FANCM_HUMAN - dbPTM
FANCM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FANCM_HUMAN
UniProt AC Q8IYD8
Protein Name Fanconi anemia group M protein
Gene Name FANCM
Organism Homo sapiens (Human).
Sequence Length 2048
Subcellular Localization Nucleus .
Protein Description DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. [PubMed: 16116422 Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage]
Protein Sequence MSGRQRTLFQTWGSSISRSSGTPGCSSGTERPQSPGSSKAPLPAAAEAQLESDDDVLLVAAYEAERQLCLENGGFCTSAGALWIYPTNCPVRDYQLHISRAALFCNTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQIEACYQVMGIPQSHMAEMTGSTQASTRKEIWCSKRVLFLTPQVMVNDLSRGACPAAEIKCLVIDEAHKALGNYAYCQVVRELVKYTNHFRILALSATPGSDIKAVQQVITNLLIGQIELRSEDSPDILTYSHERKVEKLIVPLGEELAAIQKTYIQILESFARSLIQRNVLMRRDIPNLTKYQIILARDQFRKNPSPNIVGIQQGIIEGEFAICISLYHGYELLQQMGMRSLYFFLCGIMDGTKGMTRSKNELGRNEDFMKLYNHLECMFARTRSTSANGISAIQQGDKNKKFVYSHPKLKKLEEVVIEHFKSWNAENTTEKKRDETRVMIFSSFRDSVQEIAEMLSQHQPIIRVMTFVGHASGKSTKGFTQKEQLEVVKQFRDGGYNTLVSTCVGEEGLDIGEVDLIICFDSQKSPIRLVQRMGRTGRKRQGRIVIILSEGREERIYNQSQSNKRSIYKAISSNRQVLHFYQRSPRMVPDGINPKLHKMFITHGVYEPEKPSRNLQRKSSIFSYRDGMRQSSLKKDWFLSEEEFKLWNRLYRLRDSDEIKEITLPQVQFSSLQNEENKPAQESTTGIHQLSLSEWRLWQDHPLPTHQVDHSDRCRHFIGLMQMIEGMRHEEGECSYELEVESYLQMEDVTSTFIAPRNESNNLASDTFITHKKSSFIKNINQGSSSSVIESDEECAEIVKQTHIKPTKIVSLKKKVSKEIKKDQLKKENNHGIIDSVDNDRNSTVENIFQEDLPNDKRTSDTDEIAATCTINENVIKEPCVLLTECQFTNKSTSSLAGNVLDSGYNSFNDEKSVSSNLFLPFEEELYIVRTDDQFYNCHSLTKEVLANVERFLSYSPPPLSGLSDLEYEIAKGTALENLLFLPCAEHLRSDKCTCLLSHSAVNSQQNLELNSLKCINYPSEKSCLYDIPNDNISDEPSLCDCDVHKHNQNENLVPNNRVQIHRSPAQNLVGENNHDVDNSDLPVLSTDQDESLLLFEDVNTEFDDVSLSPLNSKSESLPVSDKTAISETPLVSQFLISDELLLDNNSELQDQITRDANSFKSRDQRGVQEEKVKNHEDIFDCSRDLFSVTFDLGFCSPDSDDEILEHTSDSNRPLDDLYGRYLEIKEISDANYVSNQALIPRDHSKNFTSGTVIIPSNEDMQNPNYVHLPLSAAKNEELLSPGYSQFSLPVQKKVMSTPLSKSNTLNSFSKIRKEILKTPDSSKEKVNLQRFKEALNSTFDYSEFSLEKSKSSGPMYLHKSCHSVEDGQLLTSNESEDDEIFRRKVKRAKGNVLNSPEDQKNSEVDSPLHAVKKRRFPINRSELSSSDESENFPKPCSQLEDFKVCNGNARRGIKVPKRQSHLKHVARKFLDDEAELSEEDAEYVSSDENDESENEQDSSLLDFLNDETQLSQAINDSEMRAIYMKSLRSPMMNNKYKMIHKTHKNINIFSQIPEQDETYLEDSFCVDEEESCKGQSSEEEVCVDFNLITDDCFANSKKYKTRRAVMLKEMMEQNCAHSKKKLSRIILPDDSSEEENNVNDKRESNIAVNPSTVKKNKQQDHCLNSVPSGSSAQSKVRSTPRVNPLAKQSKQTSLNLKDTISEVSDFKPQNHNEVQSTTPPFTTVDSQKDCRKFPVPQKDGSALEDSSTSGASCSKSRPHLAGTHTSLRLPQEGKGTCILVGGHEITSGLEVISSLRAIHGLQVEVCPLNGCDYIVSNRMVVERRSQSEMLNSVNKNKFIEQIQHLQSMFERICVIVEKDREKTGDTSRMFRRTKSYDSLLTTLIGAGIRILFSSCQEETADLLKELSLVEQRKNVGIHVPTVVNSNKSEALQFYLSIPNISYITALNMCHQFSSVKRMANSSLQEISMYAQVTHQKAEEIYRYIHYVFDIQMLPNDLNQDRLKSDI
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
7Phosphorylation-MSGRQRTLFQTWGS
-CCCCCCHHHHHCCC
24.4822468782
11PhosphorylationRQRTLFQTWGSSISR
CCCHHHHHCCCCHHC
25.1822468782
14PhosphorylationTLFQTWGSSISRSSG
HHHHHCCCCHHCCCC
18.9622468782
19PhosphorylationWGSSISRSSGTPGCS
CCCCHHCCCCCCCCC
26.7423186163
20PhosphorylationGSSISRSSGTPGCSS
CCCHHCCCCCCCCCC
45.6423186163
22PhosphorylationSISRSSGTPGCSSGT
CHHCCCCCCCCCCCC
20.6023186163
26PhosphorylationSSGTPGCSSGTERPQ
CCCCCCCCCCCCCCC
37.4023927012
27PhosphorylationSGTPGCSSGTERPQS
CCCCCCCCCCCCCCC
54.5323927012
29PhosphorylationTPGCSSGTERPQSPG
CCCCCCCCCCCCCCC
30.6723927012
34PhosphorylationSGTERPQSPGSSKAP
CCCCCCCCCCCCCCC
33.6323401153
37PhosphorylationERPQSPGSSKAPLPA
CCCCCCCCCCCCCCH
31.8628450419
38PhosphorylationRPQSPGSSKAPLPAA
CCCCCCCCCCCCCHH
38.4628450419
52PhosphorylationAAEAQLESDDDVLLV
HHHHHCCCCCCEEEH
55.7324532841
123UbiquitinationGKTFIAAVVMYNFYR
CHHHHHHHHHHHHHH
1.5627667366
197UbiquitinationTPQVMVNDLSRGACP
CCHHHHCCCCCCCCC
34.3127667366
245PhosphorylationHFRILALSATPGSDI
CCEEEEEECCCCCHH
25.2123403867
247PhosphorylationRILALSATPGSDIKA
EEEEEECCCCCHHHH
25.4723403867
250PhosphorylationALSATPGSDIKAVQQ
EEECCCCCHHHHHHH
37.0523403867
262UbiquitinationVQQVITNLLIGQIEL
HHHHHHHHHHCCEEE
2.4929967540
271PhosphorylationIGQIELRSEDSPDIL
HCCEEECCCCCCCCC
59.3824719451
274PhosphorylationIELRSEDSPDILTYS
EEECCCCCCCCCCCC
22.0324719451
281PhosphorylationSPDILTYSHERKVEK
CCCCCCCCCCCCEEE
17.4024719451
288UbiquitinationSHERKVEKLIVPLGE
CCCCCEEEEEECCHH
46.6429967540
310PhosphorylationTYIQILESFARSLIQ
HHHHHHHHHHHHHHH
22.29-
393PhosphorylationLCGIMDGTKGMTRSK
HHHHHCCCCCCCCCC
21.84-
397PhosphorylationMDGTKGMTRSKNELG
HCCCCCCCCCCCCCC
40.22-
400AcetylationTKGMTRSKNELGRNE
CCCCCCCCCCCCCCH
51.677483995
413UbiquitinationNEDFMKLYNHLECMF
CHHHHHHHHHHHHHH
8.6029967540
416UbiquitinationFMKLYNHLECMFART
HHHHHHHHHHHHHCC
4.8929967540
432PhosphorylationSTSANGISAIQQGDK
CCCCCCCCCEECCCC
22.25-
436UbiquitinationNGISAIQQGDKNKKF
CCCCCEECCCCCCCE
56.8129967540
439UbiquitinationSAIQQGDKNKKFVYS
CCEECCCCCCCEEEC
76.9829967540
442UbiquitinationQQGDKNKKFVYSHPK
ECCCCCCCEEECCHH
49.8329967540
462UbiquitinationEVVIEHFKSWNAENT
HHHHHHHHHCCCCCC
57.3729967540
470PhosphorylationSWNAENTTEKKRDET
HCCCCCCCCCCCCCC
58.3418452278
477PhosphorylationTEKKRDETRVMIFSS
CCCCCCCCEEEEEHH
32.6229083192
483PhosphorylationETRVMIFSSFRDSVQ
CCEEEEEHHHHHHHH
20.0329083192
484PhosphorylationTRVMIFSSFRDSVQE
CEEEEEHHHHHHHHH
17.3529083192
492UbiquitinationFRDSVQEIAEMLSQH
HHHHHHHHHHHHHCC
1.8927667366
497UbiquitinationQEIAEMLSQHQPIIR
HHHHHHHHCCCCCEE
25.0629967540
518UbiquitinationHASGKSTKGFTQKEQ
CCCCCCCCCCCHHHH
60.1527667366
523UbiquitinationSTKGFTQKEQLEVVK
CCCCCCHHHHHHHHH
44.3529967540
540UbiquitinationRDGGYNTLVSTCVGE
HCCCCCCEEEEECCC
2.2627667366
551UbiquitinationCVGEEGLDIGEVDLI
ECCCCCCCCCCCEEE
58.6727667366
609PhosphorylationQSNKRSIYKAISSNR
CCCHHHHHHHHHCCC
8.8022817900
614PhosphorylationSIYKAISSNRQVLHF
HHHHHHHCCCCEEEE
29.8922817900
643PhosphorylationKLHKMFITHGVYEPE
HHHHHHHHCCCCCCC
11.0028509920
647PhosphorylationMFITHGVYEPEKPSR
HHHHCCCCCCCCCCC
30.2928509920
650UbiquitinationTHGVYEPEKPSRNLQ
HCCCCCCCCCCCCCC
66.7029967540
653PhosphorylationVYEPEKPSRNLQRKS
CCCCCCCCCCCCCCH
44.8928509920
660PhosphorylationSRNLQRKSSIFSYRD
CCCCCCCHHHHCCCC
30.7526434776
661PhosphorylationRNLQRKSSIFSYRDG
CCCCCCHHHHCCCCC
30.5926434776
664PhosphorylationQRKSSIFSYRDGMRQ
CCCHHHHCCCCCCCC
20.0023186163
665PhosphorylationRKSSIFSYRDGMRQS
CCHHHHCCCCCCCCC
11.2823186163
676UbiquitinationMRQSSLKKDWFLSEE
CCCCCCCCCCCCCHH
66.5429967540
807UbiquitinationESNNLASDTFITHKK
CCCCCCCCCEEECCH
39.7827667366
816PhosphorylationFITHKKSSFIKNINQ
EEECCHHHHHCCCCC
39.6124719451
818UbiquitinationTHKKSSFIKNINQGS
ECCHHHHHCCCCCCC
3.4527667366
823UbiquitinationSFIKNINQGSSSSVI
HHHCCCCCCCCCCCC
49.72-
825PhosphorylationIKNINQGSSSSVIES
HCCCCCCCCCCCCCC
19.7927251275
826PhosphorylationKNINQGSSSSVIESD
CCCCCCCCCCCCCCH
33.1927251275
827PhosphorylationNINQGSSSSVIESDE
CCCCCCCCCCCCCHH
30.2627251275
828PhosphorylationINQGSSSSVIESDEE
CCCCCCCCCCCCHHH
29.1227251275
832PhosphorylationSSSSVIESDEECAEI
CCCCCCCCHHHHHHH
38.9230576142
849UbiquitinationQTHIKPTKIVSLKKK
HCCCCCCEEEECHHH
50.03-
852PhosphorylationIKPTKIVSLKKKVSK
CCCCEEEECHHHHCH
37.6328258704
859AcetylationSLKKKVSKEIKKDQL
ECHHHHCHHHHHHHH
67.4618584559
862AcetylationKKVSKEIKKDQLKKE
HHHCHHHHHHHHHHH
51.9218584565
867AcetylationEIKKDQLKKENNHGI
HHHHHHHHHHCCCCC
53.0218584571
872UbiquitinationQLKKENNHGIIDSVD
HHHHHCCCCCCCCCC
40.1729967540
881UbiquitinationIIDSVDNDRNSTVEN
CCCCCCCCCCCHHHH
46.8327667366
892UbiquitinationTVENIFQEDLPNDKR
HHHHHHHHCCCCCCC
51.2527667366
898UbiquitinationQEDLPNDKRTSDTDE
HHCCCCCCCCCCHHH
65.3029967540
948PhosphorylationVLDSGYNSFNDEKSV
CHHCCCCCCCCCCCC
19.5525159151
995PhosphorylationANVERFLSYSPPPLS
HCHHHHHCCCCCCCC
22.3528387310
996PhosphorylationNVERFLSYSPPPLSG
CHHHHHCCCCCCCCC
27.6128450419
997PhosphorylationVERFLSYSPPPLSGL
HHHHHCCCCCCCCCC
27.7928348404
1002PhosphorylationSYSPPPLSGLSDLEY
CCCCCCCCCCCHHHH
43.3826074081
1005PhosphorylationPPPLSGLSDLEYEIA
CCCCCCCCHHHHHHH
43.6123186163
1045PhosphorylationLSHSAVNSQQNLELN
ECCHHCCCCCCEECC
26.92-
1067PhosphorylationPSEKSCLYDIPNDNI
CCCCCCCEECCCCCC
19.0227642862
1158PhosphorylationPLNSKSESLPVSDKT
CCCCCCCCCCCCCCC
45.0925159151
1162PhosphorylationKSESLPVSDKTAISE
CCCCCCCCCCCCCCC
31.3025159151
1176UbiquitinationETPLVSQFLISDELL
CCCCCHHHHHCCHHH
5.2227667366
1187UbiquitinationDELLLDNNSELQDQI
CHHHCCCCHHHHHHH
36.2127667366
1202UbiquitinationTRDANSFKSRDQRGV
HHCHHHHHCHHHHCC
44.3927667366
1213UbiquitinationQRGVQEEKVKNHEDI
HHCCCHHHHCCCHHH
58.7327667366
1322PhosphorylationAKNEELLSPGYSQFS
HCCHHHCCCCCCCCC
28.9821815630
1326PhosphorylationELLSPGYSQFSLPVQ
HHCCCCCCCCCCCCC
30.5725627689
1342O-linked_GlycosylationKVMSTPLSKSNTLNS
HHHCCCCCCCCCHHH
34.9330379171
1349PhosphorylationSKSNTLNSFSKIRKE
CCCCCHHHHHHHHHH
33.7324719451
1352AcetylationNTLNSFSKIRKEILK
CCHHHHHHHHHHHHC
44.5125953088
1413PhosphorylationVEDGQLLTSNESEDD
CCCCCCCCCCCCCCH
37.7930576142
1414PhosphorylationEDGQLLTSNESEDDE
CCCCCCCCCCCCCHH
38.2729449344
1417PhosphorylationQLLTSNESEDDEIFR
CCCCCCCCCCHHHHH
51.0425849741
1437PhosphorylationAKGNVLNSPEDQKNS
HHCCCCCCHHHHCCC
26.0429255136
1444PhosphorylationSPEDQKNSEVDSPLH
CHHHHCCCCCCCHHH
46.1321815630
1448PhosphorylationQKNSEVDSPLHAVKK
HCCCCCCCHHHHHHH
34.2421815630
1551UbiquitinationDFLNDETQLSQAIND
HHHCCHHHHHHHCCH
36.7530230243
1568PhosphorylationMRAIYMKSLRSPMMN
HHHHHHHHCCCHHHC
16.6928122231
1571PhosphorylationIYMKSLRSPMMNNKY
HHHHHCCCHHHCCCH
23.5725159151
1577UbiquitinationRSPMMNNKYKMIHKT
CCHHHCCCHHHHHHH
41.0430230243
1673PhosphorylationRIILPDDSSEEENNV
CEECCCCCCCCCCCC
47.2125159151
1674PhosphorylationIILPDDSSEEENNVN
EECCCCCCCCCCCCC
56.9010997877
1686PhosphorylationNVNDKRESNIAVNPS
CCCCCHHHCCCCCHH
37.25-
1693PhosphorylationSNIAVNPSTVKKNKQ
HCCCCCHHHHCCCCC
40.40-
1720PhosphorylationSAQSKVRSTPRVNPL
CHHHHHCCCCCCCHH
45.8320363803
1721PhosphorylationAQSKVRSTPRVNPLA
HHHHHCCCCCCCHHH
12.4420363803
1735PhosphorylationAKQSKQTSLNLKDTI
HHHCCCCCCCHHHHH
16.86-
1746PhosphorylationKDTISEVSDFKPQNH
HHHHHHHHCCCCCCC
33.0225627689
1758PhosphorylationQNHNEVQSTTPPFTT
CCCCCCCCCCCCCCC
39.1525627689
1759PhosphorylationNHNEVQSTTPPFTTV
CCCCCCCCCCCCCCC
26.6525627689
