Full text data of ARHGAP18
ARHGAP18
[Confidence: low (only semi-automatic identification from reviews)]
Rho GTPase-activating protein 18 (MacGAP; Rho-type GTPase-activating protein 18)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Rho GTPase-activating protein 18 (MacGAP; Rho-type GTPase-activating protein 18)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8N392
ID RHG18_HUMAN Reviewed; 663 AA.
AC Q8N392; E1P575; Q58EZ3; Q6P679; Q6PJD7; Q96S64;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Rho GTPase-activating protein 18;
DE AltName: Full=MacGAP;
DE AltName: Full=Rho-type GTPase-activating protein 18;
GN Name=ARHGAP18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-23.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP SPLICING (ISOFORM 2).
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-23.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-23.
RC TISSUE=Brain, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-663 (ISOFORM 1).
RC TISSUE=Mast cell;
RA Uchida T., Kuramasu A., Okumura K., Nakao A., Ogawa H., Ra C.;
RT "Molecular cloning and characterization of a novel GTPase activating
RT Protein that regulated mast cell degranulation.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH MPHOSPH6.
RX PubMed=15231747; DOI=10.1101/gr.2122004;
RA Lehner B., Sanderson C.M.;
RT "A protein interaction framework for human mRNA degradation.";
RL Genome Res. 14:1315-1323(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting
CC them to an inactive GDP-bound state (By similarity).
CC -!- SUBUNIT: Interacts with MPHOSPH6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N392-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N392-2; Sequence=VSP_052092;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17223.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH39611.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH62417.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=BAB61887.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL834511; CAD39167.2; -; mRNA.
DR EMBL; AL450310; CAH72298.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48076.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48077.1; -; Genomic_DNA.
DR EMBL; BC017223; AAH17223.1; ALT_SEQ; mRNA.
DR EMBL; BC039611; AAH39611.1; ALT_SEQ; mRNA.
DR EMBL; BC062417; AAH62417.1; ALT_SEQ; mRNA.
DR EMBL; BC101708; AAI01709.1; -; mRNA.
DR EMBL; BC107416; AAI07417.1; -; mRNA.
DR EMBL; BC111940; AAI11941.1; -; mRNA.
DR EMBL; AB053293; BAB61887.1; ALT_INIT; mRNA.
DR PIR; G59432; G59432.
DR RefSeq; NP_277050.2; NM_033515.2.
DR RefSeq; XP_005267269.1; XM_005267212.1.
DR UniGene; Hs.486458; -.
DR ProteinModelPortal; Q8N392; -.
DR SMR; Q8N392; 342-533.
DR IntAct; Q8N392; 2.
DR STRING; 9606.ENSP00000275189; -.
DR PhosphoSite; Q8N392; -.
DR DMDM; 296452981; -.
DR PaxDb; Q8N392; -.
DR PRIDE; Q8N392; -.
DR Ensembl; ENST00000368149; ENSP00000357131; ENSG00000146376.
DR GeneID; 93663; -.
DR KEGG; hsa:93663; -.
DR UCSC; uc003qbr.3; human.
DR CTD; 93663; -.
DR GeneCards; GC06M129897; -.
DR H-InvDB; HIX0006211; -.
DR HGNC; HGNC:21035; ARHGAP18.
DR HPA; HPA031595; -.
DR MIM; 613351; gene.
DR neXtProt; NX_Q8N392; -.
DR PharmGKB; PA134884487; -.
DR eggNOG; NOG329973; -.
DR HOGENOM; HOG000015106; -.
DR HOVERGEN; HBG072023; -.
DR InParanoid; Q8N392; -.
DR OMA; TANTMHL; -.
DR OrthoDB; EOG7ZGX3J; -.
DR Reactome; REACT_111102; Signal Transduction.
DR GenomeRNAi; 93663; -.
DR NextBio; 78204; -.
DR PRO; PR:Q8N392; -.
DR Bgee; Q8N392; -.
DR CleanEx; HS_ARHGAP18; -.
DR Genevestigator; Q8N392; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; GTPase activation;
KW Polymorphism; Reference proteome.
FT CHAIN 1 663 Rho GTPase-activating protein 18.
FT /FTId=PRO_0000245789.
FT DOMAIN 324 523 Rho-GAP.
FT VAR_SEQ 1 45 Missing (in isoform 2).
FT /FTId=VSP_052092.
FT VARIANT 23 23 T -> A (in dbSNP:rs3752536).
FT /FTId=VAR_060460.
FT VARIANT 91 91 N -> S (in dbSNP:rs11544371).
