ULA1_HUMAN - dbPTM
ULA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ULA1_HUMAN
UniProt AC Q13564
Protein Name NEDD8-activating enzyme E1 regulatory subunit
Gene Name NAE1
Organism Homo sapiens (Human).
Sequence Length 534
Subcellular Localization Cell membrane . Colocalizes with APP in lipid rafts.
Protein Description Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation..
Protein Sequence MAQLGKLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILKNENGAPEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL
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------MAQLGKLLK
------CHHHHHHHH
17.1922814378
6Acetylation--MAQLGKLLKEQKY
--CHHHHHHHHHCCC
60.2719608861
6Ubiquitination--MAQLGKLLKEQKY
--CHHHHHHHHHCCC
60.2723000965
6Acetylation--MAQLGKLLKEQKY
--CHHHHHHHHHCCC
60.27-
6Ubiquitination--MAQLGKLLKEQKY
--CHHHHHHHHHCCC
60.27-
7 (in isoform 2)Ubiquitination-8.62-
9UbiquitinationAQLGKLLKEQKYDRQ
HHHHHHHHHCCCHHH
69.4123000965
9UbiquitinationAQLGKLLKEQKYDRQ
HHHHHHHHHCCCHHH
69.41-
12UbiquitinationGKLLKEQKYDRQLRL
HHHHHHCCCHHHHHC
50.6523000965
12UbiquitinationGKLLKEQKYDRQLRL
HHHHHHCCCHHHHHC
50.65-
13PhosphorylationKLLKEQKYDRQLRLW
HHHHHCCCHHHHHCC
18.95-
78UbiquitinationGNNFFLQRSSIGKNR
CCCCEEEHHHCCCCH
34.2221890473
78UbiquitinationGNNFFLQRSSIGKNR
CCCCEEEHHHCCCCH
34.2221890473
98UbiquitinationEFLQELNSDVSGSFV
HHHHHHCCCCCCCCC
52.6021890473
98UbiquitinationEFLQELNSDVSGSFV
HHHHHHCCCCCCCCC
52.6021890473
117UbiquitinationENLLDNDPSFFCRFT
CCCCCCCCCCCCEEE
39.0133845483
118UbiquitinationNLLDNDPSFFCRFTV
CCCCCCCCCCCEEEE
33.5433845483
124PhosphorylationPSFFCRFTVVVATQL
CCCCCEEEEEEEECC
7.9521406692
129PhosphorylationRFTVVVATQLPESTS
EEEEEEEECCCCCCC
21.0121406692
134PhosphorylationVATQLPESTSLRLAD
EEECCCCCCCHHHHH
22.7421406692
135PhosphorylationATQLPESTSLRLADV
EECCCCCCCHHHHHH
30.0721406692
136PhosphorylationTQLPESTSLRLADVL
ECCCCCCCHHHHHHH
22.2921406692
151UbiquitinationWNSQIPLLICRTYGL
HHCCCCHHHHHHHCH
2.6629967540
161UbiquitinationRTYGLVGYMRIIIKE
HHHCHHHEEEEEECC
3.9221890473
161 (in isoform 2)Ubiquitination-3.92-
161UbiquitinationRTYGLVGYMRIIIKE
HHHCHHHEEEEEECC
3.9221890473
164UbiquitinationGLVGYMRIIIKEHPV
CHHHEEEEEECCCCC
1.8623000965
164NeddylationGLVGYMRIIIKEHPV
CHHHEEEEEECCCCC
1.8632015554
164UbiquitinationGLVGYMRIIIKEHPV
CHHHEEEEEECCCCC
1.8621890473
167UbiquitinationGYMRIIIKEHPVIES
HEEEEEECCCCCCCC
39.2921906983
170UbiquitinationRIIIKEHPVIESHPD
EEEECCCCCCCCCCC
29.8521890473
170UbiquitinationRIIIKEHPVIESHPD
EEEECCCCCCCCCCC
29.8521890473
181UbiquitinationSHPDNALEDLRLDKP
CCCCCHHHHHCCCCC
53.2223000965
181NeddylationSHPDNALEDLRLDKP
CCCCCHHHHHCCCCC
53.2232015554
181 (in isoform 2)Ubiquitination-53.22-
181UbiquitinationSHPDNALEDLRLDKP
CCCCCHHHHHCCCCC
53.2221890473
187UbiquitinationLEDLRLDKPFPELRE
HHHHCCCCCCHHHHH
53.8223000965
190UbiquitinationLRLDKPFPELREHFQ
HCCCCCCHHHHHHHH
48.5221890473
190UbiquitinationLRLDKPFPELREHFQ
HCCCCCCHHHHHHHH
48.5221890473
200UbiquitinationREHFQSYDLDHMEKK
HHHHHHCCCHHHHHC
51.3633845483
200 (in isoform 2)Ubiquitination-51.36-
201UbiquitinationEHFQSYDLDHMEKKD
HHHHHCCCHHHHHCC
3.5633845483
201 (in isoform 2)Ubiquitination-3.56-
204SulfoxidationQSYDLDHMEKKDHSH
HHCCCHHHHHCCCCC
8.9030846556
206UbiquitinationYDLDHMEKKDHSHTP
CCCHHHHHCCCCCCC
56.7933845483
207UbiquitinationDLDHMEKKDHSHTPW
CCHHHHHCCCCCCCH
47.5733845483
209UbiquitinationDHMEKKDHSHTPWIV
HHHHHCCCCCCCHHH
30.2933845483
209UbiquitinationDHMEKKDHSHTPWIV
HHHHHCCCCCCCHHH
30.29-
210UbiquitinationHMEKKDHSHTPWIVI
HHHHCCCCCCCHHHH
38.9121963094
210UbiquitinationHMEKKDHSHTPWIVI
HHHHCCCCCCCHHHH
38.91-
210UbiquitinationHMEKKDHSHTPWIVI
HHHHCCCCCCCHHHH
38.9121890473
223UbiquitinationVIIAKYLAQWYSETN
HHHHHHHHHHHHHHC
8.5123000965
223UbiquitinationVIIAKYLAQWYSETN
HHHHHHHHHHHHHHC
8.5121890473
226PhosphorylationAKYLAQWYSETNGRI
HHHHHHHHHHHCCCC
5.6418083107
228UbiquitinationYLAQWYSETNGRIPK
HHHHHHHHHCCCCCC
30.5123000965
228UbiquitinationYLAQWYSETNGRIPK
HHHHHHHHHCCCCCC
30.5121890473
229 (in isoform 2)Ubiquitination-36.71-
232 (in isoform 2)Ubiquitination-44.07-
234UbiquitinationSETNGRIPKTYKEKE
HHHCCCCCCCHHCHH
22.9029967540
234 (in isoform 2)Ubiquitination-22.90-
237PhosphorylationNGRIPKTYKEKEDFR
CCCCCCCHHCHHHHH
24.2318083107
238UbiquitinationGRIPKTYKEKEDFRD
CCCCCCHHCHHHHHH
68.49-
238UbiquitinationGRIPKTYKEKEDFRD
CCCCCCHHCHHHHHH
68.49-
240UbiquitinationIPKTYKEKEDFRDLI
CCCCHHCHHHHHHHH
59.4329967540
241UbiquitinationPKTYKEKEDFRDLIR
CCCHHCHHHHHHHHH
64.57-
243UbiquitinationTYKEKEDFRDLIRQG
CHHCHHHHHHHHHHH
7.4029967540
243UbiquitinationTYKEKEDFRDLIRQG
CHHCHHHHHHHHHHH
7.40-
247UbiquitinationKEDFRDLIRQGILKN
HHHHHHHHHHHHHHC
3.4623000965
247NeddylationKEDFRDLIRQGILKN
HHHHHHHHHHHHHHC
3.4632015554
247 (in isoform 2)Ubiquitination-3.46-
249UbiquitinationDFRDLIRQGILKNEN
HHHHHHHHHHHHCCC
35.9623000965
249UbiquitinationDFRDLIRQGILKNEN
HHHHHHHHHHHHCCC
35.9621890473
252UbiquitinationDLIRQGILKNENGAP
HHHHHHHHHCCCCCC
6.6123000965
252UbiquitinationDLIRQGILKNENGAP
HHHHHHHHHCCCCCC
6.6121890473
253UbiquitinationLIRQGILKNENGAPE
HHHHHHHHCCCCCCC
61.3623000965
253SumoylationLIRQGILKNENGAPE
HHHHHHHHCCCCCCC
61.36-
253NeddylationLIRQGILKNENGAPE
HHHHHHHHCCCCCCC
61.3632015554
256UbiquitinationQGILKNENGAPEDEE
HHHHHCCCCCCCCHH
62.4123000965
256NeddylationQGILKNENGAPEDEE
HHHHHCCCCCCCCHH
62.4132015554
256UbiquitinationQGILKNENGAPEDEE
HHHHHCCCCCCCCHH
62.41-
260UbiquitinationKNENGAPEDEENFEE
HCCCCCCCCHHHHHH
77.0029967540
263UbiquitinationNGAPEDEENFEEAIK
CCCCCCHHHHHHHHH
78.5133845483
264UbiquitinationGAPEDEENFEEAIKN
CCCCCHHHHHHHHHH
47.8132015554
264NeddylationGAPEDEENFEEAIKN
CCCCCHHHHHHHHHH
47.8132015554
270UbiquitinationENFEEAIKNVNTALN
HHHHHHHHHHHHHHH
62.9932015554
270NeddylationENFEEAIKNVNTALN
HHHHHHHHHHHHHHH
62.9932015554
273UbiquitinationEEAIKNVNTALNTTQ
HHHHHHHHHHHHCCC
29.0932015554
273NeddylationEEAIKNVNTALNTTQ
HHHHHHHHHHHHCCC
29.0932015554
274UbiquitinationEAIKNVNTALNTTQI
HHHHHHHHHHHCCCC
28.3923000965
274UbiquitinationEAIKNVNTALNTTQI
HHHHHHHHHHHCCCC
28.3921890473
283PhosphorylationLNTTQIPSSIEDIFN
HHCCCCCCCHHHHHC
45.6525693802
284PhosphorylationNTTQIPSSIEDIFND
HCCCCCCCHHHHHCC
25.3325693802
289UbiquitinationPSSIEDIFNDDRCIN
CCCHHHHHCCCCEEE
14.7021963094
289UbiquitinationPSSIEDIFNDDRCIN
CCCHHHHHCCCCEEE
14.7021890473
292UbiquitinationIEDIFNDDRCINITK
HHHHHCCCCEEECCC
48.7522817900
293UbiquitinationEDIFNDDRCINITKQ
HHHHCCCCEEECCCC
26.5321963094
293 (in isoform 2)Ubiquitination-26.53-
293UbiquitinationEDIFNDDRCINITKQ
HHHHCCCCEEECCCC
26.5321890473
294GlutathionylationDIFNDDRCINITKQT
HHHCCCCEEECCCCC
3.4322555962
299UbiquitinationDRCINITKQTPSFWI
CCEEECCCCCHHHHH
48.6721963094
302UbiquitinationINITKQTPSFWILAR
EECCCCCHHHHHHHH
25.6521963094
302UbiquitinationINITKQTPSFWILAR
EECCCCCHHHHHHHH
25.6521890473
306UbiquitinationKQTPSFWILARALKE
CCCHHHHHHHHHHHH
1.7123000965
306 (in isoform 2)Ubiquitination-1.71-
306UbiquitinationKQTPSFWILARALKE
CCCHHHHHHHHHHHH
1.7121890473
311UbiquitinationFWILARALKEFVAKE
HHHHHHHHHHHHHHH
4.5623000965
311 (in isoform 2)Ubiquitination-4.56-
311UbiquitinationFWILARALKEFVAKE
HHHHHHHHHHHHHHH
4.5621890473
312UbiquitinationWILARALKEFVAKEG
HHHHHHHHHHHHHHC
48.3923000965
315UbiquitinationARALKEFVAKEGQGN
HHHHHHHHHHHCCCC
8.5723000965
315UbiquitinationARALKEFVAKEGQGN
HHHHHHHHHHHCCCC
8.5721890473
317UbiquitinationALKEFVAKEGQGNLP
HHHHHHHHHCCCCCC
58.0123000965
320UbiquitinationEFVAKEGQGNLPVRG
HHHHHHCCCCCCCCC
38.4023000965
320UbiquitinationEFVAKEGQGNLPVRG
HHHHHHCCCCCCCCC
38.4021890473
332UbiquitinationVRGTIPDMIADSGKY
CCCCCCHHHHCCCCE
1.9823000965
332 (in isoform 2)Ubiquitination-1.98-
332UbiquitinationVRGTIPDMIADSGKY
CCCCCCHHHHCCCCE
1.9821890473
