ARHGQ_HUMAN
ID ARHGQ_HUMAN Reviewed; 871 AA.
AC Q96DR7; B3KVP8; E9PBD0; Q68CL1; Q6AZ96; Q6Q8Q8; Q96AW8; Q96DR6; Q9H9D7;
AC Q9H9R2; Q9UFW5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Rho guanine nucleotide exchange factor 26;
DE AltName: Full=SH3 domain-containing guanine exchange factor;
GN Name=ARHGEF26; Synonyms=SGEF; ORFNames=HMFN1864;
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), TISSUE SPECIFICITY, INDUCTION, AND
RP VARIANT LEU-29.
RC TISSUE=Prostatic carcinoma;
RX PubMed=12697679; DOI=10.1210/en.2002-220984;
RA Qi H., Fournier A., Grenier J., Fillion C., Labrie Y., Labrie C.;
RT "Isolation of the novel human guanine nucleotide exchange factor Src
RT homology 3 domain-containing guanine nucleotide exchange factor (SGEF) and
RT of C-terminal SGEF, an N-terminally truncated form of SGEF, the expression
RT of which is regulated by androgen in prostate cancer cells.";
RL Endocrinology 144:1742-1752(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RHOG,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-826, AND
RP VARIANT LEU-29.
RC TISSUE=Brain;
RX PubMed=15133129; DOI=10.1091/mbc.e04-02-0146;
RA Ellerbroek S.M., Wennerberg K., Arthur W.T., Dunty J.M., Bowman D.R.,
RA DeMali K.A., Der C., Burridge K.;
RT "SGEF, a RhoG guanine nucleotide exchange factor that stimulates
RT macropinocytosis.";
RL Mol. Biol. Cell 15:3309-3319(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 402-871 (ISOFORM 1), AND VARIANT LEU-29.
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 MRNA] (ISOFORM 2), AND VARIANTS LEU-29;
RP PRO-60 AND SER-203.
RC TISSUE=Liver;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-29.
RC TISSUE=Prostate, and Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 661-871 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP FUNCTION.
RX PubMed=17074883; DOI=10.1083/jcb.200605144;
RA Patel J.C., Galan J.E.;
RT "Differential activation and function of Rho GTPases during Salmonella-host
RT cell interactions.";
RL J. Cell Biol. 175:453-463(2006).
RN [9]
RP FUNCTION, INTERACTION WITH ICAM1, AND SUBCELLULAR LOCATION.
RX PubMed=17875742; DOI=10.1083/jcb.200612053;
RA van Buul J.D., Allingham M.J., Samson T., Meller J., Boulter E.,
RA Garcia-Mata R., Burridge K.;
RT "RhoG regulates endothelial apical cup assembly downstream from ICAM1
RT engagement and is involved in leukocyte trans-endothelial migration.";
RL J. Cell Biol. 178:1279-1293(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-392, VARIANT
RP [LARGE SCALE ANALYSIS] LEU-29, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Activates RhoG GTPase by promoting the exchange of GDP by
CC GTP. Required for the formation of membrane ruffles during
CC macropinocytosis. Required for the formation of cup-like structures
CC during trans-endothelial migration of leukocytes. In case of Salmonella
CC enterica infection, activated by SopB, which induces cytoskeleton
CC rearrangements and promotes bacterial entry.
CC {ECO:0000269|PubMed:15133129, ECO:0000269|PubMed:17074883,
CC ECO:0000269|PubMed:17875742}.
CC -!- SUBUNIT: Interacts with ICAM1 and RHOG. {ECO:0000269|PubMed:15133129,
CC ECO:0000269|PubMed:17875742}.
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle
CC {ECO:0000269|PubMed:15133129, ECO:0000269|PubMed:17875742}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96DR7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DR7-3; Sequence=VSP_031934, VSP_031935;
CC Name=3;
CC IsoId=Q96DR7-4; Sequence=VSP_045570;
CC -!- TISSUE SPECIFICITY: Isoform 1 is broadly expressed, with highest levels
CC in liver (at protein level). Certain mRNA species appear to be
CC specifically expressed in prostate and liver.
CC {ECO:0000269|PubMed:12697679, ECO:0000269|PubMed:15133129}.
CC -!- INDUCTION: Certain mRNA species appear to be up-regulated by androgens
CC in prostate cancer cells. {ECO:0000269|PubMed:12697679}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16628.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL27002.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAB14159.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14292.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF415175; AAL27001.1; -; mRNA.
DR EMBL; AF415176; AAL27002.1; ALT_SEQ; mRNA.
DR EMBL; AY552599; AAS59842.1; -; mRNA.
