Search Results

Overview

Uniprot IDQ9Y5K6
Protein NameCD2-associated protein
Gene NameCD2AP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
221 IGFGDIFKEGSVKLR
267 TKTDTEGKIKAKEYC
360 ELIAAEKKYFSLKPE
369 FSLKPEEKDEKSTLE
397 KKPTPPTKASNLLRS
444 FETEPVSKLKLDSEQ
446 TEPVSKLKLDSEQLP
537 LKPSELKKDTCYSPK
544 KDTCYSPKPSVYLST

Function

Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (PubMed:10339567). In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (By similarity). May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (By similarity). May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis (PubMed:15800069). Plays a role in epithelial cell junctions formation (PubMed:22891260)

Protein Sequence

10 MVDYIVEYDY 20 DAVHDDELTI 30 RVGEIIRNVK 40 KLQEEGWLEG 50 ELNGRRGMFP 60 DNFVKEIKRE 70 TEFKDDSLPI 80 KRERHGNVAS 90 LVQRISTYGL 100 PAGGIQPHPQ 110 TKNIKKKTKK 120 RQCKVLFEYI 130 PQNEDELELK 140 VGDIIDINEE 150 VEEGWWSGTL 160 NNKLGLFPSN 170 FVKELEVTDD 180 GETHEAQDDS 190 ETVLAGPTSP 200 IPSLGNVSET 210 ASGSVTQPKK 220 IRGIGFGDIF 230 KEGSVKLRTR 240 TSSSETEEKK 250 PEKPLILQSL 260 GPKTQSVEIT 270 KTDTEGKIKA 280 KEYCRTLFAY 290 EGTNEDELTF 300 KEGEIIHLIS 310 KETGEAGWWR 320 GELNGKEGVF 330 PDNFAVQINE 340 LDKDFPKPKK 350 PPPPAKAPAP 360 KPELIAAEKK 370 YFSLKPEEKD 380 EKSTLEQKPS 390 KPAAPQVPPK 400 KPTPPTKASN 410 LLRSSGTVYP 420 KRPEKPVPPP 430 PPIAKINGEV 440 SSISSKFETE 450 PVSKLKLDSE 460 QLPLRPKSVD 470 FDSLTVRTSK 480 ETDVVNFDDI 490 ASSENLLHLT 500 ANRPKMPGRR 510 LPGRFNGGHS 520 PTHSPEKILK 530 LPKEEDSANL 540 KPSELKKDTC 550 YSPKPSVYLS 560 TPSSASKANT 570 TAFLTPLEIK 580 AKVETDDVKK 590 NSLDELRAQI 600 IELLCIVEAL 610 KKDHGKELEK 620 LRKDLEEEKT 630 MRSNLEMEIE KLKKAVLSS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0030424 axon
Cellular Component GO:0031252 cell leading edge
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0030425 dendrite
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0031941 filamentous actin
Cellular Component GO:0030426 growth cone
Cellular Component GO:0005770 late endosome
Cellular Component GO:0031594 neuromuscular junction
Cellular Component GO:0005641 nuclear envelope lumen
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0002102 podosome
Cellular Component GO:0001726 ruffle
Cellular Component GO:0036057 slit diaphragm
Cellular Component GO:0032588 trans-Golgi network membrane
Cellular Component GO:0031982 vesicle
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0030276 clathrin binding
Molecular Function GO:0036312 phosphatidylinositol 3-kinase regulatory subunit binding
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0017124 SH3 domain binding
Molecular Function GO:0005200 structural constituent of cytoskeleton
Biological Process GO:0007015 actin filament organization
Biological Process GO:0051301 cell division
Biological Process GO:0016477 cell migration
Biological Process GO:0051058 negative regulation of small GTPase mediated signal transduction
Biological Process GO:0050714 positive regulation of protein secretion
Biological Process GO:0065003 protein-containing complex assembly
Biological Process GO:0007165 signal transduction
Biological Process GO:0006930 substrate-dependent cell migration, cell extension
Biological Process GO:0050808 synapse 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] 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] 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.