ARHGC_HUMAN
ID ARHGC_HUMAN Reviewed; 1544 AA.
AC Q9NZN5; O15086; Q6P526;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Rho guanine nucleotide exchange factor 12;
DE AltName: Full=Leukemia-associated RhoGEF;
GN Name=ARHGEF12; Synonyms=KIAA0382, LARG;
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] (ISOFORMS 1 AND 2), AND CHROMOSOMAL
RP TRANSLOCATION.
RC TISSUE=Prostate;
RX PubMed=10681437; DOI=10.1073/pnas.040569197;
RA Kourlas P.J., Strout M.P., Becknell B., Veronese M.L., Croce C.M.,
RA Theil K.S., Krahe R., Ruutu T., Knuutila S., Bloomfield C.D.,
RA Caligiuri M.A.;
RT "Identification of a gene at 11q23 encoding a guanine nucleotide exchange
RT factor: evidence for its fusion with MLL in acute myeloid leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2145-2150(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-584 (ISOFORM 2).
RC TISSUE=Thyroid;
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 102-1544, AND VARIANT PHE-973.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INTERACTION WITH RHOA; GNA12 AND GNA13.
RX PubMed=11094164; DOI=10.1016/s0014-5793(00)02224-9;
RA Fukuhara S., Chikumi H., Gutkind J.S.;
RT "Leukemia-associated Rho guanine nucleotide exchange factor (LARG) links
RT heterotrimeric G proteins of the G(12) family to Rho.";
RL FEBS Lett. 485:183-188(2000).
RN [6]
RP INTERACTION WITH IGF1R.
RX PubMed=11724822; DOI=10.1083/jcb.200106139;
RA Taya S., Inagaki N., Sengiku H., Makino H., Iwamatsu A., Urakawa I.,
RA Nagao K., Kataoka S., Kaibuchi K.;
RT "Direct interaction of insulin-like growth factor-1 receptor with leukemia-
RT associated RhoGEF.";
RL J. Cell Biol. 155:809-820(2001).
RN [7]
RP INTERACTION WITH PLXNB1 AND PLXNB2.
RX PubMed=12372594; DOI=10.1016/s0014-5793(02)03323-9;
RA Driessens M.H.E., Olivo C., Nagata K., Inagaki M., Collard J.G.;
RT "B plexins activate Rho through PDZ-RhoGEF.";
RL FEBS Lett. 529:168-172(2002).
RN [8]
RP INTERACTION WITH PLXNB1 AND PLXNB2.
RX PubMed=12183458; DOI=10.1074/jbc.m206005200;
RA Perrot V., Vazquez-Prado J., Gutkind J.S.;
RT "Plexin B regulates Rho through the guanine nucleotide exchange factors
RT leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF.";
RL J. Biol. Chem. 277:43115-43120(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-736, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-41 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP IDENTIFICATION BY 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 [15]
RP INTERACTION WITH GCSAM.
RX PubMed=20844236; DOI=10.1182/blood-2010-04-281568;
RA Jiang X., Lu X., McNamara G., Liu X., Cubedo E., Sarosiek K.A.,
RA Sanchez-Garcia I., Helfman D.M., Lossos I.S.;
RT "HGAL, a germinal center specific protein, decreases lymphoma cell motility
RT by modulation of the RhoA signaling pathway.";
RL Blood 116:5217-5227(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-309; SER-341;
RP SER-637; THR-736 AND SER-1288, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-637; SER-1327;
RP SER-1377; SER-1457 AND SER-1541, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-41 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 766-1138 IN COMPLEX WITH RHOA,
RP AND SUBUNIT.
RX PubMed=15331592; DOI=10.1074/jbc.m406056200;
RA Kristelly R., Gao G., Tesmer J.J.;
RT "Structural determinants of RhoA binding and nucleotide exchange in
RT leukemia-associated Rho guanine-nucleotide exchange factor.";
RL J. Biol. Chem. 279:47352-47362(2004).
RN [21]
RP STRUCTURE BY NMR OF 67-151 IN COMPLEX WITH PLXNB1, AND SUBUNIT.
RX PubMed=18411422; DOI=10.1110/ps.073416508;
RA Liu J., Zhang J., Yang Y., Huang H., Shen W., Hu Q., Wang X., Wu J.,
RA Shi Y.;
RT "Conformational change upon ligand binding and dynamics of the PDZ domain
RT from leukemia-associated Rho guanine nucleotide exchange factor.";
RL Protein Sci. 17:1003-1014(2008).
CC -!- FUNCTION: May play a role in the regulation of RhoA GTPase by guanine
CC nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as
CC guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as
CC GTPase-activating protein (GAP) for GNA12 and GNA13.
CC {ECO:0000269|PubMed:11094164}.
CC -!- SUBUNIT: Interacts with GNA12 and GNA13, probably through the RGS-like
CC domain. Interacts with RHOA, PLXNB1 and PLXNB2. Interacts through its
CC PDZ domain with IGF1R beta subunit. Interacts with GCSAM.
CC {ECO:0000269|PubMed:11094164, ECO:0000269|PubMed:11724822,
CC ECO:0000269|PubMed:12183458, ECO:0000269|PubMed:12372594,
CC ECO:0000269|PubMed:15331592, ECO:0000269|PubMed:18411422,
CC ECO:0000269|PubMed:20844236}.
CC -!- INTERACTION:
CC Q9NZN5; P08069: IGF1R; NbExp=7; IntAct=EBI-821440, EBI-475981;
CC Q9NZN5; P61586: RHOA; NbExp=2; IntAct=EBI-821440, EBI-446668;
CC Q9NZN5; P61793: Lpar1; Xeno; NbExp=3; IntAct=EBI-821440, EBI-7512335;
CC Q9NZN5-1; Q96PX9: PLEKHG4B; NbExp=3; IntAct=EBI-9640168, EBI-11741362;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}.
CC Note=Translocated to the membrane upon stimulation. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZN5-2; Sequence=VSP_008131;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is found in
CC jejunum and testis.
CC -!- DISEASE: Note=A chromosomal aberration involving ARHGEF12 may be a
CC cause of acute leukemia. Translocation t(11;11)(q23;23) with
CC KMT2A/MLL1. {ECO:0000269|PubMed:10681437}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63117.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LARGID243.html";
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DR EMBL; AF180681; AAF36817.1; -; mRNA.
DR EMBL; AB002380; BAA20836.2; -; mRNA.
DR EMBL; BC063117; AAH63117.1; ALT_SEQ; mRNA.
DR CCDS; CCDS41727.1; -. [Q9NZN5-1]
DR CCDS; CCDS55794.1; -. [Q9NZN5-2]
DR RefSeq; NP_001185594.1; NM_001198665.1. [Q9NZN5-2]
DR RefSeq; NP_001288013.1; NM_001301084.1.
DR RefSeq; NP_056128.1; NM_015313.2. [Q9NZN5-1]
DR RefSeq; XP_011541022.1; XM_011542720.2.
DR RefSeq; XP_016872910.1; XM_017017421.1.
DR PDB; 1TXD; X-ray; 2.13 A; A=766-1138.
DR PDB; 1X86; X-ray; 3.22 A; A/C/E/G=766-1138.
DR PDB; 2OMJ; NMR; -; A=67-151.
DR PDB; 2OS6; NMR; -; A=67-151.
DR PDBsum; 1TXD; -.
DR PDBsum; 1X86; -.
DR PDBsum; 2OMJ; -.
DR PDBsum; 2OS6; -.
DR AlphaFoldDB; Q9NZN5; -.
DR BMRB; Q9NZN5; -.
DR SMR; Q9NZN5; -.
DR BioGRID; 116945; 117.
DR DIP; DIP-37887N; -.
DR IntAct; Q9NZN5; 31.
DR MINT; Q9NZN5; -.
DR STRING; 9606.ENSP00000380942; -.
DR ChEMBL; CHEMBL4523477; -.
DR GlyGen; Q9NZN5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZN5; -.
DR PhosphoSitePlus; Q9NZN5; -.
DR BioMuta; ARHGEF12; -.
DR DMDM; 34395525; -.
DR EPD; Q9NZN5; -.
DR jPOST; Q9NZN5; -.
DR MassIVE; Q9NZN5; -.
DR MaxQB; Q9NZN5; -.
DR PaxDb; Q9NZN5; -.
DR PeptideAtlas; Q9NZN5; -.
DR PRIDE; Q9NZN5; -.
DR ProteomicsDB; 83460; -. [Q9NZN5-1]
DR ProteomicsDB; 83461; -. [Q9NZN5-2]
DR Antibodypedia; 9144; 171 antibodies from 27 providers.
