ID AKNA_HUMAN Reviewed; 1439 AA. AC Q7Z591; Q05BK5; Q5T535; Q5T536; Q5T537; Q64FX6; Q64FX7; Q64FX8; Q64FY2; AC Q6ZMK0; Q6ZNL2; Q6ZTX0; Q8TET1; Q8TF33; Q96RR9; Q9H7P7; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 147. DE RecName: Full=Microtubule organization protein AKNA {ECO:0000305}; DE AltName: Full=AT-hook-containing transcription factor {ECO:0000303|PubMed:15869410}; GN Name=AKNA {ECO:0000303|PubMed:15869410, ECO:0000312|HGNC:HGNC:24108}; GN Synonyms=KIAA1968 {ECO:0000303|PubMed:11853319}; 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] (ISOFORMS 1; 2; 5; 6 AND 7). RX PubMed=15869410; DOI=10.1089/dna.2005.24.325; RA Sims-Mourtada J.C., Bruce S., McKeller M.R., Rangel R., Guzman-Rojas L., RA Cain K., Lopez C., Zimonjic D.B., Popescu N.C., Gordon J., Wilkinson M.F., RA Martinez-Valdez H.; RT "The human AKNA gene expresses multiple transcripts and protein isoforms as RT a result of alternative promoter usage, splicing, and polyadenylation."; RL DNA Cell Biol. 24:325-338(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-624. RC TISSUE=Brain; RX PubMed=11853319; DOI=10.1093/dnares/8.6.319; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXII. The RT complete sequences of 50 new cDNA clones which code for large proteins."; RL DNA Res. 8:319-327(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 8), AND VARIANTS RP LEU-624; GLN-1119 AND PRO-1303. RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT RP PRO-1303. RC TISSUE=Eye; 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 762-1395, FUNCTION, SUBCELLULAR LOCATION, RP DNA-BINDING, AND TISSUE SPECIFICITY. RX PubMed=11268217; DOI=10.1038/35066602; RA Siddiqa A., Sims-Mourtada J.C., Guzman-Rojas L., Rangel R., Guret C., RA Madrid-Marina V., Sun Y., Martinez-Valdez H.; RT "Regulation of CD40 and CD40 ligand by the AT-hook transcription factor RT AKNA."; RL Nature 410:383-387(2001). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534 AND SER-1387, AND RP IDENTIFICATION BY 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-52; SER-316; SER-499; RP SER-767; SER-770; SER-848; SER-886; SER-997; SER-1010; SER-1228; SER-1377 RP AND SER-1424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Erythroleukemia; 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). CC -!- FUNCTION: Centrosomal protein that plays a key role in cell CC delamination by regulating microtubule organization (By similarity). CC Required for the delamination and retention of neural stem cells from CC the subventricular zone during neurogenesis (By similarity). Also CC regulates the epithelial-to-mesenchymal transition in other epithelial CC cells (By similarity). Acts by increasing centrosomal microtubule CC nucleation and recruiting nucleation factors and minus-end stabilizers, CC thereby destabilizing microtubules at the adherens junctions and CC mediating constriction of the apical endfoot (By similarity). In CC addition, may also act as a transcription factor that specifically CC activates the expression of the CD40 receptor and its ligand CC CD40L/CD154, two cell surface molecules on lymphocytes that are CC critical for antigen-dependent-B-cell development (PubMed:11268217). CC Binds to A/T-rich promoters (PubMed:11268217). It is unclear how it can CC both act as a microtubule organizer and as a transcription factor; CC additional evidences are required to reconcile these two apparently CC contradictory functions (Probable). {ECO:0000250|UniProtKB:Q80VW7, CC ECO:0000269|PubMed:11268217, ECO:0000305}. CC -!