DR EMBL; AK022655; BAB14159.1; ALT_INIT; mRNA.
DR EMBL; AK022884; BAB14292.1; ALT_INIT; mRNA.
DR EMBL; AK123040; BAG53860.1; -; mRNA.
DR EMBL; AB073386; BAD38637.1; -; mRNA.
DR EMBL; AC018452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ695204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016628; AAH16628.1; ALT_INIT; mRNA.
DR EMBL; BC078655; AAH78655.1; -; mRNA.
DR EMBL; AL117429; CAB55918.1; -; mRNA.
DR CCDS; CCDS46938.1; -. [Q96DR7-1]
DR CCDS; CCDS58858.1; -. [Q96DR7-4]
DR PIR; T17228; T17228.
DR RefSeq; NP_001238891.1; NM_001251962.1. [Q96DR7-1]
DR RefSeq; NP_001238892.1; NM_001251963.1. [Q96DR7-4]
DR RefSeq; NP_056410.3; NM_015595.3. [Q96DR7-1]
DR PDB; 6MYE; X-ray; 1.10 A; B=42-52.
DR PDBsum; 6MYE; -.
DR AlphaFoldDB; Q96DR7; -.
DR SMR; Q96DR7; -.
DR BioGRID; 117537; 40.
DR IntAct; Q96DR7; 15.
DR STRING; 9606.ENSP00000348828; -.
DR iPTMnet; Q96DR7; -.
DR PhosphoSitePlus; Q96DR7; -.
DR BioMuta; ARHGEF26; -.
DR DMDM; 317373555; -.
DR EPD; Q96DR7; -.
DR jPOST; Q96DR7; -.
DR MassIVE; Q96DR7; -.
DR MaxQB; Q96DR7; -.
DR PaxDb; Q96DR7; -.
DR PeptideAtlas; Q96DR7; -.
DR PRIDE; Q96DR7; -.
DR ProteomicsDB; 19196; -.
DR ProteomicsDB; 76307; -. [Q96DR7-1]
DR ProteomicsDB; 76308; -. [Q96DR7-3]
DR Antibodypedia; 2847; 92 antibodies from 19 providers.
DR DNASU; 26084; -.
DR Ensembl; ENST00000356448.8; ENSP00000348828.4; ENSG00000114790.13. [Q96DR7-1]
DR Ensembl; ENST00000465093.6; ENSP00000423418.1; ENSG00000114790.13. [Q96DR7-1]
DR Ensembl; ENST00000465817.1; ENSP00000423295.1; ENSG00000114790.13. [Q96DR7-3]
DR Ensembl; ENST00000496710.5; ENSP00000424446.1; ENSG00000114790.13. [Q96DR7-4]
DR Ensembl; ENST00000614308.3; ENSP00000481927.1; ENSG00000277101.4. [Q96DR7-1]
DR Ensembl; ENST00000618535.3; ENSP00000484367.1; ENSG00000277101.4. [Q96DR7-1]
DR Ensembl; ENST00000629129.2; ENSP00000486665.1; ENSG00000277101.4. [Q96DR7-3]
DR Ensembl; ENST00000630729.2; ENSP00000487265.1; ENSG00000277101.4. [Q96DR7-4]
DR GeneID; 26084; -.
DR KEGG; hsa:26084; -.
DR MANE-Select; ENST00000465093.6; ENSP00000423418.1; NM_015595.4; NP_056410.3.
DR UCSC; uc011bog.2; human. [Q96DR7-1]
DR CTD; 26084; -.
DR DisGeNET; 26084; -.
DR GeneCards; ARHGEF26; -.
DR HGNC; HGNC:24490; ARHGEF26.
DR HPA; ENSG00000114790; Low tissue specificity.
DR MIM; 617552; gene.
DR neXtProt; NX_Q96DR7; -.
DR OpenTargets; ENSG00000114790; -.
DR VEuPathDB; HostDB:ENSG00000114790; -.
DR eggNOG; KOG3523; Eukaryota.
DR GeneTree; ENSGT01030000234571; -.
DR HOGENOM; CLU_012820_2_0_1; -.
DR InParanoid; Q96DR7; -.
DR OMA; NTSTMLY; -.
DR PhylomeDB; Q96DR7; -.
DR TreeFam; TF316357; -.
DR PathwayCommons; Q96DR7; -.
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-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; Q96DR7; -.
DR SIGNOR; Q96DR7; -.
DR BioGRID-ORCS; 26084; 5 hits in 1058 CRISPR screens.
DR ChiTaRS; ARHGEF26; human.
DR GenomeRNAi; 26084; -.
DR Pharos; Q96DR7; Tbio.
