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UniProtKB/Swiss-Prot entry P18846


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ATF1_HUMAN
Primary accession number P18846
Secondary accession numbers P25168 Q9H4A8
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on November 1, 1995 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 97)
Name and origin of the protein
Protein name Cyclic AMP-dependent transcription factor ATF-1
Synonyms cAMP-dependent transcription factor ATF-1
Activating transcription factor 1
Protein TREB36
Gene name
Name: ATF1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2196176 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshimura T., Fujisawa J., Yoshida M.;
"Multiple cDNA clones encoding nuclear proteins that bind to the tax-dependent enhancer of HTLV-1: all contain a leucine zipper structure and basic amino acid domain.";
EMBO J. 9:2537-2542(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1655749 [NCBI, ExPASy, EBI, Israel, Japan]
Rehfuss R.P., Walton K.M., Loriaux M.M., Goodman R.H.;
"The cAMP-regulated enhancer-binding protein ATF-1 activates transcription in response to cAMP-dependent protein kinase A.";
J. Biol. Chem. 266:18431-18434(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 39-271.
PubMed=2516827 [NCBI, ExPASy, EBI, Israel, Japan]
Hai T., Liu F., Coukos W.J., Green M.R.;
"Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers.";
Genes Dev. 3:2083-2090(1989).
[5]
ERRATUM.
Hai T., Liu F., Coukos W.J., Green M.R.;
Genes Dev. 4:682-682(1990).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-246, CHROMOSOMAL TRANSLOCATION WITH FUS, AND ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
DOI=10.1016/S0165-4608(00)00237-5; PubMed=11063792 [NCBI, ExPASy, EBI, Israel, Japan]
Waters B.L., Panagopoulos I., Allen E.F.;
"Genetic characterization of angiomatoid fibrous histiocytoma identifies fusion of the FUS and ATF-1 genes induced by a chromosomal translocation involving bands 12q13 and 16p11.";
Cancer Genet. Cytogenet. 121:109-116(2000).
[7]
PHOSPHORYLATION AT SER-63, AND PHOSPHORYLATION BY CAMK1.
DOI=10.1074/jbc.271.16.9503; PubMed=8621702 [NCBI, ExPASy, EBI, Israel, Japan]
Sun P., Lou L., Maurer R.A.;
"Regulation of activating transcription factor-1 and the cAMP response element-binding protein by Ca2+/calmodulin-dependent protein kinases type I, II, and IV.";
J. Biol. Chem. 271:3066-3073(1996).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
CHROMOSOMAL TRANSLOCATION WITH EWSR1, AND ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
DOI=10.1002/gcc.20201; PubMed=15884099 [NCBI, ExPASy, EBI, Israel, Japan]
Hallor K.H., Mertens F., Jin Y., Meis-Kindblom J.M., Kindblom L.-G., Behrendtz M., Kalen A., Mandahl N., Panagopoulos I.;
"Fusion of the EWSR1 and ATF1 genes without expression of the MITF-M transcript in angiomatoid fibrous histiocytoma.";
Genes Chromosomes Cancer 44:97-102(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X55544; CAA39150.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC029619; AAH29619.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ295163; CAC15058.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00002501; -.
PIR S12560; S12560.
RefSeq NP_005162.1; -.
UniGene Hs.648565
3D structure databases
HSSP Q01147; 1DH3. [HSSP ENTRY / PDB]
SMR P18846; 215-269.
ModBase P18846.
Protein-protein interaction databases
DIP DIP:652N; -.
IntAct P18846; 1.
PTM databases
PhosphoSite P18846; -.
Enzyme and pathway databases
Pathway_Interaction_DB p38alphabetadownstreampathway; Signaling mediated by p38-alpha and p38-beta.
Reactome REACT_11061; Signalling by NGF.
Organism-specific databases
GeneCards GC12P049444; -.
H-InvDB HIX0010631; -.
HGNC HGNC:783; ATF1.
GenAtlas ATF1.
HPA CAB016222; -.
MIM 123803; gene. [NCBI / EBI]
612160; phenotype. [NCBI / EBI]
PharmGKB PA25083; -.
Gene expression databases
ArrayExpress P18846; -.
Bgee P18846; -.
CleanEx HS_ATF1; -.
GermOnline ENSG00000123268; Homo sapiens.
Ontologies
GO
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0043565; Molecular function: sequence-specific DNA binding (inferred from electronic annotation from InterPro).
GO:0003700; Molecular function: transcription factor activity (traceable author statement from ProtInc).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR011616; bZIP_1.
IPR003102; Coactivator_CBP_pKID.
IPR001630; Leuzip_CREB.
IPR004827; TF_bZIP.
Graphical view of domain structure.
Pfam PF00170; bZIP_1; 1.
PF02173; pKID; 1.
Pfam graphical view of domain structure.
PRINTS PR00041; LEUZIPPRCREB.
SMART SM00338; BRLZ; 1.
SMART graphical view of domain structure.
PROSITE PS50217; BZIP; 1.
PS00036; BZIP_BASIC; 1.
PS50953; KID; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSG00000123268; Homo sapiens. [Contig view]
GeneID 466; -.
KEGG hsa:466; -.
Phylogenomic databases
HOGENOM P18846; -.
HOVERGEN P18846; -.
OMA P18846; EDSHKST.
Other
NextBio 1921; -.
SOURCE ATF1; Homo sapiens.
ProtoNet P18846.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Activator; Chromosomal rearrangement; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   271  271     Cyclic AMP-dependent transcription factor ATF-1. PRO_0000076575
DOMAIN   31    90  60     KID. 
DOMAIN   241   262  22     Leucine-zipper. 
DNA_BIND   215   235  21     Basic motif. 
SITE   110   110  1     Breakpoint for translocation to form chimeric EWSR1/ATF1 protein. 
SITE   112   112  1     Breakpoint for translocation to form chimeric FUS/ATF1 protein. 
MOD_RES   63    63        Phosphoserine; by CaMK1. 
MOD_RES   198   198        Phosphoserine. 
VARIANT   191   191  1     P -> A (in dbSNP:rs2230674 [NCBI]). VAR_024382 
CONFLICT   55    55        H -> A (in Ref. 4). 
CONFLICT   227   227        Missing (in Ref. 4). 
Sequence information
Length: 271 AA [This is the length of the unprocessed precursor] Molecular weight: 29233 Da [This is the MW of the unprocessed precursor] CRC64: BAFECBFFB244FCED [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEDSHKSTTS ETAPQPGSAV QGAHISHIAQ QVSSLSESEE SQDSSDSIGS SQKAHGILAR 

        70         80         90        100        110        120 
RPSYRKILKD LSSEDTRGRK GDGENSGVSA AVTSMSVPTP IYQTSSGQYI AIAPNGALQL 

       130        140        150        160        170        180 
ASPGTDGVQG LQTLTMTNSG STQQGTTILQ YAQTSDGQQI LVPSNQVVVQ TASGDMQTYQ 

       190        200        210        220        230        240 
IRTTPSATSL PQTVVMTSPV TLTSQTTKTD DPQLKREIRL MKNREAAREC RRKKKEYVKC 

       250        260        270 
LENRVAVLEN QNKTLIEELK TLKDLYSNKS V 

P18846 in FASTA format

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