335UbiquitinationTIPDMIADSGKYIKL
CCCHHHHCCCCEEEE
47.1823000965
335 (in isoform 2)Ubiquitination-47.18-
335UbiquitinationTIPDMIADSGKYIKL
CCCHHHHCCCCEEEE
47.1821890473
336PhosphorylationIPDMIADSGKYIKLQ
CCHHHHCCCCEEEEH
28.3223532336
338AcetylationDMIADSGKYIKLQNV
HHHHCCCCEEEEHHH
47.9923954790
338UbiquitinationDMIADSGKYIKLQNV
HHHHCCCCEEEEHHH
47.9923000965
339PhosphorylationMIADSGKYIKLQNVY
HHHCCCCEEEEHHHH
13.55-
341AcetylationADSGKYIKLQNVYRE
HCCCCEEEEHHHHHH
40.7123954790
341UbiquitinationADSGKYIKLQNVYRE
HCCCCEEEEHHHHHH
40.7123000965
341AcetylationADSGKYIKLQNVYRE
HCCCCEEEEHHHHHH
40.71-
341UbiquitinationADSGKYIKLQNVYRE
HCCCCEEEEHHHHHH
40.7121890473
343UbiquitinationSGKYIKLQNVYREKA
CCCEEEEHHHHHHHH
32.1329967540
344UbiquitinationGKYIKLQNVYREKAK
CCEEEEHHHHHHHHH
43.1323000965
344AcetylationGKYIKLQNVYREKAK
CCEEEEHHHHHHHHH
43.13-
344UbiquitinationGKYIKLQNVYREKAK
CCEEEEHHHHHHHHH
43.1321890473
346PhosphorylationYIKLQNVYREKAKKD
EEEEHHHHHHHHHHH
22.17-
346UbiquitinationYIKLQNVYREKAKKD
EEEEHHHHHHHHHHH
22.1733845483
349UbiquitinationLQNVYREKAKKDAAA
EHHHHHHHHHHHHHH
57.4129967540
352UbiquitinationVYREKAKKDAAAVGN
HHHHHHHHHHHHHHH
58.4133845483
355UbiquitinationEKAKKDAAAVGNHVA
HHHHHHHHHHHHHHH
16.8933845483
357UbiquitinationAKKDAAAVGNHVAKL
HHHHHHHHHHHHHHH
7.2723000965
357 (in isoform 2)Ubiquitination-7.27-
357UbiquitinationAKKDAAAVGNHVAKL
HHHHHHHHHHHHHHH
7.2721890473
363UbiquitinationAVGNHVAKLLQSIGQ
HHHHHHHHHHHHHCC
48.9523000965
366UbiquitinationNHVAKLLQSIGQAPE
HHHHHHHHHHCCCCC
43.3623000965
366UbiquitinationNHVAKLLQSIGQAPE
HHHHHHHHHHCCCCC
43.3621890473
367UbiquitinationHVAKLLQSIGQAPES
HHHHHHHHHCCCCCC
28.7621963094
367UbiquitinationHVAKLLQSIGQAPES
HHHHHHHHHCCCCCC
28.7621890473
372UbiquitinationLQSIGQAPESISEKE
HHHHCCCCCCCCHHH
28.1621963094
372 (in isoform 2)Ubiquitination-28.16-
372UbiquitinationLQSIGQAPESISEKE
HHHHCCCCCCCCHHH
28.1621890473
374PhosphorylationSIGQAPESISEKELK
HHCCCCCCCCHHHHH
30.2920860994
375UbiquitinationIGQAPESISEKELKL
HCCCCCCCCHHHHHH
6.1722817900
375 (in isoform 2)Ubiquitination-6.17-
376PhosphorylationGQAPESISEKELKLL
CCCCCCCCHHHHHHH
52.4720860994
378AcetylationAPESISEKELKLLCS
CCCCCCHHHHHHHHC
62.6523954790
378UbiquitinationAPESISEKELKLLCS
CCCCCCHHHHHHHHC
62.6521906983
381UbiquitinationSISEKELKLLCSNSA
CCCHHHHHHHHCCCH
40.2721963094
381AcetylationSISEKELKLLCSNSA
CCCHHHHHHHHCCCH
40.27-
381UbiquitinationSISEKELKLLCSNSA
CCCHHHHHHHHCCCH
40.2721890473
381AcetylationSISEKELKLLCSNSA
CCCHHHHHHHHCCCH
40.2725953088
384UbiquitinationEKELKLLCSNSAFLR
HHHHHHHHCCCHHHH
5.4022817900
384UbiquitinationEKELKLLCSNSAFLR
HHHHHHHHCCCHHHH
5.40-
384GlutathionylationEKELKLLCSNSAFLR
HHHHHHHHCCCHHHH
5.4022555962
397PhosphorylationLRVVRCRSLAEEYGL
HHHHHHHHHHHHHCC
35.2419845377
406PhosphorylationAEEYGLDTINKDEII
HHHHCCCCCCHHHHH
31.3419845377
442PhosphorylationFHKQQGRYPGVSNYQ
HHHHCCCCCCCCCCC
15.9129396449
446PhosphorylationQGRYPGVSNYQVEED
CCCCCCCCCCCHHCH
35.4229396449
448PhosphorylationRYPGVSNYQVEEDIG
CCCCCCCCCHHCHHH
13.3629396449
450UbiquitinationPGVSNYQVEEDIGKL
CCCCCCCHHCHHHHH
6.4921963094
450 (in isoform 2)Ubiquitination-6.49-
456UbiquitinationQVEEDIGKLKSCLTG
CHHCHHHHHHHHHHH
53.7421906983
459UbiquitinationEDIGKLKSCLTGFLQ
CHHHHHHHHHHHHHH
25.4621963094
459UbiquitinationEDIGKLKSCLTGFLQ
CHHHHHHHHHHHHHH
25.46-
501 (in isoform 2)Ubiquitination-16.98-
507UbiquitinationAAAQEVIKIITKQFV
HHHHHHHHHHHCCEE
32.98-
510UbiquitinationQEVIKIITKQFVIFN
HHHHHHHHCCEEEEC
23.43-
522PhosphorylationIFNNTYIYSGMSQTS
EECCEEEEECCCCCE
6.6925022875

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
-KUbiquitinationE3 ubiquitin ligaseTRIP12Q14669
PMID:18627766

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ULA1_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 ULA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
8626687
UBA3_HUMANUBA3physical
10722740
UBA3_HUMANUBA3physical
18264111
NEDD8_HUMANNEDD8physical
18264111
UBA3_HUMANUBA3physical
17220875
NEDD8_HUMANNEDD8physical
17220875
UBC12_HUMANUBE2Mphysical
17220875
UBA3_HUMANUBA3physical
12646924
UBA3_HUMANUBA3physical
12740388
UBC12_HUMANUBE2Mphysical
18652489
UBA3_HUMANUBA3physical
9694792
SRBP2_HUMANSREBF2physical
21988832
APEX1_HUMANAPEX1physical
22863883
CAN2_HUMANCAPN2physical
22863883
DCPS_HUMANDCPSphysical
22863883
MCTS1_HUMANMCTS1physical
22863883
MOES_HUMANMSNphysical
22863883
NSF1C_HUMANNSFL1Cphysical
22863883
PAPS1_HUMANPAPSS1physical
22863883
PCY2_HUMANPCYT2physical
22863883
IPP2_HUMANPPP1R2physical
22863883
TRXR1_HUMANTXNRD1physical
22863883
XPO1_HUMANXPO1physical
22863883
UBA3_HUMANUBA3physical
15361859
UBC12_HUMANUBE2Mphysical
19250909
UBE2F_HUMANUBE2Fphysical
19250909
PLOD1_HUMANPLOD1physical
26344197
UBA3_HUMANUBA3physical
26344197
UBA5_HUMANUBA5physical
26344197
XRCC6_HUMANXRCC6physical
26344197

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
D10413 Pevonedistat (USAN)
DrugBank
DB00171Adenosine triphosphate
Regulatory Network of ULA1_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-6, AND MASS SPECTROMETRY.

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