NASP_HUMAN - dbPTM
NASP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NASP_HUMAN
UniProt AC P49321
Protein Name Nuclear autoantigenic sperm protein
Gene Name NASP
Organism Homo sapiens (Human).
Sequence Length 788
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA..
Protein Sequence MAMESTATAAVAAELVSADKIEDVPAPSTSADKVESLDVDSEAKKLLGLGQKHLVMGDIPAAVNAFQEAASLLGKKYGETANECGEAFFFYGKSLLELARMENGVLGNALEGVHVEEEEGEKTEDESLVENNDNIDEEAREELREQVYDAMGEKEEAKKTEDKSLAKPETDKEQDSEMEKGGREDMDISKSAEEPQEKVDLTLDWLTETSEEAKGGAAPEGPNEAEVTSGKPEQEVPDAEEEKSVSGTDVQEECREKGGQEKQGEVIVSIEEKPKEVSEEQPVVTLEKQGTAVEVEAESLDPTVKPVDVGGDEPEEKVVTSENEAGKAVLEQLVGQEVPPAEESPEVTTEAAEASAVEAGSEVSEKPGQEAPVLPKDGAVNGPSVVGDQTPIEPQTSIERLTETKDGSGLEEKVRAKLVPSQEETKLSVEESEAAGDGVDTKVAQGATEKSPEDKVQIAANEETQEREEQMKEGEETEGSEEDDKENDKTEEMPNDSVLENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGSSAEYKKEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVESSTSGFTPGGGGSSVSMIASRKPTDGASSSNCVTDISHLVRKKRKPEEESPRKDDAKKAKQEPEVNGGSGDAVPSGNEVSENMEEEAENQAESRAAVEGTVEAGATVESTAC
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------MAMESTATA
------CCCCHHHHH
15.5122223895
17PhosphorylationAVAAELVSADKIEDV
HHHHHHHCCHHCCCC
43.2926074081
20AcetylationAELVSADKIEDVPAP
HHHHCCHHCCCCCCC
47.9530585385
28PhosphorylationIEDVPAPSTSADKVE
CCCCCCCCCCCHHCC
36.7828450419
29PhosphorylationEDVPAPSTSADKVES
CCCCCCCCCCHHCCC
27.2028450419
30PhosphorylationDVPAPSTSADKVESL
CCCCCCCCCHHCCCC
38.5221815630
33AcetylationAPSTSADKVESLDVD
CCCCCCHHCCCCCCC
47.8519608861
33UbiquitinationAPSTSADKVESLDVD
CCCCCCHHCCCCCCC
47.8519608861
33 (in isoform 1)Ubiquitination-47.8521890473
33 (in isoform 2)Ubiquitination-47.8521890473
33 (in isoform 4)Acetylation-47.85-
36PhosphorylationTSADKVESLDVDSEA
CCCHHCCCCCCCHHH
32.6225159151
41PhosphorylationVESLDVDSEAKKLLG
CCCCCCCHHHHHHHC
39.0227732954
442-HydroxyisobutyrylationLDVDSEAKKLLGLGQ
CCCCHHHHHHHCCCC
39.64-
45UbiquitinationDVDSEAKKLLGLGQK
CCCHHHHHHHCCCCC
56.8621890473
45UbiquitinationDVDSEAKKLLGLGQK
CCCHHHHHHHCCCCC
56.8621890473
45 (in isoform 1)Ubiquitination-56.8621890473
45 (in isoform 2)Ubiquitination-56.8621890473
47 (in isoform 3)Ubiquitination-7.9521890473
52UbiquitinationKLLGLGQKHLVMGDI
HHHCCCCCEEECCCH
36.7921906983
52 (in isoform 1)Ubiquitination-36.7921890473
52 (in isoform 2)Ubiquitination-36.7921890473
54 (in isoform 3)Ubiquitination-3.5021890473
71PhosphorylationNAFQEAASLLGKKYG
HHHHHHHHHHCHHHC
31.0425159151
752-HydroxyisobutyrylationEAASLLGKKYGETAN
HHHHHHCHHHCCHHH
42.67-
75UbiquitinationEAASLLGKKYGETAN
HHHHHHCHHHCCHHH
42.67-
76UbiquitinationAASLLGKKYGETANE
HHHHHCHHHCCHHHH
57.60-
