NF1_HUMAN - dbPTM
NF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NF1_HUMAN
UniProt AC P21359
Protein Name Neurofibromin
Gene Name NF1
Organism Homo sapiens (Human).
Sequence Length 2839
Subcellular Localization Nucleus . Nucleus, nucleolus .
Protein Description Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity..
Protein Sequence MAAHRPVEWVQAVVSRFDEQLPIKTGQQNTHTKVSTEHNKECLINISKYKFSLVISGLTTILKNVNNMRIFGEAAEKNLYLSQLIILDTLEKCLAGQPKDTMRLDETMLVKQLLPEICHFLHTCREGNQHAAELRNSASGVLFSLSCNNFNAVFSRISTRLQELTVCSEDNVDVHDIELLQYINVDCAKLKRLLKETAFKFKALKKVAQLAVINSLEKAFWNWVENYPDEFTKLYQIPQTDMAECAEKLFDLVDGFAESTKRKAAVWPLQIILLILCPEIIQDISKDVVDENNMNKKLFLDSLRKALAGHGGSRQLTESAAIACVKLCKASTYINWEDNSVIFLLVQSMVVDLKNLLFNPSKPFSRGSQPADVDLMIDCLVSCFRISPHNNQHFKICLAQNSPSTFHYVLVNSLHRIITNSALDWWPKIDAVYCHSVELRNMFGETLHKAVQGCGAHPAIRMAPSLTFKEKVTSLKFKEKPTDLETRSYKYLLLSMVKLIHADPKLLLCNPRKQGPETQGSTAELITGLVQLVPQSHMPEIAQEAMEALLVLHQLDSIDLWNPDAPVETFWEISSQMLFYICKKLTSHQMLSSTEILKWLREILICRNKFLLKNKQADRSSCHFLLFYGVGCDIPSSGNTSQMSMDHEELLRTPGASLRKGKGNSSMDSAAGCSGTPPICRQAQTKLEVALYMFLWNPDTEAVLVAMSCFRHLCEEADIRCGVDEVSVHNLLPNYNTFMEFASVSNMMSTGRAALQKRVMALLRRIEHPTAGNTEAWEDTHAKWEQATKLILNYPKAKMEDGQAAESLHKTIVKRRMSHVSGGGSIDLSDTDSLQEWINMTGFLCALGGVCLQQRSNSGLATYSPPMGPVSERKGSMISVMSSEGNADTPVSKFMDRLLSLMVCNHEKVGLQIRTNVKDLVGLELSPALYPMLFNKLKNTISKFFDSQGQVLLTDTNTQFVEQTIAIMKNLLDNHTEGSSEHLGQASIETMMLNLVRYVRVLGNMVHAIQIKTKLCQLVEVMMARRDDLSFCQEMKFRNKMVEYLTDWVMGTSNQAADDDVKCLTRDLDQASMEAVVSLLAGLPLQPEEGDGVELMEAKSQLFLKYFTLFMNLLNDCSEVEDESAQTGGRKRGMSRRLASLRHCTVLAMSNLLNANVDSGLMHSIGLGYHKDLQTRATFMEVLTKILQQGTEFDTLAETVLADRFERLVELVTMMGDQGELPIAMALANVVPCSQWDELARVLVTLFDSRHLLYQLLWNMFSKEVELADSMQTLFRGNSLASKIMTFCFKVYGATYLQKLLDPLLRIVITSSDWQHVSFEVDPTRLEPSESLEENQRNLLQMTEKFFHAIISSSSEFPPQLRSVCHCLYQATCHSLLNKATVKEKKENKKSVVSQRFPQNSIGAVGSAMFLRFINPAIVSPYEAGILDKKPPPRIERGLKLMSKILQSIANHVLFTKEEHMRPFNDFVKSNFDAARRFFLDIASDCPTSDAVNHSLSFISDGNVLALHRLLWNNQEKIGQYLSSNRDHKAVGRRPFDKMATLLAYLGPPEHKPVADTHWSSLNLTSSKFEEFMTRHQVHEKEEFKALKTLSIFYQAGTSKAGNPIFYYVARRFKTGQINGDLLIYHVLLTLKPYYAKPYEIVVDLTHTGPSNRFKTDFLSKWFVVFPGFAYDNVSAVYIYNCNSWVREYTKYHERLLTGLKGSKRLVFIDCPGKLAEHIEHEQQKLPAATLALEEDLKVFHNALKLAHKDTKVSIKVGSTAVQVTSAERTKVLGQSVFLNDIYYASEIEEICLVDENQFTLTIANQGTPLTFMHQECEAIVQSIIHIRTRWELSQPDSIPQHTKIRPKDVPGTLLNIALLNLGSSDPSLRSAAYNLLCALTCTFNLKIEGQLLETSGLCIPANNTLFIVSISKTLAANEPHLTLEFLEECISGFSKSSIELKHLCLEYMTPWLSNLVRFCKHNDDAKRQRVTAILDKLITMTINEKQMYPSIQAKIWGSLGQITDLLDVVLDSFIKTSATGGLGSIKAEVMADTAVALASGNVKLVSSKVIGRMCKIIDKTCLSPTPTLEQHLMWDDIAILARYMLMLSFNNSLDVAAHLPYLFHVVTFLVATGPLSLRASTHGLVINIIHSLCTCSQLHFSEETKQVLRLSLTEFSLPKFYLLFGISKVKSAAVIAFRSSYRDRSFSPGSYERETFALTSLETVTEALLEIMEACMRDIPTCKWLDQWTELAQRFAFQYNPSLQPRALVVFGCISKRVSHGQIKQIIRILSKALESCLKGPDTYNSQVLIEATVIALTKLQPLLNKDSPLHKALFWVAVAVLQLDEVNLYSAGTALLEQNLHTLDSLRIFNDKSPEEVFMAIRNPLEWHCKQMDHFVGLNFNSNFNFALVGHLLKGYRHPSPAIVARTVRILHTLLTLVNKHRNCDKFEVNTQSVAYLAALLTVSEEVRSRCSLKHRKSLLLTDISMENVPMDTYPIHHGDPSYRTLKETQPWSSPKGSEGYLAATYPTVGQTSPRARKSMSLDMGQPSQANTKKLLGTRKSFDHLISDTKAPKRQEMESGITTPPKMRRVAETDYEMETQRISSSQQHPHLRKVSVSESNVLLDEEVLTDPKIQALLLTVLATLVKYTTDEFDQRILYEYLAEASVVFPKVFPVVHNLLDSKINTLLSLCQDPNLLNPIHGIVQSVVYHEESPPQYQTSYLQSFGFNGLWRFAGPFSKQTQIPDYAELIVKFLDALIDTYLPGIDEETSEESLLTPTSPYPPALQSQLSITANLNLSNSMTSLATSQHSPGIDKENVELSPTTGHCNSGRTRHGSASQVQKQRSAGSFKRNSIKKIV
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
2Acetylation------MAAHRPVEW
------CCCCCCHHH
24.23-
15PhosphorylationEWVQAVVSRFDEQLP
HHHHHHHHHCHHCCC
22.1930631047
24UbiquitinationFDEQLPIKTGQQNTH
CHHCCCCCCCCCCCC
44.6729967540
40UbiquitinationKVSTEHNKECLINIS
EECCCCCCCEEEEHH
52.2729967540
52PhosphorylationNISKYKFSLVISGLT
EHHHHHHEEHHHCHH
19.9920068231
56PhosphorylationYKFSLVISGLTTILK
HHHEEHHHCHHHHHH
21.9220068231
59PhosphorylationSLVISGLTTILKNVN
EEHHHCHHHHHHHHC
18.4720068231
60PhosphorylationLVISGLTTILKNVNN
EHHHCHHHHHHHHCC
29.3820068231
107PhosphorylationDTMRLDETMLVKQLL
CCCCCCHHHHHHHHH
18.5723403867
146PhosphorylationSGVLFSLSCNNFNAV
CCEEEEEECCCHHHH
17.3822468782
155PhosphorylationNNFNAVFSRISTRLQ
CCHHHHHHHHHHHHH
23.3122468782
261UbiquitinationDGFAESTKRKAAVWP
HHHHHHHHHHHCHHH
62.2729967540
297UbiquitinationDENNMNKKLFLDSLR
CCCCCCHHHHHHHHH
39.1929967540
302PhosphorylationNKKLFLDSLRKALAG
CHHHHHHHHHHHHCC
32.0226091039
361PhosphorylationKNLLFNPSKPFSRGS
HHHCCCCCCCCCCCC
54.8129396449
362UbiquitinationNLLFNPSKPFSRGSQ
HHCCCCCCCCCCCCC
51.8723000965
449UbiquitinationMFGETLHKAVQGCGA
HHHHHHHHHHCCCCC
54.06-
465PhosphorylationPAIRMAPSLTFKEKV
HHHHCCCCCCHHHHH
30.4220860994
467PhosphorylationIRMAPSLTFKEKVTS
HHCCCCCCHHHHHHC
36.6820860994
469MethylationMAPSLTFKEKVTSLK
CCCCCCHHHHHHCCC
51.93115973915
469UbiquitinationMAPSLTFKEKVTSLK
CCCCCCHHHHHHCCC
51.9333845483
471MethylationPSLTFKEKVTSLKFK
CCCCHHHHHHCCCCC
51.9415612473
471UbiquitinationPSLTFKEKVTSLKFK
CCCCHHHHHHCCCCC
51.94-
476MethylationKEKVTSLKFKEKPTD
HHHHHCCCCCCCCCC
54.9115612485
476UbiquitinationKEKVTSLKFKEKPTD
HHHHHCCCCCCCCCC
54.9133845483
478UbiquitinationKVTSLKFKEKPTDLE
HHHCCCCCCCCCCCC
64.3429967540
480UbiquitinationTSLKFKEKPTDLETR
HCCCCCCCCCCCCHH
54.5333845483
491PhosphorylationLETRSYKYLLLSMVK
CCHHHHHHHHHHHHH
8.37-
505UbiquitinationKLIHADPKLLLCNPR
HHHHCCCCEEECCCC
52.9229967540
575 (in isoform 5)Phosphorylation-25.8525072903
577 (in isoform 5)Phosphorylation-2.7825072903
579 (in isoform 5)Phosphorylation-3.0325072903
583 (in isoform 5)Phosphorylation-41.0625072903
584 (in isoform 5)Phosphorylation-53.2225072903
593 (in isoform 5)Phosphorylation-26.54-
620PhosphorylationKNKQADRSSCHFLLF
CCCCCCHHCCEEEEE
37.5527251275
621PhosphorylationNKQADRSSCHFLLFY
CCCCCHHCCEEEEEE
16.7127251275
628PhosphorylationSCHFLLFYGVGCDIP
CCEEEEEEECCCCCC
15.7527642862
653PhosphorylationDHEELLRTPGASLRK
CHHHHHCCCCCCCCC
26.5023186163
657PhosphorylationLLRTPGASLRKGKGN
HHCCCCCCCCCCCCC
34.3227422710
660UbiquitinationTPGASLRKGKGNSSM
CCCCCCCCCCCCCCC
70.9822817900
662UbiquitinationGASLRKGKGNSSMDS
CCCCCCCCCCCCCHH
58.9321963094
665PhosphorylationLRKGKGNSSMDSAAG
CCCCCCCCCCHHCCC
35.3926471730
666PhosphorylationRKGKGNSSMDSAAGC
CCCCCCCCCHHCCCC
30.5226471730
669PhosphorylationKGNSSMDSAAGCSGT
CCCCCCHHCCCCCCC
16.0426471730
669UbiquitinationKGNSSMDSAAGCSGT
CCCCCCHHCCCCCCC
16.0422817900
670UbiquitinationGNSSMDSAAGCSGTP
CCCCCHHCCCCCCCC
12.0122817900
671UbiquitinationNSSMDSAAGCSGTPP
CCCCHHCCCCCCCCH
24.3921963094
672UbiquitinationSSMDSAAGCSGTPPI
CCCHHCCCCCCCCHH
13.0721963094
674PhosphorylationMDSAAGCSGTPPICR
CHHCCCCCCCCHHHH
44.79-
676PhosphorylationSAAGCSGTPPICRQA
HCCCCCCCCHHHHHH
15.03-
783UbiquitinationAWEDTHAKWEQATKL
HHHHHHHHHHHHHHH
43.5929967540
796UbiquitinationKLILNYPKAKMEDGQ
HHHHHCCHHHCCCCH
50.7229967540
798UbiquitinationILNYPKAKMEDGQAA
HHHCCHHHCCCCHHH
49.28-
807PhosphorylationEDGQAAESLHKTIVK
CCCHHHHHHHHHHHH
30.9229255136
810UbiquitinationQAAESLHKTIVKRRM
HHHHHHHHHHHHHHH
45.2833845483
811O-linked_GlycosylationAAESLHKTIVKRRMS
HHHHHHHHHHHHHHC
21.9131492838
856PhosphorylationGVCLQQRSNSGLATY
CEEEECCCCCCCCCC
30.8921945579
858PhosphorylationCLQQRSNSGLATYSP
EEECCCCCCCCCCCC
36.1121945579
862PhosphorylationRSNSGLATYSPPMGP
CCCCCCCCCCCCCCC
29.5821945579
863PhosphorylationSNSGLATYSPPMGPV
CCCCCCCCCCCCCCC
17.3621945579
864PhosphorylationNSGLATYSPPMGPVS
CCCCCCCCCCCCCCC
20.4119664994
871PhosphorylationSPPMGPVSERKGSMI
CCCCCCCCCCCCCEE
34.5121945579
874UbiquitinationMGPVSERKGSMISVM
CCCCCCCCCCEEEEE
51.81-
876PhosphorylationPVSERKGSMISVMSS
CCCCCCCCEEEEECC
18.9123401153
879PhosphorylationERKGSMISVMSSEGN
CCCCCEEEEECCCCC
11.7929255136
882PhosphorylationGSMISVMSSEGNADT
CCEEEEECCCCCCCC
24.0729255136
883PhosphorylationSMISVMSSEGNADTP
CEEEEECCCCCCCCH
31.2829255136
889PhosphorylationSSEGNADTPVSKFMD
CCCCCCCCHHHHHHH
24.1525850435
892PhosphorylationGNADTPVSKFMDRLL
