Search Results

Overview

Uniprot IDP14625
Protein NameEndoplasmin
Gene NameHSP90B1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
114 NASDALDKIRLISLT
142 KIKCDKEKNLLHVTD
161 MTREELVKNLGTIAK
168 KNLGTIAKSGTSEFL
270 TIKNLVKKYSQFINF
348 PIWQRPSKEVEEDEY
356 EVEEDEYKAFYKSFS
404 LFDEYGSKKSDYIKL
405 FDEYGSKKSDYIKLY
410 SKKSDYIKLYVRRVF
455 RETLQQHKLLKVIRK
467 IRKKLVRKTLDMIKK
473 RKTLDMIKKIADDKY
474 KTLDMIKKIADDKYN
479 IKKIADDKYNDTFWK
486 KYNDTFWKEFGTNIK
493 KEFGTNIKLGVIEDH
547 FMAGSSRKEAESSPF
593 KRFQNVAKEGVKFDE
597 NVAKEGVKFDESEKT
603 VKFDESEKTKESREA
623 EPLLNWMKDKALKDK
633 ALKDKIEKAVVSQRL
663 GNMERIMKAQAYQTG
671 AQAYQTGKDISTNYY
682 TNYYASQKKTFEINP
683 NYYASQKKTFEINPR
733 GYLLPDTKAYGDRIE
75 ELREKSEKFAFQAEV
95 LIINSLYKNKEIFLR
97 INSLYKNKEIFLREL

Function

ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed:23572575, PubMed:39509507). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (PubMed:23572575, PubMed:39509507). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:11584270). Promotes folding and trafficking of TLR4 to the cell surface (PubMed:11584270). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059)

Protein Sequence

10 MRALWVLGLC 20 CVLLTFGSVR 30 ADDEVDVDGT 40 VEEDLGKSRE 50 GSRTDDEVVQ 60 REEEAIQLDG 70 LNASQIRELR 80 EKSEKFAFQA 90 EVNRMMKLII 100 NSLYKNKEIF 110 LRELISNASD 120 ALDKIRLISL 130 TDENALSGNE 140 ELTVKIKCDK 150 EKNLLHVTDT 160 GVGMTREELV 170 KNLGTIAKSG 180 TSEFLNKMTE 190 AQEDGQSTSE 200 LIGQFGVGFY 210 SAFLVADKVI 220 VTSKHNNDTQ 230 HIWESDSNEF 240 SVIADPRGNT 250 LGRGTTITLV 260 LKEEASDYLE 270 LDTIKNLVKK 280 YSQFINFPIY 290 VWSSKTETVE 300 EPMEEEEAAK 310 EEKEESDDEA 320 AVEEEEEEKK 330 PKTKKVEKTV 340 WDWELMNDIK 350 PIWQRPSKEV 360 EEDEYKAFYK 370 SFSKESDDPM 380 AYIHFTAEGE 390 VTFKSILFVP 400 TSAPRGLFDE 410 YGSKKSDYIK 420 LYVRRVFITD 430 DFHDMMPKYL 440 NFVKGVVDSD 450 DLPLNVSRET 460 LQQHKLLKVI 470 RKKLVRKTLD 480 MIKKIADDKY 490 NDTFWKEFGT 500 NIKLGVIEDH 510 SNRTRLAKLL 520 RFQSSHHPTD 530 ITSLDQYVER 540 MKEKQDKIYF 550 MAGSSRKEAE 560 SSPFVERLLK 570 KGYEVIYLTE 580 PVDEYCIQAL 590 PEFDGKRFQN 600 VAKEGVKFDE 610 SEKTKESREA 620 VEKEFEPLLN 630 WMKDKALKDK 640 IEKAVVSQRL 650 TESPCALVAS 660 QYGWSGNMER 670 IMKAQAYQTG 680 KDISTNYYAS 690 QKKTFEINPR 700 HPLIRDMLRR 710 IKEDEDDKTV 720 LDLAVVLFET 730 ATLRSGYLLP 740 DTKAYGDRIE 750 RMLRLSLNID 760 PDAKVEEEPE 770 EEPEETAEDT 780 TEDTEQDEDE 790 EMDVGTDEEE 800 ETAKESTAEK DEL

Gene Ontology

Classification GO ID Description
Biological Process GO:0051208 sequestering of calcium ion
Cellular Component GO:0005829 cytosol
Cellular Component GO:0071682 endocytic vesicle lumen
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0034663 endoplasmic reticulum chaperone complex
Cellular Component GO:0005788 endoplasmic reticulum lumen
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0042470 melanosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0030496 midbody
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0033018 sarcoplasmic reticulum lumen
Cellular Component GO:0005790 smooth endoplasmic reticulum
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0140662 ATP-dependent protein folding chaperone
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0050750 low-density lipoprotein particle receptor binding
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0019903 protein phosphatase binding
Molecular Function GO:0004864 protein phosphatase inhibitor activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0031247 actin rod assembly
Biological Process GO:0071318 cellular response to ATP
Biological Process GO:0071287 cellular response to manganese ion
Biological Process GO:0036503 ERAD pathway
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0034123 positive regulation of toll-like receptor signaling pathway
Biological Process GO:0030177 positive regulation of Wnt signaling pathway
Biological Process GO:0006457 protein folding
Biological Process GO:0034975 protein folding in endoplasmic reticulum
Biological Process GO:0072659 protein localization to plasma membrane
Biological Process GO:0015031 protein transport
Biological Process GO:0034976 response to endoplasmic reticulum stress
Biological Process GO:0001666 response to hypoxia
Biological Process GO:0030970 retrograde protein transport, ER to cytosol

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] 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] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[8] 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.

[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.