RHG42_HUMAN
ID RHG42_HUMAN Reviewed; 874 AA.
AC A6NI28; Q96M56;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Rho GTPase-activating protein 42 {ECO:0000305};
DE AltName: Full=Rho GTPase-activating protein 10-like;
DE AltName: Full=Rho-type GTPase-activating protein 42;
GN Name=ARHGAP42 {ECO:0000312|HGNC:HGNC:26545};
GN Synonyms=GRAF3 {ECO:0000303|PubMed:24335996},
GN TMEM133 {ECO:0000312|HGNC:HGNC:26545};
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=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-128.
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 389-819.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-811 AND TYR-870, AND
RP IDENTIFICATION BY 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 TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=24335996; DOI=10.1038/ncomms3910;
RA Bai X., Lenhart K.C., Bird K.E., Suen A.A., Rojas M., Kakoki M., Li F.,
RA Smithies O., Mack C.P., Taylor J.M.;
RT "The smooth muscle-selective RhoGAP GRAF3 is a critical regulator of
RT vascular tone and hypertension.";
RL Nat. Commun. 4:2910-2910(2013).
CC -!- FUNCTION: May influence blood pressure by functioning as a GTPase-
CC activating protein for RHOA in vascular smooth muscle.
CC {ECO:0000269|PubMed:24335996}.
CC -!- TISSUE SPECIFICITY: Highly and selectively expressed in smooth muscle
CC cells. {ECO:0000269|PubMed:24335996}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71456.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BF511460; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AC015600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BF511460; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK057372; BAB71456.1; ALT_SEQ; mRNA.
DR RefSeq; NP_689645.2; NM_152432.2.
DR AlphaFoldDB; A6NI28; -.
DR SMR; A6NI28; -.
DR BioGRID; 126819; 23.
DR IntAct; A6NI28; 7.
DR STRING; 9606.ENSP00000298815; -.
DR iPTMnet; A6NI28; -.
DR PhosphoSitePlus; A6NI28; -.
DR BioMuta; ARHGAP42; -.
DR EPD; A6NI28; -.
DR jPOST; A6NI28; -.
DR MassIVE; A6NI28; -.
DR MaxQB; A6NI28; -.
DR PaxDb; A6NI28; -.
DR PeptideAtlas; A6NI28; -.
DR PRIDE; A6NI28; -.
DR ProteomicsDB; 1242; -.
DR Antibodypedia; 51394; 53 antibodies from 13 providers.
DR DNASU; 143872; -.
DR Ensembl; ENST00000298815.13; ENSP00000298815.7; ENSG00000165895.19.
DR GeneID; 143872; -.
DR KEGG; hsa:143872; -.
DR MANE-Select; ENST00000298815.13; ENSP00000298815.7; NM_152432.4; NP_689645.2.
DR UCSC; uc001pge.2; human.
DR CTD; 143872; -.
DR DisGeNET; 143872; -.
DR GeneCards; ARHGAP42; -.
DR HGNC; HGNC:26545; ARHGAP42.
DR HPA; ENSG00000165895; Tissue enhanced (retina).
DR MIM; 615936; gene.
DR neXtProt; NX_A6NI28; -.
DR OpenTargets; ENSG00000165895; -.
DR PharmGKB; PA165543186; -.
DR VEuPathDB; HostDB:ENSG00000165895; -.
DR eggNOG; KOG1451; Eukaryota.
DR GeneTree; ENSGT00940000155492; -.
DR HOGENOM; CLU_011532_1_0_1; -.
DR InParanoid; A6NI28; -.
DR OMA; KASGKMN; -.
DR OrthoDB; 693048at2759; -.
DR PhylomeDB; A6NI28; -.
DR TreeFam; TF316851; -.
DR PathwayCommons; A6NI28; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; A6NI28; -.
DR BioGRID-ORCS; 143872; 4 hits in 220 CRISPR screens.
DR ChiTaRS; ARHGAP42; human.
DR GenomeRNAi; 143872; -.
DR Pharos; A6NI28; Tbio.
DR PRO; PR:A6NI28; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; A6NI28; protein.
DR Bgee; ENSG00000165895; Expressed in calcaneal tendon and 153 other tissues.
DR ExpressionAtlas; A6NI28; baseline and differential.
DR Genevisible; A6NI28; HS.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:1904694; P:negative regulation of vascular associated smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; GTPase activation; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..874
FT /note="Rho GTPase-activating protein 42"
FT /id="PRO_0000342407"
FT DOMAIN 7..262
FT /note="BAR"
FT DOMAIN 265..374
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 376..572
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 816..874
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 575..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 225..261
FT /evidence="ECO:0000255"
FT COMPBIAS 584..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 376
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:B2RQE8"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RQE8"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RQE8"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RQE8"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RQE8"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 870
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CONFLICT 18
FT /note="F -> V (in Ref. 2; BF511460)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="N -> D (in Ref. 2; BF511460)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="I -> M (in Ref. 2; BF511460)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="I -> V (in Ref. 3; BAB71456)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="V -> I (in Ref. 3; BAB71456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 874 AA; 98569 MW; 3828623C52C52629 CRC64;
MGLPTLEFSD SYLDSPDFRE RLQCHEIELE RTNKFIKELI KDGSLLIGAL RNLSMAVQKF
SQSLQDFQFE CIGDAETDDE ISIAQSLKEF ARLLIAVEEE RRRLIQNAND VLIAPLEKFR
KEQIGAAKDG KKKFDKESEK YYSILEKHLN LSAKKKESHL QEADTQIDRE HQNFYEASLE
YVFKIQEVQE KKKFEFVEPL LSFLQGLFTF YHEGYELAQE FAPYKQQLQF NLQNTRNNFE
STRQEVERLM QRMKSANQDY RPPSQWTMEG YLYVQEKRPL GFTWIKHYCT YDKGSKTFTM
SVSEMKSSGK MNGLVTSSPE MFKLKSCIRR KTDSIDKRFC FDIEVVERHG IITLQAFSEA
NRKLWLEAMD GKEPIYTLPA IISKKEEMYL NEAGFNFVRK CIQAVETRGI TILGLYRIGG
VNSKVQKLMN TTFSPKSPPD IDIDIELWDN KTITSGLKNY LRCLAEPLMT YKLHKDFIIA
VKSDDQNYRV EAVHALVHKL PEKNREMLDI LIKHLVKVSL HSQQNLMTVS NLGVIFGPTL
MRAQEETVAA MMNIKFQNIV VEILIEHYEK IFHTAPDPSI PLPQPQSRSG SRRTRAICLS
TGSRKPRGRY TPCLAEPDSD SYSSSPDSTP MGSIESLSSH SSEQNSTTKS ASCQPREKSG
GIPWIATPSS SNGQKSLGLW TTSPESSSRE DATKTDAESD CQSVASVTSP GDVSPPIDLV
KKEPYGLSGL KRASASSLRS ISAAEGNKSY SGSIQSLTSV GSKETPKASP NPDLPPKMCR
RLRLDTASSN GYQRPGSVVA AKAQLFENVG SPKPVSSGRQ AKAMYSCKAE HSHELSFPQG
AIFSNVYPSV EPGWLKATYE GKTGLVPENY VVFL
