FANCJ_HUMAN - dbPTM
FANCJ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FANCJ_HUMAN
UniProt AC Q9BX63
Protein Name Fanconi anemia group J protein
Gene Name BRIP1
Organism Homo sapiens (Human).
Sequence Length 1249
Subcellular Localization Nucleus .
Protein Description DNA-dependent ATPase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination. Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1..
Protein Sequence MSSMWSEYTIGGVKIYFPYKAYPSQLAMMNSILRGLNSKQHCLLESPTGSGKSLALLCSALAWQQSLSGKPADEGVSEKAEVQLSCCCACHSKDFTNNDMNQGTSRHFNYPSTPPSERNGTSSTCQDSPEKTTLAAKLSAKKQASIYRDENDDFQVEKKRIRPLETTQQIRKRHCFGTEVHNLDAKVDSGKTVKLNSPLEKINSFSPQKPPGHCSRCCCSTKQGNSQESSNTIKKDHTGKSKIPKIYFGTRTHKQIAQITRELRRTAYSGVPMTILSSRDHTCVHPEVVGNFNRNEKCMELLDGKNGKSCYFYHGVHKISDQHTLQTFQGMCKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIEDCARESASYSVTEVQLRFARDELDSMVNNNIRKKDHEPLRAVCCSLINWLEANAEYLVERDYESACKIWSGNEMLLTLHKMGITTATFPILQGHFSAVLQKEEKISPIYGKEEAREVPVISASTQIMLKGLFMVLDYLFRQNSRFADDYKIAIQQTYSWTNQIDISDKNGLLVLPKNKKRSRQKTAVHVLNFWCLNPAVAFSDINGKVQTIVLTSGTLSPMKSFSSELGVTFTIQLEANHIIKNSQVWVGTIGSGPKGRNLCATFQNTETFEFQDEVGALLLSVCQTVSQGILCFLPSYKLLEKLKERWLSTGLWHNLELVKTVIVEPQGGEKTNFDELLQVYYDAIKYKGEKDGALLVAVCRGKVSEGLDFSDDNARAVITIGIPFPNVKDLQVELKRQYNDHHSKLRGLLPGRQWYEIQAYRALNQALGRCIRHRNDWGALILVDDRFRNNPSRYISGLSKWVRQQIQHHSTFESALESLAEFSKKHQKVLNVSIKDRTNIQDNESTLEVTSLKYSTPPYLLEAASHLSPENFVEDEAKICVQELQCPKIITKNSPLPSSIISRKEKNDPVFLEEAGKAEKIVISRSTSPTFNKQTKRVSWSSFNSLGQYFTGKIPKATPELGSSENSASSPPRFKTEKMESKTVLPFTDKCESSNLTVNTSFGSCPQSETIISSLKIDATLTRKNHSEHPLCSEEALDPDIELSLVSEEDKQSTSNRDFETEAEDESIYFTPELYDPEDTDEEKNDLAETDRGNRLANNSDCILAKDLFEIRTIKEVDSAREVKAEDCIDTKLNGILHIEESKIDDIDGNVKTTWINELELGKTHEIEIKNFKPSPSKNKGMFPGFK
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
2Phosphorylation------MSSMWSEYT
------CCCCCCEEE
39.9624505115
22PhosphorylationIYFPYKAYPSQLAMM
EECCCCCCHHHHHHH
10.16-
24PhosphorylationFPYKAYPSQLAMMNS
CCCCCCHHHHHHHHH
25.7524275569
39UbiquitinationILRGLNSKQHCLLES
HHHCCCCCCCEEEEC
42.8821963094
77PhosphorylationKPADEGVSEKAEVQL
CCCCCCCCCCCCHHE
44.2119413330
110PhosphorylationGTSRHFNYPSTPPSE
CCCCCCCCCCCCCHH
9.5230266825
112PhosphorylationSRHFNYPSTPPSERN
CCCCCCCCCCCHHCC
43.0930266825
113PhosphorylationRHFNYPSTPPSERNG
CCCCCCCCCCHHCCC
34.4130266825
116PhosphorylationNYPSTPPSERNGTSS
CCCCCCCHHCCCCCC
50.8530266825
121PhosphorylationPPSERNGTSSTCQDS
CCHHCCCCCCCCCCC
24.0523090842
122PhosphorylationPSERNGTSSTCQDSP
CHHCCCCCCCCCCCC
25.6623090842
123PhosphorylationSERNGTSSTCQDSPE
HHCCCCCCCCCCCCC
32.8023090842
124PhosphorylationERNGTSSTCQDSPEK
HCCCCCCCCCCCCCC
17.6023090842
128PhosphorylationTSSTCQDSPEKTTLA
CCCCCCCCCCCCHHH
14.7421712546
129UbiquitinationSSTCQDSPEKTTLAA