77PhosphorylationASLLGKKYGETANEC
HHHHCHHHCCHHHHH
24.5528152594
78 (in isoform 3)Ubiquitination-34.36-
84GlutathionylationYGETANECGEAFFFY
HCCHHHHHHHHHHHH
6.3122555962
93UbiquitinationEAFFFYGKSLLELAR
HHHHHHHHHHHHHHH
26.9321906983
93 (in isoform 1)Ubiquitination-26.9321890473
93 (in isoform 2)Ubiquitination-26.9321890473
94PhosphorylationAFFFYGKSLLELARM
HHHHHHHHHHHHHHH
33.5521712546
95 (in isoform 3)Ubiquitination-4.9921890473
123PhosphorylationEEEEGEKTEDESLVE
CHHCCCCCCCHHHHC
44.3519664994
123 (in isoform 2)Phosphorylation-44.3520068231
127PhosphorylationGEKTEDESLVENNDN
CCCCCCHHHHCCCCC
50.4619664994
127 (in isoform 2)Phosphorylation-50.4620068231
138 (in isoform 2)Phosphorylation-49.6428355574
140MethylationDNIDEEAREELREQV
CCCCHHHHHHHHHHH
41.00115484511
141 (in isoform 2)Phosphorylation-69.3126503892
148PhosphorylationEELREQVYDAMGEKE
HHHHHHHHHHHCCHH
9.5525884760
151 (in isoform 2)Phosphorylation-6.9525159151
154AcetylationVYDAMGEKEEAKKTE
HHHHHCCHHHHHHHC
55.9423954790
158 (in isoform 2)Phosphorylation-64.6023909892
164PhosphorylationAKKTEDKSLAKPETD
HHHHCCCCCCCCCCC
45.9719664994
169 (in isoform 3)Ubiquitination-69.77-
170PhosphorylationKSLAKPETDKEQDSE
CCCCCCCCCHHHHHH
61.9829255136
176PhosphorylationETDKEQDSEMEKGGR
CCCHHHHHHHHHCCH
38.2429255136
180AcetylationEQDSEMEKGGREDMD
HHHHHHHHCCHHCCC
66.4123236377
189PhosphorylationGREDMDISKSAEEPQ
CHHCCCCHHCCCCCH
19.1223401153
191PhosphorylationEDMDISKSAEEPQEK
HCCCCHHCCCCCHHH
33.8421712546
196 (in isoform 2)Ubiquitination-67.4321890473
202PhosphorylationPQEKVDLTLDWLTET
CHHHHCCCHHHHHCC
20.4330301811
207PhosphorylationDLTLDWLTETSEEAK
CCCHHHHHCCCHHHC
32.7227732954
209PhosphorylationTLDWLTETSEEAKGG
CHHHHHCCCHHHCCC
35.8827732954
210PhosphorylationLDWLTETSEEAKGGA
HHHHHCCCHHHCCCC
27.4919664994
228PhosphorylationGPNEAEVTSGKPEQE
CCCCCCCCCCCCCCC
24.2225159151
229PhosphorylationPNEAEVTSGKPEQEV
CCCCCCCCCCCCCCC
50.4225159151
231AcetylationEAEVTSGKPEQEVPD
CCCCCCCCCCCCCCC
45.1923236377
231UbiquitinationEAEVTSGKPEQEVPD
CCCCCCCCCCCCCCC
45.1921906983
231 (in isoform 1)Ubiquitination-45.1921890473
233 (in isoform 3)Ubiquitination-63.9621890473
243AcetylationVPDAEEEKSVSGTDV
CCCHHHHHCCCCCHH
60.48-
244PhosphorylationPDAEEEKSVSGTDVQ
CCHHHHHCCCCCHHH
25.4619664994
246PhosphorylationAEEEKSVSGTDVQEE
HHHHHCCCCCHHHHH
42.9619664994
248PhosphorylationEEKSVSGTDVQEECR
HHHCCCCCHHHHHHH
26.0319664994
269PhosphorylationKQGEVIVSIEEKPKE
CCCEEEEEEECCCCC
17.1028348404
278PhosphorylationEEKPKEVSEEQPVVT
ECCCCCCCCCCCCEE
36.1925849741
285PhosphorylationSEEQPVVTLEKQGTA
CCCCCCEEEEECCEE
29.4521406692
287 (in isoform 2)Ubiquitination-33.6921890473
288AcetylationQPVVTLEKQGTAVEV
CCCEEEEECCEEEEE
58.08-
291O-linked_GlycosylationVTLEKQGTAVEVEAE
EEEEECCEEEEEEEH
25.6523301498
291PhosphorylationVTLEKQGTAVEVEAE
EEEEECCEEEEEEEH
25.6528464451
298 (in isoform 2)Ubiquitination-38.0321890473
299PhosphorylationAVEVEAESLDPTVKP
EEEEEEHHCCCCCCC
45.1525159151
303PhosphorylationEAESLDPTVKPVDVG
EEHHCCCCCCCCCCC
40.6123403867
304 (in isoform 2)Ubiquitination-8.8621890473
313 (in isoform 2)Ubiquitination-58.8621890473
318 (in isoform 2)Ubiquitination-6.8521890473
320PhosphorylationEPEEKVVTSENEAGK
CCCHHEECCCCHHHH
33.0525850435
321PhosphorylationPEEKVVTSENEAGKA
CCHHEECCCCHHHHH
27.1529255136
332 (in isoform 2)Ubiquitination-36.9721890473
344PhosphorylationEVPPAEESPEVTTEA
CCCCCHHCCCCCHHH
20.1928464451
348PhosphorylationAEESPEVTTEAAEAS
CHHCCCCCHHHHHHH
19.7725627689
349PhosphorylationEESPEVTTEAAEASA
HHCCCCCHHHHHHHH
28.8928464451
361PhosphorylationASAVEAGSEVSEKPG
HHHHHCCCCCCCCCC
41.7022210691
384PhosphorylationDGAVNGPSVVGDQTP
CCCCCCCCCCCCCCC
30.7330266825
390PhosphorylationPSVVGDQTPIEPQTS
CCCCCCCCCCCCCCC
30.8530266825
396PhosphorylationQTPIEPQTSIERLTE
CCCCCCCCCHHHHHC
42.2430266825
397PhosphorylationTPIEPQTSIERLTET
CCCCCCCCHHHHHCC
19.7330266825
402PhosphorylationQTSIERLTETKDGSG
CCCHHHHHCCCCCCC
48.0728450419
404PhosphorylationSIERLTETKDGSGLE
CHHHHHCCCCCCCHH
29.2428450419
405UbiquitinationIERLTETKDGSGLEE
HHHHHCCCCCCCHHH
54.59-
408O-linked_GlycosylationLTETKDGSGLEEKVR
HHCCCCCCCHHHHHH
50.7923301498
408PhosphorylationLTETKDGSGLEEKVR
HHCCCCCCCHHHHHH
50.7921712546
413UbiquitinationDGSGLEEKVRAKLVP
CCCCHHHHHHHEECC
27.87-
417AcetylationLEEKVRAKLVPSQEE
HHHHHHHEECCCHHH
39.1823954790
417UbiquitinationLEEKVRAKLVPSQEE
HHHHHHHEECCCHHH
39.18-
421PhosphorylationVRAKLVPSQEETKLS
HHHEECCCHHHHCCC
42.6229255136
425PhosphorylationLVPSQEETKLSVEES
ECCCHHHHCCCHHHH
36.2130266825
426UbiquitinationVPSQEETKLSVEESE
CCCHHHHCCCHHHHH
41.88-
428PhosphorylationSQEETKLSVEESEAA
CHHHHCCCHHHHHHC
29.1030266825
428 (in isoform 3)Ubiquitination-29.10-
432PhosphorylationTKLSVEESEAAGDGV
HCCCHHHHHHCCCCC
21.0130266825
441PhosphorylationAAGDGVDTKVAQGAT
HCCCCCCCCHHCCCC
25.6320873877
442UbiquitinationAGDGVDTKVAQGATE
CCCCCCCCHHCCCCC
30.9821906983
442 (in isoform 1)Ubiquitination-30.9821890473
444 (in isoform 3)Ubiquitination-12.0221890473
448PhosphorylationTKVAQGATEKSPEDK
CCHHCCCCCCCHHHH
51.2630266825
450AcetylationVAQGATEKSPEDKVQ
HHCCCCCCCHHHHHH
67.9425953088
451PhosphorylationAQGATEKSPEDKVQI
HCCCCCCCHHHHHHH
27.5629255136
455AcetylationTEKSPEDKVQIAANE
CCCCHHHHHHHHCCH
34.0823954790
464PhosphorylationQIAANEETQEREEQM
HHHCCHHHHHHHHHH
29.5619664994
477PhosphorylationQMKEGEETEGSEEDD
HHHHHCCCCCCCCCC
