AUTS2_HUMAN
ID AUTS2_HUMAN Reviewed; 1259 AA.
AC Q8WXX7; A4D1Y9; L7QET3; L7QF75; Q5D049; Q6PJU5; Q9Y4F2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Autism susceptibility gene 2 protein;
GN Name=AUTS2; Synonyms=KIAA0442;
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, AND VARIANT
RP SER-303.
RX PubMed=12160723; DOI=10.1006/geno.2002.6810;
RA Sultana R., Yu C.-H., Yu J., Munson J., Chen D., Hua W., Estes A.,
RA Cortes F., de la Barra F., Yu D., Haider S.T., Trask B.J., Green E.D.,
RA Raskind W.H., Disteche C.M., Wijsman E., Dawson G., Storm D.R.,
RA Schellenberg G.D., Villacres E.C.;
RT "Identification of a novel gene on chromosome 7q11.2 interrupted by a
RT translocation breakpoint in a pair of autistic twins.";
RL Genomics 80:129-134(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), INVOLVEMENT IN MRD26, AND
RP TISSUE SPECIFICITY.
RX PubMed=23332918; DOI=10.1016/j.ajhg.2012.12.011;
RA Beunders G., Voorhoeve E., Golzio C., Pardo L.M., Rosenfeld J.A.,
RA Talkowski M.E., Simonic I., Lionel A.C., Vergult S., Pyatt R.E.,
RA van de Kamp J., Nieuwint A., Weiss M.M., Rizzu P., Verwer L.E.,
RA van Spaendonk R.M., Shen Y., Wu B.L., Yu T., Yu Y., Chiang C.,
RA Gusella J.F., Lindgren A.M., Morton C.C., van Binsbergen E., Bulk S.,
RA van Rossem E., Vanakker O., Armstrong R., Park S.M., Greenhalgh L.,
RA Maye U., Neill N.J., Abbott K.M., Sell S., Ladda R., Farber D.M.,
RA Bader P.I., Cushing T., Drautz J.M., Konczal L., Nash P., de Los Reyes E.,
RA Carter M.T., Hopkins E., Marshall C.R., Osborne L.R., Gripp K.W.,
RA Thrush D.L., Hashimoto S., Gastier-Foster J.M., Astbury C., Ylstra B.,
RA Meijers-Heijboer H., Posthuma D., Menten B., Mortier G., Scherer S.W.,
RA Eichler E.E., Girirajan S., Katsanis N., Groffen A.J., Sistermans E.A.;
RT "Exonic deletions in AUTS2 cause a syndromic form of intellectual
RT disability and suggest a critical role for the C terminus.";
RL Am. J. Hum. Genet. 92:210-220(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Muscle, and Placenta;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1233, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1233, 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).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH PCGF5;
RP RNF2; CSNK2B AND RYBP, AND INTERACTION WITH EP300.
RX PubMed=25519132; DOI=10.1038/nature13921;
RA Gao Z., Lee P., Stafford J.M., von Schimmelmann M., Schaefer A.,
RA Reinberg D.;
RT "An AUTS2-polycomb complex activates gene expression in the CNS.";
RL Nature 516:349-354(2014).
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development. PcG PRC1 complex acts via chromatin remodeling and
CC modification of histones; it mediates monoubiquitination of histone H2A
CC 'Lys-119', rendering chromatin heritably changed in its expressibility
CC (PubMed:25519132). The PRC1-like complex that contains PCGF5, RNF2,
CC CSNK2B, RYBP and AUTS2 has decreased histone H2A ubiquitination
CC activity, due to the phosphorylation of RNF2 by CSNK2B
CC (PubMed:25519132). As a consequence, the complex mediates
CC transcriptional activation (PubMed:25519132). In the cytoplasm, plays a
CC role in axon and dendrite elongation and in neuronal migration during
CC embryonic brain development. Promotes reorganization of the actin
CC cytoskeleton, lamellipodia formation and neurite elongation via its
CC interaction with RAC guanine nucleotide exchange factors, which then
CC leads to the activation of RAC1 (By similarity).
