FANCI_HUMAN - dbPTM
FANCI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FANCI_HUMAN
UniProt AC Q9NVI1
Protein Name Fanconi anemia group I protein
Gene Name FANCI
Organism Homo sapiens (Human).
Sequence Length 1328
Subcellular Localization Nucleus . Observed in spots localized in pairs on the sister chromatids of mitotic chromosome arms and not centromeres, one on each chromatids. These foci coincide with common fragile sites. They are frequently interlinked through BLM-associated ultr
Protein Description Plays an essential role in the repair of DNA double-strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites. Required for maintenance of chromosomal stability. Specifically binds branched DNA: binds both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates in S phase and G2 phase checkpoint activation upon DNA damage..
Protein Sequence MDQKILSLAAEKTADKLQEFLQTLREGDLTNLLQNQAVKGKVAGALLRAIFKGSPCSEEAGTLRRRKIYTCCIQLVESGDLQKEIASEIIGLLMLEAHHFPGPLLVELANEFISAVREGSLVNGKSLELLPIILTALATKKENLAYGKGVLSGEECKKQLINTLCSGRWDQQYVIQLTSMFKDVPLTAEEVEFVVEKALSMFSKMNLQEIPPLVYQLLVLSSKGSRKSVLEGIIAFFSALDKQHNEEQSGDELLDVVTVPSGELRHVEGTIILHIVFAIKLDYELGRELVKHLKVGQQGDSNNNLSPFSIALLLSVTRIQRFQDQVLDLLKTSVVKSFKDLQLLQGSKFLQNLVPHRSYVSTMILEVVKNSVHSWDHVTQGLVELGFILMDSYGPKKVLDGKTIETSPSLSRMPNQHACKLGANILLETFKIHEMIRQEILEQVLNRVVTRASSPISHFLDLLSNIVMYAPLVLQSCSSKVTEAFDYLSFLPLQTVQRLLKAVQPLLKVSMSMRDCLILVLRKAMFANQLDARKSAVAGFLLLLKNFKVLGSLSSSQCSQSLSVSQVHVDVHSHYNSVANETFCLEIMDSLRRCLSQQADVRLMLYEGFYDVLRRNSQLANSVMQTLLSQLKQFYEPKPDLLPPLKLEACILTQGDKISLQEPLDYLLCCIQHCLAWYKNTVIPLQQGEEEEEEEEAFYEDLDDILESITNRMIKSELEDFELDKSADFSQSTSIGIKNNICAFLVMGVCEVLIEYNFSISSFSKNRFEDILSLFMCYKKLSDILNEKAGKAKTKMANKTSDSLLSMKFVSSLLTALFRDSIQSHQESLSVLRSSNEFMRYAVNVALQKVQQLKETGHVSGPDGQNPEKIFQNLCDITRVLLWRYTSIPTSVEESGKKEKGKSISLLCLEGLQKIFSAVQQFYQPKIQQFLRALDVTDKEGEEREDADVSVTQRTAFQIRQFQRSLLNLLSSQEEDFNSKEALLLVTVLTSLSKLLEPSSPQFVQMLSWTSKICKENSREDALFCKSLMNLLFSLHVSYKSPVILLRDLSQDIHGHLGDIDQDVEVEKTNHFAIVNLRTAAPTVCLLVLSQAEKVLEEVDWLITKLKGQVSQETLSEEASSQATLPNQPVEKAIIMQLGTLLTFFHELVQTALPSGSCVDTLLKDLCKMYTTLTALVRYYLQVCQSSGGIPKNMEKLVKLSGSHLTPLCYSFISYVQNKSKSLNYTGEKKEKPAAVATAMARVLRETKPIPNLIFAIEQYEKFLIHLSKKSKVNLMQHMKLSTSRDFKIKGNILDMVLREDGEDENEEGTASEHGGQNKEPAKKKRKK
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
4Acetylation----MDQKILSLAAE
----CCHHHHHHHHH		58.9325953088
4Ubiquitination----MDQKILSLAAE
----CCHHHHHHHHH		58.9321890473
4 (in isoform 4)Ubiquitination-58.9321890473
12UbiquitinationILSLAAEKTADKLQE
HHHHHHHHHHHHHHH		44.2621906983
12 (in isoform 1)Ubiquitination-44.2621890473
12 (in isoform 2)Ubiquitination-44.2621890473
12 (in isoform 3)Ubiquitination-44.2621890473
