P15336 (ATF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclic AMP-dependent transcription factor ATF-2
Short name=cAMP-dependent transcription factor ATF-2

Alternative name(s):
Activating transcription factor 2
Cyclic AMP-responsive element-binding protein 2
Short name=CREB-2
Short name=cAMP-responsive element-binding protein 2
HB16
cAMP response element-binding protein CRE-BP1

Gene names

Name:	ATF2
Synonyms:	CREB2, CREBP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional activator, probably constitutive, which binds to the cAMP-responsive element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Interaction with JUN redirects JUN to bind to CRES preferentially over the 12-O-tetradecanoylphorbol-13-acetate response elements (TRES) as part of an ATF2/JUN complex.
Subunit structure	Binds DNA as a dimer and can form a homodimer in the absence of DNA. Can form a heterodimer with JUN. Interacts with SMAD3 and SMAD4. Binds through its N-terminal region to UTF1 which acts as a coactivator of ATF2 transcriptional activity. Ref.9
Subcellular location	Nucleus Ref.15.
Tissue specificity	Abundant expression seen in the brain.
Post-translational modification	Phosphorylation of Thr-69 by MAPK14 and MAPK11, and at Thr-71 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity. Phosphorylated by PLK3 following hyperosmotic stress. Also phosphorylated and activated by JNK and CaMK4. Ref.7 Ref.8 Ref.10 Ref.15
Sequence similarities	Belongs to the bZIP family. ATF subfamily. Contains 1 bZIP (basic-leucine zipper) domain. Contains 1 C2H2-type zinc finger.
Caution	It is uncertain whether Met-1 or Met-19 is the initiator.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome adipose tissue development Inferred from electronic annotation. Source: Compara fat cell differentiation Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome outflow tract morphogenesis Inferred from electronic annotation. Source: Compara positive regulation of transforming growth factor beta2 production Inferred from electronic annotation. Source: Compara regulation of sequence-specific DNA binding transcription factor activity Traceable author statement. Source: Reactome response to osmotic stress Inferred from direct assay Ref.15. Source: UniProtKB stress-activated MAPK cascade Traceable author statement. Source: Reactome toll-like receptor 1 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome
Cellular_component	membrane Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from electronic annotation. Source: Compara RNA polymerase II distal enhancer sequence-specific DNA binding Inferred from direct assay PubMed 19861239. Source: BHF-UCL RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred by curator PubMed 19861239. Source: BHF-UCL RNA polymerase II transcription factor binding transcription factor activity Inferred by curator PubMed 19861239. Source: BHF-UCL cAMP response element binding Inferred from direct assay PubMed 19861239. Source: BHF-UCL cAMP response element binding protein binding Inferred from direct assay PubMed 19861239. Source: BHF-UCL chromatin binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FOS	P01100	4	EBI-1170906,EBI-852851
JUN	P05412	4	EBI-1170906,EBI-852823
SS18	Q15532	2	EBI-1170906,EBI-2560599
SYT-SSX2	A4PIW0	11	EBI-1170906,EBI-6050533
VRK1	Q99986	5	EBI-1170906,EBI-1769146

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P15336-1)

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.

Isoform 2 (identifier: P15336-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-176: Missing.
     177-185: TSSDSSVII → MSTAYFQMM

Isoform 3 (identifier: P15336-3)

The sequence of this isoform differs from the canonical sequence as follows:
     210-505: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 505

505

Cyclic AMP-dependent transcription factor ATF-2

PRO_0000076577

Regions

Domain

352 – 415

64

bZIP

Zinc finger

25 – 49

25

C2H2-type

Region

354 – 374

21

Basic motif By similarity

Region

380 – 408

29

Leucine-zipper By similarity

Amino acid modifications

Modified residue

69

1

Phosphothreonine; by MAPK11 and MAPK14 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.16

Modified residue

71

1

Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK3 Ref.8 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16

Modified residue

90

1

Phosphoserine Ref.16

Modified residue

112

1

Phosphoserine Ref.12 Ref.13 Ref.14 Ref.16

Modified residue

116

1

Phosphothreonine Ref.14

Modified residue

328

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1 – 176

176

Missing in isoform 2.

VSP_000587

Alternative sequence

177 – 185

9

TSSDSSVII → MSTAYFQMM in isoform 2.

VSP_000588

Alternative sequence

210 – 505

296

Missing in isoform 3.

VSP_045161

Natural variant

352

1

D → H in a breast cancer sample; somatic mutation. Ref.18

VAR_035999

Experimental info

Mutagenesis

71

1

T → A: Impairs phosphorylation by PLK3. Ref.15

Sequence conflict

209

1

V → L in AAB64017. Ref.2

Sequence conflict

223

1

N → S in CAA33886. Ref.1

Sequence conflict

311

1

R → L in AAB64017. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

505

Helix Strand Turn

Details...

Turn

30 – 32

3

Beta strand

35 – 38

4

Helix

39 – 50

12

Turn

51 – 55

5

Helix

355 – 412

58

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 4. Checksum: 0190EEFAEC8891A7	FASTA	505	54,537
	10 20 30 40 50 60 MKFKLHVNSA RQYKDLWNMS DDKPFLCTAP GCGQRFTNED HLAVHKHKHE MTLKFGPARN 70 80 90 100 110 120 DSVIVADQTP TPTRFLKNCE EVGLFNELAS PFENEFKKAS EDDIKKMPLD LSPLATPIIR 130 140 150 160 170 180 SKIEEPSVVE TTHQDSPLPH PESTTSDEKE VPLAQTAQPT SAIVRPASLQ VPNVLLTSSD 190 200 210 220 230 240 SSVIIQQAVP SPTSSTVITQ APSSNRPIVP VPGPFPLLLH LPNGQTMPVA IPASITSSNV 250 260 270 280 290 300 HVPAAVPLVR PVTMVPSVPG IPGPSSPQPV QSEAKMRLKA ALTQQHPPVT NGDTVKGHGS 310 320 330 340 350 360 GLVRTQSEES RPQSLQQPAT STTETPASPA HTTPQTQSTS GRRRRAANED PDEKRRKFLE 370 380 390 400 410 420 RNRAAASRCR QKRKVWVQSL EKKAEDLSSL NGQLQSEVTL LRNEVAQLKQ LLLAHKDCPV 430 440 450 460 470 480 TAMQKKSGYH TADKDDSSED ISVPSSPHTE AIQHSSVSTS NGVSSTSKAE AVATSVLTQM 490 500 ADQSTEPALS QIVMAPSSQS QPSGS
	Isoform 2 [UniParc]. Checksum: FA37EF544698FEFA	FASTA	329	35,044
	10 20 30 40 50 60 MSTAYFQMMQ QAVPSPTSST VITQAPSSNR PIVPVPGPFP LLLHLPNGQT MPVAIPASIT 70 80 90 100 110 120 SSNVHVPAAV PLVRPVTMVP SVPGIPGPSS PQPVQSEAKM RLKAALTQQH PPVTNGDTVK 130 140 150 160 170 180 GHGSGLVRTQ SEESRPQSLQ QPATSTTETP ASPAHTTPQT QSTSGRRRRA ANEDPDEKRR 190 200 210 220 230 240 KFLERNRAAA SRCRQKRKVW VQSLEKKAED LSSLNGQLQS EVTLLRNEVA QLKQLLLAHK 250 260 270 280 290 300 DCPVTAMQKK SGYHTADKDD SSEDISVPSS PHTEAIQHSS VSTSNGVSST SKAEAVATSV 310 320 LTQMADQSTE PALSQIVMAP SSQSQPSGS
	Isoform 3 [UniParc]. Checksum: A26AF07CA5D8D5E7	FASTA	209	23,050
	10 20 30 40 50 60 MKFKLHVNSA RQYKDLWNMS DDKPFLCTAP GCGQRFTNED HLAVHKHKHE MTLKFGPARN 70 80 90 100 110 120 DSVIVADQTP TPTRFLKNCE EVGLFNELAS PFENEFKKAS EDDIKKMPLD LSPLATPIIR 130 140 150 160 170 180 SKIEEPSVVE TTHQDSPLPH PESTTSDEKE VPLAQTAQPT SAIVRPASLQ VPNVLLTSSD 190 200 SSVIIQQAVP SPTSSTVITQ APSSNRPIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Leucine zipper structure of the protein CRE-BP1 binding to the cyclic AMP response element in brain." Maekawa T., Sakura H., Kanei-Ishii C., Sudo T., Yoshimura T., Fujisawa J., Yoshida M., Ishii S. EMBO J. 8:2023-2028(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal brain.
[2]	"Identification of a novel, spliced variant of CREB that is preferentially expressed in the thymus." Yang L., Lanier E.R., Kraig E. J. Immunol. 158:2522-2525(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Thymus.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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] (ISOFORMS 1 AND 3). Tissue: Brain.
[6]	"A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain." Kara C.J., Liou H.-C., Ivashkiv L.B., Glimcher L.H. Mol. Cell. Biol. 10:1347-1357(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 211-505 (ISOFORMS 1/2).
[7]	"Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade." Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R. Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY CAMK4.
[8]	"Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6." Enslen H., Raingeaud J., Davis R.J. J. Biol. Chem. 273:1741-1748(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-69 AND THR-71.
[9]	"Characterization of functional domains of an embryonic stem cell coactivator UTF1 which are conserved and essential for potentiation of ATF-2 activity." Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A., Muramatsu M. J. Biol. Chem. 273:25840-25849(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UTF1.
[10]	"Growth factors can activate ATF2 via a two-step mechanism: phosphorylation of Thr71 through the Ras-MEK-ERK pathway and of Thr69 through RalGDS-Src-p38." Ouwens D.M., de Ruiter N.D., van der Zon G.C., Carter A.P., Schouten J., van der Burgt C., Kooistra K., Bos J.L., Maassen J.A., van Dam H. EMBO J. 21:3782-3793(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-69 AND THR-71.
[11]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69 AND SER-112, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71 AND SER-112, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71; SER-112 AND THR-116, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Hyperosmotic stress-induced ATF-2 activation through Polo-like kinase 3 in human corneal epithelial cells." Wang L., Payton R., Dai W., Lu L. J. Biol. Chem. 286:1951-1958(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-71, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-71.
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71; SER-90 AND SER-112, MASS SPECTROMETRY.
[17]	"Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain." Nagadoi A., Nakazawa K., Uda H., Okuno K., Maekawa T., Ishii S., Nishimura Y. J. Mol. Biol. 287:593-607(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 19-56.
[18]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-352.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15875 mRNA. Translation: CAA33886.1.
U16028 mRNA. Translation: AAB64017.1.
AC131958 Genomic DNA. Translation: AAX88876.1.
AC074291 Genomic DNA. Translation: AAY15004.1.
AC007435 Genomic DNA. No translation available.
AC096649 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11111.1.
CH471058 Genomic DNA. Translation: EAX11112.1.
BC026175 mRNA. Translation: AAH26175.1.
BC130335 mRNA. Translation: AAI30336.1.
BC130337 mRNA. Translation: AAI30338.1.
M31630 mRNA. Translation: AAA35951.1.

