Full text data of IQGAP2
IQGAP2
[Confidence: low (only semi-automatic identification from reviews)]
Ras GTPase-activating-like protein IQGAP2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ras GTPase-activating-like protein IQGAP2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q13576
ID IQGA2_HUMAN Reviewed; 1575 AA.
AC Q13576; A8K4V1; B7Z8A4;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-MAR-2010, sequence version 4.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Ras GTPase-activating-like protein IQGAP2;
GN Name=IQGAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLU-527; GLU-532;
RP PHE-629 AND VAL-724.
RC TISSUE=Liver;
RX PubMed=8756646;
RA Brill S., Li S., Lyman C.W., Church D.M., Wasmuth J.J., Weissbach L.,
RA Bernards A., Snijders A.J.;
RT "The Ras GTPase-activating-protein-related human protein IQGAP2
RT harbors a potential actin binding domain and interacts with calmodulin
RT and Rho family GTPases.";
RL Mol. Cell. Biol. 16:4869-4878(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS GLU-527; GLU-532;
RP PHE-629 AND VAL-724.
RA Wang H., Huo R., Xu Z.Y., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning and characterization of a novel isoform of IQGAP2 in human
RT adult testis.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS GLU-527 AND GLU-532.
RC TISSUE=Teratocarcinoma, and 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-13.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-629, AND MASS SPECTROMETRY.
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., 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 [10]
RP VARIANTS CYS-1445 AND ILE-1530.
RX PubMed=23033978; DOI=10.1056/NEJMoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
RA Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
RA Brunner H.G., Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Binds to activated CDC42 and RAC1 but does not seem to
CC stimulate their GTPase activity. Associates with calmodulin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13576-2; Sequence=VSP_010629, VSP_010630, VSP_010631;
CC -!- TISSUE SPECIFICITY: Isoform 2 expression is enhanced in testis.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 3 IQ domains.
CC -!- SIMILARITY: Contains 1 Ras-GAP domain.
CC -!- SIMILARITY: Contains 1 WW domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U51903; AAB37765.1; -; mRNA.
DR EMBL; AY351902; AAQ81291.1; -; mRNA.
DR EMBL; AK291066; BAF83755.1; -; mRNA.
DR EMBL; AK303054; BAH13890.1; -; mRNA.
DR EMBL; AC025188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001272389.1; NM_001285460.1.
DR RefSeq; NP_001272390.1; NM_001285461.1.
DR RefSeq; NP_001272391.1; NM_001285462.1.
DR RefSeq; NP_006624.2; NM_006633.3.
DR UniGene; Hs.291030; -.
DR PDB; 3IEZ; X-ray; 1.50 A; A/B=1476-1571.
DR PDB; 4EZA; X-ray; 1.50 A; A/B=1476-1571.
DR PDBsum; 3IEZ; -.
DR PDBsum; 4EZA; -.
DR ProteinModelPortal; Q13576; -.
DR SMR; Q13576; 23-207, 875-1252, 1477-1571.
DR DIP; DIP-27542N; -.
DR IntAct; Q13576; 12.
DR MINT; MINT-5004527; -.
DR STRING; 9606.ENSP00000274364; -.
DR PhosphoSite; Q13576; -.
DR DMDM; 292495090; -.
DR OGP; Q13576; -.
DR PaxDb; Q13576; -.
DR PRIDE; Q13576; -.
DR DNASU; 10788; -.
DR Ensembl; ENST00000274364; ENSP00000274364; ENSG00000145703.
DR Ensembl; ENST00000396234; ENSP00000379535; ENSG00000145703.
DR GeneID; 10788; -.
DR KEGG; hsa:10788; -.
DR UCSC; uc003kek.3; human.
DR CTD; 10788; -.
DR GeneCards; GC05P075699; -.
DR HGNC; HGNC:6111; IQGAP2.
DR HPA; CAB004241; -.
DR MIM; 605401; gene.
DR neXtProt; NX_Q13576; -.
DR PharmGKB; PA29911; -.
DR eggNOG; COG5261; -.
DR HOGENOM; HOG000004842; -.
DR HOVERGEN; HBG052143; -.
DR InParanoid; Q13576; -.
DR KO; K05767; -.
DR OMA; MEKVQLH; -.