DR DNASU; 23365; -.
DR Ensembl; ENST00000356641.7; ENSP00000349056.3; ENSG00000196914.9. [Q9NZN5-2]
DR Ensembl; ENST00000397843.7; ENSP00000380942.2; ENSG00000196914.9. [Q9NZN5-1]
DR GeneID; 23365; -.
DR KEGG; hsa:23365; -.
DR MANE-Select; ENST00000397843.7; ENSP00000380942.2; NM_015313.3; NP_056128.1.
DR UCSC; uc001pxl.3; human. [Q9NZN5-1]
DR CTD; 23365; -.
DR DisGeNET; 23365; -.
DR GeneCards; ARHGEF12; -.
DR HGNC; HGNC:14193; ARHGEF12.
DR HPA; ENSG00000196914; Low tissue specificity.
DR MIM; 604763; gene.
DR neXtProt; NX_Q9NZN5; -.
DR OpenTargets; ENSG00000196914; -.
DR PharmGKB; PA24969; -.
DR VEuPathDB; HostDB:ENSG00000196914; -.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000157662; -.
DR HOGENOM; CLU_003962_1_0_1; -.
DR InParanoid; Q9NZN5; -.
DR OMA; GNIGELM; -.
DR PhylomeDB; Q9NZN5; -.
DR TreeFam; TF106495; -.
DR PathwayCommons; Q9NZN5; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR SignaLink; Q9NZN5; -.
DR SIGNOR; Q9NZN5; -.
DR BioGRID-ORCS; 23365; 22 hits in 1075 CRISPR screens.
DR ChiTaRS; ARHGEF12; human.
DR EvolutionaryTrace; Q9NZN5; -.
DR GeneWiki; ARHGEF12; -.
DR GenomeRNAi; 23365; -.
DR Pharos; Q9NZN5; Tchem.
DR PRO; PR:Q9NZN5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NZN5; protein.
DR Bgee; ENSG00000196914; Expressed in upper leg skin and 203 other tissues.
DR ExpressionAtlas; Q9NZN5; baseline and differential.
DR Genevisible; Q9NZN5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR CDD; cd13390; PH_LARG; 1.
DR CDD; cd08754; RGS_LARG; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR037801; ARHGEF12_PH.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR037884; LARG_RGS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Coiled coil; Cytoplasm; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Proto-oncogene; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1544
FT /note="Rho guanine nucleotide exchange factor 12"
FT /id="PRO_0000080930"
FT DOMAIN 72..151
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 367..558
FT /note="RGSL"
FT DOMAIN 787..977
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1019..1132
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..262
FT /evidence="ECO:0000255"
FT COMPBIAS 13..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 308..309
FT /note="Breakpoint for translocation to form KMT2A/MLL1-
FT ARHGEF12 oncogene"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 736
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 48..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10681437,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008131"
FT VARIANT 973
FT /note="Y -> F (in dbSNP:rs2305013)"
FT /evidence="ECO:0000269|PubMed:9205841"
FT /id="VAR_020191"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2OMJ"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2OMJ"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2OMJ"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2OMJ"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:2OMJ"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:2OMJ"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2OS6"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:2OMJ"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:2OMJ"
FT HELIX 769..772
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 775..778
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 783..812
