XPF_HUMAN - dbPTM
XPF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XPF_HUMAN
UniProt AC Q92889
Protein Name DNA repair endonuclease XPF
Gene Name ERCC4
Organism Homo sapiens (Human).
Sequence Length 916
Subcellular Localization Nucleus .
Protein Description Catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link..
Protein Sequence MESGQPARRIAMAPLLEYERQLVLELLDTDGLVVCARGLGADRLLYHFLQLHCHPACLVLVLNTQPAEEEYFINQLKIEGVEHLPRRVTNEITSNSRYEVYTQGGVIFATSRILVVDFLTDRIPSDLITGILVYRAHRIIESCQEAFILRLFRQKNKRGFIKAFTDNAVAFDTGFCHVERVMRNLFVRKLYLWPRFHVAVNSFLEQHKPEVVEIHVSMTPTMLAIQTAILDILNACLKELKCHNPSLEVEDLSLENAIGKPFDKTIRHYLDPLWHQLGAKTKSLVQDLKILRTLLQYLSQYDCVTFLNLLESLRATEKAFGQNSGWLFLDSSTSMFINARARVYHLPDAKMSKKEKISEKMEIKEGEETKKELVLESNPKWEALTEVLKEIEAENKESEALGGPGQVLICASDDRTCSQLRDYITLGAEAFLLRLYRKTFEKDSKAEEVWMKFRKEDSSKRIRKSHKRPKDPQNKERASTKERTLKKKKRKLTLTQMVGKPEELEEEGDVEEGYRREISSSPESCPEEIKHEEFDVNLSSDAAFGILKEPLTIIHPLLGCSDPYALTRVLHEVEPRYVVLYDAELTFVRQLEIYRASRPGKPLRVYFLIYGGSTEEQRYLTALRKEKEAFEKLIREKASMVVPEEREGRDETNLDLVRGTASADVSTDTRKAGGQEQNGTQQSIVVDMREFRSELPSLIHRRGIDIEPVTLEVGDYILTPEMCVERKSISDLIGSLNNGRLYSQCISMSRYYKRPVLLIEFDPSKPFSLTSRGALFQEISSNDISSKLTLLTLHFPRLRILWCPSPHATAELFEELKQSKPQPDAATALAITADSETLPESEKYNPGPQDFLLKMPGVNAKNCRSLMHHVKNIAELAALSQDELTSILGNAANAKQLYDFIHTSFAEVVSKGKGKK
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
89PhosphorylationEHLPRRVTNEITSNS
CCCCCHHHCCCCCCC		25.8929978859
93PhosphorylationRRVTNEITSNSRYEV
CHHHCCCCCCCCEEE		18.7129978859
94PhosphorylationRVTNEITSNSRYEVY
HHHCCCCCCCCEEEE		38.1729978859
96PhosphorylationTNEITSNSRYEVYTQ
HCCCCCCCCEEEEEC		35.6929978859
191PhosphorylationNLFVRKLYLWPRFHV
HHHHHHHHHHHHHHH		15.12-
260AcetylationSLENAIGKPFDKTIR
CHHHCCCCCCHHHHH		36.0823954790
260AcetylationSLENAIGKPFDKTIR
CHHHCCCCCCHHHHH		36.08-
260UbiquitinationSLENAIGKPFDKTIR
CHHHCCCCCCHHHHH		36.08-
264UbiquitinationAIGKPFDKTIRHYLD
CCCCCCHHHHHHHHH		46.35-
282UbiquitinationHQLGAKTKSLVQDLK
HHCCCCHHHHHHHHH		40.88-
289AcetylationKSLVQDLKILRTLLQ
HHHHHHHHHHHHHHH		48.2419608861
371UbiquitinationKEGEETKKELVLESN
CCCHHHHHHHHHHCC		64.80-
377PhosphorylationKKELVLESNPKWEAL
HHHHHHHCCHHHHHH		55.0327794612
380UbiquitinationLVLESNPKWEALTEV
HHHHCCHHHHHHHHH		63.01-
389UbiquitinationEALTEVLKEIEAENK
HHHHHHHHHHHHHCH		62.92-
441UbiquitinationRLYRKTFEKDSKAEE
HHHHHHHCCCCCHHH		62.2721890473
445UbiquitinationKTFEKDSKAEEVWMK
HHHCCCCCHHHHHHH		70.70-
452UbiquitinationKAEEVWMKFRKEDSS
CHHHHHHHHCCCCHH		26.7221890473
465PhosphorylationSSKRIRKSHKRPKDP
HHHHHHHHCCCCCCC		25.13-
493PhosphorylationKKKKRKLTLTQMVGK
HHHHHHCCHHHCCCC		30.6924719451
500SumoylationTLTQMVGKPEELEEE
CHHHCCCCHHHHHHC		37.5328112733
500AcetylationTLTQMVGKPEELEEE
CHHHCCCCHHHHHHC		37.5326051181
519PhosphorylationEGYRREISSSPESCP
HHHHHHCCCCCCCCC		21.7323663014
520PhosphorylationGYRREISSSPESCPE
HHHHHCCCCCCCCCH		56.4225159151
521PhosphorylationYRREISSSPESCPEE
HHHHCCCCCCCCCHH		26.3725159151