DR OrthoDB; EOG7FNC6M; -.
DR PhylomeDB; Q13576; -.
DR EvolutionaryTrace; Q13576; -.
DR GenomeRNAi; 10788; -.
DR NextBio; 40978; -.
DR PRO; PR:Q13576; -.
DR ArrayExpress; Q13576; -.
DR Bgee; Q13576; -.
DR CleanEx; HS_IQGAP2; -.
DR Genevestigator; Q13576; -.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005099; F:Ras GTPase activator activity; IEA:InterPro.
DR GO; GO:0032320; P:positive regulation of Ras GTPase activity; IEA:GOC.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001936; RasGAP.
DR InterPro; IPR000593; RasGAP_C.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001202; WW_dom.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF03836; RasGAP_C; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48350; SSF48350; 2.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calmodulin-binding;
KW Complete proteome; Direct protein sequencing; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1575 Ras GTPase-activating-like protein
FT IQGAP2.
FT /FTId=PRO_0000056650.
FT DOMAIN 41 156 CH.
FT DOMAIN 594 627 WW.
FT DOMAIN 690 719 IQ 1.
FT DOMAIN 720 749 IQ 2.
FT DOMAIN 750 779 IQ 3.
FT DOMAIN 917 1150 Ras-GAP.
FT COMPBIAS 263 266 Poly-Lys.
FT MOD_RES 16 16 Phosphoserine.
FT VAR_SEQ 1 447 Missing (in isoform 2).
FT /FTId=VSP_010629.
FT VAR_SEQ 448 453 QEENDR -> MHSLPG (in isoform 2).
FT /FTId=VSP_010630.
FT VAR_SEQ 642 698 Missing (in isoform 2).
FT /FTId=VSP_010631.
FT VARIANT 455 455 V -> A (in dbSNP:rs7722711).
FT /FTId=VAR_055823.
FT VARIANT 479 479 P -> R (in dbSNP:rs3822530).
FT /FTId=VAR_055824.
FT VARIANT 527 527 D -> E (in dbSNP:rs2431352).
FT /FTId=VAR_062958.
FT VARIANT 532 532 K -> E (in dbSNP:rs2909888).
FT /FTId=VAR_059292.
FT VARIANT 629 629 L -> F (in dbSNP:rs2455230).
FT /FTId=VAR_062959.
FT VARIANT 714 714 R -> W (in dbSNP:rs35366349).
FT /FTId=VAR_055825.
FT VARIANT 724 724 I -> V (in dbSNP:rs2431363).
FT /FTId=VAR_062960.
FT VARIANT 894 894 T -> I (in dbSNP:rs34950321).
FT /FTId=VAR_055826.
FT VARIANT 1052 1052 R -> I (in dbSNP:rs2287932).
FT /FTId=VAR_055827.
FT VARIANT 1184 1184 N -> S (in dbSNP:rs10454915).
FT /FTId=VAR_055828.
FT VARIANT 1379 1379 R -> W (in dbSNP:rs17681908).
FT /FTId=VAR_055829.
FT VARIANT 1445 1445 Y -> C.
FT /FTId=VAR_069434.
FT VARIANT 1530 1530 M -> I.
FT /FTId=VAR_069435.
FT CONFLICT 95 95 V -> E (in Ref. 3; BAF83755).
FT CONFLICT 778 778 N -> S (in Ref. 3; BAF83755).
FT CONFLICT 1101 1101 G -> R (in Ref. 3; BAF83755).
FT CONFLICT 1333 1333 V -> L (in Ref. 3; BAH13890).