FT /FTId=VAR_060461.
FT VARIANT 165 165 Q -> H (in dbSNP:rs11544372).
FT /FTId=VAR_060462.
FT CONFLICT 307 307 K -> E (in Ref. 4; AAH17223).
FT CONFLICT 467 467 N -> K (in Ref. 4; AAH62417).
SQ SEQUENCE 663 AA; 74977 MW; 2DD127301026928D CRC64;
MSWLSSSQGV VLTAYHPSGK DQTVGNSHAK AGEEATSSRR YGQYTMNQES TTIKVMEKPP
FDRSISQDSL DELSMEDYWI ELENIKKSSE NSQEDQEVVV VKEPDEGELE EEWLKEAGLS
NLFGESAGDP QESIVFLSTL TRTQAAAVQK RVETVSQTLR KKNKQYQIPD VRDIFAQQRE
SKETAPGGTE SQSLRTNENK YQGRDDEASN LVGEEKLIPP EETPAPETDI NLEVSFAEQA
LNQKESSKEK IQKSKGDDAT LPSFRLPKDK TGTTRIGDLA PQDMKKVCHL ALIELTALYD
VLGIELKQQK AVKIKTKDSG LFCVPLTALL EQDQRKVPGM RIPLIFQKLI SRIEERGLET
EGLLRIPGAA IRIKNLCQEL EAKFYEGTFN WESVKQHDAA SLLKLFIREL PQPLLSVEYL
KAFQAVQNLP TKKQQLQALN LLVILLPDAN RDTLKALLEF LQRVIDNKEK NKMTVMNVAM
VMAPNLFMCH ALGLKSSEQR EFVMAAGTAN TMHLLIKYQK LLWTIPKFIV NQVRKQNTEN
HKKDKRAMKK LLKKMAYDRE KYEKQDKSTN DADVPQGVIR VQAPHLSKVS MAIQLTEELK
ASDVLARFLS QESGVAQTLK KGEVFLYEIG GNIGERCLDD DTYMKDLYQL NPNAEWVIKS
KPL
//
ID RHG18_HUMAN Reviewed; 663 AA.
AC Q8N392; E1P575; Q58EZ3; Q6P679; Q6PJD7; Q96S64;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Rho GTPase-activating protein 18;
DE AltName: Full=MacGAP;
DE AltName: Full=Rho-type GTPase-activating protein 18;
GN Name=ARHGAP18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-23.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP SPLICING (ISOFORM 2).
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-23.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ALA-23.
RC TISSUE=Brain, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-663 (ISOFORM 1).
RC TISSUE=Mast cell;
RA Uchida T., Kuramasu A., Okumura K., Nakao A., Ogawa H., Ra C.;
RT "Molecular cloning and characterization of a novel GTPase activating
RT Protein that regulated mast cell degranulation.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH MPHOSPH6.
RX PubMed=15231747; DOI=10.1101/gr.2122004;
RA Lehner B., Sanderson C.M.;
RT "A protein interaction framework for human mRNA degradation.";
RL Genome Res. 14:1315-1323(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting
CC them to an inactive GDP-bound state (By similarity).
CC -!- SUBUNIT: Interacts with MPHOSPH6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N392-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N392-2; Sequence=VSP_052092;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17223.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH39611.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH62417.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=BAB61887.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL834511; CAD39167.2; -; mRNA.
DR EMBL; AL450310; CAH72298.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48076.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48077.1; -; Genomic_DNA.
DR EMBL; BC017223; AAH17223.1; ALT_SEQ; mRNA.
DR EMBL; BC039611; AAH39611.1; ALT_SEQ; mRNA.
DR EMBL; BC062417; AAH62417.1; ALT_SEQ; mRNA.
DR EMBL; BC101708; AAI01709.1; -; mRNA.
DR EMBL; BC107416; AAI07417.1; -; mRNA.
DR EMBL; BC111940; AAI11941.1; -; mRNA.
DR EMBL; AB053293; BAB61887.1; ALT_INIT; mRNA.
DR PIR; G59432; G59432.
DR RefSeq; NP_277050.2; NM_033515.2.
DR RefSeq; XP_005267269.1; XM_005267212.1.
DR UniGene; Hs.486458; -.
DR ProteinModelPortal; Q8N392; -.
DR SMR; Q8N392; 342-533.
DR IntAct; Q8N392; 2.
DR STRING; 9606.ENSP00000275189; -.
DR PhosphoSite; Q8N392; -.
DR DMDM; 296452981; -.
DR PaxDb; Q8N392; -.
DR PRIDE; Q8N392; -.
