TIAM2_HUMAN
ID TIAM2_HUMAN Reviewed; 1701 AA.
AC Q8IVF5; B2RP56; C9JZV2; Q6NXN9; Q6ZUP9; Q9UFG6; Q9UKV9; Q9UKW0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Rho guanine nucleotide exchange factor TIAM2 {ECO:0000305|PubMed:10512681};
DE AltName: Full=SIF and TIAM1-like exchange factor;
DE AltName: Full=T-lymphoma invasion and metastasis-inducing protein 2;
DE Short=TIAM-2;
GN Name=TIAM2; Synonyms=KIAA2016, STEF;
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 3), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 634-1701 (ISOFORM 5), FUNCTION, TISSUE SPECIFICITY, AND VARIANT PRO-1089.
RX PubMed=10512681; DOI=10.1006/geno.1999.5936;
RA Chiu C.-Y., Leng S., Martin K.A., Kim E., Gorman S., Duhl D.M.;
RT "Cloning and characterization of T-cell lymphoma invasion and metastasis 2
RT (TIAM2), a novel guanine nucleotide exchange factor related to TIAM1.";
RL Genomics 61:66-73(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-1089.
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT PRO-1089.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP PRO-1089.
RC TISSUE=Brain;
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 446-1701 (ISOFORM 2), AND VARIANT
RP PRO-1089.
RC TISSUE=Fetal brain;
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).
CC -!- FUNCTION: Modulates the activity of RHO-like proteins and connects
CC extracellular signals to cytoskeletal activities. Acts as a GDP-
CC dissociation stimulator protein that stimulates the GDP-GTP exchange
CC activity of RHO-like GTPases and activates them. Mediates extracellular
CC laminin signals to activate Rac1, contributing to neurite growth.
CC Involved in lamellipodial formation and advancement of the growth cone
CC of embryonic hippocampal neurons. Promotes migration of neurons in the
CC cerebral cortex. When overexpressed, induces membrane ruffling
CC accompanied by the accumulation of actin filaments along the altered
CC plasma membrane (By similarity). Activates specifically RAC1, but not
CC CDC42 and RHOA. {ECO:0000250, ECO:0000269|PubMed:10512681}.
CC -!- SUBUNIT: Interacts with MAP1A, MAP1B, PARP1 and YWHAE. Interacts with
CC CD44, PARD3 and MAPK8IP2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZPF3}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:Q6ZPF3}. Cell
CC projection, filopodium {ECO:0000250|UniProtKB:Q6ZPF3}. Cell projection,
CC growth cone {ECO:0000250|UniProtKB:Q6ZPF3}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:Q6ZPF3}. Perikaryon
CC {ECO:0000250|UniProtKB:Q6ZPF3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8IVF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IVF5-2; Sequence=VSP_030975;
CC Name=3; Synonyms=Short;
CC IsoId=Q8IVF5-3; Sequence=VSP_030971;
CC Name=4;
CC IsoId=Q8IVF5-4; Sequence=VSP_030972;
CC Name=5; Synonyms=Long;
CC IsoId=Q8IVF5-5; Sequence=VSP_030974;
CC -!- TISSUE SPECIFICITY: Expressed in the occipital, frontal and temporal
CC lobes, cerebellum, putamen and testis. {ECO:0000269|PubMed:10512681}.
CC -!- DOMAIN: The PH 1 domain and amino acids 621-782 (a region called TSS;
CC otherwise known as CC-Ex) are necessary for membrane localization. The
CC PH 1 and TSS domains are necessary for Rac1 activity. The PH 2 domain
CC is engaged in the enhancement of the catalytic activity of the adjacent
CC DH domain. The PH 1, TSS and DH domains are necessary to induce
CC neurite-like structure (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine and threonine residues. Phosphorylated on
CC Thr-1648 by Rho-kinase. Its phosphorylation by Rho-kinase inhibits its
CC guanine nucleotide exchange activity, its interaction with MAP1A,
CC MAP1B, PARP1 and YWHAE and reduces its ability to promote neurite
CC growth (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TIAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF05900.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC23112.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86170.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF120323; AAF05900.1; ALT_INIT; mRNA.
DR EMBL; AF120324; AAF05901.1; -; mRNA.
DR EMBL; AB095936; BAC23112.2; ALT_INIT; mRNA.
DR EMBL; AL122086; CAB59259.2; -; mRNA.
DR EMBL; AL139101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47693.1; -; Genomic_DNA.
DR EMBL; BC066979; AAH66979.1; -; mRNA.
DR EMBL; BC137275; AAI37276.1; -; mRNA.
DR EMBL; AK125459; BAC86170.1; ALT_INIT; mRNA.
DR CCDS; CCDS34558.1; -. [Q8IVF5-1]
DR CCDS; CCDS34559.1; -. [Q8IVF5-3]
DR RefSeq; NP_001010927.1; NM_001010927.2. [Q8IVF5-3]
DR RefSeq; NP_036586.2; NM_012454.3. [Q8IVF5-1]
DR AlphaFoldDB; Q8IVF5; -.
DR SMR; Q8IVF5; -.
DR BioGRID; 117621; 13.
DR IntAct; Q8IVF5; 9.
DR MINT; Q8IVF5; -.
DR STRING; 9606.ENSP00000437188; -.
DR iPTMnet; Q8IVF5; -.
DR PhosphoSitePlus; Q8IVF5; -.
DR BioMuta; TIAM2; -.
DR DMDM; 296453025; -.
DR jPOST; Q8IVF5; -.
DR MassIVE; Q8IVF5; -.
DR MaxQB; Q8IVF5; -.
DR PaxDb; Q8IVF5; -.
DR PeptideAtlas; Q8IVF5; -.
DR PRIDE; Q8IVF5; -.
DR ProteomicsDB; 70693; -. [Q8IVF5-1]
DR ProteomicsDB; 70694; -. [Q8IVF5-2]
DR ProteomicsDB; 70695; -. [Q8IVF5-3]
DR ProteomicsDB; 70696; -. [Q8IVF5-4]
DR ProteomicsDB; 70697; -. [Q8IVF5-5]
DR Antibodypedia; 2773; 184 antibodies from 25 providers.
DR DNASU; 26230; -.
DR Ensembl; ENST00000275246.11; ENSP00000275246.7; ENSG00000146426.19. [Q8IVF5-3]
DR Ensembl; ENST00000360366.8; ENSP00000353528.4; ENSG00000146426.19. [Q8IVF5-5]
DR Ensembl; ENST00000456877.6; ENSP00000407183.2; ENSG00000146426.19. [Q8IVF5-4]
DR Ensembl; ENST00000461783.7; ENSP00000437188.2; ENSG00000146426.19. [Q8IVF5-1]
DR Ensembl; ENST00000529824.6; ENSP00000433348.2; ENSG00000146426.19. [Q8IVF5-2]
DR Ensembl; ENST00000682666.1; ENSP00000507157.1; ENSG00000146426.19. [Q8IVF5-1]
DR GeneID; 26230; -.
DR KEGG; hsa:26230; -.
DR MANE-Select; ENST00000682666.1; ENSP00000507157.1; NM_012454.4; NP_036586.3.
DR UCSC; uc003qqb.3; human. [Q8IVF5-1]
DR CTD; 26230; -.
DR DisGeNET; 26230; -.
DR GeneCards; TIAM2; -.
DR HGNC; HGNC:11806; TIAM2.
DR HPA; ENSG00000146426; Tissue enhanced (brain, testis).
DR MIM; 604709; gene.
DR neXtProt; NX_Q8IVF5; -.
DR OpenTargets; ENSG00000146426; -.
DR PharmGKB; PA36515; -.
DR VEuPathDB; HostDB:ENSG00000146426; -.
DR eggNOG; KOG3519; Eukaryota.
DR GeneTree; ENSGT00940000157012; -.
DR HOGENOM; CLU_000494_2_1_1; -.
DR InParanoid; Q8IVF5; -.
DR OMA; SHFKSHQ; -.
DR OrthoDB; 34437at2759; -.
DR PhylomeDB; Q8IVF5; -.