FT STRAND 1479 1482
FT HELIX 1483 1488
FT STRAND 1491 1495
FT HELIX 1500 1505
FT STRAND 1506 1512
FT STRAND 1518 1525
FT STRAND 1528 1536
FT HELIX 1537 1545
FT STRAND 1550 1554
FT STRAND 1557 1560
FT HELIX 1561 1569
SQ SEQUENCE 1575 AA; 180578 MW; BCC8CED6645CB09B CRC64;
MPHEELPSLQ RPRYGSIVDD ERLSAEEMDE RRRQNIAYEY LCHLEEAKRW MEVCLVEELP
PTTELEEGLR NGVYLAKLAK FFAPKMVSEK KIYDVEQTRY KKSGLHFRHT DNTVQWLRAM
ESIGLPKIFY PETTDVYDRK NIPRMIYCIH ALSLYLFKLG IAPQIQDLLG KVDFTEEEIS
NMRKELEKYG IQMPSFSKIG GILANELSVD EAALHAAVIA INEAVEKGIA EQTVVTLRNP
NAVLTLVDDN LAPEYQKELW DAKKKKEENA RLKNSCISEE ERDAYEELLT QAEIQGNINK
VNRQAAVDHI NAVIPEGDPE NTLLALKKPE AQLPAVYPFA AAMYQNELFN LQKQNTMNYL
AHEELLIAVE MLSAVALLNQ ALESNDLVSV QNQLRSPAIG LNNLDKAYVE RYANTLLSVK
LEVLSQGQDN LSWNEIQNCI DMVNAQIQEE NDRVVAVGYI NEAIDEGNPL RTLETLLLPT
ANISDVDPAH AQHYQDVLYH AKSQKLGDSE SVSKVLWLDE IQQAVDDANV DKDRAKQWVT
LVVDVNQCLE GKKSSDILSV LKSSTSNAND IIPECADKYY DALVKAKELK SERVSSDGSW
LKLNLHKKYD YYYNTDSKES SWVTPESCLY KESWLTGKEI EDIIEEVTVG YIRENIWSAS
EELLLRFQAT SSGPILREEF EARKSFLHEQ EENVVKIQAF WKGYKQRKEY MHRRQTFIDN
TDSIVKIQSW FRMATARKSY LSRLQYFRDH NNEIVKIQSL LRANKARDDY KTLVGSENPP
LTVIRKFVYL LDQSDLDFQE ELEVARLREE VVTKIRANQQ LEKDLNLMDI KIGLLVKNRI
TLEDVISHSK KLNKKKGGEM EILNNTDNQG IKSLSKERRK TLETYQQLFY LLQTNPLYLA
KLIFQMPQNK STKFMDTVIF TLYNYASNQR EEYLLLKLFK TALEEEIKSK VDQVQDIVTG
NPTVIKMVVS FNRGARGQNT LRQLLAPVVK EIIDDKSLII NTNPVEVYKA WVNQLETQTG
EASKLPYDVT TEQALTYPEV KNKLEASIEN LRRVTDKVLN SIISSLDLLP YGLRYIAKVL
KNSIHEKFPD ATEDELLKIV GNLLYYRYMN PAIVAPDGFD IIDMTAGGQI NSDQRRNLGS
VAKVLQHAAS NKLFEGENEH LSSMNNYLSE TYQEFRKYFK EACNVPEPEE KFNMDKYTDL
VTVSKPVIYI SIEEIISTHS LLLEHQDAIA PEKNDLLSEL LGSLGEVPTV ESFLGEGAVD
PNDPNKANTL SQLSKTEISL VLTSKYDIED GEAIDSRSLM IKTKKLIIDV IRNQPGNTLT
EILETPATAQ QEVDHATDMV SRAMIDSRTP EEMKHSQSMI EDAQLPLEQK KRKIQRNLRT
LEQTGHVSSE NKYQDILNEI AKDIRNQRIY RKLRKAELAK LQQTLNALNK KAAFYEEQIN
YYDTYIKTCL DNLKRKNTRR SIKLDGKGEP KGAKRAKPVK YTAAKLHEKG VLLDIDDLQT
NQFKNVTFDI IATEDVGIFD VRSKFLGVEM EKVQLNIQDL LQMQYEGVAV MKMFDKVKVN
VNLLIYLLNK KFYGK
//
ID IQGA2_HUMAN Reviewed; 1575 AA.
AC Q13576; A8K4V1; B7Z8A4;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-MAR-2010, sequence version 4.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Ras GTPase-activating-like protein IQGAP2;
GN Name=IQGAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLU-527; GLU-532;
RP PHE-629 AND VAL-724.
RC TISSUE=Liver;
RX PubMed=8756646;
RA Brill S., Li S., Lyman C.W., Church D.M., Wasmuth J.J., Weissbach L.,
RA Bernards A., Snijders A.J.;
RT "The Ras GTPase-activating-protein-related human protein IQGAP2
RT harbors a potential actin binding domain and interacts with calmodulin
RT and Rho family GTPases.";
RL Mol. Cell. Biol. 16:4869-4878(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS GLU-527; GLU-532;
RP PHE-629 AND VAL-724.
RA Wang H., Huo R., Xu Z.Y., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning and characterization of a novel isoform of IQGAP2 in human
RT adult testis.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS GLU-527 AND GLU-532.
RC TISSUE=Teratocarcinoma, and 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-13.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-629, AND MASS SPECTROMETRY.
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., 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 [10]
RP VARIANTS CYS-1445 AND ILE-1530.
RX PubMed=23033978; DOI=10.1056/NEJMoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
RA Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
RA Brunner H.G., Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Binds to activated CDC42 and RAC1 but does not seem to
CC stimulate their GTPase activity. Associates with calmodulin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13576-2; Sequence=VSP_010629, VSP_010630, VSP_010631;
CC -!- TISSUE SPECIFICITY: Isoform 2 expression is enhanced in testis.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 3 IQ domains.
CC -!- SIMILARITY: Contains 1 Ras-GAP domain.
CC -!- SIMILARITY: Contains 1 WW domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U51903; AAB37765.1; -; mRNA.
DR EMBL; AY351902; AAQ81291.1; -; mRNA.
DR EMBL; AK291066; BAF83755.1; -; mRNA.
DR EMBL; AK303054; BAH13890.1; -; mRNA.
DR EMBL; AC025188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001272389.1; NM_001285460.1.
DR RefSeq; NP_001272390.1; NM_001285461.1.
DR RefSeq; NP_001272391.1; NM_001285462.1.
DR RefSeq; NP_006624.2; NM_006633.3.
DR UniGene; Hs.291030; -.
DR PDB; 3IEZ; X-ray; 1.50 A; A/B=1476-1571.
DR PDB; 4EZA; X-ray; 1.50 A; A/B=1476-1571.
DR PDBsum; 3IEZ; -.
DR PDBsum; 4EZA; -.
DR ProteinModelPortal; Q13576; -.
DR SMR; Q13576; 23-207, 875-1252, 1477-1571.
DR DIP; DIP-27542N; -.
DR IntAct; Q13576; 12.
DR MINT; MINT-5004527; -.
DR STRING; 9606.ENSP00000274364; -.
DR PhosphoSite; Q13576; -.
DR DMDM; 292495090; -.
DR OGP; Q13576; -.
DR PaxDb; Q13576; -.
DR PRIDE; Q13576; -.
DR DNASU; 10788; -.
DR Ensembl; ENST00000274364; ENSP00000274364; ENSG00000145703.
DR Ensembl; ENST00000396234; ENSP00000379535; ENSG00000145703.
DR GeneID; 10788; -.
DR KEGG; hsa:10788; -.
DR UCSC; uc003kek.3; human.
DR CTD; 10788; -.
DR GeneCards; GC05P075699; -.
DR HGNC; HGNC:6111; IQGAP2.
DR HPA; CAB004241; -.
DR MIM; 605401; gene.
DR neXtProt; NX_Q13576; -.
DR PharmGKB; PA29911; -.
DR eggNOG; COG5261; -.
DR HOGENOM; HOG000004842; -.
DR HOVERGEN; HBG052143; -.
DR InParanoid; Q13576; -.
DR KO; K05767; -.
DR OMA; MEKVQLH; -.
DR OrthoDB; EOG7FNC6M; -.
DR PhylomeDB; Q13576; -.
DR EvolutionaryTrace; Q13576; -.
DR GenomeRNAi; 10788; -.
DR NextBio; 40978; -.
DR PRO; PR:Q13576; -.
DR ArrayExpress; Q13576; -.
DR Bgee; Q13576; -.
DR CleanEx; HS_IQGAP2; -.
DR Genevestigator; Q13576; -.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005099; F:Ras GTPase activator activity; IEA:InterPro.
DR GO; GO:0032320; P:positive regulation of Ras GTPase activity; IEA:GOC.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001936; RasGAP.
DR InterPro; IPR000593; RasGAP_C.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001202; WW_dom.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF03836; RasGAP_C; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48350; SSF48350; 2.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calmodulin-binding;
KW Complete proteome; Direct protein sequencing; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1575 Ras GTPase-activating-like protein
FT IQGAP2.
