Search Results

Overview

Uniprot IDQ9H0H5
Protein NameRac GTPase-activating protein 1
Gene NameRACGAP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
199 DGPPGPVKKTRSIGS
200 GPPGPVKKTRSIGSA
248 YWTRSRRKTGTLQPW
404 KEKFLRVKTVPLLSK
604 RVRSTLTKNTPRFGS
614 PRFGSKSKSATNLGR

Function

Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which regulates cleavage furrow ingression and abscission during cytokinesis (PubMed:18511905). Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity (PubMed:10979956). Has a critical role in erythropoiesis (PubMed:34818416). Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells

Protein Sequence

10 MDTMMLNVRN 20 LFEQLVRRVE 30 ILSEGNEVQF 40 IQLAKDFEDF 50 RKKWQRTDHE 60 LGKYKDLLMK 70 AETERSALDV 80 KLKHARNQVD 90 VEIKRRQRAE 100 ADCEKLERQI 110 QLIREMLMCD 120 TSGSIQLSEE 130 QKSALAFLNR 140 GQPSSSNAGN 150 KRLSTIDESG 160 SILSDISFDK 170 TDESLDWDSS 180 LVKTFKLKKR 190 EKRRSTSRQF 200 VDGPPGPVKK 210 TRSIGSAVDQ 220 GNESIVAKTT 230 VTVPNDGGPI 240 EAVSTIETVP 250 YWTRSRRKTG 260 TLQPWNSDST 270 LNSRQLEPRT 280 ETDSVGTPQS 290 NGGMRLHDFV 300 SKTVIKPESC 310 VPCGKRIKFG 320 KLSLKCRDCR 330 VVSHPECRDR 340 CPLPCIPTLI 350 GTPVKIGEGM 360 LADFVSQTSP 370 MIPSIVVHCV 380 NEIEQRGLTE 390 TGLYRISGCD 400 RTVKELKEKF 410 LRVKTVPLLS 420 KVDDIHAICS 430 LLKDFLRNLK 440 EPLLTFRLNR 450 AFMEAAEITD 460 EDNSIAAMYQ 470 AVGELPQANR 480 DTLAFLMIHL 490 QRVAQSPHTK 500 MDVANLAKVF 510 GPTIVAHAVP 520 NPDPVTMLQD 530 IKRQPKVVER 540 LLSLPLEYWS 550 QFMMVEQENI 560 DPLHVIENSN 570 AFSTPQTPDI 580 KVSLLGPVTT 590 PEHQLLKTPS 600 SSSLSQRVRS 610 TLTKNTPRFG 620 SKSKSATNLG 630 RQGNFFASPM LK

Gene Ontology

Classification GO ID Description
Biological Process GO:0007266 Rho protein signal transduction
Cellular Component GO:0001669 acrosomal vesicle
Cellular Component GO:0097149 centralspindlin complex
Cellular Component GO:0032154 cleavage furrow
Cellular Component GO:0009898 cytoplasmic side of plasma membrane
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0090543 Flemming body
Cellular Component GO:0005874 microtubule
Cellular Component GO:0030496 midbody
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0072686 mitotic spindle
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005819 spindle
Cellular Component GO:0051233 spindle midzone
Molecular Function GO:0043014 alpha-tubulin binding
Molecular Function GO:0048487 beta-tubulin binding
Molecular Function GO:0043015 gamma-tubulin binding
Molecular Function GO:0005096 GTPase activator activity
Molecular Function GO:0008017 microtubule binding
Molecular Function GO:0005547 phosphatidylinositol-3,4,5-trisphosphate binding
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0000915 actomyosin contractile ring assembly
Biological Process GO:0030218 erythrocyte differentiation
Biological Process GO:0000281 mitotic cytokinesis
Biological Process GO:0051256 mitotic spindle midzone assembly
Biological Process GO:0006811 monoatomic ion transport
Biological Process GO:0007405 neuroblast proliferation
Biological Process GO:0032467 positive regulation of cytokinesis
Biological Process GO:0051988 regulation of attachment of spindle microtubules to kinetochore
Biological Process GO:0045995 regulation of embryonic development
Biological Process GO:0051056 regulation of small GTPase mediated signal transduction
Biological Process GO:0007283 spermatogenesis
Biological Process GO:1902358 sulfate transmembrane transport

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] 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.

[3] 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.

[4] 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.

[5] 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.

[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.