41.1520201521
480PhosphorylationEGEETEGSEEDDKEN
HHCCCCCCCCCCCCC
31.4220201521
490PhosphorylationDDKENDKTEEMPNDS
CCCCCCCCCCCCCCH
39.7930266825
497PhosphorylationTEEMPNDSVLENKSL
CCCCCCCHHHCCCCC
34.9325159151
503PhosphorylationDSVLENKSLQENEEE
CHHHCCCCCCCCCHH
47.0319664994
534PhosphorylationIIFKRQETKEAQLYA
HHHHCCCHHHHHHHH
26.3330624053
535UbiquitinationIFKRQETKEAQLYAA
HHHCCCHHHHHHHHH
50.7521890473
535UbiquitinationIFKRQETKEAQLYAA
HHHCCCHHHHHHHHH
50.7521890473
535 (in isoform 1)Ubiquitination-50.7521890473
537 (in isoform 3)Ubiquitination-13.2621890473
540NitrationETKEAQLYAAQAHLK
CHHHHHHHHHHHHHH
6.44-
540PhosphorylationETKEAQLYAAQAHLK
CHHHHHHHHHHHHHH
6.4428152594
567PhosphorylationQAVEEFQSCLNLQEQ
HHHHHHHHHHHHHHH
26.37-
575PhosphorylationCLNLQEQYLEAHDRL
HHHHHHHHHHHHHHH
13.03-
598PhosphorylationGLAYGYNSQYDEAVA
HCCCCCCHHHHHHHH
22.95-
608O-linked_GlycosylationDEAVAQFSKSIEVIE
HHHHHHHHHHHHHHH
17.2623301498
610PhosphorylationAVAQFSKSIEVIENR
HHHHHHHHHHHHHHH
23.8427732954
617MethylationSIEVIENRMAVLNEQ
HHHHHHHHHHHHHHH
11.14115484503
618SulfoxidationIEVIENRMAVLNEQV
HHHHHHHHHHHHHHH
4.5721406390
626UbiquitinationAVLNEQVKEAEGSSA
HHHHHHHHHHCCCCH
51.4021906983
626 (in isoform 1)Ubiquitination-51.4021890473
628 (in isoform 3)Ubiquitination-22.2621890473
631PhosphorylationQVKEAEGSSAEYKKE
HHHHHCCCCHHHHHH
20.2021815630
632PhosphorylationVKEAEGSSAEYKKEI
HHHHCCCCHHHHHHH
35.6628985074
635PhosphorylationAEGSSAEYKKEIEEL
HCCCCHHHHHHHHHH
27.3828985074
636SumoylationEGSSAEYKKEIEELK
CCCCHHHHHHHHHHH
35.12-
636AcetylationEGSSAEYKKEIEELK
CCCCHHHHHHHHHHH
35.1225953088
636SumoylationEGSSAEYKKEIEELK
CCCCHHHHHHHHHHH
35.12-
637UbiquitinationGSSAEYKKEIEELKE
CCCHHHHHHHHHHHH
64.1221890473
6372-HydroxyisobutyrylationGSSAEYKKEIEELKE
CCCHHHHHHHHHHHH
64.12-
637UbiquitinationGSSAEYKKEIEELKE
CCCHHHHHHHHHHHH
64.1221890473
637 (in isoform 1)Ubiquitination-64.1221890473
639 (in isoform 3)Ubiquitination-7.3721890473
643UbiquitinationKKEIEELKELLPEIR
HHHHHHHHHHHHHHH
49.9821890473
6432-HydroxyisobutyrylationKKEIEELKELLPEIR
HHHHHHHHHHHHHHH
49.98-
643AcetylationKKEIEELKELLPEIR
HHHHHHHHHHHHHHH
49.9823954790
643UbiquitinationKKEIEELKELLPEIR
HHHHHHHHHHHHHHH
49.9821890473
643 (in isoform 1)Ubiquitination-49.9821890473
645 (in isoform 3)Ubiquitination-10.3921890473
652UbiquitinationLLPEIREKIEDAKES
HHHHHHHHHHHHHHH
41.3621906983
652 (in isoform 1)Ubiquitination-41.3621890473
654 (in isoform 3)Ubiquitination-64.0821890473
657SuccinylationREKIEDAKESQRSGN
HHHHHHHHHHHHCCC
70.9423954790
657UbiquitinationREKIEDAKESQRSGN
HHHHHHHHHHHHCCC
70.94-
657 (in isoform 1)Ubiquitination-70.9421890473
659PhosphorylationKIEDAKESQRSGNVA
