Search Results

Overview

Uniprot IDQ9H2M9
Protein NameRab3 GTPase-activating protein non-catalytic subunit
Gene NameRAB3GAP2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
567 LAALLKTKSPNLDLV
913 KGNTQTSKVSSLQAE

Function

Regulatory subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of RAB3GAP1 and RAB3GAP2, which accelerates the otherwise slow GTP hydrolysis catalyzed by Rab proteins (PubMed:9733780, PubMed:39779760). The complex has GTPase-activating protein (GAP) activity towards various Rab3 subfamily members (RAB3A, RAB3B, RAB3C and RAB3D), RAB5A and RAB43, and has guanine nucleotide exchange factor (GEF) activity towards RAB18 (PubMed:9733780, PubMed:39779760, PubMed:24891604). The Rab3GAP complex acts as a GEF for RAB18 by promoting GDP release from RAB18 and the conversion of inactive RAB18-GDP to the active form RAB18-GTP (PubMed:39779760, PubMed:24891604). Recruits and stabilizes RAB18 at the cis-Golgi membrane in human fibroblasts where RAB18 is most likely activated (PubMed:26063829). Also involved in RAB18 recruitment at the endoplasmic reticulum (ER) membrane where it maintains proper ER structure (PubMed:24891604). Required for normal eye and brain development (By similarity). May participate in neurodevelopmental processes such as cell proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (By similarity)

Protein Sequence

10 MACSIVQFCY 20 FQDLQAARDF 30 LFPHLREEIL 40 SGALRRDPSK 50 STDWEDDGWG 60 AWEENEPQEP 70 EEEGNTCKTQ 80 KTSWLQDCVL 90 SLSPTNDLMV 100 IAREQKAVFL 110 VPKWKYSDKG 120 KEEMQFAVGW 130 SGSLNVEEGE 140 CVTSALCIPL 150 ASQKRSSTGR 160 PDWTCIVVGF 170 TSGYVRFYTE 180 NGVLLLAQLL 190 NEDPVLQLKC 200 RTYEIPRHPG 210 VTEQNEELSI 220 LYPAAIVTID 230 GFSLFQSLRA 240 CRNQVAKAAA 250 SGNENIQPPP 260 LAYKKWGLQD 270 IDTIIDHASV 280 GIMTLSPFDQ 290 MKTASNIGGF 300 NAAIKNSPPA 310 MSQYITVGSN 320 PFTGFFYALE 330 GSTQPLLSHV 340 ALAVASKLTS 350 ALFNAASGWL 360 GWKSKHEEEA 370 VQKQKPKVEP 380 ATPLAVRFGL 390 PDSRRHGESI 400 CLSPCNTLAA 410 VTDDFGRVIL 420 LDVARGIAIR 430 MWKGYRDAQI 440 GWIQTVEDLH 450 ERVPEKADFS 460 PFGNSQGPSR 470 VAQFLVIYAP 480 RRGILEVWST 490 QQGPRVGAFN 500 VGKHCRLLYP 510 GYKIMGLNNV 520 TSQSWQPQTY 530 QICLVDPVSG 540 SVKTVNVPFH 550 LALSDKKSER 560 AKDMHLVKKL 570 AALLKTKSPN 580 LDLVETEIKE 590 LILDIKYPAT 600 KKQALESILA 610 SERLPFSCLR 620 NITQTLMDTL 630 KSQELESVDE 640 GLLQFCANKL 650 KLLQLYESVS 660 QLNSLDFHLD 670 TPFSDNDLAL 680 LLRLDEKELL 690 KLQALLEKYK 700 QENTRTNVRF 710 SDDKDGVLPV 720 KTFLEYLEYE 730 KDVLNIKKIS 740 EEEYVALGSF 750 FFWKCLHGES 760 STEDMCHTLE 770 SAGLSPQLLL 780 SLLLSVWLSK 790 EKDILDKPQS 800 ICCLHTMLSL 810 LSKMKVAIDE 820 TWDSQSVSPW 830 WQQMRTACIQ 840 SENNGAALLS 850 AHVGHSVAAQ 860 ISNNMTEKKF 870 SQTVLGADSE 880 ALTDSWEALS 890 LDTEYWKLLL 900 KQLEDCLILQ 910 TLLHSKGNTQ 920 TSKVSSLQAE 930 PLPRLSVKKL 940 LEGGKGGIAD 950 SVAKWIFKQD 960 FSPEVLKLAN 970 EERDAENPDE 980 PKEGVNRSFL 990 EVSEMEMDLG 1000 AIPDLLHLAY 1010 EQFPCSLELD 1020 VLHAHCCWEY 1030 VVQWNKDPEE 1040 ARFFVRSIEH 1050 LKQIFNAHVQ 1060 NGIALMMWNT 1070 FLVKRFSAAT 1080 YLMDKVGKSP 1090 KDRLCRRDVG 1100 MSDTAMTSFL 1110 GSCLDLLQIL 1120 MEADVSRDEI 1130 QVPVLDTEDA 1140 WLSVEGPISI 1150 VELALEQKHI 1160 HYPLVEHHSI 1170 LCSILYAVMR 1180 FSLKTVKPLS 1190 LFDSKGKNAF 1200 FKDLTSIQLL 1210 PSGEMDPNFI 1220 SVRQQFLLKV 1230 VSAAVQAQHS 1240 ATKVKDPTEE 1250 ATPTPFGKDQ 1260 DWPALAVDLA 1270 HHLQVSEDVV 1280 RRHYVGELYN 1290 YGVDHLGEEA 1300 ILQVHDKEVL 1310 ASQLLVLTGQ 1320 RLAHALLHTQ 1330 TKEGMELLAR 1340 LPPTLCTWLK 1350 AMDPQDLQNT 1360 EVPIATTAKL 1370 VNKVIELLPE 1380 KHGQYGLALH 1390 LIEAVEAISL PSL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005776 autophagosome
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0042734 presynaptic membrane
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0008047 enzyme activator activity
Molecular Function GO:0030234 enzyme regulator activity
Molecular Function GO:0005096 GTPase activator activity
Molecular Function GO:0031267 small GTPase binding
Biological Process GO:0097051 establishment of protein localization to endoplasmic reticulum membrane
Biological Process GO:0006886 intracellular protein transport
Biological Process GO:0016236 macroautophagy
Biological Process GO:2000786 positive regulation of autophagosome assembly
Biological Process GO:1903373 positive regulation of endoplasmic reticulum tubular network organization
Biological Process GO:1903061 positive regulation of protein lipidation
Biological Process GO:0043087 regulation of GTPase activity
Biological Process GO:0099536 synaptic signaling

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 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.

[3] 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.

[4] 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.

[5] 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.