IPI

IPI00234446.
IPI01008990.

PIR

S05380.

RefSeq

NP_001243019.1. NM_001256090.1.
NP_001243020.1. NM_001256091.1.
NP_001243023.1. NM_001256094.1.
NP_001871.2. NM_001880.3.

UniGene

Hs.592510.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BHI	NMR	-	A	19-56	[»]
1T2K	X-ray	3.00	D	354-414	[»]
4H36	X-ray	3.00	B	48-55	[»]

ProteinModelPortal

P15336.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-632N.

IntAct

P15336. 175 interactions.

MINT

MINT-1788434.

STRING

9606.ENSP00000264110.

PTM databases

PhosphoSite

P15336.

Polymorphism databases

DMDM

215274241.

Proteomic databases

PaxDb

P15336.

PRIDE

P15336.

Protocols and materials databases

DNASU

1386.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264110; ENSP00000264110; ENSG00000115966.
ENST00000392544; ENSP00000376327; ENSG00000115966.
ENST00000409833; ENSP00000386526; ENSG00000115966.

GeneID

1386.

KEGG

hsa:1386.

UCSC

uc002ujl.3. human.
uc002ujv.3. human.

Organism-specific databases

CTD

1386.

GeneCards

GC02M175937.

HGNC

HGNC:784. ATF2.

HPA

CAB003769.
HPA022134.

MIM

123811. gene.

neXtProt

NX_P15336.

PharmGKB

PA25084.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG306955.

HOGENOM

HOG000220894.

HOVERGEN

HBG004300.

InParanoid

P15336.

KO

K04450.

OMA

TPIIRNK.

OrthoDB

EOG45MN5N.

PhylomeDB

P15336.

Enzyme and pathway databases

Pathway_Interaction_DB

il12_2pathway. IL12-mediated signaling events.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P15336.

Bgee

P15336.

CleanEx

HS_ATF2.

Genevestigator

P15336.

GermOnline

ENSG00000115966. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.60. 1 hit.

InterPro

IPR004827. bZIP.
IPR016378. TF_cAMP-dep.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF00170. bZIP_1. 1 hit.
[Graphical view]

PIRSF

PIRSF003153. ATF2_CRE-BP1. 1 hit.

SMART

SM00338. BRLZ. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

PROSITE

PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ATF2. human.

EvolutionaryTrace

P15336.

GenomeRNAi

1386.

NextBio

5631.

SOURCE

Search...

Entry information

Entry name

ATF2_HUMAN

Accession

Primary (citable) accession number: P15336
Secondary accession number(s): A1L3Z2 , D3DPE9, Q13000, Q4ZFU9, Q53RY2, Q8TAR1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 150 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.