[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). DOI=10.1093/nar/18.12.3467; PubMed=1694576 [NCBI, ExPASy, EBI, Israel, Japan] Gaire M., Chatton B., Kedinger C.; "Isolation and characterization of two novel, closely related ATF cDNA clones from HeLa cells."; Nucleic Acids Res. 18:3467-3473(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Chatton B., Gaire M., Goetz J., Hauss C., Kedinger C.; "ATF-a1, a new member of the human ATF family."; Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). PubMed=8288576 [NCBI, ExPASy, EBI, Israel, Japan] Pescini R., Kaszubska W., Whelan J., DeLamarter J.F., Hooft van Huijsduijnen R.; "ATF-a0, a novel variant of the ATF/CREB transcription factor family, forms a dominant transcription inhibitor in ATF-a heterodimers."; J. Biol. Chem. 269:1159-1165(1994).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-53; SER-111; THR-112; SER-127; SER-128; SER-132; SER-135; SER-136 AND SER-139, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND THR-112, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-53; SER-108 AND THR-112, 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).

Comments

FUNCTION: Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3'), a sequence present in many viral and cellular promoters.
SUBUNIT: Binds DNA as a dimer.
SUBCELLULAR LOCATION: Nucleus.

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	3
Synonyms	ATF-A1
Isoform ID	P17544-1
This is the isoform sequence displayed in this entry.

Name	1
Synonyms	ATF-A
Isoform ID	P17544-2
Features which should be applied to build the isoform sequence: VSP_000594, VSP_000595.

Name	2
Synonyms	ATF-A-delta
Isoform ID	P17544-3
Features which should be applied to build the isoform sequence: VSP_000595.

Name	4
Synonyms	ATF-A0
Isoform ID	P17544-4
Features which should be applied to build the isoform sequence: VSP_000594, VSP_034543.

SIMILARITY: Belongs to the bZIP family.
SIMILARITY: Contains 1 bZIP domain.
SIMILARITY: Contains 1 C2H2-type zinc finger.

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

X52943; CAA37118.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57197; CAA40483.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00009975; -.
IPI00015147; -.
IPI00218344; -.
IPI00909393; -.

PIR

S12741; S12741.

RefSeq

NP_001123531.1; -.
NP_001123532.1; -.
NP_006847.1; -.

UniGene

Hs.12286

3D structure databases

HSSP

P15336; 1BHI. [HSSP ENTRY / PDB]

P17544; 345-405.

PTM databases

P17544; -.

Organism-specific databases

GeneCards

GC12M052196; -.

H-InvDB

HIX0010676; -.
HIX0026384; -.

HGNC:792; ATF7.

HPA003384; -.

606371; gene. [NCBI / EBI]

PharmGKB

PA25092; -.

Gene expression databases

P17544; -.

P17544; -.

HS_ATF7; -.

ENSG00000170653; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from HPA).
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 (non-traceable author statement from ProtInc).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
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.
IPR004827; TF_bZIP.
IPR016378; TF_cAMP-dep.
IPR007087; Znf_C2H2.
IPR015880; Znf_C2H2-like.
Graphical view of domain structure.

Pfam

PF00170; bZIP_1; 1.
PF00096; zf-C2H2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF003153; ATF2_CRE-BP1; 1.

SMART

SM00338; BRLZ; 1.
SM00355; ZnF_C2H2; 1.
SMART graphical view of domain structure.

PROSITE

PS50217; BZIP; 1.
PS00036; BZIP_BASIC; 1.
PS00028; ZINC_FINGER_C2H2_1; 1.
PS50157; ZINC_FINGER_C2H2_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P17544; -.

Genome annotation databases

Ensembl

ENSG00000170653; Homo sapiens. [Contig view]

GeneID

11016; -.

KEGG

hsa:11016; -.

NMPDR

fig|9606.3.peg.7644; -.

Phylogenomic databases

HOGENOM

P17544; -.

HOVERGEN

P17544; -.

OMA

P17544; EFKKASD.

Other

41853; -.

ATF7; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Activator; Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Transcription; Transcription regulation; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 494`	`494`	`Cyclic AMP-dependent transcription factor ATF-7.`	`PRO_0000076592`
`DOMAIN`	`371 399`	`29`	`Leucine-zipper.`
`ZN_FING`	`7 31`	`25`	`C2H2-type.`
`DNA_BIND`	`342 365`	`24`	`Basic motif.`
`MOD_RES`	`51 51`		`Phosphothreonine.`
`MOD_RES`	`53 53`		`Phosphothreonine.`
`MOD_RES`	`108 108`		`Phosphoserine.`
`MOD_RES`	`111 111`		`Phosphoserine.`
`MOD_RES`	`112 112`		`Phosphothreonine.`
`MOD_RES`	`127 127`		`Phosphoserine.`
`MOD_RES`	`128 128`		`Phosphoserine.`
`MOD_RES`	`132 132`		`Phosphoserine.`
`MOD_RES`	`135 135`		`Phosphoserine.`
`MOD_RES`	`136 136`		`Phosphoserine.`
`MOD_RES`	`139 139`		`Phosphoserine.`
`VAR_SEQ`	`89 99`		`Missing (in isoform 1 and isoform 4).`	`VSP_000594`
`VAR_SEQ`	`125 145`		`Missing (in isoform 1 and isoform 2).`	`VSP_000595`
`VAR_SEQ`	`146 321`		`Missing (in isoform 4).`	`VSP_034543`

Sequence information

Length: 494 AA [This is the length of the unprocessed precursor]

Molecular weight: 52967 Da [This is the MW of the unprocessed precursor]

CRC64: 511EAF79C6503300 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN 

        70         80         90        100        110        120 
CEEVGLFNEL ASSFEHEFKK AADEDEKKAR SRTVAKKLVA AAGPLDMSLP STPDIKIKEE 

       130        140        150        160        170        180 
EPVEVDSSPP DSPASSPCSP PLKEKEVTPK PVLISTPTPT IVRPGSLPLH LGYDPLHPTL 

       190        200        210        220        230        240 
PSPTSVITQA PPSNRQMGSP TGSLPLVMHL ANGQTMPVLP GPPVQMPSVI SLARPVSMVP 

       250        260        270        280        290        300 
NIPGIPGPPV NSSGSISPSG HPIPSEAKMR LKATLTHQVS SINGGCGMVV GTASTMVTAR 

       310        320        330        340        350        360 
PEQSQILIQH PDAPSPAQPQ VSPAQPTPST GGRRRRTVDE DPDERRQRFL ERNRAAASRC 

       370        380        390        400        410        420 
RQKRKLWVSS LEKKAEELTS QNIQLSNEVT LLRNEVAQLK QLLLAHKDCP VTALQKKTQG 

       430        440        450        460        470        480 
YLESPKESSE PTGSPAPVIQ HSSATAPSNG LSVRSAAEAV ATSVLTQMAS QRTELSMPIQ 

       490 
SHVIMTPQSQ SAGR

P17544 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools