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Database: UniProt
Entry: PKHG2_MOUSE
LinkDB: PKHG2_MOUSE
Original site: PKHG2_MOUSE 
ID   PKHG2_MOUSE             Reviewed;        1340 AA.
AC   Q6KAU7; A0PJD9; Q3UNL4; Q6PGK2; Q7TS89; Q8R4H6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-NOV-2023, entry version 116.
DE   RecName: Full=Pleckstrin homology domain-containing family G member 2;
DE            Short=PH domain-containing family G member 2;
DE   AltName: Full=Common site lymphoma/leukemia guanine nucleotide exchange factor;
DE            Short=Common site lymphoma/leukemia GEF;
GN   Name=Plekhg2;
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 [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND FUNCTION.
RC   STRAIN=BXH2;
RX   PubMed=11839748; DOI=10.1074/jbc.m110981200;
RA   Himmel K.L., Bi F., Shen H., Jenkins N.A., Copeland N.G., Zheng Y.,
RA   Largaespada D.A.;
RT   "Activation of clg, a novel dbl family guanine nucleotide exchange factor
RT   gene, by proviral insertion at evi24, a common integration site in B cell
RT   and myeloid leukemias.";
RL   J. Biol. Chem. 277:13463-13472(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT   complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT   by screening of terminal sequences of cDNA clones randomly sampled from
RT   size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-912.
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).
CC   -!- FUNCTION: May be a transforming oncogene with exchange activity for
CC       CDC42. May be a guanine-nucleotide exchange factor (GEF) for RAC1 and
CC       CDC42 (PubMed:11839748). Activated by the binding to subunits beta and
CC       gamma of the heterotrimeric guanine nucleotide-binding protein (G
CC       protein) (By similarity). Involved in the regulation of actin
CC       polymerization (By similarity). {ECO:0000250|UniProtKB:Q9H7P9,
CC       ECO:0000269|PubMed:11839748}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6KAU7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6KAU7-2; Sequence=VSP_028531;
CC       Name=3;
CC         IsoId=Q6KAU7-3; Sequence=VSP_028532;
CC   -!- TISSUE SPECIFICITY: Expressed in thymus, skeletal muscle, lung, testis,
CC       uterus, pancreas and heart and also expressed during embryogenesis.
CC       {ECO:0000269|PubMed:11839748}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52436.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH56971.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD21360.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF465238; AAL93134.1; -; mRNA.
DR   EMBL; AK131110; BAD21360.1; ALT_INIT; mRNA.
DR   EMBL; BC025625; AAH25625.1; -; mRNA.
DR   EMBL; BC052436; AAH52436.1; ALT_INIT; mRNA.
DR   EMBL; BC056971; AAH56971.1; ALT_INIT; mRNA.
DR   EMBL; AK144152; BAE25733.1; -; mRNA.
DR   CCDS; CCDS52162.1; -. [Q6KAU7-1]
DR   RefSeq; NP_001077381.1; NM_001083912.1.
DR   RefSeq; NP_001277471.1; NM_001290542.1.
DR   RefSeq; NP_620091.2; NM_138752.2.
DR   RefSeq; XP_006539504.1; XM_006539441.2.
DR   RefSeq; XP_006539505.1; XM_006539442.3.
DR   AlphaFoldDB; Q6KAU7; -.
DR   SMR; Q6KAU7; -.
DR   BioGRID; 221673; 10.
DR   IntAct; Q6KAU7; 6.
DR   STRING; 10090.ENSMUSP00000092228; -.
DR   GlyGen; Q6KAU7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6KAU7; -.
DR   PhosphoSitePlus; Q6KAU7; -.
DR   SwissPalm; Q6KAU7; -.
DR   jPOST; Q6KAU7; -.
DR   MaxQB; Q6KAU7; -.
DR   PaxDb; 10090-ENSMUSP00000092228; -.
DR   ProteomicsDB; 288222; -. [Q6KAU7-1]
DR   ProteomicsDB; 288223; -. [Q6KAU7-2]
DR   ProteomicsDB; 288224; -. [Q6KAU7-3]
DR   Pumba; Q6KAU7; -.
DR   DNASU; 101497; -.
DR   GeneID; 101497; -.
DR   KEGG; mmu:101497; -.
DR   AGR; MGI:2141874; -.
DR   CTD; 64857; -.
DR   MGI; MGI:2141874; Plekhg2.
DR   eggNOG; KOG3518; Eukaryota.
DR   InParanoid; Q6KAU7; -.
DR   OrthoDB; 5400510at2759; -.
DR   Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR   Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR   Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR   Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR   BioGRID-ORCS; 101497; 5 hits in 78 CRISPR screens.
DR   ChiTaRS; Plekhg2; mouse.
DR   PRO; PR:Q6KAU7; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q6KAU7; Protein.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; ISS:UniProtKB.
DR   CDD; cd13243; PH_PLEKHG1_G2_G3; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR043324; PH_PLEKHG1_G2_G3.
DR   PANTHER; PTHR45924; FI17866P1; 1.
DR   PANTHER; PTHR45924:SF3; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY G MEMBER 2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   Reference proteome; Tumor suppressor.
FT   CHAIN           1..1340
FT                   /note="Pleckstrin homology domain-containing family G
FT                   member 2"
FT                   /id="PRO_0000306862"
FT   DOMAIN          98..279
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          309..407
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          34..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          820..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          907..979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1047..1069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1125..1146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1250..1340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..853
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..921
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..979
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1063
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1273..1289
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         441
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7P9"
FT   MOD_RES         446
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7P9"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7P9"
FT   MOD_RES         1215
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7P9"
FT   MOD_RES         1219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7P9"
FT   MOD_RES         1269
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7P9"
FT   VAR_SEQ         1..42
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11839748"
FT                   /id="VSP_028531"
FT   VAR_SEQ         478
FT                   /note="S -> SGEYPPLEGDPGSQWPGLLTSFFLPP (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028532"
FT   CONFLICT        37
FT                   /note="A -> AA (in Ref. 3; AAH56971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        519
FT                   /note="L -> P (in Ref. 3; AAH52436/AAH56971 and 4;
FT                   BAE25733)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        823..825
FT                   /note="AET -> TRP (in Ref. 3; AAH25625)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1340 AA;  143376 MW;  E4FD7C9382658173 CRC64;
     MPEGARGLSL PKPSLRLGCG HQGEVCDCAA VSDTPTAQAA TTMASPRGSG SSTSLSTVGS
     EGDPSPACSA SRPEPLPEPP IRLHLLPVGI QGSVKPSRLE RVAREIVETE RAYVRDLRSI
     VEDYLGPLMD GRALGLNMEQ VGTLFANIED IYEFSSELLE DLEGCSSAGG IAECFVQRSE
     DFDIYTLYCM NYPSSLALLR ELSVSPPATL WLQERQAQLR HSLPLQSFLL KPVQRILKYH
     LLLQELGKHW AEGPDSGGRE MVEEAIVSMT AVAWYINDMK RKQEHAARLQ EVQRRLGGWT
     GPELSAFGEL VLEGTFRGGG GGGPRLRGGE RLLFLFSRML LVAKRRGPEY TYKGHIFCCN
     LSVSETPRDP LGFKVSDLTI PKHRHLFQAK NQEEKRLWIH CLQRLFFENH PASIPAKAKQ
     VLLENSLHCA PKSKHIPEPP TSPLDSPRPR DAPGFTPGRR NPAPSPRLSG SRRGRRQSEP
     AKEAYVIFPQ NDKPQVKHAG SEGELHPSSE LQPVSASGLP EDLEDAGPPT LDPSGTSITE
     EILELLNQRG LRDSGPATHD IPKFPRDSRV PVESEPLPFQ SLPSRESSEE EEEEDLETDE
     REPSPLHVLE GLEGSSAAEI PCIPSLTDIP SEVPSLPEIP EAPCLPCLSD ISGVFEVPCL
     SPTSTVPDIP SLATTPSFPC GSWLPGPLQE AAQPQATRRE LLSGSNPGRL SESPSESREG
     QEDDTEGVSF SAVQREAGTS VQGFPEELEY RSCSEIRSAW QALEQGQLAR PGFPEPLLIL
     EDSDLRGGST SGKTGMPHSE RSASRVRELA RLYSERIQQM QRAETRASTN APRRRPRVLA
     QPQPSPCPPQ EEAEPGALPA FGHVLVCELA FPLNCTQESV PLGPAVLVQA ATPLCIQGDD
     LSGQNLNVSD LSKQGHLSSN SIPPPVPLPG QSNFQNIQVP STSLLPKQEP PDVQVPTAST
     LPDTSQLQSQ VPAATPSAGH RNCVEIQVQS TTSLPGQECQ ADTVALSKQE GHEDSQNPNK
     APGAEQRDVS IDQGLAVVGG RPVSPLPVCT SSPDQQIPAT TPLPLSTDFP DMEGPGALPL
     PTQEGRPDCS IPCNPLPSLS QDVQVPAVIP VSQLQGLTDT RATVPLSSHK QEDAPECLGP
     EPSLTDTPAP RLLSSLGQQN TTDGPVSAAA VPLTEQGCSQ DLQGLITSPV QTTMELPKPR
     GLVSRVATSE SLDLTPPHSP SLSTRQLLGP SAAALSRYLA ASYISQSLAR RQGPGGEGTV
     ASQGHWSSSA PTSRAPSPPP QPQPPAPPAR RLSYATTVSI QVGGGGRLRP AKAQVRLNHP
     ALLAAPHPGA VGPSQGPGGS
//
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