CCCCCHHHHHHHHHH
22.7523186163
915PhosphorylationKVGLQIRTNVKDLVG
CCCEEEECCHHHHCC
46.09-
926PhosphorylationDLVGLELSPALYPML
HHCCCCCCHHHHHHH
9.96-
930PhosphorylationLELSPALYPMLFNKL
CCCCHHHHHHHHHHH
6.68-
1036UbiquitinationLSFCQEMKFRNKMVE
CHHHHHHHHHHHHHH
40.18-
1052PhosphorylationLTDWVMGTSNQAADD
HHHHHHCCCCCCCCC
13.3528985074
1053PhosphorylationTDWVMGTSNQAADDD
HHHHHCCCCCCCCCC
22.6328985074
1140PhosphorylationGMSRRLASLRHCTVL
HHHHHHHHHHHHHHH
30.4425394399
1204MethylationAETVLADRFERLVEL
HHHHHHHHHHHHHHH
29.7118567601
1283AcetylationRGNSLASKIMTFCFK
CCCHHHHHHHHHHHH
30.7819821473
1375PhosphorylationLYQATCHSLLNKATV
HHHHHHHHHHHHHCH
36.3824719451
1440MalonylationPRIERGLKLMSKILQ
CHHHHHHHHHHHHHH
44.9932601280
1456PhosphorylationIANHVLFTKEEHMRP
HHHCCCCCCHHHCCC
33.1318452278
1496UbiquitinationSDAVNHSLSFISDGN
HHHCCCCEEECCCCC
3.6421890473
1496 (in isoform 2)Ubiquitination-3.6421890473
1506UbiquitinationISDGNVLALHRLLWN
CCCCCHHEEHHHHHC
9.3121890473
1517UbiquitinationLLWNNQEKIGQYLSS
HHHCCHHHHHHHHHC
42.2322817900
1517 (in isoform 1)Ubiquitination-42.2321890473
1517 (in isoform 4)Ubiquitination-42.2321890473
1521PhosphorylationNQEKIGQYLSSNRDH
CHHHHHHHHHCCCCC
11.8825147952
1523PhosphorylationEKIGQYLSSNRDHKA
HHHHHHHHCCCCCCC
22.1924961811
1526UbiquitinationGQYLSSNRDHKAVGR
HHHHHCCCCCCCCCC
49.7321890473
1527UbiquitinationQYLSSNRDHKAVGRR
HHHHCCCCCCCCCCC
52.4621890473
1560AcetylationPVADTHWSSLNLTSS
CCCCCCHHHCCCCHH
19.8319608861
1567PhosphorylationSSLNLTSSKFEEFMT
HHCCCCHHHHHHHHH
35.81-
1581AcetylationTRHQVHEKEEFKALK
HHCCCCCHHHHHHHH
47.9019608861
1589PhosphorylationEEFKALKTLSIFYQA
HHHHHHHHHHHHHHC
26.9628258704
1680UbiquitinationNVSAVYIYNCNSWVR
CEEEEEEEECCHHHH
8.9329967540
1701UbiquitinationERLLTGLKGSKRLVF
HHHHHCCCCCCEEEE
63.5829967540
1724UbiquitinationEHIEHEQQKLPAATL
HHHHHHHHHCCHHHH
46.3929967540
1730PhosphorylationQQKLPAATLALEEDL
HHHCCHHHHHHHHHH
18.0529396449
1745UbiquitinationKVFHNALKLAHKDTK
HHHHHHHHHHCCCCC
41.0129967540
1751PhosphorylationLKLAHKDTKVSIKVG
HHHHCCCCCEEEEEC
37.84-
1834PhosphorylationIRTRWELSQPDSIPQ
HHHCHHHCCCCCCCC
28.3127461979
1838PhosphorylationWELSQPDSIPQHTKI
HHHCCCCCCCCCCCC
42.7427461979
2013PhosphorylationLLDVVLDSFIKTSAT
HHHHHHHHHHHCCCC
25.3924719451
2028UbiquitinationGGLGSIKAEVMADTA
CCCCCHHHHHHHHHH
16.9729967540
2040PhosphorylationDTAVALASGNVKLVS
HHHHHHHCCCEEEEC
31.5825599653
2049UbiquitinationNVKLVSSKVIGRMCK
CEEEECHHHHHHHHH
30.3029967540
2157PhosphorylationRLSLTEFSLPKFYLL
HHHCHHCCCCHHHHH
37.2124719451
2180PhosphorylationAAVIAFRSSYRDRSF
EEEEEECCCCCCCCC
25.8523312004
