Search Results

Overview

Uniprot IDP31948
Protein NameStress-induced-phosphoprotein 1
Gene NameSTIP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
169 KPSDLGTKLQDPRIM
207 PPPPPPKKETKPEPM
229 KKQALKEKELGNDAY
237 ELGNDAYKKKDFDTA
238 LGNDAYKKKDFDTAL
246 KDFDTALKHYDKAKE
284 KCRELCEKAIEVGRE
317 YFKEEKYKDAIHFYN
325 DAIHFYNKSLAEHRT
337 HRTPDVLKKCQQAEK
338 RTPDVLKKCQQAEKI
364 PDLALEEKNKGNECF
366 LALEEKNKGNECFQK
388 KHYTEAIKRNPKDAK
395 KRNPKDAKLYSNRAA
434 FIKGYTRKAAALEAM
442 AAALEAMKDYTKAMD
446 EAMKDYTKAMDVYQK
462 LDLDSSCKEAADGYQ
523 QALSEHLKNPVIAQK
530 KNPVIAQKIQKLMDV
73 DLKPDWGKGYSRKAA
78 WGKGYSRKAAALEFL

Function

Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity)

Protein Sequence

10 MEQVNELKEK 20 GNKALSVGNI 30 DDALQCYSEA 40 IKLDPHNHVL 50 YSNRSAAYAK 60 KGDYQKAYED 70 GCKTVDLKPD 80 WGKGYSRKAA 90 ALEFLNRFEE 100 AKRTYEEGLK 110 HEANNPQLKE 120 GLQNMEARLA 130 ERKFMNPFNM 140 PNLYQKLESD 150 PRTRTLLSDP 160 TYRELIEQLR 170 NKPSDLGTKL 180 QDPRIMTTLS 190 VLLGVDLGSM 200 DEEEEIATPP 210 PPPPPKKETK 220 PEPMEEDLPE 230 NKKQALKEKE 240 LGNDAYKKKD 250 FDTALKHYDK 260 AKELDPTNMT 270 YITNQAAVYF 280 EKGDYNKCRE 290 LCEKAIEVGR 300 ENREDYRQIA 310 KAYARIGNSY 320 FKEEKYKDAI 330 HFYNKSLAEH 340 RTPDVLKKCQ 350 QAEKILKEQE 360 RLAYINPDLA 370 LEEKNKGNEC 380 FQKGDYPQAM 390 KHYTEAIKRN 400 PKDAKLYSNR 410 AACYTKLLEF 420 QLALKDCEEC 430 IQLEPTFIKG 440 YTRKAAALEA 450 MKDYTKAMDV 460 YQKALDLDSS 470 CKEAADGYQR 480 CMMAQYNRHD 490 SPEDVKRRAM 500 ADPEVQQIMS 510 DPAMRLILEQ 520 MQKDPQALSE 530 HLKNPVIAQK 540 IQKLMDVGLI AIR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0120293 dynein axonemal particle
Cellular Component GO:0005794 Golgi apparatus
Cellular Component GO:0005634 nucleus
Cellular Component GO:0101031 protein folding chaperone complex
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0051879 Hsp90 protein binding
Molecular Function GO:0003723 RNA binding

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] 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.

[4] 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.

[5] 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.

[6] 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.

[7] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[8] 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.