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Protein

B-cell lymphoma/leukemia 11A

Gene

BCL11A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).2 PublicationsBy similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri170 – 193C2H2-type 1PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri377 – 399C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri405 – 429C2H2-type 3PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri742 – 764C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri770 – 792C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri800 – 823C2H2-type 6PROSITE-ProRule annotationAdd BLAST24

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB

GO - Biological processi

  • negative regulation of axon extension Source: BHF-UCL
  • negative regulation of collateral sprouting Source: BHF-UCL
  • negative regulation of dendrite development Source: BHF-UCL
  • negative regulation of neuron projection development Source: BHF-UCL
  • negative regulation of protein homooligomerization Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • positive regulation of collateral sprouting Source: BHF-UCL
  • positive regulation of neuron projection development Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein sumoylation Source: UniProtKB
  • regulation of dendrite development Source: BHF-UCL
  • signal transduction Source: GO_Central
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
B-cell lymphoma/leukemia 11A
Short name:
BCL-11A
Alternative name(s):
B-cell CLL/lymphoma 11A
COUP-TF-interacting protein 1
Ecotropic viral integration site 9 protein homolog
Short name:
EVI-9
Zinc finger protein 856
Gene namesi
Name:BCL11A
Synonyms:CTIP1, EVI9, KIAA1809, ZNF856
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:13221. BCL11A.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Associates with the nuclear body. Colocalizes with SUMO1 and SENP2 in nuclear speckles (By similarity).By similarity
Isoform 2 :
Isoform 3 :

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Chromosomal aberrations involving BCL11A may be a cause of lymphoid malignancies. Translocation t(2;14)(p13;q32.3) causes BCL11A deregulation and amplification.

Intellectual developmental disorder with persistence of fetal hemoglobin (IDPFH)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Disease descriptionAn 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.
See also OMIM:617101
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07692147T → 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. 1 Publication1
Natural variantiVAR_07692248C → 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. 1 Publication1
Natural variantiVAR_07692366H → 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. 1 Publication1
Isoform 2 (identifier: Q9H165-2)
Natural varianti47T → 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. 1 Publication1
Natural varianti48C → 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. 1 Publication1
Natural varianti66H → 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. 1 Publication1
Isoform 3 (identifier: Q9H165-3)
Natural varianti47T → 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. 1 Publication1
Natural varianti48C → 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. 1 Publication1
Natural varianti66H → 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. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi53335.
MalaCardsiBCL11A.
MIMi142335. phenotype.
617101. phenotype.
OpenTargetsiENSG00000119866.
Orphaneti46532. Hereditary persistence of fetal hemoglobin - beta-thalassemia.
PharmGKBiPA25300.

Polymorphism and mutation databases

BioMutaiBCL11A.
DMDMi44887724.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000471021 – 835B-cell lymphoma/leukemia 11AAdd BLAST835

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei86PhosphoserineBy similarity1
Cross-linki123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei205PhosphoserineCombined sources1
Modified residuei271Asymmetric dimethylarginineBy similarity1
Modified residuei332PhosphoserineCombined sources1
Modified residuei337PhosphoserineBy similarity1
Modified residuei446PhosphoserineBy similarity1
Modified residuei447PhosphoserineBy similarity1
Modified residuei608PhosphoserineCombined sources1
Modified residuei625PhosphoserineCombined sources1
Modified residuei630PhosphoserineCombined sources1
Cross-linki634Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei701PhosphothreonineCombined sources1
Cross-linki833Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Sumoylated with SUMO1.By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9H165.
MaxQBiQ9H165.
PaxDbiQ9H165.
PeptideAtlasiQ9H165.
PRIDEiQ9H165.

PTM databases

iPTMnetiQ9H165.
PhosphoSitePlusiQ9H165.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiENSG00000119866.
CleanExiHS_BCL11A.
ExpressionAtlasiQ9H165. baseline and differential.
GenevisibleiQ9H165. HS.

