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Q16520 (BATF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:BATF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length125 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.1 Ref.6

Subcellular location

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

Tissue specificity

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 (Ref.7). Ref.1 Ref.2 Ref.7

Induction

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. Ref.8 Ref.9

Post-translational modification

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.

Phosphorylated By similarity.

Sequence similarities

Belongs to the bZIP family.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

T-helper 17 cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

T-helper 17 cell lineage commitment

Inferred from sequence or structural similarity. Source: UniProtKB

T-helper 2 cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

defense response to protozoan

Inferred from sequence or structural similarity. Source: UniProtKB

hematopoietic stem cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

isotype switching

Inferred from sequence or structural similarity. Source: UniProtKB

lymphoid progenitor cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

myeloid dendritic cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionsequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 125125Basic leucine zipper transcriptional factor ATF-like
PRO_0000076595

Regions

Domain26 – 8964bZIP
Region28 – 5023Basic motif By similarity
Region54 – 7522Leucine-zipper By similarity

Amino acid modifications

Modified residue431Phosphoserine By similarity
Modified residue481Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q16520 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7FD633C6F1963DF4

FASTA12514,120
        10         20         30         40         50         60 
MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK ADTLHLESED 

        70         80         90        100        110        120 
LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST PSPPEVVYSA HAFHQPHVSS 


PRFQP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"EBNA2 and activated Notch induce expression of BATF."
Johansen L.M., Deppmann C.D., Erickson K.D., Coffin W.F. III, Thornton T.M., Humphrey S.E., Martin J.M., Taparowsky E.J.
J. Virol. 77:6029-6040(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[9]"Transcriptional analysis of HIV-specific CD8+ T cells shows that PD-1 inhibits T cell function by upregulating BATF."
Quigley M., Pereyra F., Nilsson B., Porichis F., Fonseca C., Eichbaum Q., Julg B., Jesneck J.L., Brosnahan K., Imam S., Russell K., Toth I., Piechocka-Trocha A., Dolfi D., Angelosanto J., Crawford A., Shin H., Kwon D.S. expand/collapse author list , Zupkosky J., Francisco L., Freeman G.J., Wherry E.J., Kaufmann D.E., Walker B.D., Ebert B., Haining W.N.
Nat. Med. 16:1147-1151(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC4799.
RefSeqNP_006390.1. NM_006399.3.
UniGeneHs.509964.

3D structure databases

ProteinModelPortalQ16520.
SMRQ16520. Positions 29-80.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115792. 18 interactions.
IntActQ16520. 4 interactions.
MINTMINT-1440747.
STRING9606.ENSP00000286639.

PTM databases

PhosphoSiteQ16520.

Polymorphism databases

DMDM32171340.

Proteomic databases

PaxDbQ16520.
PRIDEQ16520.

Protocols and materials databases

DNASU10538.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286639; ENSP00000286639; ENSG00000156127.
GeneID10538.
KEGGhsa:10538.
UCSCuc001xrr.3. human.

Organism-specific databases

CTD10538.
GeneCardsGC14P075988.
HGNCHGNC:958. BATF.
MIM612476. gene.
neXtProtNX_Q16520.
PharmGKBPA25268.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG257556.
HOGENOMHOG000236325.
HOVERGENHBG039173.
InParanoidQ16520.
KOK09034.
OMATHAFHQP.
OrthoDBEOG7H794S.
PhylomeDBQ16520.
TreeFamTF332340.

Gene expression databases

ArrayExpressQ16520.
BgeeQ16520.
CleanExHS_BATF.
GenevestigatorQ16520.

Family and domain databases

InterProIPR004827. bZIP.
IPR000837. Leuzip_Fos.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSPR00042. LEUZIPPRFOS.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBATF_(gene).
GenomeRNAi10538.
NextBio39981.
PROQ16520.
SOURCESearch...

Entry information

Entry nameBATF_HUMAN
AccessionPrimary (citable) accession number: Q16520
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM