Search Results

Overview

Uniprot IDQ92609
Protein NameTBC1 domain family member 5
Gene NameTBC1D5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
448 NKSRTNAKGAPLNIN
519 QQQQRLMKSESMPVQ
534 LNKGLSSKNISSSPS
562 PPSSATKKDSFFSNI

Function

May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity (PubMed:19531583, PubMed:20923837). Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy (PubMed:22354992). May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (PubMed:24603492)

Protein Sequence

10 MYHSLSETRH 20 PLQPEEQEVG 30 IDPLSSYSNK 40 SGGDSNKNGR 50 RTSSTLDSEG 60 TFNSYRKEWE 70 ELFVNNNYLA 80 TIRQKGINGQ 90 LRSSRFRSIC 100 WKLFLCVLPQ 110 DKSQWISRIE 120 ELRAWYSNIK 130 EIHITNPRKV 140 VGQQDLMINN 150 PLSQDEGSLW 160 NKFFQDKELR 170 SMIEQDVKRT 180 FPEMQFFQQE 190 NVRKILTDVL 200 FCYARENEQL 210 LYKQGMHELL 220 APIVFVLHCD 230 HQAFLHASES 240 AQPSEEMKTV 250 LNPEYLEHDA 260 YAVFSQLMET 270 AEPWFSTFEH 280 DGQKGKETLM 290 TPIPFARPQD 300 LGPTIAIVTK 310 VNQIQDHLLK 320 KHDIELYMHL 330 NRLEIAPQIY 340 GLRWVRLLFG 350 REFPLQDLLV 360 VWDALFADGL 370 SLGLVDYIFV 380 AMLLYIRDAL 390 ISSNYQTCLG 400 LLMHYPFIGD 410 VHSLILKALF 420 LRDPKRNPRP 430 VTYQFHPNLD 440 YYKARGADLM 450 NKSRTNAKGA 460 PLNINKVSNS 470 LINFGRKLIS 480 PAMAPGSAGG 490 PVPGGNSSSS 500 SSVVIPTRTS 510 AEAPSHHLQQ 520 QQQQQRLMKS 530 ESMPVQLNKG 540 LSSKNISSSP 550 SVESLPGGRE 560 FTGSPPSSAT 570 KKDSFFSNIS 580 RSRSHSKTMG 590 RKESEEELEA 600 QISFLQGQLN 610 DLDAMCKYCA 620 KVMDTHLVNI 630 QDVILQENLE 640 KEDQILVSLA 650 GLKQIKDILK 660 GSLRFNQSQL 670 EAEENEQITI 680 ADNHYCSSGQ 690 GQGRGQGQSV 700 QMSGAIKQAS 710 SETPGCTDRG 720 NSDDFILISK 730 DDDGSSARGS 740 FSGQAQPLRT 750 LRSTSGKSQA 760 PVCSPLVFSD 770 PLMGPASASS 780 SNPSSSPDDD 790 SSKDSGFTIV SPLDI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005776 autophagosome
Cellular Component GO:0005829 cytosol
Cellular Component GO:0010008 endosome membrane
Cellular Component GO:0005794 Golgi apparatus
Cellular Component GO:0030904 retromer complex
Molecular Function GO:0035612 AP-2 adaptor complex binding
Molecular Function GO:0005096 GTPase activator activity
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:1905394 retromer complex binding
Biological Process GO:0006914 autophagy
Biological Process GO:0016236 macroautophagy
Biological Process GO:0002092 positive regulation of receptor internalization
Biological Process GO:0015031 protein transport
Biological Process GO:0042594 response to starvation
Biological Process GO:0042147 retrograde transport, endosome to Golgi

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] 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.

[3] 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.