UBA6_HUMAN - dbPTM
UBA6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBA6_HUMAN
UniProt AC A0AVT1
Protein Name Ubiquitin-like modifier-activating enzyme 6
Gene Name UBA6
Organism Homo sapiens (Human).
Sequence Length 1052
Subcellular Localization
Protein Description Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Specific for ubiquitin, does not activate ubiquitin-like peptides. Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34. Essential for embryonic development. Required for UBD/FAT10 conjugation. Isoform 2 may play a key role in ubiquitin system and may influence spermatogenesis and male fertility..
Protein Sequence MEGSEPVAAHQGEEASCSSWGTGSTNKNLPIMSTASVEIDDALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNRAEAVLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVVLTEMKLPLQKKINDFCRSQCPPIKFISADVHGIWSRLFCDFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHKLETGQFLTFREINGMTGLNGSIQQITVISPFSFSIGDTTELEPYLHGGIAVQVKTPKTVFFESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLKLATSISETLEEKPDVNADIVHWLSWTAQGFLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLYLEAADIVESLGKPECEEFLPRGDRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTSKEKGMITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAHLNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHLTESYNSHRDPPEEEIPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNKFWQTYSSAEEVLQKIQSGHSLEGCFQVIKLLSRRPRNWSQCVELARLKFEKYFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPFAEEDLSADALLNILSEVKIQEFKPSNKVVQTDETARKPDHVPISSEDERNAIFQLEKAILSNEATKSDLQMAVLSFEKDDDHNGHIDFITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVTGGYPFEAYKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRWTVHGKEDFTLLDFINAVKEKYGIEPTMVVQGVKMLYVPVMPGHAKRLKLTMHKLVKPTTEKKYVDLTVSFAPDIDGDEDLPGPPVRYYFSHDTD
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-------MEGSEPVA
-------CCCCCCCC		51.8819413330
4Phosphorylation----MEGSEPVAAHQ
----CCCCCCCCCCC		41.8623186163
16PhosphorylationAHQGEEASCSSWGTG
CCCCCCCCCCCCCCC		20.1525159151
18PhosphorylationQGEEASCSSWGTGST
CCCCCCCCCCCCCCC		26.9923186163
19PhosphorylationGEEASCSSWGTGSTN
CCCCCCCCCCCCCCC		33.5823186163
22PhosphorylationASCSSWGTGSTNKNL
CCCCCCCCCCCCCCC		23.0023186163
24PhosphorylationCSSWGTGSTNKNLPI
CCCCCCCCCCCCCCE		28.7523186163
29 (in isoform 2)Ubiquitination-3.0421890473
33PhosphorylationNKNLPIMSTASVEID
CCCCCEEEEEEEEEC		22.8826657352
34PhosphorylationKNLPIMSTASVEIDD
CCCCEEEEEEEEECH		12.9321712546
36PhosphorylationLPIMSTASVEIDDAL
CCEEEEEEEEECHHH		21.9921712546
44PhosphorylationVEIDDALYSRQRYVL
EEECHHHHHCCCHHH		11.9728796482
45PhosphorylationEIDDALYSRQRYVLG
EECHHHHHCCCHHHC		23.8428796482
54PhosphorylationQRYVLGDTAMQKMAK
CCHHHCHHHHHHHHH		23.4128857561
56SulfoxidationYVLGDTAMQKMAKSH
HHHCHHHHHHHHHHC		4.2321406390
58UbiquitinationLGDTAMQKMAKSHVF
HCHHHHHHHHHHCEE		27.95-
61UbiquitinationTAMQKMAKSHVFLSG
HHHHHHHHHCEEHHC		37.28-
70 (in isoform 2)Ubiquitination-31.5321890473
86AcetylationNLVLAGIKAVTIHDT
HHHHCCCEEEEECCC		35.5725953088
95UbiquitinationVTIHDTEKCQAWDLG
EEECCCCCCCCCCCC		33.47-
115UbiquitinationSEDDVVNKRNRAEAV
CHHHHHCCCHHHHHH		39.17-
146PhosphorylationSVPFNETTDLSFLDK
CCCCCCCCCCHHHCC		28.85-
149PhosphorylationFNETTDLSFLDKYQC
CCCCCCCHHHCCCCE		26.94-
169UbiquitinationMKLPLQKKINDFCRS
CCCCHHHHHHHHHHH		33.51-
170 (in isoform 2)Ubiquitination-8.4521890473
178 (in isoform 2)Ubiquitination-4.5721890473
182UbiquitinationRSQCPPIKFISADVH
HHHCCCCEEEEECCC		42.28-
213 (in isoform 2)Ubiquitination-34.9721890473
238UbiquitinationCLENHPHKLETGQFL
EECCCCCCCCCCCEE		53.09-
241PhosphorylationNHPHKLETGQFLTFR
CCCCCCCCCCEEEEE		46.87-
246PhosphorylationLETGQFLTFREINGM
CCCCCEEEEEEECCC		23.18-
255 (in isoform 2)Ubiquitination-14.3021890473
265 (in isoform 2)Ubiquitination-4.3321890473
295UbiquitinationAVQVKTPKTVFFESL
EEEEECCCCCCHHHH		63.6521906983
295 (in isoform 1)Ubiquitination-63.6521890473
295 (in isoform 3)Ubiquitination-63.6521906983
295 (in isoform 4)Ubiquitination-63.6521906983
301PhosphorylationPKTVFFESLERQLKH
CCCCCHHHHHHHHCC		30.3023917254
310UbiquitinationERQLKHPKCLIVDFS
HHHHCCCCEEEEECC		41.20-
326 (in isoform 2)Ubiquitination-9.7421890473
342UbiquitinationFQEKYSRKPNVGCQQ
HHHHHCCCCCCCCCC		34.70-
356 (in isoform 2)Ubiquitination-49.0121890473
408 (in isoform 2)Ubiquitination-23.5521890473
415 (in isoform 2)Ubiquitination-40.6721890473
488UbiquitinationLLGVGTSKEKGMITV
EECCCCCCCCCCEEE		64.38-
490UbiquitinationGVGTSKEKGMITVTD
CCCCCCCCCCEEECC		58.47-
492SulfoxidationGTSKEKGMITVTDPD
CCCCCCCCEEECCHH		3.2521406390
503UbiquitinationTDPDLIEKSNLNRQF
CCHHHHHHCCCCCCC		37.3421906983
503 (in isoform 1)Ubiquitination-37.3421890473
521UbiquitinationPHHIQKPKSYTAADA
HHHCCCCCCEECCCC		64.23-
522PhosphorylationHHIQKPKSYTAADAT
HHCCCCCCEECCCCE		35.9230622161
524PhosphorylationIQKPKSYTAADATLK
CCCCCCEECCCCEEE		23.5930622161
529PhosphorylationSYTAADATLKINSQI
CEECCCCEEEECCEE		29.1825599653
531UbiquitinationTAADATLKINSQIKI
ECCCCEEEECCEEEE		35.17-
544AcetylationKIDAHLNKVCPTTET
EECEECCCCCCCCCC		52.1219608861
544UbiquitinationKIDAHLNKVCPTTET
EECEECCCCCCCCCC		52.1221890473
544MalonylationKIDAHLNKVCPTTET
EECEECCCCCCCCCC		52.1226320211
544 (in isoform 1)Ubiquitination-52.1221890473
558PhosphorylationTIYNDEFYTKQDVII
CCCCCCCCCCCCEEE		15.8127642862
560UbiquitinationYNDEFYTKQDVIITA
CCCCCCCCCCEEEEE		32.87-
597UbiquitinationDSGTMGTKGHTEVIV
HCCCCCCCCCCEEEC		42.86-
628UbiquitinationEIPFCTLKSFPAAIE
HCCCCEECCHHHHHH		31.7120639865
629PhosphorylationIPFCTLKSFPAAIEH
CCCCEECCHHHHHHH		39.3128857561
637PhosphorylationFPAAIEHTIQWARDK
HHHHHHHHHHHHHHH		11.3220068231
644UbiquitinationTIQWARDKFESSFSH
HHHHHHHHHHHHHCC		45.5421890473
644 (in isoform 1)Ubiquitination-45.5421890473
647PhosphorylationWARDKFESSFSHKPS
HHHHHHHHHHCCCHH		39.5526270265
648PhosphorylationARDKFESSFSHKPSL
HHHHHHHHHCCCHHH		24.4626270265
650PhosphorylationDKFESSFSHKPSLFN
HHHHHHHCCCHHHHH		32.3326270265
