NUSAP_HUMAN - dbPTM
NUSAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUSAP_HUMAN
UniProt AC Q9BXS6
Protein Name Nucleolar and spindle-associated protein 1
Gene Name NUSAP1
Organism Homo sapiens (Human).
Sequence Length 441
Subcellular Localization Cytoplasm. Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Chromosome. Found in the cytoplasm and nucleolus during interphase and redistributes to the mitotic spindle in prometaphase (By similarity). Localizes to the mitotic spindle during anap
Protein Description Microtubule-associated protein with the capacity to bundle and stabilize microtubules (By similarity). May associate with chromosomes and promote the organization of mitotic spindle microtubules around them..
Protein Sequence MIIPSLEELDSLKYSDLQNLAKSLGLRANLRATKLLKALKGYIKHEARKGNENQDESQTSASSCDETEIQISNQEEAERQPLGHVTKTRRRCKTVRVDPDSQQNHSEIKISNPTEFQNHEKQESQDLRATAKVPSPPDEHQEAENAVSSGNRDSKVPSEGKKSLYTDESSKPGKNKRTAITTPNFKKLHEAHFKEMESIDQYIERKKKHFEEHNSMNELKQQPINKGGVRTPVPPRGRLSVASTPISQRRSQGRSCGPASQSTLGLKGSLKRSAISAAKTGVRFSAATKDNEHKRSLTKTPARKSAHVTVSGGTPKGEAVLGTHKLKTITGNSAAVITPFKLTTEATQTPVSNKKPVFDLKASLSRPLNYEPHKGKLKPWGQSKENNYLNQHVNRINFYKKTYKQPHLQTKEEQRKKREQERKEKKAKVLGMRRGLILAED
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
5Phosphorylation---MIIPSLEELDSL
---CCCCCHHHHHHC
37.7026552605
11PhosphorylationPSLEELDSLKYSDLQ
CCHHHHHHCCHHHHH
39.1126552605
33PhosphorylationLRANLRATKLLKALK
HHHHHHHHHHHHHHH
18.78-
57PhosphorylationGNENQDESQTSASSC
CCCCCCHHHCCHHHC
47.2323663014
59PhosphorylationENQDESQTSASSCDE
CCCCHHHCCHHHCCC
35.2223663014
60PhosphorylationNQDESQTSASSCDET
CCCHHHCCHHHCCCC
20.6523663014
62PhosphorylationDESQTSASSCDETEI
CHHHCCHHHCCCCEE
31.1323663014
63PhosphorylationESQTSASSCDETEIQ
HHHCCHHHCCCCEEE
25.8823663014
67PhosphorylationSASSCDETEIQISNQ
CHHHCCCCEEECCCH
25.7423663014
84UbiquitinationAERQPLGHVTKTRRR
HHHCCCCCHHHCCCC
31.5824816145
87AcetylationQPLGHVTKTRRRCKT
CCCCCHHHCCCCEEE
38.6625953088
99UbiquitinationCKTVRVDPDSQQNHS
EEEEEECCCCCCCCC
40.0524816145
101PhosphorylationTVRVDPDSQQNHSEI
EEEECCCCCCCCCCC
38.7725849741
106PhosphorylationPDSQQNHSEIKISNP
CCCCCCCCCCCCCCC
48.8725159151
109 (in isoform 4)Phosphorylation-35.7125849741
109 (in isoform 6)Phosphorylation-35.7125849741
111PhosphorylationNHSEIKISNPTEFQN
CCCCCCCCCCHHHCC
31.5823186163
114PhosphorylationEIKISNPTEFQNHEK
CCCCCCCHHHCCCCH
54.4023186163
121UbiquitinationTEFQNHEKQESQDLR
HHHCCCCHHHCCCHH
52.3816196087
124PhosphorylationQNHEKQESQDLRATA
CCCCHHHCCCHHHHC
26.8817525332
130PhosphorylationESQDLRATAKVPSPP
HCCCHHHHCCCCCCC
22.1524732914
132AcetylationQDLRATAKVPSPPDE
CCHHHHCCCCCCCHH
50.7725953088
135PhosphorylationRATAKVPSPPDEHQE
HHHCCCCCCCHHHHH
52.6429255136
139UbiquitinationKVPSPPDEHQEAENA
CCCCCCHHHHHHHHH
53.9324816145
147UbiquitinationHQEAENAVSSGNRDS
HHHHHHHHHCCCCCC
7.6424816145
148PhosphorylationQEAENAVSSGNRDSK
HHHHHHHHCCCCCCC
30.0725159151
148UbiquitinationQEAENAVSSGNRDSK
HHHHHHHHCCCCCCC
30.0716196087
149PhosphorylationEAENAVSSGNRDSKV
HHHHHHHCCCCCCCC
33.2225159151
151UbiquitinationENAVSSGNRDSKVPS
HHHHHCCCCCCCCCC
46.6716196087
153UbiquitinationAVSSGNRDSKVPSEG
HHHCCCCCCCCCCCC
57.7324816145
154PhosphorylationVSSGNRDSKVPSEGK
HHCCCCCCCCCCCCC
32.1125056879
156UbiquitinationSGNRDSKVPSEGKKS
CCCCCCCCCCCCCCC
7.9416196087
158PhosphorylationNRDSKVPSEGKKSLY
CCCCCCCCCCCCCCC
63.0726055452
159UbiquitinationRDSKVPSEGKKSLYT
CCCCCCCCCCCCCCC
69.8016196087
161UbiquitinationSKVPSEGKKSLYTDE
CCCCCCCCCCCCCCC
34.8324816145
162UbiquitinationKVPSEGKKSLYTDES
CCCCCCCCCCCCCCC
57.4624816145
164UbiquitinationPSEGKKSLYTDESSK
CCCCCCCCCCCCCCC
7.9829967540
165PhosphorylationSEGKKSLYTDESSKP
CCCCCCCCCCCCCCC
21.1625884760
165UbiquitinationSEGKKSLYTDESSKP
CCCCCCCCCCCCCCC
21.1616196087
166PhosphorylationEGKKSLYTDESSKPG
CCCCCCCCCCCCCCC
38.2928555341
167UbiquitinationGKKSLYTDESSKPGK
CCCCCCCCCCCCCCC
39.9824816145
168UbiquitinationKKSLYTDESSKPGKN
CCCCCCCCCCCCCCC
49.4624816145
169PhosphorylationKSLYTDESSKPGKNK
CCCCCCCCCCCCCCC
46.6128985074
170PhosphorylationSLYTDESSKPGKNKR
CCCCCCCCCCCCCCC
40.60-
170UbiquitinationSLYTDESSKPGKNKR
CCCCCCCCCCCCCCC
40.6016196087
171UbiquitinationLYTDESSKPGKNKRT
CCCCCCCCCCCCCCC
68.0516196087
172UbiquitinationYTDESSKPGKNKRTA
CCCCCCCCCCCCCCE
62.0229967540
173UbiquitinationTDESSKPGKNKRTAI
CCCCCCCCCCCCCEE
50.3216196087
174UbiquitinationDESSKPGKNKRTAIT
CCCCCCCCCCCCEEE
68.7516196087
176UbiquitinationSSKPGKNKRTAITTP
CCCCCCCCCCEEECC
55.3916196087
177UbiquitinationSKPGKNKRTAITTPN
CCCCCCCCCEEECCC
38.4916196087
178PhosphorylationKPGKNKRTAITTPNF
CCCCCCCCEEECCCH
24.8330266825
179UbiquitinationPGKNKRTAITTPNFK
CCCCCCCEEECCCHH
10.9316196087
180UbiquitinationGKNKRTAITTPNFKK
CCCCCCEEECCCHHH
4.3316196087
181PhosphorylationKNKRTAITTPNFKKL
CCCCCEEECCCHHHH
33.4630266825
182PhosphorylationNKRTAITTPNFKKLH
CCCCEEECCCHHHHH
15.3230266825
186AcetylationAITTPNFKKLHEAHF
EEECCCHHHHHHHHH
62.1525953088
186MethylationAITTPNFKKLHEAHF
EEECCCHHHHHHHHH
62.15115974413
186UbiquitinationAITTPNFKKLHEAHF
EEECCCHHHHHHHHH
62.1529967540
187UbiquitinationITTPNFKKLHEAHFK
EECCCHHHHHHHHHH
51.4429967540
192 (in isoform 7)Phosphorylation-31.1820068231
198PhosphorylationAHFKEMESIDQYIER
HHHHHHHHHHHHHHH
30.1028674419
