NU107_HUMAN - dbPTM
NU107_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NU107_HUMAN
UniProt AC P57740
Protein Name Nuclear pore complex protein Nup107
Gene Name NUP107
Organism Homo sapiens (Human).
Sequence Length 925
Subcellular Localization Nucleus membrane . Nucleus, nuclear pore complex . Chromosome, centromere, kinetochore . Located on both the cytoplasmic and nuclear sides of the NPC core structure (PubMed:11564755). During mitosis, localizes to the kinetochores (PubMed:11564755). D
Protein Description Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. [PubMed: 12552102]
Protein Sequence MDRSGFGEISSPVIREAEVTRTARKQSAQKRVLLQASQDENFGNTTPRNQVIPRTPSSFRQPFTPTSRSLLRQPDISCILGTGGKSPRLTQSSGFFGNLSMVTNLDDSNWAAAFSSQRSGLFTNTEPHSITEDVTISAVMLREDDPGEAASMSMFSDFLQSFLKHSSSTVFDLVEEYENICGSQVNILSKIVSRATPGLQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSALEEESVFAVTAVNASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGEFSDNIEFYAKSVYWENTLHTLKQRQLTSYVGSVRPLVTELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLYHDPNVNGGTELEPVEGNPYRRIWKISCWRMAEDELFNRYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIQTSVATLDETEELPREYLGANWTLEKVFEELQATDKKRVLEENQEHYHIVQKFLILGDIDGLMDEFSKWLSKSRNNLPGHLLRFMTHLILFFRTLGLQTKEEVSIEVLKTYIQLLIREKHTNLIAFYTCHLPQDLAVAQYALFLESVTEFEQRHHCLELAKEADLDVATITKTVVENIRKKDNGEFSHHDLAPALDTGTTEEDRLKIDVIDWLVFDPAQRAEALKQGNAIMRKFLASKKHEAAKEVFVKIPQDSIAEIYNQCEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNEWFKHMNSVPQKPALIPQPTFTEKVAHEHKEKKYEMDFGIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAKEDHERTHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADMVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQL
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
1Acetylation-------MDRSGFGE
-------CCCCCCCC
9.7320068231
4Phosphorylation----MDRSGFGEISS
----CCCCCCCCCCC
33.9230266825
10PhosphorylationRSGFGEISSPVIREA
CCCCCCCCCHHHHHH
25.0429255136
11PhosphorylationSGFGEISSPVIREAE
CCCCCCCCHHHHHHH
28.9319664994
20PhosphorylationVIREAEVTRTARKQS
HHHHHHHHHHHHHHH
17.5121949786
22PhosphorylationREAEVTRTARKQSAQ
HHHHHHHHHHHHHHH
22.8123879269
25MethylationEVTRTARKQSAQKRV
HHHHHHHHHHHHHHH
46.25116252445
37PhosphorylationKRVLLQASQDENFGN
HHHHHHHHCCCCCCC
25.7929255136
45PhosphorylationQDENFGNTTPRNQVI
CCCCCCCCCCCCCCC
38.2623401153
46PhosphorylationDENFGNTTPRNQVIP
CCCCCCCCCCCCCCC
25.0129255136
50UbiquitinationGNTTPRNQVIPRTPS
CCCCCCCCCCCCCCC
35.4821890473
55PhosphorylationRNQVIPRTPSSFRQP
CCCCCCCCCCCCCCC
23.3627273156
56UbiquitinationNQVIPRTPSSFRQPF
CCCCCCCCCCCCCCC
29.2932015554
56UbiquitinationNQVIPRTPSSFRQPF
CCCCCCCCCCCCCCC
29.29-
57PhosphorylationQVIPRTPSSFRQPFT
CCCCCCCCCCCCCCC
41.3123401153
58PhosphorylationVIPRTPSSFRQPFTP
CCCCCCCCCCCCCCC
26.1723401153
60Asymmetric dimethylargininePRTPSSFRQPFTPTS
CCCCCCCCCCCCCCH
45.25-
60MethylationPRTPSSFRQPFTPTS
