BAIP2_MOUSE
ID BAIP2_MOUSE Reviewed; 535 AA.
AC Q8BKX1; Q91V97; Q923V9; Q923W0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2;
DE Short=BAI-associated protein 2;
DE Short=BAI1-associated protein 2;
DE AltName: Full=Insulin receptor substrate protein of 53 kDa;
DE Short=IRSp53;
DE Short=Insulin receptor substrate p53;
DE AltName: Full=Insulin receptor tyrosine kinase 53 kDa substrate;
GN Name=Baiap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11514062; DOI=10.1016/s0304-3940(01)02064-x;
RA Thomas E.A., Foye P.E., Alvarez C.E., Usui H., Sutcliffe J.G.;
RT "Insulin receptor substrate protein p53 localization in rats suggests
RT mechanism for specific polyglutamine neurodegeneration.";
RL Neurosci. Lett. 309:145-148(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 4).
RX PubMed=12884081; DOI=10.1007/s10038-003-0047-x;
RA Miyahara A., Okumura-Oho Y., Miyashita T., Hoshika A., Yamada M.;
RT "Genomic structure and alternative splicing of the insulin receptor
RT tyrosine kinase substrate of 53-kDa protein.";
RL J. Hum. Genet. 48:410-414(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 DIAPH1.
RX PubMed=10814512; DOI=10.1006/bbrc.2000.2671;
RA Fujiwara T., Mammoto A., Kim Y., Takai Y.;
RT "Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-
RT containing IRSp53/BAIAP2.";
RL Biochem. Biophys. Res. Commun. 271:626-629(2000).
RN [6]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=12006592; DOI=10.1074/jbc.m202512200;
RA Alvarez C.E., Sutcliffe J.G., Thomas E.A.;
RT "Novel isoform of insulin receptor substrate p53/p58 is generated by
RT alternative splicing in the CRIB/SH3-binding region.";
RL J. Biol. Chem. 277:24728-24734(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH EPS8.
RX PubMed=17115031; DOI=10.1038/ncb1502;
RA Disanza A., Mantoani S., Hertzog M., Gerboth S., Frittoli E., Steffen A.,
RA Berhoerster K., Kreienkamp H.J., Milanesi F., Di Fiore P.P., Ciliberto A.,
RA Stradal T.E., Scita G.;
RT "Regulation of cell shape by Cdc42 is mediated by the synergic actin-
RT bundling activity of the Eps8-IRSp53 complex.";
RL Nat. Cell Biol. 8:1337-1347(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Adapter protein that links membrane-bound small G-proteins to
CC cytoplasmic effector proteins. Necessary for CDC42-mediated
CC reorganization of the actin cytoskeleton and for RAC1-mediated membrane
CC ruffling. Involved in the regulation of the actin cytoskeleton by WASF
CC family members and the Arp2/3 complex. Plays a role in neurite growth.
CC Acts syngeristically with ENAH to promote filipodia formation. Plays a
CC role in the reorganization of the actin cytoskeleton in response to
CC bacterial infection. Participates in actin bundling when associated
CC with EPS8, promoting filopodial protrusions.
CC {ECO:0000269|PubMed:17115031}.
CC -!- SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been
CC activated by GTP binding. Binds DIAPH1. Interacts with ATN1, ADGRB1,
CC SHANK1, SHANK2, SHANK3, TIAM1, WASF1 and WASF2. Interacts with ENAH
CC after recruitment of CDC42 (By similarity). Interacts with EPS8.
CC {ECO:0000250, ECO:0000269|PubMed:10814512,
CC ECO:0000269|PubMed:17115031}.
CC -!- INTERACTION:
CC Q8BKX1; O08808: Diaph1; NbExp=3; IntAct=EBI-771498, EBI-1026445;
CC Q8BKX1; Q62108: Dlg4; NbExp=4; IntAct=EBI-771498, EBI-300895;
CC Q8BKX1; A4GZ26: Iqsec2; NbExp=7; IntAct=EBI-771498, EBI-8526464;
CC Q8BKX1; Q4ACU6: Shank3; NbExp=6; IntAct=EBI-771498, EBI-771450;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell projection, filopodium
CC {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Detected throughout the cytoplasm in
CC the absence of specific binding partners. Detected in filopodia and
CC close to membrane ruffles. Recruited to actin pedestals that are formed
CC upon infection by bacteria at bacterial attachment sites (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BKX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BKX1-2; Sequence=VSP_015508;
CC Name=3;
CC IsoId=Q8BKX1-3; Sequence=VSP_015509;
CC Name=4; Synonyms=Short form;
CC IsoId=Q8BKX1-4; Sequence=VSP_015507, VSP_015508;
CC -!- TISSUE SPECIFICITY: Detected in liver, brain, olfactory bulb, brain
CC cortex, caudate putamen, hypothalamus and cerebellum.
CC {ECO:0000269|PubMed:12006592}.
CC -!- DOMAIN: The IMD domain forms a coiled coil. The isolated domain can
CC induce actin bundling and filopodia formation. In the absence of G-
CC proteins intramolecular interaction between the IMD and the SH3 domain
CC gives rise to an auto-inhibited state of the protein. Interaction of
CC the IMD with RAC1 or CDC42 leads to activation (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The SH3 domain interacts with ATN1, ADGRB1, WASF1, WASF2,
CC SHANK1, DIAPH1 and ENAH. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues by INSR in response to insulin
CC treatment. {ECO:0000250}.
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DR EMBL; AF390178; AAK68153.1; -; mRNA.
DR EMBL; AF390179; AAK81838.1; -; mRNA.
