Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

B-cell lymphoma/leukemia 11A (BCL-11A) (B-cell CLL/lymphoma 11A) (COUP-TF-interacting protein 1) (Ecotropic viral integration site 9 protein homolog) (EVI-9) (Zinc finger protein 856)

 BC11A_HUMAN             Reviewed;         835 AA.
Q9H165; D6W5D7; Q66LN6; Q86W14; Q8WU92; Q96JL6; Q9H163; Q9H164;
Q9H3G9; Q9NWA7;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
25-OCT-2017, entry version 154.
RecName: Full=B-cell lymphoma/leukemia 11A;
Short=BCL-11A;
AltName: Full=B-cell CLL/lymphoma 11A;
AltName: Full=COUP-TF-interacting protein 1;
AltName: Full=Ecotropic viral integration site 9 protein homolog;
Short=EVI-9;
AltName: Full=Zinc finger protein 856;
Name=BCL11A; Synonyms=CTIP1, EVI9, KIAA1809, ZNF856;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY,
AND CHROMOSOMAL TRANSLOCATION.
PubMed=11719382; DOI=10.1182/blood.V98.12.3413;
Satterwhite E., Sonoki T., Willis T.G., Harder L., Nowak R.,
Arriola E.L., Liu H., Price H.P., Gesk S., Steinemann D.,
Schlegelberger B., Oscier D.G., Siebert R., Tucker P.W., Dyer M.J.;
"The BCL11 gene family: involvement of BCL11A in lymphoid
malignancies.";
Blood 98:3413-3420(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
Suriyapperuma S.P., Sarfarazi M.;
"Identification of a new isoform for B-cell CLL/lymphoma 11A (BCL11A)
gene.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
TISSUE=Tonsil;
Ippolito G.C., Wall J.K., Allred L.K., Tucker P.W.;
"Identification of a novel isoform of BCL11A: BCL11A-XS (extra-
short).";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-744 (ISOFORM 1), SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=11161790; DOI=10.1006/geno.2000.6385;
Saiki Y., Yamazaki Y., Yoshida M., Katoh O., Nakamura T.;
"Human EVI9, a homologue of the mouse myeloid leukemia gene, is
expressed in the hematopoietic progenitors and down-regulated during
myeloid differentiation of HL60 cells.";
Genomics 70:387-391(2000).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 636-835.
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 7).
PubMed=16704730; DOI=10.1186/1476-4598-5-18;
Liu H., Ippolito G.C., Wall J.K., Niu T., Probst L., Lee B.S.,
Pulford K., Banham A.H., Stockwin L., Shaffer A.L., Staudt L.M.,
Das C., Dyer M.J., Tucker P.W.;
"Functional studies of BCL11A: characterization of the conserved
BCL11A-XL splice variant and its interaction with BCL6 in nuclear
paraspeckles of germinal center B cells.";
Mol. Cancer 5:18-34(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-608, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-625; SER-630
AND THR-701, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
REVIEW ON FUNCTION.
PubMed=26375765; DOI=10.1016/j.gde.2015.08.001;
Bauer D.E., Orkin S.H.;
"Hemoglobin switching's surprise: the versatile transcription factor
BCL11A is a master repressor of fetal hemoglobin.";
Curr. Opin. Genet. Dev. 33:62-70(2015).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-833, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-164; LYS-620 AND
LYS-833, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123 (ISOFORM 6),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[16]
VARIANT [LARGE SCALE ANALYSIS] PHE-142.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[17]
POLYMORPHISM, AND ASSOCIATION WITH FETAL HEMOGLOBIN QUANTITATIVE TRAIT
LOCUS 5.
PubMed=17767159; DOI=10.1038/ng2108;
Menzel S., Garner C., Gut I., Matsuda F., Yamaguchi M., Heath S.,
Foglio M., Zelenika D., Boland A., Rooks H., Best S., Spector T.D.,
Farrall M., Lathrop M., Thein S.L.;
"A QTL influencing F cell production maps to a gene encoding a zinc-
finger protein on chromosome 2p15.";
Nat. Genet. 39:1197-1199(2007).
[18]
INVOLVEMENT IN IDPFH, VARIANTS IDPFH PRO-47; PHE-48 AND GLN-66,
CHARACTERIZATION OF VARIANTS IDPFH PRO-47; PHE-48 AND GLN-66,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=27453576; DOI=10.1016/j.ajhg.2016.05.030;
DDD Study;
Dias C., Estruch S.B., Grmaham S.A., McRae J., Sawiak S.J.,
Hurst J.A., Joss S.K., Holder S.E., Morton J.E., Turner C.,
Thevenon J., Mellul K., Sanchez-Andrade G., Ibarra-Soria X.,
Deriziotis P., Santos R.F., Lee S.C., Faivre L., Kleefstra T., Liu P.,
Hurles M.E., Fisher S.E., Logan D.W.;
"BCL11A haploinsufficiency causes an intellectual disability syndrome
and dysregulates transcription.";
Am. J. Hum. Genet. 99:253-274(2016).
-!- FUNCTION: Transcription factor associated with the BAF SWI/SNF
chromatin remodeling complex (By similarity). Repressor of fetal
hemoglobin (HbF) level (PubMed:26375765). Involved in brain
development (PubMed:27453576). Functions as a myeloid and B-cell
proto-oncogene. May play important roles in leukemogenesis and
hematopoiesis. Essential factor in lymphopoiesis required for B-
cell formation in fetal liver. May function as a modulator of the
transcriptional repression activity of ARP1 (By similarity).
{ECO:0000250|UniProtKB:Q9QYE3, ECO:0000303|PubMed:26375765,
ECO:0000303|PubMed:27453576}.
-!- SUBUNIT: Interacts with TFCOUP1, PIAS3, ARP1 and EAR2 (By
similarity). Isoform 1, isoform 2 and isoform 3 form homodimers
and heterodimers (PubMed:27453576). {ECO:0000250|UniProtKB:Q9QYE3,
ECO:0000269|PubMed:27453576}.
-!- INTERACTION:
Q8NEA9:GMCL1P1; NbExp=5; IntAct=EBI-10183342, EBI-745707;
P25800:LMO1; NbExp=3; IntAct=EBI-10183342, EBI-8639312;
Q15014:MORF4L2; NbExp=4; IntAct=EBI-10183342, EBI-399257;
O43639:NCK2; NbExp=5; IntAct=EBI-10183342, EBI-713635;
O43167:ZBTB24; NbExp=3; IntAct=EBI-10183342, EBI-744471;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11161790}.
Nucleus {ECO:0000269|PubMed:11161790}. Note=Associates with the
nuclear body. Colocalizes with SUMO1 and SENP2 in nuclear speckles
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:27453576}. Nucleus
{ECO:0000269|PubMed:27453576}. Note=Predominantly localized in the
nucleus in nuclear paraspeckles. {ECO:0000269|PubMed:27453576}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm
{ECO:0000269|PubMed:27453576}. Nucleus
{ECO:0000269|PubMed:27453576}. Note=Predominantly localized in the
cytoplasm in the absence of interaction with isoform 1 and isoform
2. In presence of isoform 1 or isoform 2, translocates from the
cytoplasm into nuclear paraspeckles.
{ECO:0000269|PubMed:27453576}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=BCL11A-XL, BCL11A eXtra long form;
IsoId=Q9H165-1; Sequence=Displayed;
Note=Expressed in fetal and adult brain, and in the plasmacytoid
dendritic cell. Partitions into the nuclear matrix and
colocalizes with BCL6 in nuclear paraspeckles.
