UBA3_HUMAN - dbPTM
UBA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBA3_HUMAN
UniProt AC Q8TBC4
Protein Name NEDD8-activating enzyme E1 catalytic subunit
Gene Name UBA3
Organism Homo sapiens (Human).
Sequence Length 463
Subcellular Localization
Protein Description Catalytic 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. Down-regulates steroid receptor activity. Necessary for cell cycle progression..
Protein Sequence MADGEEPEKKRRRIEELLAEKMAVDGGCGDTGDWEGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEHCIEYVRMLQWPKEQPFGEGVPLDGDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNSASLQMKSPAITATLEGKNRTLYLQSVTSIEERTRPNLSKTLKELGLVDGQELAVADVTTPQTVLFKLHFTS
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------MADGEEPEK
------CCCCCCHHH		33.2522814378
9MethylationADGEEPEKKRRRIEE
CCCCCHHHHHHHHHH		63.4023748837
9UbiquitinationADGEEPEKKRRRIEE
CCCCCHHHHHHHHHH		63.4033845483
10MethylationDGEEPEKKRRRIEEL
CCCCHHHHHHHHHHH		49.8523748837
10UbiquitinationDGEEPEKKRRRIEEL
CCCCHHHHHHHHHHH		49.8524816145
21UbiquitinationIEELLAEKMAVDGGC
HHHHHHHHHCCCCCC		26.93-
21AcetylationIEELLAEKMAVDGGC
HHHHHHHHHCCCCCC		26.9326051181
57UbiquitinationPFTHPDFEPSTESLQ
CCCCCCCCCCHHHHH		45.8033845483
71UbiquitinationQFLLDTCKVLVIGAG
HHHHHHCCEEEECCC		40.4733845483
72UbiquitinationFLLDTCKVLVIGAGG
HHHHHCCEEEECCCH		5.8533845483
77UbiquitinationCKVLVIGAGGLGCEL
CCEEEECCCHHHHHH		9.5827667366
83UbiquitinationGAGGLGCELLKNLAL
CCCHHHHHHHHHHHH		56.1733845483
86UbiquitinationGLGCELLKNLALSGF
HHHHHHHHHHHHCCC		63.6421906983
91PhosphorylationLLKNLALSGFRQIHV
HHHHHHHCCCCEEEE		30.2223403867
91UbiquitinationLLKNLALSGFRQIHV
HHHHHHHCCCCEEEE		30.2227667366
101SulfoxidationRQIHVIDMDTIDVSN
CEEEEEECCCCCHHH		3.1730846556
103PhosphorylationIHVIDMDTIDVSNLN
EEEEECCCCCHHHCC		16.6721406692
104UbiquitinationHVIDMDTIDVSNLNR
EEEECCCCCHHHCCC		4.2527667366
106UbiquitinationIDMDTIDVSNLNRQF
EECCCCCHHHCCCEE		3.4523000965
107PhosphorylationDMDTIDVSNLNRQFL
ECCCCCHHHCCCEEC		31.6721406692
110UbiquitinationTIDVSNLNRQFLFRP
CCCHHHCCCEECCCH		39.7033845483
118UbiquitinationRQFLFRPKDIGRPKA
CEECCCHHHCCCCHH		58.6927667366
120UbiquitinationFLFRPKDIGRPKAEV
ECCCHHHCCCCHHHH		6.6923000965
124UbiquitinationPKDIGRPKAEVAAEF
HHHCCCCHHHHHHHH		56.6833845483
1242-HydroxyisobutyrylationPKDIGRPKAEVAAEF
HHHCCCCHHHHHHHH		56.68-
133UbiquitinationEVAAEFLNDRVPNCN
HHHHHHHHCCCCCCE		40.1223000965
133UbiquitinationEVAAEFLNDRVPNCN
HHHHHHHHCCCCCCE		40.1221890473
135MethylationAAEFLNDRVPNCNVV
HHHHHHCCCCCCEEC		44.73115919233
147UbiquitinationNVVPHFNKIQDFNDT
EECCCCCCCCCCCHH		40.5823000965
147SumoylationNVVPHFNKIQDFNDT
EECCCCCCCCCCCHH		40.58-
147UbiquitinationNVVPHFNKIQDFNDT
EECCCCCCCCCCCHH		40.5821890473
147AcetylationNVVPHFNKIQDFNDT
EECCCCCCCCCCCHH		40.5826051181
185PhosphorylationMLISLLNYEDGVLDP
HHHHHHCCCCCCCCH		18.50-
203PhosphorylationVPLIDGGTEGFKGNA
EEEECCCCCCCCCCE		38.16-
207UbiquitinationDGGTEGFKGNARVIL
CCCCCCCCCCEEEEC		63.21-
207SumoylationDGGTEGFKGNARVIL
CCCCCCCCCCEEEEC		63.21-
219UbiquitinationVILPGMTACIECTLE
EECCCCCEEEEEEHH		5.3822817900
233UbiquitinationELYPPQVNFPMCTIA
HHCCCCCCCCCCCHH		30.0122817900
243UbiquitinationMCTIASMPRLPEHCI
CCCHHCCCCCCHHHH		31.9621963094
246UbiquitinationIASMPRLPEHCIEYV
HHCCCCCCHHHHHHH		30.4822817900
246 (in isoform 2)Ubiquitination-30.48-
249GlutathionylationMPRLPEHCIEYVRML
CCCCCHHHHHHHHHH		2.1122555962
252PhosphorylationLPEHCIEYVRMLQWP
CCHHHHHHHHHHCCC		3.5628152594
257UbiquitinationIEYVRMLQWPKEQPF
HHHHHHHCCCCCCCC		45.1121963094
260UbiquitinationVRMLQWPKEQPFGEG
HHHHCCCCCCCCCCC		67.0521906983
266UbiquitinationPKEQPFGEGVPLDGD
CCCCCCCCCCCCCCC		58.3523000965
270UbiquitinationPFGEGVPLDGDDPEH
CCCCCCCCCCCCHHH		12.2021963094
270 (in isoform 2)Ubiquitination-12.20-
270UbiquitinationPFGEGVPLDGDDPEH
CCCCCCCCCCCCHHH		12.2021890473
280UbiquitinationDDPEHIQWIFQKSLE
CCHHHHHHHHHHHHH		7.8621890473
284UbiquitinationHIQWIFQKSLERASQ
HHHHHHHHHHHHHHH		46.3821963094
284SumoylationHIQWIFQKSLERASQ
HHHHHHHHHHHHHHH		46.38-
284UbiquitinationHIQWIFQKSLERASQ
HHHHHHHHHHHHHHH		46.3821890473
293UbiquitinationLERASQYNIRGVTYR
HHHHHHCCCCCHHEE		15.1623000965
293 (in isoform 2)Ubiquitination-15.16-
293UbiquitinationLERASQYNIRGVTYR
HHHHHHCCCCCHHEE		15.1621890473
295MethylationRASQYNIRGVTYRLT
HHHHCCCCCHHEEEC		29.86115919237
307UbiquitinationRLTQGVVKRIIPAVA
EECHHHHHHHHHHHH		35.1623000965
3072-HydroxyisobutyrylationRLTQGVVKRIIPAVA
EECHHHHHHHHHHHH		35.16-
307UbiquitinationRLTQGVVKRIIPAVA
EECHHHHHHHHHHHH		35.1621890473
307AcetylationRLTQGVVKRIIPAVA
EECHHHHHHHHHHHH		35.1625953088
320UbiquitinationVASTNAVIAAVCATE
HHCCHHHHHHHHHHH		1.5721963094
320NeddylationVASTNAVIAAVCATE
HHCCHHHHHHHHHHH		1.5732015554
334UbiquitinationEVFKIATSAYIPLNN
HHHHHHHHCEECCCC		15.2821890473
347UbiquitinationNNYLVFNDVDGLYTY
CCEEEEECCCCEEEE		28.5521963094
347NeddylationNNYLVFNDVDGLYTY
CCEEEEECCCCEEEE		28.5532015554
347UbiquitinationNNYLVFNDVDGLYTY
CCEEEEECCCCEEEE		28.5521890473
357UbiquitinationGLYTYTFEAERKENC
CEEEEEEEHHHHCCC		41.6521963094
357NeddylationGLYTYTFEAERKENC
CEEEEEEEHHHHCCC		41.6532015554
361UbiquitinationYTFEAERKENCPACS
EEEEHHHHCCCCCCC		44.7921906983
361NeddylationYTFEAERKENCPACS
EEEEHHHHCCCCCCC		44.7932015554
361UbiquitinationYTFEAERKENCPACS
EEEEHHHHCCCCCCC		44.7921890473
368UbiquitinationKENCPACSQLPQNIQ
HCCCCCCCCCCCCCC		36.5423000965
368PhosphorylationKENCPACSQLPQNIQ
HCCCCCCCCCCCCCC		36.5427251275
371UbiquitinationCPACSQLPQNIQFSP
CCCCCCCCCCCCCCC		19.9621963094
377PhosphorylationLPQNIQFSPSAKLQE
CCCCCCCCCCHHHHH		11.1125159151
379PhosphorylationQNIQFSPSAKLQEVL
CCCCCCCCHHHHHHH		36.5228450419
382UbiquitinationQFSPSAKLQEVLDYL
CCCCCHHHHHHHHHH		5.4023000965
384UbiquitinationSPSAKLQEVLDYLTN
CCCHHHHHHHHHHHC		56.3221963094
384NeddylationSPSAKLQEVLDYLTN
CCCHHHHHHHHHHHC		56.3232015554
384 (in isoform 2)Ubiquitination-56.32-
388PhosphorylationKLQEVLDYLTNSASL
HHHHHHHHHHCCCCC		15.9728851738
390PhosphorylationQEVLDYLTNSASLQM
HHHHHHHHCCCCCCC		22.3918212344
390UbiquitinationQEVLDYLTNSASLQM
HHHHHHHHCCCCCCC		22.3922817900
392PhosphorylationVLDYLTNSASLQMKS
HHHHHHCCCCCCCCC		17.63-
393UbiquitinationLDYLTNSASLQMKSP
HHHHHCCCCCCCCCC		19.1422817900
394PhosphorylationDYLTNSASLQMKSPA
HHHHCCCCCCCCCCC		20.9628851738
395UbiquitinationYLTNSASLQMKSPAI
HHHCCCCCCCCCCCE		6.0423000965
395 (in isoform 2)Ubiquitination-6.04-
398UbiquitinationNSASLQMKSPAITAT
CCCCCCCCCCCEEEE		40.0821906983
398NeddylationNSASLQMKSPAITAT
CCCCCCCCCCCEEEE		40.0832015554
399PhosphorylationSASLQMKSPAITATL
CCCCCCCCCCEEEEE		17.7729255136
403PhosphorylationQMKSPAITATLEGKN
CCCCCCEEEEEECCC		18.7227251275
404UbiquitinationMKSPAITATLEGKNR
CCCCCEEEEEECCCC		12.2222817900
407UbiquitinationPAITATLEGKNRTLY
CCEEEEEECCCCEEE		64.8622817900
409AcetylationITATLEGKNRTLYLQ
EEEEEECCCCEEEEE		33.6023954790
409UbiquitinationITATLEGKNRTLYLQ
EEEEEECCCCEEEEE		33.6023000965
4092-HydroxyisobutyrylationITATLEGKNRTLYLQ
EEEEEECCCCEEEEE		33.60-
409MalonylationITATLEGKNRTLYLQ
EEEEEECCCCEEEEE		33.6026320211
414PhosphorylationEGKNRTLYLQSVTSI
ECCCCEEEEEECCCH		11.3329759185
417UbiquitinationNRTLYLQSVTSIEER
CCEEEEEECCCHHHH		25.4333845483
417PhosphorylationNRTLYLQSVTSIEER
CCEEEEEECCCHHHH		25.4328450419
419PhosphorylationTLYLQSVTSIEERTR
EEEEEECCCHHHHHC		29.2728450419
420PhosphorylationLYLQSVTSIEERTRP
EEEEECCCHHHHHCC		26.3328450419
420UbiquitinationLYLQSVTSIEERTRP
EEEEECCCHHHHHCC		26.3322817900
430PhosphorylationERTRPNLSKTLKELG
HHHCCCHHHHHHHCC		30.1828188228
431UbiquitinationRTRPNLSKTLKELGL
HHCCCHHHHHHHCCC		62.1322817900
434UbiquitinationPNLSKTLKELGLVDG
CCHHHHHHHCCCCCC		57.0021906983
444UbiquitinationGLVDGQELAVADVTT
CCCCCEEEEEEECCC		3.4133845483
458UbiquitinationTPQTVLFKLHFTS--
CCCEEEEEEEECC--		36.5733845483
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 UBA3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBA3_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 UBA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD3_HUMANCHD3physical
16169070
ULA1_HUMANNAE1physical
10722740
UBC12_HUMANUBE2Mphysical
15361859
UBC12_HUMANUBE2Mphysical
18652489
ULA1_HUMANNAE1physical
22939629
UFC1_HUMANUFC1physical
22939629
WDR61_HUMANWDR61physical
22939629
UBE2H_HUMANUBE2Hphysical
22939629
VINC_HUMANVCLphysical
22939629
KDM1A_HUMANKDM1Aphysical
23455924
THIC_HUMANACAT2physical
22863883
SAHH_HUMANAHCYphysical
22863883
CAN2_HUMANCAPN2physical
22863883
DCPS_HUMANDCPSphysical
22863883
ULA1_HUMANNAE1physical
22863883
NSF1C_HUMANNSFL1Cphysical
22863883
PAPS1_HUMANPAPSS1physical
22863883
PCY2_HUMANPCYT2physical
22863883
XPO1_HUMANXPO1physical
22863883
UBA3_HUMANUBA3physical
25416956
CPNE2_HUMANCPNE2physical
25416956
UBC12_HUMANUBE2Mphysical
19250909
UBE2F_HUMANUBE2Fphysical
19250909
UBA3_HUMANUBA3physical
10207026
UBC12_HUMANUBE2Mphysical
10207026
ULA1_HUMANNAE1physical
10207026
ATG7_HUMANATG7physical
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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBA3_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory