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Database: UniProt
Entry: P53539
LinkDB: P53539
Original site: P53539 
ID   FOSB_HUMAN              Reviewed;         338 AA.
AC   P53539; A8K9K5; A8VJE1; A8VJE6; A8VJF0; A8VJF3; A8VJF7; A8VJG1; A8VJG5;
AC   A8VJG9; E7EPR6; E9PHJ3; K7EMJ6; Q49AD7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-JUN-2021, entry version 171.
DE   RecName: Full=Protein fosB;
DE   AltName: Full=G0/G1 switch regulatory protein 3;
GN   Name=FOSB; Synonyms=G0S3;
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 [GENOMIC DNA].
RX   PubMed=1301997; DOI=10.1038/ng0492-34;
RA   Martin-Gallardo A., McCombie W.R., Gocayne J.D., Fitzgerald M.G.,
RA   Wallace S., Lee B.M., Lamerdin J.E., Trapp S., Kelley J.M., Liu L.-I.,
RA   Dubnick M., Johnston-Dow L.A., Kerlavage A.R., de Jong P., Carrano A.,
RA   Fields C., Venter J.C.;
RT   "Automated DNA sequencing and analysis of 106 kilobases from human
RT   chromosome 19q13.3.";
RL   Nat. Genet. 1:34-39(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Blood;
RX   PubMed=8985116; DOI=10.1089/dna.1996.15.1025;
RA   Heximer S.P., Cristillo A.D., Russell L., Forsdyke D.R.;
RT   "Sequence analysis and expression in cultured lymphocytes of the human FOSB
RT   gene (G0S3).";
RL   DNA Cell Biol. 15:1025-1038(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8 AND 9), AND
RP   ALTERNATIVE SPLICING.
RA   Xiong F., Zeng Z., Xiong W.;
RT   "Novel transcript variants of human FOSB gene.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-33.
RG   NIEHS SNPs program;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thyroid;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(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] (ISOFORMS 1 AND 10).
RC   TISSUE=Blood, and Brain;
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).
CC   -!- FUNCTION: FosB interacts with Jun proteins enhancing their DNA binding
CC       activity.
CC   -!- SUBUNIT: Heterodimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P53539; P21549: AGXT; NbExp=3; IntAct=EBI-2806743, EBI-727098;
CC       P53539; P15336: ATF2; NbExp=3; IntAct=EBI-2806743, EBI-1170906;
CC       P53539; Q9BU64: CENPO; NbExp=3; IntAct=EBI-2806743, EBI-745954;
CC       P53539; Q02930-3: CREB5; NbExp=3; IntAct=EBI-2806743, EBI-10192698;
CC       P53539; Q9UIA0: CYTH4; NbExp=3; IntAct=EBI-2806743, EBI-11521003;
CC       P53539; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-2806743, EBI-744099;
CC       P53539; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-2806743, EBI-2807642;
CC       P53539; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-2806743, EBI-6658203;
CC       P53539; Q9BZS1: FOXP3; NbExp=3; IntAct=EBI-2806743, EBI-983719;
CC       P53539; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-2806743, EBI-7251368;
CC       P53539; P17275: JUNB; NbExp=6; IntAct=EBI-2806743, EBI-748062;
CC       P53539; O43639: NCK2; NbExp=3; IntAct=EBI-2806743, EBI-713635;
CC       P53539; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-2806743, EBI-11746523;
CC       P53539; Q16236: NFE2L2; NbExp=6; IntAct=EBI-2806743, EBI-2007911;
CC       P53539; B7ZLY0: PHC2; NbExp=3; IntAct=EBI-2806743, EBI-14568740;
CC       P53539; O43189: PHF1; NbExp=3; IntAct=EBI-2806743, EBI-530034;
CC       P53539; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-2806743, EBI-1389308;
CC       P53539; P78424: POU6F2; NbExp=5; IntAct=EBI-2806743, EBI-12029004;
CC       P53539; Q01974: ROR2; NbExp=3; IntAct=EBI-2806743, EBI-6422642;
CC       P53539; Q96A09: TENT5B; NbExp=5; IntAct=EBI-2806743, EBI-752030;
CC       P53539; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2806743, EBI-11741437;
CC       P53539; O43711: TLX3; NbExp=3; IntAct=EBI-2806743, EBI-3939165;
CC       P53539; Q14119: VEZF1; NbExp=3; IntAct=EBI-2806743, EBI-11980193;
CC       P53539; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-2806743, EBI-742550;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=10;
CC       Name=1; Synonyms=FosB-L;
CC         IsoId=P53539-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P53539-2; Sequence=VSP_046167;
CC       Name=3;
CC         IsoId=P53539-3; Sequence=VSP_055563;
CC       Name=4;
CC         IsoId=P53539-4; Sequence=VSP_055565;
CC       Name=5;
CC         IsoId=P53539-5; Sequence=VSP_055563, VSP_046167;
CC       Name=6;
CC         IsoId=P53539-6; Sequence=VSP_046167, VSP_055565;
CC       Name=7;
CC         IsoId=P53539-7; Sequence=VSP_055563, VSP_055565;
CC       Name=8;
CC         IsoId=P53539-8; Sequence=VSP_055564;
CC       Name=9;
CC         IsoId=P53539-9; Sequence=VSP_055564, VSP_055565;
CC       Name=10;
CC         IsoId=P53539-10; Sequence=VSP_055562;
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/fosb/";
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DR   EMBL; L49169; AAB53946.1; -; mRNA.