DR Ensembl; ENST00000368149; ENSP00000357131; ENSG00000146376.
DR GeneID; 93663; -.
DR KEGG; hsa:93663; -.
DR UCSC; uc003qbr.3; human.
DR CTD; 93663; -.
DR GeneCards; GC06M129897; -.
DR H-InvDB; HIX0006211; -.
DR HGNC; HGNC:21035; ARHGAP18.
DR HPA; HPA031595; -.
DR MIM; 613351; gene.
DR neXtProt; NX_Q8N392; -.
DR PharmGKB; PA134884487; -.
DR eggNOG; NOG329973; -.
DR HOGENOM; HOG000015106; -.
DR HOVERGEN; HBG072023; -.
DR InParanoid; Q8N392; -.
DR OMA; TANTMHL; -.
DR OrthoDB; EOG7ZGX3J; -.
DR Reactome; REACT_111102; Signal Transduction.
DR GenomeRNAi; 93663; -.
DR NextBio; 78204; -.
DR PRO; PR:Q8N392; -.
DR Bgee; Q8N392; -.
DR CleanEx; HS_ARHGAP18; -.
DR Genevestigator; Q8N392; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; GTPase activation;
KW Polymorphism; Reference proteome.
FT CHAIN 1 663 Rho GTPase-activating protein 18.
FT /FTId=PRO_0000245789.
FT DOMAIN 324 523 Rho-GAP.
FT VAR_SEQ 1 45 Missing (in isoform 2).
FT /FTId=VSP_052092.
FT VARIANT 23 23 T -> A (in dbSNP:rs3752536).
FT /FTId=VAR_060460.
FT VARIANT 91 91 N -> S (in dbSNP:rs11544371).
FT /FTId=VAR_060461.
FT VARIANT 165 165 Q -> H (in dbSNP:rs11544372).
FT /FTId=VAR_060462.
FT CONFLICT 307 307 K -> E (in Ref. 4; AAH17223).
FT CONFLICT 467 467 N -> K (in Ref. 4; AAH62417).
SQ SEQUENCE 663 AA; 74977 MW; 2DD127301026928D CRC64;
MSWLSSSQGV VLTAYHPSGK DQTVGNSHAK AGEEATSSRR YGQYTMNQES TTIKVMEKPP
FDRSISQDSL DELSMEDYWI ELENIKKSSE NSQEDQEVVV VKEPDEGELE EEWLKEAGLS
NLFGESAGDP QESIVFLSTL TRTQAAAVQK RVETVSQTLR KKNKQYQIPD VRDIFAQQRE
SKETAPGGTE SQSLRTNENK YQGRDDEASN LVGEEKLIPP EETPAPETDI NLEVSFAEQA
LNQKESSKEK IQKSKGDDAT LPSFRLPKDK TGTTRIGDLA PQDMKKVCHL ALIELTALYD
VLGIELKQQK AVKIKTKDSG LFCVPLTALL EQDQRKVPGM RIPLIFQKLI SRIEERGLET
EGLLRIPGAA IRIKNLCQEL EAKFYEGTFN WESVKQHDAA SLLKLFIREL PQPLLSVEYL
KAFQAVQNLP TKKQQLQALN LLVILLPDAN RDTLKALLEF LQRVIDNKEK NKMTVMNVAM
VMAPNLFMCH ALGLKSSEQR EFVMAAGTAN TMHLLIKYQK LLWTIPKFIV NQVRKQNTEN
HKKDKRAMKK LLKKMAYDRE KYEKQDKSTN DADVPQGVIR VQAPHLSKVS MAIQLTEELK
ASDVLARFLS QESGVAQTLK KGEVFLYEIG GNIGERCLDD DTYMKDLYQL NPNAEWVIKS
KPL
//
MIM
613351
*RECORD*
*FIELD* NO
613351
*FIELD* TI
*613351 RHO GTPase-ACTIVATING PROTEIN 18; ARHGAP18
*FIELD* TX
DESCRIPTION
ARHGAP18 belongs to a family of Rho (see 165390) GTPase-activating
read moreproteins that modulate cell signaling (Potkin et al., 2009).
CLONING
By PCR of a human epididymis cDNA library using primers based on rhesus
MacGAP, Li et al. (2008) cloned ARHGAP18. The deduced 618-amino acid
protein has a calculated molecular mass of 70 kD. It has a putative Rho
(RHOA; 165390) GAP domain in its C-terminal half and 34 potential
phosphorylation sites. Immunohistochemical analysis of human epididymis
revealed MacGAP expression in epithelial cells in distal caput, with
concentration near the basal membrane, but not in any other tissue
examined. Western blot analysis of caput region of epididymis detected
MacGAP at an apparent molecular mass of 70 kD.
Using Western blot analysis, Maeda et al. (2011) detected variable
expression of 2 ARHGAP18 proteins at an apparent molecular mass of 90 kD
in all human cell lines examined. The faster migrating protein was
predicted to initiate from met55. Two Arhgap18 proteins were also
detected in all mouse tissues examined except small intestine.
Endogenous or fluorescence-tagged ARHGAP18 showed a diffuse cytoplasmic
distribution in HeLa cells, with concentration at the edge of membrane
protrusions during cell spreading. ARHGAP18 also localized to the
leading edge of migrating human fibroblasts or breast cancer cells in a
wound healing assay.
GENE FUNCTION
Maeda et al. (2011) found that knockdown of ARHGAP18 by small
interfering RNA in human cell lines increased the number of actin stress
fibers and impaired cell spreading, migration, and cell polarization
required for migration. Overexpression of ARHGAP18 had the opposite
effect. The GAP domain and catalytic arg365 were required for ARGHAP18
effects. Protein pull-down assays revealed that ARHGAP18 interacted with
active RHOA, and overexpression of ARHGAP18 in HeLa cells reduced the
activity of RHOA, but not RAC1 (602048) or CDC42 (116952). Expression of
a dominant-negative RHOA suppressed stress fiber formation by ARHGAP18.
Neisch et al. (2013) found that Drosophila conundrum (Conu), an ortholog
of human ARHGAP18, preferentially localized to apical cortex in
Drosophila epithelium and immunoprecipitated with the
cytoskeleton-regulating protein moesin (MSN; 309845) from S2 Drosophila
epithelial cells. Moesin recruited Conu to the cell cortex, and cortical
Conu functioned as a GAP for Rho1, an ortholog of RHOA, inhibiting Rho1
activity. Coexpression of moesin and Conu led to overgrowth and
convoluted folding of epithelium in vivo. Conu also induced
overproliferation by synergistically functioning with the small GTPase
Arf6 (600464) to promote activation of Rac1. Neisch et al. (2013)
concluded that moesin regulates epithelial growth by recruiting Conu to
the cell cortex, resulting in Rho1 inhibition and Rac1 activation.
MAPPING
By genomic sequence analysis, Potkin et al. (2009) mapped the ARHGAP18
gene to chromosome 6q22-q24.
*FIELD* RF
1. Li, X.; Liu, Q.; Liu, S.; Zhang, J.; Zhang, Y.: New member of
the guanosine triphosphatase activating protein family in the human
epididymis. Acta Biochim. Biophys. Sin. 40: 855-863, 2008.
2. Maeda, M.; Hasegawa, H.; Hyodo, T.; Ito, S.; Asano, E.; Yuang,
H.; Funasaka, K.; Shimokata, K.; Hasegawa, Y.; Hamaguchi, M.; Senga,
T.: ARHGAP18, a GTPase-activating protein for RhoA, controls cell
shape, spreading, and motility. Molec. Biol. Cell 22: 3840-3852,
2011.
3. Neisch, A. L.; Formstecher, E.; Fehon, R. G.: Conundrum, an ARHGAP18
orthologue, regulates RhoA and proliferation through interactions
with moesin. Molec. Biol. Cell 24: 1420-1433, 2013.
4. Potkin, S. G.; Turner, J. A.; Fallon, J. A.; Lakatos, A.; Keator,
D. B.; Guffanti, G.; Macciardi, F.; Functional Imaging Biomedical
Informatics Research Network: Gene discovery through imaging genetics:
identification of two novel genes associated with schizophrenia. Molec.
Psychiat. 14: 416-428, 2009.
*FIELD* CN
Patricia A. Hartz - updated: 11/26/2013
Patricia A. Hartz - updated: 7/9/2013
*FIELD* CD
Patricia A. Hartz: 4/9/2010
*FIELD* ED
mgross: 11/26/2013
mcolton: 11/25/2013
alopez: 7/10/2013
tpirozzi: 7/9/2013
mgross: 4/9/2010
*RECORD*
*FIELD* NO
613351
*FIELD* TI
*613351 RHO GTPase-ACTIVATING PROTEIN 18; ARHGAP18
*FIELD* TX
DESCRIPTION
ARHGAP18 belongs to a family of Rho (see 165390) GTPase-activating
read moreproteins that modulate cell signaling (Potkin et al., 2009).
CLONING
By PCR of a human epididymis cDNA library using primers based on rhesus
MacGAP, Li et al. (2008) cloned ARHGAP18. The deduced 618-amino acid
protein has a calculated molecular mass of 70 kD. It has a putative Rho
(RHOA; 165390) GAP domain in its C-terminal half and 34 potential
phosphorylation sites. Immunohistochemical analysis of human epididymis
revealed MacGAP expression in epithelial cells in distal caput, with
concentration near the basal membrane, but not in any other tissue
examined. Western blot analysis of caput region of epididymis detected
MacGAP at an apparent molecular mass of 70 kD.
Using Western blot analysis, Maeda et al. (2011) detected variable
expression of 2 ARHGAP18 proteins at an apparent molecular mass of 90 kD
in all human cell lines examined. The faster migrating protein was
predicted to initiate from met55. Two Arhgap18 proteins were also
detected in all mouse tissues examined except small intestine.
Endogenous or fluorescence-tagged ARHGAP18 showed a diffuse cytoplasmic
distribution in HeLa cells, with concentration at the edge of membrane
protrusions during cell spreading. ARHGAP18 also localized to the
leading edge of migrating human fibroblasts or breast cancer cells in a
wound healing assay.
GENE FUNCTION
Maeda et al. (2011) found that knockdown of ARHGAP18 by small
interfering RNA in human cell lines increased the number of actin stress
fibers and impaired cell spreading, migration, and cell polarization
required for migration. Overexpression of ARHGAP18 had the opposite
effect. The GAP domain and catalytic arg365 were required for ARGHAP18
effects. Protein pull-down assays revealed that ARHGAP18 interacted with
active RHOA, and overexpression of ARHGAP18 in HeLa cells reduced the
activity of RHOA, but not RAC1 (602048) or CDC42 (116952). Expression of
a dominant-negative RHOA suppressed stress fiber formation by ARHGAP18.
Neisch et al. (2013) found that Drosophila conundrum (Conu), an ortholog
of human ARHGAP18, preferentially localized to apical cortex in
Drosophila epithelium and immunoprecipitated with the
cytoskeleton-regulating protein moesin (MSN; 309845) from S2 Drosophila
epithelial cells. Moesin recruited Conu to the cell cortex, and cortical
Conu functioned as a GAP for Rho1, an ortholog of RHOA, inhibiting Rho1
activity. Coexpression of moesin and Conu led to overgrowth and
convoluted folding of epithelium in vivo. Conu also induced
overproliferation by synergistically functioning with the small GTPase
Arf6 (600464) to promote activation of Rac1. Neisch et al. (2013)
concluded that moesin regulates epithelial growth by recruiting Conu to
the cell cortex, resulting in Rho1 inhibition and Rac1 activation.
MAPPING
By genomic sequence analysis, Potkin et al. (2009) mapped the ARHGAP18
gene to chromosome 6q22-q24.
*FIELD* RF
1. Li, X.; Liu, Q.; Liu, S.; Zhang, J.; Zhang, Y.: New member of
the guanosine triphosphatase activating protein family in the human
epididymis. Acta Biochim. Biophys. Sin. 40: 855-863, 2008.
2. Maeda, M.; Hasegawa, H.; Hyodo, T.; Ito, S.; Asano, E.; Yuang,
H.; Funasaka, K.; Shimokata, K.; Hasegawa, Y.; Hamaguchi, M.; Senga,
T.: ARHGAP18, a GTPase-activating protein for RhoA, controls cell
shape, spreading, and motility. Molec. Biol. Cell 22: 3840-3852,
2011.
3. Neisch, A. L.; Formstecher, E.; Fehon, R. G.: Conundrum, an ARHGAP18
orthologue, regulates RhoA and proliferation through interactions
with moesin. Molec. Biol. Cell 24: 1420-1433, 2013.
4. Potkin, S. G.; Turner, J. A.; Fallon, J. A.; Lakatos, A.; Keator,
D. B.; Guffanti, G.; Macciardi, F.; Functional Imaging Biomedical
Informatics Research Network: Gene discovery through imaging genetics:
identification of two novel genes associated with schizophrenia. Molec.
Psychiat. 14: 416-428, 2009.
*FIELD* CN
Patricia A. Hartz - updated: 11/26/2013
Patricia A. Hartz - updated: 7/9/2013
*FIELD* CD
Patricia A. Hartz: 4/9/2010
*FIELD* ED
mgross: 11/26/2013
mcolton: 11/25/2013
alopez: 7/10/2013
tpirozzi: 7/9/2013
mgross: 4/9/2010