CCCCCCCCCCCHHHH
56.2321963094
131UbiquitinationTCQDSPEKTTLAAKL
CCCCCCCCCHHHHHH
50.6322817900
132PhosphorylationCQDSPEKTTLAAKLS
CCCCCCCCHHHHHHC
25.9428111955
133PhosphorylationQDSPEKTTLAAKLSA
CCCCCCCHHHHHHCH
26.0128111955
134UbiquitinationDSPEKTTLAAKLSAK
CCCCCCHHHHHHCHH
5.4422817900
137UbiquitinationEKTTLAAKLSAKKQA
CCCHHHHHHCHHHHH
37.0529967540
139PhosphorylationTTLAAKLSAKKQASI
CHHHHHHCHHHHHHH
37.0229978859
141AcetylationLAAKLSAKKQASIYR
HHHHHCHHHHHHHHC
41.8822792074
142UbiquitinationAAKLSAKKQASIYRD
HHHHCHHHHHHHHCC
51.3029967540
145PhosphorylationLSAKKQASIYRDEND
HCHHHHHHHHCCCCC
20.0528348404
146UbiquitinationSAKKQASIYRDENDD
CHHHHHHHHCCCCCC
3.5222817900
158UbiquitinationNDDFQVEKKRIRPLE
CCCCCEEECCCCCCC
48.7929967540
164UbiquitinationEKKRIRPLETTQQIR
EECCCCCCCHHHHHH
7.0222817900
165UbiquitinationKKRIRPLETTQQIRK
ECCCCCCCHHHHHHH
53.1122817900
167PhosphorylationRIRPLETTQQIRKRH
CCCCCCHHHHHHHHH
14.7623403867
167UbiquitinationRIRPLETTQQIRKRH
CCCCCCHHHHHHHHH
14.7622817900
179UbiquitinationKRHCFGTEVHNLDAK
HHHCCCCCEECCCCE
42.0022817900
184UbiquitinationGTEVHNLDAKVDSGK
CCCEECCCCEECCCC
50.0522817900
185UbiquitinationTEVHNLDAKVDSGKT
CCEECCCCEECCCCE
19.5522817900
186AcetylationEVHNLDAKVDSGKTV
CEECCCCEECCCCEE
46.3619825015
187UbiquitinationVHNLDAKVDSGKTVK
EECCCCEECCCCEEE
8.3122817900
191AcetylationDAKVDSGKTVKLNSP
CCEECCCCEEEECCC
54.8419825021
194AcetylationVDSGKTVKLNSPLEK
ECCCCEEEECCCHHH
47.3722792074
197PhosphorylationGKTVKLNSPLEKINS
CCEEEECCCHHHHHC
41.1026055452
204PhosphorylationSPLEKINSFSPQKPP
CCHHHHHCCCCCCCC
30.4923927012
206PhosphorylationLEKINSFSPQKPPGH
HHHHHCCCCCCCCCC
26.6623401153
215PhosphorylationQKPPGHCSRCCCSTK
CCCCCCCCCCCEECC
23.7623927012
222UbiquitinationSRCCCSTKQGNSQES
CCCCEECCCCCCCHH
39.66-
226PhosphorylationCSTKQGNSQESSNTI
EECCCCCCCHHCCCC
41.9920363803
229PhosphorylationKQGNSQESSNTIKKD
CCCCCCHHCCCCCCC
22.6628102081
230PhosphorylationQGNSQESSNTIKKDH
CCCCCHHCCCCCCCC
36.9228102081
232PhosphorylationNSQESSNTIKKDHTG
CCCHHCCCCCCCCCC
35.8028985074
234UbiquitinationQESSNTIKKDHTGKS
CHHCCCCCCCCCCCC
50.54-
235UbiquitinationESSNTIKKDHTGKSK
HHCCCCCCCCCCCCC
51.39-
244UbiquitinationHTGKSKIPKIYFGTR
CCCCCCCCEEEECCC
22.2621890473
254UbiquitinationYFGTRTHKQIAQITR
EECCCCHHHHHHHHH
42.6729967540
266PhosphorylationITRELRRTAYSGVPM
HHHHHHHHHHCCCCE
24.4225954137
274PhosphorylationAYSGVPMTILSSRDH
HHCCCCEEEEECCCC
16.8225954137
277PhosphorylationGVPMTILSSRDHTCV
CCCEEEEECCCCCCC
21.3425954137
278PhosphorylationVPMTILSSRDHTCVH
CCEEEEECCCCCCCC
37.9825954137
297UbiquitinationGNFNRNEKCMELLDG
CCCCCCHHHHHHHCC
42.29-
336UbiquitinationQGMCKAWDIEELVSL
HHHHHHCCHHHHHHH
43.1927667366
345UbiquitinationEELVSLGKKLKACPY
HHHHHHCHHHCCCCC
61.2922817900
345 (in isoform 1)Ubiquitination-61.2921890473
345 (in isoform 2)Ubiquitination-61.2921890473
346UbiquitinationELVSLGKKLKACPYY
HHHHHCHHHCCCCCC
54.1222817900
348UbiquitinationVSLGKKLKACPYYTA
HHHCHHHCCCCCCCH
57.7422817900
424PhosphorylationFARDELDSMVNNNIR
HHHHHHHHHHHCCCC
36.9425954137
461PhosphorylationEYLVERDYESACKIW
HHHHHCCHHHHHCHH
20.29-
503UbiquitinationAVLQKEEKISPIYGK
HHHCCCCCCCCCCCC
49.9629967540
505PhosphorylationLQKEEKISPIYGKEE
HCCCCCCCCCCCCHH
19.1325849741
508PhosphorylationEEKISPIYGKEEARE
CCCCCCCCCCHHHCC
26.0630266825
510AcetylationKISPIYGKEEAREVP
CCCCCCCCHHHCCCC
35.1026051181
510UbiquitinationKISPIYGKEEAREVP
CCCCCCCCHHHCCCC
35.1033845483
542PhosphorylationDYLFRQNSRFADDYK
HHHHHCCCCCCCHHH
22.0420068231
548PhosphorylationNSRFADDYKIAIQQT
CCCCCCHHHEEEEEE
12.5820068231
575MethylationNGLLVLPKNKKRSRQ
CCEEEEECCCCCCCC
76.7824129315
584PhosphorylationKKRSRQKTAVHVLNF
CCCCCCCCHHHHHHH
26.1019413330
586UbiquitinationRSRQKTAVHVLNFWC
CCCCCCHHHHHHHHH
3.7721963094
588UbiquitinationRQKTAVHVLNFWCLN
CCCCHHHHHHHHHCC
3.6222817900
591UbiquitinationTAVHVLNFWCLNPAV
CHHHHHHHHHCCHHH
4.2222817900
603UbiquitinationPAVAFSDINGKVQTI
HHHEHHHCCCCEEEE
7.6822817900
606UbiquitinationAFSDINGKVQTIVLT
EHHHCCCCEEEEEEE
27.0421963094
608UbiquitinationSDINGKVQTIVLTSG
HHCCCCEEEEEEECC
29.0622817900
611UbiquitinationNGKVQTIVLTSGTLS
CCCEEEEEEECCCCC
5.6122817900
618PhosphorylationVLTSGTLSPMKSFSS
EEECCCCCCCCCCCC
23.8420068231
623UbiquitinationTLSPMKSFSSELGVT
CCCCCCCCCCCCCCE
8.5322817900
636UbiquitinationVTFTIQLEANHIIKN
CEEEEEEECCEEEEC
30.9322817900
656UbiquitinationGTIGSGPKGRNLCAT
EECCCCCCCCCEEEE
74.2222817900
700UbiquitinationCFLPSYKLLEKLKER
HHCCCHHHHHHHHHH
5.9221963094
701UbiquitinationFLPSYKLLEKLKERW
HCCCHHHHHHHHHHH
4.8221890473
702UbiquitinationLPSYKLLEKLKERWL
CCCHHHHHHHHHHHH
67.7722817900
705UbiquitinationYKLLEKLKERWLSTG
HHHHHHHHHHHHHCC
57.1922817900
717UbiquitinationSTGLWHNLELVKTVI
HCCCCCCCEEEEEEE
3.3022817900
721UbiquitinationWHNLELVKTVIVEPQ
CCCCEEEEEEEECCC
50.1021890473
727UbiquitinationVKTVIVEPQGGEKTN
EEEEEECCCCCCCCC
27.5021963094
729UbiquitinationTVIVEPQGGEKTNFD
EEEECCCCCCCCCHH
57.8722817900
732UbiquitinationVEPQGGEKTNFDELL
ECCCCCCCCCHHHHH
52.6322817900
742PhosphorylationFDELLQVYYDAIKYK
HHHHHHHHHHHHHCC
5.2219835603
744UbiquitinationELLQVYYDAIKYKGE
HHHHHHHHHHHCCCC
24.9122817900
747UbiquitinationQVYYDAIKYKGEKDG
HHHHHHHHCCCCCCC
42.5021963094
747 (in isoform 2)Ubiquitination-42.50-
749UbiquitinationYYDAIKYKGEKDGAL
HHHHHHCCCCCCCCE
56.4422817900
750UbiquitinationYDAIKYKGEKDGALL
HHHHHCCCCCCCCEE
44.0622817900
752UbiquitinationAIKYKGEKDGALLVA
HHHCCCCCCCCEEEE
70.8622817900
764UbiquitinationLVAVCRGKVSEGLDF
EEEEECCCCCCCCCC
24.2021906983
764 (in isoform 1)Ubiquitination-24.2021890473
764 (in isoform 2)Ubiquitination-24.2021890473
767UbiquitinationVCRGKVSEGLDFSDD
EECCCCCCCCCCCCC
67.7621963094
769UbiquitinationRGKVSEGLDFSDDNA
CCCCCCCCCCCCCCC
5.4322817900
772UbiquitinationVSEGLDFSDDNARAV
CCCCCCCCCCCCCEE
43.6622817900
777UbiquitinationDFSDDNARAVITIGI
CCCCCCCCEEEEEEE
35.3222817900
784UbiquitinationRAVITIGIPFPNVKD
CEEEEEEECCCCHHH
2.5522817900
793UbiquitinationFPNVKDLQVELKRQY
CCCHHHHHHHHHHHH
36.4527667366
797UbiquitinationKDLQVELKRQYNDHH
HHHHHHHHHHHCCHH
24.7721906983
797 (in isoform 1)Ubiquitination-24.7721890473
797 (in isoform 2)Ubiquitination-24.7721890473
813UbiquitinationKLRGLLPGRQWYEIQ
HHCCCCCCCCHHHHH
34.0927667366
815UbiquitinationRGLLPGRQWYEIQAY
CCCCCCCCHHHHHHH
53.6821890473
817UbiquitinationLLPGRQWYEIQAYRA
CCCCCCHHHHHHHHH
8.5322817900
842UbiquitinationHRNDWGALILVDDRF
CCCCCCCEEEECHHH
2.4721890473
862UbiquitinationRYISGLSKWVRQQIQ
HHHHHHHHHHHHHHH
55.5422817900
862 (in isoform 1)Ubiquitination-55.5421890473
862 (in isoform 2)Ubiquitination-55.5421890473
882UbiquitinationESALESLAEFSKKHQ
HHHHHHHHHHHHHHH
25.6821890473
895PhosphorylationHQKVLNVSIKDRTNI
HHHEECEEECCCCCC
23.8923186163
897AcetylationKVLNVSIKDRTNIQD
HEECEEECCCCCCCC
33.3822792074
897UbiquitinationKVLNVSIKDRTNIQD
HEECEEECCCCCCCC
33.3829967540
907PhosphorylationTNIQDNESTLEVTSL
CCCCCCCCEEEEEEE
44.5428555341
907UbiquitinationTNIQDNESTLEVTSL
CCCCCCCCEEEEEEE
44.5427667366
913PhosphorylationESTLEVTSLKYSTPP
CCEEEEEEEEECCCH
28.2130631047
916PhosphorylationLEVTSLKYSTPPYLL
EEEEEEEECCCHHHH
24.0721712546
917PhosphorylationEVTSLKYSTPPYLLE
EEEEEEECCCHHHHH
32.6128450419
918PhosphorylationVTSLKYSTPPYLLEA
EEEEEECCCHHHHHH
25.7826055452
921PhosphorylationLKYSTPPYLLEAASH
EEECCCHHHHHHHHC
25.7321712546
927PhosphorylationPYLLEAASHLSPENF
HHHHHHHHCCCHHHC
31.8222115753
930PhosphorylationLEAASHLSPENFVED
HHHHHCCCHHHCCCC
25.4126055452
934UbiquitinationSHLSPENFVEDEAKI
HCCCHHHCCCCHHHH
6.4127667366
953PhosphorylationLQCPKIITKNSPLPS
HCCCCEECCCCCCCH
27.8728450419
954AcetylationQCPKIITKNSPLPSS
CCCCEECCCCCCCHH
45.0522792074
954UbiquitinationQCPKIITKNSPLPSS
CCCCEECCCCCCCHH
45.0527667366
956PhosphorylationPKIITKNSPLPSSII
CCEECCCCCCCHHHH
29.3925159151
960PhosphorylationTKNSPLPSSIISRKE
CCCCCCCHHHHCCCC
41.6829978859
961PhosphorylationKNSPLPSSIISRKEK
CCCCCCHHHHCCCCC
23.2320068231
964PhosphorylationPLPSSIISRKEKNDP
CCCHHHHCCCCCCCC
35.3120068231
966AcetylationPSSIISRKEKNDPVF
CHHHHCCCCCCCCCC
67.2722792074
974UbiquitinationEKNDPVFLEEAGKAE
CCCCCCCHHHCCCCE
6.2227667366
982UbiquitinationEEAGKAEKIVISRST
HHCCCCEEEEEECCC
47.3229967540
986PhosphorylationKAEKIVISRSTSPTF
CCEEEEEECCCCCCC
14.8625849741
988PhosphorylationEKIVISRSTSPTFNK