200 (in isoform 4)Phosphorylation-44.5020068231
214 (in isoform 3)Phosphorylation-46.3520068231
215PhosphorylationKHFEEHNSMNELKQQ
HHHHHHCCHHHHHCC
25.5420068231
215 (in isoform 2)Phosphorylation-25.5420068231
231PhosphorylationINKGGVRTPVPPRGR
CCCCCCCCCCCCCCC
26.6530266825
233UbiquitinationKGGVRTPVPPRGRLS
CCCCCCCCCCCCCCE
11.4424816145
240PhosphorylationVPPRGRLSVASTPIS
CCCCCCCEEECCCHH
17.8030266825
243O-linked_GlycosylationRGRLSVASTPISQRR
CCCCEEECCCHHHCH
32.3431373491
243PhosphorylationRGRLSVASTPISQRR
CCCCEEECCCHHHCH
32.3430266825
243UbiquitinationRGRLSVASTPISQRR
CCCCEEECCCHHHCH
32.3433845483
244PhosphorylationGRLSVASTPISQRRS
CCCEEECCCHHHCHH
18.2030266825
247PhosphorylationSVASTPISQRRSQGR
EEECCCHHHCHHCCC
20.8830266825
251PhosphorylationTPISQRRSQGRSCGP
CCHHHCHHCCCCCCC
38.8925159151
252UbiquitinationPISQRRSQGRSCGPA
CHHHCHHCCCCCCCC
49.8933845483
255PhosphorylationQRRSQGRSCGPASQS
HCHHCCCCCCCCCHH
30.1923927012
255UbiquitinationQRRSQGRSCGPASQS
HCHHCCCCCCCCCHH
30.1924816145
260PhosphorylationGRSCGPASQSTLGLK
CCCCCCCCHHHHCCC
28.0021815630
262PhosphorylationSCGPASQSTLGLKGS
CCCCCCHHHHCCCHH
24.0928152594
263PhosphorylationCGPASQSTLGLKGSL
CCCCCHHHHCCCHHH
19.7428152594
263UbiquitinationCGPASQSTLGLKGSL
CCCCCHHHHCCCHHH
19.7424816145
264UbiquitinationGPASQSTLGLKGSLK
CCCCHHHHCCCHHHH
10.2824816145
265UbiquitinationPASQSTLGLKGSLKR
CCCHHHHCCCHHHHH
25.9833845483
266UbiquitinationASQSTLGLKGSLKRS
CCHHHHCCCHHHHHH
6.8033845483
267MethylationSQSTLGLKGSLKRSA
CHHHHCCCHHHHHHH
44.66115974421
267UbiquitinationSQSTLGLKGSLKRSA
CHHHHCCCHHHHHHH
44.6633845483
269PhosphorylationSTLGLKGSLKRSAIS
HHHCCCHHHHHHHHH
29.1823401153
270UbiquitinationTLGLKGSLKRSAISA
HHCCCHHHHHHHHHH
7.9224816145
271MethylationLGLKGSLKRSAISAA
HCCCHHHHHHHHHHH
46.10115974425
273PhosphorylationLKGSLKRSAISAAKT
CCHHHHHHHHHHHHH
28.5029396449
276PhosphorylationSLKRSAISAAKTGVR
HHHHHHHHHHHHCCC
23.1433259812
277UbiquitinationLKRSAISAAKTGVRF
HHHHHHHHHHHCCCE
13.5824816145
278UbiquitinationKRSAISAAKTGVRFS
HHHHHHHHHHCCCEE
11.8024816145
279AcetylationRSAISAAKTGVRFSA
HHHHHHHHHCCCEEE
45.5925953088
279UbiquitinationRSAISAAKTGVRFSA
HHHHHHHHHCCCEEE
45.5924816145
280UbiquitinationSAISAAKTGVRFSAA
HHHHHHHHCCCEEEC
35.8629967540
284UbiquitinationAAKTGVRFSAATKDN
HHHHCCCEEECCCCC
5.6024816145
285PhosphorylationAKTGVRFSAATKDNE
HHHCCCEEECCCCCH
13.3633259812
285UbiquitinationAKTGVRFSAATKDNE
HHHCCCEEECCCCCH
13.3624816145
289AcetylationVRFSAATKDNEHKRS
CCEEECCCCCHHHCC
54.5523749302
289UbiquitinationVRFSAATKDNEHKRS
CCEEECCCCCHHHCC
54.5529967540
292UbiquitinationSAATKDNEHKRSLTK
EECCCCCHHHCCCCC
62.0033845483