2181PhosphorylationAVIAFRSSYRDRSFS
EEEEECCCCCCCCCC
21.6723312004
2182PhosphorylationVIAFRSSYRDRSFSP
EEEECCCCCCCCCCC
20.1323312004
2186PhosphorylationRSSYRDRSFSPGSYE
CCCCCCCCCCCCCHH
34.0719691289
2188PhosphorylationSYRDRSFSPGSYERE
CCCCCCCCCCCHHHC
29.6025159151
2191PhosphorylationDRSFSPGSYERETFA
CCCCCCCCHHHCCEE
27.4919691289
2192PhosphorylationRSFSPGSYERETFAL
CCCCCCCHHHCCEEE
25.5619691289
2196PhosphorylationPGSYERETFALTSLE
CCCHHHCCEEECCHH
22.0424043423
2200PhosphorylationERETFALTSLETVTE
HHCCEEECCHHHHHH
28.0324043423
2201PhosphorylationRETFALTSLETVTEA
HCCEEECCHHHHHHH
25.6724043423
2204PhosphorylationFALTSLETVTEALLE
EEECCHHHHHHHHHH
37.7124043423
2206PhosphorylationLTSLETVTEALLEIM
ECCHHHHHHHHHHHH
23.9824043423
2299PhosphorylationEATVIALTKLQPLLN
HHHHHHHHHHHHHHC
22.2322210691
2444PhosphorylationAYLAALLTVSEEVRS
HHHHHHHHCCHHHHH
23.88-
2446PhosphorylationLAALLTVSEEVRSRC
HHHHHHCCHHHHHHC
23.86-
2451PhosphorylationTVSEEVRSRCSLKHR
HCCHHHHHHCCHHCC
42.70-
2460PhosphorylationCSLKHRKSLLLTDIS
CCHHCCCHHEEEECC
24.9822617229
2464PhosphorylationHRKSLLLTDISMENV
CCCHHEEEECCCCCC
31.1227732954
2467PhosphorylationSLLLTDISMENVPMD
HHEEEECCCCCCCCC
23.89-
2468UbiquitinationLLLTDISMENVPMDT
HEEEECCCCCCCCCC
4.4229967540
2476PhosphorylationENVPMDTYPIHHGDP
CCCCCCCCCCCCCCC
8.9122817900
2484PhosphorylationPIHHGDPSYRTLKET
CCCCCCCHHCCCCCC
31.8027642862
2485PhosphorylationIHHGDPSYRTLKETQ
CCCCCCHHCCCCCCC
17.0127642862
2487PhosphorylationHGDPSYRTLKETQPW
CCCCHHCCCCCCCCC
33.6727174698
2489MethylationDPSYRTLKETQPWSS
CCHHCCCCCCCCCCC
59.09115973907
2489UbiquitinationDPSYRTLKETQPWSS
CCHHCCCCCCCCCCC
59.0929967540
2491PhosphorylationSYRTLKETQPWSSPK
HHCCCCCCCCCCCCC
38.0428450419
2494PhosphorylationTLKETQPWSSPKGSE
CCCCCCCCCCCCCCC
11.1332142685
2495PhosphorylationLKETQPWSSPKGSEG
CCCCCCCCCCCCCCC
43.3730266825
2496PhosphorylationKETQPWSSPKGSEGY
CCCCCCCCCCCCCCE
27.1130266825
2500PhosphorylationPWSSPKGSEGYLAAT
CCCCCCCCCCEEEEE
33.6921945579
2503PhosphorylationSPKGSEGYLAATYPT
CCCCCCCEEEEECCC
6.7921945579
2507PhosphorylationSEGYLAATYPTVGQT
CCCEEEEECCCCCCC
25.1521945579
2508PhosphorylationEGYLAATYPTVGQTS
CCEEEEECCCCCCCC
7.6821945579
2510PhosphorylationYLAATYPTVGQTSPR
EEEEECCCCCCCCCC
27.1921945579
2514PhosphorylationTYPTVGQTSPRARKS
ECCCCCCCCCCCHHH
34.4722167270
2515PhosphorylationYPTVGQTSPRARKSM
CCCCCCCCCCCHHHC
12.4222167270
2521PhosphorylationTSPRARKSMSLDMGQ
CCCCCHHHCCCCCCC
14.1929255136
2522PhosphorylationSPRARKSMSLDMGQP
CCCCHHHCCCCCCCC
5.3132142685
2523PhosphorylationPRARKSMSLDMGQPS
CCCHHHCCCCCCCCC
28.4529255136