Organism-specific databases

HPAiCAB014891.
HPA029003.

Interactioni

Subunit structurei

Interacts with TFCOUP1, PIAS3, ARP1 and EAR2 (By similarity). Isoform 1, isoform 2 and isoform 3 form homodimers and heterodimers (PubMed:27453576).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GMCL1P1Q8NEA95EBI-10183342,EBI-745707
LMO1P258003EBI-10183342,EBI-8639312
NCK2O436395EBI-10183342,EBI-713635
ZBTB24O431673EBI-10183342,EBI-744471

GO - Molecular functioni

  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi119737. 32 interactors.
IntActiQ9H165. 18 interactors.
STRINGi9606.ENSP00000338774.

Structurei

3D structure databases

ProteinModelPortaliQ9H165.
SMRiQ9H165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 210Required for nuclear body formation and for SUMO1 recruitmentBy similarityAdd BLAST210

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi260 – 373Pro-richAdd BLAST114
Compositional biasi481 – 509Glu-richAdd BLAST29

Domaini

The N-terminus is involved in protein dimerization and in transactivation of transcription.1 Publication

Sequence similaritiesi

Contains 6 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri170 – 193C2H2-type 1PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri377 – 399C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri405 – 429C2H2-type 3PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri742 – 764C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri770 – 792C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri800 – 823C2H2-type 6PROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00530000063542.
HOGENOMiHOG000088605.
HOVERGENiHBG050673.
InParanoidiQ9H165.
OMAiGEGRFPP.
OrthoDBiEOG091G160N.
PhylomeDBiQ9H165.
TreeFamiTF318131.

Family and domain databases

Gene3Di3.30.160.60. 4 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 6 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 6 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H165-1) [UniParc]FASTAAdd to basket
Also known as: BCL11A-XL, BCL11A eXtra long form

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSRRKQGKPQ HLSKREFSPE PLEAILTDDE PDHGPLGAPE GDHDLLTCGQ
60 70 80 90 100
CQMNFPLGDI LIFIEHKRKQ CNGSLCLEKA VDKPPSPSPI EMKKASNPVE
110 120 130 140 150
VGIQVTPEDD DCLSTSSRGI CPKQEHIADK LLHWRGLSSP RSAHGALIPT
160 170 180 190 200
PGMSAEYAPQ GICKDEPSSY TCTTCKQPFT SAWFLLQHAQ NTHGLRIYLE
210 220 230 240 250
SEHGSPLTPR VGIPSGLGAE CPSQPPLHGI HIADNNPFNL LRIPGSVSRE
260 270 280 290 300
ASGLAEGRFP PTPPLFSPPP RHHLDPHRIE RLGAEEMALA THHPSAFDRV
310 320 330 340 350
LRLNPMAMEP PAMDFSRRLR ELAGNTSSPP LSPGRPSPMQ RLLQPFQPGS
360 370 380 390 400
KPPFLATPPL PPLQSAPPPS QPPVKSKSCE FCGKTFKFQS NLVVHRRSHT
410 420 430 440 450
GEKPYKCNLC DHACTQASKL KRHMKTHMHK SSPMTVKSDD GLSTASSPEP
460 470 480 490 500
GTSDLVGSAS SALKSVVAKF KSENDPNLIP ENGDEEEEED DEEEEEEEEE
510 520 530 540 550
EEEELTESER VDYGFGLSLE AARHHENSSR GAVVGVGDES RALPDVMQGM
560 570 580 590 600
VLSSMQHFSE AFHQVLGEKH KRGHLAEAEG HRDTCDEDSV AGESDRIDDG
610 620 630 640 650
TVNGRGCSPG ESASGGLSKK LLLGSPSSLS PFSKRIKLEK EFDLPPAAMP
660 670 680 690 700
NTENVYSQWL AGYAASRQLK DPFLSFGDSR QSPFASSSEH SSENGSLRFS
710 720 730 740 750
TPPGELDGGI SGRSGTGSGG STPHISGPGP GRPSSKEGRR SDTCEYCGKV
760 770 780 790 800
FKNCSNLTVH RRSHTGERPY KCELCNYACA QSSKLTRHMK THGQVGKDVY
810 820 830
KCEICKMPFS VYSTLEKHMK KWHSDRVLNN DIKTE
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.1 Publication
Length:835
Mass (Da):91,197
Last modified:March 1, 2004 - v2
Checksum:iD36A7D0BE6976DCF
GO
Isoform 2 (identifier: Q9H165-2) [UniParc]FASTAAdd to basket
Also known as: BCL11A-L, BCL11A long form

