RACGAP1
entrez
29127
canonical
uniprot
Q9H0H5
canonical
ensembl
ENSG00000161800
resolver
ensp
ENSP00000309871
resolver
ensp
ENSP00000404190
resolver
ensp
ENSP00000404808
resolver
ensp
ENSP00000449370
resolver
ensp
ENSP00000449374
resolver
ensp
ENSP00000553786
resolver
ensp
ENSP00000553787
resolver
ensp
ENSP00000553789
resolver
ensp
ENSP00000553790
resolver
ensp
ENSP00000553793
resolver
ensp
ENSP00000553795
resolver
ensp
ENSP00000553796
resolver
ensp
ENSP00000591856
resolver
ensp
ENSP00000591857
resolver
ensp
ENSP00000591858
resolver
ensp
ENSP00000591859
resolver
ensp
ENSP00000591860
resolver
ensp
ENSP00000591861
resolver
ensp
ENSP00000591863
resolver
ensp
ENSP00000591864
resolver
ensp
ENSP00000621167
resolver
enst
ENST00000312377
resolver
enst
ENST00000427314
resolver
enst
ENST00000454520
resolver
enst
ENST00000547905
resolver
enst
ENST00000551016
resolver
enst
ENST00000883727
resolver
enst
ENST00000883728
resolver
enst
ENST00000883730
resolver
enst
ENST00000883731
resolver
enst
ENST00000883734
resolver
enst
ENST00000883736
resolver
enst
ENST00000883737
resolver
enst
ENST00000921797
resolver
enst
ENST00000921798
resolver
enst
ENST00000921799
resolver
enst
ENST00000921800
resolver
enst
ENST00000921801
resolver
enst
ENST00000921802
resolver
enst
ENST00000921804
resolver
enst
ENST00000921805
resolver
enst
ENST00000951108
resolver
genesymbol
RACGAP1
resolver
genesymbol_syn
KIAA1478
resolver
genesymbol_syn
MGCRACGAP
resolver
hgnc
HGNC:9804
resolver
uniprot
B2RE34
resolver
uniprot
Q6PJ26
resolver
uniprot
Q9NWN2
resolver
uniprot
Q9P250
resolver
uniprot
Q9P2W2
resolver
uniprot_entry
B2RE34_HUMAN
resolver
uniprot_entry
RGAP1_HUMAN
resolver
uniprot_sec
Q6PJ26
resolver
uniprot_sec
Q9NWN2
resolver
uniprot_sec
Q9P250
resolver
uniprot_sec
Q9P2W2
resolver
amino_acid_sequence
MDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREMLMCDTSGSIQLSEEQKSALAFLNRGQPSSSNAGNKRLSTIDESGSILSDISFDKTDESLDWDSSLVKTFKLKKREKRRSTSRQFVDGPPGPVKKTRSIGSAVDQGNESIVAKTTVTVPNDGGPIEAVSTIETVPYWTRSRRKTGTLQPWNSDSTLNSRQLEPRTETDSVGTPQSNGGMRLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIPTLIGTPVKIGEGMLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPHTKMDVANLAKVFGPTIVAHAVPNPDPVTMLQDIKRQPKVVERLLSLPLEYWSQFMMVEQENIDPLHVIENSNAFSTPQTPDIKVSLLGPVTTPEHQLLKTPSSSSLSQRVRSTLTKNTPRFGSKSKSATNLGRQGNFFASPMLK
uniprot
proteins
disease_involvement
DISEASE: Anemia, congenital dyserythropoietic, 3B, autosomal recessive (CDAN3B) [MIM:619789]: An autosomal recessive blood disorder characterized by marked dyserythropoiesis, hemolytic anemia, macrocytosis in the peripheral blood, and giant multinucleated erythroblasts in the bone marrow. {ECO:0000269|PubMed:34818416}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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. {ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:11085985, ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11782313, ECO:0000269|PubMed:14729465, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16129829, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:23235882, ECO:0000269|PubMed:9497316}.