DR EMBL; AB105196; BAC65241.1; -; Genomic_DNA.
DR EMBL; AB105196; BAC65242.1; -; Genomic_DNA.
DR EMBL; AK049469; BAC33764.1; -; mRNA.
DR EMBL; BC006620; AAH06620.1; -; mRNA.
DR EMBL; BC016411; AAH16411.1; -; mRNA.
DR CCDS; CCDS25722.1; -. [Q8BKX1-1]
DR CCDS; CCDS25723.1; -. [Q8BKX1-4]
DR CCDS; CCDS25724.1; -. [Q8BKX1-2]
DR RefSeq; NP_001032843.1; NM_001037754.3. [Q8BKX1-4]
DR RefSeq; NP_001032844.2; NM_001037755.3. [Q8BKX1-1]
DR RefSeq; NP_570932.2; NM_130862.4. [Q8BKX1-2]
DR AlphaFoldDB; Q8BKX1; -.
DR SMR; Q8BKX1; -.
DR BioGRID; 223833; 23.
DR DIP; DIP-32392N; -.
DR IntAct; Q8BKX1; 13.
DR MINT; Q8BKX1; -.
DR STRING; 10090.ENSMUSP00000026436; -.
DR iPTMnet; Q8BKX1; -.
DR PhosphoSitePlus; Q8BKX1; -.
DR EPD; Q8BKX1; -.
DR jPOST; Q8BKX1; -.
DR MaxQB; Q8BKX1; -.
DR PaxDb; Q8BKX1; -.
DR PeptideAtlas; Q8BKX1; -.
DR PRIDE; Q8BKX1; -.
DR ProteomicsDB; 277157; -. [Q8BKX1-1]
DR ProteomicsDB; 277158; -. [Q8BKX1-2]
DR ProteomicsDB; 277159; -. [Q8BKX1-3]
DR ProteomicsDB; 277160; -. [Q8BKX1-4]
DR ABCD; Q8BKX1; 1 sequenced antibody.
DR Antibodypedia; 19790; 561 antibodies from 38 providers.
DR DNASU; 108100; -.
DR Ensembl; ENSMUST00000026436; ENSMUSP00000026436; ENSMUSG00000025372. [Q8BKX1-1]
DR Ensembl; ENSMUST00000075180; ENSMUSP00000074674; ENSMUSG00000025372. [Q8BKX1-2]
DR Ensembl; ENSMUST00000103021; ENSMUSP00000099310; ENSMUSG00000025372. [Q8BKX1-4]
DR Ensembl; ENSMUST00000106231; ENSMUSP00000101838; ENSMUSG00000025372. [Q8BKX1-3]
DR GeneID; 108100; -.
DR KEGG; mmu:108100; -.
DR UCSC; uc007mrh.1; mouse. [Q8BKX1-4]
DR UCSC; uc007mri.1; mouse. [Q8BKX1-1]
DR CTD; 10458; -.
DR MGI; MGI:2137336; Baiap2.
DR VEuPathDB; HostDB:ENSMUSG00000025372; -.
DR eggNOG; ENOG502QUM6; Eukaryota.
DR GeneTree; ENSGT00940000153560; -.
DR HOGENOM; CLU_025877_0_1_1; -.
DR InParanoid; Q8BKX1; -.
DR OMA; EYAVHSH; -.
DR PhylomeDB; Q8BKX1; -.
DR TreeFam; TF325648; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 108100; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Baiap2; mouse.
DR PRO; PR:Q8BKX1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BKX1; protein.
DR Bgee; ENSMUSG00000025372; Expressed in superior frontal gyrus and 183 other tissues.
DR ExpressionAtlas; Q8BKX1; baseline and differential.
DR Genevisible; Q8BKX1; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0061846; C:dendritic spine cytoplasm; ISO:MGI.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0061845; C:neuron projection branch point; ISO:MGI.
DR GO; GO:0044306; C:neuron projection terminus; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0051764; P:actin crosslink formation; IMP:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0099564; P:modification of synaptic structure, modulating synaptic transmission; IDA:SynGO.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0035418; P:protein localization to synapse; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:MGI.
DR CDD; cd11915; SH3_Irsp53; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR030128; IRSp53.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR035594; Irsp53_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF3; PTHR14206:SF3; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..535
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2"
FT /id="PRO_0000064817"
FT DOMAIN 1..250
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 375..438
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 299..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..153
FT /evidence="ECO:0000255"
FT COMPBIAS 323..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT VAR_SEQ 290..329
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11514062"
FT /id="VSP_015507"
FT VAR_SEQ 513..535
FT /note="RNPFANVHLKPTVTNDRSAPLLS -> SGSGTLVSTV (in isoform 2
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11514062"
FT /id="VSP_015508"
FT VAR_SEQ 514..535
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015509"
FT CONFLICT 87..88
FT /note="QN -> HI (in Ref. 3; BAC33764)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="S -> F (in Ref. 3; BAC33764)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="S -> F (in Ref. 3; BAC33764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59237 MW; 45B4C660FBB07F72 CRC64;
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG
ELASESQGSK ELGDVLFQMA EVHRQIQNQL EETLKSFHNE LLTQLEQKVE LDSRYLSAAL
KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS
DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPNKIPDRA
VQLMQQMANS NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM
NGVAGPDSED YNPWADRKAA QPKSLSPPQS QSKLSDSYSN TLPVRKSVTP KNSYATTENK
TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE
KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLALPPP DYGTSSRAFP
TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSRNPFANVH LKPTVTNDRS APLLS
