FANCE_HUMAN - dbPTM
FANCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FANCE_HUMAN
UniProt AC Q9HB96
Protein Name Fanconi anemia group E protein
Gene Name FANCE
Organism Homo sapiens (Human).
Sequence Length 536
Subcellular Localization Nucleus .
Protein Description As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2..
Protein Sequence MATPDAGLPGAEGVEPAPWAQLEAPARLLLQALQAGPEGARRGLGVLRALGSRGWEPFDWGRLLEALCREEPVVQGPDGRLELKPLLLRLPRICQRNLMSLLMAVRPSLPESGLLSVLQIAQQDLAPDPDAWLRALGELLRRDLGVGTSMEGASPLSERCQRQLQSLCRGLGLGGRRLKSPQAPDPEEEENRDSQQPGKRRKDSEEEAASPEGKRVPKRLRCWEEEEDHEKERPEHKSLESLADGGSASPIKDQPVMAVKTGEDGSNLDDAKGLAESLELPKAIQDQLPRLQQLLKTLEEGLEGLEDAPPVELQLLHECSPSQMDLLCAQLQLPQLSDLGLLRLCTWLLALSPDLSLSNATVLTRSLFLGRILSLTSSASRLLTTALTSFCAKYTYPVCSALLDPVLQAPGTGPAQTELLCCLVKMESLEPDAQVLMLGQILELPWKEETFLVLQSLLERQVEMTPEKFSVLMEKLCKKGLAATTSMAYAKLMLTVMTKYQANITETQRLGLAMALEPNTTFLRKSLKAALKHLGP
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
84UbiquitinationPDGRLELKPLLLRLP
CCCCEEHHHHHHHHH		25.0121890473
101UbiquitinationCQRNLMSLLMAVRPS
HHHHHHHHHHHHCCC		2.0622817900
104UbiquitinationNLMSLLMAVRPSLPE
HHHHHHHHHCCCCCC		8.3022817900
116UbiquitinationLPESGLLSVLQIAQQ
CCCCCHHHHHHHHHH		26.3124816145
142DimethylationALGELLRRDLGVGTS
HHHHHHHHHCCCCCC		43.40-
148PhosphorylationRRDLGVGTSMEGASP
HHHCCCCCCCCCCCC		23.6123532336
154PhosphorylationGTSMEGASPLSERCQ
CCCCCCCCCHHHHHH		36.9121815630
157PhosphorylationMEGASPLSERCQRQL
CCCCCCHHHHHHHHH		26.7823532336
159DimethylationGASPLSERCQRQLQS
CCCCHHHHHHHHHHH		20.63-
162UbiquitinationPLSERCQRQLQSLCR
CHHHHHHHHHHHHHH		42.6822817900
166PhosphorylationRCQRQLQSLCRGLGL
HHHHHHHHHHHHCCC		37.7224719451
174UbiquitinationLCRGLGLGGRRLKSP
HHHHCCCCCCCCCCC		26.2622817900
180PhosphorylationLGGRRLKSPQAPDPE
CCCCCCCCCCCCCHH		27.1730266825
194PhosphorylationEEEENRDSQQPGKRR
HHHCCCCCCCCCCCC		27.7228985074
199UbiquitinationRDSQQPGKRRKDSEE
CCCCCCCCCCCCHHH		56.5721906983
202UbiquitinationQQPGKRRKDSEEEAA
CCCCCCCCCHHHHHC		70.4222817900
204PhosphorylationPGKRRKDSEEEAASP
CCCCCCCHHHHHCCC		50.3623401153
210PhosphorylationDSEEEAASPEGKRVP
CHHHHHCCCCCCCCC		30.4523401153
214UbiquitinationEAASPEGKRVPKRLR
HHCCCCCCCCCCHHC		48.8624816145
238PhosphorylationKERPEHKSLESLADG
CCCCCCCCHHHHCCC		39.0029255136
241PhosphorylationPEHKSLESLADGGSA
CCCCCHHHHCCCCCC		33.8623401153
247PhosphorylationESLADGGSASPIKDQ
HHHCCCCCCCCCCCC		30.9723401153
249PhosphorylationLADGGSASPIKDQPV
HCCCCCCCCCCCCCE		28.9319664994
252UbiquitinationGGSASPIKDQPVMAV
CCCCCCCCCCCEEEE		54.4129967540
260UbiquitinationDQPVMAVKTGEDGSN
CCCEEEEEECCCCCC		41.0721906983
261PhosphorylationQPVMAVKTGEDGSNL
CCEEEEEECCCCCCH		38.9226074081
266PhosphorylationVKTGEDGSNLDDAKG
EEECCCCCCHHHHCH		46.6826074081
272UbiquitinationGSNLDDAKGLAESLE
CCCHHHHCHHHHHCC		62.5422817900
272MethylationGSNLDDAKGLAESLE
CCCHHHHCHHHHHCC		62.54-
282UbiquitinationAESLELPKAIQDQLP
HHHCCHHHHHHHHHH		71.4029967540
346PhosphorylationLGLLRLCTWLLALSP
HHHHHHHHHHHHHCC		24.6018995830
374PhosphorylationLFLGRILSLTSSASR
HHHHHHHHHCHHHHH		27.5117924555
378PhosphorylationRILSLTSSASRLLTT
HHHHHCHHHHHHHHH		25.6528674151
380PhosphorylationLSLTSSASRLLTTAL
HHHCHHHHHHHHHHH		25.9628674151
484PhosphorylationCKKGLAATTSMAYAK
HHCCCHHHHHHHHHH		17.5021406692
485PhosphorylationKKGLAATTSMAYAKL
HCCCHHHHHHHHHHH		16.2721406692
486PhosphorylationKGLAATTSMAYAKLM
CCCHHHHHHHHHHHH		9.3221406692
489PhosphorylationAATTSMAYAKLMLTV
HHHHHHHHHHHHHHH		8.8121406692
495PhosphorylationAYAKLMLTVMTKYQA
HHHHHHHHHHHHHHC		8.3522210691
500PhosphorylationMLTVMTKYQANITET
HHHHHHHHHCCCCHH		12.0528796482
505PhosphorylationTKYQANITETQRLGL
HHHHCCCCHHHHHHH		32.5522210691
507PhosphorylationYQANITETQRLGLAM
HHCCCCHHHHHHHHH		15.4428796482
520PhosphorylationAMALEPNTTFLRKSL
HHHCCCCCHHHHHHH		29.6428796482
521PhosphorylationMALEPNTTFLRKSLK
HHCCCCCHHHHHHHH		27.5828796482
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
346TPhosphorylationKinaseCHK1O14757
PSP
374SPhosphorylationKinaseCHK1O14757
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
346TPhosphorylation