CCCCCCCCCCCCCCH
45.2524129315
64PhosphorylationSSFRQPFTPTSRSLL
CCCCCCCCCCHHHHH
32.1327273156
64O-linked_GlycosylationSSFRQPFTPTSRSLL
CCCCCCCCCCHHHHH
32.1330059200
66PhosphorylationFRQPFTPTSRSLLRQ
CCCCCCCCHHHHHCC
33.4430266825
67PhosphorylationRQPFTPTSRSLLRQP
CCCCCCCHHHHHCCC
22.5221712546
67O-linked_GlycosylationRQPFTPTSRSLLRQP
CCCCCCCHHHHHCCC
22.5230059200
68MethylationQPFTPTSRSLLRQPD
CCCCCCHHHHHCCCC
33.5358858727
69PhosphorylationPFTPTSRSLLRQPDI
CCCCCHHHHHCCCCE
31.3623927012
77PhosphorylationLLRQPDISCILGTGG
HHCCCCEEEEECCCC
11.5023401153
82PhosphorylationDISCILGTGGKSPRL
CEEEEECCCCCCCCC
39.0429255136
85UbiquitinationCILGTGGKSPRLTQS
EEECCCCCCCCCCCC
59.6433845483
85AcetylationCILGTGGKSPRLTQS
EEECCCCCCCCCCCC
59.6425953088
86PhosphorylationILGTGGKSPRLTQSS
EECCCCCCCCCCCCC
20.6629255136
103PhosphorylationFGNLSMVTNLDDSNW
CCCEEEEECCCCCCH
22.7927732954
108PhosphorylationMVTNLDDSNWAAAFS
EEECCCCCCHHHHHH
33.6627732954
115PhosphorylationSNWAAAFSSQRSGLF
CCHHHHHHHCCCCCC
22.3426074081
116PhosphorylationNWAAAFSSQRSGLFT
CHHHHHHHCCCCCCC
24.1426074081
119PhosphorylationAAFSSQRSGLFTNTE
HHHHHCCCCCCCCCC
32.0126074081
123PhosphorylationSQRSGLFTNTEPHSI
HCCCCCCCCCCCCCC
46.3926074081
125PhosphorylationRSGLFTNTEPHSITE
CCCCCCCCCCCCCCC
48.0826074081
129PhosphorylationFTNTEPHSITEDVTI
CCCCCCCCCCCCCEE
41.7526074081
131PhosphorylationNTEPHSITEDVTISA
CCCCCCCCCCCEEEE
29.1926074081
135PhosphorylationHSITEDVTISAVMLR
CCCCCCCEEEEEEEC
22.8727732954
137PhosphorylationITEDVTISAVMLRED
CCCCCEEEEEEECCC
12.8727732954
153PhosphorylationPGEAASMSMFSDFLQ
CCHHHHHHHHHHHHH
17.7420068231
156PhosphorylationAASMSMFSDFLQSFL
HHHHHHHHHHHHHHH
20.8620068231
161PhosphorylationMFSDFLQSFLKHSSS
HHHHHHHHHHHCCCC
34.3924719451
172UbiquitinationHSSSTVFDLVEEYEN
CCCCCHHHHHHHHHH
45.5327667366
172UbiquitinationHSSSTVFDLVEEYEN
CCCCCHHHHHHHHHH
45.53-
175UbiquitinationSTVFDLVEEYENICG
CCHHHHHHHHHHHCH
63.2622817900
193PhosphorylationNILSKIVSRATPGLQ
HHHHHHHHHCCCCHH
21.4829514088
196PhosphorylationSKIVSRATPGLQKFS
HHHHHHCCCCHHHHH
19.4429514088
201UbiquitinationRATPGLQKFSKTASM
HCCCCHHHHHHHHHH
57.5621906983
201UbiquitinationRATPGLQKFSKTASM
HCCCCHHHHHHHHHH
57.5621890473
204UbiquitinationPGLQKFSKTASMLWL
CCHHHHHHHHHHHHH
51.7722817900
232PhosphorylationLYRDRIQSALEEESV
HHHHHHHHHHHHCCC
32.23-
251PhosphorylationAVNASEKTVVEALFQ
ECCCCHHHHHHHHHC
26.2328555341
261PhosphorylationEALFQRDSLVRQSQL
HHHHCCCHHHHHHHH
30.8420860994
276UbiquitinationVVDWLESIAKDEIGE
HHHHHHHHHCCHHCC
3.9421963094
276UbiquitinationVVDWLESIAKDEIGE
HHHHHHHHHCCHHCC
3.94-
296PhosphorylationEFYAKSVYWENTLHT
HHHEEEHHHHCHHHH
17.6928796482
303UbiquitinationYWENTLHTLKQRQLT
HHHCHHHHHHHHHHH
38.4729967540
303UbiquitinationYWENTLHTLKQRQLT
HHHCHHHHHHHHHHH
38.47-
305MethylationENTLHTLKQRQLTSY
HCHHHHHHHHHHHHH
44.5942360801
305UbiquitinationENTLHTLKQRQLTSY
HCHHHHHHHHHHHHH
