BC11A_HUMAN
ID BC11A_HUMAN Reviewed; 835 AA.
AC Q9H165; D6W5D7; Q66LN6; Q86W14; Q8WU92; Q96JL6; Q9H163; Q9H164; Q9H3G9;
AC Q9NWA7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=B-cell lymphoma/leukemia 11A {ECO:0000303|PubMed:11719382};
DE Short=BCL-11A;
DE AltName: Full=B-cell CLL/lymphoma 11A;
DE AltName: Full=COUP-TF-interacting protein 1;
DE AltName: Full=Ecotropic viral integration site 9 protein homolog;
DE Short=EVI-9;
DE AltName: Full=Zinc finger protein 856;
GN Name=BCL11A; Synonyms=CTIP1, EVI9, KIAA1809, ZNF856;
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; 2 AND 3), TISSUE SPECIFICITY, AND
RP CHROMOSOMAL TRANSLOCATION.
RX PubMed=11719382; DOI=10.1182/blood.v98.12.3413;
RA Satterwhite E., Sonoki T., Willis T.G., Harder L., Nowak R., Arriola E.L.,
RA Liu H., Price H.P., Gesk S., Steinemann D., Schlegelberger B., Oscier D.G.,
RA Siebert R., Tucker P.W., Dyer M.J.;
RT "The BCL11 gene family: involvement of BCL11A in lymphoid malignancies.";
RL Blood 98:3413-3420(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RA Suriyapperuma S.P., Sarfarazi M.;
RT "Identification of a new isoform for B-cell CLL/lymphoma 11A (BCL11A)
RT gene.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
RC TISSUE=Tonsil;
RA Ippolito G.C., Wall J.K., Allred L.K., Tucker P.W.;
RT "Identification of a novel isoform of BCL11A: BCL11A-XS (extra-short).";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-744 (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11161790; DOI=10.1006/geno.2000.6385;
RA Saiki Y., Yamazaki Y., Yoshida M., Katoh O., Nakamura T.;
RT "Human EVI9, a homologue of the mouse myeloid leukemia gene, is expressed
RT in the hematopoietic progenitors and down-regulated during myeloid
RT differentiation of HL60 cells.";
RL Genomics 70:387-391(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 636-835.
RC TISSUE=Embryo;
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 [9]
RP FUNCTION, AND ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 7).
RX PubMed=16704730; DOI=10.1186/1476-4598-5-18;
RA Liu H., Ippolito G.C., Wall J.K., Niu T., Probst L., Lee B.S., Pulford K.,
RA Banham A.H., Stockwin L., Shaffer A.L., Staudt L.M., Das C., Dyer M.J.,
RA Tucker P.W.;
RT "Functional studies of BCL11A: characterization of the conserved BCL11A-XL
RT splice variant and its interaction with BCL6 in nuclear paraspeckles of
RT germinal center B cells.";
RL Mol. Cancer 5:18-34(2006).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-608, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-625; SER-630 AND
RP THR-701, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP REVIEW ON FUNCTION.
RX PubMed=26375765; DOI=10.1016/j.gde.2015.08.001;
RA Bauer D.E., Orkin S.H.;
RT "Hemoglobin switching's surprise: the versatile transcription factor BCL11A
RT is a master repressor of fetal hemoglobin.";
RL Curr. Opin. Genet. Dev. 33:62-70(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-833, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-164; LYS-620 AND
RP LYS-833, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123 (ISOFORM 6), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-142.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [17]
RP POLYMORPHISM, AND ASSOCIATION WITH FETAL HEMOGLOBIN QUANTITATIVE TRAIT
RP LOCUS 5.
RX PubMed=17767159; DOI=10.1038/ng2108;
RA Menzel S., Garner C., Gut I., Matsuda F., Yamaguchi M., Heath S.,
RA Foglio M., Zelenika D., Boland A., Rooks H., Best S., Spector T.D.,
RA Farrall M., Lathrop M., Thein S.L.;
RT "A QTL influencing F cell production maps to a gene encoding a zinc-finger
RT protein on chromosome 2p15.";
RL Nat. Genet. 39:1197-1199(2007).
RN [18]
RP FUNCTION.