{ECO:0000269|PubMed:16704730};
Name=2; Synonyms=BCL11A-L, BCL11A long form;
IsoId=Q9H165-2; Sequence=VSP_009554, VSP_009555;
Note=Predominantly localized in the nucleus in nuclear
paraspeckles. Variant in position: 47:T->P (in IDPFH, de novo
mutation, loss of function in transactivation of transcription,
reduces the interaction between isoform 2 and isoform 3,
disrupts the nuclear paraspeckle distribution of isoform 2 and
isoform 3). Variant in position: 48:C->F (in IDPFH, de novo
mutation, loss of function in transactivation of transcription,
reduces the interaction between isoform 2 and isoform 3,
disrupts the nuclear paraspeckle distribution of isoform 2 and
isoform 3). Variant in position: 66:H->Q (in IDPFH, de novo
mutation, loss of function in transactivation of transcription,
reduces the interaction between isoform 2 and isoform 3,
disrupts the nuclear paraspeckle distribution of isoform 2 and
isoform 3). {ECO:0000269|PubMed:16704730};
Name=3; Synonyms=BCL11A-S, BCL11A short form;
IsoId=Q9H165-3; Sequence=VSP_009550, VSP_009552;
Note=Predominantly localized in the cytoplasm in the absence of
interaction with isoform 1 and isoform 2. In presence of isoform
1 or isoform 2, translocates from the cytoplasm into nuclear
paraspeckles. Variant in position: 47:T->P (in IDPFH, de novo
mutation, loss of function transactivation of transcription,
reduces the interaction between isoform 2 and isoform 3,
disrupts the nuclear paraspeckle distribution of isoform 2 and
isoform 3). Variant in position: 48:C->F (in IDPFH, de novo
mutation, loss of function in transactivation of transcription,
reduces the interaction between isoform 2 and isoform 3,
disrupts the nuclear paraspeckle distribution of isoform 2 and
isoform 3). Variant in position: 66:H->Q (in IDPFH, de novo
mutation, loss of function in transactivation of transcription,
reduces the interaction between isoform 2 and isoform 3,
disrupts the nuclear paraspeckle distribution of isoform 2 and
isoform 3). {ECO:0000269|PubMed:16704730};
Name=6;
IsoId=Q9H165-6; Sequence=VSP_009548;
Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
with G-Cter in SUMO2) at position 123.
{ECO:0000244|PubMed:28112733};
Name=7; Synonyms=BCL11A-XS, BCL11A eXtra short form;
IsoId=Q9H165-8; Sequence=VSP_058656, VSP_058657;
-!- TISSUE SPECIFICITY: Expressed at high levels in brain, spleen
thymus, bone marrow and testis. Expressed in CD34-positive myeloid
precursor cells, B-cells, monocytes and megakaryocytes. Expression
is tightly regulated during B-cell development.
{ECO:0000269|PubMed:11161790, ECO:0000269|PubMed:11719382}.
-!- DOMAIN: The N-terminus is involved in protein dimerization and in
transactivation of transcription. {ECO:0000269|PubMed:27453576}.
-!- PTM: Sumoylated with SUMO1. {ECO:0000250|UniProtKB:Q9QYE3}.
-!- POLYMORPHISM: Genetic variation in BCL11A underlies the fetal
hemoglobin quantitative trait locus 5 [MIM:142335]. It is
associated with quantitative variation in the production of F
cells, that is erythrocytes containing measurable amounts of fetal
hemoglobin (HbF). In healthy adults, HbF is present at residual
levels (less than 0.6% of total hemoglobin) with over twenty-fold
variation. Ten to fifteen percent of adults in the upper tail of
the distribution have HbF levels between 0.8% and 5.0%, a
condition referred to as heterocellular hereditary persistence of
fetal hemoglobin (hHPFH). Although these HbF levels are modest in
otherwise healthy individuals, interaction of hHPFH with beta
thalassemia or sickle cell disease can increase HbF output in
these individuals to levels that are clinically beneficial.
{ECO:0000269|PubMed:17767159}.
-!- DISEASE: Note=Chromosomal aberrations involving BCL11A may be a
cause of lymphoid malignancies. Translocation t(2;14)(p13;q32.3)
causes BCL11A deregulation and amplification.
{ECO:0000269|PubMed:11719382}.
-!- DISEASE: Intellectual developmental disorder with persistence of
fetal hemoglobin (IDPFH) [MIM:617101]: An autosomal dominant
disorder characterized by delayed psychomotor development,
intellectual disability, variable dysmorphic features, including
microcephaly, downslanting palpebral fissures, strabismus, and
external ear abnormalities, and asymptomatic persistence of fetal
hemoglobin. {ECO:0000269|PubMed:27453576}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
{ECO:0000269|PubMed:27453576}.
-!- SEQUENCE CAUTION:
Sequence=AAG49025.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
Sequence=BAB47438.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCL11AID391.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ404611; CAC17723.1; -; mRNA.
EMBL; AJ404612; CAC17724.1; -; mRNA.
EMBL; AJ404613; CAC17725.1; -; mRNA.
EMBL; AY228763; AAO88272.1; -; mRNA.
EMBL; AB058712; BAB47438.1; ALT_INIT; mRNA.
EMBL; AY692278; AAU04557.1; -; mRNA.
EMBL; AC007381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC009970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471053; EAX00035.1; -; Genomic_DNA.
EMBL; CH471053; EAX00040.1; -; Genomic_DNA.
EMBL; CH471053; EAX00041.1; -; Genomic_DNA.
EMBL; BC021098; AAH21098.1; -; mRNA.
EMBL; AF080216; AAG49025.1; ALT_SEQ; mRNA.
EMBL; AK001035; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS1861.1; -. [Q9H165-2]
CCDS; CCDS1862.1; -. [Q9H165-1]
CCDS; CCDS46295.1; -. [Q9H165-3]
RefSeq; NP_060484.2; NM_018014.3. [Q9H165-2]
RefSeq; NP_075044.2; NM_022893.3. [Q9H165-1]
RefSeq; NP_612569.1; NM_138559.1. [Q9H165-3]
RefSeq; XP_011531211.1; XM_011532909.1. [Q9H165-1]
RefSeq; XP_016859823.1; XM_017004334.1. [Q9H165-6]
UniGene; Hs.370549; -.
ProteinModelPortal; Q9H165; -.
SMR; Q9H165; -.
BioGrid; 119737; 32.
DIP; DIP-45629N; -.
IntAct; Q9H165; 20.
STRING; 9606.ENSP00000338774; -.
iPTMnet; Q9H165; -.
PhosphoSitePlus; Q9H165; -.
BioMuta; BCL11A; -.
DMDM; 44887724; -.
EPD; Q9H165; -.
MaxQB; Q9H165; -.
PaxDb; Q9H165; -.
PeptideAtlas; Q9H165; -.
PRIDE; Q9H165; -.
DNASU; 53335; -.
Ensembl; ENST00000335712; ENSP00000338774; ENSG00000119866. [Q9H165-1]
Ensembl; ENST00000356842; ENSP00000349300; ENSG00000119866. [Q9H165-2]
Ensembl; ENST00000358510; ENSP00000351307; ENSG00000119866. [Q9H165-6]
Ensembl; ENST00000359629; ENSP00000352648; ENSG00000119866. [Q9H165-3]
Ensembl; ENST00000409351; ENSP00000487844; ENSG00000119866. [Q9H165-8]
GeneID; 53335; -.
KEGG; hsa:53335; -.
UCSC; uc002sab.4; human. [Q9H165-1]
CTD; 53335; -.
DisGeNET; 53335; -.
EuPathDB; HostDB:ENSG00000119866.20; -.
GeneCards; BCL11A; -.
HGNC; HGNC:13221; BCL11A.
HPA; CAB014891; -.
HPA; HPA029003; -.
MalaCards; BCL11A; -.
MIM; 142335; phenotype.
MIM; 606557; gene.
MIM; 617101; phenotype.
neXtProt; NX_Q9H165; -.
OpenTargets; ENSG00000119866; -.
Orphanet; 46532; Hereditary persistence of fetal hemoglobin - beta-thalassemia.
PharmGKB; PA25300; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00530000063542; -.
HOGENOM; HOG000088605; -.
HOVERGEN; HBG050673; -.
InParanoid; Q9H165; -.
KO; K22045; -.
OMA; GEGRFPP; -.
OrthoDB; EOG091G160N; -.
PhylomeDB; Q9H165; -.
TreeFam; TF318131; -.
SIGNOR; Q9H165; -.
ChiTaRS; BCL11A; human.
GeneWiki; BCL11A; -.
GenomeRNAi; 53335; -.
PRO; PR:Q9H165; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000119866; -.
CleanEx; HS_BCL11A; -.
ExpressionAtlas; Q9H165; baseline and differential.
Genevisible; Q9H165; HS.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; TAS:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl.
GO; GO:0030517; P:negative regulation of axon extension; ISS:BHF-UCL.
GO; GO:2000173; P:negative regulation of branching morphogenesis of a nerve; IEA:Ensembl.
GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:BHF-UCL.
GO; GO:2000171; P:negative regulation of dendrite development; IMP:BHF-UCL.
GO; GO:1903860; P:negative regulation of dendrite extension; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:BHF-UCL.
GO; GO:1904800; P:negative regulation of neuron remodeling; IEA:Ensembl.
GO; GO:0032463; P:negative regulation of protein homooligomerization; IC:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
GO; GO:0048672; P:positive regulation of collateral sprouting; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
GO; GO:0050773; P:regulation of dendrite development; IMP:BHF-UCL.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 6.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
1: Evidence at protein level;
Alternative splicing; Chromosomal rearrangement; Complete proteome;
Cytoplasm; Disease mutation; Isopeptide bond; Mental retardation;
Metal-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 835 B-cell lymphoma/leukemia 11A.
/FTId=PRO_0000047102.
ZN_FING 170 193 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 377 399 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 405 429 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 742 764 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 770 792 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 800 823 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 1 210 Required for nuclear body formation and
for SUMO1 recruitment. {ECO:0000250}.
COMPBIAS 260 373 Pro-rich.
COMPBIAS 481 509 Glu-rich.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QYE3}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 271 271 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9QYE3}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QYE3}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QYE3}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QYE3}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 625 625 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 630 630 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 701 701 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
CROSSLNK 123 123 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 164 164 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 620 620 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 634 634 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q9QYE3}.
CROSSLNK 833 833 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 129 163 DKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGIC -> G
(in isoform 6). {ECO:0000303|Ref.2}.
/FTId=VSP_009548.
VAR_SEQ 129 142 DKLLHWRGLSSPRS -> AQTELEDVFVYLMV (in
isoform 7).
/FTId=VSP_058656.
VAR_SEQ 143 835 Missing (in isoform 7).
/FTId=VSP_058657.
VAR_SEQ 212 243 GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI -> LHTPP
FGVVPRELKMCGSFRMEAREPLSSEKI (in isoform
3). {ECO:0000303|PubMed:11719382}.
/FTId=VSP_009550.
VAR_SEQ 244 835 Missing (in isoform 3).
{ECO:0000303|PubMed:11719382}.
/FTId=VSP_009552.
VAR_SEQ 745 773 EYCGKVFKNCSNLTVHRRSHTGERPYKCE -> SSHTPIRR
STQRAQDVWQFSDGSSRALKF (in isoform 2).
{ECO:0000303|PubMed:11347906,
ECO:0000303|PubMed:11719382,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_009554.
VAR_SEQ 774 835 Missing (in isoform 2).
{ECO:0000303|PubMed:11347906,
ECO:0000303|PubMed:11719382,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_009555.
VARIANT 47 47 T -> P (in IDPFH; de novo mutation; loss
of function in transactivation of
transcription; reduces the interaction
between isoform 2 and isoform 3; disrupts
the nuclear paraspeckle distribution of
isoform 2 and isoform 3).
{ECO:0000269|PubMed:27453576}.
/FTId=VAR_076921.
VARIANT 48 48 C -> F (in IDPFH; de novo mutation; loss
of function in transactivation of
transcription; reduces the interaction
between isoform 2 and isoform 3; disrupts
the nuclear paraspeckle distribution of
isoform 2 and isoform 3).
{ECO:0000269|PubMed:27453576}.
/FTId=VAR_076922.
VARIANT 66 66 H -> Q (in IDPFH; de novo mutation; loss
of function in transactivation of
transcription; reduces the interaction
between isoform 2 and isoform 3; disrupts
the nuclear paraspeckle distribution of
isoform 2 and isoform 3).
{ECO:0000269|PubMed:27453576}.
/FTId=VAR_076923.
VARIANT 142 142 S -> F (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035553.
CONFLICT 119 119 G -> R (in Ref. 1; CAC17723/CAC17724/
CAC17725). {ECO:0000305}.
CONFLICT 316 316 S -> F (in Ref. 7; AAG49025).
{ECO:0000305}.
CONFLICT 386 386 F -> L (in Ref. 7; AAG49025).
{ECO:0000305}.
CONFLICT 522 532 Missing (in Ref. 7; AAG49025).
{ECO:0000305}.
CONFLICT 648 648 A -> T (in Ref. 1; CAC17723/CAC17724).
{ECO:0000305}.
CONFLICT 653 653 E -> D (in Ref. 7; AAG49025).
{ECO:0000305}.
