ID   BTF3_HUMAN              Reviewed;         206 AA.
AC   P20290; A8K510; Q13893; Q76M56;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   28-JAN-2026, entry version 206.
DE   RecName: Full=Transcription factor BTF3;
DE   AltName: Full=Nascent polypeptide-associated complex subunit beta;
DE            Short=NAC-beta;
DE   AltName: Full=RNA polymerase B transcription factor 3;
GN   Name=BTF3; Synonyms=NACB; ORFNames=OK/SW-cl.8;
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 AND 2).
RX   PubMed=2320128; DOI=10.1038/344556a0;
RA   Zheng X.M., Black D., Chambon P., Egly J.-M.;
RT   "Sequencing and expression of complementary DNA for the general
RT   transcription factor BTF3.";
RL   Nature 344:556-559(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leukocyte;
RX   PubMed=1386332; DOI=10.1016/0378-1119(92)90732-5;
RA   Kanno M., Chalut C., Egly J.-M.;
RT   "Genomic structure of the putative BTF3 transcription factor.";
RL   Gene 117:219-228(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Leffers H., Honore B., Madsen A., Nielsen M.S., Anderson A.H., Celis J.E.;
RT   "cDNA expression and human 2D-gel data bases: towards integrating protein
RT   and DNA information.";
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon adenocarcinoma;
RA   Shichijo S., Itoh K.;
RT   "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT   CTL generated from TIL of colon cancer patients.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Skin;
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   [9]
RP   FUNCTION, INTERACTION WITH NACA, ASSOCIATION WITH RIBOSOMES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=10982809; DOI=10.1074/jbc.m006368200;
RA   Beatrix B., Sakai H., Wiedmann M.;
RT   "The alpha and beta subunit of the nascent polypeptide-associated complex
RT   have distinct functions.";
RL   J. Biol. Chem. 275:37838-37845(2000).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP   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   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-173, 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, 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).
RN   [14]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-19; LYS-46 AND LYS-54, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [15]
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   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 97-154, AND SUBUNIT.
RX   PubMed=21203952; DOI=10.1007/s13238-010-0049-3;
RA   Wang L., Zhang W., Wang L., Zhang X.C., Li X., Rao Z.;
RT   "Crystal structures of NAC domains of human nascent polypeptide-associated
RT   complex (NAC) and its alphaNAC subunit.";
RL   Protein Cell 1:406-416(2010).
CC   -!- FUNCTION: When associated with NACA, prevents inappropriate targeting
CC       of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds
CC       to nascent polypeptide chains as they emerge from the ribosome and
CC       blocks their interaction with the signal recognition particle (SRP),
CC       which normally targets nascent secretory peptides to the ER. BTF3 is
CC       also a general transcription factor that can form a stable complex with
CC       RNA polymerase II. Required for the initiation of transcription.
CC       {ECO:0000269|PubMed:10982809}.
CC   -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC       which is a heterodimer of NACA and BTF3 (via NAC-A/B domains). NAC
CC       associates with ribosomes through the BTF3/NACB subunit. Both subunits
CC       can contact nascent polypeptide chains. {ECO:0000269|PubMed:21203952}.
CC   -!- INTERACTION:
CC       P20290; Q86VG3: IFTAP; NbExp=4; IntAct=EBI-1054687, EBI-3923037;
CC       P20290; P40222: TXLNA; NbExp=4; IntAct=EBI-1054687, EBI-359793;
CC       P20290; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-1054687, EBI-6116822;
CC       P20290-2; P03372: ESR1; NbExp=5; IntAct=EBI-1054703, EBI-78473;
CC       P20290-2; Q86UY6: NAA40; NbExp=3; IntAct=EBI-1054703, EBI-16356946;
CC       P20290-2; O60551: NMT2; NbExp=3; IntAct=EBI-1054703, EBI-3920273;
CC       P20290-2; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-1054703, EBI-17490746;
CC       P20290-2; Q9NRG4: SMYD2; NbExp=3; IntAct=EBI-1054703, EBI-1055671;
CC       P20290-2; P38879: EGD2; Xeno; NbExp=3; IntAct=EBI-1054703, EBI-6379;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10982809}. Nucleus
CC       {ECO:0000269|PubMed:10982809}. Note=The heterodimer with NACA is
CC       cytoplasmic.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=BTF3a;
CC         IsoId=P20290-1; Sequence=Displayed;
CC       Name=2; Synonyms=BTF3b;
CC         IsoId=P20290-2; Sequence=VSP_013587;
CC   -!- SIMILARITY: Belongs to the NAC-beta family. {ECO:0000305}.
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DR   EMBL; X53280; CAA37375.1; -; mRNA.
DR   EMBL; X53281; CAA37376.1; -; mRNA.
DR   EMBL; M90357; AAA58398.1; -; Genomic_DNA.
DR   EMBL; M90352; AAA58398.1; JOINED; Genomic_DNA.
DR   EMBL; X74070; CAA52200.1; -; mRNA.
DR   EMBL; AB062126; BAB93458.1; -; mRNA.
DR   EMBL; BT007120; AAP35784.1; -; mRNA.
DR   EMBL; AK291125; BAF83814.1; -; mRNA.
DR   EMBL; CH471084; EAW95727.1; -; Genomic_DNA.
DR   EMBL; BC008062; AAH08062.1; -; mRNA.
DR   CCDS; CCDS34185.1; -. [P20290-1]
DR   CCDS; CCDS4019.1; -. [P20290-2]
DR   PIR; JC1235; JC1235.
DR   RefSeq; NP_001032726.1; NM_001037637.2. [P20290-1]
DR   RefSeq; NP_001198.2; NM_001207.4. [P20290-2]
DR   PDB; 3LKX; X-ray; 2.50 A; A=97-162.
DR   PDB; 3MCB; X-ray; 1.90 A; B=97-154.
DR   PDB; 7QWQ; EM; 2.83 A; u=45-206.
DR   PDB; 7QWR; EM; 2.90 A; u=45-206.
DR   PDB; 9F1B; EM; 3.01 A; Cu=45-206.
DR   PDB; 9F1C; EM; 3.78 A; Cu=45-206.
DR   PDB; 9F1D; EM; 3.26 A; Cu=45-206.
DR   PDB; 9FQ0; EM; 4.67 A; D=1-206.
DR   PDB; 9MR4; EM; 2.65 A; EF=45-206.
DR   PDB; 9NDP; EM; 2.82 A; EF=45-206.
DR   PDB; 9QQA; EM; 2.80 A; Nu=45-206.
DR   PDB; 9QQB; EM; 3.43 A; Nu=45-206.
DR   PDBsum; 3LKX; -.
DR   PDBsum; 3MCB; -.
DR   PDBsum; 7QWQ; -.
DR   PDBsum; 7QWR; -.
DR   PDBsum; 9F1B; -.
DR   PDBsum; 9F1C; -.
DR   PDBsum; 9F1D; -.
DR   PDBsum; 9FQ0; -.
DR   PDBsum; 9MR4; -.
DR   PDBsum; 9NDP; -.
DR   PDBsum; 9QQA; -.
DR   PDBsum; 9QQB; -.
DR   AlphaFoldDB; P20290; -.
DR   EMDB; EMD-14191; -.
DR   EMDB; EMD-14192; -.
DR   EMDB; EMD-48552; -.
DR   EMDB; EMD-50124; -.
DR   EMDB; EMD-50125; -.
DR   EMDB; EMD-50126; -.
DR   EMDB; EMD-50642; -.
DR   EMDB; EMD-53295; -.
DR   EMDB; EMD-53296; -.
DR   SMR; P20290; -.
DR   BioGRID; 107154; 817.
DR   ComplexPortal; CPX-676; Nascent polypeptide-associated complex.
DR   CORUM; P20290; -.
DR   FunCoup; P20290; 4075.
DR   IntAct; P20290; 104.
DR   MINT; P20290; -.
DR   STRING; 9606.ENSP00000369965; -.
DR   GlyGen; P20290; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P20290; -.
DR   MetOSite; P20290; -.
DR   PhosphoSitePlus; P20290; -.
DR   SwissPalm; P20290; -.
DR   BioMuta; BTF3; -.
DR   DMDM; 115143; -.
DR   jPOST; P20290; -.
DR   MassIVE; P20290; -.
DR   PaxDb; 9606-ENSP00000369965; -.
DR   PeptideAtlas; P20290; -.
DR   ProteomicsDB; 53742; -. [P20290-1]
DR   ProteomicsDB; 53743; -. [P20290-2]
DR   Pumba; P20290; -.
DR   TopDownProteomics; P20290-1; -. [P20290-1]
DR   TopDownProteomics; P20290-2; -. [P20290-2]
DR   Antibodypedia; 4573; 208 antibodies from 30 providers.
DR   DNASU; 689; -.
DR   Ensembl; ENST00000335895.12; ENSP00000338516.8; ENSG00000145741.17. [P20290-2]
DR   Ensembl; ENST00000380591.8; ENSP00000369965.3; ENSG00000145741.17. [P20290-1]
DR   GeneID; 689; -.
DR   KEGG; hsa:689; -.
DR   MANE-Select; ENST00000380591.8; ENSP00000369965.3; NM_001037637.2; NP_001032726.1.
DR   UCSC; uc003kcq.2; human. [P20290-1]
DR   AGR; HGNC:1125; -.
DR   ClinPGx; PA25445; -.
DR   CTD; 689; -.
DR   DisGeNET; 689; -.
DR   GeneCards; BTF3; -.
DR   HGNC; HGNC:1125; BTF3.
DR   HPA; ENSG00000145741; Low tissue specificity.
DR   MIM; 602542; gene.
DR   OpenTargets; ENSG00000145741; -.
DR   VEuPathDB; HostDB:ENSG00000145741; -.
DR   eggNOG; KOG2240; Eukaryota.
DR   GeneTree; ENSGT00940000153288; -.
DR   HOGENOM; CLU_098726_3_0_1; -.
DR   InParanoid; P20290; -.
DR   OMA; AGDTYME; -.
DR   OrthoDB; 9531199at2759; -.
DR   PAN-GO; P20290; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; P20290; -.
DR   PathwayCommons; P20290; -.
DR   SignaLink; P20290; -.
DR   SIGNOR; P20290; -.
DR   Agora; ENSG00000145741; -.
DR   BioGRID-ORCS; 689; 278 hits in 1150 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   ChiTaRS; BTF3; human.
DR   EvolutionaryTrace; P20290; -.
DR   GeneWiki; BTF3; -.
DR   GenomeRNAi; 689; -.
DR   Pharos; P20290; Tbio.
DR   PRO; PR:P20290; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P20290; protein.
DR   Bgee; ENSG00000145741; Expressed in mucosa of sigmoid colon and 211 other cell types or tissues.
DR   ExpressionAtlas; P20290; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005854; C:nascent polypeptide-associated complex; IPI:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:1905551; P:negative regulation of protein localization to endoplasmic reticulum; IDA:ComplexPortal.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd22055; NAC_BTF3; 1.
DR   FunFam; 2.20.70.30:FF:000001; Transcription factor BTF3 homolog; 1.
DR   Gene3D; 2.20.70.30; Nascent polypeptide-associated complex domain; 1.
DR   IDEAL; IID00444; -.
DR   InterPro; IPR039370; BTF3.
DR   InterPro; IPR038187; NAC_A/B_dom_sf.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR   PANTHER; PTHR10351; TRANSCRIPTION FACTOR BTF3 FAMILY MEMBER; 1.
DR   Pfam; PF01849; NAC; 1.
DR   SMART; SM01407; NAC; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chaperone; Cytoplasm; Methylation;
KW   Nucleus; Phosphoprotein; Protein transport; Proteomics identification;
KW   Reference proteome; Transcription; Transcription regulation; Transport.
FT   CHAIN           1..206
FT                   /note="Transcription factor BTF3"
FT                   /id="PRO_0000213548"
FT   DOMAIN          82..147
FT                   /note="NAC-A/B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..198
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         46
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         54
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         160
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..44
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2320128,
FT                   ECO:0000303|Ref.3, ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT                   /id="VSP_013587"
FT   CONFLICT        41
FT                   /note="Q -> E (in Ref. 2; AAA58398)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68..105
FT                   /note="Missing (in Ref. 2; AAA58398)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192..196
FT                   /note="DLVEN -> GG (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="D -> Q (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:3MCB"
FT   STRAND          113..120
FT                   /evidence="ECO:0007829|PDB:3MCB"
FT   STRAND          122..126
FT                   /evidence="ECO:0007829|PDB:3MCB"
FT   TURN            127..130
FT                   /evidence="ECO:0007829|PDB:3MCB"
FT   STRAND          131..136
FT                   /evidence="ECO:0007829|PDB:3MCB"
FT   STRAND          138..142
FT                   /evidence="ECO:0007829|PDB:3MCB"
FT   HELIX           143..146
FT                   /evidence="ECO:0007829|PDB:3MCB"
FT   HELIX           149..153
FT                   /evidence="ECO:0007829|PDB:3MCB"
FT   HELIX           158..161
FT                   /evidence="ECO:0007829|PDB:3LKX"
SQ   SEQUENCE   206 AA;  22168 MW;  9653AC480EAF64C6 CRC64;
     MRRTGAPAQA DSRGRGRARG GCPGGEATLS QPPPRGGTRG QEPQMKETIM NQEKLAKLQA
     QVRIGGKGTA RRKKKVVHRT ATADDKKLQF SLKKLGVNNI SGIEEVNMFT NQGTVIHFNN
     PKVQASLAAN TFTITGHAET KQLTEMLPSI LNQLGADSLT SLRRLAEALP KQSVDGKAPL
     ATGEDDDDEV PDLVENFDEA SKNEAN
//