KANL3_HUMAN
ID KANL3_HUMAN Reviewed; 904 AA.
AC Q9P2N6; A1L184; D3DXH3; D3DXH4; Q05BU4; Q6P3X2; Q6PJH6; Q86T19; Q96L64;
AC Q9H0C9; Q9H8C9; Q9HAP8; Q9NWE5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=KAT8 regulatory NSL complex subunit 3;
DE AltName: Full=NSL complex protein NSL3;
DE AltName: Full=Non-specific lethal 3 homolog;
DE AltName: Full=Serum inhibited-related protein;
DE AltName: Full=Testis development protein PRTD;
GN Name=KANSL3; Synonyms=KIAA1310, NSL3, PRTD, SI1;
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 4).
RA Tan D., Lai J., Yu M., He Y., Qian W., Jiang Y.;
RT "Cloning and characterization of a gene which is inhibited by serum.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RC TISSUE=Testis;
RA Cheng L.J., Li J.M., Sha J.H.;
RT "A novel gene related to testis development (PRTD).";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
RC TISSUE=Embryo, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 75-904 (ISOFORM 1).
RC TISSUE=Duodenum, PNS, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 645-898.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [9]
RP IDENTIFICATION IN THE NSL COMPLEX.
RX PubMed=16543150; DOI=10.1016/j.molcel.2006.02.007;
RA Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M.,
RA Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M.,
RA Stunnenberg H.G., Saumweber H., Akhtar A.;
RT "Nuclear pore components are involved in the transcriptional regulation of
RT dosage compensation in Drosophila.";
RL Mol. Cell 21:811-823(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND SER-540, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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 [13]
RP FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20018852; DOI=10.1074/jbc.c109.087981;
RA Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
RA Washburn M.P., Conaway J.W., Conaway R.C.;
RT "Subunit composition and substrate specificity of a MOF-containing histone
RT acetyltransferase distinct from the male-specific lethal (MSL) complex.";
RL J. Biol. Chem. 285:4268-4272(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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: As part of the NSL complex it is involved in acetylation of
CC nucleosomal histone H4 on several lysine residues and therefore may be
CC involved in the regulation of transcription.
CC {ECO:0000269|PubMed:20018852}.
CC -!- SUBUNIT: Component of the NSL complex at least composed of MOF/KAT8,
CC KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1.
CC {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:20018852}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20018852}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q9P2N6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2N6-2; Sequence=VSP_025333;
CC Name=3;
CC IsoId=Q9P2N6-3; Sequence=VSP_025329;
CC Name=4;
CC IsoId=Q9P2N6-4; Sequence=VSP_025325, VSP_025329;
CC Name=5;
CC IsoId=Q9P2N6-5; Sequence=VSP_025325, VSP_025329, VSP_025332;
CC Name=6;
CC IsoId=Q9P2N6-6; Sequence=VSP_025324, VSP_025326, VSP_025329,
CC VSP_025332;
CC Name=7;
CC IsoId=Q9P2N6-7; Sequence=VSP_025325, VSP_025327, VSP_025328;
CC Name=8;
CC IsoId=Q9P2N6-8; Sequence=VSP_025325, VSP_025329, VSP_025330,
CC VSP_025331;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15469.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI27821.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAA92548.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY050169; AAL13159.1; -; mRNA.
DR EMBL; AF311326; AAG33852.1; -; mRNA.
DR EMBL; AB037731; BAA92548.1; ALT_INIT; mRNA.
DR EMBL; AK000943; BAA91437.1; -; mRNA.
DR EMBL; AK023813; BAB14688.1; -; mRNA.
DR EMBL; AC079754; AAX88890.1; -; Genomic_DNA.
DR EMBL; CH471207; EAW71349.1; -; Genomic_DNA.
DR EMBL; CH471207; EAW71350.1; -; Genomic_DNA.
DR EMBL; CH471207; EAW71352.1; -; Genomic_DNA.
DR EMBL; CH471207; EAW71357.1; -; Genomic_DNA.
DR EMBL; CH471207; EAW71358.1; -; Genomic_DNA.
DR EMBL; BC015469; AAH15469.1; ALT_SEQ; mRNA.
DR EMBL; BC032746; AAH32746.1; -; mRNA.
DR EMBL; BC051763; AAH51763.1; -; mRNA.
DR EMBL; BC063792; AAH63792.1; -; mRNA.
DR EMBL; BC127820; AAI27821.1; ALT_SEQ; mRNA.
DR EMBL; AL136849; CAB66783.2; -; mRNA.
DR CCDS; CCDS46361.1; -. [Q9P2N6-3]
DR RefSeq; NP_001108488.1; NM_001115016.2. [Q9P2N6-3]
DR RefSeq; XP_005264041.1; XM_005263984.1.
DR AlphaFoldDB; Q9P2N6; -.
DR SMR; Q9P2N6; -.
DR BioGRID; 120811; 78.
DR ComplexPortal; CPX-809; NSL histone acetyltransferase complex.
DR CORUM; Q9P2N6; -.
DR IntAct; Q9P2N6; 28.
DR MINT; Q9P2N6; -.
DR STRING; 9606.ENSP00000396749; -.
DR DrugBank; DB03467; Naringenin.
DR ESTHER; human-KANSL3; NLS3-Tex30.
DR GlyConnect; 2906; 1 O-Linked glycan (1 site).
DR GlyGen; Q9P2N6; 9 sites, 1 O-linked glycan (9 sites).
DR iPTMnet; Q9P2N6; -.
DR PhosphoSitePlus; Q9P2N6; -.
DR BioMuta; KANSL3; -.
DR DMDM; 147646907; -.
DR EPD; Q9P2N6; -.
DR jPOST; Q9P2N6; -.
DR MassIVE; Q9P2N6; -.
DR MaxQB; Q9P2N6; -.
DR PaxDb; Q9P2N6; -.
DR PeptideAtlas; Q9P2N6; -.
DR PRIDE; Q9P2N6; -.
DR ProteomicsDB; 83859; -. [Q9P2N6-1]
DR ProteomicsDB; 83860; -. [Q9P2N6-2]
DR ProteomicsDB; 83861; -. [Q9P2N6-3]
DR ProteomicsDB; 83862; -. [Q9P2N6-4]
DR ProteomicsDB; 83863; -. [Q9P2N6-5]
DR ProteomicsDB; 83864; -. [Q9P2N6-6]
DR ProteomicsDB; 83865; -. [Q9P2N6-7]
DR ProteomicsDB; 83866; -. [Q9P2N6-8]
DR Antibodypedia; 32468; 119 antibodies from 21 providers.
DR DNASU; 55683; -.
DR Ensembl; ENST00000420155.5; ENSP00000414426.1; ENSG00000114982.19. [Q9P2N6-2]
DR Ensembl; ENST00000431828.6; ENSP00000396749.1; ENSG00000114982.19. [Q9P2N6-3]
DR Ensembl; ENST00000666923.1; ENSP00000499674.1; ENSG00000114982.19. [Q9P2N6-1]
DR GeneID; 55683; -.
DR KEGG; hsa:55683; -.
DR MANE-Select; ENST00000431828.6; ENSP00000396749.1; NM_001115016.3; NP_001108488.1. [Q9P2N6-3]
DR UCSC; uc002swn.6; human. [Q9P2N6-1]
DR CTD; 55683; -.
DR DisGeNET; 55683; -.
DR GeneCards; KANSL3; -.
DR HGNC; HGNC:25473; KANSL3.
DR HPA; ENSG00000114982; Low tissue specificity.
DR MIM; 617742; gene.
DR neXtProt; NX_Q9P2N6; -.
DR OpenTargets; ENSG00000114982; -.
DR PharmGKB; PA162393058; -.
DR VEuPathDB; HostDB:ENSG00000114982; -.
DR eggNOG; KOG3253; Eukaryota.
DR GeneTree; ENSGT00390000007636; -.
DR HOGENOM; CLU_009783_0_0_1; -.
DR InParanoid; Q9P2N6; -.
DR OMA; GADDNLX; -.
DR OrthoDB; 316190at2759; -.
DR PhylomeDB; Q9P2N6; -.
DR TreeFam; TF323466; -.
DR PathwayCommons; Q9P2N6; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9P2N6; -.
DR SIGNOR; Q9P2N6; -.
DR BioGRID-ORCS; 55683; 652 hits in 1078 CRISPR screens.
DR ChiTaRS; KANSL3; human.
DR GeneWiki; FLJ10081; -.
DR GenomeRNAi; 55683; -.
DR Pharos; Q9P2N6; Tbio.
DR PRO; PR:Q9P2N6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9P2N6; protein.
DR Bgee; ENSG00000114982; Expressed in sperm and 186 other tissues.
DR ExpressionAtlas; Q9P2N6; baseline and differential.
DR Genevisible; Q9P2N6; HS.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0044545; C:NSL complex; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR026555; NSL3/Tex30.
DR PANTHER; PTHR13136; PTHR13136; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..904
FT /note="KAT8 regulatory NSL complex subunit 3"
FT /id="PRO_0000416242"
FT REGION 476..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2RSY1"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025324"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 4, isoform 5, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_025325"
FT VAR_SEQ 113..129
FT /note="DADAPPPPEDWEEHVNR -> MTLPHCHRLMLTHHLFW (in isoform
FT 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025326"
FT VAR_SEQ 222..228
FT /note="IPTLIDR -> VILTFCG (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025327"
FT VAR_SEQ 229..904
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025328"
FT VAR_SEQ 581..606
FT /note="Missing (in isoform 3, isoform 4, isoform 5, isoform
FT 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_025329"
FT VAR_SEQ 637..643
FT /note="GSKTSKR -> VYSWFHH (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025330"
FT VAR_SEQ 644..904
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025331"
FT VAR_SEQ 671..672
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_025332"
FT VAR_SEQ 781..904
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_025333"
FT VARIANT 707
FT /note="V -> I (in dbSNP:rs34406082)"
FT /id="VAR_032268"
FT CONFLICT 529
FT /note="D -> G (in Ref. 4; BAA91437)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="T -> I (in Ref. 2; AAG33852 and 4; BAB14688)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="P -> S (in Ref. 2; AAG33852 and 4; BAB14688)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="S -> C (in Ref. 2; AAG33852 and 4; BAB14688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 95992 MW; 698DD46EC443B5DD CRC64;
MAHRGGERDF QTSARRMGTS LLFQLSVHER ELDLVFLDHS YAKPWSAHPD ASSARPTRML
FVTPRRQHES TIESDVPIDV ETVTSTPMPL YDNQKARSVM NECERHVIFA RTDADAPPPP
EDWEEHVNRT GWTMAQNKLF NKILKALQSD RLARLANEGA CNEPVLRRVA VDKCARRVRQ
ALASVSWDTK LIQWLHTTLV ETLSLPMLAA YLDALQTLKG KIPTLIDRML VSSNTKTGAA
GAEALSLLLK RPWDPAVGVL SHNKPSKLPG SPLILIASSG PSSSVFPTSR RHRFWQSQLS
CLGKVIPVAT HLLNNGSGVG VLQCLEHMIG AVRSKVLEIH SHFPHKPIIL IGWNTGALVA
CHVSVMEYVT AVVCLGFPLL TVDGPRGDVD DPLLDMKTPV LFVIGQNSLQ CHPEAMEDFR
EKIRAENSLV VVGGADDNLR ISKAKKKSEG LTQSMVDRCI QDEIVDFLTG VLTRAEGHMG
SEPRDQDAEK KKKPRDVARR DLAFEVPERG SRPASPAAKL PASPSGSEDL SSVSSSPTSS
PKTKVTTVTS AQKSSQIGSS QLLKRHVQRT EAVLTHKQAQ AQFAAFLKQN MLVRKALPPG
TSSCLFVPIS SEPPEEGEKE DLRVQLKRHH PSSPLPGSKT SKRPKIKVSL ISQGDTAGGP
CAPSQGSAPE AAGGKPITMT LGQASAGAKE LTGLLTTAKS SSSEGGVSAS PVPSVVSSST
APSALHTLQS RLVATSPGSS LPGATSASSL LQGLSFSLQD ISSKTSGLPA NPSPGPAPQA
TSVKLPTPMQ SLGAITTGTS TIVRTIPVAT TLSSLGATPG GKPTAIHQLL TNGGLAKLAS
SLPGLAQISN QASGLKVPTT ITLTLRGQPS RITTLSPMGS GAAPSEESSS QVLPSSSQRL
PPAP
