TACC2_HUMAN
ID TACC2_HUMAN Reviewed; 2948 AA.
AC O95359; Q4VXL0; Q4VXL3; Q4VXL6; Q4VXL7; Q5U5T7; Q86WG6; Q86WG7; Q8TCK9;
AC Q9BVQ1; Q9NZ41; Q9NZR5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Transforming acidic coiled-coil-containing protein 2;
DE AltName: Full=Anti-Zuai-1;
DE Short=AZU-1;
GN Name=TACC2;
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 2), SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10749935; DOI=10.1091/mbc.11.4.1357;
RA Chen H.-M., Schmeichel K.L., Mian I.S., Lelievre S., Petersen O.W.,
RA Bissell M.J.;
RT "AZU-1: a candidate breast tumor suppressor and biomarker for tumor
RT progression.";
RL Mol. Biol. Cell 11:1357-1367(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain, Fetal brain, and Skeletal muscle;
RX PubMed=11121038; DOI=10.1073/pnas.97.26.14352;
RA Gergely F., Karlsson C., Still I.H., Cowell J.K., Kilmartin J., Raff J.W.;
RT "The TACC domain identifies a family of centrosomal proteins that can
RT interact with microtubules.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14352-14357(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, INTERACTION WITH YEATS4, AND VARIANTS PHE-830;
RP ARG-1103 AND LYS-2900.
RX PubMed=12620397; DOI=10.1016/s0888-7543(02)00039-3;
RA Lauffart B., Gangisetty O., Still I.H.;
RT "Molecular cloning, genomic structure and interactions of the putative
RT breast tumor suppressor TACC2.";
RL Genomics 81:192-201(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Placenta, 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1990-2948 (ISOFORM 3), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Endothelial cell;
RX PubMed=11161455; DOI=10.1006/cyto.2000.0812;
RA Pu J.J., Li C., Rodriguez M., Banerjee D.;
RT "Cloning and structural characterization of ECTACC, a new member of the
RT transforming acidic coiled coil (TACC) gene family: cDNA sequence and
RT expression analysis in human microvascular endothelial cells.";
RL Cytokine 13:129-137(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2065-2948 (ISOFORM 3), AND
RP VARIANT THR-2732.
RC TISSUE=Brain;
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 PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=15304323; DOI=10.1016/j.febslet.2004.06.092;
RA Dou Z., Ding X., Zereshki A., Zhang Y., Zhang J., Wang F., Sun J.,
RA Huang H., Yao X.;
RT "TTK kinase is essential for the centrosomal localization of TACC2.";
RL FEBS Lett. 572:51-56(2004).
RN [9]
RP INTERACTION WITH GCN5L2 AND PCAF, AND SUBCELLULAR LOCATION.
RX PubMed=14767476; DOI=10.1038/sj.onc.1207424;
RA Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.;
RT "The transforming acidic coiled coil proteins interact with nuclear histone
RT acetyltransferases.";
RL Oncogene 23:2559-2563(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2317 AND SER-2321, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2256 AND SER-2512, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-201; SER-571;
RP SER-575; SER-758; SER-962; SER-1025; SER-1267; SER-1313; SER-1562;
RP SER-2072; THR-2246; SER-2256; SER-2317; SER-2321; SER-2359; SER-2389;
RP SER-2394; SER-2403 AND SER-2512, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP THR-325 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2625
RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-201; SER-269;
RP SER-493; SER-561; SER-2226; THR-2246; SER-2256; SER-2317; SER-2321;
RP THR-2451; THR-2455; THR-2458; SER-2512 AND SER-2557, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2072; SER-2256; SER-2317 AND
RP SER-2321, AND IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2256; SER-2317; THR-2430;
RP SER-2512; SER-2534 AND SER-2569, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2072; SER-2226 AND SER-2317,
RP AND IDENTIFICATION BY 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 [18]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-798 AND SER-1347.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays a role in the microtubule-dependent coupling of the
CC nucleus and the centrosome. Involved in the processes that regulate
CC centrosome-mediated interkinetic nuclear migration (INM) of neural
CC progenitors (By similarity). May play a role in organizing centrosomal
CC microtubules. May act as a tumor suppressor protein. May represent a
CC tumor progression marker. {ECO:0000250, ECO:0000269|PubMed:10749935}.