12 (in isoform 4)Ubiquitination-44.2621890473
16AcetylationAAEKTADKLQEFLQT
HHHHHHHHHHHHHHH		50.0025953088
16UbiquitinationAAEKTADKLQEFLQT
HHHHHHHHHHHHHHH		50.0021890473
16 (in isoform 1)Ubiquitination-50.0021890473
16 (in isoform 2)Ubiquitination-50.0021890473
16 (in isoform 3)Ubiquitination-50.0021890473
16 (in isoform 4)Ubiquitination-50.0021890473
39UbiquitinationLLQNQAVKGKVAGAL
HHHCHHHHHHHHHHH		56.9021890473
39 (in isoform 1)Ubiquitination-56.9021890473
39 (in isoform 2)Ubiquitination-56.9021890473
39 (in isoform 3)Ubiquitination-56.9021890473
39 (in isoform 4)Ubiquitination-56.9021890473
412-HydroxyisobutyrylationQNQAVKGKVAGALLR
HCHHHHHHHHHHHHH		24.16-
41UbiquitinationQNQAVKGKVAGALLR
HCHHHHHHHHHHHHH		24.16-
52AcetylationALLRAIFKGSPCSEE
HHHHHHHHCCCCCCC		52.9826051181
52UbiquitinationALLRAIFKGSPCSEE
HHHHHHHHCCCCCCC		52.9821890473
52 (in isoform 4)Ubiquitination-52.9821890473
54PhosphorylationLRAIFKGSPCSEEAG
HHHHHHCCCCCCCCC		24.2730387612
57PhosphorylationIFKGSPCSEEAGTLR
HHHCCCCCCCCCCCC		41.6830387612
62PhosphorylationPCSEEAGTLRRRKIY
CCCCCCCCCCHHHHH		24.9230387612
125UbiquitinationEGSLVNGKSLELLPI
HCCCCCCCCHHHHHH		46.81-
140UbiquitinationILTALATKKENLAYG
HHHHHHHCHHHHCCC		53.10-
141UbiquitinationLTALATKKENLAYGK
HHHHHHCHHHHCCCC		47.70-
148UbiquitinationKENLAYGKGVLSGEE
HHHHCCCCCCCCHHH		32.92-
152PhosphorylationAYGKGVLSGEECKKQ
CCCCCCCCHHHHHHH		41.58-
157UbiquitinationVLSGEECKKQLINTL
CCCHHHHHHHHHHHH		47.00-
158UbiquitinationLSGEECKKQLINTLC
CCHHHHHHHHHHHHH		63.09-
200PhosphorylationFVVEKALSMFSKMNL
HHHHHHHHHHHCCCH		23.7320068231
203PhosphorylationEKALSMFSKMNLQEI
HHHHHHHHCCCHHHC		23.5020068231
215PhosphorylationQEIPPLVYQLLVLSS
HHCCHHHHHHHHHCC		10.9217053785
221PhosphorylationVYQLLVLSSKGSRKS
HHHHHHHCCCCCHHH		23.6420068231
222PhosphorylationYQLLVLSSKGSRKSV
HHHHHHCCCCCHHHH		36.5520068231
249PhosphorylationKQHNEEQSGDELLDV
HHCCCCCCCCCCEEE		52.0320873877
331UbiquitinationDQVLDLLKTSVVKSF
HHHHHHHHHHHHHHH		46.1521906983
331 (in isoform 1)Ubiquitination-46.1521890473
331 (in isoform 2)Ubiquitination-46.1521890473
331 (in isoform 3)Ubiquitination-46.1521890473
336AcetylationLLKTSVVKSFKDLQL
HHHHHHHHHHHHHHH		48.2825953088
336UbiquitinationLLKTSVVKSFKDLQL
HHHHHHHHHHHHHHH		48.2821890473
336 (in isoform 1)Ubiquitination-48.2821890473
336 (in isoform 2)Ubiquitination-48.2821890473
336 (in isoform 3)Ubiquitination-48.2821890473
3392-HydroxyisobutyrylationTSVVKSFKDLQLLQG
HHHHHHHHHHHHHCC		65.70-
339UbiquitinationTSVVKSFKDLQLLQG
HHHHHHHHHHHHHCC		65.7021890473
339 (in isoform 1)Ubiquitination-65.7021890473
339 (in isoform 2)Ubiquitination-65.7021890473
339 (in isoform 3)Ubiquitination-65.7021890473
347PhosphorylationDLQLLQGSKFLQNLV
HHHHHCCCHHHHHCC		13.7928509920
348UbiquitinationLQLLQGSKFLQNLVP
HHHHCCCHHHHHCCC		57.8421890473
348 (in isoform 1)Ubiquitination-57.8421890473
348 (in isoform 2)Ubiquitination-57.8421890473
348 (in isoform 3)Ubiquitination-57.8421890473
402UbiquitinationPKKVLDGKTIETSPS
CCCEECCCEEECCCC		46.1021890473
402 (in isoform 1)Ubiquitination-46.1021890473
402 (in isoform 2)Ubiquitination-46.1021890473
402 (in isoform 3)Ubiquitination-46.1021890473
403PhosphorylationKKVLDGKTIETSPSL
CCEECCCEEECCCCH		29.5824732914
406PhosphorylationLDGKTIETSPSLSRM
ECCCEEECCCCHHCC		41.9330266825
407PhosphorylationDGKTIETSPSLSRMP
CCCEEECCCCHHCCC		10.3319664994
409PhosphorylationKTIETSPSLSRMPNQ
CEEECCCCHHCCCCC		38.4530266825
411PhosphorylationIETSPSLSRMPNQHA
EECCCCHHCCCCCHH		30.7622115753
420UbiquitinationMPNQHACKLGANILL
CCCCHHHHHCHHHHH		51.22-
431UbiquitinationNILLETFKIHEMIRQ
HHHHHHHHHHHHHHH		51.04-
487PhosphorylationKVTEAFDYLSFLPLQ
CHHHHHHHHHCCCHH		9.5920071362
495PhosphorylationLSFLPLQTVQRLLKA
HHCCCHHHHHHHHHH		26.7020071362
501AcetylationQTVQRLLKAVQPLLK
HHHHHHHHHHHHHHH		51.6225953088
501UbiquitinationQTVQRLLKAVQPLLK
HHHHHHHHHHHHHHH		51.6221890473
501 (in isoform 1)Ubiquitination-51.6221890473
501 (in isoform 2)Ubiquitination-51.6221890473
501 (in isoform 3)Ubiquitination-51.6221890473
508UbiquitinationKAVQPLLKVSMSMRD
HHHHHHHHHCCCHHH		39.69-
512PhosphorylationPLLKVSMSMRDCLIL
HHHHHCCCHHHHHHH		11.8024719451
523UbiquitinationCLILVLRKAMFANQL
HHHHHHHHHHHHCCH		39.7921890473
523 (in isoform 1)Ubiquitination-39.7921890473
523 (in isoform 2)Ubiquitination-39.7921890473
523 (in isoform 3)Ubiquitination-39.7921890473
556PhosphorylationVLGSLSSSQCSQSLS
EECCCCHHHHCCCCC		31.6517478428
559PhosphorylationSLSSSQCSQSLSVSQ
CCCHHHHCCCCCEEE		18.3717478428
565PhosphorylationCSQSLSVSQVHVDVH
HCCCCCEEEEEEECH		24.10-
606PhosphorylationADVRLMLYEGFYDVL
CCHHHHHHHHHHHHH		10.4729759185
610PhosphorylationLMLYEGFYDVLRRNS
HHHHHHHHHHHHHCH		18.9229759185
629PhosphorylationSVMQTLLSQLKQFYE
HHHHHHHHHHHHHHC		36.2624719451
638UbiquitinationLKQFYEPKPDLLPPL
HHHHHCCCCCCCCCC		38.9421890473
638 (in isoform 1)Ubiquitination-38.9421890473
638 (in isoform 2)Ubiquitination-38.9421890473
638 (in isoform 3)Ubiquitination-38.9421890473
646AcetylationPDLLPPLKLEACILT
CCCCCCCEEEEEEEC		50.487964679
653PhosphorylationKLEACILTQGDKISL
EEEEEEECCCCCCCC		15.59-
715UbiquitinationSITNRMIKSELEDFE
HHHHHHHHHHHHHCC		28.6522053931
715 (in isoform 1)Ubiquitination-28.6521890473
715 (in isoform 2)Ubiquitination-28.6521890473
715 (in isoform 3)Ubiquitination-28.6521890473
725UbiquitinationLEDFELDKSADFSQS
HHHCCCCCCCCCCCC		61.2321906983
725 (in isoform 1)Ubiquitination-61.2321890473
725 (in isoform 2)Ubiquitination-61.2321890473
725 (in isoform 3)Ubiquitination-61.2321890473
726PhosphorylationEDFELDKSADFSQST
HHCCCCCCCCCCCCC		32.5130266825
730PhosphorylationLDKSADFSQSTSIGI
CCCCCCCCCCCCHHC		24.6217525332
732PhosphorylationKSADFSQSTSIGIKN
CCCCCCCCCCHHCCC		23.9530266825
733PhosphorylationSADFSQSTSIGIKNN
CCCCCCCCCHHCCCC		19.4130266825
734PhosphorylationADFSQSTSIGIKNNI
CCCCCCCCHHCCCCH		24.8629396449
762PhosphorylationEYNFSISSFSKNRFE
HCCCCCCCCCCCHHH		31.6924719451
780UbiquitinationSLFMCYKKLSDILNE
HHHHHHHHHHHHHHH		27.09-
782PhosphorylationFMCYKKLSDILNEKA
HHHHHHHHHHHHHHH		31.3323403867
788UbiquitinationLSDILNEKAGKAKTK
HHHHHHHHHCCHHHH		62.4621906983
788 (in isoform 1)Ubiquitination-62.4621890473
788 (in isoform 2)Ubiquitination-62.4621890473
788 (in isoform 3)Ubiquitination-62.4621890473
799UbiquitinationAKTKMANKTSDSLLS
HHHHHCCCCCHHHHH		39.61-
800PhosphorylationKTKMANKTSDSLLSM
HHHHCCCCCHHHHHH		37.2620068231
801PhosphorylationTKMANKTSDSLLSMK
HHHCCCCCHHHHHHH		27.1528348404
803PhosphorylationMANKTSDSLLSMKFV
HCCCCCHHHHHHHHH		30.8628348404
806PhosphorylationKTSDSLLSMKFVSSL
CCCHHHHHHHHHHHH		25.8120068231
811PhosphorylationLLSMKFVSSLLTALF
HHHHHHHHHHHHHHH		20.5720068231
812PhosphorylationLSMKFVSSLLTALFR
HHHHHHHHHHHHHHH		23.3020068231
815PhosphorylationKFVSSLLTALFRDSI
HHHHHHHHHHHHHHH		26.9720068231
821PhosphorylationLTALFRDSIQSHQES
HHHHHHHHHHHHHHH		20.4720068231
824PhosphorylationLFRDSIQSHQESLSV
HHHHHHHHHHHHHHH		26.0120068231
828PhosphorylationSIQSHQESLSVLRSS
HHHHHHHHHHHHHCC		21.2620068231
830PhosphorylationQSHQESLSVLRSSNE
HHHHHHHHHHHCCHH		28.5224719451
837 (in isoform 1)Ubiquitination-42.6521890473
837 (in isoform 2)Ubiquitination-42.6521890473
849UbiquitinationAVNVALQKVQQLKET
HHHHHHHHHHHHHHH		42.7521890473
849 (in isoform 3)Ubiquitination-42.7521890473
854AcetylationLQKVQQLKETGHVSG
HHHHHHHHHHCCCCC		49.2225953088
854UbiquitinationLQKVQQLKETGHVSG
HHHHHHHHHHCCCCC		49.2221906983
854 (in isoform 3)Ubiquitination-49.2221890473
869AcetylationPDGQNPEKIFQNLCD
CCCCCHHHHHHHHHH		50.5125953088
869UbiquitinationPDGQNPEKIFQNLCD
CCCCCHHHHHHHHHH		50.51-
879 (in isoform 1)Ubiquitination-19.8821890473
879 (in isoform 2)Ubiquitination-19.8821890473
892PhosphorylationYTSIPTSVEESGKKE
HCCCCCCHHHCCCCC		11.8617412408
895PhosphorylationIPTSVEESGKKEKGK
CCCCHHHCCCCCCCC		42.2728555341
897UbiquitinationTSVEESGKKEKGKSI
CCHHHCCCCCCCCCC		68.0289784
897 (in isoform 3)Ubiquitination-68.0221890473
898UbiquitinationSVEESGKKEKGKSIS
CHHHCCCCCCCCCCH		69.09-
900UbiquitinationEESGKKEKGKSISLL
HHCCCCCCCCCCHHH		79.22-
902UbiquitinationSGKKEKGKSISLLCL
CCCCCCCCCCHHHHH		56.54-
903PhosphorylationGKKEKGKSISLLCLE
CCCCCCCCCHHHHHH		26.5221712546
926UbiquitinationVQQFYQPKIQQFLRA
HHHHHHHHHHHHHHH		37.31-
937PhosphorylationFLRALDVTDKEGEER
HHHHCCCCCCCCCCC		40.8118691976
939UbiquitinationRALDVTDKEGEERED
HHCCCCCCCCCCCCC		59.2521906983
939 (in isoform 3)Ubiquitination-59.2521890473
950PhosphorylationEREDADVSVTQRTAF
CCCCCCCCCHHHHHH		21.7223186163
952PhosphorylationEDADVSVTQRTAFQI
CCCCCCCHHHHHHHH		12.5817525332
965PhosphorylationQIRQFQRSLLNLLSS
HHHHHHHHHHHHHHC		26.8220068231
971PhosphorylationRSLLNLLSSQEEDFN
HHHHHHHHCCCCCCC		32.8921712546
972PhosphorylationSLLNLLSSQEEDFNS
HHHHHHHCCCCCCCC		41.3917478428
979PhosphorylationSQEEDFNSKEALLLV
CCCCCCCCHHHHHHH		31.6920068231
1000PhosphorylationSKLLEPSSPQFVQML
HHHHCCCCHHHHHHH		33.17-
1015UbiquitinationSWTSKICKENSREDA
HHHHHHHHHCCHHHH		64.50-
1027PhosphorylationEDALFCKSLMNLLFS
HHHHHHHHHHHHHHH		33.75-
1039PhosphorylationLFSLHVSYKSPVILL
HHHHHCCCCCCEEEE		17.8829759185
1040UbiquitinationFSLHVSYKSPVILLR
HHHHCCCCCCEEEEC		40.55-
1045 (in isoform 1)Ubiquitination-3.0621890473
1045 (in isoform 2)Ubiquitination-3.0621890473
1047 (in isoform 1)Ubiquitination-39.1021890473
1050PhosphorylationVILLRDLSQDIHGHL
EEEECCCCCCCCCCC		30.0520873877
1061PhosphorylationHGHLGDIDQDVEVEK
CCCCCCCCCCCEEEE		43.2817412408
1068UbiquitinationDQDVEVEKTNHFAIV
CCCCEEEECCCEEEE		60.86-
1069PhosphorylationQDVEVEKTNHFAIVN
CCCEEEECCCEEEEE		22.0325599653
1105UbiquitinationEVDWLITKLKGQVSQ
HCHHHHHHHCCCCCH		41.0021890473
1105 (in isoform 3)Ubiquitination-41.0021890473
1107UbiquitinationDWLITKLKGQVSQET
HHHHHHHCCCCCHHH		49.1821906983
1107 (in isoform 3)Ubiquitination-49.1821890473
1111PhosphorylationTKLKGQVSQETLSEE
HHHCCCCCHHHHCHH		17.8923663014
1114PhosphorylationKGQVSQETLSEEASS
CCCCCHHHHCHHHHH		28.1323663014
1116PhosphorylationQVSQETLSEEASSQA
CCCHHHHCHHHHHCC		40.5923663014
1120PhosphorylationETLSEEASSQATLPN
HHHCHHHHHCCCCCC		26.6823401153
1121PhosphorylationTLSEEASSQATLPNQ
HHCHHHHHCCCCCCC		30.7717525332
1124PhosphorylationEEASSQATLPNQPVE
HHHHHCCCCCCCHHH		34.8023663014
1160 (in isoform 2)Ubiquitination-35.6421890473
1161 (in isoform 1)Ubiquitination-17.3721890473
1170PhosphorylationLKDLCKMYTTLTALV
HHHHHHHHHHHHHHH		5.1029759185
1171PhosphorylationKDLCKMYTTLTALVR
HHHHHHHHHHHHHHH		16.3029759185
1172PhosphorylationDLCKMYTTLTALVRY
HHHHHHHHHHHHHHH		12.4829759185
1187 (in isoform 2)Ubiquitination-18.3721890473
1188 (in isoform 1)Ubiquitination-43.2121890473
1196UbiquitinationGIPKNMEKLVKLSGS
CCCCCHHHHHHHCCC		48.05-
1199UbiquitinationKNMEKLVKLSGSHLT
CCHHHHHHHCCCCCH		47.58-
1221UbiquitinationSYVQNKSKSLNYTGE
HHHHCCCCCCCCCCC		61.6521890473
1221 (in isoform 3)Ubiquitination-61.6521890473