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 814..820
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 825..832
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 835..853
FT /evidence="ECO:0007829|PDB:1TXD"
FT STRAND 857..860
FT /evidence="ECO:0007829|PDB:1X86"
FT HELIX 865..872
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 875..889
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 891..904
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 906..917
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 919..921
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 926..929
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 932..949
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 954..993
FT /evidence="ECO:0007829|PDB:1TXD"
FT STRAND 1001..1003
FT /evidence="ECO:0007829|PDB:1X86"
FT HELIX 1005..1007
FT /evidence="ECO:0007829|PDB:1X86"
FT HELIX 1008..1011
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 1015..1017
FT /evidence="ECO:0007829|PDB:1TXD"
FT STRAND 1020..1033
FT /evidence="ECO:0007829|PDB:1TXD"
FT STRAND 1038..1053
FT /evidence="ECO:0007829|PDB:1TXD"
FT STRAND 1056..1058
FT /evidence="ECO:0007829|PDB:1TXD"
FT STRAND 1078..1081
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 1082..1084
FT /evidence="ECO:0007829|PDB:1TXD"
FT STRAND 1085..1089
FT /evidence="ECO:0007829|PDB:1TXD"
FT STRAND 1091..1093
FT /evidence="ECO:0007829|PDB:1X86"
FT STRAND 1096..1102
FT /evidence="ECO:0007829|PDB:1TXD"
FT STRAND 1107..1113
FT /evidence="ECO:0007829|PDB:1TXD"
FT HELIX 1117..1137
FT /evidence="ECO:0007829|PDB:1TXD"
FT MOD_RES Q9NZN5-2:41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"
SQ SEQUENCE 1544 AA; 173232 MW; 0B7E319CF7C7A224 CRC64;
MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERIA SHDFDPTDSS SKKTKSSSEE
SRSEIYGLVQ RCVIIQKDDN GFGLTVSGDN PVFVQSVKED GAAMRAGVQT GDRIIKVNGT
LVTHSNHLEV VKLIKSGSYV ALTVQGRPPG SPQIPLADSE VEPSVIGHMS PIMTSPHSPG
ASGNMERITS PVLMGEENNV VHNQKVEILR KMLQKEQERL QLLQEDYNRT PAQRLLKEIQ
EAKKHIPQLQ EQLSKATGSA QDGAVVTPSR PLGDTLTVSE AETDPGDVLG RTDCSSGDAS
RPSSDNADSP KSGPKERIYL EENPEKSETI QDTDTQSLVG SPSTRIAPHI IGAEDDDFGT
EHEQINGQCS CFQSIELLKS RPAHLAVFLH HVVSQFDPAT LLCYLYSDLY KHTNSKETRR
IFLEFHQFFL DRSAHLKVSV PDEMSADLEK RRPELIPEDL HRHYIQTMQE RVHPEVQRHL
EDFRQKRSMG LTLAESELTK LDAERDKDRL TLEKERTCAE QIVAKIEEVL MTAQAVEEDK
SSTMQYVILM YMKHLGVKVK EPRNLEHKRG RIGFLPKIKQ SMKKDKEGEE KGKRRGFPSI
LGPPRRPSRH DNSAIGRAME LQKARHPKHL STPSSVSPEP QDSAKLRQSG LANEGTDAGY
LPANSMSSVA SGASFSQEGG KENDTGSKQV GETSAPGDTL DGTPRTLNTV FDFPPPPLDQ
VQEEECEVER VTEHGTPKPF RKFDSVAFGE SQSEDEQFEN DLETDPPNWQ QLVSREVLLG
LKPCEIKRQE VINELFYTER AHVRTLKVLD QVFYQRVSRE GILSPSELRK IFSNLEDILQ
LHIGLNEQMK AVRKRNETSV IDQIGEDLLT WFSGPGEEKL KHAAATFCSN QPFALEMIKS
RQKKDSRFQT FVQDAESNPL CRRLQLKDII PTQMQRLTKY PLLLDNIAKY TEWPTEREKV
KKAADHCRQI LNYVNQAVKE AENKQRLEDY QRRLDTSSLK LSEYPNVEEL RNLDLTKRKM
IHEGPLVWKV NRDKTIDLYT LLLEDILVLL QKQDDRLVLR CHSKILASTA DSKHTFSPVI
KLSTVLVRQV ATDNKALFVI SMSDNGAQIY ELVAQTVSEK TVWQDLICRM AASVKEQSTK
PIPLPQSTPG EGDNDEEDPS KLKEEQHGIS VTGLQSPDRD LGLESTLISS KPQSHSLSTS
GKSEVRDLFV AERQFAKEQH TDGTLKEVGE DYQIAIPDSH LPVSEERWAL DALRNLGLLK
QLLVQQLGLT EKSVQEDWQH FPRYRTASQG PQTDSVIQNS ENIKAYHSGE GHMPFRTGTG
DIATCYSPRT STESFAPRDS VGLAPQDSQA SNILVMDHMI MTPEMPTMEP EGGLDDSGEH
FFDAREAHSD ENPSEGDGAV NKEEKDVNLR ISGNYLILDG YDPVQESSTD EEVASSLTLQ
PMTGIPAVES THQQQHSPQN THSDGAISPF TPEFLVQQRW GAMEYSCFEI QSPSSCADSQ
SQIMEYIHKI EADLEHLKKV EESYTILCQR LAGSALTDKH SDKS