44.5921906983
3052-HydroxyisobutyrylationENTLHTLKQRQLTSY
HCHHHHHHHHHHHHH
44.59-
315PhosphorylationQLTSYVGSVRPLVTE
HHHHHHCCCCHHEEC
12.62-
321PhosphorylationGSVRPLVTELDPDAP
CCCCHHEECCCCCCC
38.21-
332UbiquitinationPDAPIRQKMPLDDLD
CCCCCCCCCCHHHCC
32.4121906983
333SulfoxidationDAPIRQKMPLDDLDR
CCCCCCCCCHHHCCH
2.7721406390
348UbiquitinationEDEVRLLKYLFTLIR
HHHHHHHHHHHHHHH
44.49-
349PhosphorylationDEVRLLKYLFTLIRA
HHHHHHHHHHHHHHC
13.6628188228
352PhosphorylationRLLKYLFTLIRAGMT
HHHHHHHHHHHCCCC
20.7628188228
353UbiquitinationLLKYLFTLIRAGMTE
HHHHHHHHHHCCCCH
1.6321963094
353UbiquitinationLLKYLFTLIRAGMTE
HHHHHHHHHHCCCCH
1.63-
359PhosphorylationTLIRAGMTEEAQRLC
HHHHCCCCHHHHHHH
29.7428188228
379UbiquitinationAWRAATLEGWKLYHD
HHHHHCCCCCCCCCC
59.6722505724
379UbiquitinationAWRAATLEGWKLYHD
HHHHHCCCCCCCCCC
59.67-
382UbiquitinationAATLEGWKLYHDPNV
HHCCCCCCCCCCCCC
50.4521906983
408UbiquitinationNPYRRIWKISCWRMA
CCCCEEEEEEEHHHH
23.5222505724
408AcetylationNPYRRIWKISCWRMA
CCCCEEEEEEEHHHH
23.5226051181
428PhosphorylationNRYERAIYAALSGNL
HHHHHHHHHHHCCCH
5.7128152594
432PhosphorylationRAIYAALSGNLKQLL
HHHHHHHCCCHHHHH
22.4028152594
462UbiquitinationVMVDSLVEQEIQTSV
HHHHHHHHHHHHHCC
48.0329967540
462UbiquitinationVMVDSLVEQEIQTSV
HHHHHHHHHHHHHCC
48.03-
472UbiquitinationIQTSVATLDETEELP
HHHCCCCCCCCCCCC
3.9522817900
472UbiquitinationIQTSVATLDETEELP
HHHCCCCCCCCCCCC
3.95-
473UbiquitinationQTSVATLDETEELPR
HHCCCCCCCCCCCCH
57.3122817900
473UbiquitinationQTSVATLDETEELPR
HHCCCCCCCCCCCCH
57.31-
475PhosphorylationSVATLDETEELPREY
CCCCCCCCCCCCHHH
34.1320860994
481UbiquitinationETEELPREYLGANWT
CCCCCCHHHHCCCCH
43.0722817900
482UbiquitinationTEELPREYLGANWTL
CCCCCHHHHCCCCHH
16.2422817900
482PhosphorylationTEELPREYLGANWTL
CCCCCHHHHCCCCHH
16.2421406692
488PhosphorylationEYLGANWTLEKVFEE
HHHCCCCHHHHHHHH
25.5021406692
491UbiquitinationGANWTLEKVFEELQA
CCCCHHHHHHHHHHC
56.1729967540
501UbiquitinationEELQATDKKRVLEEN
HHHHCCCHHHHHHHH
37.8221906983
502UbiquitinationELQATDKKRVLEENQ
HHHCCCHHHHHHHHH
51.0222817900
512PhosphorylationLEENQEHYHIVQKFL
HHHHHHHHHHHHHHH
7.78-
534UbiquitinationLMDEFSKWLSKSRNN
HHHHHHHHHHHHCCC
12.5021890473
569PhosphorylationLQTKEEVSIEVLKTY
CCCCCCHHHHHHHHH
19.1320068231
597UbiquitinationAFYTCHLPQDLAVAQ
EEEEECCCHHHHHHH
11.2821963094
597UbiquitinationAFYTCHLPQDLAVAQ
EEEEECCCHHHHHHH
11.28-
606UbiquitinationDLAVAQYALFLESVT
HHHHHHHHHHHHHHC
4.6321963094
608UbiquitinationAVAQYALFLESVTEF
HHHHHHHHHHHHCHH
5.6021963094
608UbiquitinationAVAQYALFLESVTEF
HHHHHHHHHHHHCHH
5.60-
616UbiquitinationLESVTEFEQRHHCLE
HHHHCHHHHHHHHHH
40.24-
617UbiquitinationESVTEFEQRHHCLEL
HHHCHHHHHHHHHHH
56.1621963094
626UbiquitinationHHCLELAKEADLDVA
HHHHHHHHHCCCCHH
67.0921963094
637UbiquitinationLDVATITKTVVENIR
CCHHEEEHHHHHHHH
35.1621906983
642UbiquitinationITKTVVENIRKKDNG
EEHHHHHHHHHHCCC
27.9633845483
645UbiquitinationTVVENIRKKDNGEFS
