ARG28_HUMAN
ID ARG28_HUMAN Reviewed; 1705 AA.
AC Q8N1W1; B2RXG7; B4E3K4; B5MDA3; B7ZW32; E9PC75; Q8NCM7; Q96E37; Q9H6L3;
AC Q9H6W0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Rho guanine nucleotide exchange factor 28;
DE AltName: Full=190 kDa guanine nucleotide exchange factor;
DE Short=p190-RhoGEF;
DE Short=p190RhoGEF;
DE AltName: Full=Rho guanine nucleotide exchange factor;
GN Name=ARHGEF28; Synonyms=KIAA1998, RGNEF;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12056414; DOI=10.1093/dnares/9.2.47;
RA Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S.,
RA Takahashi Y., Kitajima S., Saga Y., Koseki H.;
RT "Characterization of size-fractionated cDNA libraries generated by the in
RT vitro recombination-assisted method.";
RL DNA Res. 9:47-57(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-945 AND 977-1705 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1037-1705 (ISOFORM 3), AND VARIANT GLN-1640.
RC TISSUE=Amygdala, Hepatoma, and Kidney epithelium;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND VARIANTS
RP GLN-284 AND GLN-1640.
RC TISSUE=Brain, and Kidney;
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 [5]
RP INTERACTION WITH MAPK8IP1.
RX PubMed=10574993; DOI=10.1074/jbc.274.49.35113;
RA Meyer D., Liu A., Margolis B.;
RT "Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190
RT rhoGEF and its localization in differentiated neurons.";
RL J. Biol. Chem. 274:35113-35118(1999).
RN [6]
RP INTERACTION WITH CTNND2.
RX PubMed=17993462; DOI=10.1074/jbc.m707158200;
RA Kim H., Han J.-R., Park J., Oh M., James S.E., Chang S., Lu Q., Lee K.Y.,
RA Ki H., Song W.-J., Kim K.;
RT "Delta-catenin-induced dendritic morphogenesis. An essential role of
RT p190RhoGEF interaction through Akt1-mediated phosphorylation.";
RL J. Biol. Chem. 283:977-987(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND IDENTIFICATION BY
RP MASS 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1538, 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: Functions as a RHOA-specific guanine nucleotide exchange
CC factor regulating signaling pathways downstream of integrins and growth
CC factor receptors. Functions in axonal branching, synapse formation and
CC dendritic morphogenesis. Functions also in focal adhesion formation,
CC cell motility and B-lymphocytes activation. May regulate NEFL
CC expression and aggregation and play a role in apoptosis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer; forms cytoplasmic aggregates. Forms a complex
CC with MAPK8 and MAPK8IP1. Interacts with RHOA. Interacts with
CC microtubules. Interacts with YWHAE and YWHAH. Interacts with PTK2/FAK1.
CC Interacts with NEFL (By similarity). Interacts with CTNND2; prevents
CC interaction with RHOA. {ECO:0000250, ECO:0000269|PubMed:10574993,
CC ECO:0000269|PubMed:17993462}.
CC -!- INTERACTION:
CC Q8N1W1-4; P27797: CALR; NbExp=3; IntAct=EBI-13062134, EBI-1049597;
CC Q8N1W1-4; P78358: CTAG1B; NbExp=3; IntAct=EBI-13062134, EBI-1188472;
CC Q8N1W1-4; P36957: DLST; NbExp=3; IntAct=EBI-13062134, EBI-351007;
CC Q8N1W1-4; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-13062134, EBI-1055945;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Colocalizes with the microtubule radial and
CC cortical systems. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8N1W1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N1W1-2; Sequence=VSP_032140, VSP_032141;
CC Name=3;
CC IsoId=Q8N1W1-3; Sequence=VSP_032142, VSP_032143;
CC Name=4;
CC IsoId=Q8N1W1-4; Sequence=VSP_032144;
CC Name=5;
CC IsoId=Q8N1W1-5; Sequence=VSP_044737, VSP_044738;
CC Name=6;
CC IsoId=Q8N1W1-6; Sequence=VSP_032143;
CC -!- PTM: Phosphorylated on tyrosine upon stimulation of cells by laminin.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12946.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15243.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC02707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB082529; BAC02707.1; ALT_INIT; mRNA.
DR EMBL; AK025470; BAB15141.1; -; mRNA.
DR EMBL; AK025816; BAB15243.1; ALT_INIT; mRNA.
DR EMBL; AK094713; BAC04405.1; -; mRNA.
DR EMBL; AK304761; BAG65516.1; -; mRNA.