The sequence of this isoform differs from the canonical sequence as follows:
     745-773: EYCGKVFKNCSNLTVHRRSHTGERPYKCE → SSHTPIRRSTQRAQDVWQFSDGSSRALKF
     774-835: Missing.

Note: Predominantly localized in the nucleus in nuclear paraspeckles.1 Publication
Show »
Length:773
Mass (Da):83,860
Checksum:i251E8A1F3EB87956
GO
Isoform 3 (identifier: Q9H165-3) [UniParc]FASTAAdd to basket
Also known as: BCL11A-S, BCL11A short form

The sequence of this isoform differs from the canonical sequence as follows:
     212-243: GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI → LHTPPFGVVPRELKMCGSFRMEAREPLSSEKI
     244-835: Missing.

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.1 Publication
Show »
Length:243
Mass (Da):26,866
Checksum:i5B24FE61F3831226
GO
Isoform 4 (identifier: Q9H165-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSKGTDEDIFSGVSFFLTRLSRCEPSRRPPAPQPT
     522-532: Missing.
     745-773: EYCGKVFKNCSNLTVHRRSHTGERPYKCE → SSHTPIRRSTQRAQDVWQFSDGSSRALKF
     774-835: Missing.

Show »
Length:796
Mass (Da):86,419
Checksum:iDE7726EEECF40070
GO
Isoform 5 (identifier: Q9H165-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSKGTDEDIFSGVSFFLTRLSRCEPSRRPPAPQPT
     211-239: VGIPSGLGAECPSQPPLHGIHIADNNPFN → CSSHTPIRRSTQRAQDVWQFSDGSRALKF
     240-835: Missing.

Show »
Length:273
Mass (Da):30,251
Checksum:i901EB02453006AF7
GO
Isoform 6 (identifier: Q9H165-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     129-163: DKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGIC → G

Show »
Length:801
Mass (Da):87,554
Checksum:i3DFB3B3A0798B567
GO
Isoform 7 (identifier: Q9H165-8) [UniParc]FASTAAdd to basket
Also known as: BCL11A-XS, BCL11A eXtra short form

The sequence of this isoform differs from the canonical sequence as follows:
     129-142: DKLLHWRGLSSPRS → AQTELEDVFVYLMV
     143-835: Missing.

Show »
Length:142
Mass (Da):15,720
Checksum:i135EA16BBA202DB3
GO

Sequence cautioni

The sequence BAB47438 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti119G → R in CAC17723 (PubMed:11719382).Curated1
Sequence conflicti119G → R in CAC17724 (PubMed:11719382).Curated1
Sequence conflicti119G → R in CAC17725 (PubMed:11719382).Curated1
Sequence conflicti316S → F in AAG49025 (PubMed:11161790).Curated1
Sequence conflicti386F → L in AAG49025 (PubMed:11161790).Curated1
Sequence conflicti648A → T in CAC17723 (PubMed:11719382).Curated1
Sequence conflicti648A → T in CAC17724 (PubMed:11719382).Curated1
Sequence conflicti653E → D in AAG49025 (PubMed:11161790).Curated1
Sequence conflicti730P → T in CAC17723 (PubMed:11719382).Curated1
Sequence conflicti730P → T in CAC17724 (PubMed:11719382).Curated1

Polymorphismi

Genetic variation in BCL11A underlies the fetal hemoglobin quantitative trait locus 5 [MIMi: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.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07692147T → 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. 1 Publication1
Natural variantiVAR_07692248C → 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. 1 Publication1
Natural variantiVAR_07692366H → 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. 1 Publication1
Natural variantiVAR_035553142S → F in a breast cancer sample; somatic mutation. 1 Publication1
Isoform 2 (identifier: Q9H165-2)
Natural varianti47T → 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. 1 Publication1
Natural varianti48C → 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. 1 Publication1
Natural varianti66H → 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. 1 Publication1
Isoform 3 (identifier: Q9H165-3)
Natural varianti47T → 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. 1 Publication1
Natural varianti48C → 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. 1 Publication1
Natural varianti66H → 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. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0095471M → MSKGTDEDIFSGVSFFLTRL SRCEPSRRPPAPQPT in isoform 4 and isoform 5. 1 Publication1
Alternative sequenceiVSP_009548129 – 163DKLLH…PQGIC → G in isoform 6. 1 PublicationAdd BLAST35
Alternative sequenceiVSP_058656129 – 142DKLLH…SSPRS → AQTELEDVFVYLMV in isoform 7. Add BLAST14
Alternative sequenceiVSP_058657143 – 835Missing in isoform 7. Add BLAST693
Alternative sequenceiVSP_009549211 – 239VGIPS…NNPFN → CSSHTPIRRSTQRAQDVWQF SDGSRALKF in isoform 5. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_009550212 – 243GIPSG…NLLRI → LHTPPFGVVPRELKMCGSFR MEAREPLSSEKI in isoform 3. 1 PublicationAdd BLAST32
Alternative sequenceiVSP_009551240 – 835Missing in isoform 5. 1 PublicationAdd BLAST596
Alternative sequenceiVSP_009552244 – 835Missing in isoform 3. 1 PublicationAdd BLAST592
Alternative sequenceiVSP_009553522 – 532Missing in isoform 4. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_009554745 – 773EYCGK…PYKCE → SSHTPIRRSTQRAQDVWQFS DGSSRALKF in isoform 2 and isoform 4. 4 PublicationsAdd BLAST29
Alternative sequenceiVSP_009555774 – 835Missing in isoform 2 and isoform 4. 4 PublicationsAdd BLAST62

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080216 mRNA. Translation: AAG49025.1.
AJ404611 mRNA. Translation: CAC17723.1.
AJ404612 mRNA. Translation: CAC17724.1.
AJ404613 mRNA. Translation: CAC17725.1.
AY228763 mRNA. Translation: AAO88272.1.
AB058712 mRNA. Translation: BAB47438.1. Different initiation.
AY692278 mRNA. Translation: AAU04557.1.
AC007381 Genomic DNA. No translation available.
AC009970 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00035.1.
CH471053 Genomic DNA. Translation: EAX00040.1.
CH471053 Genomic DNA. Translation: EAX00041.1.
BC021098 mRNA. Translation: AAH21098.1.
AK001035 mRNA. No translation available.
CCDSiCCDS1861.1. [Q9H165-2]
CCDS1862.1. [Q9H165-1]
CCDS46295.1. [Q9H165-3]
RefSeqiNP_060484.2. NM_018014.3. [Q9H165-2]
NP_075044.2. NM_022893.3. [Q9H165-1]
NP_612569.1. NM_138559.1. [Q9H165-3]
XP_011531211.1. XM_011532909.1. [Q9H165-1]
XP_016859823.1. XM_017004334.1. [Q9H165-6]
UniGeneiHs.370549.

Genome annotation databases

EnsembliENST00000335712; ENSP00000338774; ENSG00000119866. [Q9H165-1]
ENST00000356842; ENSP00000349300; ENSG00000119866. [Q9H165-2]
ENST00000358510; ENSP00000351307; ENSG00000119866. [Q9H165-6]
ENST00000359629; ENSP00000352648; ENSG00000119866. [Q9H165-3]
GeneIDi53335.
KEGGihsa:53335.
UCSCiuc002sab.4. human. [Q9H165-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080216 mRNA. Translation: AAG49025.1.
AJ404611 mRNA. Translation: CAC17723.1.
AJ404612 mRNA. Translation: CAC17724.1.
AJ404613 mRNA. Translation: CAC17725.1.
AY228763 mRNA. Translation: AAO88272.1.
AB058712 mRNA. Translation: BAB47438.1. Different initiation.
AY692278 mRNA. Translation: AAU04557.1.
AC007381 Genomic DNA. No translation available.
AC009970 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00035.1.
CH471053 Genomic DNA. Translation: EAX00040.1.
CH471053 Genomic DNA. Translation: EAX00041.1.
BC021098 mRNA. Translation: AAH21098.1.
AK001035 mRNA. No translation available.
CCDSiCCDS1861.1. [Q9H165-2]
CCDS1862.1. [Q9H165-1]
CCDS46295.1. [Q9H165-3]
RefSeqiNP_060484.2. NM_018014.3. [Q9H165-2]
NP_075044.2. NM_022893.3. [Q9H165-1]
NP_612569.1. NM_138559.1. [Q9H165-3]
XP_011531211.1. XM_011532909.1. [Q9H165-1]
XP_016859823.1. XM_017004334.1. [Q9H165-6]
UniGeneiHs.370549.

3D structure databases

ProteinModelPortaliQ9H165.
SMRiQ9H165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119737. 32 interactors.
IntActiQ9H165. 18 interactors.
STRINGi9606.ENSP00000338774.

PTM databases

iPTMnetiQ9H165.
PhosphoSitePlusiQ9H165.

Polymorphism and mutation databases

BioMutaiBCL11A.
DMDMi44887724.

Proteomic databases

EPDiQ9H165.
MaxQBiQ9H165.
PaxDbiQ9H165.
PeptideAtlasiQ9H165.
PRIDEiQ9H165.

Protocols and materials databases

DNASUi53335.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335712; ENSP00000338774; ENSG00000119866. [Q9H165-1]
ENST00000356842; ENSP00000349300; ENSG00000119866. [Q9H165-2]
ENST00000358510; ENSP00000351307; ENSG00000119866. [Q9H165-6]
ENST00000359629; ENSP00000352648; ENSG00000119866. [Q9H165-3]
GeneIDi53335.
KEGGihsa:53335.
UCSCiuc002sab.4. human. [Q9H165-1]

Organism-specific databases

CTDi53335.
DisGeNETi53335.
GeneCardsiBCL11A.
HGNCiHGNC:13221. BCL11A.
HPAiCAB014891.
HPA029003.
MalaCardsiBCL11A.
MIMi142335. phenotype.
606557. gene.
617101. phenotype.
neXtProtiNX_Q9H165.
OpenTargetsiENSG00000119866.
Orphaneti46532. Hereditary persistence of fetal hemoglobin - beta-thalassemia.
PharmGKBiPA25300.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00530000063542.
HOGENOMiHOG000088605.
HOVERGENiHBG050673.
InParanoidiQ9H165.
OMAiGEGRFPP.
OrthoDBiEOG091G160N.
PhylomeDBiQ9H165.
TreeFamiTF318131.

Miscellaneous databases

ChiTaRSiBCL11A. human.
GeneWikiiBCL11A.
GenomeRNAii53335.
PROiQ9H165.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000119866.
CleanExiHS_BCL11A.
ExpressionAtlasiQ9H165. baseline and differential.
GenevisibleiQ9H165. HS.

Family and domain databases

Gene3Di3.30.160.60. 4 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 6 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 6 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBC11A_HUMAN
AccessioniPrimary (citable) accession number: Q9H165
Secondary accession number(s): D6W5D7
, Q66LN6, Q86W14, Q8WU92, Q96JL6, Q9H163, Q9H164, Q9H3G9, Q9NWA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: November 30, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.