DR PRO; PR:Q96DR7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96DR7; protein.
DR Bgee; ENSG00000114790; Expressed in lower esophagus muscularis layer and 95 other tissues.
DR ExpressionAtlas; Q96DR7; baseline and differential.
DR Genevisible; Q96DR7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11938; SH3_ARHGEF16_26; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035797; ARHGEF16/ARHGEF26_SH3.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..871
FT /note="Rho guanine nucleotide exchange factor 26"
FT /id="PRO_0000322568"
FT DOMAIN 439..623
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 655..782
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 789..850
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 428..446
FT /note="GLSQTVSQEERKRQEAIFE -> VILIVGFMEMKDGRLRGGK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15221005"
FT /id="VSP_031934"
FT VAR_SEQ 447..871
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15221005"
FT /id="VSP_031935"
FT VAR_SEQ 790..871
FT /note="SLTQVEIVRSFTAKQPDELSLQVADVVLIYQRVSDGWYEGERLRDGERGWFP
FT MECAKEITCQATIDKNVERMGRLLGLETNV -> CG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045570"
FT VARIANT 29
FT /note="V -> L (in dbSNP:rs12493885)"
FT /evidence="ECO:0000269|PubMed:12697679,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15133129,
FT ECO:0000269|PubMed:15221005, ECO:0000269|PubMed:15489334,
FT ECO:0007744|PubMed:21406692"
FT /id="VAR_039425"
FT VARIANT 60
FT /note="L -> P (in dbSNP:rs12497267)"
FT /evidence="ECO:0000269|PubMed:15221005"
FT /id="VAR_058205"
FT VARIANT 203
FT /note="F -> S (in dbSNP:rs13096373)"
FT /evidence="ECO:0000269|PubMed:15221005"
FT /id="VAR_039426"
FT MUTAGEN 826
FT /note="W->R: Fails to localize at sites of membrane
FT ruffling."
FT /evidence="ECO:0000269|PubMed:15133129"
FT CONFLICT 60
FT /note="L -> S (in Ref. 1; AAL27001, 2; AAS59842, 3;
FT BAG53860 and 6; AAH78655)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="N -> K (in Ref. 6; AAH16628)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="S -> T (in Ref. 6; AAH78655)"
FT /evidence="ECO:0000305"
FT CONFLICT 781
FT /note="S -> R (in Ref. 1; AAL27001)"
FT /evidence="ECO:0000305"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:6MYE"
SQ SEQUENCE 871 AA; 97346 MW; E6EB57BAE7DD224B CRC64;
MDGESEVDFS SNSITPLWRR RSIPQPHQVL GRSKPRPQSY QSPNGLLITD FPVEDGGTLL
AAQIPAQVPT ASDSRTVHRS PLLLGAQRRA VANGGTASPE YRAASPRLRR PKSPKLPKAV
PGGSPKSPAN GAVTLPAPPP PPVLRPPRTP NAPAPCTPEE DLTGLTASPV PSPTANGLAA
NNDSPGSGSQ SGRKAKDPER GLFPGPQKSS SEQKLPLQRL PSQENELLEN PSVVLSTNSP
AALKVGKQQI IPKSLASEIK ISKSNNQNVE PHKRLLKVRS MVEGLGGPLG HAGEESEVDN
DVDSPGSLRR GLRSTSYRRA VVSGFDFDSP TSSKKKNRMS QPVLKVVMED KEKFSSLGRI
KKKMLKGQGT FDGEENAVLY QNYKEKALDI DSDEESEPKE QKSDEKIVIH HKPLRSTWSQ
LSAVKRKGLS QTVSQEERKR QEAIFEVISS EHSYLLSLEI LIRMFKNSKE LSDTMTKTER
HHLFSNITDV CEASKKFFIE LEARHQNNIF IDDISDIVEK HTASTFDPYV KYCTNEVYQQ
RTLQKLLATN PSFKEVLSRI ESHEDCRNLP MISFLILPMQ RVTRLPLLMD TICQKTPKDS
PKYEVCKRAL KEVSKLVRLC NEGARKMERT EMMYTINSQL EFKIKPFPLV SSSRWLVKRG
ELTAYVEDTV LFSRRTSKQQ VYFFLFNDVL IITKKKSEES YNVNDYSLRD QLLVESCDNE
ELNSSPGKNS STMLYSRQSS ASHLFTLTVL SNHANEKVEM LLGAETQSER ARWITALGHS
SGKPPADRTS LTQVEIVRSF TAKQPDELSL QVADVVLIYQ RVSDGWYEGE RLRDGERGWF
PMECAKEITC QATIDKNVER MGRLLGLETN V