HHHHHHHHHCCCCCC
61.76-
646UbiquitinationVVENIRKKDNGEFSH
HHHHHHHHCCCCCCC
46.7229967540
652PhosphorylationKKDNGEFSHHDLAPA
HHCCCCCCCCCCCCC
18.6623898821
655UbiquitinationNGEFSHHDLAPALDT
CCCCCCCCCCCCCCC
38.8221890473
661UbiquitinationHDLAPALDTGTTEED
CCCCCCCCCCCCHHH
45.2427667366
661UbiquitinationHDLAPALDTGTTEED
CCCCCCCCCCCCHHH
45.24-
670UbiquitinationGTTEEDRLKIDVIDW
CCCHHHHHCEEEEEE
9.8527667366
671UbiquitinationTTEEDRLKIDVIDWL
CCHHHHHCEEEEEEE
37.4433845483
674UbiquitinationEDRLKIDVIDWLVFD
HHHHCEEEEEEEECC
4.9527667366
675UbiquitinationDRLKIDVIDWLVFDP
HHHCEEEEEEEECCH
2.5222817900
680UbiquitinationDVIDWLVFDPAQRAE
EEEEEEECCHHHHHH
9.7322817900
680UbiquitinationDVIDWLVFDPAQRAE
EEEEEEECCHHHHHH
9.73-
683UbiquitinationDWLVFDPAQRAEALK
EEEECCHHHHHHHHH
17.2127667366
684UbiquitinationWLVFDPAQRAEALKQ
EEECCHHHHHHHHHH
50.9722817900
685UbiquitinationLVFDPAQRAEALKQG
EECCHHHHHHHHHHC
36.1821963094
685UbiquitinationLVFDPAQRAEALKQG
EECCHHHHHHHHHHC
36.18-
689UbiquitinationPAQRAEALKQGNAIM
HHHHHHHHHHCHHHH
2.9922817900
690UbiquitinationAQRAEALKQGNAIMR
HHHHHHHHHCHHHHH
64.3121906983
694UbiquitinationEALKQGNAIMRKFLA
HHHHHCHHHHHHHHH
12.0921963094
702PhosphorylationIMRKFLASKKHEAAK
HHHHHHHHCCHHHHH
44.3722964224
703UbiquitinationMRKFLASKKHEAAKE
HHHHHHHCCHHHHHH
53.1727667366
704UbiquitinationRKFLASKKHEAAKEV
HHHHHHCCHHHHHHH
44.1522817900
709AcetylationSKKHEAAKEVFVKIP
HCCHHHHHHHEEECC
62.5524889073
709UbiquitinationSKKHEAAKEVFVKIP
HCCHHHHHHHEEECC
62.5521906983
714AcetylationAAKEVFVKIPQDSIA
HHHHHEEECCHHHHH
36.8924889081
714UbiquitinationAAKEVFVKIPQDSIA
HHHHHEEECCHHHHH
36.8921963094
724PhosphorylationQDSIAEIYNQCEEQG
HHHHHHHHHHHHHCC
7.2326714015
734PhosphorylationCEEQGMESPLPAEDD
HHHCCCCCCCCCCCC
23.8926714015
744UbiquitinationPAEDDNAIREHLCIR
CCCCCHHHHHHHHHH
7.1433845483
744UbiquitinationPAEDDNAIREHLCIR
CCCCCHHHHHHHHHH
7.14-
753UbiquitinationEHLCIRAYLEAHETF
HHHHHHHHHHHHHHH
8.6721890473
756UbiquitinationCIRAYLEAHETFNEW
HHHHHHHHHHHHHHH
11.8333845483
756UbiquitinationCIRAYLEAHETFNEW
HHHHHHHHHHHHHHH
11.83-
773UbiquitinationHMNSVPQKPALIPQP
HHCCCCCCCCCCCCC
26.6222817900
773UbiquitinationHMNSVPQKPALIPQP
HHCCCCCCCCCCCCC
26.6221890473
774UbiquitinationMNSVPQKPALIPQPT
HCCCCCCCCCCCCCC
27.3529967540
781PhosphorylationPALIPQPTFTEKVAH
CCCCCCCCCCHHHHH
37.6328555341
785UbiquitinationPQPTFTEKVAHEHKE
CCCCCCHHHHHHHHH
41.4821963094
785UbiquitinationPQPTFTEKVAHEHKE
CCCCCCHHHHHHHHH
41.48-
787UbiquitinationPTFTEKVAHEHKEKK
CCCCHHHHHHHHHHC
17.2622817900
794UbiquitinationAHEHKEKKYEMDFGI
HHHHHHHCEEECCCC
47.7521963094
796UbiquitinationEHKEKKYEMDFGIWK
HHHHHCEEECCCCHH
40.9522817900
803UbiquitinationEMDFGIWKGHLDALT
EECCCCHHHHHHHHC
34.2329967540
808UbiquitinationIWKGHLDALTADVKE
CHHHHHHHHCHHHHH
17.1133845483
814UbiquitinationDALTADVKEKMYNVL
HHHCHHHHHHHCCEE
52.7621963094
8142-HydroxyisobutyrylationDALTADVKEKMYNVL
