Search Results

Overview

Uniprot IDP42166
Protein NameLamina-associated polypeptide 2, isoform alpha
Gene NameTMPO
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
13 EDPSVLTKDKLKSEL
17 VLTKDKLKSELVANN
248 AKKVHTSKGDLPREP
269 PGRGQLQKLASERNL
281 RNLFISCKSSHDRCL
290 SHDRCLEKSSSSSSQ
323 ETTTGYYKDIVENIC
334 ENICGREKSGIQPLC
356 DQSPLSSKRKALEES
358 SPLSSKRKALEESES
416 QKRIDQSKFQETEFL
435 KVPRLSEKSVEERDS
60 LPAGTNSKGPPDFSS
656 GRRYLWLKDCKINLA
667 INLASKNKLASTPFK
685 LFGGEVCKVIKKRGN

Function

May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1

Protein Sequence

10 MPEFLEDPSV 20 LTKDKLKSEL 30 VANNVTLPAG 40 EQRKDVYVQL 50 YLQHLTARNR 60 PPLPAGTNSK 70 GPPDFSSDEE 80 REPTPVLGSG 90 AAAAGRSRAA 100 VGRKATKKTD 110 KPRQEDKDDL 120 DVTELTNEDL 130 LDQLVKYGVN 140 PGPIVGTTRK 150 LYEKKLLKLR 160 EQGTESRSST 170 PLPTISSSAE 180 NTRQNGSNDS 190 DRYSDNEEGK 200 KKEHKKVKST 210 RDIVPFSELG 220 TTPSGGGFFQ 230 GISFPEISTR 240 PPLGSTELQA 250 AKKVHTSKGD 260 LPREPLVATN 270 LPGRGQLQKL 280 ASERNLFISC 290 KSSHDRCLEK 300 SSSSSSQPEH 310 SAMLVSTAAS 320 PSLIKETTTG 330 YYKDIVENIC 340 GREKSGIQPL 350 CPERSHISDQ 360 SPLSSKRKAL 370 EESESSQLIS 380 PPLAQAIRDY 390 VNSLLVQGGV 400 GSLPGTSNSM 410 PPLDVENIQK 420 RIDQSKFQET 430 EFLSPPRKVP 440 RLSEKSVEER 450 DSGSFVAFQN 460 IPGSELMSSF 470 AKTVVSHSLT 480 TLGLEVAKQS 490 QHDKIDASEL 500 SFPFHESILK 510 VIEEEWQQVD 520 RQLPSLACKY 530 PVSSREATQI 540 LSVPKVDDEI 550 LGFISEATPL 560 GGIQAASTES 570 CNQQLDLALC 580 RAYEAAASAL 590 QIATHTAFVA 600 KAMQADISQA 610 AQILSSDPSR 620 THQALGILSK 630 TYDAASYICE 640 AAFDEVKMAA 650 HTMGNATVGR 660 RYLWLKDCKI 670 NLASKNKLAS 680 TPFKGGTLFG 690 GEVCKVIKKR GNKH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0031965 nuclear membrane
Cellular Component GO:0005634 nucleus
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0005521 lamin 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] 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] 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.

[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.