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Q16520

- BATF_HUMAN

UniProt

Q16520 - BATF_HUMAN

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Protein

Basic leucine zipper transcriptional factor ATF-like

Gene

BATF

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

Functioni

AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8+ dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8+ dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8+ T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs (By similarity).By similarity

GO - Molecular functioni

  1. sequence-specific DNA binding Source: UniProtKB
  2. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. cytokine production Source: UniProtKB
  3. defense response to protozoan Source: UniProtKB
  4. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  5. hematopoietic stem cell differentiation Source: UniProtKB
  6. isotype switching Source: UniProtKB
  7. lymphoid progenitor cell differentiation Source: UniProtKB
  8. myeloid dendritic cell differentiation Source: UniProtKB
  9. T-helper 17 cell differentiation Source: UniProtKB
  10. T-helper 17 cell lineage commitment Source: UniProtKB
  11. T-helper 2 cell differentiation Source: UniProtKB
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Basic leucine zipper transcriptional factor ATF-like
Alternative name(s):
B-cell-activating transcription factor
Short name:
B-ATF
SF-HT-activated gene 2 protein
Short name:
SFA-2
Gene namesi
Name:BATF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:958. BATF.

Subcellular locationi

Nucleus PROSITE-ProRule annotation. Cytoplasm By similarity
Note: Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25268.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 125125Basic leucine zipper transcriptional factor ATF-likePRO_0000076595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineBy similarity
Modified residuei48 – 481PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated on serine and threonine residues and at least one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription (By similarity).By similarity
Phosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ16520.
PaxDbiQ16520.
PRIDEiQ16520.

PTM databases

PhosphoSiteiQ16520.

Expressioni

Tissue specificityi

Expressed at highest levels in lung, and at lower levels in placenta, liver, kidney, spleen, and peripheral blood. Detected in SW480 colorectal cancer cell line and several hematopoietic tumor cell lines, including Raji Burkitt's lymphoma. Strongly expressed in mature B- and T-lymphocytes. Also expressed in moderate levels in lymph node and appendix and at low levels in thymus and bone marrow (PubMed:10777209).3 Publications

Inductioni

Up-regulated by PDCD1 following infection by HIV-1 virus, leading to inhibit T-cell functions and exhaust T-cells. Up-regulated by Epstein-Barr virus (EBV) protein EBNA2 following infection by EBV.2 Publications

Gene expression databases

BgeeiQ16520.
CleanExiHS_BATF.
ExpressionAtlasiQ16520. baseline and differential.
GenevestigatoriQ16520.

Interactioni

Subunit structurei

Heterodimer; mainly heterodimerizes with JUNB. The BATF-JUNB heterodimer interacts with IRF4 and IRF8. Interacts (via bZIP domain) with IRF4 and IRF8; the interaction is direct (By similarity). Also forms heterodimers with JUN and JUND. Also interacts with IFI35.By similarity2 Publications

Protein-protein interaction databases

BioGridi115792. 18 interactions.
IntActiQ16520. 4 interactions.
MINTiMINT-1440747.
STRINGi9606.ENSP00000286639.

Structurei

3D structure databases

ProteinModelPortaliQ16520.
SMRiQ16520. Positions 32-77.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 8964bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 5023Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni54 – 7522Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG257556.
GeneTreeiENSGT00390000016869.
HOGENOMiHOG000236325.
HOVERGENiHBG039173.
InParanoidiQ16520.
KOiK09034.
OMAiEEMKHFT.
OrthoDBiEOG7H794S.
PhylomeDBiQ16520.
TreeFamiTF332340.

Family and domain databases

InterProiIPR000837. AP-1.
IPR004827. bZIP.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSiPR00042. LEUZIPPRFOS.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q16520-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK
60 70 80 90 100
ADTLHLESED LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST
110 120
PSPPEVVYSA HAFHQPHVSS PRFQP
Length:125
Mass (Da):14,120
Last modified:November 1, 1996 - v1
Checksum:i7FD633C6F1963DF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15460 mRNA. Translation: AAC50314.1.
D42106 mRNA. Translation: BAA07686.1.
AF016898 Genomic DNA. Translation: AAC78243.1.
AC007182 Genomic DNA. Translation: AAD51372.1.
BC032294 mRNA. Translation: AAH32294.1.
CCDSiCCDS9843.1.
PIRiJC4799.
RefSeqiNP_006390.1. NM_006399.3.
UniGeneiHs.509964.

Genome annotation databases

EnsembliENST00000286639; ENSP00000286639; ENSG00000156127.
GeneIDi10538.
KEGGihsa:10538.
UCSCiuc001xrr.3. human.

Polymorphism databases

DMDMi32171340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15460 mRNA. Translation: AAC50314.1 .
D42106 mRNA. Translation: BAA07686.1 .
AF016898 Genomic DNA. Translation: AAC78243.1 .
AC007182 Genomic DNA. Translation: AAD51372.1 .
BC032294 mRNA. Translation: AAH32294.1 .
CCDSi CCDS9843.1.
PIRi JC4799.
RefSeqi NP_006390.1. NM_006399.3.
UniGenei Hs.509964.

3D structure databases

ProteinModelPortali Q16520.
SMRi Q16520. Positions 32-77.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115792. 18 interactions.
IntActi Q16520. 4 interactions.
MINTi MINT-1440747.
STRINGi 9606.ENSP00000286639.

PTM databases

PhosphoSitei Q16520.

Polymorphism databases

DMDMi 32171340.

Proteomic databases

MaxQBi Q16520.
PaxDbi Q16520.
PRIDEi Q16520.

Protocols and materials databases

DNASUi 10538.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000286639 ; ENSP00000286639 ; ENSG00000156127 .
GeneIDi 10538.
KEGGi hsa:10538.
UCSCi uc001xrr.3. human.

Organism-specific databases

CTDi 10538.
GeneCardsi GC14P075988.
HGNCi HGNC:958. BATF.
MIMi 612476. gene.
neXtProti NX_Q16520.
PharmGKBi PA25268.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG257556.
GeneTreei ENSGT00390000016869.
HOGENOMi HOG000236325.
HOVERGENi HBG039173.
InParanoidi Q16520.
KOi K09034.
OMAi EEMKHFT.
OrthoDBi EOG7H794S.
PhylomeDBi Q16520.
TreeFami TF332340.

Miscellaneous databases

GeneWikii BATF_(gene).
GenomeRNAii 10538.
NextBioi 39981.
PROi Q16520.
SOURCEi Search...

Gene expression databases

Bgeei Q16520.
CleanExi HS_BATF.
ExpressionAtlasi Q16520. baseline and differential.
Genevestigatori Q16520.

Family and domain databases

InterProi IPR000837. AP-1.
IPR004827. bZIP.
[Graphical view ]
Pfami PF00170. bZIP_1. 1 hit.
[Graphical view ]
PRINTSi PR00042. LEUZIPPRFOS.
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "B-ATF: a novel human bZIP protein that associates with members of the AP-1 transcription factor family."
    Dorsey M.J., Tae H.-J., Sollenberger K.G., Mascarenhas N.T., Johansen L.M., Taparowsky E.J.
    Oncogene 11:2255-2265(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH JUN PROTEINS, TISSUE SPECIFICITY.
  2. "SFA-2, a novel bZIP transcription factor induced by human T-cell leukemia virus type I, is highly expressed in mature lymphocytes."
    Hasegawa H., Utsunomiya Y., Kishimoto K., Tange Y., Yasukawa M., Fujita S.
    Biochem. Biophys. Res. Commun. 222:164-170(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Genomic organization of human B-ATF, a target for regulation by EBV and HTLV-1."
    Meyer N.P., Johansen L.M., Tae H.-J., Budde P.P., Williams K.L., Taparowsky E.J.
    Mamm. Genome 9:849-852(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Melanoma.
  6. "IFP 35 forms complexes with B-ATF, a member of the AP1 family of transcription factors."
    Wang X., Johansen L.M., Tae H.-J., Taparowsky E.J.
    Biochem. Biophys. Res. Commun. 229:316-322(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IFI35.
  7. "B-ATF functions as a negative regulator of AP-1 mediated transcription and blocks cellular transformation by Ras and Fos."
    Echlin D.R., Tae H.-J., Mitin N., Taparowsky E.J.
    Oncogene 19:1752-1763(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. Cited for: INDUCTION.
  9. Cited for: INDUCTION.

Entry informationi

Entry nameiBATF_HUMAN
AccessioniPrimary (citable) accession number: Q16520
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 127 of the entry and version 1 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3