293UbiquitinationAATKDNEHKRSLTKT
ECCCCCHHHCCCCCC
36.7624816145
294UbiquitinationATKDNEHKRSLTKTP
CCCCCHHHCCCCCCC
37.1924816145
296PhosphorylationKDNEHKRSLTKTPAR
CCCHHHCCCCCCCCC
45.2325849741
298PhosphorylationNEHKRSLTKTPARKS
CHHHCCCCCCCCCCC
33.8333259812
299AcetylationEHKRSLTKTPARKSA
HHHCCCCCCCCCCCC
58.7825953088
299PhosphorylationEHKRSLTKTPARKSA
HHHCCCCCCCCCCCC
58.7833259812
299UbiquitinationEHKRSLTKTPARKSA
HHHCCCCCCCCCCCC
58.7824816145
300PhosphorylationHKRSLTKTPARKSAH
HHCCCCCCCCCCCCE
19.5625849741
300UbiquitinationHKRSLTKTPARKSAH
HHCCCCCCCCCCCCE
19.5624816145
301UbiquitinationKRSLTKTPARKSAHV
HCCCCCCCCCCCCEE
31.4633845483
302UbiquitinationRSLTKTPARKSAHVT
CCCCCCCCCCCCEEE
36.4429967540
303UbiquitinationSLTKTPARKSAHVTV
CCCCCCCCCCCEEEE
34.3629967540
304UbiquitinationLTKTPARKSAHVTVS
CCCCCCCCCCEEEEE
54.8529967540
305O-linked_GlycosylationTKTPARKSAHVTVSG
CCCCCCCCCEEEEEC
20.3231373491
305PhosphorylationTKTPARKSAHVTVSG
CCCCCCCCCEEEEEC
20.3225159151
307UbiquitinationTPARKSAHVTVSGGT
CCCCCCCEEEEECCC
23.9116196087
309PhosphorylationARKSAHVTVSGGTPK
CCCCCEEEEECCCCC
10.0923927012
310UbiquitinationRKSAHVTVSGGTPKG
CCCCEEEEECCCCCC
4.9433845483
311PhosphorylationKSAHVTVSGGTPKGE
CCCEEEEECCCCCCE
23.3423927012
312UbiquitinationSAHVTVSGGTPKGEA
CCEEEEECCCCCCEE
39.3933845483
314PhosphorylationHVTVSGGTPKGEAVL
EEEEECCCCCCEEEE
25.9220201521
314UbiquitinationHVTVSGGTPKGEAVL
EEEEECCCCCCEEEE
25.9233845483
315UbiquitinationVTVSGGTPKGEAVLG
EEEECCCCCCEEEEE
46.0233845483
316UbiquitinationTVSGGTPKGEAVLGT
EEECCCCCCEEEEEE
70.0433845483
321UbiquitinationTPKGEAVLGTHKLKT
CCCCEEEEEEEEEEE
9.3816196087
322UbiquitinationPKGEAVLGTHKLKTI
CCCEEEEEEEEEEEE
21.1216196087
323PhosphorylationKGEAVLGTHKLKTIT
CCEEEEEEEEEEEEC
16.2130576142
323UbiquitinationKGEAVLGTHKLKTIT
CCEEEEEEEEEEEEC
16.2133845483
324UbiquitinationGEAVLGTHKLKTITG
CEEEEEEEEEEEECC
31.4933845483
325UbiquitinationEAVLGTHKLKTITGN
EEEEEEEEEEEECCC
52.0633845483
326UbiquitinationAVLGTHKLKTITGNS
EEEEEEEEEEECCCC
4.6133845483
327UbiquitinationVLGTHKLKTITGNSA
EEEEEEEEEECCCCC
42.5633845483
333PhosphorylationLKTITGNSAAVITPF
EEEECCCCCEEEECE
20.9619664995
338PhosphorylationGNSAAVITPFKLTTE
CCCCEEEECEEEECC
18.9725159151
339UbiquitinationNSAAVITPFKLTTEA
CCCEEEECEEEECCC
17.1633845483
340UbiquitinationSAAVITPFKLTTEAT
CCEEEECEEEECCCC
8.3033845483
341UbiquitinationAAVITPFKLTTEATQ
CEEEECEEEECCCCC
46.2429967540
343PhosphorylationVITPFKLTTEATQTP
EEECEEEECCCCCCC
24.1518669648
344PhosphorylationITPFKLTTEATQTPV
EECEEEECCCCCCCC
33.7830266825
346UbiquitinationPFKLTTEATQTPVSN
CEEEECCCCCCCCCC
11.6929967540
347PhosphorylationFKLTTEATQTPVSNK
EEEECCCCCCCCCCC
27.0930266825
348AcetylationKLTTEATQTPVSNKK
EEECCCCCCCCCCCC
51.3519608861
349PhosphorylationLTTEATQTPVSNKKP
EECCCCCCCCCCCCC
22.6923401153
352PhosphorylationEATQTPVSNKKPVFD
CCCCCCCCCCCCEEE
44.1023401153
352UbiquitinationEATQTPVSNKKPVFD
CCCCCCCCCCCCEEE
44.1033845483
353UbiquitinationATQTPVSNKKPVFDL
CCCCCCCCCCCEEEC
57.5133845483
354AcetylationTQTPVSNKKPVFDLK
CCCCCCCCCCEEECC
51.4525953088
354UbiquitinationTQTPVSNKKPVFDLK
CCCCCCCCCCEEECC
51.4533845483
355UbiquitinationQTPVSNKKPVFDLKA
CCCCCCCCCEEECCH
51.1433845483
359UbiquitinationSNKKPVFDLKASLSR
CCCCCEEECCHHHCC
47.7129967540
360UbiquitinationNKKPVFDLKASLSRP
CCCCEEECCHHHCCC
3.2029967540
361UbiquitinationKKPVFDLKASLSRPL
CCCEEECCHHHCCCC
37.4629967540
363PhosphorylationPVFDLKASLSRPLNY
CEEECCHHHCCCCCC
25.8725159151
363UbiquitinationPVFDLKASLSRPLNY
CEEECCHHHCCCCCC
25.8729967540
365PhosphorylationFDLKASLSRPLNYEP
EECCHHHCCCCCCCC
29.3820068231
365UbiquitinationFDLKASLSRPLNYEP
EECCHHHCCCCCCCC
29.3824816145
369UbiquitinationASLSRPLNYEPHKGK
HHHCCCCCCCCCCCC
41.6329967540
370PhosphorylationSLSRPLNYEPHKGKL
HHCCCCCCCCCCCCC
38.2227080861
373UbiquitinationRPLNYEPHKGKLKPW
CCCCCCCCCCCCCCC
39.2924816145
374UbiquitinationPLNYEPHKGKLKPWG
CCCCCCCCCCCCCCC
69.3429967540
375UbiquitinationLNYEPHKGKLKPWGQ
CCCCCCCCCCCCCCC
37.1829967540
376AcetylationNYEPHKGKLKPWGQS
CCCCCCCCCCCCCCC
59.1325953088
376UbiquitinationNYEPHKGKLKPWGQS
CCCCCCCCCCCCCCC
59.1329967540
377UbiquitinationYEPHKGKLKPWGQSK
CCCCCCCCCCCCCCC
12.5729967540
378UbiquitinationEPHKGKLKPWGQSKE
CCCCCCCCCCCCCCC
42.0629967540
382UbiquitinationGKLKPWGQSKENNYL
CCCCCCCCCCCCCHH
47.6829967540
383UbiquitinationKLKPWGQSKENNYLN
CCCCCCCCCCCCHHH
37.6929967540
384MethylationLKPWGQSKENNYLNQ
CCCCCCCCCCCHHHH
57.48115974429
384UbiquitinationLKPWGQSKENNYLNQ
CCCCCCCCCCCHHHH
57.4829967540
388PhosphorylationGQSKENNYLNQHVNR
CCCCCCCHHHHHHHH
20.7227642862
388UbiquitinationGQSKENNYLNQHVNR
CCCCCCCHHHHHHHH
20.7224816145
389UbiquitinationQSKENNYLNQHVNRI
CCCCCCHHHHHHHHH
5.5929967540
394UbiquitinationNYLNQHVNRINFYKK
CHHHHHHHHHHHHHH
36.6724816145
395UbiquitinationYLNQHVNRINFYKKT
HHHHHHHHHHHHHHH
24.9224816145
396AcetylationLNQHVNRINFYKKTY
HHHHHHHHHHHHHHH
3.3619608861
402UbiquitinationRINFYKKTYKQPHLQ
HHHHHHHHHCCCCCC
31.6229967540
403UbiquitinationINFYKKTYKQPHLQT
HHHHHHHHCCCCCCC
19.2629967540
404AcetylationNFYKKTYKQPHLQTK
HHHHHHHCCCCCCCH
63.6925953088
404UbiquitinationNFYKKTYKQPHLQTK
HHHHHHHCCCCCCCH
63.6929967540
409AcetylationTYKQPHLQTKEEQRK
HHCCCCCCCHHHHHH
47.7119608861
410AcetylationYKQPHLQTKEEQRKK
HCCCCCCCHHHHHHH