HHHHHHHHHHCCCHH
30.1325159151
659 (in isoform 3)Ubiquitination-30.1321890473
662PhosphorylationDAKESQRSGNVAELA
HHHHHHHCCCHHHHH
27.3825159151
671UbiquitinationNVAELALKATLVESS
CHHHHHHHHHEEECC
33.452190698
671 (in isoform 1)Ubiquitination-33.4521890473
673O-linked_GlycosylationAELALKATLVESSTS
HHHHHHHHEEECCCC
29.7423301498
673PhosphorylationAELALKATLVESSTS
HHHHHHHHEEECCCC
29.7427080861
673 (in isoform 3)Ubiquitination-29.7421890473
677O-linked_GlycosylationLKATLVESSTSGFTP
HHHHEEECCCCCCCC
31.2823301498
677PhosphorylationLKATLVESSTSGFTP
HHHHEEECCCCCCCC
31.2830576142
678O-linked_GlycosylationKATLVESSTSGFTPG
HHHEEECCCCCCCCC
17.0623301498
678PhosphorylationKATLVESSTSGFTPG
HHHEEECCCCCCCCC
17.0629978859
679O-linked_GlycosylationATLVESSTSGFTPGG
HHEEECCCCCCCCCC
41.9923301498
679PhosphorylationATLVESSTSGFTPGG
HHEEECCCCCCCCCC
41.9925850435
680O-linked_GlycosylationTLVESSTSGFTPGGG
HEEECCCCCCCCCCC
33.5823301498
680PhosphorylationTLVESSTSGFTPGGG
HEEECCCCCCCCCCC
33.5830576142
683O-linked_GlycosylationESSTSGFTPGGGGSS
ECCCCCCCCCCCCCC
25.2523301498
683PhosphorylationESSTSGFTPGGGGSS
ECCCCCCCCCCCCCC
25.2525159151
689O-linked_GlycosylationFTPGGGGSSVSMIAS
CCCCCCCCCCHHEEE
30.7323301498
689PhosphorylationFTPGGGGSSVSMIAS
CCCCCCCCCCHHEEE
30.7325850435
690PhosphorylationTPGGGGSSVSMIASR
CCCCCCCCCHHEEEC
22.8325850435
692PhosphorylationGGGGSSVSMIASRKP
CCCCCCCHHEEECCC
13.3526074081
693SulfoxidationGGGSSVSMIASRKPT
CCCCCCHHEEECCCC
2.5130846556
696PhosphorylationSSVSMIASRKPTDGA
CCCHHEEECCCCCCC
29.8826074081
698AcetylationVSMIASRKPTDGASS
CHHEEECCCCCCCCC
50.1823749302
698UbiquitinationVSMIASRKPTDGASS
CHHEEECCCCCCCCC
50.18-
700PhosphorylationMIASRKPTDGASSSN
HEEECCCCCCCCCCC
50.5323401153
700 (in isoform 3)Ubiquitination-50.53-
704PhosphorylationRKPTDGASSSNCVTD
CCCCCCCCCCCHHHH
39.5723401153
705PhosphorylationKPTDGASSSNCVTDI
CCCCCCCCCCHHHHH
25.6530266825
706PhosphorylationPTDGASSSNCVTDIS
CCCCCCCCCHHHHHH
31.5830266825
708GlutathionylationDGASSSNCVTDISHL
CCCCCCCHHHHHHHH
3.6322555962
710O-linked_GlycosylationASSSNCVTDISHLVR
CCCCCHHHHHHHHHH
29.80OGP
710PhosphorylationASSSNCVTDISHLVR
CCCCCHHHHHHHHHH
29.8030266825
713PhosphorylationSNCVTDISHLVRKKR
CCHHHHHHHHHHHCC
17.3623403867
721MethylationHLVRKKRKPEEESPR
HHHHHCCCCCCCCCC
66.71116252357
726PhosphorylationKRKPEEESPRKDDAK
CCCCCCCCCCHHHHH
33.0329255136
733AcetylationSPRKDDAKKAKQEPE
CCCHHHHHHHHCCCC
61.337481363
734AcetylationPRKDDAKKAKQEPEV
CCHHHHHHHHCCCCC
63.646570403
736AcetylationKDDAKKAKQEPEVNG
HHHHHHHHCCCCCCC
65.1623236377
736SumoylationKDDAKKAKQEPEVNG
HHHHHHHHCCCCCCC
65.1625114211
745PhosphorylationEPEVNGGSGDAVPSG
CCCCCCCCCCCCCCC