DR   EMBL; EU178109; ABW34730.1; -; mRNA.
DR   EMBL; EU178110; ABW34731.1; -; mRNA.
DR   EMBL; EU178111; ABW34732.1; -; mRNA.
DR   EMBL; EU178112; ABW34733.1; -; mRNA.
DR   EMBL; EU178113; ABW34734.1; -; mRNA.
DR   EMBL; EU178114; ABW34735.1; -; mRNA.
DR   EMBL; EU178115; ABW34736.1; -; mRNA.
DR   EMBL; EU178116; ABW34737.1; -; mRNA.
DR   EMBL; AY898963; AAW65374.1; -; Genomic_DNA.
DR   EMBL; AK292720; BAF85409.1; -; mRNA.
DR   EMBL; AC138128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471126; EAW57351.1; -; Genomic_DNA.
DR   EMBL; BC036724; AAH36724.1; -; mRNA.
DR   EMBL; BC040197; AAH40197.1; -; mRNA.
DR   CCDS; CCDS12664.1; -. [P53539-1]
DR   CCDS; CCDS46113.1; -. [P53539-2]
DR   PIR; I53043; I53043.
DR   RefSeq; NP_001107643.1; NM_001114171.1. [P53539-2]
DR   RefSeq; NP_006723.2; NM_006732.2. [P53539-1]
DR   PDB; 5VPA; X-ray; 2.83 A; A=153-219.
DR   PDB; 5VPB; X-ray; 2.69 A; A/C=153-219.
DR   PDB; 5VPC; X-ray; 2.50 A; A/C=153-219.
DR   PDB; 5VPD; X-ray; 2.79 A; A/C=153-219.
DR   PDB; 5VPE; X-ray; 2.05 A; A/C=153-219.
DR   PDB; 5VPF; X-ray; 2.69 A; A/C=153-219.
DR   PDB; 6UCI; X-ray; 2.09 A; A/B/C/D=153-219.
DR   PDB; 6UCL; X-ray; 2.21 A; A=153-219.
DR   PDB; 6UCM; X-ray; 2.42 A; A/B/C=153-219.
DR   PDBsum; 5VPA; -.
DR   PDBsum; 5VPB; -.
DR   PDBsum; 5VPC; -.
DR   PDBsum; 5VPD; -.
DR   PDBsum; 5VPE; -.
DR   PDBsum; 5VPF; -.
DR   PDBsum; 6UCI; -.
DR   PDBsum; 6UCL; -.
DR   PDBsum; 6UCM; -.
DR   SMR; P53539; -.
DR   BioGRID; 108637; 31.
DR   CORUM; P53539; -.
DR   DIP; DIP-60013N; -.
DR   IntAct; P53539; 28.
DR   MINT; P53539; -.
DR   STRING; 9606.ENSP00000245919; -.
DR   iPTMnet; P53539; -.
DR   PhosphoSitePlus; P53539; -.
DR   BioMuta; FOSB; -.
DR   DMDM; 1706888; -.
DR   CPTAC; CPTAC-1760; -.
DR   MassIVE; P53539; -.
DR   MaxQB; P53539; -.
DR   PaxDb; P53539; -.
DR   PeptideAtlas; P53539; -.
DR   PRIDE; P53539; -.
DR   ProteomicsDB; 17421; -.
DR   ProteomicsDB; 20551; -.
DR   ProteomicsDB; 56584; -. [P53539-1]
DR   Antibodypedia; 4139; 533 antibodies.
DR   DNASU; 2354; -.
DR   Ensembl; ENST00000353609; ENSP00000245919; ENSG00000125740. [P53539-1]
DR   Ensembl; ENST00000417353; ENSP00000407207; ENSG00000125740. [P53539-2]
DR   Ensembl; ENST00000443841; ENSP00000414177; ENSG00000125740. [P53539-8]
DR   Ensembl; ENST00000585836; ENSP00000467497; ENSG00000125740. [P53539-5]
DR   Ensembl; ENST00000586615; ENSP00000468207; ENSG00000125740. [P53539-10]
DR   Ensembl; ENST00000591858; ENSP00000466530; ENSG00000125740. [P53539-3]
DR   Ensembl; ENST00000615753; ENSP00000485018; ENSG00000125740. [P53539-4]
DR   GeneID; 2354; -.
DR   KEGG; hsa:2354; -.
DR   UCSC; uc002pbx.5; human. [P53539-1]
DR   CTD; 2354; -.
DR   DisGeNET; 2354; -.
DR   GeneCards; FOSB; -.
DR   HGNC; HGNC:3797; FOSB.
DR   HPA; ENSG00000125740; Low tissue specificity.
DR   MIM; 164772; gene.
DR   neXtProt; NX_P53539; -.
DR   OpenTargets; ENSG00000125740; -.
DR   PharmGKB; PA28213; -.
DR   VEuPathDB; HostDB:ENSG00000125740.13; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   GeneTree; ENSGT00940000160358; -.
DR   HOGENOM; CLU_049742_4_0_1; -.
DR   InParanoid; P53539; -.
DR   OMA; QANCKIP; -.
DR   PhylomeDB; P53539; -.
DR   TreeFam; TF326301; -.
DR   PathwayCommons; P53539; -.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR   SIGNOR; P53539; -.
DR   BioGRID-ORCS; 2354; 7 hits in 1008 CRISPR screens.
DR   ChiTaRS; FOSB; human.
DR   GeneWiki; FOSB; -.
DR   GenomeRNAi; 2354; -.
DR   Pharos; P53539; Tbio.
DR   PRO; PR:P53539; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P53539; protein.
DR   Bgee; ENSG00000125740; Expressed in mucosa of stomach and 210 other tissues.
DR   ExpressionAtlas; P53539; baseline and differential.
DR   Genevisible; P53539; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0008134; F:transcription factor binding; TAS:ProtInc.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR   GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR   GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR029813; FosB.
DR   PANTHER; PTHR23351; PTHR23351; 1.
DR   PANTHER; PTHR23351:SF3; PTHR23351:SF3; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..338
FT                   /note="Protein fosB"
FT                   /id="PRO_0000076476"
FT   DOMAIN          155..218
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..182
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          183..211
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          222..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..269
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..49
FT                   /note="Missing (in isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055562"
FT   VAR_SEQ         42..80
FT                   /note="Missing (in isoform 3, isoform 5 and isoform 7)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_055563"
FT   VAR_SEQ         43..185
FT                   /note="Missing (in isoform 8 and isoform 9)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_055564"
FT   VAR_SEQ         150..185
FT                   /note="Missing (in isoform 2, isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_046167"
FT   VAR_SEQ         238..284
FT                   /note="Missing (in isoform 4, isoform 6, isoform 7 and
FT                   isoform 9)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_055565"
FT   VARIANT         33
FT                   /note="G -> S (in dbSNP:rs28381241)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_022286"
FT   CONFLICT        338
FT                   /note="L -> R (in Ref. 2; AAB53946 and 3; ABW34730/
FT                   ABW34731/ABW34732/ABW34733/ABW34734/ABW34735/ABW34736/
FT                   ABW34737)"
FT                   /evidence="ECO:0000305"
FT   HELIX           157..217
FT                   /evidence="ECO:0007829|PDB:5VPE"
SQ   SEQUENCE   338 AA;  35928 MW;  DDFF827C5047850F CRC64;
     MFQAFPGDYD SGSRCSSSPS AESQYLSSVD SFGSPPTAAA SQECAGLGEM PGSFVPTVTA
     ITTSQDLQWL VQPTLISSMA QSQGQPLASQ PPVVDPYDMP GTSYSTPGMS GYSSGGASGS
     GGPSTSGTTS GPGPARPARA RPRRPREETL TPEEEEKRRV RRERNKLAAA KCRNRRRELT
     DRLQAETDQL EEEKAELESE IAELQKEKER LEFVLVAHKP GCKIPYEEGP GPGPLAEVRD
     LPGSAPAKED GFSWLLPPPP PPPLPFQTSQ DAPPNLTASL FTHSEVQVLG DPFPVVNPSY
     TSSFVLTCPE VSAFAGAQRT SGSDQPSDPL NSPSLLAL
//
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