46.9419608861
411AcetylationKQPHLQTKEEQRKKR
CCCCCCCHHHHHHHH
46.4219608861
412UbiquitinationQPHLQTKEEQRKKRE
CCCCCCHHHHHHHHH
63.8524816145
413UbiquitinationPHLQTKEEQRKKREQ
CCCCCHHHHHHHHHH
58.1924816145
419UbiquitinationEEQRKKREQERKEKK
HHHHHHHHHHHHHHH
66.7224816145
426UbiquitinationEQERKEKKAKVLGMR
HHHHHHHHHHHHHHH
55.3124816145
427UbiquitinationQERKEKKAKVLGMRR
HHHHHHHHHHHHHHC
20.4624816145
428UbiquitinationERKEKKAKVLGMRRG
HHHHHHHHHHHHHCC
47.0424816145
433UbiquitinationKAKVLGMRRGLILAE
HHHHHHHHCCEEEEC
27.9324816145
434UbiquitinationAKVLGMRRGLILAED
HHHHHHHCCEEEECC
35.0624816145

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
124SPhosphorylationKinaseATMQ13315
Uniprot
240SPhosphorylationKinaseAURKAO14965
GPS
240SPhosphorylationKinaseAURKBQ96GD4
GPS
300TPhosphorylationKinaseCDK1P06493
PSP
338TPhosphorylationKinaseCDK1P06493
PSP
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:17618083

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUSAP_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 NUSAP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
UBE4B_HUMANUBE4Bphysical
22863883
CEP70_HUMANCEP70physical
25416956
IMB1_HUMANKPNB1physical
26186194
IPO7_HUMANIPO7physical
26186194
G3PT_HUMANGAPDHSphysical
26186194
RBP2_HUMANRANBP2physical
26186194
CYTM_HUMANCST6physical
26186194
NU153_HUMANNUP153physical
26186194
S100P_HUMANS100Pphysical
26186194
CE030_HUMANC5orf30physical
26186194
GSTA2_HUMANGSTA2physical
26186194
CAF1A_HUMANCHAF1Aphysical
26344197
CE030_HUMANC5orf30physical
28514442
S100P_HUMANS100Pphysical
28514442
G3PT_HUMANGAPDHSphysical
28514442
GSTA2_HUMANGSTA2physical
28514442
RBP2_HUMANRANBP2physical
28514442
CYTM_HUMANCST6physical
28514442
NU153_HUMANNUP153physical
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 NUSAP_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-411, AND MASS SPECTROMETRY.
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 THR-349 AND SER-352, 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-135; THR-182; SER-240;THR-244; SER-247; THR-314; THR-349 AND SER-352, 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-240; THR-244 ANDSER-247, AND MASS SPECTROMETRY.
"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-135, 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-124, 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-135, AND MASSSPECTROMETRY.
"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-338, 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 THR-314, AND MASSSPECTROMETRY.

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