RHG39_MOUSE
ID RHG39_MOUSE Reviewed; 1107 AA.
AC P59281; Q69ZD4; Q6P9R6;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Rho GTPase-activating protein 39;
GN Name=Arhgap39; Synonyms=D15Wsu169e, Kiaa1688;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 11-1107 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-597; SER-708 AND
RP SER-719, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P59281-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P59281-2; Sequence=VSP_013707;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32510.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173232; BAD32510.1; ALT_INIT; mRNA.
DR EMBL; BC060637; AAH60637.1; -; mRNA.
DR EMBL; AK035479; BAC29074.1; -; mRNA.
DR CCDS; CCDS27592.3; -. [P59281-2]
DR CCDS; CCDS49654.2; -. [P59281-1]
DR RefSeq; NP_001161760.1; NM_001168288.1. [P59281-1]
DR RefSeq; NP_940812.2; NM_198420.2. [P59281-2]
DR AlphaFoldDB; P59281; -.
DR SMR; P59281; -.
DR BioGRID; 230172; 9.
DR IntAct; P59281; 8.
DR MINT; P59281; -.
DR STRING; 10090.ENSMUSP00000036697; -.
DR iPTMnet; P59281; -.
DR PhosphoSitePlus; P59281; -.
DR MaxQB; P59281; -.
DR PaxDb; P59281; -.
DR PRIDE; P59281; -.
DR ProteomicsDB; 255265; -. [P59281-1]
DR ProteomicsDB; 255266; -. [P59281-2]
DR Antibodypedia; 49512; 79 antibodies from 21 providers.
DR DNASU; 223666; -.
DR Ensembl; ENSMUST00000036176; ENSMUSP00000036697; ENSMUSG00000033697. [P59281-1]
DR Ensembl; ENSMUST00000239134; ENSMUSP00000158984; ENSMUSG00000033697. [P59281-2]
DR GeneID; 223666; -.
DR KEGG; mmu:223666; -.
DR CTD; 80728; -.
DR MGI; MGI:107858; Arhgap39.
DR VEuPathDB; HostDB:ENSMUSG00000033697; -.
DR eggNOG; ENOG502QR6X; Eukaryota.
DR GeneTree; ENSGT00390000003161; -.
DR InParanoid; P59281; -.
DR OrthoDB; 1123653at2759; -.
DR PhylomeDB; P59281; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 223666; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Arhgap39; mouse.
DR PRO; PR:P59281; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P59281; protein.
DR Bgee; ENSMUSG00000033697; Expressed in ear vesicle and 239 other tissues.
DR ExpressionAtlas; P59281; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0099173; P:postsynapse organization; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.25.40.530; -; 1.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00784; MyTH4; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00139; MyTH4; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS51016; MYTH4; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H5"
FT CHAIN 2..1107
FT /note="Rho GTPase-activating protein 39"
FT /id="PRO_0000076093"
FT DOMAIN 25..58
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 63..97
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 715..867
FT /note="MyTH4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 914..1102
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H5"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H5"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H5"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H5"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H5"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H5"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 834..864
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013707"
FT CONFLICT 1032
FT /note="R -> Q (in Ref. 2; AAH60637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1107 AA; 125206 MW; BCEF3C200664DF31 CRC64;
MSQAQDYECR SHHVDEQEPR IPGSSTRLEW VEIIEPRTRE RMYANLVTGE CVWDPPAGVR
IKRTSEDQWW ELFDPNTSRF YYYSAASQRT VWHRPQNCDI IPLAKLQTLK QNTESPRASA
DNSPGRGSRD GSTGSSLEPE LEERTQELPV RSGRATTLVT SKEDTSSCSP PGVLLEKDYE
VYRDYSADGQ LLHYRTSSLR WNSGNKERML IKVADREPSF LTPQGNGYPA DNQPGGHHRR
PSGSQHSPNL QTFVPDTDGT VFFPERRPSP FLRRAELSGN CSPLLIQPRK PSSDSQPSSP
RYGYEPPLYE EPPVEYQAPI YDEPPMDVQF EANSPYQTGS PQRSPGRKPH PFLQTTKQTP
TSPCQQLMRT KQKCPERFLS LEYSPVGKEY VRQLVYVEQA GSSPKLRAGP RHKYAPNPGG
GTYSLQPSPC LLRDQRLGVR SGDYSTMEGP ESRPSQPPTP LPQAQEDAMS WSSQQDTMSS
TGYSPGTRKR KNRKPSLCQV PSTSSTDGAG GLLGEQPLTE ERSPCRASLT PVKAEADLVR
GTPEPFLAQA RLAWEAQQAH FHMKQRGSWD SQQDGSGYES DGAVPLPMPG PVVRAFSEDE
ALAQQDSKHW KRSTFDKLGF PQILLEKSVS VQTNLASPEP HLHPSQSEDL GACAQFESSR
QNRSAMPSSS CVFPTFTLRK PSSETDIENW ASKHFNKHTQ GLFRRKVSIA NMLAWSSESI
KKPMIVTSDR HVKKEACEIF KLIQMYMGDR RAKADPLHVA LEIATKGWSA QGLRDELYIQ
LCRQTTENFR LESLARGWEL MAICLAFFPP TPKFHSYLEG YIYRHMDPVN DTKVTQHIKE
LLERNSKKKS KLRKKPKPYV EEPDGVAIST YAKYCYHKLQ KAALTGAKKG LKKPNVEEIR
HAKNAVFSPS MFGSALQEVM SMQKERYPDR QLPWVQTRLS EEVLALNGDQ TEGIFRVPGD
IDEVNALKLQ VDQWKVPTGL EDPHVPASLL KLWYRELEEP LIPHEFYEQC IAHYESPEAA
VAVVHALPRI NRMVLCYLIR FLQVFVQPAN VAITKMDVSN LAMVMAPNCL RCQSDDPRVI
FENTRKEMSF LRVLIQHLDT SFMEGVL
