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Overview

Uniprot ID	O43252
Protein Name	Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
Gene Name	PAPSS1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
10	IPGSLCKKVKLSNNA
12	GSLCKKVKLSNNAQN

Function

Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway (PubMed:14747722, PubMed:9576487, PubMed:9648242, PubMed:9668121). Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells (PubMed:9576487)

Protein Sequence

10 MEIPGSLCKK 20 VKLSNNAQNW 30 GMQRATNVTY 40 QAHHVSRNKR 50 GQVVGTRGGF 60 RGCTVWLTGL 70 SGAGKTTVSM 80 ALEEYLVCHG 90 IPCYTLDGDN 100 IRQGLNKNLG 110 FSPEDREENV 120 RRIAEVAKLF 130 ADAGLVCITS 140 FISPYTQDRN 150 NARQIHEGAS 160 LPFFEVFVDA 170 PLHVCEQRDV 180 KGLYKKARAG 190 EIKGFTGIDS 200 EYEKPEAPEL 210 VLKTDSCDVN 220 DCVQQVVELL 230 QERDIVPVDA 240 SYEVKELYVP 250 ENKLHLAKTD 260 AETLPALKIN 270 KVDMQWVQVL 280 AEGWATPLNG 290 FMREREYLQC 300 LHFDCLLDGG 310 VINLSVPIVL 320 TATHEDKERL 330 DGCTAFALMY 340 EGRRVAILRN 350 PEFFEHRKEE 360 RCARQWGTTC 370 KNHPYIKMVM 380 EQGDWLIGGD 390 LQVLDRVYWN 400 DGLDQYRLTP 410 TELKQKFKDM 420 NADAVFAFQL 430 RNPVHNGHAL 440 LMQDTHKQLL 450 ERGYRRPVLL 460 LHPLGGWTKD 470 DDVPLMWRMK 480 QHAAVLEEGV 490 LNPETTVVAI 500 FPSPMMYAGP 510 TEVQWHCRAR 520 MVAGANFYIV 530 GRDPAGMPHP 540 ETGKDLYEPS 550 HGAKVLTMAP 560 GLITLEIVPF 570 RVAAYNKKKK 580 RMDYYDSEHH 590 EDFEFISGTR 600 MRKLAREGQK 610 PPEGFMAPKA 620 WTVLTEYYKS LEKA

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0004020	adenylylsulfate kinase activity
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0016779	nucleotidyltransferase activity
Molecular Function	GO:0042803	protein homodimerization activity
Molecular Function	GO:0004781	sulfate adenylyltransferase (ATP) activity
Biological Process	GO:0050428	3'-phosphoadenosine 5'-phosphosulfate biosynthetic process
Biological Process	GO:0001501	skeletal system development
Biological Process	GO:0000103	sulfate assimilation

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] 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.

[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[4] 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.

[5] 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.