FT /FTId=PRO_0000056650.
FT DOMAIN 41 156 CH.
FT DOMAIN 594 627 WW.
FT DOMAIN 690 719 IQ 1.
FT DOMAIN 720 749 IQ 2.
FT DOMAIN 750 779 IQ 3.
FT DOMAIN 917 1150 Ras-GAP.
FT COMPBIAS 263 266 Poly-Lys.
FT MOD_RES 16 16 Phosphoserine.
FT VAR_SEQ 1 447 Missing (in isoform 2).
FT /FTId=VSP_010629.
FT VAR_SEQ 448 453 QEENDR -> MHSLPG (in isoform 2).
FT /FTId=VSP_010630.
FT VAR_SEQ 642 698 Missing (in isoform 2).
FT /FTId=VSP_010631.
FT VARIANT 455 455 V -> A (in dbSNP:rs7722711).
FT /FTId=VAR_055823.
FT VARIANT 479 479 P -> R (in dbSNP:rs3822530).
FT /FTId=VAR_055824.
FT VARIANT 527 527 D -> E (in dbSNP:rs2431352).
FT /FTId=VAR_062958.
FT VARIANT 532 532 K -> E (in dbSNP:rs2909888).
FT /FTId=VAR_059292.
FT VARIANT 629 629 L -> F (in dbSNP:rs2455230).
FT /FTId=VAR_062959.
FT VARIANT 714 714 R -> W (in dbSNP:rs35366349).
FT /FTId=VAR_055825.
FT VARIANT 724 724 I -> V (in dbSNP:rs2431363).
FT /FTId=VAR_062960.
FT VARIANT 894 894 T -> I (in dbSNP:rs34950321).
FT /FTId=VAR_055826.
FT VARIANT 1052 1052 R -> I (in dbSNP:rs2287932).
FT /FTId=VAR_055827.
FT VARIANT 1184 1184 N -> S (in dbSNP:rs10454915).
FT /FTId=VAR_055828.
FT VARIANT 1379 1379 R -> W (in dbSNP:rs17681908).
FT /FTId=VAR_055829.
FT VARIANT 1445 1445 Y -> C.
FT /FTId=VAR_069434.
FT VARIANT 1530 1530 M -> I.
FT /FTId=VAR_069435.
FT CONFLICT 95 95 V -> E (in Ref. 3; BAF83755).
FT CONFLICT 778 778 N -> S (in Ref. 3; BAF83755).
FT CONFLICT 1101 1101 G -> R (in Ref. 3; BAF83755).
FT CONFLICT 1333 1333 V -> L (in Ref. 3; BAH13890).
FT STRAND 1479 1482
FT HELIX 1483 1488
FT STRAND 1491 1495
FT HELIX 1500 1505
FT STRAND 1506 1512
FT STRAND 1518 1525
FT STRAND 1528 1536
FT HELIX 1537 1545
FT STRAND 1550 1554
FT STRAND 1557 1560
FT HELIX 1561 1569
SQ SEQUENCE 1575 AA; 180578 MW; BCC8CED6645CB09B CRC64;
MPHEELPSLQ RPRYGSIVDD ERLSAEEMDE RRRQNIAYEY LCHLEEAKRW MEVCLVEELP
PTTELEEGLR NGVYLAKLAK FFAPKMVSEK KIYDVEQTRY KKSGLHFRHT DNTVQWLRAM
ESIGLPKIFY PETTDVYDRK NIPRMIYCIH ALSLYLFKLG IAPQIQDLLG KVDFTEEEIS
NMRKELEKYG IQMPSFSKIG GILANELSVD EAALHAAVIA INEAVEKGIA EQTVVTLRNP
NAVLTLVDDN LAPEYQKELW DAKKKKEENA RLKNSCISEE ERDAYEELLT QAEIQGNINK
VNRQAAVDHI NAVIPEGDPE NTLLALKKPE AQLPAVYPFA AAMYQNELFN LQKQNTMNYL
AHEELLIAVE MLSAVALLNQ ALESNDLVSV QNQLRSPAIG LNNLDKAYVE RYANTLLSVK
LEVLSQGQDN LSWNEIQNCI DMVNAQIQEE NDRVVAVGYI NEAIDEGNPL RTLETLLLPT
ANISDVDPAH AQHYQDVLYH AKSQKLGDSE SVSKVLWLDE IQQAVDDANV DKDRAKQWVT
LVVDVNQCLE GKKSSDILSV LKSSTSNAND IIPECADKYY DALVKAKELK SERVSSDGSW