CONFLICT 730 730 P -> T (in Ref. 1; CAC17723/CAC17724).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
EIAAB47541 Ecotropic viral integration site 3 protein,Evi3,Mouse,Mus musculus,Zfp521,Zinc finger protein 521,Znf521
E0890b Human ELISA Kit FOR Ecotropic viral integration site 5 protein homolog 96T
EIAAB13419 Ecotropic viral integration site 5 protein homolog,EVI5,EVI-5,Homo sapiens,Human,NB4S,Neuroblastoma stage 4S gene protein
CSB-EL007867HU Human Ecotropic viral integration site 5 protein homolog(EVI5) ELISA kit 96T
CSB-EL007867MO Mouse Ecotropic viral integration site 5 protein homolog(EVI5) ELISA kit 96T
CSB-EL007867HU Human Ecotropic viral integration site 5 protein homolog(EVI5) ELISA kit SpeciesHuman 96T
CSB-EL007867MO Mouse Ecotropic viral integration site 5 protein homolog(EVI5) ELISA kit SpeciesMouse 96T
EIAAB47660 CTCL-associated antigen se33-1,Cutaneous T-cell lymphoma-associated antigen se33-1,Homo sapiens,Human,NP220,Nuclear protein 220,ZFML,Zinc finger matrin-like protein,Zinc finger protein 638,ZNF638
EIAAB13418 Ecotropic viral integration site 2B protein homolog,EVDB,EVI2B,EVI-2B,Homo sapiens,Human,Protein EVI2B
EIAAB13415 Ecotropic viral integration site 2A protein homolog,EVDA,EVI2,EVI2A,EVI-2A,Homo sapiens,Human,Protein EVI2A
abx111190 Polyclonal Rabbit B-Cell Cll per Lymphoma 11A (Zinc Finger Protein) Antibody 50 μl
EIAAB47457 Early B-cell factor-associated zinc finger protein,Ebfaz,Kiaa0760,Mouse,Mus musculus,Nur12,Oaz,Olf1_EBF-associated zinc finger protein,Smad- and Olf-interacting zinc finger protein,Zfp423,Zinc finger
EIAAB13421 Ecotropic viral integration site 5-like protein,EVI5L,EVI5-like protein,Homo sapiens,Human
EIAAB47355 Homo sapiens,Human,Neurotrophin receptor-interacting factor homolog,SP2114,Zf2,Zinc finger protein 274,Zinc finger protein HFB101,Zinc finger protein with KRAB and SCAN domains 19,Zinc finger protein
EIAAB13420 Ecotropic viral integration site 5 protein,Evi5,EVI-5,Mouse,Mus musculus
'CS20-00-003 Human Lymphoma tissue array (Plasmacytic lymphoma B-cell Large B-cell Burkitts lymphoma T-lymphoblastoma, etc.) tissues 7 x 9
EIAAB47340 BMZF5,BMZF-5,Bone marrow zinc finger 5,HD-ZNF1,Hematopoietic cell-derived zinc finger protein 1,Homo sapiens,Human,Zinc finger protein 254,Zinc finger protein 539,Zinc finger protein 91-like,ZNF254,ZN
25-496 BCL11A Is a C2H2 type zinc-finger protein by its similarity to the mouse Bcl11a_Evi9 protein. The corresponding mouse gene is a common site of retroviral integration in myeloid leukemia, and may funct 0.05 mg
EVI5_MOUSE ELISA Kit FOR Ecotropic viral integration site 5 protein; organism: Mouse; gene name: Evi5 96T
E1138m Human ELISA Kit FOR T-cell leukemia per lymphoma protein 1B 96T
EIAAB13416 Ecotropic viral integration site 2A protein,Evi2,Evi-2,Evi2a,EVI-2A,Evi-2a,Mouse,Mus musculus,Protein EVI2A
EIAAB13417 Ecotropic viral integration site 2B protein,Evi2b,EVI-2B,Mouse,Mus musculus,Protein EVI2B
UT-E04512 Human T-Cell Leukemia Lymphoma Protein 1A (TCL1A) ELISA Kit 96T
H4294 T-cell leukemia lymphoma protein 1A (TCL1A), Human, ELISA Kit 96T
UB-E04512 Human T-Cell Leukemia per Lymphoma Protein 1A(TCL1A)ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur