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 24-JAN-2024, entry version 160. 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}; 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; 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; 108. DR CORUM; Q5T1M5; -. DR IntAct; Q5T1M5; 33. DR MINT; Q5T1M5; -. DR STRING; 9606.ENSP00000416158; -. DR CarbonylDB; Q5T1M5; -. DR GlyCosmos; Q5T1M5; 1 site, 1 glycan. DR GlyGen; Q5T1M5; 5 sites, 1 O-linked glycan (5 sites). 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; 9606-ENSP00000238256; -. DR PeptideAtlas; Q5T1M5; -. DR ProteomicsDB; 64271; -. [Q5T1M5-1] DR ProteomicsDB; 64272; -. [Q5T1M5-2] DR ProteomicsDB; 64273; -. [Q5T1M5-3] DR Pumba; Q5T1M5; -. DR Antibodypedia; 1961; 112 antibodies from 22 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 AGR; HGNC:23397; -. 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; VALKAHY; -. DR OrthoDB; 3152232at2759; -. DR PhylomeDB; Q5T1M5; -. DR TreeFam; TF328592; -. DR PathwayCommons; Q5T1M5; -. DR SignaLink; Q5T1M5; -. DR SIGNOR; Q5T1M5; -. DR BioGRID-ORCS; 23307; 14 hits in 1095 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 212 other cell types or 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 PANTHER; PTHR44927; FK506-BINDING PROTEIN 15; 1. DR PANTHER; PTHR44927:SF1; FK506-BINDING PROTEIN 15; 1. DR Pfam; PF00254; FKBP_C; 1. DR SUPFAM; SSF54534; FKBP-like; 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 //