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P17544 (ATF7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 124. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclic AMP-dependent transcription factor ATF-7
Short name=cAMP-dependent transcription factor ATF-7
Alternative name(s):
Activating transcription factor 7
Transcription factor ATF-A
Gene names
Name:ATF7
Synonyms:ATFA
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays important functions in early cell signaling. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3'), a sequence present in many viral and cellular promoters. Activator of the NF-ELAM1/delta-A site of the E-selectin promoter. Has no intrinsic transcriptional activity, but activates transcription on formation of JUN or FOS heterodimers. Also can bind TRE promoter sequences when heterodimerized with members of the JUN family. Ref.3 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13

Isoform 4/ATF-A0 acts as a dominant repressor of the E-selectin/NF-ELAM1/delta-A promoter. Ref.3 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13

Subunit structure

Homodimer; binds DNA as homodimer. Heterodimer; heterodimerizes with other members of ATF family and with JUN family members. Interacts with JNK2; the interaction does not phosphorylate ATF7 but acts as a docking site for other ATF-associated partners such as JUN family members. Interacts (via its transactivation domain) with TAF12 (isoforms TAFII15 and TAFII20); the interaction potentiates the transactivation activity (isoform TAFII20 only) and is inhibited by ATF7 sumoylation. Interacts with TAF4; the interaction inhibits the TAF12-dependent transactivation. Interacts with adenovirus 2 E1A; the interaction enhances the ATF7-mediated viral transactivation activity which requires the zinc-binding domains of both E1A and ATF7. Interacts with MAPK9; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Subcellular location

Nucleus. Nucleus › nucleoplasm. Note: Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear periphery. Ref.12

Tissue specificity

Expressed in heart, lung and skeletal muscle. Isoform 4 is expressed in various tissues including heart, brain, placenta, lung and skeletal muscle. Highest levels in skeletal muscle. Lowest in lung and placenta. Ref.3

Post-translational modification

On EGF stimulation, phosphorylated first on Thr-53 allowing subsequent phosphorylation on Thr-51. This latter phosphorylation prevents sumoylation, increases binding to TAF12 and enhances transcriptional activity. Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Sumoylation delays nuclear localization and inhibits transactivation activity through preventing binding to TAF12. RANBP2 appears to be the specific E3 ligase.

Sequence similarities

Belongs to the bZIP family.

Contains 1 bZIP domain.

Contains 1 C2H2-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OCIAD1Q9NX402EBI-765623,EBI-2683029

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: P17544-1)

Also known as: ATF-A1;

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 1 (identifier: P17544-2)

Also known as: ATF-A;

The sequence of this isoform differs from the canonical sequence as follows:
     89-99: Missing.
     125-145: Missing.
Isoform 2 (identifier: P17544-3)

Also known as: ATF-A-delta;

The sequence of this isoform differs from the canonical sequence as follows:
     125-145: Missing.
Isoform 4 (identifier: P17544-4)

Also known as: ATF-A0;

The sequence of this isoform differs from the canonical sequence as follows:
     89-99: Missing.
     146-321: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Cyclic AMP-dependent transcription factor ATF-7
PRO_0000076592

Regions

Domain371 – 39929Leucine-zipper
Zinc finger7 – 3125C2H2-type
DNA binding342 – 36524Basic motif
Region1 – 296296Transactivation domain
Region336 – 494159Essential for binding adenovirus 2 E1A

Amino acid modifications

Modified residue421Phosphothreonine Ref.17
Modified residue511Phosphothreonine; by MAPK11 Ref.11 Ref.13 Ref.15 Ref.16 Ref.17
Modified residue531Phosphothreonine Ref.11 Ref.13 Ref.15 Ref.16 Ref.17
Modified residue551Phosphothreonine Ref.16
Modified residue1081Phosphoserine Ref.14 Ref.15 Ref.17
Modified residue1111Phosphoserine Ref.11
Modified residue1121Phosphothreonine Ref.11 Ref.13 Ref.14 Ref.15 Ref.17
Modified residue1271Phosphoserine Ref.11
Modified residue1281Phosphoserine Ref.11
Modified residue1321Phosphoserine Ref.11
Modified residue1351Phosphoserine Ref.11
Modified residue1361Phosphoserine Ref.11
Modified residue1391Phosphoserine Ref.11
Modified residue4241Phosphoserine Ref.16
Cross-link118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.12 Ref.13

Natural variations

Alternative sequence89 – 9911Missing in isoform 1 and isoform 4.
VSP_000594
Alternative sequence125 – 14521Missing in isoform 1 and isoform 2.
VSP_000595
Alternative sequence146 – 321176Missing in isoform 4.
VSP_034543

