XPC_MOUSE - dbPTM
XPC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XPC_MOUSE
UniProt AC P51612
Protein Name DNA repair protein complementing XP-C cells homolog
Gene Name Xpc
Organism Mus musculus (Mouse).
Sequence Length 930
Subcellular Localization Nucleus. Cytoplasm. Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions (By si
Protein Description Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by Rad23b and Rad23a. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity.; The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, Xpa, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the Xpc:Rad23b dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. Xpc:Rad23b induces a bend in DNA upon binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and Smug1 (By similarity)..
Protein Sequence MAPKRTADGRRRKRGQKTEDNKVARHEESVADDFEDEKQKPRRKSSFPKVSQGKRKRGCSDPGDPTNGAAKKKVAKATAKSKNLKVLKEEALSDGDDFRDSPADCKKAKKHPKSKVVDQGTDEDDSEDDWEEVEELTEPVLDMGENSATSPSDMPVKAVEIEIETPQQAKERERSEKIKMEFETYLRRMMKRFNKEVQENMHKVHLLCLLASGFYRNSICRQPDLLAIGLSIIPIRFTKVPLQDRDAYYLSNLVKWFIGTFTVNADLSASEQDDLQTTLERRIAIYSARDNEELVHIFLLILRALQLLTRLVLSLQPIPLKSAVTKGRKSSKETSVEGPGGSSELSSNSPESHNKPTTSRRIKEEETLSEGRGKATARGKRGTGTAGSRQRRKPSCSEGEEAEQKVQGRPHARKRRVAAKVSYKEESESDGAGSGSDFEPSSGEGQHSSDEDCEPGPRKQKRASAPQRTKAGSKSASKTQRGSQCEPSSFPEASSSSSGCKRGKKVSSGAEEMADRKPAGVDQWLEVYCEPQAKWVCVDCVHGVVGQPVACYKYATKPMTYVVGIDSDGWVRDVTQRYDPAWMTATRKCRVDAEWWAETLRPYRSLLTEREKKEDQEFQAKHLDQPLPTSISTYKNHPLYALKRHLLKFQAIYPETAAVLGYCRGEAVYSRDCVHTLHSRDTWLKQARVVRLGEVPYKMVKGFSNRARKARLSEPQLHDHNDLGLYGHWQTEEYQPPIAVDGKVPRNEFGNVYLFLPSMMPVGCVQMTLPNLNRVARKLGIDCVQAITGFDFHGGYCHPVTDGYIVCEEFRDVLLAAWENEQAIIEKKEKEKKEKRALGNWKLLVRGLLIRERLKLRYGAKSEAAAPHAAGGGLSSDEEEGTSSQAEAARVLAASWPQNREDPEQKSEYTKMTRKRRAAEASHLFPFEKL
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
60PhosphorylationGKRKRGCSDPGDPTN
CCCCCCCCCCCCCCC		50.0622802335
93PhosphorylationVLKEEALSDGDDFRD
HHHHHHHCCCCCCCC		46.7425521595
101PhosphorylationDGDDFRDSPADCKKA
CCCCCCCCHHHHHHH		20.1025619855
126PhosphorylationQGTDEDDSEDDWEEV
CCCCCCCCCCCHHHH		56.07-
165PhosphorylationAVEIEIETPQQAKER
EEEEEECCHHHHHHH		31.8725266776
170UbiquitinationIETPQQAKERERSEK
ECCHHHHHHHHHHHH		53.6322790023
195UbiquitinationRMMKRFNKEVQENMH
HHHHHHHHHHHHHHH		57.4627667366
239UbiquitinationIIPIRFTKVPLQDRD
EEEEEEEECCCCCCH		38.8627667366
330PhosphorylationAVTKGRKSSKETSVE
HHHCCCCCCCCCCCC		45.3321082442
331PhosphorylationVTKGRKSSKETSVEG
HHCCCCCCCCCCCCC		37.2321082442
334PhosphorylationGRKSSKETSVEGPGG
CCCCCCCCCCCCCCC		41.6325619855
335PhosphorylationRKSSKETSVEGPGGS
CCCCCCCCCCCCCCC		21.1825619855
342PhosphorylationSVEGPGGSSELSSNS
CCCCCCCCCCCCCCC		26.9325619855
343PhosphorylationVEGPGGSSELSSNSP
CCCCCCCCCCCCCCC		45.9225619855
346PhosphorylationPGGSSELSSNSPESH
CCCCCCCCCCCCCCC		24.3427742792
347PhosphorylationGGSSELSSNSPESHN
CCCCCCCCCCCCCCC		54.6927742792
349PhosphorylationSSELSSNSPESHNKP
CCCCCCCCCCCCCCC		31.8027087446
352PhosphorylationLSSNSPESHNKPTTS
CCCCCCCCCCCCCCC		35.4325619855
357PhosphorylationPESHNKPTTSRRIKE
CCCCCCCCCCHHHCH		38.7325619855
358PhosphorylationESHNKPTTSRRIKEE
CCCCCCCCCHHHCHH		28.8525619855
359PhosphorylationSHNKPTTSRRIKEEE
CCCCCCCCHHHCHHH		23.2625619855
367PhosphorylationRRIKEEETLSEGRGK
HHHCHHHHHCCCCCC		38.5729472430
369PhosphorylationIKEEETLSEGRGKAT
HCHHHHHCCCCCCCC		45.4826824392
395PhosphorylationSRQRRKPSCSEGEEA
CCCCCCCCCCCCHHH		33.0525521595
397PhosphorylationQRRKPSCSEGEEAEQ
CCCCCCCCCCHHHHH		53.6325521595
643UbiquitinationNHPLYALKRHLLKFQ
CCHHHHHHHHHHHHH		29.6022790023
685UbiquitinationHSRDTWLKQARVVRL
HCCCCHHHHCEEEEE		33.2122790023
743UbiquitinationPPIAVDGKVPRNEFG
CCEEECCEECCCCCC		44.6022790023
862PhosphorylationKLRYGAKSEAAAPHA
HHHHCCCCCCCCCCC		31.7525619855
875PhosphorylationHAAGGGLSSDEEEGT
CCCCCCCCCCCCCCC		38.7325521595
876PhosphorylationAAGGGLSSDEEEGTS
CCCCCCCCCCCCCCC		54.8325521595
882PhosphorylationSSDEEEGTSSQAEAA
CCCCCCCCCHHHHHH		28.6024723360
883PhosphorylationSDEEEGTSSQAEAAR
CCCCCCCCHHHHHHH		31.1725619855
884PhosphorylationDEEEGTSSQAEAARV
CCCCCCCHHHHHHHH		32.9925619855
895PhosphorylationAARVLAASWPQNRED
HHHHHHHHCCCCCCC		33.41-
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
-KUbiquitinationE3 ubiquitin ligaseDdb2Q99J79
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XPC_MOUSE !!
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 XPC_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of XPC_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XPC_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-395 AND SER-397,AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-876, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory