FKB15_HUMAN
ID FKB15_HUMAN Reviewed; 1219 AA.
AC Q5T1M5; Q05DK8; Q5T1M2; Q6DD85; Q9Y4D0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=FK506-binding protein 15;
DE Short=FKBP-15;
DE AltName: Full=133 kDa FK506-binding protein;
DE Short=133 kDa FKBP;
DE Short=FKBP-133;
DE AltName: Full=WASP- and FKBP-like protein;
DE Short=WAFL;
GN Name=FKBP15; Synonyms=KIAA0674;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-413.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 548-1219 (ISOFORM 2), AND VARIANT GLN-413.
RC TISSUE=Eye, and Prostate;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-956, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161 AND SER-1162, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-356; SER-939;
RP SER-940; SER-941; SER-956; SER-979; SER-1114 AND SER-1164, 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ACTIN AND WIP.
RX PubMed=19121306; DOI=10.1016/j.yexcr.2008.12.004;
RA Viklund I.-M., Aspenstroem P., Meas-Yedid V., Zhang B., Kopec J., Agren D.,
RA Schneider G., D'Amato M., Olivo-Marin J.-C., Sansonetti P., Van Nhieu G.T.,
RA Pettersson S.;
RT "WAFL, a new protein involved in regulation of early endocytic transport at
RT the intersection of actin and microtubule dynamics.";
RL Exp. Cell Res. 315:1040-1052(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-356; SER-1114;
RP SER-1164; SER-1195 AND THR-1203, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-14; SER-956; SER-1114 AND SER-1164, 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1164, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; SER-346; SER-356;
RP SER-956; SER-1114; SER-1162 AND SER-1164, AND IDENTIFICATION BY MASS
RP 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).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-956; SER-979;
RP SER-1024; SER-1061; SER-1065; SER-1097; THR-1099; SER-1114 AND SER-1158,
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP INTERACTION WITH TBC1D23.
RX PubMed=29084197; DOI=10.1038/ncb3627;
RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT the trans-Golgi.";
RL Nat. Cell Biol. 19:1424-1432(2017).
CC -!- FUNCTION: May be involved in the cytoskeletal organization of neuronal
CC growth cones. Seems to be inactive as a PPIase (By similarity).
CC Involved in the transport of early endosomes at the level of transition
CC between microfilament-based and microtubule-based movement.
CC {ECO:0000250, ECO:0000269|PubMed:19121306}.
CC -!- SUBUNIT: Interacts with WIP and actin (PubMed:19121306). Interacts with
CC TBC1D23 (PubMed:29084197). {ECO:0000269|PubMed:19121306,
CC ECO:0000269|PubMed:29084197}.
CC -!- INTERACTION:
CC Q5T1M5; Q9QZ88: Vps29; Xeno; NbExp=7; IntAct=EBI-5235934, EBI-8334188;
CC Q5T1M5; Q9EQH3: Vps35; Xeno; NbExp=3; IntAct=EBI-5235934, EBI-775825;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6P9Q6}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q6P9Q6}. Early endosome
CC {ECO:0000269|PubMed:19121306}. Note=Present in axons and neuronal
CC growth cones. {ECO:0000250|UniProtKB:Q6P9Q6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5T1M5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T1M5-2; Sequence=VSP_027758;
CC Name=3;
CC IsoId=Q5T1M5-3; Sequence=VSP_027756, VSP_027757;
CC -!- DOMAIN: The PPIase FKBP-type domain seems to be inactive both for
CC FK506-binding and enzymatic activity. {ECO:0000250}.
CC -!- DOMAIN: The central coiled-coil region is responsible for association
CC with early endosomes.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA31649.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB014574; BAA31649.1; ALT_INIT; mRNA.
DR EMBL; AL449105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009609; AAH09609.1; ALT_INIT; mRNA.
DR EMBL; BC077732; AAH77732.1; -; mRNA.
DR CCDS; CCDS48007.1; -. [Q5T1M5-1]
DR PIR; T00363; T00363.
DR RefSeq; NP_056073.1; NM_015258.1. [Q5T1M5-1]
DR RefSeq; XP_006717081.1; XM_006717018.2. [Q5T1M5-2]
DR AlphaFoldDB; Q5T1M5; -.
DR SMR; Q5T1M5; -.
DR BioGRID; 116899; 82.
DR CORUM; Q5T1M5; -.
DR IntAct; Q5T1M5; 32.
DR MINT; Q5T1M5; -.
DR STRING; 9606.ENSP00000238256; -.
DR CarbonylDB; Q5T1M5; -.
DR GlyGen; Q5T1M5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5T1M5; -.
DR MetOSite; Q5T1M5; -.
DR PhosphoSitePlus; Q5T1M5; -.
DR BioMuta; FKBP15; -.
DR DMDM; 158563913; -.
DR EPD; Q5T1M5; -.
DR jPOST; Q5T1M5; -.
DR MassIVE; Q5T1M5; -.
DR MaxQB; Q5T1M5; -.
DR PaxDb; Q5T1M5; -.
DR PeptideAtlas; Q5T1M5; -.
DR PRIDE; Q5T1M5; -.
DR ProteomicsDB; 64271; -. [Q5T1M5-1]
DR ProteomicsDB; 64272; -. [Q5T1M5-2]
DR ProteomicsDB; 64273; -. [Q5T1M5-3]
DR Antibodypedia; 1961; 101 antibodies from 21 providers.
DR DNASU; 23307; -.
DR Ensembl; ENST00000238256.8; ENSP00000238256.3; ENSG00000119321.10. [Q5T1M5-1]
DR Ensembl; ENST00000414250.2; ENSP00000415733.2; ENSG00000119321.10. [Q5T1M5-3]
DR Ensembl; ENST00000446284.6; ENSP00000416158.2; ENSG00000119321.10. [Q5T1M5-1]
DR GeneID; 23307; -.
DR KEGG; hsa:23307; -.
DR MANE-Select; ENST00000238256.8; ENSP00000238256.3; NM_015258.2; NP_056073.1.
DR UCSC; uc004bgs.3; human. [Q5T1M5-1]
DR CTD; 23307; -.
DR DisGeNET; 23307; -.
DR GeneCards; FKBP15; -.
DR HGNC; HGNC:23397; FKBP15.
DR HPA; ENSG00000119321; Low tissue specificity.
DR MIM; 617398; gene.
DR neXtProt; NX_Q5T1M5; -.
DR OpenTargets; ENSG00000119321; -.
DR PharmGKB; PA162388608; -.
DR VEuPathDB; HostDB:ENSG00000119321; -.
DR eggNOG; KOG0552; Eukaryota.
DR eggNOG; KOG4725; Eukaryota.
DR GeneTree; ENSGT00530000064286; -.
DR HOGENOM; CLU_007194_1_0_1; -.
DR InParanoid; Q5T1M5; -.
DR OMA; NQHEREK; -.
DR OrthoDB; 936280at2759; -.
DR PhylomeDB; Q5T1M5; -.
DR TreeFam; TF328592; -.
DR PathwayCommons; Q5T1M5; -.
DR SignaLink; Q5T1M5; -.
DR SIGNOR; Q5T1M5; -.
DR BioGRID-ORCS; 23307; 13 hits in 1035 CRISPR screens.
DR ChiTaRS; FKBP15; human.
DR GenomeRNAi; 23307; -.
DR Pharos; Q5T1M5; Tbio.
DR PRO; PR:Q5T1M5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5T1M5; protein.
DR Bgee; ENSG00000119321; Expressed in monocyte and 210 other tissues.
DR Genevisible; Q5T1M5; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell projection;
KW Coiled coil; Cytoplasm; Endocytosis; Endosome; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..1219
FT /note="FK506-binding protein 15"
FT /id="PRO_0000299556"
FT DOMAIN 197..290
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 41..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..169
FT /note="Important for function in growth cone organization"
FT /evidence="ECO:0000250"
FT REGION 294..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 522..789
FT /evidence="ECO:0000255"
FT COILED 818..878
FT /evidence="ECO:0000255"
FT COILED 925..951
FT /evidence="ECO:0000255"
FT COMPBIAS 46..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9Q6"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9Q6"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9Q6"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 956
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1024
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9Q6"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1099
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1203
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 462..472
FT /note="PYAGMQAYAYP -> VTFYNRINYIL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027756"
FT VAR_SEQ 473..1219
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027757"
FT VAR_SEQ 629..638
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027758"
FT VARIANT 106
FT /note="A -> T (in dbSNP:rs1133618)"
FT /id="VAR_034851"
FT VARIANT 413
FT /note="H -> Q (in dbSNP:rs10435864)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_034852"
FT VARIANT 434
FT /note="L -> F (in dbSNP:rs10465129)"
FT /id="VAR_034853"
FT VARIANT 847
FT /note="A -> S (in dbSNP:rs1128116)"
FT /id="VAR_061543"
FT VARIANT 993
FT /note="P -> T (in dbSNP:rs57348436)"
FT /id="VAR_061544"
SQ SEQUENCE 1219 AA; 133630 MW; 86563D82B540B51D CRC64;
MFGAGDEDDT DFLSPSGGAR LASLFGLDQA AAGHGNEFFQ YTAPKQPKKG QGTAATGNQA
TPKTAPATMS TPTILVATAV HAYRYTNGQY VKQGKFGAAV LGNHTAREYR ILLYISQQQP
VTVARIHVNF ELMVRPNNYS TFYDDQRQNW SIMFESEKAA VEFNKQVCIA KCNSTSSLDA
VLSQDLIVAD GPAVEVGDSL EVAYTGWLFQ NHVLGQVFDS TANKDKLLRL KLGSGKVIKG
WEDGMLGMKK GGKRLLIVPP ACAVGSEGVI GWTQATDSIL VFEVEVRRVK FARDSGSDGH
SVSSRDSAAP SPIPGADNLS ADPVVSPPTS IPFKSGEPAL RTKSNSLSEQ LAINTSPDAV
KAKLISRMAK MGQPMLPILP PQLDSNDSEI EDVNTLQGGG QPVVTPSVQP SLHPAHPALP
QMTSQAPQPS VTGLQAPSAA LMQVSSLDSH SAVSGNAQSF QPYAGMQAYA YPQASAVTSQ
LQPVRPLYPA PLSQPPHFQG SGDMASFLMT EARQHNTEIR MAVSKVADKM DHLMTKVEEL
QKHSAGNSML IPSMSVTMET SMIMSNIQRI IQENERLKQE ILEKSNRIEE QNDKISELIE
RNQRYVEQSN LMMEKRNNSL QTATENTQAR VLHAEQEKAK VTEELAAATA QVSHLQLKMT
AHQKKETELQ MQLTESLKET DLLRGQLTKV QAKLSELQET SEQAQSKFKS EKQNRKQLEL
KVTSLEEELT DLRVEKESLE KNLSERKKKS AQERSQAEEE IDEIRKSYQE ELDKLRQLLK
KTRVSTDQAA AEQLSLVQAE LQTQWEAKCE HLLASAKDEH LQQYQEVCAQ RDAYQQKLVQ
LQEKCLALQA QITALTKQNE QHIKELEKNK SQMSGVEAAA SDPSEKVKKI MNQVFQSLRR
EFELEESYNG RTILGTIMNT IKMVTLQLLN QQEQEKEESS SEEEEEKAEE RPRRPSQEQS
ASASSGQPQA PLNRERPESP MVPSEQVVEE AVPLPPQALT TSQDGHRRKG DSEAEALSEI
KDGSLPPELS CIPSHRVLGP PTSIPPEPLG PVSMDSECEE SLAASPMAAK PDNPSGKVCV
REVAPDGPLQ ESSTRLSLTS DPEEGDPLAL GPESPGEPQP PQLKKDDVTS STGPHKELSS
TEAGSTVAGA ALRPSHHSQR SSLSGDEEDE LFKGATLKAL RPKAQPEEED EDEVSMKGRP
PPTPLFGDDD DDDDIDWLG