DR EMBL; AC008387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012946; AAH12946.1; ALT_INIT; mRNA.
DR EMBL; BC157846; AAI57847.1; -; mRNA.
DR EMBL; BC171850; AAI71850.1; -; mRNA.
DR CCDS; CCDS47231.2; -. [Q8N1W1-6]
DR CCDS; CCDS54870.1; -. [Q8N1W1-1]
DR CCDS; CCDS58957.1; -. [Q8N1W1-5]
DR RefSeq; NP_001073948.2; NM_001080479.2. [Q8N1W1-6]
DR RefSeq; NP_001171164.1; NM_001177693.1. [Q8N1W1-1]
DR RefSeq; NP_001231293.1; NM_001244364.1. [Q8N1W1-5]
DR RefSeq; XP_011541848.1; XM_011543546.1. [Q8N1W1-6]
DR PDB; 6BC0; X-ray; 2.20 A; A=1049-1194.
DR PDB; 6BC1; X-ray; 2.90 A; C/D=1049-1194.
DR PDBsum; 6BC0; -.
DR PDBsum; 6BC1; -.
DR AlphaFoldDB; Q8N1W1; -.
DR SMR; Q8N1W1; -.
DR BioGRID; 122127; 19.
DR IntAct; Q8N1W1; 14.
DR MINT; Q8N1W1; -.
DR STRING; 9606.ENSP00000441913; -.
DR iPTMnet; Q8N1W1; -.
DR PhosphoSitePlus; Q8N1W1; -.
DR BioMuta; ARHGEF28; -.
DR DMDM; 327478563; -.
DR EPD; Q8N1W1; -.
DR jPOST; Q8N1W1; -.
DR MassIVE; Q8N1W1; -.
DR MaxQB; Q8N1W1; -.
DR PaxDb; Q8N1W1; -.
DR PeptideAtlas; Q8N1W1; -.
DR PRIDE; Q8N1W1; -.
DR ProteomicsDB; 19386; -.
DR ProteomicsDB; 6165; -.
DR ProteomicsDB; 71639; -. [Q8N1W1-1]
DR ProteomicsDB; 71640; -. [Q8N1W1-2]
DR ProteomicsDB; 71641; -. [Q8N1W1-3]
DR ProteomicsDB; 71642; -. [Q8N1W1-4]
DR Antibodypedia; 48924; 32 antibodies from 12 providers.
DR DNASU; 64283; -.
DR Ensembl; ENST00000296794.10; ENSP00000296794.6; ENSG00000214944.10. [Q8N1W1-4]
DR Ensembl; ENST00000296799.8; ENSP00000296799.4; ENSG00000214944.10. [Q8N1W1-5]
DR Ensembl; ENST00000426542.6; ENSP00000412175.2; ENSG00000214944.10. [Q8N1W1-1]
DR Ensembl; ENST00000437974.5; ENSP00000411459.1; ENSG00000214944.10. [Q8N1W1-6]
DR Ensembl; ENST00000513042.7; ENSP00000441436.1; ENSG00000214944.10. [Q8N1W1-1]
DR Ensembl; ENST00000545377.5; ENSP00000441913.1; ENSG00000214944.10. [Q8N1W1-6]
DR GeneID; 64283; -.
DR KEGG; hsa:64283; -.
DR MANE-Select; ENST00000513042.7; ENSP00000441436.1; NM_001177693.2; NP_001171164.1.
DR UCSC; uc010izf.4; human. [Q8N1W1-1]
DR CTD; 64283; -.
DR DisGeNET; 64283; -.
DR GeneCards; ARHGEF28; -.
DR HGNC; HGNC:30322; ARHGEF28.
DR HPA; ENSG00000214944; Tissue enhanced (kidney).
DR MIM; 612790; gene.
DR neXtProt; NX_Q8N1W1; -.
DR OpenTargets; ENSG00000214944; -.
DR VEuPathDB; HostDB:ENSG00000214944; -.
DR eggNOG; KOG3520; Eukaryota.
DR eggNOG; KOG4305; Eukaryota.
DR GeneTree; ENSGT00940000155831; -.
DR HOGENOM; CLU_002466_2_1_1; -.
DR InParanoid; Q8N1W1; -.
DR OMA; EQECQSQ; -.
DR OrthoDB; 69816at2759; -.
DR PhylomeDB; Q8N1W1; -.
DR TreeFam; TF334740; -.
DR PathwayCommons; Q8N1W1; -.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
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 SignaLink; Q8N1W1; -.