2530PhosphorylationSLDMGQPSQANTKKL
CCCCCCCCCCCHHHH
33.7523927012
2540PhosphorylationNTKKLLGTRKSFDHL
CHHHHHCCHHHHHHH
34.5929214152
2543PhosphorylationKLLGTRKSFDHLISD
HHHCCHHHHHHHHCC
32.3929255136
2544PhosphorylationLLGTRKSFDHLISDT
HHCCHHHHHHHHCCC
8.4432645325
2549PhosphorylationKSFDHLISDTKAPKR
HHHHHHHCCCCCCCH
45.6623927012
2551PhosphorylationFDHLISDTKAPKRQE
HHHHHCCCCCCCHHH
23.4723312004
2561PhosphorylationPKRQEMESGITTPPK
CCHHHHHCCCCCCHH
33.9028176443
2564PhosphorylationQEMESGITTPPKMRR
HHHHCCCCCCHHHHH
36.4530266825
2565PhosphorylationEMESGITTPPKMRRV
HHHCCCCCCHHHHHH
35.3623401153
2574UbiquitinationPKMRRVAETDYEMET
HHHHHHHCCCHHHHH
39.0829967540
2575PhosphorylationKMRRVAETDYEMETQ
HHHHHHCCCHHHHHH
33.8621945579
2577PhosphorylationRRVAETDYEMETQRI
HHHHCCCHHHHHHHC
25.2921945579
2580PhosphorylationAETDYEMETQRISSS
HCCCHHHHHHHCCCC
29.8332142685
2581PhosphorylationETDYEMETQRISSSQ
CCCHHHHHHHCCCCC
23.1030576142
2585PhosphorylationEMETQRISSSQQHPH
HHHHHHCCCCCCCCC
26.5628555341
2586PhosphorylationMETQRISSSQQHPHL
HHHHHCCCCCCCCCC
29.7825627689
2587PhosphorylationETQRISSSQQHPHLR
HHHHCCCCCCCCCCE
27.3725159151
2595UbiquitinationQQHPHLRKVSVSESN
CCCCCCEECCCCCCC
45.2629967540
2597PhosphorylationHPHLRKVSVSESNVL
CCCCEECCCCCCCCC
23.9830266825
2599PhosphorylationHLRKVSVSESNVLLD
CCEECCCCCCCCCCC
28.0030266825
2601PhosphorylationRKVSVSESNVLLDEE
EECCCCCCCCCCCHH
25.4029255136
2611PhosphorylationLLDEEVLTDPKIQAL
CCCHHHCCCHHHHHH
56.2723927012
2781PhosphorylationANLNLSNSMTSLATS
EECCCCCCHHHHHHC
21.7720068231
2799 (in isoform 6)Phosphorylation-9.0925849741
2802PhosphorylationDKENVELSPTTGHCN
CHHCEEECCCCCCCC
13.4929255136
2804PhosphorylationENVELSPTTGHCNSG
HCEEECCCCCCCCCC
41.8729255136
2805PhosphorylationNVELSPTTGHCNSGR
CEEECCCCCCCCCCC
28.4521815630
2810PhosphorylationPTTGHCNSGRTRHGS
CCCCCCCCCCCCCCC
34.7425159151
2813PhosphorylationGHCNSGRTRHGSASQ
CCCCCCCCCCCCHHH
30.4629514088
2817PhosphorylationSGRTRHGSASQVQKQ
CCCCCCCCHHHHHHH
20.7228176443
2819PhosphorylationRTRHGSASQVQKQRS
CCCCCCHHHHHHHHH
32.3630576142
2826PhosphorylationSQVQKQRSAGSFKRN
HHHHHHHHCCCCCHH
34.1933259812
2829PhosphorylationQKQRSAGSFKRNSIK
HHHHHCCCCCHHHCH
27.5828102081
2834PhosphorylationAGSFKRNSIKKIV--
CCCCCHHHCHHCC--
39.5626074081

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
2808SPhosphorylationKinasePRKCAP17252
GPS
-KUbiquitinationE3 ubiquitin ligaseFAF2Q96CS3
PMID:20160012
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseSAGP10523
PMID:23136067

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NF1_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 NF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB1_HUMANPOLR2Aphysical
15999204
SMCA4_HUMANSMARCA4physical
15999204
TERA_HUMANVCPphysical
22105171
NSF1C_HUMANNSFL1Cphysical
22105171
FAF2_HUMANFAF2physical
20160012
NOSIP_HUMANNOSIPphysical
26344197
A4_HUMANAPPphysical
16374483
1433F_HUMANYWHAHphysical
14741381
PML_HUMANPMLphysical
22293200
PTEN_HUMANPTENgenetic
28319113
SDC2_HUMANSDC2physical
11356864
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
CING_HUMANCGNphysical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
RGPS2_HUMANRALGPS2physical
27173435
MAGI1_HUMANMAGI1physical
27173435
CBY1_HUMANCBY1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
GGYF2_HUMANGIGYF2physical
27173435
HDAC4_HUMANHDAC4physical
27173435
NADK_HUMANNADKphysical
27173435
SRS12_HUMANSRSF12physical
27173435
NGAP_HUMANRASAL2physical
27173435
SYDE1_HUMANSYDE1physical
27173435
AGAP1_HUMANAGAP1physical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
F110B_HUMANFAM110Bphysical
27173435
UBP21_HUMANUSP21physical
27173435
NAV1_HUMANNAV1physical
27173435
STA13_HUMANSTARD13physical
27173435
RASN_HUMANNRASphysical
7499408

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
162200Neurofibromatosis 1 (NF1)
607785Leukemia, juvenile myelomonocytic (JMML)
193520Watson syndrome (WS)
162210Familial spinal neurofibromatosis (FSNF)
601321Neurofibromatosis-Noonan syndrome (NFNS)
114500Colorectal cancer (CRC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NF1_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-1581, AND MASS SPECTROMETRY.
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-864; SER-876 ANDSER-2515, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2515; SER-2543 ANDSER-2597, 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-864 AND SER-2523, 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 SER-864; SER-2188; SER-2515;SER-2521 AND SER-2543, AND MASS SPECTROMETRY.
"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-2188; SER-2496 ANDSER-2543, 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-2515, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2188, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2829, AND MASSSPECTROMETRY.
"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-864 AND SER-2515, ANDMASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2577, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2476, AND MASSSPECTROMETRY.

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