RHG23_HUMAN
ID RHG23_HUMAN Reviewed; 1491 AA.
AC Q9P227;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Rho GTPase-activating protein 23;
DE AltName: Full=Rho-type GTPase-activating protein 23;
GN Name=ARHGAP23; Synonyms=KIAA1501;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 410-1491 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15254754;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human ARHGAP23 gene in silico.";
RL Int. J. Oncol. 25:535-540(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-372; SER-423 AND
RP SER-677, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-854, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P227-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P227-2; Sequence=VSP_023708, VSP_023709;
CC -!- TISSUE SPECIFICITY: Expressed in placenta, prostate, hippocampus and
CC brain medulla. Also expressed in brain tumor, salivary gland tumor,
CC head and neck tumor. {ECO:0000269|PubMed:15254754}.
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DR EMBL; AC115090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB040934; BAA96025.1; -; mRNA.
DR CCDS; CCDS56027.1; -. [Q9P227-1]
DR PIR; A59434; A59434.
DR RefSeq; NP_001186346.1; NM_001199417.1. [Q9P227-1]
DR AlphaFoldDB; Q9P227; -.
DR SMR; Q9P227; -.
DR BioGRID; 121677; 61.
DR IntAct; Q9P227; 23.
DR MINT; Q9P227; -.
DR STRING; 9606.ENSP00000481862; -.
DR iPTMnet; Q9P227; -.
DR PhosphoSitePlus; Q9P227; -.
DR SwissPalm; Q9P227; -.
DR BioMuta; ARHGAP23; -.
DR EPD; Q9P227; -.
DR jPOST; Q9P227; -.
DR MassIVE; Q9P227; -.
DR MaxQB; Q9P227; -.
DR PaxDb; Q9P227; -.
DR PeptideAtlas; Q9P227; -.
DR PRIDE; Q9P227; -.
DR ProteomicsDB; 83718; -. [Q9P227-1]
DR ProteomicsDB; 83719; -. [Q9P227-2]
DR Antibodypedia; 73731; 36 antibodies from 16 providers.
DR DNASU; 57636; -.
DR Ensembl; ENST00000610551.2; ENSP00000479208.1; ENSG00000273780.2. [Q9P227-1]
DR Ensembl; ENST00000620417.4; ENSP00000482992.1; ENSG00000275832.5. [Q9P227-2]
DR Ensembl; ENST00000622683.5; ENSP00000481862.1; ENSG00000275832.5. [Q9P227-1]
DR Ensembl; ENST00000631799.1; ENSP00000488428.1; ENSG00000273780.2. [Q9P227-2]
DR GeneID; 57636; -.
DR KEGG; hsa:57636; -.
DR MANE-Select; ENST00000622683.5; ENSP00000481862.1; NM_001199417.2; NP_001186346.1.
DR UCSC; uc021twd.2; human. [Q9P227-1]
DR CTD; 57636; -.
DR DisGeNET; 57636; -.
DR GeneCards; ARHGAP23; -.
DR HGNC; HGNC:29293; ARHGAP23.
DR HPA; ENSG00000275832; Tissue enhanced (brain).
DR MIM; 610590; gene.
DR neXtProt; NX_Q9P227; -.
DR OpenTargets; ENSG00000275832; -.
DR VEuPathDB; HostDB:ENSG00000275832; -.
DR eggNOG; KOG4407; Eukaryota.
DR GeneTree; ENSGT00940000157982; -.
DR HOGENOM; CLU_001776_1_0_1; -.
DR InParanoid; Q9P227; -.
DR OMA; WHRARSE; -.
DR OrthoDB; 142586at2759; -.
DR PhylomeDB; Q9P227; -.
DR TreeFam; TF329345; -.
DR PathwayCommons; Q9P227; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q9P227; -.
DR SIGNOR; Q9P227; -.
DR BioGRID-ORCS; 57636; 21 hits in 1065 CRISPR screens.
DR ChiTaRS; ARHGAP23; human.
DR GenomeRNAi; 57636; -.
DR Pharos; Q9P227; Tdark.
DR PRO; PR:Q9P227; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9P227; protein.
DR Bgee; ENSG00000275832; Expressed in sural nerve and 98 other tissues.
DR ExpressionAtlas; Q9P227; baseline and differential.
DR Genevisible; Q9P227; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1491
FT /note="Rho GTPase-activating protein 23"
FT /id="PRO_0000280471"
FT DOMAIN 71..155
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 688..808
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 905..1097
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZH9"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZH9"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZH9"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZH9"
FT MOD_RES 656
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZH9"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZH9"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZH9"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 854
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1139..1144
FT /note="DSTTCS -> ADLLEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_023708"
FT VAR_SEQ 1145..1491
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_023709"
SQ SEQUENCE 1491 AA; 162192 MW; 1700D3F1AEF5C0B1 CRC64;
MNGVAFCLVG IPPRPEPRPP QLPLGPRDGC SPRRPFPWQG PRTLLLYKSP QDGFGFTLRH
FIVYPPESAV HCSLKEEENG GRGGGPSPRY RLEPMDTIFV KNVKEDGPAH RAGLRTGDRL
VKVNGESVIG KTYSQVIALI QNSDDTLELS IMPKDEDILQ LAYSQDAYLK GNEPYSGEAR
SIPEPPPICY PRKTYAPPAR ASTRATMVPE PTSALPSDPR SPAAWSDPGL RVPPAARAHL
DNSSLGMSQP RPSPGAFPHL SSEPRTPRAF PEPGSRVPPS RLECQQALSH WLSNQVPRRA
GERRCPAMAP RARSASQDRL EEVAAPRPWP CSTSQDALSQ LGQEGWHRAR SDDYLSRATR
SAEALGPGAL VSPRFERCGW ASQRSSARTP ACPTRDLPGP QAPPPSGLQG LDDLGYIGYR
SYSPSFQRRT GLLHALSFRD SPFGGLPTFN LAQSPASFPP EASEPPRVVR PEPSTRALEP
PAEDRGDEVV LRQKPPTGRK VQLTPARQMN LGFGDESPEP EASGRGERLG RKVAPLATTE
DSLASIPFID EPTSPSIDLQ AKHVPASAVV SSAMNSAPVL GTSPSSPTFT FTLGRHYSQD
CSSIKAGRRS SYLLAITTER SKSCDDGLNT FRDEGRVLRR LPNRIPSLRM LRSFFTDGSL
DSWGTSEDAD APSKRHSTSD LSDATFSDIR REGWLYYKQI LTKKGKKAGS GLRQWKRVYA
ALRARSLSLS KERREPGPAA AGAAAAGAGE DEAAPVCIGS CLVDISYSET KRRHVFRLTT
ADFCEYLFQA EDRDDMLGWI RAIRENSRAE GEDPGCANQA LISKKLNDYR KVSHSSGPKA
DSSPKGSRGL GGLKSEFLKQ SAARGLRTQD LPAGSKDDSA AAPKTPWGIN IIKKNKKAAP
RAFGVRLEEC QPATENQRVP LIVAACCRIV EARGLESTGI YRVPGNNAVV SSLQEQLNRG
PGDINLQDER WQDLNVISSL LKSFFRKLPE PLFTDDKYND FIEANRIEDA RERMRTLRKL
IRDLPGHYYE TLKFLVGHLK TIADHSEKNK MEPRNLALVF GPTLVRTSED NMTDMVTHMP
DRYKIVETLI QHSDWFFSDE EDKGERTPVG DKEPQAVPNI EYLLPNIGRT VPPGDPGSDS
TTCSSAKSKG SWAPKKEPYA REMLAISFIS AVNRKRKKRR EARGLGSSTD DDSEQEAHKP
GAGATAPGTQ ERPQGPLPGA VAPEAPGRLS PPAAPEERPA ADTRSIVSGY STLSTMDRSV
CSGASGRRAG AGDEADDERS ELSHVETDTE GAAGAGPGGR LTRRPSFSSH HLMPCDTLAR
RRLARGRPDG EGAGRGGPRA PEPPGSASSS SQESLRPPAA ALASRPSRME ALRLRLRGTA
DDMLAVRLRR PLSPETRRRR SSWRRHTVVV QSPLTDLNFN EWKELGGGGP PEPAGARAHS
DNKDSGLSSL ESTKARAPSS AASQPPAPGD TGSLQSQPPR RSAASRLHQC L