- SUBUNIT: Interacts with DCTN1. Interacts with MAPRE1/EB1. Interacts CC with ODF2. Interacts with CAMSAP3. {ECO:0000250|UniProtKB:Q80VW7}. CC -!- INTERACTION: CC Q7Z591; O95400: CD2BP2; NbExp=2; IntAct=EBI-2799297, EBI-768015; CC Q7Z591; P25800: LMO1; NbExp=3; IntAct=EBI-2799297, EBI-8639312; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q80VW7}. Nucleus CC {ECO:0000269|PubMed:11268217}. Note=Localizes to the distal part of the CC subdistal appendages of the mother centriole in interphase. Also found CC at the proximal ends of centrioles and along microtubules. The CC centrosomal localization is dependent on centrioles. Dissociates from CC centrosomes during M-phase without proteolytic degradation and CC reassembles at the centrosomes during late telophase and early G1 CC phase. Dissociation and reassembly is regulated by phosphorylation. CC {ECO:0000250|UniProtKB:Q80VW7}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=1; Synonyms=B2 {ECO:0000303|PubMed:15869410}, D CC {ECO:0000303|PubMed:15869410}; CC IsoId=Q7Z591-1; Sequence=Displayed; CC Name=2; Synonyms=E {ECO:0000303|PubMed:15869410}; CC IsoId=Q7Z591-2; Sequence=VSP_025936; CC Name=3; CC IsoId=Q7Z591-3; Sequence=VSP_025939; CC Name=4; CC IsoId=Q7Z591-4; Sequence=VSP_025932, VSP_025940; CC Name=5; Synonyms=F1 {ECO:0000303|PubMed:15869410}; CC IsoId=Q7Z591-5; Sequence=VSP_025933; CC Name=6; CC IsoId=Q7Z591-6; Sequence=VSP_025937, VSP_025938; CC Name=7; Synonyms=A {ECO:0000303|PubMed:15869410}; CC IsoId=Q7Z591-7; Sequence=VSP_025935; CC Name=8; CC IsoId=Q7Z591-8; Sequence=VSP_025934; CC -!- TISSUE SPECIFICITY: Predominantly expressed by lymphoid tissues. Highly CC expressed in the spleen, lymph nodes and peripheral blood leukocytes, CC expressed at lower level in the thymus. Mainly expressed by germinal CC center B-lymphocytes, a stage in which receptor and ligand interactions CC are crucial for B-lymphocyte maturation. Expressed by B- and T- CC lymphocytes, Natural killer cells and CD1a(+)CD14(-) but not CC CD1a(-)CD14(+) dendritic cells. Weakly or not expressed in fetal liver CC and in adult bone marrow. {ECO:0000269|PubMed:11268217}. CC -!- PTM: Phosphorylated; phosphorylation regulates dissociation from and CC reassembly at the centrosome. {ECO:0000250|UniProtKB:Q80VW7}. CC -!- SIMILARITY: Belongs to the AKNA family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK83024.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAU34192.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB84866.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB85554.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC85132.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAD18725.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY703039; AAU34186.1; -; mRNA. DR EMBL; AY703043; AAU34190.1; -; mRNA. DR EMBL; AY703044; AAU34191.1; -; mRNA. DR EMBL; AY703045; AAU34192.1; ALT_FRAME; mRNA. DR EMBL; AB075848; BAB85554.1; ALT_INIT; mRNA. DR EMBL; AK024431; BAB15721.1; -; mRNA. DR EMBL; AK074040; BAB84866.1; ALT_INIT; mRNA. DR EMBL; AK131082; BAC85132.1; ALT_SEQ; mRNA. DR EMBL; AK160382; BAD18725.1; ALT_SEQ; mRNA. DR EMBL; AL356796; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC042202; AAH42202.1; -; mRNA. DR EMBL; BC055285; AAH55285.1; -; mRNA. DR EMBL; AF286341; AAK83024.1; ALT_FRAME; mRNA. DR CCDS; CCDS6805.1; -. [Q7Z591-1] DR RefSeq; NP_001304879.1; NM_001317950.1. [Q7Z591-1] DR RefSeq; NP_001304881.1; NM_001317952.1. [Q7Z591-7] DR RefSeq; NP_110394.3; NM_030767.5. [Q7Z591-1] DR RefSeq; XP_005252301.1; XM_005252244.2. [Q7Z591-1] DR RefSeq; XP_005252302.1; XM_005252245.1. [Q7Z591-1] DR RefSeq; XP_005252304.1; XM_005252247.4. [Q7Z591-1] DR RefSeq; XP_006717357.1; XM_006717294.1. [Q7Z591-1] DR RefSeq; XP_006717358.1; XM_006717295.2. DR RefSeq; XP_011517365.1; XM_011519063.2. [Q7Z591-7] DR RefSeq; XP_011517367.2; XM_011519065.2. [Q7Z591-7] DR RefSeq; XP_016870661.1; XM_017015172.1. DR AlphaFoldDB; Q7Z591; -. DR SMR; Q7Z591; -. DR BioGRID; 123268; 6. DR IntAct; Q7Z591; 5. DR MINT; Q7Z591; -. DR STRING; 9606.ENSP00000303769; -. DR GlyGen; Q7Z591; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q7Z591; -. DR PhosphoSitePlus; Q7Z591; -. DR BioMuta; AKNA; -. DR DMDM; 150416853; -. DR EPD; Q7Z591; -. DR jPOST; Q7Z591; -. DR MassIVE; Q7Z591; -. DR MaxQB; Q7Z591; -. DR PaxDb; 9606-ENSP00000303769; -. DR PeptideAtlas; Q7Z591; -. DR ProteomicsDB; 69266; -. [Q7Z591-1] DR ProteomicsDB; 69267; -. [Q7Z591-2] DR ProteomicsDB; 69268; -. [Q7Z591-3] DR ProteomicsDB; 69269; -. [Q7Z591-4] DR ProteomicsDB; 69270; -. [Q7Z591-5] DR ProteomicsDB; 69271; -. [Q7Z591-6] DR ProteomicsDB; 69272; -. [Q7Z591-7] DR ProteomicsDB; 69273; -. [Q7Z591-8] DR Pumba; Q7Z591; -. DR Antibodypedia; 54667; 44 antibodies from 14 providers. DR DNASU; 80709; -. DR Ensembl; ENST00000223791.7; ENSP00000223791.3; ENSG00000106948.17. [Q7Z591-8] DR Ensembl; ENST00000307564.8; ENSP00000303769.4; ENSG00000106948.17. [Q7Z591-1] DR Ensembl; ENST00000312033.3; ENSP00000309222.3; ENSG00000106948.17. [Q7Z591-3] DR Ensembl; ENST00000374075.9; ENSP00000363188.5; ENSG00000106948.17. [Q7Z591-2] DR Ensembl; ENST00000374079.8; ENSP00000363192.4; ENSG00000106948.17. [Q7Z591-4] DR Ensembl; ENST00000374088.8; ENSP00000363201.3; ENSG00000106948.17. [Q7Z591-1] DR GeneID; 80709; -. DR KEGG; hsa:80709; -. DR MANE-Select; ENST00000374088.8; ENSP00000363201.3; NM_001317950.2; NP_001304879.1. DR UCSC; uc004bio.5; human. [Q7Z591-1] DR AGR; HGNC:24108; -. DR CTD; 80709; -. DR DisGeNET; 80709; -. DR GeneCards; AKNA; -. DR HGNC; HGNC:24108; AKNA. DR HPA; ENSG00000106948; Tissue enhanced (lymphoid). DR MIM; 605729; gene. DR neXtProt; NX_Q7Z591; -. DR OpenTargets; ENSG00000106948; -. DR PharmGKB; PA134908332; -. DR VEuPathDB; HostDB:ENSG00000106948; -. DR eggNOG; ENOG502QRSN; Eukaryota. DR GeneTree; ENSGT00940000154254; -. DR HOGENOM; CLU_005641_0_0_1; -. DR InParanoid; Q7Z591; -. DR OMA; YHPPKAR; -. DR OrthoDB; 4212098at2759; -. DR PhylomeDB; Q7Z591; -. DR TreeFam; TF336885; -. DR PathwayCommons; Q7Z591; -. DR SignaLink; Q7Z591; -. DR BioGRID-ORCS; 80709; 11 hits in 1160 CRISPR screens. DR ChiTaRS; AKNA; human. DR GenomeRNAi; 80709; -. DR Pharos; Q7Z591; Tbio. DR PRO; PR:Q7Z591; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q7Z591; Protein. DR Bgee; ENSG00000106948; Expressed in granulocyte and 148 other cell types or tissues. DR GO; GO:0005814; C:centriole; ISS:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0060232; P:delamination; ISS:UniProtKB. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB. DR GO; GO:0060234; P:neuroblast delamination; ISS:UniProtKB. DR GO; GO:0021849; P:neuroblast division in subventricular zone; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB. DR InterPro; IPR022150; AKNA_dom. DR PANTHER; PTHR21510; AKNA DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR21510:SF15; MICROTUBULE ORGANIZATION PROTEIN AKNA; 1. DR Pfam; PF12443; AKNA; 1. DR Genevisible; Q7Z591; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Cytoplasm; Cytoskeleton; DNA-binding; KW Microtubule; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..1439 FT /note="Microtubule organization protein AKNA" FT /id="PRO_0000289159" FT DNA_BIND 1115..1123 FT /note="A.T hook" FT REGION 1..394 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 507..562 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 659..682 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 771..804 FT /note="PEST" FT REGION 775..942 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 911..932 FT /note="PEST" FT REGION 977..1005 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1095..1165 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1180..1211 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1252..1329 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 22..41 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 184..224 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 302..322 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 366..381 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 530..544 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 777..795 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 878..895 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 922..942 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 982..1004 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1291..1317 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 316 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 499 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 534 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 767 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 770 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 848 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 886 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 997 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1010 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1172 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80VW7" FT MOD_RES 1173 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80VW7" FT MOD_RES 1228 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1377 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1387 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1424 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..1055 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_025932" FT VAR_SEQ 1..753 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15869410" FT /id="VSP_025933" FT VAR_SEQ 1..540 FT /note="Missing (in isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_025934" FT VAR_SEQ 1..119 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:15869410" FT /id="VSP_025935" FT VAR_SEQ 1..91 FT /note="MASSETEIRWAEPGLGKGPQRRRWAWAEDKRDVDRSSSQSWEEERLFPNATS FT PELLEDFRLAQQHLPPLEWDPHPQPDGHQDSESGETSGE -> MLRSEWPVFP (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15869410" FT /id="VSP_025936" FT VAR_SEQ 448..572 FT /note="EDYHRLLTKYAEAENTIDQLRLGAKVNLFSDPPQPNHSIHTGMVPQGTKVLS FT