Search Results
Overview
| Uniprot ID | P46013 |
|---|---|
| Protein Name | Proliferation marker protein Ki-67 |
| Gene Name | MKI67 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1004 | SEKGKITKMPCQSLQ |
| 1022 | INTPTHTKQQLKASL |
| 1026 | THTKQQLKASLGKVG |
| 1031 | QLKASLGKVGVKEEL |
| 1043 | EELLAVGKFTRTSGE |
| 1063 | REPAGDGKSIRTFKE |
| 1069 | GKSIRTFKESPKQIL |
| 107 | ESLQNGRKSTEFPRK |
| 1130 | KTTKIACKSPPPESV |
| 1144 | VDTPTSTKQWPKRSL |
| 1153 | WPKRSLRKADVEEEF |
| 1165 | EEFLALRKLTPSAGK |
| 1197 | FMGTPVQKLDLAGTL |
| 1208 | AGTLPGSKRQLQTPK |
| 1217 | QLQTPKEKAQALEDL |
| 1248 | VAAGKTTKIPCDSPQ |
| 1270 | TSTKQRPKRSIRKAD |
| 1275 | RPKRSIRKADVEGEL |
| 1330 | TENLTGSKRRPQTPK |
| 1370 | VAAGKTTKMPCESSP |
| 1408 | QKELSALKKLTQTSG |
| 1409 | KELSALKKLTQTSGE |
| 141 | DEKAQDSKAYSKITE |
| 1422 | GETTHTDKVPGGEDK |
| 1441 | FRETAKQKLDPAASV |
| 145 | QDSKAYSKITEGKVS |
| 1452 | AASVTGSKRHPKTKE |
| 1460 | RHPKTKEKAQPLEDL |
| 1482 | QTPVCTDKPTTHEKT |
| 1491 | TTHEKTTKIACRSQP |
| 150 | YSKITEGKVSGNPQV |
| 1508 | VDTPTSSKPQSKRSL |
| 1512 | TSSKPQSKRSLRKVD |
| 160 | GNPQVHIKNVKEDST |
| 1616 | KTAKVACKSSQPDPD |
| 1630 | DKNPASSKRRLKTSL |
| 1634 | ASSKRRLKTSLGKVG |
| 1639 | RLKTSLGKVGVKEEL |
| 1651 | EELLAVGKLTQTSGE |
| 1694 | AASLTGSKRQLRTPK |
| 1734 | MTNEKTTKVSYRASQ |
| 1756 | TSSKPQPKRSLRKAD |
| 1855 | TTDEKTTKKILCKSP |
| 1856 | TDEKTTKKILCKSPQ |
| 1860 | TTKKILCKSPQSDPA |
| 1874 | ADTPTNTKQRPKRSL |
| 1938 | LGNLPGSKRRPQTPK |
| 2000 | TSSKQRLKISLGKVG |
| 2005 | RLKISLGKVGVKEEV |
| 2017 | EEVLPVGKLTQTSGK |
| 2024 | KLTQTSGKTTQTHRE |
| 2167 | FRETAKQKLDPAASV |
| 2178 | AASVTGSKRQPRTPK |
| 2187 | QPRTPKGKAQPLEDL |
| 219 | VSRYGELKSVPTTQC |
| 2209 | QTPICTDKPTTHEKT |
| 2218 | TTHEKTTKIACRSPQ |
| 2240 | TIFKPQSKRSLRKAD |
| 2245 | QSKRSLRKADVEEES |
| 2289 | FMGTPVQKLDLPGNL |
| 2300 | PGNLPGSKRWPQTPK |
| 2343 | KTTKIACKSPQPDPV |
| 2357 | VDTPASTKQRPKRNL |
| 2473 | SPQPESFKTSRSSKQ |
| 2483 | RSSKQRLKIPLVKVD |
| 2500 | EEPLAVSKLTRTSGE |
| 263 | NVLQYCRKSGLQTDY |
| 2652 | VLKQRAKKKPNPVEE |
| 2672 | RPRAPKEKAQPLEDL |
| 2703 | LTAGKATKIPCESPP |
| 2730 | HLRTRVQKVQVKEEP |
| 2826 | KTTKIPCKSSPELED |
| 2839 | EDTATSSKRRPRTRA |
| 2880 | KEPVGEGKGTKAFKQ |
| 2883 | VGEGKGTKAFKQPAK |
| 2886 | GKGTKAFKQPAKRKL |
| 2892 | FKQPAKRKLDAEDVI |
| 295 | VSRKSRPKSGGSGHA |
| 2957 | PDSGKPLKISRRVLR |
| 2967 | RRVLRAPKVEPVGDV |
| 3049 | SEPVVIMKRSLRTSA |
| 3168 | QNESSQPKVAEESGG |
| 3204 | SMCLRSRKTKSQPAA |
| 3206 | CLRSRKTKSQPAAST |
| 3217 | AASTLESKSVQRVTR |
| 3243 | AEDNVCVKKIRTRSH |
| 331 | ESVQTPSKAVGASFP |
| 344 | FPLYEPAKMKTPVQY |
| 346 | LYEPAKMKTPVQYSQ |
| 364 | SPQKHKNKDLYTTGR |
| 379 | RESVNLGKSEGFKAG |
| 421 | KPENLSSKTRGSIPT |
| 458 | QVERKIQKDSLSKPE |
| 548 | MHTPPVLKKIIKEQP |
| 549 | HTPPVLKKIIKEQPQ |
| 552 | PVLKKIIKEQPQPSG |
| 600 | DQRRRSCKTAPASSS |
| 843 | RENGNVAKTPRNTYK |
| 850 | KTPRNTYKMTSLETK |
| 886 | TEFRNIQKLPVESKS |
| 906 | EIVECILKRGQKATL |
| 910 | CILKRGQKATLLQQR |
| 957 | RSRTWGQKCAPMSDL |
| 977 | LPDTELMKDTARGQN |
| 993 | LQTQDHAKAPKSEKG |
Function
Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0000793 | condensed chromosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0140693 | molecular condensate scaffold activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0008283 | cell population proliferation |
| Biological Process | GO:0007059 | chromosome segregation |
| Biological Process | GO:0051321 | meiotic cell cycle |
| Biological Process | GO:1902275 | regulation of chromatin organization |
| Biological Process | GO:0007088 | regulation of mitotic nuclear division |
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] 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.
[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] 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.
[5] 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.
[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] 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.