PAXX_HUMAN - dbPTM
PAXX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAXX_HUMAN
UniProt AC Q9BUH6
Protein Name Protein PAXX {ECO:0000305}
Gene Name PAXX {ECO:0000303|PubMed:25574025, ECO:0000312|HGNC:HGNC:27849}
Organism Homo sapiens (Human).
Sequence Length 204
Subcellular Localization Nucleus . Predominantly localizes to the nucleus. Accumulates at sites of DNA damage generated by laser microirradiation.
Protein Description Involved in non-homologous end joining (NHEJ), a major pathway to repair double-strand breaks in DNA. May act as a scaffold required to stabilize the Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at double-strand break sites and promote the assembly and/or stability of the NHEJ machinery..
Protein Sequence MDPLSPPLCTLPPGPEPPRFVCYCEGEESGEGDRGGFNLYVTDAAELWSTCFTPDSLAALKARFGLSAAEDITPRFRAACEQQAVALTLQEDRASLTLSGGPSALAFDLSKVPGPEAAPRLRALTLGLAKRVWSLERRLAAAEETAVSPRKSPRPAGPQLFLPDPDPQRGGPGPGVRRRCPGESLINPGFKSKKPAGGVDFDET
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
5O-linked_Glycosylation---MDPLSPPLCTLP
---CCCCCCCCCCCC
23301498
5Phosphorylation---MDPLSPPLCTLP
---CCCCCCCCCCCC
28188228
10PhosphorylationPLSPPLCTLPPGPEP
CCCCCCCCCCCCCCC
27732954
56PhosphorylationSTCFTPDSLAALKAR
HHCCCHHHHHHHHHH
24719451
67PhosphorylationLKARFGLSAAEDITP
HHHHHCCCHHHHCCH
20068231
73PhosphorylationLSAAEDITPRFRAAC
CCHHHHCCHHHHHHH
20068231
95PhosphorylationTLQEDRASLTLSGGP
EEECCCCCEEECCCC
-
99PhosphorylationDRASLTLSGGPSALA
CCCCEEECCCCEEEE
-
103PhosphorylationLTLSGGPSALAFDLS
EEECCCCEEEEEEHH
-
130AcetylationALTLGLAKRVWSLER
HHHHHHHHHHHHHHH
25953088
134PhosphorylationGLAKRVWSLERRLAA
HHHHHHHHHHHHHHH
28857561
145PhosphorylationRLAAAEETAVSPRKS
HHHHHHHHCCCCCCC
22167270
148PhosphorylationAAEETAVSPRKSPRP
HHHHHCCCCCCCCCC
19664994
152PhosphorylationTAVSPRKSPRPAGPQ
HCCCCCCCCCCCCCC
22167270
169MethylationLPDPDPQRGGPGPGV
CCCCCCCCCCCCCCC
115486555
184PhosphorylationRRRCPGESLINPGFK
HHCCCCCCCCCCCCC
20068231
191AcetylationSLINPGFKSKKPAGG
CCCCCCCCCCCCCCC
25953088
192PhosphorylationLINPGFKSKKPAGGV
CCCCCCCCCCCCCCC
17192257
192O-linked_GlycosylationLINPGFKSKKPAGGV
CCCCCCCCCCCCCCC
23301498

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 PAXX_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAXX_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 PAXX_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 PAXX_HUMAN

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Related Literatures of Post-Translational Modification

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