17296736
374SPhosphorylation

17296736
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 FANCE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FANCC_HUMANFANCCphysical
15262960
FANCC_HUMANFANCCphysical
12649160
FANCA_HUMANFANCAphysical
12239156
FANCC_HUMANFANCCphysical
12239156
FANCG_HUMANFANCGphysical
12239156
FANCC_HUMANFANCCphysical
11157805
FANCA_HUMANFANCAphysical
11157805
FANCG_HUMANFANCGphysical
11157805
FANCA_HUMANFANCAphysical
12093742
FANCG_HUMANFANCGphysical
12093742
FANCF_HUMANFANCFphysical
12093742
FANCC_HUMANFANCCphysical
12093742
FACD2_HUMANFANCD2physical
12093742
FACD2_HUMANFANCD2physical
19704162
FACD2_HUMANFANCD2physical
17308347
FANCC_HUMANFANCCphysical
16513431
FACD2_HUMANFANCD2physical
16513431
FANCC_HUMANFANCCphysical
16127171
FACD2_HUMANFANCD2physical
16127171
FANCF_HUMANFANCFphysical
16127171
FANCM_HUMANFANCMphysical
16116434
FANCA_HUMANFANCAphysical
16116434
FANCG_HUMANFANCGphysical
15262960
FANCF_HUMANFANCFphysical
15262960
FANCA_HUMANFANCAphysical
15262960
FANCA_HUMANFANCAphysical
24451376
FANCG_HUMANFANCGphysical
24451376
FANCC_HUMANFANCCphysical
24451376
FACD2_HUMANFANCD2physical
24451376
FANCM_HUMANFANCMphysical
24451376
FANCC_HUMANFANCCphysical
26277624
FANCE_HUMANFANCEphysical
26277624
RAB21_HUMANRAB21physical
28514442
ENPP1_HUMANENPP1physical
28514442
GNPAT_HUMANGNPATphysical
28514442
P4K2A_HUMANPI4K2Aphysical
28514442
GNA13_HUMANGNA13physical
28514442
FANCA_HUMANFANCAphysical
23303816
FANCC_HUMANFANCCphysical
23303816
FACD2_HUMANFANCD2physical
23303816
CTBP1_HUMANCTBP1physical
23303816
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600901Fanconi anemia complementation group E (FANCE)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FANCE_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND MASSSPECTROMETRY.

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