DR TreeFam; TF319686; -.
DR PathwayCommons; Q8IVF5; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q8IVF5; -.
DR SIGNOR; Q8IVF5; -.
DR BioGRID-ORCS; 26230; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; TIAM2; human.
DR GenomeRNAi; 26230; -.
DR Pharos; Q8IVF5; Tbio.
DR PRO; PR:Q8IVF5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8IVF5; protein.
DR Bgee; ENSG00000146426; Expressed in cortical plate and 167 other tissues.
DR ExpressionAtlas; Q8IVF5; baseline and differential.
DR Genevisible; Q8IVF5; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR043537; Tiam1/Tiam2/Sif.
DR InterPro; IPR040655; TIAM1_CC-Ex.
DR PANTHER; PTHR46001; PTHR46001; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF18385; Tiam_CC_Ex; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00455; RBD; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 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.
DR PROSITE; PS50898; RBD; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Guanine-nucleotide releasing factor; Lipoprotein; Myristate;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..1701
FT /note="Rho guanine nucleotide exchange factor TIAM2"
FT /id="PRO_0000317467"
FT DOMAIN 506..620
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 810..881
FT /note="RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 890..976
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1099..1293
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1347..1478
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 628..695
FT /evidence="ECO:0000255"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPF3"
FT MOD_RES 1648
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPF3"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..1075
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10512681,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030971"
FT VAR_SEQ 1..688
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030972"
FT VAR_SEQ 787
FT /note="Q -> QIFDSSGSHGFSGTQLPQNSSNSSE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10512681"
FT /id="VSP_030974"
FT VAR_SEQ 1317
FT /note="E -> EQPEWSSEVMDVLDPRGKLTKGTLEEPRTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030975"
FT VARIANT 332
FT /note="R -> H (in dbSNP:rs931312)"
FT /id="VAR_051994"
FT VARIANT 913
FT /note="R -> H (in dbSNP:rs7770537)"
FT /id="VAR_051995"
FT VARIANT 1089
FT /note="S -> P (in dbSNP:rs4259257)"
FT /evidence="ECO:0000269|PubMed:10512681,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.2"
FT /id="VAR_051996"
FT VARIANT 1101
FT /note="R -> C (in dbSNP:rs11751128)"
FT /id="VAR_038534"
FT VARIANT 1572
FT /note="D -> E (in dbSNP:rs1571767)"
FT /id="VAR_038535"
FT CONFLICT 506
FT /note="V -> A (in Ref. 7; BAC86170)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="L -> P (in Ref. 1; AAF05900)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="L -> P (in Ref. 1; AAF05900)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="A -> T (in Ref. 1; AAF05900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="R -> K (in Ref. 7; BAC86170)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="R -> G (in Ref. 6; AAH66979)"
FT /evidence="ECO:0000305"
FT CONFLICT 1154
FT /note="Q -> R (in Ref. 6; AAH66979)"
FT /evidence="ECO:0000305"
FT CONFLICT 1186
FT /note="S -> P (in Ref. 7; BAC86170)"
FT /evidence="ECO:0000305"
FT CONFLICT 1306
FT /note="Q -> R (in Ref. 7; BAC86170)"
FT /evidence="ECO:0000305"
FT CONFLICT 1365
FT /note="E -> K (in Ref. 7; BAC86170)"
FT /evidence="ECO:0000305"
FT CONFLICT 1376
FT /note="N -> Y (in Ref. 6; AAH66979)"
FT /evidence="ECO:0000305"
FT CONFLICT 1451
FT /note="R -> S (in Ref. 6; AAH66979)"
FT /evidence="ECO:0000305"
FT CONFLICT 1482
FT /note="R -> G (in Ref. 6; AAH66979)"
FT /evidence="ECO:0000305"
FT CONFLICT 1519
FT /note="D -> Y (in Ref. 7; BAC86170)"
FT /evidence="ECO:0000305"
FT CONFLICT 1639
FT /note="A -> T (in Ref. 7; BAC86170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1701 AA; 190103 MW; C2C9C9B1782B7823 CRC64;
MGNSDSQYTL QGSKNHSNTI TGAKQIPCSL KIRGIHAKEE KSLHGWGHGS NGAGYKSRSL
ARSCLSHFKS NQPYASRLGG PTCKVSRGVA YSTHRTNAPG KDFQGISAAF STENGFHSVG
HELADNHITS RDCNGHLLNC YGRNESIAST PPGEDRKSPR VLIKTLGKLD GCLRVEFHNG
GNPSKVPAED CSEPVQLLRY SPTLASETSP VPEARRGSSA DSLPSHRPSP TDSRLRSSKG
SSLSSESSWY DSPWGNAGEL SEAEGSFLAP GMPDPSLHAS FPPGDAKKPF NQSSSLSSLR
ELYKDANLGS LSPSGIRLSD EYMGTHASLS NRVSFASDID VPSRVAHGDP IQYSSFTLPC
RKPKAFVEDT AKKDSLKARM RRISDWTGSL SRKKRKLQEP RSKEGSDYFD SRSDGLNTDV
QGSSQASAFL WSGGSTQILS QRSESTHAIG SDPLRQNIYE NFMRELEMSR TNTENIETST
ETAESSSESL SSLEQLDLLF EKEQGVVRKA GWLFFKPLVT VQKERKLELV ARRKWKQYWV
TLKGCTLLFY ETYGKNSMDQ SSAPRCALFA EDSIVQSVPE HPKKENVFCL SNSFGDVYLF
QATSQTDLEN WVTAVHSACA SLFAKKHGKE DTLRLLKNQT KNLLQKIDMD SKMKKMAELQ
LSVVSDPKNR KAIENQIQQW EQNLEKFHMD LFRMRCYLAS LQGGELPNPK SLLAAASRPS
KLALGRLGIL SVSSFHALVC SRDDSALRKR TLSLTQRGRN KKGIFSSLKG LDTLARKGKE
KRPSITQVDE LLHIYGSTVD GVPRDNAWEI QTYVHFQDNH GVTVGIKPEH RVEDILTLAC
KMRQLEPSHY GLQLRKLVDD NVEYCIPAPY EYMQQQVYDE IEVFPLNVYD VQLTKTGSVC
DFGFAVTAQV DERQHLSRIF ISDVLPDGLA YGEGLRKGNE IMTLNGEAVS DLDLKQMEAL
FSEKSVGLTL IARPPDTKAT LCTSWSDSDL FSRDQKSLLP PPNQSQLLEE FLDNFKKNTA
NDFSNVPDIT TGLKRSQTDG TLDQVSHREK MEQTFRSAEQ ITALCRSFND SQANGMEGPR
ENQDPPPRSL ARHLSDADRL RKVIQELVDT EKSYVKDLSC LFELYLEPLQ NETFLTQDEM
ESLFGSLPEM LEFQKVFLET LEDGISASSD FNTLETPSQF RKLLFSLGGS FLYYADHFKL
YSGFCANHIK VQKVLERAKT DKAFKAFLDA RNPTKQHSST LESYLIKPVQ RVLKYPLLLK
ELVSLTDQES EEHYHLTEAL KAMEKVASHI NEMQKIYEDY GTVFDQLVAE QSGTEKEVTE
LSMGELLMHS TVSWLNPFLS LGKARKDLEL TVFVFKRAVI LVYKENCKLK KKLPSNSRPA
HNSTDLDPFK FRWLIPISAL QVRLGNPAGT ENNSIWELIH TKSEIEGRPE TIFQLCCSDS
ESKTNIVKVI RSILRENFRR HIKCELPLEK TCKDRLVPLK NRVPVSAKLA SSRSLKVLKN
SSSNEWTGET GKGTLLDSDE GSLSSGTQSS GCPTAEGRQD SKSTSPGKYP HPGLADFADN
LIKESDILSD EDDDHRQTVK QGSPTKDIEI QFQRLRISED PDVHPEAEQQ PGPESGEGQK
GGEQPKLVRG HFCPIKRKAN STKRDRGTLL KAQIRHQSLD SQSENATIDL NSVLEREFSV
QSLTSVVSEE CFYETESHGK S