CC -!- SUBUNIT: Interacts with CCDC100/CEP120 (By similarity). Interacts with
CC microtubules. Interacts with YEATS4, GCN5L2 and PCAF. {ECO:0000250,
CC ECO:0000269|PubMed:12620397, ECO:0000269|PubMed:14767476}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10749935}. Nucleus
CC {ECO:0000269|PubMed:10749935, ECO:0000269|PubMed:14767476}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:15304323}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=4; Synonyms=Long, TACC2s;
CC IsoId=O95359-4; Sequence=Displayed;
CC Name=1; Synonyms=Short;
CC IsoId=O95359-1; Sequence=VSP_022153, VSP_022156;
CC Name=2;
CC IsoId=O95359-2; Sequence=VSP_022151, VSP_006368, VSP_006369;
CC Name=3; Synonyms=ECTACC;
CC IsoId=O95359-3; Sequence=VSP_006369;
CC Name=5; Synonyms=TACC21;
CC IsoId=O95359-5; Sequence=VSP_022154, VSP_022155;
CC Name=6;
CC IsoId=O95359-6; Sequence=VSP_022153, VSP_022156, VSP_022158;
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, skeletal muscle,
CC brain, prostate, thyroid and trachea. {ECO:0000269|PubMed:11161455,
CC ECO:0000269|PubMed:12620397}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, lung, liver and kidney.
CC {ECO:0000269|PubMed:12620397}.
CC -!- PTM: Phosphorylated by TTK; which is required for localization in
CC centrosome. {ECO:0000269|PubMed:15304323}.
CC -!- SIMILARITY: Belongs to the TACC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29537.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAF63433.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF176646; AAF63433.1; ALT_INIT; mRNA.
DR EMBL; AF095791; AAC64968.2; -; mRNA.
DR EMBL; AF528098; AAO62629.1; -; mRNA.
DR EMBL; AF528099; AAO62630.1; -; mRNA.
DR EMBL; AC063960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL135793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000999; AAH00999.1; -; mRNA.
DR EMBL; BC039311; AAH39311.1; -; mRNA.
DR EMBL; AF220152; AAF29537.2; ALT_SEQ; mRNA.
DR EMBL; AL713712; CAD28509.1; -; mRNA.
DR CCDS; CCDS7625.1; -. [O95359-5]
DR CCDS; CCDS7626.1; -. [O95359-4]
DR CCDS; CCDS7627.1; -. [O95359-1]
DR CCDS; CCDS7628.1; -. [O95359-6]
DR RefSeq; NP_001278807.1; NM_001291878.1.
DR RefSeq; NP_008928.1; NM_006997.3. [O95359-1]
DR RefSeq; NP_996742.1; NM_206860.2. [O95359-6]
DR RefSeq; NP_996743.1; NM_206861.2. [O95359-5]
DR RefSeq; NP_996744.3; NM_206862.3. [O95359-4]
DR BioGRID; 115830; 58.
DR CORUM; O95359; -.
DR IntAct; O95359; 12.
DR MINT; O95359; -.
DR STRING; 9606.ENSP00000358001; -.
DR CarbonylDB; O95359; -.
DR iPTMnet; O95359; -.
DR PhosphoSitePlus; O95359; -.
DR BioMuta; TACC2; -.
DR CPTAC; CPTAC-1011; -.
DR EPD; O95359; -.
DR jPOST; O95359; -.
DR MassIVE; O95359; -.
DR MaxQB; O95359; -.
DR PaxDb; O95359; -.
DR PeptideAtlas; O95359; -.
DR PRIDE; O95359; -.
DR ProteomicsDB; 50816; -. [O95359-4]
DR ProteomicsDB; 50817; -. [O95359-1]
DR ProteomicsDB; 50818; -. [O95359-2]
DR ProteomicsDB; 50819; -. [O95359-3]
DR ProteomicsDB; 50820; -. [O95359-5]
DR ProteomicsDB; 50821; -. [O95359-6]
DR Antibodypedia; 46332; 272 antibodies from 20 providers.
DR DNASU; 10579; -.
DR Ensembl; ENST00000260733.7; ENSP00000260733.3; ENSG00000138162.19. [O95359-1]
DR Ensembl; ENST00000334433.7; ENSP00000334280.2; ENSG00000138162.19. [O95359-4]
DR Ensembl; ENST00000358010.5; ENSP00000350701.1; ENSG00000138162.19. [O95359-5]
DR Ensembl; ENST00000360561.7; ENSP00000353763.3; ENSG00000138162.19. [O95359-6]
DR Ensembl; ENST00000369000.5; ENSP00000357996.1; ENSG00000138162.19. [O95359-2]
DR Ensembl; ENST00000369005.6; ENSP00000358001.1; ENSG00000138162.19. [O95359-4]
DR Ensembl; ENST00000513429.5; ENSP00000425062.1; ENSG00000138162.19. [O95359-5]
DR GeneID; 10579; -.
