ID PBX2_HUMAN Reviewed; 430 AA. AC P40425; A2BFJ2; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 04-NOV-2026, entry version 216. DE RecName: Full=Pre-B-cell leukemia transcription factor 2; DE AltName: Full=Homeobox protein PBX2; DE AltName: Full=Protein G17; GN Name=PBX2; Synonyms=G17; 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]. RX PubMed=1682799; DOI=10.1128/mcb.11.12.6149-6157.1991; RA Monica K., Galili N., Nourse J., Saltman D., Cleary M.L.; RT "PBX2 and PBX3, new homeobox genes with extensive homology to the human RT proto-oncogene PBX1."; RL Mol. Cell. Biol. 11:6149-6157(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7759099; DOI=10.1016/0888-7543(95)80007-9; RA Aguado B., Campbell R.D.; RT "The novel gene G17, located in the human major histocompatibility complex, RT encodes PBX2, a homeodomain-containing protein."; RL Genomics 25:650-659(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7835890; DOI=10.1006/geno.1994.1517; RA Sugaya K., Fukagawa T., Matsumoto K., Mita K., Takahashi E., Ando A., RA Inoko H., Ikemura T.; RT "Three genes in the human MHC class III region near the junction with the RT class II: gene for receptor of advanced glycosylation end products, PBX2 RT homeobox gene and a notch homolog, human counterpart of mouse mammary tumor RT gene int-3."; RL Genomics 23:408-419(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14656967; DOI=10.1101/gr.1736803; RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., RA Hood L.; RT "Analysis of the gene-dense major histocompatibility complex class III RT region and its comparison to mouse."; RL Genome Res. 13:2621-2636(2003). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 CHARACTERIZATION. RX PubMed=7910944; DOI=10.1128/mcb.14.6.3938-3948.1994; RA Lu Q., Wright D.D., Kamps M.P.; RT "Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive RT transcriptional activator in human leukemias carrying the t(1;19) RT translocation."; RL Mol. Cell. Biol. 14:3938-3948(1994). RN [9] RP INTERACTION WITH PBXIP1. RX PubMed=10825160; DOI=10.1074/jbc.m001323200; RA Abramovich C., Shen W.-F., Pineault N., Imren S., Montpetit B., Largman C., RA Humphries R.K.; RT "Functional cloning and characterization of a novel nonhomeodomain protein RT that inhibits the binding of PBX1-HOX complexes to DNA."; RL J. Biol. Chem. 275:26172-26177(2000). RN [10] RP FUNCTION, AND INTERACTION WITH MEIS1. RX PubMed=12609849; DOI=10.1182/blood-2002-02-0380; RA Okada Y., Nagai R., Sato T., Matsuura E., Minami T., Morita I., Doi T.; RT "Homeodomain proteins MEIS1 and PBXs regulate the lineage-specific RT transcription of the platelet factor 4 gene."; RL Blood 101:4748-4756(2003). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-330, 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, 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 [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-151 AND SER-330, AND RP IDENTIFICATION BY 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). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY RP 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). CC -!- FUNCTION: Transcriptional activator that binds the sequence 5'- CC ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1. CC {ECO:0000269|PubMed:12609849}. CC -!- SUBUNIT: Forms heterodimers with MEIS1 and heterotrimers with MEIS1 and CC HOXA9. Interacts with PBXIP1. {ECO:0000269|PubMed:10825160, CC ECO:0000269|PubMed:12609849}. CC -!- INTERACTION: CC P40425; Q13515: BFSP2; NbExp=3; IntAct=EBI-348489, EBI-10229433; CC P40425; Q8TDH9: BLOC1S5; NbExp=3; IntAct=EBI-348489, EBI-465861; CC P40425; Q5PSV4: BRMS1L; NbExp=3; IntAct=EBI-348489, EBI-5666615; CC P40425; Q9H257: CARD9; NbExp=3; IntAct=EBI-348489, EBI-751319; CC P40425; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-348489, EBI-5278764; CC P40425; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-348489, EBI-743105; CC P40425; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-348489, EBI-6658203; CC P40425; P49639: HOXA1; NbExp=3; IntAct=EBI-348489, EBI-740785; CC P40425; P20719: HOXA5; NbExp=5; IntAct=EBI-348489, EBI-8470697; CC P40425; P09067: HOXB5; NbExp=3; IntAct=EBI-348489, EBI-3893317; CC P40425; Q00444: HOXC5; NbExp=3; IntAct=EBI-348489, EBI-11955357; CC P40425; P31273: HOXC8; NbExp=3; IntAct=EBI-348489, EBI-1752118; CC P40425; P31274: HOXC9; NbExp=3; IntAct=EBI-348489, EBI-1779423; CC P40425; Q13394: MAB21L1; NbExp=3; IntAct=EBI-348489, EBI-10229059; CC P40425; O60682: MSC; NbExp=3; IntAct=EBI-348489, EBI-740310; CC P40425; P55347: PKNOX1; NbExp=4; IntAct=EBI-348489, EBI-1373569; CC P40425; Q86W92: PPFIBP1; NbExp=3; IntAct=EBI-348489, EBI-1045582; CC P40425; Q5TAB7: RIPPLY2; NbExp=5; IntAct=EBI-348489, EBI-10246897; CC P40425; P31314: TLX1; NbExp=3; IntAct=EBI-348489, EBI-2820655; CC P40425; Q504Y3: ZCWPW2; NbExp=3; IntAct=EBI-348489, EBI-12274792; CC P40425; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-348489, EBI-6427977; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC -!- SIMILARITY: Belongs to the TALE/PBX homeobox family. {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; X59842; CAA42503.1; -; mRNA. DR EMBL; X80700; CAA56717.1; -; Genomic_DNA. DR EMBL; D28769; BAA05957.1; -; Genomic_DNA. DR EMBL; U89336; AAB47490.1; -; Genomic_DNA. DR EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662830; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL845464; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX284686; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927239; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR933878; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR812478; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03613.1; -; Genomic_DNA. DR EMBL; BC082261; AAH82261.1; -; mRNA. DR CCDS; CCDS4748.1; -. DR PIR; A56002; A56002. DR RefSeq; NP_002577.2; NM_002586.5. DR AlphaFoldDB; P40425; -. DR SMR; P40425; -. DR BioGRID; 111122; 74. DR CORUM; P40425; -. DR FunCoup; P40425; 2745. DR IntAct; P40425; 74. DR NDEx; MUSIC2-C5266-PBX2; Osteosarcoma (U2OS) cell map - Ribosome biogenesis and RNA processing (12 proteins). DR STRING; 9606.ENSP00000364190; -. DR GlyCosmos; P40425; 5 sites, 1 glycan. DR GlyGen; P40425; 5 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P40425; -. DR MetOSite; P40425; -. DR PhosphoSitePlus; P40425; -. DR BioMuta; PBX2; -. DR DMDM; 1352729; -. DR jPOST; P40425; -. DR MassIVE; P40425; -. DR PaxDb; 9606-ENSP00000364190; -. DR PeptideAtlas; P40425; -. DR ProteomicsDB; 55369; -. DR Pumba; P40425; -. DR Antibodypedia; 28518; 233 antibodies from 28 providers. DR DNASU; 5089; -. DR Ensembl; ENST00000375050.6; ENSP00000364190.3; ENSG00000204304.12. DR Ensembl; ENST00000383270.4; ENSP00000372757.4; ENSG00000206315.9. DR Ensembl; ENST00000420432.2; ENSP00000410710.2; ENSG00000236353.7. DR Ensembl; ENST00000431537.2; ENSP00000390009.2; ENSG00000232005.7. DR Ensembl; ENST00000433552.2; ENSP00000391745.2; ENSG00000224952.7. DR Ensembl; ENST00000453487.2; ENSP00000403948.2; ENSG00000225987.7. DR Ensembl; ENST00000453961.2; ENSP00000397177.2; ENSG00000237344.7. DR GeneID; 5089; -. DR KEGG; hsa:5089; -. DR MANE-Select; ENST00000375050.6; ENSP00000364190.3; NM_002586.5; NP_002577.2. DR UCSC; uc003oav.2; human. DR AGR; HGNC:8633; -. DR ClinPGx; PA32971; -. DR CTD; 5089; -. DR DisGeNET; 5089; -. DR GeneCards; PBX2; -. DR HGNC; HGNC:8633; PBX2. DR HPA; ENSG00000204304; Low tissue specificity. DR MIM; 176311; gene. DR OpenTargets; ENSG00000204304; -. DR VEuPathDB; HostDB:ENSG00000204304; -. DR eggNOG; KOG0774; Eukaryota. DR GeneTree; ENSGT00940000160293; -. DR HOGENOM; CLU_041153_0_0_1; -. DR InParanoid; P40425; -. DR OMA; AGWMPQR; -. DR OrthoDB; 4187154at2759; -. DR PAN-GO; P40425; 9 GO annotations based on evolutionary models. DR PhylomeDB; P40425; -. DR PathwayCommons; P40425; -. DR SignaLink; P40425; -. DR SIGNOR; P40425; -. DR Agora; ENSG00000204304; -. DR BioGRID-ORCS; 5089; 28 hits in 1172 CRISPR screens. DR ChiTaRS; PBX2; human. DR GeneWiki; PBX2; -. DR GenomeRNAi; 5089; -. DR Pharos; P40425; Tbio. DR PRO; PR:P40425; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P40425; protein. DR Bgee; ENSG00000204304; Expressed in right lobe of thyroid gland and 98 other cell types or tissues. DR ExpressionAtlas; P40425; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central. DR GO; GO:0007420; P:brain development; IBA:GO_Central. DR GO; GO:0048568; P:embryonic organ development; IBA:GO_Central. DR GO; GO:0001654; P:eye development; IBA:GO_Central. DR GO; GO:0048666; P:neuron development; IBA:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR CDD; cd00086; homeodomain; 1. DR FunFam; 1.10.10.60:FF:000008; Pre-B-cell leukemia transcription factor 1; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR001356; HD. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR009057; Homeodomain-like_sf. DR InterPro; IPR008422; KN_HD. DR InterPro; IPR005542; PBX_PBC_dom. DR PANTHER; PTHR11850; HOMEOBOX PROTEIN TRANSCRIPTION FACTORS; 1. DR Pfam; PF05920; Homeobox_KN; 1. DR Pfam; PF03792; PBC; 1. DR SMART; SM00389; HOX; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS51978; PBC; 1. PE 1: Evidence at protein level; KW Activator; DNA-binding; Homeobox; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..430 FT /note="Pre-B-cell leukemia transcription factor 2" FT /id="PRO_0000049237" FT DOMAIN 48..243 FT /note="PBC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322" FT DNA_BIND 244..306 FT /note="Homeobox; TALE-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 55..134 FT /note="PBC-A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322" FT REGION 137..243 FT /note="PBC-B" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322" FT REGION 326..347 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 378..430 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 13..48 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 380..392 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 403..418 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 136 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 159 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35984" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35984" FT CONFLICT 393 FT /note="M -> I (in Ref. 1; CAA42503)" FT /evidence="ECO:0000305" SQ SEQUENCE 430 AA; 45881 MW; EF2FFA158C4DAF68 CRC64; MDERLLGPPP PGGGRGGLGL VSGEPGGPGE PPGGGDPGGG SGGVPGGRGK QDIGDILQQI MTITDQSLDE AQAKKHALNC HRMKPALFSV LCEIKEKTGL SIRSSQEEEP VDPQLMRLDN MLLAEGVAGP EKGGGSAAAA AAAAASGGGV SPDNSIEHSD YRSKLAQIRH IYHSELEKYE QACNEFTTHV MNLLREQSRT RPVAPKEMER MVSIIHRKFS AIQMQLKQST CEAVMILRSR FLDARRKRRN FSKQATEVLN EYFYSHLSNP YPSEEAKEEL AKKCGITVSQ VSNWFGNKRI RYKKNIGKFQ EEANIYAVKT AVSVTQGGHS RTSSPTPPSS AGSGGSFNLS GSGDMFLGMP GLNGDSYSAS QVESLRHSMG PGGYGDNLGG GQMYSPREMR ANGSWQEAVT PSSVTSPTEG PGSVHSDTSN //