524PhosphorylationEISSSPESCPEEIKH
HCCCCCCCCCHHHCC		38.0525159151
577PhosphorylationLHEVEPRYVVLYDAE
HHHCCCCEEEEEECE		12.9618083107
581PhosphorylationEPRYVVLYDAELTFV
CCCEEEEEECEEEEE		11.0718083107
594PhosphorylationFVRQLEIYRASRPGK
EEEEEEHHHCCCCCC		7.2518083107
606PhosphorylationPGKPLRVYFLIYGGS
CCCCEEEEEEEECCC		6.0427732954
610PhosphorylationLRVYFLIYGGSTEEQ
EEEEEEEECCCHHHH		19.9927732954
613PhosphorylationYFLIYGGSTEEQRYL
EEEEECCCHHHHHHH		28.4327732954
614PhosphorylationFLIYGGSTEEQRYLT
EEEECCCHHHHHHHH		46.9827732954
621PhosphorylationTEEQRYLTALRKEKE
HHHHHHHHHHHHHHH		18.0824719451
632UbiquitinationKEKEAFEKLIREKAS
HHHHHHHHHHHHHHC		42.64-
640SulfoxidationLIREKASMVVPEERE
HHHHHHCCCCCCCCC		4.1521406390
660PhosphorylationNLDLVRGTASADVST
CHHCCCCCCCCCCCC		13.58-
662PhosphorylationDLVRGTASADVSTDT
HCCCCCCCCCCCCCC		25.49-
666PhosphorylationGTASADVSTDTRKAG
CCCCCCCCCCCHHCC		22.5525627689
667PhosphorylationTASADVSTDTRKAGG
CCCCCCCCCCHHCCC		41.0425627689
669PhosphorylationSADVSTDTRKAGGQE
CCCCCCCCHHCCCCC		33.87-
710PhosphorylationGIDIEPVTLEVGDYI
CCCCCCEEEEECCEE		28.10-
728PhosphorylationEMCVERKSISDLIGS
HHHCCCCCHHHHHHH		33.2822210691
741UbiquitinationGSLNNGRLYSQCISM
HHCCCCCHHHHHHHH		5.2421890473
742PhosphorylationSLNNGRLYSQCISMS
HCCCCCHHHHHHHHH		8.7122210691
743PhosphorylationLNNGRLYSQCISMSR
CCCCCHHHHHHHHHH		24.1422210691
752PhosphorylationCISMSRYYKRPVLLI
HHHHHHHCCCCEEEE		10.22-
753UbiquitinationISMSRYYKRPVLLIE
HHHHHHCCCCEEEEE		41.0921890473
764PhosphorylationLLIEFDPSKPFSLTS
EEEEECCCCCCCCCC		55.60-
843UbiquitinationETLPESEKYNPGPQD
CCCCCHHCCCCCCCC		60.65-
861UbiquitinationKMPGVNAKNCRSLMH
CCCCCCHHHHHHHHH		51.91-
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 XPF_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XPF_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 XPF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPTN1_HUMANSPTAN1physical
12571280
FANCA_HUMANFANCAphysical
12571280
ERCC1_HUMANERCC1physical
8197175
PLK1_HUMANPLK1physical
19596235
SLX4_HUMANSLX4physical
19596235
SPTN1_HUMANSPTAN1physical
11401546
SLX4_HUMANSLX4physical
19595721
MSH2_HUMANMSH2physical
14706347
ERCC1_HUMANERCC1physical
14706347
SLX4_HUMANSLX4physical
23994477
SLX4_HUMANSLX4physical
24012755
ERCC1_HUMANERCC1physical
26344197
ERCC1_HUMANERCC1physical
25538220
SLX4_HUMANSLX4physical
25538220
SPTA1_HUMANSPTA1physical
16889989
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
278760Xeroderma pigmentosum complementation group F (XP-F)
610965XFE progeroid syndrome (XFEPS)
278760Xeroderma pigmentosum type F/Cockayne syndrome (XPF/CS)
615272Fanconi anemia complementation group Q (FANCQ)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XPF_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-289, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520; SER-521 ANDSER-524, AND MASS SPECTROMETRY.

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