FTIPQPRSAEWWPGPAEDPQASAASGWPSARGDLSPSSLTSMPTLGWLPENRDISEDQS FT SAEQTQALASQASQ -> VSGTHGCGCVTKAPVGLGWRLIGVGRPGVEAGWGGEAWDRA FT WLGWEALGRRLVGWGGLGWRLARVGSPGMEASGVGRPGVGSPGVEPGGVGRPGVEAGWG FT RKPWDRGWWGGEAWGGGWLGQEALG (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15869410" FT /id="VSP_025937" FT VAR_SEQ 573..1439 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15869410" FT /id="VSP_025938" FT VAR_SEQ 832..1439 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11853319" FT /id="VSP_025939" FT VAR_SEQ 1056..1074 FT /note="PCGPTETIPSFLLTRAGRD -> MSAGGGTRGYSPRSPGATS (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_025940" FT VARIANT 624 FT /note="P -> L (in dbSNP:rs3748176)" FT /evidence="ECO:0000269|PubMed:11853319, FT ECO:0000269|PubMed:14702039" FT /id="VAR_032586" FT VARIANT 1097 FT /note="Q -> R (in dbSNP:rs1265891)" FT /id="VAR_032587" FT VARIANT 1119 FT /note="R -> Q (in dbSNP:rs3748178)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_032588" FT VARIANT 1303 FT /note="S -> P (in dbSNP:rs2250242)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_032589" FT VARIANT 1327 FT /note="Y -> C (in dbSNP:rs2787344)" FT /id="VAR_032590" FT CONFLICT 799 FT /note="D -> V (in Ref. 3; BAD18725/BAC85132)" FT /evidence="ECO:0000305" FT CONFLICT 816 FT /note="R -> S (in Ref. 3; BAD18725)" FT /evidence="ECO:0000305" FT CONFLICT 1037 FT /note="L -> F (in Ref. 6; AAK83024)" FT /evidence="ECO:0000305" FT CONFLICT 1103 FT /note="P -> Q (in Ref. 3; BAD18725)" FT /evidence="ECO:0000305" FT CONFLICT 1114 FT /note="A -> P (in Ref. 3; BAD18725)" FT /evidence="ECO:0000305" FT CONFLICT 1429 FT /note="Q -> P (in Ref. 3; BAD18725)" FT /evidence="ECO:0000305" FT CONFLICT 1435..1436 FT /note="GS -> AP (in Ref. 3; BAD18725)" FT /evidence="ECO:0000305" SQ SEQUENCE 1439 AA; 155139 MW; 51688A0C5C55A7BE CRC64; MASSETEIRW AEPGLGKGPQ RRRWAWAEDK RDVDRSSSQS WEEERLFPNA TSPELLEDFR LAQQHLPPLE WDPHPQPDGH QDSESGETSG EEAEAEDVDS PASSHEPLAW LPQQGRQLDM TEEEPDGTLG SLEVEEAGES SSRLGYEAGL SLEGHGNTSP MALGHGQARG WVASGEQASG DKLSEHSEVN PSVELSPARS WSSGTVSLDH PSDSLDSTWE GETDGPQPTA LAETLPEGPS HHLLSPDGRT GGSVARATPM EFQDSSAPPA QSPQHATDRW RRETTRFFCP QPKEHIWKQT KTSPKPLPSR FIGSISPLNP QPRPTRQGRP LPRQGATLAG RSSSNAPKYG RGQLNYPLPD FSKVGPRVRF PKDESYRPPK SRSHNRKPQA PARPLIFKSP AEIVQEVLLS SGEAALAKDT PPAHPITRVP QEFQTPEQAT ELVHQLQEDY HRLLTKYAEA ENTIDQLRLG AKVNLFSDPP QPNHSIHTGM VPQGTKVLSF TIPQPRSAEW WPGPAEDPQA SAASGWPSAR GDLSPSSLTS MPTLGWLPEN RDISEDQSSA EQTQALASQA SQFLAKVESF ERLIQAGRLM PQDQVKGFQR LKAAHAALEE EYLKACREQH PAQPLAGSKG TPGRFDPRRE LEAEIYRLGS CLEELKEHID QTQQEPEPPG SDSALDSTPA LPCLHQPTHL PAPSGQAPMP AIKTSCPEPA TTTAAASTGP CPLHVNVEVS SGNSEVEDRP QDPLARLRHK ELQMEQVYHG LMERYLSVKS LPEAMRMEEE EEGEEEEEEE GGGDSLEVDG VAATPGKAEA TRVLPRQCPV QAEKSHGAPL EEATEKMVSM KPPGFQASLA RDGHMSGLGK AEAAPPGPGV PPHPPGTKSA ASHQSSMTSL EGSGISERLP QKPLHRGGGP HLEETWMASP ETDSGFVGSE TSRVSPLTQT PEHRLSHIST AGTLAQPFAA SVPRDGASYP KARGSLIPRR ATEPSTPRSQ AQRYLSSPSG PLRQRAPNFS LERTLAAEMA VPGSEFEGHK RISEQPLPNK TISPPPAPAP AAAPLPCGPT ETIPSFLLTR AGRDQAICEL QEEVSRLRLR LEDSLHQPLQ GSPTRPASAF DRPARTRGRP ADSPATWGSH YGSKSTERLP GEPRGEEQIV PPGRQRARSS SVPREVLRLS LSSESELPSL PLFSEKSKTT KDSPQAARDG KRGVGSAGWP DRVTFRGQYT GHEYHVLSPK AVPKGNGTVS CPHCRPIRTQ DAGGAVTGDP LGPPPADTLQ CPLCGQVGSP PEADGPGSAT SGAEKATTRR KASSTPSPKQ RSKQAGSSPR PPPGLWYLAT APPAPAPPAF AYISSVPIMP YPPAAVYYAP AGPTSAQPAA KWPPTASPPP ARRHRHSIQL DLGDLEELNK ALSRAVQAAE SVRSTTRQMR SSLSADLRQA HSLRGSCLF //