IQGA2_HUMAN
ID IQGA2_HUMAN Reviewed; 1575 AA.
AC Q13576; A8K4V1; B7Z8A4; J3KR91;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 4.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Ras GTPase-activating-like protein IQGAP2;
GN Name=IQGAP2;
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 [MRNA] (ISOFORM 1), AND VARIANTS GLU-527; GLU-532;
RP PHE-629 AND VAL-724.
RC TISSUE=Liver;
RX PubMed=8756646; DOI=10.1128/mcb.16.9.4869;
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 harbors a
RT potential actin binding domain and interacts with calmodulin and Rho family
RT 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 adult
RT testis.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., 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 (ISOFORM 1).
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT 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 enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-595; SER-1358 AND
RP SER-1461, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-356; SER-599;
RP SER-685; THR-716; THR-782; THR-1002; THR-1269; SER-1271; SER-1279 AND
RP SER-1358, AND IDENTIFICATION BY 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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-629, AND IDENTIFICATION BY MASS
RP 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 [13]
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., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA 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=3;
CC Name=1;
CC IsoId=Q13576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13576-2; Sequence=VSP_010629, VSP_010630, VSP_010631;
CC Name=3;
CC IsoId=Q13576-3; Sequence=VSP_010629, VSP_055149, VSP_010631;
CC -!- TISSUE SPECIFICITY: Isoform 2 expression is enhanced in testis.
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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 CCDS; CCDS34188.1; -. [Q13576-1]
DR CCDS; CCDS68897.1; -. [Q13576-2]
DR CCDS; CCDS68898.1; -. [Q13576-3]
DR RefSeq; NP_001272389.1; NM_001285460.1.
DR RefSeq; NP_001272390.1; NM_001285461.1. [Q13576-2]
DR RefSeq; NP_001272391.1; NM_001285462.1. [Q13576-3]
DR RefSeq; NP_006624.2; NM_006633.3. [Q13576-1]
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 PDB; 5CJP; X-ray; 2.60 A; E/F=875-1258.
DR PDBsum; 3IEZ; -.
DR PDBsum; 4EZA; -.
DR PDBsum; 5CJP; -.
DR AlphaFoldDB; Q13576; -.
DR SMR; Q13576; -.
DR BioGRID; 116004; 133.
DR CORUM; Q13576; -.
DR DIP; DIP-27542N; -.
DR IntAct; Q13576; 35.
DR MINT; Q13576; -.
DR STRING; 9606.ENSP00000274364; -.
DR CarbonylDB; Q13576; -.
DR GlyGen; Q13576; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q13576; -.
DR MetOSite; Q13576; -.
DR PhosphoSitePlus; Q13576; -.
DR BioMuta; IQGAP2; -.
DR DMDM; 292495090; -.
DR OGP; Q13576; -.
DR EPD; Q13576; -.
DR jPOST; Q13576; -.
DR MassIVE; Q13576; -.
DR MaxQB; Q13576; -.
DR PaxDb; Q13576; -.
DR PeptideAtlas; Q13576; -.
DR PRIDE; Q13576; -.
DR ProteomicsDB; 59581; -. [Q13576-1]
DR ProteomicsDB; 59582; -. [Q13576-2]
DR Antibodypedia; 3789; 203 antibodies from 33 providers.
DR DNASU; 10788; -.
DR Ensembl; ENST00000274364.11; ENSP00000274364.6; ENSG00000145703.17. [Q13576-1]
DR Ensembl; ENST00000396234.7; ENSP00000379535.3; ENSG00000145703.17. [Q13576-2]
DR Ensembl; ENST00000502745.5; ENSP00000426027.1; ENSG00000145703.17. [Q13576-3]
DR GeneID; 10788; -.
DR KEGG; hsa:10788; -.
DR MANE-Select; ENST00000274364.11; ENSP00000274364.6; NM_006633.5; NP_006624.3.
DR UCSC; uc003kek.5; human. [Q13576-1]
DR CTD; 10788; -.
DR DisGeNET; 10788; -.
DR GeneCards; IQGAP2; -.
DR HGNC; HGNC:6111; IQGAP2.
DR HPA; ENSG00000145703; Tissue enhanced (liver).
DR MIM; 605401; gene.
DR neXtProt; NX_Q13576; -.
DR OpenTargets; ENSG00000145703; -.
DR PharmGKB; PA29911; -.
DR VEuPathDB; HostDB:ENSG00000145703; -.
DR eggNOG; KOG2128; Eukaryota.
DR GeneTree; ENSGT00950000183076; -.
DR HOGENOM; CLU_000972_2_1_1; -.
DR InParanoid; Q13576; -.
DR OMA; PECANKY; -.
DR OrthoDB; 674320at2759; -.
DR PhylomeDB; Q13576; -.
DR TreeFam; TF313078; -.
DR PathwayCommons; Q13576; -.
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; Q13576; -.
DR BioGRID-ORCS; 10788; 12 hits in 1082 CRISPR screens.
DR ChiTaRS; IQGAP2; human.
DR EvolutionaryTrace; Q13576; -.
DR GeneWiki; IQGAP2; -.
DR GenomeRNAi; 10788; -.
DR Pharos; Q13576; Tbio.
DR PRO; PR:Q13576; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q13576; protein.
DR Bgee; ENSG00000145703; Expressed in jejunal mucosa and 165 other tissues.
DR ExpressionAtlas; Q13576; baseline and differential.
DR Genevisible; Q13576; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
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:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; IDA:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR000593; RasGAP_C.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
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; 1.
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 Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1575
FT /note="Ras GTPase-activating-like protein IQGAP2"
FT /id="PRO_0000056650"
FT DOMAIN 41..156
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 594..627
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 690..719
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 720..749
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 750..779
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 917..1150
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 716
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 881
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQ44"
FT MOD_RES 1002
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1269
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..447
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_010629"
FT VAR_SEQ 448..453
FT /note="QEENDR -> MHSLPG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010630"
FT VAR_SEQ 448..453
FT /note="QEENDR -> MGCFKG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055149"
FT VAR_SEQ 642..698
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_010631"
FT VARIANT 455
FT /note="V -> A (in dbSNP:rs7722711)"
FT /id="VAR_055823"
FT VARIANT 479
FT /note="P -> R (in dbSNP:rs3822530)"
FT /id="VAR_055824"
FT VARIANT 527
FT /note="D -> E (in dbSNP:rs2431352)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8756646, ECO:0000269|Ref.2"
FT /id="VAR_062958"
FT VARIANT 532
FT /note="K -> E (in dbSNP:rs2909888)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8756646, ECO:0000269|Ref.2"
FT /id="VAR_059292"
FT VARIANT 629
FT /note="L -> F (in dbSNP:rs2455230)"
FT /evidence="ECO:0000269|PubMed:8756646, ECO:0000269|Ref.2,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_062959"
FT VARIANT 714
FT /note="R -> W (in dbSNP:rs35366349)"
FT /id="VAR_055825"
FT VARIANT 724
FT /note="I -> V (in dbSNP:rs2431363)"
FT /evidence="ECO:0000269|PubMed:8756646, ECO:0000269|Ref.2"
FT /id="VAR_062960"
FT VARIANT 894
FT /note="T -> I (in dbSNP:rs34950321)"
FT /id="VAR_055826"
FT VARIANT 1052
FT /note="R -> I (in dbSNP:rs2287932)"
FT /id="VAR_055827"
FT VARIANT 1184
FT /note="N -> S (in dbSNP:rs10454915)"
FT /id="VAR_055828"
FT VARIANT 1379
FT /note="R -> W (in dbSNP:rs17681908)"
FT /id="VAR_055829"
FT VARIANT 1445
FT /note="Y -> C (in dbSNP:rs369078465)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069434"
FT VARIANT 1530
FT /note="M -> I (in dbSNP:rs150409607)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069435"
FT CONFLICT 95
FT /note="V -> E (in Ref. 3; BAF83755)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="N -> S (in Ref. 3; BAF83755)"
FT /evidence="ECO:0000305"
FT CONFLICT 1101
FT /note="G -> R (in Ref. 3; BAF83755)"
FT /evidence="ECO:0000305"
FT CONFLICT 1333
FT /note="V -> L (in Ref. 3; BAH13890)"
FT /evidence="ECO:0000305"
FT HELIX 878..894
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 896..905
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 908..911
FT /evidence="ECO:0007829|PDB:5CJP"
FT TURN 912..914
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 915..925
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 929..950
FT /evidence="ECO:0007829|PDB:5CJP"
FT STRAND 952..955
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 956..959
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 963..973
FT /evidence="ECO:0007829|PDB:5CJP"
FT STRAND 974..977
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 982..994
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1004..1010
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1012..1015
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1016..1018
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1031..1034
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1038..1064
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1065..1068
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1071..1087
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1093..1104
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1105..1109
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1110..1114
FT /evidence="ECO:0007829|PDB:5CJP"
FT TURN 1116..1120
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1132..1149
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1159..1164
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1165..1182
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1188..1191
FT /evidence="ECO:0007829|PDB:5CJP"
FT TURN 1192..1194
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1195..1198
FT /evidence="ECO:0007829|PDB:5CJP"
FT STRAND 1208..1214
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1223..1225
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1226..1229
FT /evidence="ECO:0007829|PDB:5CJP"
FT HELIX 1232..1243
FT /evidence="ECO:0007829|PDB:5CJP"
FT STRAND 1479..1482
FT /evidence="ECO:0007829|PDB:3IEZ"
FT HELIX 1483..1488
FT /evidence="ECO:0007829|PDB:3IEZ"
FT STRAND 1491..1495
FT /evidence="ECO:0007829|PDB:3IEZ"
FT HELIX 1500..1505
FT /evidence="ECO:0007829|PDB:3IEZ"
FT STRAND 1506..1512
FT /evidence="ECO:0007829|PDB:3IEZ"
FT STRAND 1518..1525
FT /evidence="ECO:0007829|PDB:3IEZ"
FT STRAND 1528..1536
FT /evidence="ECO:0007829|PDB:3IEZ"
FT HELIX 1537..1545
FT /evidence="ECO:0007829|PDB:3IEZ"
FT STRAND 1550..1554
FT /evidence="ECO:0007829|PDB:3IEZ"
FT STRAND 1557..1560
FT /evidence="ECO:0007829|PDB:3IEZ"
FT HELIX 1561..1569
FT /evidence="ECO:0007829|PDB:3IEZ"
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