34.5930576142
751PhosphorylationGSGDAVPSGNEVSEN
CCCCCCCCCCHHCHH
47.8828102081
756PhosphorylationVPSGNEVSENMEEEA
CCCCCHHCHHHHHHH
19.6429978859
769PhosphorylationEAENQAESRAAVEGT
HHHHHHHHHHHHHCE
30.1822210691
782PhosphorylationGTVEAGATVESTAC-
CEECCCCEEEECCC-
24.7222817901
785PhosphorylationEAGATVESTAC----
CCCCEEEECCC----
19.5722817901
788GlutathionylationATVESTAC-------
CEEEECCC-------
6.0822555962

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
158SPhosphorylationKinaseCSNK2A1P68400
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NASP_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 NASP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H32_HUMANHIST2H3Cphysical
16189514
LC7L2_HUMANLUC7L2physical
16169070
H31_HUMANHIST1H3Aphysical
20167597
AIRE_HUMANAIREphysical
20085707
TERA_HUMANVCPphysical
22939629
STIP1_HUMANSTIP1physical
22939629
ERF3B_HUMANGSPT2physical
22863883
H3C_HUMANH3F3Cphysical
25416956
DKC1_HUMANDKC1physical
26344197
RBBP4_HUMANRBBP4physical
26496610
RBBP7_HUMANRBBP7physical
26496610
KCAB2_HUMANKCNAB2physical
26496610
HAT1_HUMANHAT1physical
26496610
ASF1A_HUMANASF1Aphysical
26496610
S43A3_HUMANSLC43A3physical
26496610
DONS_HUMANDONSONphysical
26496610
ASF1B_HUMANASF1Bphysical
26496610
PYRG2_HUMANCTPS2physical
26496610
KLF16_HUMANKLF16physical
26496610
H2A1_YEASTHTA1physical
27618665
H2B1_YEASTHTB1physical
27618665
H3_YEASTHHT1physical
27618665
H4_YEASTHHF1physical
27618665
EKI1_HUMANETNK1physical
28514442
RBBP4_HUMANRBBP4physical
28514442

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 NASP_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-30; SER-421 AND SER-497, AND MASS SPECTROMETRY.
"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-33, 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 THR-390 AND SER-503, ANDMASS 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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-30; SER-421 AND SER-497, AND MASS 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-189; SER-244; THR-390;SER-408 AND THR-683, AND MASS SPECTROMETRY.
"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-421; SER-451 ANDTHR-464, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228; THR-390; THR-477;SER-480; SER-497 AND SER-726, 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-189; SER-244; SER-451;THR-477; SER-480; SER-503 AND SER-726, AND MASS 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 THR-390 AND SER-421, ANDMASS 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 THR-390, AND MASSSPECTROMETRY.

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