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P15336 (ATF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-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_componentmembrane

Inferred from electronic annotation. Source: Compara

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA 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...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505Cyclic AMP-dependent transcription factor ATF-2
PRO_0000076577

Regions

Domain352 – 41564bZIP
Zinc finger25 – 4925C2H2-type
Region354 – 37421Basic motif By similarity
Region380 – 40829Leucine-zipper By similarity

Amino acid modifications

Modified residue691Phosphothreonine; by MAPK11 and MAPK14 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.16
Modified residue711Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK3 Ref.8 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16
Modified residue901Phosphoserine Ref.16
Modified residue1121Phosphoserine Ref.12 Ref.13 Ref.14 Ref.16
Modified residue1161Phosphothreonine Ref.14
Modified residue3281Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 176176Missing in isoform 2.
VSP_000587
Alternative sequence177 – 1859TSSDSSVII → MSTAYFQMM in isoform 2.
VSP_000588
Alternative sequence210 – 505296Missing in isoform 3.
VSP_045161
Natural variant3521D → H in a breast cancer sample; somatic mutation. Ref.18
VAR_035999

Experimental info

Mutagenesis711T → A: Impairs phosphorylation by PLK3. Ref.15
Sequence conflict2091V → L in AAB64017. Ref.2
Sequence conflict2231N → S in CAA33886. Ref.1
Sequence conflict3111R → L in AAB64017. Ref.2

Secondary structure

......... 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: 0190EEFAEC8891A7

FASTA50554,537
        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 

« Hide

Isoform 2 [UniParc].

Checksum: FA37EF544698FEFA
Show »

FASTA32935,044
Isoform 3 [UniParc].

Checksum: A26AF07CA5D8D5E7
Show »

FASTA20923,050

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.

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.
IPIIPI00234446.
IPI01008990.
PIRS05380.
RefSeqNP_001243019.1. NM_001256090.1.
NP_001243020.1. NM_001256091.1.
NP_001243023.1. NM_001256094.1.
NP_001871.2. NM_001880.3.
UniGeneHs.592510.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHINMR-A19-56[»]
1T2KX-ray3.00D354-414[»]
4H36X-ray3.00B48-55[»]
ProteinModelPortalP15336.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-632N.
IntActP15336. 175 interactions.
MINTMINT-1788434.
STRING9606.ENSP00000264110.

PTM databases

PhosphoSiteP15336.

Polymorphism databases

DMDM215274241.

Proteomic databases

PaxDbP15336.
PRIDEP15336.

Protocols and materials databases

DNASU1386.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264110; ENSP00000264110; ENSG00000115966.
ENST00000392544; ENSP00000376327; ENSG00000115966.
ENST00000409833; ENSP00000386526; ENSG00000115966.
GeneID1386.
KEGGhsa:1386.
UCSCuc002ujl.3. human.
uc002ujv.3. human.

Organism-specific databases

CTD1386.
GeneCardsGC02M175937.
HGNCHGNC:784. ATF2.
HPACAB003769.
HPA022134.
MIM123811. gene.
neXtProtNX_P15336.
PharmGKBPA25084.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306955.
HOGENOMHOG000220894.
HOVERGENHBG004300.
InParanoidP15336.
KOK04450.
OMATPIIRNK.
OrthoDBEOG45MN5N.
PhylomeDBP15336.

Enzyme and pathway databases

Pathway_Interaction_DBil12_2pathway. IL12-mediated signaling events.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.
ReactomeREACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP15336.
BgeeP15336.
CleanExHS_ATF2.
GenevestigatorP15336.
GermOnlineENSG00000115966. Homo sapiens.

Family and domain databases

Gene3D3.30.160.60. 1 hit.
InterProIPR004827. bZIP.
IPR016378. TF_cAMP-dep.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
PIRSFPIRSF003153. ATF2_CRE-BP1. 1 hit.
SMARTSM00338. BRLZ. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATF2. human.
EvolutionaryTraceP15336.
GenomeRNAi1386.
NextBio5631.
SOURCESearch...

Entry information

Entry nameATF2_HUMAN
AccessionPrimary (citable) accession number: P15336
Secondary accession number(s): A1L3Z2 expand/collapse secondary AC list , 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 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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families