Search Results

Overview

Uniprot IDQ16891
Protein NameMICOS complex subunit MIC60
Gene NameIMMT
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
102 YNVPLPKKSIQSGPL
211 ARLAQQEKQEQVKIE
216 QEKQEQVKIESLAKS
269 NSEIAGEKKSAQWRT
282 RTVEGALKERRKAVD
286 GALKERRKAVDEAAD
297 EAADALLKAKEELEK
299 ADALLKAKEELEKMK
306 KEELEKMKSVIENAK
313 KSVIENAKKKEVAGA
321 KKEVAGAKPHITAAE
344 DLDNVVKKVQAAQSE
353 QAAQSEAKVVSQYHE
423 NRELAEQKATEKQHI
427 AEQKATEKQHITLAL
436 HITLALEKQKLEEKR
451 AFDSAVAKALEHHRS
565 VAEEEARKAHQLWLS
640 ARFYAVQKLARRVAM
714 AKFVNQLKGESRRVA
77 HFRESVEKTIPYSDK

Function

Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane (PubMed:22114354, PubMed:25781180, PubMed:32567732, PubMed:33130824). Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology (PubMed:22114354, PubMed:25781180, PubMed:32567732, PubMed:33130824)

Protein Sequence

10 MLRACQLSGV 20 TAAAQSCLCG 30 KFVLRPLRPC 40 RRYSTSGSSG 50 LTTGKIAGAG 60 LLFVGGGIGG 70 TILYAKWDSH 80 FRESVEKTIP 90 YSDKLFEMVL 100 GPAAYNVPLP 110 KKSIQSGPLK 120 ISSVSEVMKE 130 SKQPASQLQK 140 QKGDTPASAT 150 APTEAAQIIS 160 AAGDTLSVPA 170 PAVQPEESLK 180 TDHPEIGEGK 190 PTPALSEEAS 200 SSSIRERPPE 210 EVAARLAQQE 220 KQEQVKIESL 230 AKSLEDALRQ 240 TASVTLQAIA 250 AQNAAVQAVN 260 AHSNILKAAM 270 DNSEIAGEKK 280 SAQWRTVEGA 290 LKERRKAVDE 300 AADALLKAKE 310 ELEKMKSVIE 320 NAKKKEVAGA 330 KPHITAAEGK 340 LHNMIVDLDN 350 VVKKVQAAQS 360 EAKVVSQYHE 370 LVVQARDDFK 380 RELDSITPEV 390 LPGWKGMSVS 400 DLADKLSTDD 410 LNSLIAHAHR 420 RIDQLNRELA 430 EQKATEKQHI 440 TLALEKQKLE 450 EKRAFDSAVA 460 KALEHHRSEI 470 QAEQDRKIEE 480 VRDAMENEMR 490 TQLRRQAAAH 500 TDHLRDVLRV 510 QEQELKSEFE 520 QNLSEKLSEQ 530 ELQFRRLSQE 540 QVDNFTLDIN 550 TAYARLRGIE 560 QAVQSHAVAE 570 EEARKAHQLW 580 LSVEALKYSM 590 KTSSAETPTI 600 PLGSAVEAIK 610 ANCSDNEFTQ 620 ALTAAIPPES 630 LTRGVYSEET 640 LRARFYAVQK 650 LARRVAMIDE 660 TRNSLYQYFL 670 SYLQSLLLFP 680 PQQLKPPPEL 690 CPEDINTFKL 700 LSYASYCIEH 710 GDLELAAKFV 720 NQLKGESRRV 730 AQDWLKEARM 740 TLETKQIVEI 750 LTAYASAVGI GTTQVQPE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016020 membrane
Cellular Component GO:0140275 MIB complex
Cellular Component GO:0061617 MICOS complex
Cellular Component GO:0044284 mitochondrial crista junction
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005758 mitochondrial intermembrane space
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0001401 SAM complex
Molecular Function GO:0003723 RNA binding
Biological Process GO:0042407 cristae formation
Biological Process GO:0007007 inner mitochondrial membrane organization

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] 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.

[3] 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.

[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.