Experimental info

Mutagenesis91C → A: Severely reduced TAF12-mediated enhancement of transcriptional activity. Ref.10
Mutagenesis141C → A: Greatly reduced JNK2- or adenovirus E1A-mediated transactivation. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-51; A-53 and G-112. Ref.9
Mutagenesis221D → K: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness. Ref.7
Mutagenesis271H → N: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness. Ref.7
Mutagenesis331M → D: Severely reduced TAF12-induced transcriptional activity; when associated with S-35. Ref.10
Mutagenesis351L → S: Severely reduced TAF12-induced transcriptional activity; when associated with D-33. Ref.10
Mutagenesis511T → A: Severely reduced TAF12-induced transcriptional activity. No effect on MAPK9-mediated phosphorylation; when associated with A-53. Greatly reduces MAPK9- and adenovirus E1A-mediated transactivation; when associated with A-53 and G-112. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-53 and G-112. Ref.9 Ref.10 Ref.13
Mutagenesis511T → D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-53. Ref.9 Ref.10 Ref.13
Mutagenesis531T → A: Severely reduced TAF12-induced transcriptional activity. No effect on MAPK9-mediated phosphorylation; when associated with A-51. Greatly reduces MAPK9- and adenovirus E1A-mediated transactivation; when associated with A-51 and G-112. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-51 and G-112. Ref.9 Ref.10 Ref.13
Mutagenesis531T → D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-51. Ref.9 Ref.10 Ref.13
Mutagenesis1121T → G: Some reduction in transactivation but, completely abolishes MAPK9-mediated activation. Abolishes MAPK9-mediated and greatly reduces adenovirus E1A-mediated transactivation; when associated with A-51 and A-53. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-51 and A-53. Ref.9 Ref.10 Ref.13
Mutagenesis1181K → R: Abolishes sumoylation. Exclusive nucleoplasmic location. Increase in binding the E-selectin promoter. Ref.13
Mutagenesis1561T → A: No effect on transactivation; when associated with A-158. Ref.9
Mutagenesis1581T → A: No effect on transactivation; when associated with A-156. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (ATF-A1) [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 511EAF79C6503300

FASTA49452,967
        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

« Hide

Isoform 1 (ATF-A) [UniParc].

Checksum: 92AB6DF8D2A954CD
Show »

FASTA46249,650
Isoform 2 (ATF-A-delta) [UniParc].

Checksum: 6CB9C4D7A0128AA9
Show »

FASTA47350,860
Isoform 4 (ATF-A0) [UniParc].

Checksum: 01665BFA649C6CA1
Show »

FASTA30733,681

References

« Hide 'large scale' references
[1]"Isolation and characterization of two novel, closely related ATF cDNA clones from HeLa cells."
Gaire M., Chatton B., Kedinger C.
Nucleic Acids Res. 18:3467-3473(1990) [PubMed: 1694576] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Cervix carcinoma.
[2]"ATF-a1, a new member of the human ATF family."
Chatton B., Gaire M., Goetz J., Hauss C., Kedinger C.
Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"ATF-a0, a novel variant of the ATF/CREB transcription factor family, forms a dominant transcription inhibitor in ATF-a heterodimers."
Pescini R., Kaszubska W., Whelan J., DeLamarter J.F., Hooft van Huijsduijnen R.
J. Biol. Chem. 269:1159-1165(1994) [PubMed: 8288576] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, SUBUNIT.
Tissue: Cervix carcinoma.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity."
Hai T., Curran T.
Proc. Natl. Acad. Sci. U.S.A. 88:3720-3724(1991) [PubMed: 1827203] [Abstract]
Cited for: SUBUNIT, FUNCTION.
[7]"Transcriptional activation by the adenovirus larger E1a product is mediated by members of the cellular transcription factor ATF family which can directly associate with E1a."
Chatton B., Bocco J.L., Gaire M., Hauss C., Reimund B., Goetz J., Kedinger C.
Mol. Cell. Biol. 13:561-570(1993) [PubMed: 8417352] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS 2 E1A, ZINC-BINDING, MUTAGENESIS OF ASP-22 AND HIS-27.
[8]"Jun and Fos heterodimerize with ATFa, a member of the ATF/CREB family and modulate its transcriptional activity."
Chatton B., Bocco J.L., Goetz J., Gaire M., Lutz Y., Kedinger C.
Oncogene 9:375-385(1994) [PubMed: 8290251] [Abstract]
Cited for: SUBUNIT, FUNCTION.
[9]"Role of the ATFa/JNK2 complex in Jun activation."
De Graeve F., Bahr A., Sabapathy K.T., Hauss C., Wagner E.F., Kedinger C., Chatton B.
Oncogene 18:3491-3500(1999) [PubMed: 10376527] [Abstract]
Cited for: INTERACTION WITH JUN; MAPK9 AND HUMAN ADENOVIRUS 2 E1A, SUBUNIT, FUNCTION, MUTAGENESIS OF CYS-14; THR-51; THR-53; THR-112; THR-156 AND THR-158.
[10]"A functional interaction between ATF7 and TAF12 that is modulated by TAF4."
Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C., Chatton B.
Oncogene 24:3472-3483(2005) [PubMed: 15735663] [Abstract]
Cited for: INTERACTION WITH TAF4 AND TAF12, FUNCTION, TRANSACTIVATION DOMAIN, MUTAGENESIS OF CYS-9; MET-33; LEU-35; THR-51 AND THR-53.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: 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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity."
Hamard P.J., Boyer-Guittaut M., Camuzeaux B., Dujardin D., Hauss C., Oelgeschlager T., Vigneron M., Kedinger C., Chatton B.
Nucleic Acids Res. 35:1134-1144(2007) [PubMed: 17264123] [Abstract]
Cited for: SUMOYLATION AT LYS-118, SUBCELLULAR LOCATION, INTERACTION WITH TAF12, FUNCTION.
[13]"p38beta2-mediated phosphorylation and sumoylation of ATF7 are mutually exclusive."
Camuzeaux B., Diring J., Hamard P.J., Oulad-Abdelghani M., Donzeau M., Vigneron M., Kedinger C., Chatton B.
J. Mol. Biol. 384:980-991(2008) [PubMed: 18950637] [Abstract]
Cited for: PHOSPHORYLATION AT THR-51; THR-53 AND THR-112, SUMOYLATION AT LYS-118, FUNCTION, MUTAGENESIS OF THR-51; THR-53; THR-112 AND LYS-118.
[14]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND THR-112, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-53; SER-108 AND THR-112, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-53; THR-55 AND SER-424, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[17]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42; THR-51; THR-53; SER-108 AND THR-112, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52943 mRNA. Translation: CAA37118.1.
X57197 mRNA. Translation: CAA40483.1.
AK298853 mRNA. Translation: BAG60976.1.
CH471054 Genomic DNA. Translation: EAW96723.1.
IPIIPI00009975.
IPI00015147.
IPI00218344.
IPI00909393.
PIRS12741.
RefSeqNP_001123531.1. NM_001130059.1.
NP_001123532.1. NM_001130060.1.
NP_006847.1. NM_006856.2.
UniGeneHs.12286.

3D structure databases

ProteinModelPortalP17544.
SMRP17544. Positions 1-38, 345-405.
ModBaseSearch...

Protein-protein interaction databases

IntActP17544. 7 interactions.
STRINGP17544.

PTM databases

PhosphoSiteP17544.

Polymorphism databases

DMDM12643393.

Proteomic databases

PRIDEP17544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328463; ENSP00000329212; ENSG00000170653.
GeneID11016.
KEGGhsa:11016.
NMPDRfig|9606.3.peg.7644.
UCSCuc001sdy.1. human.

Organism-specific databases

CTD11016.
GeneCardsGC12M053905.
H-InvDBHIX0026384.
HGNCHGNC:792. ATF7.
HPAHPA003384.
MIM606371. gene.
neXtProtNX_P17544.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12169.
GeneTreeENSGT00390000020106.
HOGENOMHBG714930.
HOVERGENHBG004300.
InParanoidP17544.
OMAEFKKASD.
OrthoDBEOG4QFWDQ.
PhylomeDBP17544.

Gene expression databases

ArrayExpressP17544.
BgeeP17544.
CleanExHS_ATF7.
GenevestigatorP17544.
GermOnlineENSG00000170653. Homo sapiens.

Family and domain databases

InterProIPR004827. bZIP.
IPR011616. bZIP_1.
IPR016378. TF_cAMP-dep.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
Gene3DG3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 1 hit.
KOK09045.
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

NextBio41853.
SOURCESearch...

Entry information

Entry nameATF7_HUMAN
AccessionPrimary (citable) accession number: P17544
Secondary accession number(s): B4DQL4, Q13814, Q9UD83
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 24, 2001
Last modified: January 25, 2012
This is version 124 of the entry and version 2 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 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

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