1760PhosphorylationHNEVQSTTPPFTTVD
CCCCCCCCCCCCCCC
33.9225159151
1771UbiquitinationTTVDSQKDCRKFPVP
CCCCCCCCCCCCCCC
29.8029967540
1780AcetylationRKFPVPQKDGSALED
CCCCCCCCCCCCCCC
58.9726051181
1783PhosphorylationPVPQKDGSALEDSST
CCCCCCCCCCCCCCC
39.55-
1794PhosphorylationDSSTSGASCSKSRPH
CCCCCCCCCCCCCCC
23.5825627689
1796PhosphorylationSTSGASCSKSRPHLA
CCCCCCCCCCCCCCC
31.0425627689
1797UbiquitinationTSGASCSKSRPHLAG
CCCCCCCCCCCCCCC
55.6129967540
1829O-linked_GlycosylationVGGHEITSGLEVISS
ECCEECCCCHHHHHH
47.2230379171
1835PhosphorylationTSGLEVISSLRAIHG
CCCHHHHHHHHHHHC
28.6124719451
1836PhosphorylationSGLEVISSLRAIHGL
CCHHHHHHHHHHHCC
15.6825954137
1867PhosphorylationRMVVERRSQSEMLNS
CCEEEEHHHHHHHHH
44.2630576142
1869PhosphorylationVVERRSQSEMLNSVN
EEEEHHHHHHHHHHC
26.6430576142
1874PhosphorylationSQSEMLNSVNKNKFI
HHHHHHHHHCHHHHH
24.0930576142
1890UbiquitinationQIQHLQSMFERICVI
HHHHHHHHHHHHEEE
2.33-
1916UbiquitinationSRMFRRTKSYDSLLT
HHHCHHCCCHHHHHH
45.25-
2003PhosphorylationSVKRMANSSLQEISM
HHHHHHCCCHHHHHH
23.9230622161
2004PhosphorylationVKRMANSSLQEISMY
HHHHHCCCHHHHHHH
33.6030622161
2009PhosphorylationNSSLQEISMYAQVTH
CCCHHHHHHHHHHHH
12.6530622161
2011PhosphorylationSLQEISMYAQVTHQK
CHHHHHHHHHHHHHH
6.2630622161
2015PhosphorylationISMYAQVTHQKAEEI
HHHHHHHHHHHHHHH
13.4030622161

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
1045SPhosphorylationKinaseATRQ13535
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:19270156

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FANCM_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 FANCM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FANCM_HUMANFANCMphysical
18285517
FANCA_HUMANFANCAphysical
18285517
FP100_HUMANC17orf70physical
18285517
FANCE_HUMANFANCEphysical
18285517
FANCL_HUMANFANCLphysical
18285517
FAP24_HUMANC19orf40physical
18285517
BLM_HUMANBLMphysical
20347428
FANCA_HUMANFANCAphysical
20347428
FP100_HUMANC17orf70physical
20347428
RMI1_HUMANRMI1physical
20347428
RFA1_HUMANRPA1physical
20347428
FANCG_HUMANFANCGphysical
20347428
FANCE_HUMANFANCEphysical
20347428
FANCC_HUMANFANCCphysical
20347428
FANCF_HUMANFANCFphysical
20347428
RFA2_HUMANRPA2physical
20347428
FAP24_HUMANC19orf40physical
20347428
FANCB_HUMANFANCBphysical
20347428
FANCL_HUMANFANCLphysical
20347428
FANCA_HUMANFANCAphysical
20347429
FANCM_HUMANFANCMphysical
20347429
FANCG_HUMANFANCGphysical
20347429
FAP24_HUMANC19orf40physical
20347429
