Search Results

Overview

Uniprot IDQ15691
Protein NameMicrotubule-associated protein RP/EB family member 1
Gene NameMAPRE1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
113 EFVQWFKKFFDANYD
148 LVAPALNKPKKPLTS
150 APALNKPKKPLTSSS
151 PALNKPKKPLTSSSA
174 QRTAAAPKAGPGVVR
182 AGPGVVRKNPGVGNG
83 KILQAGFKRMGVDKI

Function

Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:23001180, PubMed:28726242, PubMed:28814570, PubMed:34608293). Recruits other +TIP proteins to microtubules by binding to a conserved Ser-X-Leu-Pro (SXLP) motif in their polypeptide chains (PubMed:19632184, PubMed:36592928). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection between astral microtubules and the cortex during mitotic chromosome segregation (PubMed:12388762, PubMed:34608293). Assists chromosome alignment in metaphase by recruiting the SKA complex to the spindle and stabilizing its interactions with microtubule bundles (K-fibers) (PubMed:27225956, PubMed:36592928). Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (PubMed:28814570). Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (PubMed:28726242). Functions downstream of Rho GTPases and DIAPH1 in stable microtubule formation (By similarity). Promotes microtubule-mediated GJA1/CX43 trafficking to cell membranes via its interaction with DSP, thereby facilitating gap junction intracellular communication (PubMed:25225338). May play a role in cell migration (By similarity)

Protein Sequence

10 MAVNVYSTSV 20 TSDNLSRHDM 30 LAWINESLQL 40 NLTKIEQLCS 50 GAAYCQFMDM 60 LFPGSIALKK 70 VKFQAKLEHE 80 YIQNFKILQA 90 GFKRMGVDKI 100 IPVDKLVKGK 110 FQDNFEFVQW 120 FKKFFDANYD 130 GKDYDPVAAR 140 QGQETAVAPS 150 LVAPALNKPK 160 KPLTSSSAAP 170 QRPISTQRTA 180 AAPKAGPGVV 190 RKNPGVGNGD 200 DEAAELMQQV 210 NVLKLTVEDL 220 EKERDFYFGK 230 LRNIELICQE 240 NEGENDPVLQ 250 RIVDILYATD 260 EGFVIPDEGG PQEEQEEY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0036064 ciliary basal body
Cellular Component GO:0031253 cell projection membrane
Cellular Component GO:0005813 centrosome
Cellular Component GO:0030981 cortical microtubule cytoskeleton
Cellular Component GO:0005881 cytoplasmic microtubule
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0005794 Golgi apparatus
Cellular Component GO:0005874 microtubule
Cellular Component GO:0005815 microtubule organizing center
Cellular Component GO:0035371 microtubule plus-end
Cellular Component GO:1905721 mitotic spindle astral microtubule end
Cellular Component GO:1990498 mitotic spindle microtubule
Cellular Component GO:0097431 mitotic spindle pole
Cellular Component GO:0051233 spindle midzone
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0051010 microtubule plus-end binding
Molecular Function GO:0120283 protein serine/threonine kinase binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0051315 attachment of mitotic spindle microtubules to kinetochore
Biological Process GO:0051301 cell division
Biological Process GO:0016477 cell migration
Biological Process GO:0000132 establishment of mitotic spindle orientation
Biological Process GO:0008104 intracellular protein localization
Biological Process GO:0001578 microtubule bundle formation
Biological Process GO:0046785 microtubule polymerization
Biological Process GO:0031115 negative regulation of microtubule polymerization
Biological Process GO:0031116 positive regulation of microtubule polymerization
Biological Process GO:1902888 protein localization to astral microtubule
Biological Process GO:0035372 protein localization to microtubule
Biological Process GO:1902480 protein localization to mitotic spindle
Biological Process GO:0031110 regulation of microtubule polymerization or depolymerization
Biological Process GO:0051225 spindle assembly

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.