AKNA_HUMAN
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 03-AUG-2022, entry version 139.
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};
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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. [Q7Z591-7]
DR AlphaFoldDB; Q7Z591; -.
DR SMR; Q7Z591; -.
DR BioGRID; 123268; 4.
DR IntAct; Q7Z591; 5.
DR MINT; Q7Z591; -.
DR STRING; 9606.ENSP00000303769; -.
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; Q7Z591; -.
DR PeptideAtlas; Q7Z591; -.
DR PRIDE; 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 Antibodypedia; 54667; 42 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 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; GTEVHWA; -.
DR PhylomeDB; Q7Z591; -.
DR TreeFam; TF336885; -.
DR PathwayCommons; Q7Z591; -.
DR SignaLink; Q7Z591; -.
DR BioGRID-ORCS; 80709; 7 hits in 1082 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 146 other tissues.
DR Genevisible; Q7Z591; HS.
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 Pfam; PF12443; AKNA; 1.
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