CC {ECO:0000250|UniProtKB:A0A087WPF7, ECO:0000269|PubMed:25519132}.
CC -!- SUBUNIT: Component of a PRC1-like complex that contains PCGF5, RNF2,
CC CSNK2B, RYBP and AUTS2. Within this complex, interacts directly with
CC PCGF5 and CSNK2B (PubMed:25519132). Interacts with the histone
CC acetyltransferase EP300/p300 (PubMed:25519132). Interacts (via Pro-rich
CC region) with PREX1, DOCK1 and ELMO2 (By similarity).
CC {ECO:0000250|UniProtKB:A0A087WPF7, ECO:0000269|PubMed:25519132}.
CC -!- INTERACTION:
CC Q8WXX7; Q09472: EP300; NbExp=3; IntAct=EBI-2875359, EBI-447295;
CC Q8WXX7; Q86SE9: PCGF5; NbExp=7; IntAct=EBI-2875359, EBI-2827999;
CC Q8WXX7-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12140769, EBI-3867333;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25519132}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:A0A087WPF7}. Cell projection,
CC growth cone {ECO:0000250|UniProtKB:A0A087WPF7}. Note=Detected both in
CC cytoplasm and nucleus. Colocalizes with RAC1 at actin-rich growth
CC cones. Detected on the promoter region of actively transcribed genes.
CC {ECO:0000250|UniProtKB:A0A087WPF7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000305};
CC IsoId=Q8WXX7-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q8WXX7-2; Sequence=VSP_003792;
CC Name=3 {ECO:0000305};
CC IsoId=Q8WXX7-3; Sequence=VSP_043556, VSP_043557;
CC Name=5 {ECO:0000305};
CC IsoId=Q8WXX7-5; Sequence=VSP_057063, VSP_003792;
CC -!- TISSUE SPECIFICITY: Strongly expressed in brain, skeletal muscle and
CC kidney. Also expressed in placenta, lung and leukocytes.
CC {ECO:0000269|PubMed:12160723, ECO:0000269|PubMed:23332918}.
CC -!- DOMAIN: The Pro-rich region is important for the interaction with RAC
CC guanine nucleotide exchange factors and the subsequent activation of
CC RAC1, which then promotes lamellipodia formation.
CC {ECO:0000250|UniProtKB:A0A087WPF7}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 26
CC (MRD26) [MIM:615834]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC Additional MRD26 features include autism, short stature, microcephaly,
CC cerebral palsy, and facial dysmorphisms. {ECO:0000269|PubMed:23332918}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the AUTS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23714.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; JQ670866; AFY24235.1; -; mRNA.
DR EMBL; JQ670867; AFY24236.1; -; mRNA.
DR EMBL; AF326917; AAL37411.1; -; mRNA.
DR EMBL; AB007902; BAA23714.2; ALT_INIT; mRNA.
DR EMBL; AC004773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236952; EAL23968.1; -; Genomic_DNA.
DR EMBL; BC011643; AAH11643.1; -; mRNA.
DR EMBL; BC064693; AAH64693.1; -; mRNA.
DR CCDS; CCDS47601.1; -. [Q8WXX7-2]
DR CCDS; CCDS47602.1; -. [Q8WXX7-3]
DR CCDS; CCDS5539.1; -. [Q8WXX7-1]
DR PIR; T00065; T00065.
DR RefSeq; NP_001120703.1; NM_001127231.2. [Q8WXX7-2]
DR RefSeq; NP_001120704.1; NM_001127232.2. [Q8WXX7-3]
DR RefSeq; NP_056385.1; NM_015570.3. [Q8WXX7-1]
DR AlphaFoldDB; Q8WXX7; -.
DR BioGRID; 117516; 30.
DR DIP; DIP-61355N; -.
DR IntAct; Q8WXX7; 27.
DR STRING; 9606.ENSP00000344087; -.
DR GlyGen; Q8WXX7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WXX7; -.
DR PhosphoSitePlus; Q8WXX7; -.
DR BioMuta; AUTS2; -.
DR DMDM; 23396464; -.
DR EPD; Q8WXX7; -.
DR jPOST; Q8WXX7; -.
DR MassIVE; Q8WXX7; -.
DR PaxDb; Q8WXX7; -.
DR PeptideAtlas; Q8WXX7; -.
DR PRIDE; Q8WXX7; -.
DR ProteomicsDB; 75113; -. [Q8WXX7-1]
DR ProteomicsDB; 75114; -. [Q8WXX7-2]
DR ProteomicsDB; 75115; -. [Q8WXX7-3]
DR Antibodypedia; 623; 93 antibodies from 24 providers.
DR DNASU; 26053; -.
DR Ensembl; ENST00000342771.10; ENSP00000344087.4; ENSG00000158321.18. [Q8WXX7-1]
DR Ensembl; ENST00000403018.3; ENSP00000385572.2; ENSG00000158321.18. [Q8WXX7-3]
DR Ensembl; ENST00000406775.6; ENSP00000385263.2; ENSG00000158321.18. [Q8WXX7-2]
DR GeneID; 26053; -.
DR KEGG; hsa:26053; -.
DR MANE-Select; ENST00000342771.10; ENSP00000344087.4; NM_015570.4; NP_056385.1.
DR UCSC; uc003tvv.5; human. [Q8WXX7-1]
DR CTD; 26053; -.
DR DisGeNET; 26053; -.
DR GeneCards; AUTS2; -.
DR HGNC; HGNC:14262; AUTS2.
DR HPA; ENSG00000158321; Tissue enhanced (brain).
DR MalaCards; AUTS2; -.
DR MIM; 607270; gene.
DR MIM; 615834; phenotype.
DR neXtProt; NX_Q8WXX7; -.
DR OpenTargets; ENSG00000158321; -.
DR Orphanet; 352490; Autism spectrum disorder due to AUTS2 deficiency.
DR Orphanet; 585877; B-lymphoblastic leukemia/lymphoma with recurrent genetic abnormality.
DR Orphanet; 106; NON RARE IN EUROPE: Autism.
DR PharmGKB; PA134863175; -.
DR VEuPathDB; HostDB:ENSG00000158321; -.
DR eggNOG; ENOG502QSH4; Eukaryota.
DR GeneTree; ENSGT00940000154823; -.
DR HOGENOM; CLU_1258740_0_0_1; -.
DR InParanoid; Q8WXX7; -.
DR OMA; REDYEHS; -.
DR OrthoDB; 229224at2759; -.
DR PhylomeDB; Q8WXX7; -.
DR TreeFam; TF331929; -.
DR PathwayCommons; Q8WXX7; -.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR SignaLink; Q8WXX7; -.
DR SIGNOR; Q8WXX7; -.
DR BioGRID-ORCS; 26053; 14 hits in 1067 CRISPR screens.
DR ChiTaRS; AUTS2; human.
DR GenomeRNAi; 26053; -.
DR Pharos; Q8WXX7; Tbio.
DR PRO; PR:Q8WXX7; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8WXX7; protein.
DR Bgee; ENSG00000158321; Expressed in cortical plate and 205 other tissues.
DR ExpressionAtlas; Q8WXX7; baseline and differential.
DR Genevisible; Q8WXX7; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0048675; P:axon extension; ISS:UniProtKB.
DR GO; GO:0097484; P:dendrite extension; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:MGI.
DR GO; GO:2000620; P:positive regulation of histone H4-K16 acetylation; IDA:MGI.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR023246; AUTS2.
DR PANTHER; PTHR14429; PTHR14429; 1.
DR Pfam; PF15336; Auts2; 1.
DR PRINTS; PR02044; FIBROSIN1LPF.
PE 1: Evidence at protein level;
KW Alternative splicing; Autism; Autism spectrum disorder; Cell projection;
KW Chromosomal rearrangement; Cytoplasm; Cytoskeleton;
KW Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1259
FT /note="Autism susceptibility gene 2 protein"
FT /id="PRO_0000064767"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..472
FT /note="Important for regulation of lamellipodia formation"
FT /evidence="ECO:0000250|UniProtKB:A0A087WPF7"
FT REGION 299..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..555
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:23332918"
FT /id="VSP_057063"
FT VAR_SEQ 221..266
FT /note="CDSDSDQEEKASDASSEKLFNTVIVNKDPELGVGTLPEHDSQDAGP -> RS
FT GKMCLGEEACLKSGNDMKRDVSNTSSWASNRESFFSLVKLLKGF (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043556"
FT VAR_SEQ 267..1259
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043557"
FT VAR_SEQ 611..634
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:23332918, ECO:0000303|PubMed:9455477"
FT /id="VSP_003792"
FT VARIANT 303
FT /note="A -> S (in dbSNP:rs2293507)"
FT /evidence="ECO:0000269|PubMed:12160723"
FT /id="VAR_013864"
FT CONFLICT 177
FT /note="P -> S (in Ref. 3; BAA23714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1259 AA; 138982 MW; A64D17AFF816E591 CRC64;
MDGPTRGHGL RKKRRSRSQR DRERRSRGGL GAGAAGGGGA GRTRALSLAS SSGSDKEDNG
KPPSSAPSRP RPPRRKRRES TSAEEDIIDG FAMTSFVTFE ALEKDVALKP QERVEKRQTP
LTKKKREALT NGLSFHSKKS RLSHPHHYSS DRENDRNLCQ HLGKRKKMPK ALRQLKPGQN
SCRDSDSESA SGESKGFHRS SSRERLSDSS APSSLGTGYF CDSDSDQEEK ASDASSEKLF
NTVIVNKDPE LGVGTLPEHD SQDAGPIVPK ISGLERSQEK SQDCCKEPIF EPVVLKDPCP
QVAQPIPQPQ TEPQLRAPSP DPDLVQRTEA PPQPPPLSTQ PPQGPPEAQL QPAPQPQVQR
PPRPQSPTQL LHQNLPPVQA HPSAQSLSQP LSAYNSSSLS LNSLSSSRSS TPAKTQPAPP
HISHHPSASP FPLSLPNHSP LHSFTPTLQP PAHSHHPNMF APPTALPPPP PLTSGSLQVA
GHPAGSTYSE QDILRQELNT RFLASQSADR GASLGPPPYL RTEFHQHQHQ HQHTHQHTHQ
HTFTPFPHAI PPTAIMPTPA PPMFDKYPTK VDPFYRHSLF HSYPPAVSGI PPMIPPTGPF
GSLQGAFQPK TSNPIDVAAR PGTVPHTLLQ KDPRLTDPFR PMLRKPGKWC AMHVHIAWQI
YHHQQKVKKQ MQSDPHKLDF GLKPEFLSRP PGPSLFGAIH HPHDLARPST LFSAAGAAHP
TGTPFGPPPH HSNFLNPAAH LEPFNRPSTF TGLAAVGGNA FGGLGNPSVT PNSMFGHKDG
PSVQNFSNPH EPWNRLHRTP PSFPTPPPWL KPGELERSAS AAAHDRDRDV DKRDSSVSKD
DKERESVEKR HSSHPSPAPV LPVNALGHTR SSTEQIRAHL NTEAREKDKP KERERDHSES
RKDLAADEHK AKEGHLPEKD GHGHEGRAAG EEAKQLARVP SPYVRTPVVE SARPNSTSSR
EAEPRKGEPA YENPKKSSEV KVKEERKEDH DLPPEAPQTH RASEPPPPNS SSSVHPGPLA
SMPMTVGVTG IHPMNSISSL DRTRMMTPFM GISPLPGGER FPYPSFHWDP IRDPLRDPYR
ELDIHRRDPL GRDFLLRNDP LHRLSTPRLY EADRSFRDRE PHDYSHHHHH HHHPLSVDPR
REHERGGHLD ERERLHMLRE DYEHTRLHSV HPASLDGHLP HPSLITPGLP SMHYPRISPT
AGNQNGLLNK TPPTAALSAP PPLISTLGGR PVSPRRTTPL SAEIRERPPS HTLKDIEAR