RX PubMed=23644491; DOI=10.1038/ng.2628;
RA Kadoch C., Hargreaves D.C., Hodges C., Elias L., Ho L., Ranish J.,
RA Crabtree G.R.;
RT "Proteomic and bioinformatic analysis of mammalian SWI/SNF complexes
RT identifies extensive roles in human malignancy.";
RL Nat. Genet. 45:592-601(2013).
RN [19]
RP INVOLVEMENT IN IDPFH, VARIANTS IDPFH PRO-47; PHE-48 AND GLN-66,
RP CHARACTERIZATION OF VARIANTS IDPFH PRO-47; PHE-48 AND GLN-66, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27453576; DOI=10.1016/j.ajhg.2016.05.030;
RG DDD Study;
RA Dias C., Estruch S.B., Grmaham S.A., McRae J., Sawiak S.J., Hurst J.A.,
RA Joss S.K., Holder S.E., Morton J.E., Turner C., Thevenon J., Mellul K.,
RA Sanchez-Andrade G., Ibarra-Soria X., Deriziotis P., Santos R.F., Lee S.C.,
RA Faivre L., Kleefstra T., Liu P., Hurles M.E., Fisher S.E., Logan D.W.;
RT "BCL11A haploinsufficiency causes an intellectual disability syndrome and
RT dysregulates transcription.";
RL Am. J. Hum. Genet. 99:253-274(2016).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=29606353; DOI=10.1016/j.cell.2018.03.016;
RA Liu N., Hargreaves V.V., Zhu Q., Kurland J.V., Hong J., Kim W., Sher F.,
RA Macias-Trevino C., Rogers J.M., Kurita R., Nakamura Y., Yuan G.C.,
RA Bauer D.E., Xu J., Bulyk M.L., Orkin S.H.;
RT "Direct Promoter Repression by BCL11A Controls the Fetal to Adult
RT Hemoglobin Switch.";
RL Cell 173:430-442(2018).
RN [21]
RP INTERACTION WITH TBR1, CHARACTERIZATION OF VARIANTS IDPFH PRO-47; PHE-48
RP AND GLN-66, AND DOMAIN.
RX PubMed=30250039; DOI=10.1038/s41598-018-32053-6;
RA den Hoed J., Sollis E., Venselaar H., Estruch S.B., Deriziotis P.,
RA Fisher S.E.;
RT "Functional characterization of TBR1 variants in neurodevelopmental
RT disorder.";
RL Sci. Rep. 8:14279-14279(2018).
CC -!- FUNCTION: Transcription factor (PubMed:16704730, PubMed:29606353).
CC Associated with the BAF SWI/SNF chromatin remodeling complex
CC (PubMed:23644491). Binds to the 5'-TGACCA-3' sequence motif in
CC regulatory regions of target genes, including a distal promoter of the
CC HBG1 hemoglobin subunit gamma-1 gene (PubMed:29606353). Involved in
CC regulation of the developmental switch from gamma- to beta-globin,
CC probably via direct repression of HBG1; hence indirectly repressing
CC fetal hemoglobin (HbF) level (PubMed:29606353, PubMed:26375765).
CC Involved in brain development (PubMed:27453576). May play a role in
CC hematopoiesis (By similarity). Essential factor in lymphopoiesis
CC required for B-cell formation in fetal liver (By similarity). May
CC function as a modulator of the transcriptional repression activity of
CC NR2F2 (By similarity). {ECO:0000250|UniProtKB:Q9QYE3,
CC ECO:0000269|PubMed:16704730, ECO:0000269|PubMed:23644491,
CC ECO:0000269|PubMed:29606353, ECO:0000303|PubMed:26375765,
CC ECO:0000303|PubMed:27453576}.
CC -!- SUBUNIT: Interacts with NR2F1, PIAS3, NR2F2 and NR2F6 (By similarity).
CC Isoform 1, isoform 2 and isoform 3 form homodimers and heterodimers
CC (PubMed:27453576). Isoform 2 interacts with TBR1 (PubMed:30250039).
CC {ECO:0000250|UniProtKB:Q9QYE3, ECO:0000269|PubMed:27453576,
CC ECO:0000269|PubMed:30250039}.
CC -!- INTERACTION:
CC Q9H165-2; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-10183342, EBI-745707;
CC Q9H165-2; P25800: LMO1; NbExp=3; IntAct=EBI-10183342, EBI-8639312;
CC Q9H165-2; Q15014: MORF4L2; NbExp=3; IntAct=EBI-10183342, EBI-399257;
CC Q9H165-2; O43639: NCK2; NbExp=6; IntAct=EBI-10183342, EBI-713635;
CC Q9H165-2; Q8NET5: NFAM1; NbExp=3; IntAct=EBI-10183342, EBI-11990542;
CC Q9H165-2; Q13526: PIN1; NbExp=3; IntAct=EBI-10183342, EBI-714158;
CC Q9H165-2; O43167: ZBTB24; NbExp=3; IntAct=EBI-10183342, EBI-744471;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11161790}. Nucleus
CC {ECO:0000269|PubMed:11161790}. Chromosome
CC {ECO:0000269|PubMed:29606353}. Note=Associates with the nuclear body.
CC Colocalizes with SUMO1 and SENP2 in nuclear speckles (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus matrix
CC {ECO:0000269|PubMed:16704730}. Note=Colocalizes with BCL6 in nuclear
CC paraspeckles. {ECO:0000269|PubMed:16704730}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:27453576}. Nucleus {ECO:0000269|PubMed:27453576}.
CC Note=Predominantly localized in the nucleus in nuclear paraspeckles.
CC {ECO:0000269|PubMed:27453576}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:27453576}. Nucleus {ECO:0000269|PubMed:27453576}.
CC Note=Predominantly localized in the cytoplasm in the absence of
CC interaction with isoform 1 and isoform 2. In presence of isoform 1 or
CC isoform 2, translocates from the cytoplasm into nuclear paraspeckles.
CC {ECO:0000269|PubMed:27453576}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=BCL11A-XL {ECO:0000303|PubMed:11719382}, BCL11A extra
CC long form;
CC IsoId=Q9H165-1; Sequence=Displayed;
CC Name=2; Synonyms=BCL11A-L {ECO:0000303|PubMed:11719382}, BCL11A long
CC form;
CC IsoId=Q9H165-2; Sequence=VSP_009554, VSP_009555;
CC Name=3 {ECO:0000303|PubMed:11719382}; Synonyms=BCL11A-S, BCL11A short
CC form;
CC IsoId=Q9H165-3; Sequence=VSP_009550, VSP_009552;
CC Name=6;
CC IsoId=Q9H165-6; Sequence=VSP_009548;
CC Name=7; Synonyms=BCL11A-XS, BCL11A eXtra short form;
CC IsoId=Q9H165-8; Sequence=VSP_058656, VSP_058657;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, spleen thymus,
CC bone marrow and testis. Expressed in CD34-positive myeloid precursor
CC cells, B-cells, monocytes and megakaryocytes. Expression is tightly
CC regulated during B-cell development. {ECO:0000269|PubMed:11161790,
CC ECO:0000269|PubMed:11719382}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in fetal and adult brain,
CC and in the plasmacytoid dendritic cell. {ECO:0000269|PubMed:16704730}.
CC -!- DOMAIN: The N-terminus is involved in protein dimerization and in
CC transactivation of transcription. {ECO:0000269|PubMed:27453576}.
CC -!- DOMAIN: The C-terminus of isoform 2 is necessary for isoform 2
CC interaction with TBR1. {ECO:0000269|PubMed:30250039}.
CC -!- DOMAIN: Zinc finger domains are necessary for sequence-specific binding
CC to DNA. {ECO:0000269|PubMed:29606353}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000250|UniProtKB:Q9QYE3}.
CC -!- POLYMORPHISM: Genetic variation in BCL11A underlies the fetal
CC hemoglobin quantitative trait locus 5 [MIM:142335]. It is associated
CC with quantitative variation in the production of F cells, that is
CC erythrocytes containing measurable amounts of fetal hemoglobin (HbF).
CC In healthy adults, HbF is present at residual levels (less than 0.6% of
CC total hemoglobin) with over twenty-fold variation. Ten to fifteen
CC percent of adults in the upper tail of the distribution have HbF levels
CC between 0.8% and 5.0%, a condition referred to as heterocellular
CC hereditary persistence of fetal hemoglobin (hHPFH). Although these HbF
CC levels are modest in otherwise healthy individuals, interaction of
CC hHPFH with beta thalassemia or sickle cell disease can increase HbF
CC output in these individuals to levels that are clinically beneficial.
CC {ECO:0000269|PubMed:17767159}.
CC -!- DISEASE: Note=Chromosomal aberrations involving BCL11A are associated
CC with B-cell malignancies. Translocation t(2;14)(p13;q32.3) causes
CC BCL11A deregulation and overexpression. {ECO:0000269|PubMed:11719382}.
CC -!- DISEASE: Intellectual developmental disorder with persistence of fetal
CC hemoglobin (IDPFH) [MIM:617101]: An autosomal dominant disorder
CC characterized by delayed psychomotor development, intellectual
CC disability, variable dysmorphic features, including microcephaly,
CC downslanting palpebral fissures, strabismus, and external ear
CC abnormalities, and asymptomatic persistence of fetal hemoglobin.
CC {ECO:0000269|PubMed:27453576, ECO:0000269|PubMed:30250039}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG49025.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC Sequence=BAB47438.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BCL11AID391.html";
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DR EMBL; AJ404611; CAC17723.1; -; mRNA.
DR EMBL; AJ404612; CAC17724.1; -; mRNA.
DR EMBL; AJ404613; CAC17725.1; -; mRNA.
DR EMBL; AY228763; AAO88272.1; -; mRNA.
DR EMBL; AB058712; BAB47438.1; ALT_INIT; mRNA.
DR EMBL; AY692278; AAU04557.1; -; mRNA.
DR EMBL; AC007381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00035.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00040.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00041.1; -; Genomic_DNA.
DR EMBL; BC021098; AAH21098.1; -; mRNA.
DR EMBL; AF080216; AAG49025.1; ALT_SEQ; mRNA.
DR EMBL; AK001035; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS1861.1; -. [Q9H165-2]
DR CCDS; CCDS1862.1; -. [Q9H165-1]
DR CCDS; CCDS46295.1; -. [Q9H165-3]
DR RefSeq; NP_060484.2; NM_018014.3. [Q9H165-2]
DR RefSeq; NP_075044.2; NM_022893.3. [Q9H165-1]
DR RefSeq; NP_612569.1; NM_138559.1. [Q9H165-3]
DR RefSeq; XP_011531211.1; XM_011532909.1. [Q9H165-1]
DR RefSeq; XP_016859823.1; XM_017004334.1.
DR PDB; 5VTB; X-ray; 2.40 A; B=2-16.
DR PDB; 6KI6; X-ray; 2.50 A; A/B=731-835.
DR PDB; 6U9Q; X-ray; 1.83 A; A=730-835.
DR PDBsum; 5VTB; -.
DR PDBsum; 6KI6; -.
DR PDBsum; 6U9Q; -.
DR AlphaFoldDB; Q9H165; -.
DR SMR; Q9H165; -.
DR BioGRID; 119737; 95.
DR DIP; DIP-45629N; -.
DR IntAct; Q9H165; 30.
DR MINT; Q9H165; -.
DR STRING; 9606.ENSP00000338774; -.
DR iPTMnet; Q9H165; -.
DR PhosphoSitePlus; Q9H165; -.
DR BioMuta; BCL11A; -.
DR DMDM; 44887724; -.
DR EPD; Q9H165; -.
DR jPOST; Q9H165; -.
DR MassIVE; Q9H165; -.
DR MaxQB; Q9H165; -.
DR PaxDb; Q9H165; -.
DR PeptideAtlas; Q9H165; -.
DR PRIDE; Q9H165; -.
DR ProteomicsDB; 80362; -. [Q9H165-1]
DR ProteomicsDB; 80363; -. [Q9H165-2]
DR ProteomicsDB; 80364; -. [Q9H165-3]
DR ProteomicsDB; 80367; -. [Q9H165-6]
DR Antibodypedia; 30518; 473 antibodies from 37 providers.
DR DNASU; 53335; -.
DR Ensembl; ENST00000335712.11; ENSP00000338774.7; ENSG00000119866.22. [Q9H165-6]
DR Ensembl; ENST00000356842.9; ENSP00000349300.4; ENSG00000119866.22. [Q9H165-2]
DR Ensembl; ENST00000359629.10; ENSP00000352648.5; ENSG00000119866.22. [Q9H165-3]
DR Ensembl; ENST00000409351.5; ENSP00000487844.1; ENSG00000119866.22. [Q9H165-8]
DR Ensembl; ENST00000642384.2; ENSP00000496168.1; ENSG00000119866.22. [Q9H165-1]
DR GeneID; 53335; -.
