Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

B-cell lymphoma/leukemia 11A

Gene

BCL11A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

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 by RNA polymerase II Source: NTNU_SB
  • neurogenesis Source: GO_Central
  • positive regulation of collateral sprouting Source: BHF-UCL
  • positive regulation of neuron projection development Source: BHF-UCL
  • positive regulation of transcription by RNA polymerase II 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

Keywordsi

Molecular functionRepressor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

SIGNORiQ9H165

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

EuPathDBiHostDB:ENSG00000119866.20
HGNCiHGNC:13221 BCL11A
MIMi606557 gene
neXtProtiNX_Q9H165

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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.1 Publication
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 PublicationCorresponds to variant dbSNP:rs886037864EnsemblClinVar.1
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 PublicationCorresponds to variant dbSNP:rs886037865EnsemblClinVar.1
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 PublicationCorresponds to variant dbSNP:rs886037866EnsemblClinVar.1
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
Cross-linki164Glycyl 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
Cross-linki620Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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
Isoform 6 (identifier: Q9H165-6)
Cross-linki123Glycyl 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
ProteomicsDBi80362
80363 [Q9H165-2]
80364 [Q9H165-3]
80367 [Q9H165-6]

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

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi119737, 31 interactors
DIPiDIP-45629N
IntActiQ9H165, 21 interactors
STRINGi9606.ENSP00000338774

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5VTBX-ray2.40B2-16[»]
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

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
KOiK22045
OMAiGEGRFPP
OrthoDBiEOG091G160N
PhylomeDBiQ9H165
TreeFamiTF318131

Family and domain databases

InterProiView protein in InterPro
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 6 hits
SUPFAMiSSF57667 SSF57667, 3 hits
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 6 hits
PS50157 ZINC_FINGER_C2H2_2, 6 hits

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 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 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 AAG49025 differs from that shown.Curated
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 conflicti522 – 532Missing in AAG49025 (PubMed:11161790).CuratedAdd BLAST11
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 PublicationCorresponds to variant dbSNP:rs886037864EnsemblClinVar.1
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 PublicationCorresponds to variant dbSNP:rs886037865EnsemblClinVar.1
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 PublicationCorresponds to variant dbSNP:rs886037866EnsemblClinVar.1
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_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_009550212 – 243GIPSG…NLLRI → LHTPPFGVVPRELKMCGSFR MEAREPLSSEKI in isoform 3. 1 PublicationAdd BLAST32
Alternative sequenceiVSP_009552244 – 835Missing in isoform 3. 1 PublicationAdd BLAST592
Alternative sequenceiVSP_009554745 – 773EYCGK…PYKCE → SSHTPIRRSTQRAQDVWQFS DGSSRALKF in isoform 2. 3 PublicationsAdd BLAST29
Alternative sequenceiVSP_009555774 – 835Missing in isoform 2. 3 PublicationsAdd BLAST62

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
AF080216 mRNA Translation: AAG49025.1 Sequence problems.
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 [Q9H165-6]
ENST00000356842; ENSP00000349300; ENSG00000119866 [Q9H165-2]
ENST00000359629; ENSP00000352648; ENSG00000119866 [Q9H165-3]
ENST00000409351; ENSP00000487844; ENSG00000119866 [Q9H165-8]
ENST00000642384; ENSP00000496168; ENSG00000119866 [Q9H165-1]
GeneIDi53335
KEGGihsa:53335
UCSCiuc002sab.4 human [Q9H165-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiBC11A_HUMAN
AccessioniPrimary (citable) accession number: Q9H165
Secondary accession number(s): D6W5D7
, Q66LN6, Q86W14, Q8WU92, Q96JL6, Q9H163, Q9H164, Q9H3G9, Q9NWA7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: June 20, 2018
This is version 161 of the entry and version 2 of the sequence. See 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

3D-structure, Complete proteome, Reference proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health