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Overview

Uniprot IDA0AVT1
Protein NameUbiquitin-like modifier-activating enzyme 6
Gene NameUBA6
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
169 MKLPLQKKINDFCRS
729 FPLDIRLKDGSLFWQ
78 GLGLEIAKNLVLAGI

Function

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 (PubMed:35970836, PubMed:35986001). Specific for ubiquitin, does not activate ubiquitin-like peptides. Also activates UBD/FAT10 conjugation via adenylation of its C-terminal glycine (PubMed:17889673, PubMed:35970836, PubMed:35986001). Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34. Essential for embryonic development. Isoform 2 may play a key role in ubiquitin system and may influence spermatogenesis and male fertility

Protein Sequence

10 MEGSEPVAAH 20 QGEEASCSSW 30 GTGSTNKNLP 40 IMSTASVEID 50 DALYSRQRYV 60 LGDTAMQKMA 70 KSHVFLSGMG 80 GLGLEIAKNL 90 VLAGIKAVTI 100 HDTEKCQAWD 110 LGTNFFLSED 120 DVVNKRNRAE 130 AVLKHIAELN 140 PYVHVTSSSV 150 PFNETTDLSF 160 LDKYQCVVLT 170 EMKLPLQKKI 180 NDFCRSQCPP 190 IKFISADVHG 200 IWSRLFCDFG 210 DEFEVLDTTG 220 EEPKEIFISN 230 ITQANPGIVT 240 CLENHPHKLE 250 TGQFLTFREI 260 NGMTGLNGSI 270 QQITVISPFS 280 FSIGDTTELE 290 PYLHGGIAVQ 300 VKTPKTVFFE 310 SLERQLKHPK 320 CLIVDFSNPE 330 APLEIHTAML 340 ALDQFQEKYS 350 RKPNVGCQQD 360 SEELLKLATS 370 ISETLEEKPD 380 VNADIVHWLS 390 WTAQGFLSPL 400 AAAVGGVASQ 410 EVLKAVTGKF 420 SPLCQWLYLE 430 AADIVESLGK 440 PECEEFLPRG 450 DRYDALRACI 460 GDTLCQKLQN 470 LNIFLVGCGA 480 IGCEMLKNFA 490 LLGVGTSKEK 500 GMITVTDPDL 510 IEKSNLNRQF 520 LFRPHHIQKP 530 KSYTAADATL 540 KINSQIKIDA 550 HLNKVCPTTE 560 TIYNDEFYTK 570 QDVIITALDN 580 VEARRYVDSR 590 CLANLRPLLD 600 SGTMGTKGHT 610 EVIVPHLTES 620 YNSHRDPPEE 630 EIPFCTLKSF 640 PAAIEHTIQW 650 ARDKFESSFS 660 HKPSLFNKFW 670 QTYSSAEEVL 680 QKIQSGHSLE 690 GCFQVIKLLS 700 RRPRNWSQCV 710 ELARLKFEKY 720 FNHKALQLLH 730 CFPLDIRLKD 740 GSLFWQSPKR 750 PPSPIKFDLN 760 EPLHLSFLQN 770 AAKLYATVYC 780 IPFAEEDLSA 790 DALLNILSEV 800 KIQEFKPSNK 810 VVQTDETARK 820 PDHVPISSED 830 ERNAIFQLEK 840 AILSNEATKS 850 DLQMAVLSFE 860 KDDDHNGHID 870 FITAASNLRA 880 KMYSIEPADR 890 FKTKRIAGKI 900 IPAIATTTAT 910 VSGLVALEMI 920 KVTGGYPFEA 930 YKNCFLNLAI 940 PIVVFTETTE 950 VRKTKIRNGI 960 SFTIWDRWTV 970 HGKEDFTLLD 980 FINAVKEKYG 990 IEPTMVVQGV 1000 KMLYVPVMPG 1010 HAKRLKLTMH 1020 KLVKPTTEKK 1030 YVDLTVSFAP 1040 DIDGDEDLPG 1050 PPVRYYFSHD TD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0019780 FAT10 activating enzyme activity
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0004839 ubiquitin activating enzyme activity
Biological Process GO:0006974 DNA damage response
Biological Process GO:0016567 protein ubiquitination
Biological Process GO:0006511 ubiquitin-dependent protein catabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.