DR SIGNOR; Q8N1W1; -.
DR BioGRID-ORCS; 64283; 18 hits in 1067 CRISPR screens.
DR ChiTaRS; ARHGEF28; human.
DR GenomeRNAi; 64283; -.
DR Pharos; Q8N1W1; Tbio.
DR PRO; PR:Q8N1W1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8N1W1; protein.
DR Bgee; ENSG00000214944; Expressed in sural nerve and 165 other tissues.
DR ExpressionAtlas; Q8N1W1; baseline and differential.
DR Genevisible; Q8N1W1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd00029; C1; 1.
DR CDD; cd14680; PH_p190RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR037819; ARHGEF28_PH.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Differentiation; Guanine-nucleotide releasing factor; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..1705
FT /note="Rho guanine nucleotide exchange factor 28"
FT /id="PRO_0000324119"
FT DOMAIN 849..1044
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1086..1188
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 652..699
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 287..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1304
FT /note="Interaction with PTK2/FAK1; required for regulation
FT of axonal branching and synapse formation"
FT /evidence="ECO:0000250"
FT REGION 1312..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1383
FT /note="Mediates cytoplasmic retention and interaction with
FT YWHAH"
FT /evidence="ECO:0000250"
FT REGION 1425..1705
FT /note="Interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 1496..1527
FT /note="RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 1566..1579
FT /note="Mediates cytoplasmic retention and interaction with
FT MAPK8IP1"
FT /evidence="ECO:0000250"
FT REGION 1638..1705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1488..1525
FT /evidence="ECO:0000255"
FT COMPBIAS 473..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C6P5"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C6P5"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..28
FT /note="MELSCSEAPLYGQMMIYAKFDKNVYLPE -> MDSDSDSPFNYSWPSFPKMK
FT IRRRTSKQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044737"
FT VAR_SEQ 29..341
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044738"
FT VAR_SEQ 583..602
FT /note="EQRAYSLSEPPRENRIQEEE -> GKHHLTFGFENTLFQNRFFS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12056414"
FT /id="VSP_032140"
FT VAR_SEQ 603..1705
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12056414"
FT /id="VSP_032141"
FT VAR_SEQ 1282..1325
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032142"
FT VAR_SEQ 1649
FT /note="N -> NGSSMTKCSCTLTSPPGLWTGTTSTLK (in isoform 3 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032143"
FT VAR_SEQ 1650..1705
FT /note="DLDTSHTESPTPHDSNSHRPQLQAFITEAKLNLPTRTMTRQDGETGDGAKEN
FT IVYL -> GN (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_032144"
FT VARIANT 98
FT /note="R -> M (in dbSNP:rs12659447)"
FT /id="VAR_039657"
FT VARIANT 225
FT /note="W -> R (in dbSNP:rs7714670)"
FT /id="VAR_039658"
FT VARIANT 284
FT /note="P -> Q (in dbSNP:rs6453022)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039659"
FT VARIANT 544
FT /note="S -> L (in dbSNP:rs2973571)"
FT /id="VAR_039660"
FT VARIANT 585
FT /note="R -> K (in dbSNP:rs2973566)"
FT /id="VAR_039661"
FT VARIANT 780
FT /note="H -> N (in dbSNP:rs2973558)"
FT /id="VAR_039662"
FT VARIANT 1548
FT /note="P -> S (in dbSNP:rs17634865)"
