHYMAYWMGHREPQGVDVEEAWKCRTCTYADICEWRKGSGVLSSTLAPQVKKAK
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
53UbiquitinationPSSESLGKDDKPISL
CCHHHCCCCCCCCCC
68.96-
110UbiquitinationPGFLAPEKAAVLDTG
CCCCCCCCEEEECCC
40.3529967540
116PhosphorylationEKAAVLDTGASIHLA
CCEEEECCCCCHHHH
30.41-
139UbiquitinationVTVPVTTKEDAWAIK
EECEECCHHHHHHHH
44.2029967540
159PhosphorylationLLIPTLQSEGHIREF
HHHHHCCCCCCEEEE
48.9722817900
198UbiquitinationELELAELKTRRRPML
CCHHHHHHHCCCCCC
31.3329967540
243UbiquitinationASLIHHTKLCLEKPL
HHHHHHHHHHCCCCC
32.61-
248UbiquitinationHTKLCLEKPLGPSVL
HHHHHCCCCCCHHHH
32.37-
356UbiquitinationADICEWRKGSGVLSS
HHHCHHHCCCCCCCC
59.51-
358PhosphorylationICEWRKGSGVLSSTL
HCHHHCCCCCCCCCC
28.85-
362PhosphorylationRKGSGVLSSTLAPQV
HCCCCCCCCCCCHHH
20.90-
363PhosphorylationKGSGVLSSTLAPQVK
CCCCCCCCCCCHHHH
24.23-
364PhosphorylationGSGVLSSTLAPQVKK
CCCCCCCCCCHHHHC
24.46-

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 EXO5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXO5_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 EXO5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXO5_HUMANEXO5physical
23095756

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 EXO5_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP