Search Results

Overview

Uniprot IDP22314
Protein NameUbiquitin-like modifier-activating enzyme 1
Gene NameUBA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
296 GGIVSQVKVPKKISF
528 PWDVTKLKSDTAAAA
593 RRCVYYRKPLLESGT
68 VLGHEAMKRLQTSSV
8 MSSSPLSKKRRVSGP
838 ATLPSPDKLPGFKMY
884 SADRHKSKLIAGKII

Function

Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system (PubMed:1447181, PubMed:1606621, PubMed:33108101). 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:1447181). Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites (PubMed:22456334)

Protein Sequence

10 MSSSPLSKKR 20 RVSGPDPKPG 30 SNCSPAQSVL 40 SEVPSVPTNG 50 MAKNGSEADI 60 DEGLYSRQLY 70 VLGHEAMKRL 80 QTSSVLVSGL 90 RGLGVEIAKN 100 IILGGVKAVT 110 LHDQGTAQWA 120 DLSSQFYLRE 130 EDIGKNRAEV 140 SQPRLAELNS 150 YVPVTAYTGP 160 LVEDFLSGFQ 170 VVVLTNTPLE 180 DQLRVGEFCH 190 NRGIKLVVAD 200 TRGLFGQLFC 210 DFGEEMILTD 220 SNGEQPLSAM 230 VSMVTKDNPG 240 VVTCLDEARH 250 GFESGDFVSF 260 SEVQGMVELN 270 GNQPMEIKVL 280 GPYTFSICDT 290 SNFSDYIRGG 300 IVSQVKVPKK 310 ISFKSLVASL 320 AEPDFVVTDF 330 AKFSRPAQLH 340 IGFQALHQFC 350 AQHGRPPRPR 360 NEEDAAELVA 370 LAQAVNARAL 380 PAVQQNNLDE 390 DLIRKLAYVA 400 AGDLAPINAF 410 IGGLAAQEVM 420 KACSGKFMPI 430 MQWLYFDALE 440 CLPEDKEVLT 450 EDKCLQRQNR 460 YDGQVAVFGS 470 DLQEKLGKQK 480 YFLVGAGAIG 490 CELLKNFAMI 500 GLGCGEGGEI 510 IVTDMDTIEK 520 SNLNRQFLFR 530 PWDVTKLKSD 540 TAAAAVRQMN 550 PHIRVTSHQN 560 RVGPDTERIY 570 DDDFFQNLDG 580 VANALDNVDA 590 RMYMDRRCVY 600 YRKPLLESGT 610 LGTKGNVQVV 620 IPFLTESYSS 630 SQDPPEKSIP 640 ICTLKNFPNA 650 IEHTLQWARD 660 EFEGLFKQPA 670 ENVNQYLTDP 680 KFVERTLRLA 690 GTQPLEVLEA 700 VQRSLVLQRP 710 QTWADCVTWA 720 CHHWHTQYSN 730 NIRQLLHNFP 740 PDQLTSSGAP 750 FWSGPKRCPH 760 PLTFDVNNPL 770 HLDYVMAAAN 780 LFAQTYGLTG 790 SQDRAAVATF 800 LQSVQVPEFT 810 PKSGVKIHVS 820 DQELQSANAS 830 VDDSRLEELK 840 ATLPSPDKLP 850 GFKMYPIDFE 860 KDDDSNFHMD 870 FIVAASNLRA 880 ENYDIPSADR 890 HKSKLIAGKI 900 IPAIATTTAA 910 VVGLVCLELY 920 KVVQGHRQLD 930 SYKNGFLNLA 940 LPFFGFSEPL 950 AAPRHQYYNQ 960 EWTLWDRFEV 970 QGLQPNGEEM 980 TLKQFLDYFK 990 TEHKLEITML 1000 SQGVSMLYSF 1010 FMPAAKLKER 1020 LDQPMTEIVS 1030 RVSKRKLGRH 1040 VRALVLELCC 1050 NDESGEDVEV PYVRYTIR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0003723 RNA 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 D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] 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.

[4] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[5] 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.

[6] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[7] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[8] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[9] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.