CENPS_HUMANAPITD1physical
20347429
CENPX_HUMANSTRA13physical
20347429
FANCA_HUMANFANCAphysical
20064461
FANCE_HUMANFANCEphysical
20064461
FANCF_HUMANFANCFphysical
20064461
BLM_HUMANBLMphysical
20064461
RMI1_HUMANRMI1physical
20064461
RMI2_HUMANRMI2physical
20064461
TOP3A_HUMANTOP3Aphysical
20064461
FAP24_HUMANC19orf40physical
20064461
FAP24_HUMANC19orf40physical
17289582
RMI1_HUMANRMI1physical
17289582
FANCE_HUMANFANCEphysical
17289582
FANCC_HUMANFANCCphysical
17289582
FANCF_HUMANFANCFphysical
17289582
FANCA_HUMANFANCAphysical
17289582
FANCB_HUMANFANCBphysical
17289582
FANCG_HUMANFANCGphysical
17289582
FANCL_HUMANFANCLphysical
17289582
FANCA_HUMANFANCAphysical
16720839
FANCL_HUMANFANCLphysical
16720839
FP100_HUMANC17orf70physical
16116422
FANCB_HUMANFANCBphysical
16116422
FANCG_HUMANFANCGphysical
16116422
FANCC_HUMANFANCCphysical
16116422
FANCE_HUMANFANCEphysical
16116422
FANCL_HUMANFANCLphysical
16116422
FANCF_HUMANFANCFphysical
16116422
FANCA_HUMANFANCAphysical
16116422
BLM_HUMANBLMphysical
16116422
TOP3A_HUMANTOP3Aphysical
16116422
A4_HUMANAPPphysical
21832049
FANCL_HUMANFANCLphysical
24910428
CENPS_HUMANAPITD1physical
20347428
CENPX_HUMANSTRA13physical
20347428
PCNA_HUMANPCNAphysical
28514442
MOC2B_HUMANMOCS2physical
28514442
MOC2A_HUMANMOCS2physical
28514442
PAF15_HUMANKIAA0101physical
28514442
FAP24_HUMANC19orf40physical
24003026
FANCI_HUMANFANCIphysical
26625197
FANCA_HUMANFANCAphysical
26625197
FP100_HUMANC17orf70physical
26625197
FOXF1_HUMANFOXF1physical
26625197
FAP20_HUMANC1orf86physical
26625197
CENPS_HUMANAPITD1physical
26625197
CENPX_HUMANSTRA13physical
26625197
FAP24_HUMANC19orf40physical
23932590
CENPS_HUMANAPITD1physical
24699063
CENPX_HUMANSTRA13physical
24699063
FANCC_HUMANFANCCphysical
24699063
FANCE_HUMANFANCEphysical
24699063
FANCF_HUMANFANCFphysical
24699063
FAP24_HUMANC19orf40physical
24699063
BLM_HUMANBLMphysical
24699063
TOP3A_HUMANTOP3Aphysical
24699063
PCNA_HUMANPCNAphysical
26825464
RMI1_HUMANRMI1physical
22392978
RMI2_HUMANRMI2physical
22392978
CENPS_HUMANAPITD1physical
22510687
CENPX_HUMANSTRA13physical
22510687
TELO2_HUMANTELO2physical
20064461

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614087Fanconi anemia complementation group M (FANCM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FANCM_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1437, AND MASSSPECTROMETRY.

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