HHHCHHHHHHHCCEE
52.76-
816UbiquitinationLTADVKEKMYNVLLF
HCHHHHHHHCCEEEE
40.7522817900
837UbiquitinationVDVREDAKEDHERTH
EECCHHHHHHHHHHH
75.8133845483
858UbiquitinationKLCLPMLCFLLHTIL
HHHHHHHHHHHHHHH
1.5133845483
865UbiquitinationCFLLHTILHSTGQYQ
HHHHHHHHHHCCCHH
2.4721890473
865UbiquitinationCFLLHTILHSTGQYQ
HHHHHHHHHHCCCHH
2.47-
874UbiquitinationSTGQYQECLQLADMV
HCCCHHHHHHHHHHH
1.4121890473
887UbiquitinationMVSSERHKLYLVFSK
HHCCCCCCEEEEECH
45.0833845483
893O-linked_GlycosylationHKLYLVFSKEELRKL
CCEEEEECHHHHHHH
31.5130059200
894UbiquitinationKLYLVFSKEELRKLL
CEEEEECHHHHHHHH
43.6821890473
894UbiquitinationKLYLVFSKEELRKLL
CEEEEECHHHHHHHH
43.6821890473
907PhosphorylationLLQKLRESSLMLLDQ
HHHHHHHHHHHHHHC
23.4930387612
908PhosphorylationLQKLRESSLMLLDQG
HHHHHHHHHHHHHCC
17.0330387612

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

Oops, there are no upstream regulatory protein records of NU107_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NU107_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 NU107_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU133_HUMANNUP133physical
15146057
NUP85_HUMANNUP85physical
15146057
NU160_HUMANNUP160physical
15146057
NU133_HUMANNUP133physical
11564755
IMB1_HUMANKPNB1physical
12894213
NU160_HUMANNUP160physical
20676042
NU133_HUMANNUP133physical
20676042
NUP98_HUMANNUP98physical
20676042
NUP85_HUMANNUP85physical
20676042
NUP43_HUMANNUP43physical
20676042
NUP37_HUMANNUP37physical
20676042
SEH1_HUMANSEH1Lphysical
20676042
SEC13_HUMANSEC13physical
20676042
WRIP1_HUMANWRNIP1physical
20676042
NUP98_HUMANNUP98physical
17360435
NU133_HUMANNUP133physical
17360435
NU160_HUMANNUP160physical
17360435
NUP85_HUMANNUP85physical
17360435
NUP43_HUMANNUP43physical
17360435
NUP37_HUMANNUP37physical
17360435
SEH1_HUMANSEH1Lphysical
17360435
SEC13_HUMANSEC13physical
17360435
NU133_HUMANNUP133physical
22939629
NU153_HUMANNUP153physical
22939629
TP53B_HUMANTP53BP1physical
22939629
PNPT1_HUMANPNPT1physical
22939629
NU153_HUMANNUP153physical
26344197
NUP37_HUMANNUP37physical
26344197
SYNE1_HUMANSYNE1physical
24927568
NU160_HUMANNUP160physical
24927568
APC_HUMANAPCphysical
24927568
PRKDC_HUMANPRKDCphysical
24927568
RRP1B_HUMANRRP1Bphysical
24927568
NALCN_HUMANNALCNphysical
24927568
IMB1_HUMANKPNB1physical
24927568
CD1E_HUMANCD1Ephysical
24927568
ACTBL_HUMANACTBL2physical
24927568
HS90B_HUMANHSP90AB1physical
24927568
XPO1_HUMANXPO1physical
24927568
SEH1_HUMANSEH1Lphysical
24927568
NU214_HUMANNUP214physical
24927568
SENP1_HUMANSENP1physical
24927568
SENP2_HUMANSENP2physical
24927568
ELYS_HUMANAHCTF1physical
24927568
RAGP1_HUMANRANGAP1physical
24927568
H2AV_HUMANH2AFVphysical
24927568
NUP98_HUMANNUP98physical
24927568
NU133_HUMANNUP133physical
24927568
TPR_HUMANTPRphysical
24927568
NUP50_HUMANNUP50physical
24927568
NU153_HUMANNUP153physical
24927568
RBP2_HUMANRANBP2physical
24927568
NUP85_HUMANNUP85physical
24927568
ACLY_HUMANACLYphysical
26496610
RCC1_HUMANRCC1physical
26496610
GLE1_HUMANGLE1physical
26496610
ITPR2_HUMANITPR2physical
26496610
IMB1_HUMANKPNB1physical
26496610
IMA3_HUMANKPNA4physical
26496610
NUP88_HUMANNUP88physical
26496610
NUP98_HUMANNUP98physical
26496610
RAN_HUMANRANphysical
26496610
RBP2_HUMANRANBP2physical
26496610
RAGP1_HUMANRANGAP1physical
26496610
SEC13_HUMANSEC13physical
26496610
TPR_HUMANTPRphysical
26496610
UBC9_HUMANUBE2Iphysical
26496610
SUMO1_HUMANSUMO1physical
26496610
NU214_HUMANNUP214physical
26496610
AAAS_HUMANAAASphysical
26496610
RAE1L_HUMANRAE1physical
26496610
NU155_HUMANNUP155physical
26496610
NUP93_HUMANNUP93physical
26496610
NUP58_HUMANNUPL1physical
26496610
WDR1_HUMANWDR1physical
26496610
NU153_HUMANNUP153physical
26496610
NXF1_HUMANNXF1physical
26496610
IPO7_HUMANIPO7physical
26496610
NUP50_HUMANNUP50physical
26496610
NUPL2_HUMANNUPL2physical
26496610
NU205_HUMANNUP205physical
26496610
PO210_HUMANNUP210physical
26496610
NU160_HUMANNUP160physical
26496610
NU188_HUMANNUP188physical
26496610
NUP62_HUMANNUP62physical
26496610
NXT1_HUMANNXT1physical
26496610
S61A1_HUMANSEC61A1physical
26496610
NUP54_HUMANNUP54physical
26496610
TM214_HUMANTMEM214physical
26496610
NSMA3_HUMANSMPD4physical
26496610
NDC1_HUMANNDC1physical
26496610
NU133_HUMANNUP133physical
26496610
SENP2_HUMANSENP2physical
26496610
NUP37_HUMANNUP37physical
26496610
NUP85_HUMANNUP85physical
26496610
SEH1_HUMANSEH1Lphysical
26496610
TM209_HUMANTMEM209physical
26496610
NUP53_HUMANNUP35physical
26496610
RUSD3_HUMANRPUSD3physical
26496610
NUP43_HUMANNUP43physical
26496610
RGPD8_HUMANRGPD8physical
26496610
RAF1_HUMANRAF1physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NU107_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-10 AND SER-11, 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-11; SER-37 AND THR-46,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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-10 AND SER-11, 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-11, 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-4; SER-11; SER-37;THR-46; THR-55; SER-58; THR-64; SER-69; SER-77 AND SER-86, AND MASSSPECTROMETRY.
"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-11, 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-11 AND THR-55, 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-37, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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-4; SER-11; THR-46;THR-55; SER-58 AND THR-64, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.
"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 THR-46, AND MASSSPECTROMETRY.

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