Search Results

Overview

Uniprot IDQ99961
Protein NameEndophilin-A2
Gene NameSH3GL1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
12 GLKKQFYKASQLVSE
177 YKKKRQGKIPDEELR
20 ASQLVSEKVGGAEGT
7 *MSVAGLKKQFYKAS
76 TMLNTVSKIRGQVKN

Function

Implicated in endocytosis. In a first step mediates neck formation during ultrafast endocytosis and function at a second step to aid in the removal of clathrin coats from the regenerated vesicles (By similarity). May recruit other proteins to membranes with high curvature (By similarity)

Protein Sequence

10 MSVAGLKKQF 20 YKASQLVSEK 30 VGGAEGTKLD 40 DDFKEMEKKV 50 DVTSKAVTEV 60 LARTIEYLQP 70 NPASRAKLTM 80 LNTVSKIRGQ 90 VKNPGYPQSE 100 GLLGECMIRH 110 GKELGGESNF 120 GDALLDAGES 130 MKRLAEVKDS 140 LDIEVKQNFI 150 DPLQNLCEKD 160 LKEIQHHLKK 170 LEGRRLDFDY 180 KKKRQGKIPD 190 EELRQALEKF 200 EESKEVAETS 210 MHNLLETDIE 220 QVSQLSALVD 230 AQLDYHRQAV 240 QILDELAEKL 250 KRRMREASSR 260 PKREYKPKPR 270 EPFDLGEPEQ 280 SNGGFPCTTA 290 PKIAASSSFR 300 SSDKPIRTPS 310 RSMPPLDQPS 320 CKALYDFEPE 330 NDGELGFHEG 340 DVITLTNQID 350 ENWYEGMLDG 360 QSGFFPLSYV EVLVPLPQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0031901 early endosome membrane
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0016020 membrane
Cellular Component GO:0002102 podosome
Cellular Component GO:0098793 presynapse
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0008289 lipid binding
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Biological Process GO:0007417 central nervous system development
Biological Process GO:0006897 endocytosis
Biological Process GO:0061024 membrane organization
Biological Process GO:0007165 signal transduction
Biological Process GO:0048488 synaptic vesicle endocytosis
Biological Process GO:0072319 vesicle uncoating

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] 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.