Search Results

Overview

Uniprot IDQ9H3U1
Protein NameProtein unc-45 homolog A
Gene NameUNC45A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
142 IGGQIQEKVRYMSST
279 VKKGFRGKEGAIIVD
617 VELAKYAKQHVPEQH

Function

Acts as a co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity)

Protein Sequence

10 MTVSGPGTPE 20 PRPATPGASS 30 VEQLRKEGNE 40 LFKCGDYGGA 50 LAAYTQALGL 60 DATPQDQAVL 70 HRNRAACHLK 80 LEDYDKAETE 90 ASKAIEKDGG 100 DVKALYRRSQ 110 ALEKLGRLDQ 120 AVLDLQRCVS 130 LEPKNKVFQE 140 ALRNIGGQIQ 150 EKVRYMSSTD 160 AKVEQMFQIL 170 LDPEEKGTEK 180 KQKASQNLVV 190 LAREDAGAEK 200 IFRSNGVQLL 210 QRLLDMGETD 220 LMLAALRTLV 230 GICSEHQSRT 240 VATLSILGTR 250 RVVSILGVES 260 QAVSLAACHL 270 LQVMFDALKE 280 GVKKGFRGKE 290 GAIIVDPARE 300 LKVLISNLLD 310 LLTEVGVSGQ 320 GRDNALTLLI 330 KAVPRKSLKD 340 PNNSLTLWVI 350 DQGLKKILEV 360 GGSLQDPPGE 370 LAVTANSRMS 380 ASILLSKLFD 390 DLKCDAEREN 400 FHRLCENYIK 410 SWFEGQGLAG 420 KLRAIQTVSC 430 LLQGPCDAGN 440 RALELSGVME 450 SVIALCASEQ 460 EEEQLVAVEA 470 LIHAAGKAKR 480 ASFITANGVS 490 LLKDLYKCSE 500 KDSIRIRALV 510 GLCKLGSAGG 520 TDFSMKQFAE 530 GSTLKLAKQC 540 RKWLCNDQID 550 AGTRRWAVEG 560 LAYLTFDADV 570 KEEFVEDAAA 580 LKALFQLSRL 590 EERSVLFAVA 600 SALVNCTNSY 610 DYEEPDPKMV 620 ELAKYAKQHV 630 PEQHPKDKPS 640 FVRARVKKLL 650 AAGVVSAMVC 660 MVKTESPVLT 670 SSCRELLSRV 680 FLALVEEVED 690 RGTVVAQGGG 700 RALIPLALEG 710 TDVGQTKAAQ 720 ALAKLTITSN 730 PEMTFPGERI 740 YEVVRPLVSL 750 LHLNCSGLQN 760 FEALMALTNL 770 AGISERLRQK 780 ILKEKAVPMI 790 EGYMFEEHEM 800 IRRAATECMC 810 NLAMSKEVQD 820 LFEAQGNDRL 830 KLLVLYSGED 840 DELLQRAAAG 850 GLAMLTSMRP 860 TLCSRIPQVT 870 THWLEILQAL 880 LLSSNQELQH 890 RGAVVVLNMV 900 EASREIASTL 910 MESEMMEILS 920 VLAKGDHSPV 930 TRAAAACLDK 940 AVEYGLIQPN QDGE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0048471 perinuclear region of cytoplasm
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0051879 Hsp90 protein binding
Molecular Function GO:0042802 identical protein binding
Biological Process GO:0030154 cell differentiation
Biological Process GO:0007517 muscle organ development
Biological Process GO:0006457 protein folding

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] 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.

[5] 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.

[6] 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.