652UbiquitinationFESSFSHKPSLFNKF
HHHHHCCCHHHHHHH		34.7921890473
652 (in isoform 1)Ubiquitination-34.7921890473
654PhosphorylationSSFSHKPSLFNKFWQ
HHHCCCHHHHHHHHH		50.8526270265
662PhosphorylationLFNKFWQTYSSAEEV
HHHHHHHHCCCHHHH		18.9028857561
664PhosphorylationNKFWQTYSSAEEVLQ
HHHHHHCCCHHHHHH		26.8528857561
665PhosphorylationKFWQTYSSAEEVLQK
HHHHHCCCHHHHHHH		29.3228857561
672UbiquitinationSAEEVLQKIQSGHSL
CHHHHHHHHHCCCCH		38.25-
675PhosphorylationEVLQKIQSGHSLEGC
HHHHHHHCCCCHHHH		41.7830622161
678PhosphorylationQKIQSGHSLEGCFQV
HHHHCCCCHHHHHHH		31.4830622161
687UbiquitinationEGCFQVIKLLSRRPR
HHHHHHHHHHHCCCC		44.5121890473
687 (in isoform 1)Ubiquitination-44.5121890473
697PhosphorylationSRRPRNWSQCVELAR
HCCCCCHHHHHHHHH		19.7628857561
709UbiquitinationLARLKFEKYFNHKAL
HHHHHHHHHHCHHHH		59.27-
714UbiquitinationFEKYFNHKALQLLHC
HHHHHCHHHHHHHHC		52.47-
729AcetylationFPLDIRLKDGSLFWQ
EECEEEECCCCEEEC		50.63-
729UbiquitinationFPLDIRLKDGSLFWQ
EECEEEECCCCEEEC		50.6321890473
729 (in isoform 1)Ubiquitination-50.6321890473
732PhosphorylationDIRLKDGSLFWQSPK
EEEECCCCEEECCCC		30.4428857561
737PhosphorylationDGSLFWQSPKRPPSP
CCCEEECCCCCCCCC		24.0025159151
739UbiquitinationSLFWQSPKRPPSPIK
CEEECCCCCCCCCCC		80.7921890473
739 (in isoform 1)Ubiquitination-80.7921890473
743PhosphorylationQSPKRPPSPIKFDLN
CCCCCCCCCCCCCCC		41.7729255136
746UbiquitinationKRPPSPIKFDLNEPL
CCCCCCCCCCCCCCH		35.89-
756PhosphorylationLNEPLHLSFLQNAAK
CCCCHHHHHHHHHHH		17.1123898821
796UbiquitinationEVKIQEFKPSNKVVQ
HCCCEECCCCCCEEC		46.94-
800UbiquitinationQEFKPSNKVVQTDET
EECCCCCCEECCCCC		48.3921890473
800 (in isoform 1)Ubiquitination-48.3921890473
810UbiquitinationQTDETARKPDHVPIS
CCCCCCCCCCCCCCC		52.94-
817PhosphorylationKPDHVPISSEDERNA
CCCCCCCCCHHHHHH		22.9320068231
818PhosphorylationPDHVPISSEDERNAI
CCCCCCCCHHHHHHH		50.1928985074
830UbiquitinationNAIFQLEKAILSNEA
HHHHHHHHHHHCCCC		49.6821890473
830 (in isoform 1)Ubiquitination-49.6821890473
839UbiquitinationILSNEATKSDLQMAV
HHCCCCCHHHHHHHE		49.36-
871UbiquitinationAASNLRAKMYSIEPA
EHHHHHHHHCCCCCH		31.75-
874PhosphorylationNLRAKMYSIEPADRF
HHHHHHCCCCCHHHH		19.5828857561
882UbiquitinationIEPADRFKTKRIAGK
CCCHHHHCCHHHCCC		54.7721890473
882 (in isoform 1)Ubiquitination-54.7721890473
889UbiquitinationKTKRIAGKIIPAIAT
CCHHHCCCHHCCHHC		28.5721890473
889 (in isoform 1)Ubiquitination-28.5721890473
951PhosphorylationTKIRNGISFTIWDRW
CCCCCCCCEEEEECC		20.1028857561
953PhosphorylationIRNGISFTIWDRWTV
CCCCCCEEEEECCEE		17.8629523821
976UbiquitinationLDFINAVKEKYGIEP
HHHHHHHHHHHCCCC		46.18-
978UbiquitinationFINAVKEKYGIEPTM
HHHHHHHHHCCCCCE		42.96-
979PhosphorylationINAVKEKYGIEPTMV
HHHHHHHHCCCCCEE		25.1620068231
984PhosphorylationEKYGIEPTMVVQGVK
HHHCCCCCEEEEEEE		15.1421406692
994PhosphorylationVQGVKMLYVPVMPGH
EEEEEEEEEECCCCC		10.14-
1003AcetylationPVMPGHAKRLKLTMH
ECCCCCHHHHEEEEE		53.2225953088
1003UbiquitinationPVMPGHAKRLKLTMH
ECCCCCHHHHEEEEE		53.22-
1003MalonylationPVMPGHAKRLKLTMH
ECCCCCHHHHEEEEE		53.2226320211
1006AcetylationPGHAKRLKLTMHKLV
CCCHHHHEEEEEECC		46.0425953088
1011UbiquitinationRLKLTMHKLVKPTTE
HHEEEEEECCCCCCC		44.12-
1014AcetylationLTMHKLVKPTTEKKY
EEEEECCCCCCCCCE		47.2726210075
1016PhosphorylationMHKLVKPTTEKKYVD
EEECCCCCCCCCEEE		41.7020068231
1017PhosphorylationHKLVKPTTEKKYVDL
EECCCCCCCCCEEEE		55.1020068231
1046PhosphorylationPGPPVRYYFSHDTD-
CCCCEEEEECCCCC-		6.5027642862
1051PhosphorylationRYYFSHDTD------
EEEECCCCC------		37.8822617229
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 UBA6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBA6_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 UBA6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2D2_HUMANUBE2D2physical
17580310
UBC_HUMANUBCphysical
22427669
UBD_HUMANUBDphysical
22427669
UBE2Z_HUMANUBE2Zphysical
22427669
UBE2Z_HUMANUBE2Zphysical
20975683
UBC_HUMANUBCphysical
23003343
UCHL3_HUMANUCHL3physical
22939629
VIGLN_HUMANHDLBPphysical
22939629
UBP48_HUMANUSP48physical
22939629
VP26B_HUMANVPS26Bphysical
22939629
UBE4B_HUMANUBE4Bphysical
22939629
PYRG1_HUMANCTPS1physical
22863883
FKBP9_HUMANFKBP9physical
22863883
H2AV_HUMANH2AFVphysical
22863883
HEXA_HUMANHEXAphysical
22863883
LIMD1_HUMANLIMD1physical
22863883
NOL3_HUMANNOL3physical
22863883
OGFD1_HUMANOGFOD1physical
22863883
OXSR1_HUMANOXSR1physical
22863883
PDC6I_HUMANPDCD6IPphysical
22863883
PGTB1_HUMANPGGT1Bphysical
22863883
TWF2_HUMANTWF2physical
22863883
UBE2S_HUMANUBE2Sphysical
17597759
UB2D1_HUMANUBE2D1physical
17597759
UB2D2_HUMANUBE2D2physical
17597759
UB2D3_HUMANUBE2D3physical
17597759
UBE2T_HUMANUBE2Tphysical
17597759
UBE2Z_HUMANUBE2Zphysical
17597759
UB2L3_HUMANUBE2L3physical
17597759
UB2G2_HUMANUBE2G2physical
17597759
HMBX1_HUMANHMBOX1physical
25416956
UBC2_YEASTRAD6physical
19250909
UB2D2_HUMANUBE2D2physical
19250909
UB2L3_HUMANUBE2L3physical
19250909
UB2L6_HUMANUBE2L6physical
19250909
UBE2Z_HUMANUBE2Zphysical
19250909
UBE2Z_HUMANUBE2Zphysical
24528925
ATG7_HUMANATG7physical
26344197
CA123_HUMANC1orf123physical
26344197
CLU_HUMANCLUHphysical
26344197
PYRG1_HUMANCTPS1physical
26344197
DIAP1_HUMANDIAPH1physical
26344197
DYLT1_HUMANDYNLT1physical
26344197
ENOPH_HUMANENOPH1physical
26344197
VIGLN_HUMANHDLBPphysical
26344197
IMDH2_HUMANIMPDH2physical
26344197
MTRR_HUMANMTRRphysical
26344197
NU188_HUMANNUP188physical
26344197
NUP93_HUMANNUP93physical
26344197
PFKAP_HUMANPFKPphysical
26344197
SPSY_HUMANSMSphysical
26344197
SNF8_HUMANSNF8physical
26344197
UCHL3_HUMANUCHL3physical
26344197
UBP48_HUMANUSP48physical
26344197
FMR1_HUMANFMR1physical
26496610
FXR1_HUMANFXR1physical
26496610
IF4A3_HUMANEIF4A3physical
26496610
UB2D2_HUMANUBE2D2physical
28134249
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 UBA6_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, 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-544, AND MASS SPECTROMETRY.

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