DR KEGG; hsa:10579; -.
DR MANE-Select; ENST00000369005.6; ENSP00000358001.1; NM_206862.4; NP_996744.4.
DR UCSC; uc001lfv.4; human. [O95359-4]
DR CTD; 10579; -.
DR DisGeNET; 10579; -.
DR GeneCards; TACC2; -.
DR HGNC; HGNC:11523; TACC2.
DR HPA; ENSG00000138162; Tissue enhanced (heart muscle, skeletal muscle).
DR MIM; 605302; gene.
DR neXtProt; NX_O95359; -.
DR OpenTargets; ENSG00000138162; -.
DR PharmGKB; PA36300; -.
DR VEuPathDB; HostDB:ENSG00000138162; -.
DR eggNOG; ENOG502QUT1; Eukaryota.
DR GeneTree; ENSGT00940000157052; -.
DR HOGENOM; CLU_000545_0_0_1; -.
DR InParanoid; O95359; -.
DR OMA; KAGSQHE; -.
DR OrthoDB; 669540at2759; -.
DR PhylomeDB; O95359; -.
DR TreeFam; TF333149; -.
DR PathwayCommons; O95359; -.
DR SignaLink; O95359; -.
DR BioGRID-ORCS; 10579; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; TACC2; human.
DR GeneWiki; TACC2; -.
DR GenomeRNAi; 10579; -.
DR Pharos; O95359; Tbio.
DR PRO; PR:O95359; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O95359; protein.
DR Bgee; ENSG00000138162; Expressed in apex of heart and 208 other tissues.
DR ExpressionAtlas; O95359; baseline and differential.
DR Genevisible; O95359; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:InterPro.
DR InterPro; IPR039915; TACC.
DR InterPro; IPR007707; TACC_C.
DR PANTHER; PTHR13924; PTHR13924; 1.
DR Pfam; PF05010; TACC_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2948
FT /note="Transforming acidic coiled-coil-containing protein
FT 2"
FT /id="PRO_0000179988"
FT DOMAIN 2315..2403
FT /note="SPAZ"
FT REGION 1..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1243..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..1705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1741..1878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1907..2035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2052..2460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2555..2577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2675..2703
FT /evidence="ECO:0000255"
FT COILED 2746..2947
FT /evidence="ECO:0000255"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1986
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2071..2099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2112..2128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2166..2180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2346..2397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2415..2439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2443..2457
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2072
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 2161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJG0"
FT MOD_RES 2226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2246
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 2317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJG0"
FT MOD_RES 2394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2430
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2451
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2455
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2458
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2553
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJG0"
FT MOD_RES 2557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..2296
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10749935"
FT /id="VSP_022151"
FT VAR_SEQ 1..1922
FT /note="Missing (in isoform 1 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11121038,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022153"
FT VAR_SEQ 49..1857
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12620397"
FT /id="VSP_022154"
FT VAR_SEQ 1900..1944
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12620397"
FT /id="VSP_022155"
FT VAR_SEQ 1923..1945
FT /note="APAGDRVEASTPSCPDPAKDLSR -> MGGSQSLQPAPASDLNLEASEAM
FT (in isoform 1 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11121038,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022156"
FT VAR_SEQ 2429..2432
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10749935"
FT /id="VSP_006368"
FT VAR_SEQ 2633..2709
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10749935,
FT ECO:0000303|PubMed:11161455, ECO:0000303|PubMed:17974005"
FT /id="VSP_006369"
FT VAR_SEQ 2680..2709
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022158"
FT VARIANT 170
FT /note="V -> I (in dbSNP:rs11200385)"
FT /id="VAR_053706"
FT VARIANT 798
FT /note="L -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036381"
FT VARIANT 830
FT /note="L -> F (in dbSNP:rs10887063)"
FT /evidence="ECO:0000269|PubMed:12620397"
FT /id="VAR_053707"
FT VARIANT 1103
FT /note="W -> R (in dbSNP:rs7073433)"
FT /evidence="ECO:0000269|PubMed:12620397"
FT /id="VAR_053708"
FT VARIANT 1347
FT /note="A -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036382"
FT VARIANT 1425
FT /note="A -> T (in dbSNP:rs4752642)"
FT /id="VAR_053709"
FT VARIANT 1492
FT /note="P -> L (in dbSNP:rs7920896)"
FT /id="VAR_053710"
FT VARIANT 1916
FT /note="E -> K (in dbSNP:rs12765679)"
FT /id="VAR_053711"
FT VARIANT 2078
FT /note="I -> T (in dbSNP:rs7083331)"
FT /id="VAR_029803"
FT VARIANT 2102
FT /note="N -> S (in dbSNP:rs3750843)"
FT /id="VAR_020478"
FT VARIANT 2197
FT /note="V -> A (in dbSNP:rs2295873)"
FT /id="VAR_020479"
FT VARIANT 2210
FT /note="A -> V (in dbSNP:rs2295874)"
FT /id="VAR_029804"
FT VARIANT 2216
FT /note="P -> L (in dbSNP:rs2295875)"
FT /id="VAR_053712"
FT VARIANT 2261
FT /note="L -> H (in dbSNP:rs2295876)"
FT /id="VAR_020480"
FT VARIANT 2271
FT /note="E -> D (in dbSNP:rs11200483)"
FT /id="VAR_053713"
FT VARIANT 2718
FT /note="V -> I (in dbSNP:rs2295878)"
FT /id="VAR_020481"
FT VARIANT 2732
FT /note="A -> T (in dbSNP:rs2295879)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_020482"
FT VARIANT 2900
FT /note="Q -> K (in dbSNP:rs1063627)"
FT /evidence="ECO:0000269|PubMed:12620397"
FT /id="VAR_029805"
FT CONFLICT 2896
FT /note="R -> Q (in Ref. 3; AAO62629/AAO62630)"
FT /evidence="ECO:0000305"
FT CONFLICT 2909
FT /note="S -> T (in Ref. 5; AAH39311)"
FT /evidence="ECO:0000305"
FT MOD_RES O95359-2:325
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES O95359-3:2625
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 2948 AA; 309427 MW; 9DC4CC5231A5ADBD CRC64;
MGNENSTSDN QRTLSAQTPR SAQPPGNSQN IKRKQQDTPG SPDHRDASSI GSVGLGGFCT
