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Database: UniProt
Entry: P59281
LinkDB: P59281
Original site: P59281 
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   24-JAN-2024, entry version 161.
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; 12.
DR   IntAct; P59281; 8.
DR   MINT; P59281; -.
DR   STRING; 10090.ENSMUSP00000158945; -.
DR   GlyGen; P59281; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P59281; -.
DR   PhosphoSitePlus; P59281; -.
DR   SwissPalm; P59281; -.
DR   MaxQB; P59281; -.
DR   PaxDb; 10090-ENSMUSP00000036697; -.
DR   ProteomicsDB; 255265; -. [P59281-1]
DR   ProteomicsDB; 255266; -. [P59281-2]
DR   Pumba; P59281; -.
DR   Antibodypedia; 49512; 92 antibodies from 21 providers.
DR   DNASU; 223666; -.
DR   Ensembl; ENSMUST00000036176.16; ENSMUSP00000036697.10; ENSMUSG00000033697.17. [P59281-1]
DR   Ensembl; ENSMUST00000239134.2; ENSMUSP00000158984.2; ENSMUSG00000033697.17. [P59281-2]
DR   GeneID; 223666; -.
DR   KEGG; mmu:223666; -.
DR   AGR; MGI:107858; -.
DR   CTD; 80728; -.
DR   MGI; MGI:107858; Arhgap39.
DR   VEuPathDB; HostDB:ENSMUSG00000033697; -.
DR   eggNOG; ENOG502QR6X; Eukaryota.
DR   GeneTree; ENSGT00390000003161; -.
DR   InParanoid; P59281; -.
DR   OrthoDB; 5480623at2759; -.
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; 4 hits in 79 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 241 other cell types or 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   CDD; cd04389; RhoGAP_KIAA1688; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 1.25.40.530; MyTH4 domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 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   PANTHER; PTHR45876; FI04035P; 1.
DR   PANTHER; PTHR45876:SF1; RHO GTPASE-ACTIVATING PROTEIN 39; 1.
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; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF51045; WW domain; 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
//
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