FT /id="VAR_039663"
FT VARIANT 1640
FT /note="H -> Q (in dbSNP:rs1478453)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_039664"
FT CONFLICT 1450
FT /note="E -> G (in Ref. 2; BAB15141)"
FT /evidence="ECO:0000305"
FT CONFLICT 1540
FT /note="P -> S (in Ref. 2; BAB15141)"
FT /evidence="ECO:0000305"
FT CONFLICT 1598
FT /note="S -> F (in Ref. 4; AAH12946)"
FT /evidence="ECO:0000305"
FT CONFLICT 1613
FT /note="K -> L (in Ref. 4; AAH12946)"
FT /evidence="ECO:0000305"
FT CONFLICT 1620
FT /note="S -> L (in Ref. 4; AAH12946)"
FT /evidence="ECO:0000305"
FT HELIX 1052..1060
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1066..1068
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1074..1076
FT /evidence="ECO:0007829|PDB:6BC0"
FT HELIX 1077..1080
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1088..1096
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1102..1109
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1114..1120
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1123..1126
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1134..1136
FT /evidence="ECO:0007829|PDB:6BC0"
FT HELIX 1138..1140
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1141..1145
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1152..1157
FT /evidence="ECO:0007829|PDB:6BC0"
FT STRAND 1164..1169
FT /evidence="ECO:0007829|PDB:6BC0"
FT HELIX 1173..1184
FT /evidence="ECO:0007829|PDB:6BC0"
SQ SEQUENCE 1705 AA; 191891 MW; D4DD6331BD259CC7 CRC64;
MELSCSEAPL YGQMMIYAKF DKNVYLPEDA EFYFTYDGSH QRHVMIAERI EDNVLQSSVP
GHGLQETVTV SVCLCSEGYS PVTMGSGSVT YVDNMACRLA RLLVTQANRL TACSHQTLLT
PFALTAGALP ALDEELVLAL THLELPLEWT VLGSSSLEVS SHRESLLHLA MRWGLAKLSQ
FFLCLPGGVQ ALALPNEEGA TPLDLALREG HSKLVEDVTN FQGRWSPSFS RVQLSEEASL
HYIHSSETLT LTLNHTAEHL LEADIKLFRK YFWDRAFLVK AFEPEARPEE RTAMPSSGAE
TEEEIKNSVS SRSAAEKEDI KRVKSLVVQH NEHEDQHSLD LDRSFDILKK SKPPSTLLAA
GRLSDMLNGG DEVYANCMVI DQVGDLDISY INIEGITATT SPESRGCTLW PQSSKHTLPT
ETSPSVYPLS ENVEGTAHTE AQQSFMSPSS SCASNLNLSF GWHGFEKEQS HLKKRSSSLD
ALDADSEGEG HSEPSHICYT PGSQSSSRTG IPSGDELDSF ETNTEPDFNI SRAESLPLSS
NLQSKESLLS GVRSRSYSCS SPKISLGKTR LVRELTVCSS SEEQRAYSLS EPPRENRIQE
EEWDKYIIPA KSESEKYKVS RTFSFLMNRM TSPRNKSKTK SKDAKDKEKL NRHQFAPGTF
SGVLQCLVCD KTLLGKESLQ CSNCNANVHK GCKDAAPACT KKFQEKYNKN KPQTILGNSS
FRDIPQPGLS LHPSSSVPVG LPTGRRETVG QVHPLSRSVP GTTLESFRRS ATSLESESDH
NSCRSRSHSD ELLQSMGSSP STESFIMEDV VDSSLWSDLS SDAQEFEAES WSLVVDPSFC
NRQEKDVIKR QDVIFELMQT EMHHIQTLFI MSEIFRKGMK EELQLDHSTV DKIFPCLDEL
LEIHRHFFYS MKERRQESCA GSDRNFVIDR IGDILVQQFS EENASKMKKI YGEFCCHHKE
AVNLFKELQQ NKKFQNFIKL RNSNLLARRR GIPECILLVT QRITKYPVLV ERILQYTKER
TEEHKDLRKA LCLIKDMIAT VDLKVNEYEK NQKWLEILNK IENKTYTKLK NGHVFRKQAL
MSEERTLLYD GLVYWKTATG RFKDILALLL TDVLLFLQEK DQKYIFAAVD QKPSVISLQK
LIAREVANEE RGMFLISASS AGPEMYEIHT NSKEERNNWM RRIQQAVESC PEEKGGRTSE
SDEDKRKAEA RVAKIQQCQE ILTNQDQQIC AYLEEKLHIY AELGELSGFE DVHLEPHLLI
KPDPGEPPQA ASLLAAALKE AESLQVAVKA SQMGAVSQSC EDSCGDSVLA DTLSSHDVPG
SPTASLVTGG REGRGCSDVD PGIQGVVTDL AVSDAGEKVE CRNFPGSSQS EIIQAIQNLT
RLLYSLQAAL TIQDSHIEIH RLVLQQQEGL SLGHSILRGG PLQDQKSRDA DRQHEELANV
HQLQHQLQQE QRRWLRRCEQ QQRAQATRES WLQERERECQ SQEELLLRSR GELDLQLQEY
QHSLERLREG QRLVEREQAR MRAQQSLLGH WKHGRQRSLP AVLLPGGPEV MELNRSESLC
HENSFFINEA LVQMSFNTFN KLNPSVIHQD ATYPTTQSHS DLVRTSEHQV DLKVDPSQPS
NVSHKLWTAA GSGHQILPFH ESSKDSCKND LDTSHTESPT PHDSNSHRPQ LQAFITEAKL
NLPTRTMTRQ DGETGDGAKE NIVYL