ASESSASLDP CLVSPEVTEP RKDPQGARGP EGSLLPSPPP SQEREHPSSS MPFAECPPEG
CLASPAAAPE DGPQTQSPRR EPAPNAPGDI AAAFPAERDS STPYQEIAAV PSAGRERQPK
EEGQKSSFSF SSGIDQSPGM SPVPLREPMK APLCGEGDQP GGFESQEKEA AGGFPPAESR
QGVASVQVTP EAPAAAQQGT ESSAVLEKSP LKPMAPIPQD PAPRASDRER GQGEAPPQYL
TDDLEFLRAC HLPRSNSGAA PEAEVNAASQ ESCQQPVGAY LPHAELPWGL PSPALVPEAG
GSGKEALDTI DVQGHPQTGM RGTKPNQVVC VAAGGQPEGG LPVSPEPSLL TPTEEAHPAS
SLASFPAAQI PIAVEEPGSS SRESVSKAGM PVSADAAKEV VDAGLVGLER QVSDLGSKGE
HPEGDPGEVP APSPQERGEH LNTEQSHEVQ PGVPPPPLPK EQSHEVQPGA PPPPLPKAPS
ESARGPPGPT DGAKVHEDST SPAVAKEGSR SPGDSPGGKE EAPEPPDGGD PGNLQGEDSQ
AFSSKRDPEV GKDELSKPSS DAESRDHPSS HSAQPPRKGG AGHTDGPHSQ TAEADASGLP
HKLGEEDPVL PPVPDGAGEP TVPEGAIWEG SGLQPKCPDT LQSREGLGRM ESFLTLESEK
SDFPPTPVAE VAPKAQEGES TLEIRKMGSC DGEGLLTSPD QPRGPACDAS RQEFHAGVPH
PPQGENLAAD LGLTALILDQ DQQGIPSCPG EGWIRGAASE WPLLSSEKHL QPSQAQPETS
IFDVLKEQAQ PPENGKETSP SHPGFKDQGA DSSQIHVPVE PQEDNNLPTH GGQEQALGSE
LQSQLPKGTL SDTPTSSPTD MVWESSLTEE SELSAPTRQK LPALGEKRPE GACGDGQSSR
VSPPAADVLK DFSLAGNFSR KETCCTGQGP NKSQQALADA LEEGSQHEEA CQRHPGASEA
ADGCSPLWGL SKREMASGNT GEAPPCQPDS VALLDAVPCL PALAPASPGV TPTQDAPETE
ACDETQEGRQ QPVPAPQQKM ECWATSDAES PKLLASFPSA GEQGGEAGAA ETGGSAGAGD
PGKQQAPEKP GEATLSCGLL QTEHCLTSGE EASTSALRES CQAEHPMASC QDALLPAREL
GGIPRSTMDF STHQAVPDPK ELLLSGPPEV AAPDTPYLHV DSAAQRGAED SGVKAVSSAD
PRAPGESPCP VGEPPLALEN AASLKLFAGS LAPLLQPGAA GGEIPAVQAS SGSPKARTTE
GPVDSMPCLD RMPLLAKGKQ ATGEEKAATA PGAGAKASGE GMAGDAAGET EGSMERMGEP
SQDPKQGTSG GVDTSSEQIA TLTGFPDFRE HIAKIFEKPV LGALATPGEK AGAGRSAVGK
DLTRPLGPEK LLDGPPGVDV TLLPAPPARL QVEKKQQLAG EAEISHLALQ DPASDKLLGP
AGLTWERNLP GAGVGKEMAG VPPTLREDER PEGPGAAWPG LEGQAYSQLE RSRQELASGL
PSPAATQELP VERAAAFQVA PHSHGEEAVA QDRIPSGKQH QETSACDSPH GEDGPGDFAH
TGVPGHVPRS TCAPSPQREV LTVPEANSEP WTLDTLGGER RPGVTAGILE MRNALGNQST
PAPPTGEVAD TPLEPGKVAG AAGEAEGDIT LSTAETQACA SGDLPEAGTT RTFSVVAGDL
VLPGSCQDPA CSDKAPGMEG TAALHGDSPA RPQQAKEQPG PERPIPAGDG KVCVSSPPEP
DETHDPKLQH LAPEELHTDR ESPRPGPSML PSVPKKDAPR VMDKVTSDET RGAEGTESSP
VADDIIQPAA PADLESPTLA ASSYHGDVVG QVSTDLIAQS ISPAAAHAGL PPSAAEHIVS
PSAPAGDRVE ASTPSCPDPA KDLSRSSDSE EAFETPESTT PVKAPPAPPP PPPEVIPEPE
VSTQPPPEEP GCGSETVPVP DGPRSDSVEG SPFRPPSHSF SAVFDEDKPI ASSGTYNLDF
DNIELVDTFQ TLEPRASDAK NQEGKVNTRR KSTDSVPISK STLSRSLSLQ ASDFDGASSS
GNPEAVALAP DAYSTGSSSA SSTLKRTKKP RPPSLKKKQT TKKPTETPPV KETQQEPDEE
SLVPSGENLA SETKTESAKT EGPSPALLEE TPLEPAVGPK AACPLDSESA EGVVPPASGG
GRVQNSPPVG RKTLPLTTAP EAGEVTPSDS GGQEDSPAKG LSVRLEFDYS EDKSSWDNQQ
ENPPPTKKIG KKPVAKMPLR RPKMKKTPEK LDNTPASPPR SPAEPNDIPI AKGTYTFDID
KWDDPNFNPF SSTSKMQESP KLPQQSYNFD PDTCDESVDP FKTSSKTPSS PSKSPASFEI
PASAMEANGV DGDGLNKPAK KKKTPLKTDT FRVKKSPKRS PLSDPPSQDP TPAATPETPP
VISAVVHATD EEKLAVTNQK WTCMTVDLEA DKQDYPQPSD LSTFVNETKF SSPTEELDYR
NSYEIEYMEK IGSSLPQDDD APKKQALYLM FDTSQESPVK SSPVRMSESP TPCSGSSFEE
TEALVNTAAK NQHPVPRGLA PNQESHLQVP EKSSQKELEA MGLGTPSEAI EITAPEGSFA
SADALLSRLA HPVSLCGALD YLEPDLAEKN PPLFAQKLQE ELEFAIMRIE ALKLARQIAL
ASRSHQDAKR EAAHPTDVSI SKTALYSRIG TAEVEKPAGL LFQQPDLDSA LQIARAEIIT
KEREVSEWKD KYEESRREVM EMRKIVAEYE KTIAQMIEDE QREKSVSHQT VQQLVLEKEQ
ALADLNSVEK SLADLFRRYE KMKEVLEGFR KNEEVLKRCA QEYLSRVKKE EQRYQALKVH
AEEKLDRANA EIAQVRGKAQ QEQAAHQASL RKEQLRVDAL ERTLEQKNKE IEELTKICDE
LIAKMGKS