DR KEGG; hsa:53335; -.
DR MANE-Select; ENST00000642384.2; ENSP00000496168.1; NM_022893.4; NP_075044.2.
DR UCSC; uc002sab.4; human. [Q9H165-1]
DR CTD; 53335; -.
DR DisGeNET; 53335; -.
DR GeneCards; BCL11A; -.
DR GeneReviews; BCL11A; -.
DR HGNC; HGNC:13221; BCL11A.
DR HPA; ENSG00000119866; Tissue enhanced (brain, lymphoid tissue, skin).
DR MalaCards; BCL11A; -.
DR MIM; 142335; phenotype.
DR MIM; 606557; gene.
DR MIM; 617101; phenotype.
DR neXtProt; NX_Q9H165; -.
DR OpenTargets; ENSG00000119866; -.
DR Orphanet; 619233; Hereditary persistence of fetal hemoglobin-intellectual disability syndrome.
DR Orphanet; 251380; Hereditary persistence of fetal hemoglobin-sickle cell disease syndrome.
DR PharmGKB; PA25300; -.
DR VEuPathDB; HostDB:ENSG00000119866; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156983; -.
DR HOGENOM; CLU_007684_1_0_1; -.
DR InParanoid; Q9H165; -.
DR OMA; DMCDGDS; -.
DR PhylomeDB; Q9H165; -.
DR TreeFam; TF318131; -.
DR PathwayCommons; Q9H165; -.
DR Reactome; R-HSA-9700645; ALK mutants bind TKIs.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; Q9H165; -.
DR SIGNOR; Q9H165; -.
DR BioGRID-ORCS; 53335; 15 hits in 1091 CRISPR screens.
DR ChiTaRS; BCL11A; human.
DR GeneWiki; BCL11A; -.
DR GenomeRNAi; 53335; -.
DR Pharos; Q9H165; Tbio.
DR PRO; PR:Q9H165; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H165; protein.
DR Bgee; ENSG00000119866; Expressed in cortical plate and 171 other tissues.
DR ExpressionAtlas; Q9H165; baseline and differential.
DR Genevisible; Q9H165; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0042382; C:paraspeckles; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:ARUK-UCL.
DR GO; GO:0001067; F:transcription regulatory region nucleic acid binding; IDA:ARUK-UCL.
DR GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl.
DR GO; GO:0030517; P:negative regulation of axon extension; ISS:BHF-UCL.
DR GO; GO:2000173; P:negative regulation of branching morphogenesis of a nerve; IEA:Ensembl.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:BHF-UCL.
DR GO; GO:2000171; P:negative regulation of dendrite development; IMP:BHF-UCL.
DR GO; GO:1903860; P:negative regulation of dendrite extension; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:BHF-UCL.
DR GO; GO:1904800; P:negative regulation of neuron remodeling; IEA:Ensembl.
DR GO; GO:0032463; P:negative regulation of protein homooligomerization; IC:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement; Chromosome;
KW Cytoplasm; Disease variant; Intellectual disability; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..835
FT /note="B-cell lymphoma/leukemia 11A"
FT /id="PRO_0000047102"
FT ZN_FING 170..193
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..429
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 742..764
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 770..792
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 800..823
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..210
FT /note="Required for nuclear body formation and for SUMO1
FT recruitment"
FT /evidence="ECO:0000250"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..508
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYE3"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 271
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYE3"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYE3"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYE3"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYE3"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 701
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 634
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9QYE3"
FT CROSSLNK 833
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 129..163
FT /note="DKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGIC -> G (in isoform
FT 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_009548"
FT VAR_SEQ 129..142
FT /note="DKLLHWRGLSSPRS -> AQTELEDVFVYLMV (in isoform 7)"
FT /id="VSP_058656"
FT VAR_SEQ 143..835
FT /note="Missing (in isoform 7)"
FT /id="VSP_058657"
FT VAR_SEQ 212..243
FT /note="GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI -> LHTPPFGVVPRELKMC
FT GSFRMEAREPLSSEKI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11719382"
FT /id="VSP_009550"
FT VAR_SEQ 244..835
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11719382"
FT /id="VSP_009552"
FT VAR_SEQ 745..773
FT /note="EYCGKVFKNCSNLTVHRRSHTGERPYKCE -> SSHTPIRRSTQRAQDVWQF
FT SDGSSRALKF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11347906,
FT ECO:0000303|PubMed:11719382, ECO:0000303|PubMed:15489334"
FT /id="VSP_009554"
FT VAR_SEQ 774..835
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11347906,
FT ECO:0000303|PubMed:11719382, ECO:0000303|PubMed:15489334"
FT /id="VSP_009555"
FT VARIANT 47
FT /note="T -> P (in IDPFH; de novo mutation; loss of function
FT in transactivation of transcription; reduces the
FT interaction between isoform 2 and isoform 3; disrupts the
FT nuclear paraspeckle distribution of isoform 2 and isoform
FT 3; does not affect the interaction of isoform 2 with TBR1;
FT dbSNP:rs886037864)"
FT /evidence="ECO:0000269|PubMed:27453576,
FT ECO:0000269|PubMed:30250039"
FT /id="VAR_076921"
FT VARIANT 48
FT /note="C -> F (in IDPFH; de novo mutation; loss of function
FT in transactivation of transcription; reduces the
FT interaction between isoform 2 and isoform 3; disrupts the
FT nuclear paraspeckle distribution of isoform 2 and isoform
FT 3; does not affect the interaction of isoform 2 with TBR1;
FT dbSNP:rs886037865)"
FT /evidence="ECO:0000269|PubMed:27453576,
FT ECO:0000269|PubMed:30250039"
FT /id="VAR_076922"
FT VARIANT 66
FT /note="H -> Q (in IDPFH; de novo mutation; loss of function
FT in transactivation of transcription; reduces the
FT interaction between isoform 2 and isoform 3; disrupts the
FT nuclear paraspeckle distribution of isoform 2 and isoform
FT 3; does not affect the interaction of isoform 2 with TBR1;
FT dbSNP:rs886037866)"
FT /evidence="ECO:0000269|PubMed:27453576,
FT ECO:0000269|PubMed:30250039"
FT /id="VAR_076923"
FT VARIANT 142
FT /note="S -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035553"
FT CONFLICT 119
FT /note="G -> R (in Ref. 1; CAC17723/CAC17724/CAC17725)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="S -> F (in Ref. 7; AAG49025)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="F -> L (in Ref. 7; AAG49025)"
FT /evidence="ECO:0000305"
FT CONFLICT 522..532
FT /note="Missing (in Ref. 7; AAG49025)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="A -> T (in Ref. 1; CAC17723/CAC17724)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="E -> D (in Ref. 7; AAG49025)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="P -> T (in Ref. 1; CAC17723/CAC17724)"
FT /evidence="ECO:0000305"
FT HELIX 739..742
FT /evidence="ECO:0007829|PDB:6U9Q"
FT TURN 745..747
FT /evidence="ECO:0007829|PDB:6U9Q"
FT STRAND 750..753
FT /evidence="ECO:0007829|PDB:6KI6"
FT HELIX 754..765
FT /evidence="ECO:0007829|PDB:6U9Q"
FT STRAND 773..776
FT /evidence="ECO:0007829|PDB:6U9Q"
FT STRAND 778..781
FT /evidence="ECO:0007829|PDB:6U9Q"
FT HELIX 782..789
FT /evidence="ECO:0007829|PDB:6U9Q"
FT HELIX 790..792
FT /evidence="ECO:0007829|PDB:6U9Q"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:6U9Q"
FT TURN 803..805
FT /evidence="ECO:0007829|PDB:6U9Q"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:6U9Q"
FT HELIX 812..822
FT /evidence="ECO:0007829|PDB:6U9Q"
FT VARIANT Q9H165-2:47
FT /note="T -> P (in IDPFH, de novo mutation, loss of function
FT in transactivation of transcription, reduces the
FT interaction between isoform 2 and isoform 3, disrupts the
FT nuclear paraspeckle distribution of isoform 2 and isoform
FT 3; dbSNP:rs886037864)"
FT /evidence="ECO:0000305"
FT /id="VAR_082936"
FT VARIANT Q9H165-2:48
FT /note="C -> F (in IDPFH, de novo mutation, loss of function
FT in transactivation of transcription, reduces the
FT interaction between isoform 2 and isoform 3, disrupts the
FT nuclear paraspeckle distribution of isoform 2 and isoform
FT 3; dbSNP:rs886037865)"
FT /evidence="ECO:0000305"
FT /id="VAR_082937"
FT VARIANT Q9H165-2:66
FT /note="H -> Q (in IDPFH, de novo mutation, loss of function
FT in transactivation of transcription, reduces the
FT interaction between isoform 2 and isoform 3, disrupts the
FT nuclear paraspeckle distribution of isoform 2 and isoform
FT 3; dbSNP:rs886037866)"
FT /evidence="ECO:0000305"
FT /id="VAR_082938"
FT VARIANT Q9H165-3:47
FT /note="T -> P (in IDPFH, de novo mutation, loss of function
FT transactivation of transcription, reduces the interaction
FT between isoform 2 and isoform 3, disrupts the nuclear
FT paraspeckle distribution of isoform 2 and isoform 3, does
FT not affect the interaction of isoform 2 with TBR1;
FT dbSNP:rs886037864)"
FT /evidence="ECO:0000305"
FT /id="VAR_082939"
FT VARIANT Q9H165-3:48
FT /note="C -> F (in IDPFH, de novo mutation, loss of function
FT in transactivation of transcription, reduces the
FT interaction between isoform 2 and isoform 3, disrupts the
FT nuclear paraspeckle distribution of isoform 2 and isoform
FT 3, does not affect the interaction of isoform 2 with TBR1;
FT dbSNP:rs886037865)"
FT /evidence="ECO:0000305"
FT /id="VAR_082940"
FT VARIANT Q9H165-3:66
FT /note="H -> Q (in IDPFH, de novo mutation, loss of function
FT in transactivation of transcription, reduces the
FT interaction between isoform 2 and isoform 3, disrupts the
FT nuclear paraspeckle distribution of isoform 2 and isoform
FT 3, does not affect the interaction of isoform 2 with TBR1;
FT dbSNP:rs886037866)"
FT /evidence="ECO:0000305"
FT /id="VAR_082941"
FT CROSSLNK Q9H165-6:123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 835 AA; 91197 MW; D36A7D0BE6976DCF CRC64;
MSRRKQGKPQ HLSKREFSPE PLEAILTDDE PDHGPLGAPE GDHDLLTCGQ CQMNFPLGDI
LIFIEHKRKQ CNGSLCLEKA VDKPPSPSPI EMKKASNPVE VGIQVTPEDD DCLSTSSRGI
CPKQEHIADK LLHWRGLSSP RSAHGALIPT PGMSAEYAPQ GICKDEPSSY TCTTCKQPFT
SAWFLLQHAQ NTHGLRIYLE SEHGSPLTPR VGIPSGLGAE CPSQPPLHGI HIADNNPFNL
LRIPGSVSRE ASGLAEGRFP PTPPLFSPPP RHHLDPHRIE RLGAEEMALA THHPSAFDRV
LRLNPMAMEP PAMDFSRRLR ELAGNTSSPP LSPGRPSPMQ RLLQPFQPGS KPPFLATPPL
PPLQSAPPPS QPPVKSKSCE FCGKTFKFQS NLVVHRRSHT GEKPYKCNLC DHACTQASKL
KRHMKTHMHK SSPMTVKSDD GLSTASSPEP GTSDLVGSAS SALKSVVAKF KSENDPNLIP
ENGDEEEEED DEEEEEEEEE EEEELTESER VDYGFGLSLE AARHHENSSR GAVVGVGDES
RALPDVMQGM VLSSMQHFSE AFHQVLGEKH KRGHLAEAEG HRDTCDEDSV AGESDRIDDG
TVNGRGCSPG ESASGGLSKK LLLGSPSSLS PFSKRIKLEK EFDLPPAAMP NTENVYSQWL
AGYAASRQLK DPFLSFGDSR QSPFASSSEH SSENGSLRFS TPPGELDGGI SGRSGTGSGG
STPHISGPGP GRPSSKEGRR SDTCEYCGKV FKNCSNLTVH RRSHTGERPY KCELCNYACA
QSSKLTRHMK THGQVGKDVY KCEICKMPFS VYSTLEKHMK KWHSDRVLNN DIKTE