LKLNLHKKYD YYYNTDSKES SWVTPESCLY KESWLTGKEI EDIIEEVTVG YIRENIWSAS
EELLLRFQAT SSGPILREEF EARKSFLHEQ EENVVKIQAF WKGYKQRKEY MHRRQTFIDN
TDSIVKIQSW FRMATARKSY LSRLQYFRDH NNEIVKIQSL LRANKARDDY KTLVGSENPP
LTVIRKFVYL LDQSDLDFQE ELEVARLREE VVTKIRANQQ LEKDLNLMDI KIGLLVKNRI
TLEDVISHSK KLNKKKGGEM EILNNTDNQG IKSLSKERRK TLETYQQLFY LLQTNPLYLA
KLIFQMPQNK STKFMDTVIF TLYNYASNQR EEYLLLKLFK TALEEEIKSK VDQVQDIVTG
NPTVIKMVVS FNRGARGQNT LRQLLAPVVK EIIDDKSLII NTNPVEVYKA WVNQLETQTG
EASKLPYDVT TEQALTYPEV KNKLEASIEN LRRVTDKVLN SIISSLDLLP YGLRYIAKVL
KNSIHEKFPD ATEDELLKIV GNLLYYRYMN PAIVAPDGFD IIDMTAGGQI NSDQRRNLGS
VAKVLQHAAS NKLFEGENEH LSSMNNYLSE TYQEFRKYFK EACNVPEPEE KFNMDKYTDL
VTVSKPVIYI SIEEIISTHS LLLEHQDAIA PEKNDLLSEL LGSLGEVPTV ESFLGEGAVD
PNDPNKANTL SQLSKTEISL VLTSKYDIED GEAIDSRSLM IKTKKLIIDV IRNQPGNTLT
EILETPATAQ QEVDHATDMV SRAMIDSRTP EEMKHSQSMI EDAQLPLEQK KRKIQRNLRT
LEQTGHVSSE NKYQDILNEI AKDIRNQRIY RKLRKAELAK LQQTLNALNK KAAFYEEQIN
YYDTYIKTCL DNLKRKNTRR SIKLDGKGEP KGAKRAKPVK YTAAKLHEKG VLLDIDDLQT
NQFKNVTFDI IATEDVGIFD VRSKFLGVEM EKVQLNIQDL LQMQYEGVAV MKMFDKVKVN
VNLLIYLLNK KFYGK
//
MIM
605401
*RECORD*
*FIELD* NO
605401
*FIELD* TI
*605401 IQ MOTIF-CONTAINING GTPase-ACTIVATING PROTEIN 2; IQGAP2
*FIELD* TX
CLONING
read more
GTPase-activating proteins (GAPs) accelerate the intrinsic GTPase
activity of Ras proteins, resulting in conversion of these GTPases from
their active GTP-bound form to the inactive GDP-bound form (see 139150).
IQ motif-containing GAP1 (IQGAP1; 603379) was identified based on its
homology to a RasGAP homolog from S. pombe, Sar1. Brill et al. (1996)
identified IQGAP2 by screening a mouse brain cDNA library with a human
IQGAP1 probe at low stringency. Human IQGAP2 cDNA clones were then
isolated from liver cDNA libraries. The assembled full-length sequence
encodes a 1,575-amino acid protein that is 62% identical to IQGAP1 and
contains all domains previously identified in IQGAP1. These domains
include a calponin homology (CH) domain, which is present in several
actin-binding proteins; an IQGAP repeat domain containing 5 copies of a
novel 50- to 55-amino acid repeat; a WW putative protein interaction
domain; and 4 IQ motifs implicated in calmodulin (CALM1; 114180)
binding. Like IQGAP1, IQGAP2 has several segments that have a high
probability of forming coiled-coil structures similar to those in myosin
heavy chains and intermediate filament proteins. IQGAP1 and IQGAP2 also
share 25% amino acid identity with Sar1 over a 700-amino acid region.
Northern blot analysis detected expression of an IQGAP2 transcript in
mouse liver and of a shorter transcript in mouse testis. IQGAP2
expression was also detected in human hepatoblastoma and hepatocellular
carcinoma cell lines, suggesting that IQGAP2 is expressed within
hepatocytes in the liver.
GENE FUNCTION
By transfection and coprecipitation experiments, Brill et al. (1996)
demonstrated that IQGAP2 bound CALM1 and that this binding required the
IQ motifs of IQGAP2. IQGAP2 also bound the GTPases CDC42 (116952) and
RAC1 (602048) through its C terminus, but it showed no evidence of GAP
activity toward them.
MAPPING
By Southern blot analysis of somatic cell hybrid DNA, Brill et al.
(1996) mapped the IQGAP2 gene to chromosome 5q11-q13.
*FIELD* RF
1. Brill, S.; Li, S.; Lyman, C. W.; Church, D. M.; Wasmuth, J. J.;
Weissbach, L.; Bernards, A.; Snijders, A. J.: The Ras GTPase-activating-protein-related
human protein IQGAP2 harbors a potential actin binding domain and
interacts with calmodulin and Rho family GTPases. Molec. Cell. Biol. 16:
4869-4878, 1996.
*FIELD* CD
Dawn Watkins-Chow: 11/14/2000
*FIELD* ED
mgross: 04/13/2010
carol: 11/17/2000
carol: 11/16/2000
*RECORD*
*FIELD* NO
605401
*FIELD* TI
*605401 IQ MOTIF-CONTAINING GTPase-ACTIVATING PROTEIN 2; IQGAP2
*FIELD* TX
CLONING
read more
GTPase-activating proteins (GAPs) accelerate the intrinsic GTPase
activity of Ras proteins, resulting in conversion of these GTPases from
their active GTP-bound form to the inactive GDP-bound form (see 139150).
IQ motif-containing GAP1 (IQGAP1; 603379) was identified based on its
homology to a RasGAP homolog from S. pombe, Sar1. Brill et al. (1996)
identified IQGAP2 by screening a mouse brain cDNA library with a human
IQGAP1 probe at low stringency. Human IQGAP2 cDNA clones were then
isolated from liver cDNA libraries. The assembled full-length sequence
encodes a 1,575-amino acid protein that is 62% identical to IQGAP1 and
contains all domains previously identified in IQGAP1. These domains
include a calponin homology (CH) domain, which is present in several
actin-binding proteins; an IQGAP repeat domain containing 5 copies of a
novel 50- to 55-amino acid repeat; a WW putative protein interaction
domain; and 4 IQ motifs implicated in calmodulin (CALM1; 114180)
binding. Like IQGAP1, IQGAP2 has several segments that have a high
probability of forming coiled-coil structures similar to those in myosin
heavy chains and intermediate filament proteins. IQGAP1 and IQGAP2 also
share 25% amino acid identity with Sar1 over a 700-amino acid region.
Northern blot analysis detected expression of an IQGAP2 transcript in
mouse liver and of a shorter transcript in mouse testis. IQGAP2
expression was also detected in human hepatoblastoma and hepatocellular
carcinoma cell lines, suggesting that IQGAP2 is expressed within
hepatocytes in the liver.
GENE FUNCTION
By transfection and coprecipitation experiments, Brill et al. (1996)
demonstrated that IQGAP2 bound CALM1 and that this binding required the
IQ motifs of IQGAP2. IQGAP2 also bound the GTPases CDC42 (116952) and
RAC1 (602048) through its C terminus, but it showed no evidence of GAP
activity toward them.
MAPPING
By Southern blot analysis of somatic cell hybrid DNA, Brill et al.
(1996) mapped the IQGAP2 gene to chromosome 5q11-q13.
*FIELD* RF
1. Brill, S.; Li, S.; Lyman, C. W.; Church, D. M.; Wasmuth, J. J.;
Weissbach, L.; Bernards, A.; Snijders, A. J.: The Ras GTPase-activating-protein-related
human protein IQGAP2 harbors a potential actin binding domain and
interacts with calmodulin and Rho family GTPases. Molec. Cell. Biol. 16:
4869-4878, 1996.
*FIELD* CD
Dawn Watkins-Chow: 11/14/2000
*FIELD* ED
mgross: 04/13/2010
carol: 11/17/2000
carol: 11/16/2000