RHG30_HUMAN
ID RHG30_HUMAN Reviewed; 1101 AA.
AC Q7Z6I6; Q5SY52; Q5SY53; Q5SY54; Q6ZML6; Q7Z3J8; Q86XI7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Rho GTPase-activating protein 30;
DE AltName: Full=Rho-type GTPase-activating protein 30;
GN Name=ARHGAP30;
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 MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT VAL-591.
RC TISSUE=Endometrium;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-744 (ISOFORM 3), AND VARIANTS LEU-70 AND VAL-591.
RC TISSUE=Blood, and Testis;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-996, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, INTERACTION WITH RHOU, SUBCELLULAR LOCATION, AND ALTERNATIVE
RP SPLICING (ISOFORMS 1 AND 2).
RX PubMed=21565175; DOI=10.1016/j.bbrc.2011.04.116;
RA Naji L., Pacholsky D., Aspenstrom P.;
RT "ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and
RT cell adhesion.";
RL Biochem. Biophys. Res. Commun. 409:96-102(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, 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).
CC -!- FUNCTION: GTPase-activating protein (GAP) for RAC1 and RHOA, but not
CC for CDC42. {ECO:0000269|PubMed:21565175}.
CC -!- SUBUNIT: Interacts with RHOU in a GTP-independent manner.
CC {ECO:0000269|PubMed:21565175}.
CC -!- INTERACTION:
CC Q7Z6I6; Q7L0Q8: RHOU; NbExp=2; IntAct=EBI-2814810, EBI-1638043;
CC Q7Z6I6-2; Q7L0Q8: RHOU; NbExp=3; IntAct=EBI-26970905, EBI-1638043;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:21565175}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=L-ARHGAP30, L-30;
CC IsoId=Q7Z6I6-1; Sequence=Displayed;
CC Name=2; Synonyms=S-ARHGAP30, S-30;
CC IsoId=Q7Z6I6-2; Sequence=VSP_023735;
CC Name=3;
CC IsoId=Q7Z6I6-3; Sequence=VSP_023732;
CC Name=4;
CC IsoId=Q7Z6I6-4; Sequence=VSP_023733, VSP_023734;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43387.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAD18709.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK160366; BAD18709.1; ALT_INIT; mRNA.
DR EMBL; BX537846; CAD97855.1; -; mRNA.
DR EMBL; AL591806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043387; AAH43387.1; ALT_SEQ; mRNA.
DR EMBL; BC053688; AAH53688.1; -; mRNA.
DR CCDS; CCDS1215.1; -. [Q7Z6I6-2]
DR CCDS; CCDS30918.1; -. [Q7Z6I6-1]
DR RefSeq; NP_001020769.1; NM_001025598.1. [Q7Z6I6-1]
DR RefSeq; NP_001274529.1; NM_001287600.1. [Q7Z6I6-3]
DR RefSeq; NP_001274531.1; NM_001287602.1.
DR RefSeq; NP_859071.2; NM_181720.2.
DR RefSeq; XP_005245130.1; XM_005245073.3. [Q7Z6I6-3]
DR RefSeq; XP_011507693.1; XM_011509391.2. [Q7Z6I6-3]
DR AlphaFoldDB; Q7Z6I6; -.
DR SMR; Q7Z6I6; -.
DR BioGRID; 129199; 5.
DR IntAct; Q7Z6I6; 6.
DR STRING; 9606.ENSP00000356992; -.
DR GlyGen; Q7Z6I6; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q7Z6I6; -.
DR PhosphoSitePlus; Q7Z6I6; -.
DR BioMuta; ARHGAP30; -.
DR DMDM; 334302880; -.
DR EPD; Q7Z6I6; -.
DR jPOST; Q7Z6I6; -.
DR MassIVE; Q7Z6I6; -.
DR MaxQB; Q7Z6I6; -.
DR PaxDb; Q7Z6I6; -.
DR PeptideAtlas; Q7Z6I6; -.
DR PRIDE; Q7Z6I6; -.
DR ProteomicsDB; 69411; -. [Q7Z6I6-1]
DR ProteomicsDB; 69412; -. [Q7Z6I6-2]
DR ProteomicsDB; 69413; -. [Q7Z6I6-3]
DR ProteomicsDB; 69414; -. [Q7Z6I6-4]
DR Antibodypedia; 34287; 101 antibodies from 26 providers.
DR DNASU; 257106; -.
DR Ensembl; ENST00000368013.8; ENSP00000356992.3; ENSG00000186517.14. [Q7Z6I6-1]
DR GeneID; 257106; -.
DR KEGG; hsa:257106; -.
DR MANE-Select; ENST00000368013.8; ENSP00000356992.3; NM_001025598.2; NP_001020769.1.
DR UCSC; uc001fxl.4; human. [Q7Z6I6-1]
DR CTD; 257106; -.
DR DisGeNET; 257106; -.
DR GeneCards; ARHGAP30; -.
DR HGNC; HGNC:27414; ARHGAP30.
DR HPA; ENSG00000186517; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 614264; gene.
DR neXtProt; NX_Q7Z6I6; -.
DR OpenTargets; ENSG00000186517; -.
DR PharmGKB; PA142672585; -.
DR VEuPathDB; HostDB:ENSG00000186517; -.
DR eggNOG; KOG1449; Eukaryota.
DR GeneTree; ENSGT00940000161411; -.
DR InParanoid; Q7Z6I6; -.
DR OMA; RASWRNG; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q7Z6I6; -.
DR TreeFam; TF351451; -.
DR PathwayCommons; Q7Z6I6; -.
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-9013420; RHOU GTPase cycle.
DR SignaLink; Q7Z6I6; -.
DR SIGNOR; Q7Z6I6; -.
DR BioGRID-ORCS; 257106; 11 hits in 1062 CRISPR screens.
DR ChiTaRS; ARHGAP30; human.
DR GenomeRNAi; 257106; -.
DR Pharos; Q7Z6I6; Tdark.
DR PRO; PR:Q7Z6I6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z6I6; protein.
DR Bgee; ENSG00000186517; Expressed in granulocyte and 184 other tissues.
DR ExpressionAtlas; Q7Z6I6; baseline and differential.
DR Genevisible; Q7Z6I6; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
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; Cytoplasmic vesicle; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1101
FT /note="Rho GTPase-activating protein 30"
FT /id="PRO_0000280478"
FT DOMAIN 20..215
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 224..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..148
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023732"
FT VAR_SEQ 223..243
FT /note="GEVESGWRSLPGTRASGSPED -> QCPPCPPHIPLLGSQVSYSEP (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_023733"
FT VAR_SEQ 244..1101
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_023734"
FT VAR_SEQ 679..889
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023735"
FT VARIANT 70
FT /note="F -> L (in dbSNP:rs17854839)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031157"
FT VARIANT 591
FT /note="L -> V (in dbSNP:rs3813609)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_031158"
FT CONFLICT 1034
FT /note="S -> P (in Ref. 1; BAD18709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1101 AA; 118582 MW; A2BBD3079C55C563 CRC64;
MKSRQKGKKK GSAKERVFGC DLQEHLQHSG QEVPQVLKSC AEFVEEYGVV DGIYRLSGVS
SNIQKLRQEF ESERKPDLRR DVYLQDIHCV SSLCKAYFRE LPDPLLTYRL YDKFAEAVGV
QLEPERLVKI LEVLRELPVP NYRTLEFLMR HLVHMASFSA QTNMHARNLA IVWAPNLLRS
KDIEASGFNG TAAFMEVRVQ SIVVEFILTH VDQLFGGAAL SGGEVESGWR SLPGTRASGS
PEDLMPRPLP YHLPSILQAG DGPPQMRPYH TIIEIAEHKR KGSLKVRKWR SIFNLGRSGH
ETKRKLPRGA EDREDKSNKG TLRPAKSMDS LSAAAGASDE PEGLVGPSSP RPSPLLPESL
ENDSIEAAEG EQEPEAEALG GTNSEPGTPR AGRSAIRAGG SSRAERCAGV HISDPYNVNL
PLHITSILSV PPNIISNVSL ARLTRGLECP ALQHRPSPAS GPGPGPGLGP GPPDEKLEAS
PASSPLADSG PDDLAPALED SLSQEVQDSF SFLEDSSSSE PEWVGAEDGE VAQAEAAGAA
FSPGEDDPGM GYLEELLGVG PQVEEFSVEP PLDDLSLDEA QFVLAPSCCS LDSAGPRPEV
EEENGEEVFL SAYDDLSPLL GPKPPIWKGS GSLEGEAAGC GRQALGQGGE EQACWEVGED
KQAEPGGRLD IREEAEGSPE TKVEAGKASE DRGEAGGSQE TKVRLREGSR EETEAKEEKS
KGQKKADSME AKGVEEPGGD EYTDEKEKEI EREEDEQREE AQVEAGRDLE QGAQEDQVAE
EKWEVVQKQE AEGVREDEDK GQREKGYHEA RKDQGDGEDS RSPEAATEGG AGEVSKERES
GDGEAEGDQR AGGYYLEEDT LSEGSGVASL EVDCAKEGNP HSSEMEEVAP QPPQPEEMEP
EGQPSPDGCL CPCSLGLGGV GMRLASTLVQ VQQVRSVPVV PPKPQFAKMP SAMCSKIHVA
PANPCPRPGR LDGTPGERAW GSRASRSSWR NGGSLSFDAA VALARDRQRT EAQGVRRTQT
CTEGGDYCLI PRTSPCSMIS AHSPRPLSCL ELPSEGAEGS GSRSRLSLPP REPQVPDPLL
SSQRRSYAFE TQANPGKGEG L