uniprot
proteins
mass_dalton
71027
uniprot
proteins
mutagenesis
MUTAGEN 149; /note="S->A: Does not inhibit interaction with ECT2. Strongly reduces phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170."; /evidence="ECO:0000269|PubMed:19468300"; MUTAGEN 157; /note="S->A: Does not inhibit interaction with ECT2. Strongly reduces phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-164 and A-170. Strongly reduces phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-164; A-170 and A-214."; /evidence="ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302"; MUTAGEN 164; /note="S->A: Does not inhibit interaction with ECT2. Strongly reduces phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-170. Strongly reduces phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-170 and A-214."; /evidence="ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302"; MUTAGEN 167; /note="W->A: More than 20-fold reduction in binding to ECT2."; /evidence="ECO:0000269|PubMed:25068414"; MUTAGEN 170; /note="S->A: Does not inhibit interaction with ECT2. Strongly reduces phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-164. Strongly reduces phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-214."; /evidence="ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302"; MUTAGEN 214; /note="S->A: Strongly reduces phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170."; /evidence="ECO:0000269|PubMed:19468302"; MUTAGEN 289; /note="F->G: Cytokinesis failure."; /evidence="ECO:0000269|PubMed:23235882"; MUTAGEN 292; /note="K->L: Cytokinesis failure. Abolishes localization at the cell membrane."; /evidence="ECO:0000269|PubMed:23235882"; MUTAGEN 306; /note="R->L: Cytokinesis failure. Abolishes localization at the cell membrane."; /evidence="ECO:0000269|PubMed:23235882"; MUTAGEN 309; /note="F->A: Cytokinesis failure. Abolishes localization at the cell membrane."; /evidence="ECO:0000269|PubMed:23235882"; MUTAGEN 316; /note="C->G: Cytokinesis failure."; /evidence="ECO:0000269|PubMed:23235882"; MUTAGEN 385; /note="R->A: Abolishes GAP activity towards RAC1. Abolishes GAP activity towards CDC42 in prometaphase. Abolishes GAP activity towards RHOA. Induces multiple blebs during cytokinesis."; /evidence="ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:14729465, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:34818416
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at multiple sites in the midbody during cytokinesis (PubMed:12689593). Phosphorylation by AURKB on Ser-387 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA (PubMed:12689593). Phosphorylation on multiple serine residues by PLK1 enhances its association with ECT2 and is critical for cleavage furrow formation (PubMed:19468300, PubMed:19468302). Phosphorylation on Ser-164 plays a major role in mediating interaction with ECT2 (PubMed:25068414). Phosphorylation on Ser-157 does not appear to contribute to binding to ECT2 (PubMed:25068414). {ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:25068414}.
uniprot
proteins
pubmed
10819331
uniprot
proteins
pubmed
10979956
uniprot
proteins
pubmed
11085985
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11278976
uniprot
proteins
pubmed
11782313
uniprot
proteins
pubmed
12590651
uniprot
proteins
pubmed
12689593
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14729465
uniprot
proteins
pubmed
14744859
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15642749
uniprot
proteins
pubmed
16103226
uniprot
proteins
pubmed
16129829
uniprot
proteins
pubmed
16213214
uniprot
proteins
pubmed
16236794
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18445686
uniprot
proteins
pubmed
18511905
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19468300
uniprot
proteins
pubmed
19468302
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23235882
uniprot
proteins
pubmed
25068414
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
34818416
uniprot
proteins
pubmed
36825683
uniprot
proteins
pubmed
41361016
uniprot
proteins
pubmed
9497316
uniprot
proteins
sequence_length
632
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18445686}. Cytoplasm. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18445686}. Cytoplasmic vesicle, secretory vesicle, acrosome. Cleavage furrow. Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Midbody {ECO:0000269|PubMed:36825683, ECO:0000269|PubMed:41361016}. Note=Colocalizes with RND2 in Golgi-derived proacrosomal vesicles and the acrosome (By similarity). During interphase, localized to the nucleus and cytoplasm along with microtubules, in anaphase, is redistributed to the central spindle and, in telophase and cytokinesis, to the midbody ring, also called Flemming body. Colocalizes with RHOA at the myosin contractile ring during cytokinesis. Colocalizes with ECT2 to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalizes with Cdc42 to spindle microtubules from prometaphase to telophase. Localizes to the midbody in a KIF23 and PRC1-dependent manner. {ECO:0000250|UniProtKB:Q9WVM1, ECO:0000269|PubMed:36825683}.
uniprot
proteins