1225PhosphorylationNKSKSLNYTGEKKEK
CCCCCCCCCCCCCCH		22.7827642862
1230AcetylationLNYTGEKKEKPAAVA
CCCCCCCCCHHHHHH		67.6725953088
1230UbiquitinationLNYTGEKKEKPAAVA
CCCCCCCCCHHHHHH		67.67-
1232AcetylationYTGEKKEKPAAVATA
CCCCCCCHHHHHHHH		49.1625953088
1232UbiquitinationYTGEKKEKPAAVATA
CCCCCCCHHHHHHHH		49.16-
1238PhosphorylationEKPAAVATAMARVLR
CHHHHHHHHHHHHHH		15.4619413330
1248UbiquitinationARVLRETKPIPNLIF
HHHHHHCCCCCCEEH		35.882190698
1248 (in isoform 3)Ubiquitination-35.8821890473
1269UbiquitinationKFLIHLSKKSKVNLM
HHHHHHCCCCCCCHH		68.38-
1270UbiquitinationFLIHLSKKSKVNLMQ
HHHHHCCCCCCCHHH		52.73-
1272UbiquitinationIHLSKKSKVNLMQHM
HHHCCCCCCCHHHHH		43.98-
1280UbiquitinationVNLMQHMKLSTSRDF
CCHHHHHCCCCCCCC		36.84-
1283PhosphorylationMQHMKLSTSRDFKIK
HHHHCCCCCCCCEEC		37.9129449344
1284PhosphorylationQHMKLSTSRDFKIKG
HHHCCCCCCCCEECC		26.8625627689
1290UbiquitinationTSRDFKIKGNILDMV
CCCCCEECCCEEHHH		46.63-
1310PhosphorylationEDENEEGTASEHGGQ
CCCCCCCCCCCCCCC		30.2330576142
1312PhosphorylationENEEGTASEHGGQNK
CCCCCCCCCCCCCCC		29.9330576142
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
556SPhosphorylationKinaseATMQ13315
PSP
556SPhosphorylationKinaseATRQ13535
PSP
559SPhosphorylationKinaseATMQ13315
PSP
559SPhosphorylationKinaseATRQ13535
PSP
565SPhosphorylationKinaseATRQ13535
PSP
730SPhosphorylationKinaseATMQ13315
PSP
972SPhosphorylationKinaseATMQ13315
PSP
1121SPhosphorylationKinaseATMQ13315
PSP
-KUbiquitinationE3 ubiquitin ligaseFANCLQ9NW38
PMID:19111657
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
523Kubiquitylation

17412408
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 FANCI_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FACD2_HUMANFANCD2physical
19561358
FACD2_HUMANFANCD2physical
18931676
FACD2_HUMANFANCD2physical
17460694
WDR48_HUMANWDR48physical
21896657
FANCL_HUMANFANCLphysical
21775430
A4_HUMANAPPphysical
21832049
FACD2_HUMANFANCD2physical
24623813
IMDH2_HUMANIMPDH2physical
26344197
OST48_HUMANDDOSTphysical
26496610
STXB2_HUMANSTXBP2physical
26496610
PAPS1_HUMANPAPSS1physical
26496610
CIR1_HUMANCIR1physical
26496610
DGCR8_HUMANDGCR8physical
26496610
IMPCT_HUMANIMPACTphysical
26496610
PRR3_HUMANPRR3physical
26496610
DPY30_HUMANDPY30physical
26496610
PKHA8_HUMANPLEKHA8physical
26496610
FAP20_HUMANC1orf86physical
26496610
TIM23_HUMANTIMM23physical
26496610
REV1_HUMANREV1physical
26187992
UBL5_HUMANUBL5physical
25862789
FACD2_HUMANFANCD2physical
25862789
FANCI_HUMANFANCIphysical
25862789
MCM2_HUMANMCM2physical
25843623
MCM3_HUMANMCM3physical
25843623
MCM5_HUMANMCM5physical
25843623
FACD2_HUMANFANCD2physical
21719678
FACD2_HUMANFANCD2physical
25168188
FACD2_HUMANFANCD2physical
25319828
PHLP1_HUMANPHLPP1physical
27097374
AKT1_HUMANAKT1physical
27097374
FANCI_HUMANFANCIphysical
27686023
PHLP2_HUMANPHLPP2physical
27097374
FACD2_HUMANFANCD2physical
28684355
BRCA2_HUMANBRCA2physical
28684355
FACD2_HUMANFANCD2physical
28575658
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609053Fanconi anemia complementation group I (FANCI)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FANCI_HUMAN

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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-407, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, 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-407, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730; THR-952 ANDSER-1121, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.
"Identification of the FANCI protein, a monoubiquitinated FANCD2paralog required for DNA repair.";
Smogorzewska A., Matsuoka S., Vinciguerra P., McDonald E.R. III,Hurov K.E., Luo J., Ballif B.A., Gygi S.P., Hofmann K., D'Andrea A.D.,Elledge S.J.;
Cell 129:289-301(2007).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, UBIQUITINATION ATLYS-523, PHOSPHORYLATION AT SER-730; THR-952 AND SER-1121, SUBCELLULARLOCATION, INTERACTION WITH FANCD2, VARIANTS FA LEU-55 AND GLN-1285,AND CHARACTERIZATION OF VARIANTS FA LEU-55 AND GLN-1285.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-215, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL.";
Longerich S., San Filippo J., Liu D., Sung P.;
J. Biol. Chem. 284:23182-23186(2009).
Cited for: DNA-BINDING, UBIQUITINATION AT LYS-523, AND MUTAGENESIS OF LYS-523.
"FANCI is a second monoubiquitinated member of the Fanconi anemiapathway.";
Sims A.E., Spiteri E., Sims R.J. III, Arita A.G., Lach F.P.,Landers T., Wurm M., Freund M., Neveling K., Hanenberg H.,Auerbach A.D., Huang T.T.;
Nat. Struct. Mol. Biol. 14:564-567(2007).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, UBIQUITINATION ATLYS-523, SUBCELLULAR LOCATION, INTERACTION WITH FANCD2, AND VARIANT FATYR-858.
"Identification of the FANCI protein, a monoubiquitinated FANCD2paralog required for DNA repair.";
Smogorzewska A., Matsuoka S., Vinciguerra P., McDonald E.R. III,Hurov K.E., Luo J., Ballif B.A., Gygi S.P., Hofmann K., D'Andrea A.D.,Elledge S.J.;
Cell 129:289-301(2007).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, UBIQUITINATION ATLYS-523, PHOSPHORYLATION AT SER-730; THR-952 AND SER-1121, SUBCELLULARLOCATION, INTERACTION WITH FANCD2, VARIANTS FA LEU-55 AND GLN-1285,AND CHARACTERIZATION OF VARIANTS FA LEU-55 AND GLN-1285.

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