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Overview

Uniprot IDO00499
Protein NameMyc box-dependent-interacting protein 1
Gene NameBIN1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
13 SKGVTAGKIASNVQK
146 RIAKRGRKLVDYDSA
164 YESLQTAKKKDEAKI
165 ESLQTAKKKDEAKIA
20 KIASNVQKKLTRAQE
28 KLTRAQEKVLQKLGK
295 NAPAKGNKSPSPPDG
32 AQEKVLQKLGKADET
330 TPGATLPKSPSQLRK
337 KSPSQLRKGPPVPPP
35 KVLQKLGKADETKDE
351 PPKHTPSKEVKQEQI
7 *MAEMGSKGVTAGKI

Function

Is a key player in the control of plasma membrane curvature, membrane shaping and membrane remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:24755653). Is a negative regulator of endocytosis (By similarity). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (PubMed:27179792). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity). May be involved in the regulation of MYC activity and the control cell proliferation (PubMed:8782822). Has actin bundling activity and stabilizes actin filaments against depolymerization in vitro (PubMed:28893863)

Protein Sequence

10 MAEMGSKGVT 20 AGKIASNVQK 30 KLTRAQEKVL 40 QKLGKADETK 50 DEQFEQCVQN 60 FNKQLTEGTR 70 LQKDLRTYLA 80 SVKAMHEASK 90 KLNECLQEVY 100 EPDWPGRDEA 110 NKIAENNDLL 120 WMDYHQKLVD 130 QALLTMDTYL 140 GQFPDIKSRI 150 AKRGRKLVDY 160 DSARHHYESL 170 QTAKKKDEAK 180 IAKPVSLLEK 190 AAPQWCQGKL 200 QAHLVAQTNL 210 LRNQAEEELI 220 KAQKVFEEMN 230 VDLQEELPSL 240 WNSRVGFYVN 250 TFQSIAGLEE 260 NFHKEMSKLN 270 QNLNDVLVGL 280 EKQHGSNTFT 290 VKAQPSDNAP 300 AKGNKSPSPP 310 DGSPAATPEI 320 RVNHEPEPAG 330 GATPGATLPK 340 SPSQLRKGPP 350 VPPPPKHTPS 360 KEVKQEQILS 370 LFEDTFVPEI 380 SVTTPSQFEA 390 PGPFSEQASL 400 LDLDFDPLPP 410 VTSPVKAPTP 420 SGQSIPWDLW 430 EPTESPAGSL 440 PSGEPSAAEG 450 TFAVSWPSQT 460 AEPGPAQPAE 470 ASEVAGGTQP 480 AAGAQEPGET 490 AASEAASSSL 500 PAVVVETFPA 510 TVNGTVEGGS 520 GAGRLDLPPG 530 FMFKVQAQHD 540 YTATDTDELQ 550 LKAGDVVLVI 560 PFQNPEEQDE 570 GWLMGVKESD 580 WNQHKELEKC 590 RGVFPENFTE RVP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Biological Process GO:0006997 nucleus organization
Biological Process GO:0030838 positive regulation of actin filament polymerization
Biological Process GO:0043065 positive regulation of apoptotic process
Biological Process GO:0048711 positive regulation of astrocyte differentiation
Biological Process GO:0045807 positive regulation of endocytosis
Biological Process GO:0010564 regulation of cell cycle process
Biological Process GO:0086091 regulation of heart rate by cardiac conduction
Biological Process GO:0045664 regulation of neuron differentiation
Biological Process GO:0048488 synaptic vesicle endocytosis
Biological Process GO:0033292 T-tubule organization
Cellular Component GO:0030424 axon
Cellular Component GO:0043194 axon initial segment
Cellular Component GO:0043679 axon terminus
Cellular Component GO:0044300 cerebellar mossy fiber
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0030425 dendrite
Cellular Component GO:0005768 endosome
Cellular Component GO:0098850 extrinsic component of synaptic vesicle membrane
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0031674 I band
Cellular Component GO:0060987 lipid tube
Cellular Component GO:0016020 membrane
Cellular Component GO:0033268 node of Ranvier
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0008021 synaptic vesicle
Cellular Component GO:0030315 T-tubule
Cellular Component GO:0043196 varicosity
Cellular Component GO:0031982 vesicle
Cellular Component GO:0030018 Z disc
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0019828 aspartic-type endopeptidase inhibitor activity
Molecular Function GO:0030276 clathrin binding
Molecular Function GO:0051020 GTPase binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0008289 lipid binding
Molecular Function GO:0005543 phospholipid binding
Molecular Function GO:0002020 protease binding
Molecular Function GO:0051087 protein-folding chaperone binding
Molecular Function GO:0070063 RNA polymerase binding
Molecular Function GO:0048156 tau protein binding
Biological Process GO:0007010 cytoskeleton organization
Biological Process GO:0006897 endocytosis
Biological Process GO:0008333 endosome to lysosome transport
Biological Process GO:0060988 lipid tube assembly
Biological Process GO:1902430 negative regulation of amyloid-beta formation
Biological Process GO:1904878 negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
Biological Process GO:1901380 negative regulation of potassium ion transmembrane transport
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:1903946 negative regulation of ventricular cardiac muscle cell action potential

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] 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.

[4] 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.

[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] 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.