EEEEEECCCCCCCCC
26.8430266825
989PhosphorylationKIVISRSTSPTFNKQ
EEEEECCCCCCCCCC
37.3030266825
990PhosphorylationIVISRSTSPTFNKQT
EEEECCCCCCCCCCC
24.1623401153
992PhosphorylationISRSTSPTFNKQTKR
EECCCCCCCCCCCCC
39.3430266825
1001PhosphorylationNKQTKRVSWSSFNSL
CCCCCCEEHHHCHHH
25.8525159151
1003PhosphorylationQTKRVSWSSFNSLGQ
CCCCEEHHHCHHHHH
19.9728450419
1004PhosphorylationTKRVSWSSFNSLGQY
CCCEEHHHCHHHHHH
23.3728450419
1007PhosphorylationVSWSSFNSLGQYFTG
EEHHHCHHHHHHHHC
31.6922199227
1011PhosphorylationSFNSLGQYFTGKIPK
HCHHHHHHHHCCCCC
10.9920068231
1013PhosphorylationNSLGQYFTGKIPKAT
HHHHHHHHCCCCCCC
32.4120068231
1015AcetylationLGQYFTGKIPKATPE
HHHHHHCCCCCCCCC
53.4222792074
1020PhosphorylationTGKIPKATPELGSSE
HCCCCCCCCCCCCCC
24.3426074081
1025PhosphorylationKATPELGSSENSASS
CCCCCCCCCCCCCCC
47.2930108239
1026PhosphorylationATPELGSSENSASSP
CCCCCCCCCCCCCCC
38.7128176443
1029PhosphorylationELGSSENSASSPPRF
CCCCCCCCCCCCCCC
26.0223401153
1031PhosphorylationGSSENSASSPPRFKT
CCCCCCCCCCCCCCC
43.1030266825
1032PhosphorylationSSENSASSPPRFKTE
CCCCCCCCCCCCCCE
38.3429255136
1038PhosphorylationSSPPRFKTEKMESKT
CCCCCCCCEECCCCC
37.8226074081
1045PhosphorylationTEKMESKTVLPFTDK
CEECCCCCEEECCCC
36.23-
1050PhosphorylationSKTVLPFTDKCESSN
CCCEEECCCCCCCCC
32.39-
1062PhosphorylationSSNLTVNTSFGSCPQ
CCCCEEECCCCCCCC
22.5425627689
1063PhosphorylationSNLTVNTSFGSCPQS
CCCEEECCCCCCCCC
23.5425159151
1075PhosphorylationPQSETIISSLKIDAT
CCCHHHHHHCEEEEE
26.2624719451
1082PhosphorylationSSLKIDATLTRKNHS
HHCEEEEEEECCCCC
25.5528555341
1106PhosphorylationLDPDIELSLVSEEDK
CCCCCEEEECCHHHH
17.5929449344
1109PhosphorylationDIELSLVSEEDKQST
CCEEEECCHHHHCCC
40.3325849741
1115PhosphorylationVSEEDKQSTSNRDFE
CCHHHHCCCCCCCCC
39.2729449344
1116PhosphorylationSEEDKQSTSNRDFET
CHHHHCCCCCCCCCC
27.7729449344
1117PhosphorylationEEDKQSTSNRDFETE
HHHHCCCCCCCCCCH
34.8130576142
1131PhosphorylationEAEDESIYFTPELYD
HHCCCCEEECCHHCC
15.6427642862
1133PhosphorylationEDESIYFTPELYDPE
CCCCEEECCHHCCCC
10.0125849741
1137PhosphorylationIYFTPELYDPEDTDE
EEECCHHCCCCCCCH
27.9930576142
1142PhosphorylationELYDPEDTDEEKNDL
HHCCCCCCCHHHCCC
43.5825849741
1162PhosphorylationGNRLANNSDCILAKD
HCCCCCCCCCEEECC
33.4021815630
1168AcetylationNSDCILAKDLFEIRT
CCCCEEECCCEEEEE
52.067367787
1168UbiquitinationNSDCILAKDLFEIRT
CCCCEEECCCEEEEE
52.0629967540
1181PhosphorylationRTIKEVDSAREVKAE
EEEEECCCCCEECHH
34.1120068231
1214UbiquitinationDDIDGNVKTTWINEL
CCCCCCEEEEEEEEE
44.2129967540
1216PhosphorylationIDGNVKTTWINELEL
CCCCEEEEEEEEEEC
20.7330387612
1237PhosphorylationEIKNFKPSPSKNKGM
EEECCCCCCCCCCCC
42.2523401153
1239PhosphorylationKNFKPSPSKNKGMFP
ECCCCCCCCCCCCCC
53.8830266825
1240AcetylationNFKPSPSKNKGMFPG
CCCCCCCCCCCCCCC
67.0922792074
1242AcetylationKPSPSKNKGMFPGFK
CCCCCCCCCCCCCCC
56.3322792074
1249AcetylationKGMFPGFK-------
CCCCCCCC-------
66.4022792074

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 ligaseFBXL17Q9UF56
PMID:24658274

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1249KAcetylation

22792074

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 FANCJ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRCA1_HUMANBRCA1physical
15242590
BLM_HUMANBLMphysical
21240188
BRCA1_HUMANBRCA1physical
21240188
PMS2_HUMANPMS2physical
20978114
MLH1_HUMANMLH1physical
20978114
MLH1_HUMANMLH1physical
20173781
BRCA1_HUMANBRCA1physical
20173781
TOPB1_HUMANTOPBP1physical
20159562
RFA1_HUMANRPA1physical
20159562
RFA1_HUMANRPA1physical
17596542
MLH1_HUMANMLH1physical
17581638
PMS2_HUMANPMS2physical
17581638
BRCA1_HUMANBRCA1physical
17581638
BRCA1_HUMANBRCA1physical
17596542
BRCA1_HUMANBRCA1physical
22032289
BARD1_HUMANBARD1physical
27399284
BRCA1_HUMANBRCA1physical
27399284
CBX3_HUMANCBX3physical
27399284
H31_HUMANHIST1H3Aphysical
27399284
MLH1_HUMANMLH1physical
24966277
MSH2_HUMANMSH2genetic
24966277
MLH1_HUMANMLH1physical
22968820
PMS2_HUMANPMS2physical
22968820
FACD2_HUMANFANCD2physical
26336824
FANCJ_HUMANBRIP1physical
22582397
MRE11_HUMANMRE11Aphysical
23530059
RAD50_HUMANRAD50physical
23530059
BRCA1_HUMANBRCA1physical
23530059
TOPB1_HUMANTOPBP1physical
23157317
FACD2_HUMANFANCD2physical
25070891
SPTA1_HUMANSPTA1physical
16889989
FANCJ_HUMANBRIP1physical
24573678
TOPB1_HUMANTOPBP1physical
24573678
MLH1_HUMANMLH1physical
24573678
BRCA1_HUMANBRCA1physical
24573678
DPOLN_HUMANPOLNphysical
26269593

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
114480Breast cancer (BC)
609054Fanconi anemia complementation group J (FANCJ)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FANCJ_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-930; SER-1031 ANDSER-1032, AND MASS SPECTROMETRY.
"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-77 AND SER-1032, ANDMASS SPECTROMETRY.
"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 THR-918; TYR-921; SER-927;SER-930 AND SER-990, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND THR-113, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1032, AND MASSSPECTROMETRY.
"The BRCT domain is a phospho-protein binding domain.";
Yu X., Chini C.C.S., He M., Mer G., Chen J.;
Science 302:639-642(2003).
Cited for: PHOSPHORYLATION AT SER-990, AND MUTAGENESIS OF SER-986; SER-988;THR-989; SER-990; PRO-991; THR-992; PHE-993; THR-997; SER-1001;SER-1003; SER-1004; SER-1007; TYR-1011 AND THR-1013.

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