P17544 (ATF7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	494 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Isoform 4/ATF-A0 acts as a dominant repressor of the E-selectin/NF-ELAM1/delta-A promoter. Ref.3 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Isoform 5/ATF-4 acts as a negative regulator, inhibiting both ATF2 and ATF7 transcriptional activities. It may exert these effects by sequestrating in the cytoplasm the Thr-53 phosphorylating kinase, preventing activation. Ref.3 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16
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.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Nucleus. Nucleus › nucleoplasm. Note: Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear periphery. Ref.13 Ref.16 Isoform 5: Cytoplasm Ref.13 Ref.16.
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.14 Sumoylation delays nuclear localization and inhibits transactivation activity through preventing binding to TAF12. RANBP2 appears to be the specific E3 ligase. Ref.13 Ref.14
Sequence similarities	Belongs to the bZIP family. Contains 1 bZIP (basic-leucine zipper) domain. Contains 1 C2H2-type zinc finger.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nuclear periphery Inferred from direct assay Ref.13. Source: UniProtKB nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mitogen-activated protein kinase binding Inferred from direct assay Ref.11. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Non-traceable author statement Ref.1. Source: ProtInc transcription factor binding Inferred from direct assay Ref.11. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
OCIAD1	Q9NX40	2	EBI-765623,EBI-2683029

Alternative products

This entry describes 6 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.

Isoform 5 (identifier: P17544-5)

Also known as: ATF-4;

The sequence of this isoform differs from the canonical sequence as follows:
     100-494: AAAGPLDMSL...MTPQSQSAGR → VFRPRLFLLCFGIIFLIG

Isoform 6 (identifier: P17544-6)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 494	494	Cyclic AMP-dependent transcription factor ATF-7		PRO_0000076592
Regions
	Domain	343 – 406	64	bZIP
	Zinc finger	7 – 31	25	C2H2-type
	Region	1 – 296	296	Transactivation domain
	Region	336 – 494	159	Essential for binding adenovirus 2 E1A
	Region	345 – 365	21	Basic motif By similarity
	Region	371 – 399	29	Leucine-zipper By similarity
Amino acid modifications
	Modified residue	51	1	Phosphothreonine; by MAPK11 Ref.14
	Modified residue	53	1	Phosphothreonine Ref.14
	Modified residue	112	1	Phosphothreonine Ref.14
	Modified residue	424	1	Phosphoserine Ref.15
	Cross-link	118		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.13 Ref.14
Natural variations
	Alternative sequence	89 – 99	11	Missing in isoform 1, isoform 4 and isoform 6.		VSP_000594
	Alternative sequence	100 – 494	395	AAAGP…QSAGR → VFRPRLFLLCFGIIFLIG in isoform 5.		VSP_042469
	Alternative sequence	125 – 145	21	Missing in isoform 1 and isoform 2.		VSP_000595
	Alternative sequence	146 – 321	176	Missing in isoform 4.		VSP_034543
Experimental info
	Mutagenesis	9	1	C → A: Severely reduced TAF12-mediated enhancement of transcriptional activity. Ref.12
	Mutagenesis	14	1	C → 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.11
	Mutagenesis	22	1	D → K: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness. Ref.9
	Mutagenesis	27	1	H → N: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness. Ref.9
	Mutagenesis	33	1	M → D: Severely reduced TAF12-induced transcriptional activity; when associated with S-35. Ref.12
	Mutagenesis	35	1	L → S: Severely reduced TAF12-induced transcriptional activity; when associated with D-33. Ref.12
	Mutagenesis	51	1	T → 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.11 Ref.12 Ref.14
	Mutagenesis	51	1	T → D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-53. Ref.11 Ref.12 Ref.14
	Mutagenesis	53	1	T → 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.11 Ref.12 Ref.14
	Mutagenesis	53	1	T → D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-51. Ref.11 Ref.12 Ref.14
	Mutagenesis	112	1	T → 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.11 Ref.12 Ref.14
	Mutagenesis	118	1	K → R: Abolishes sumoylation. Exclusive nucleoplasmic location. Increase in binding the E-selectin promoter. Ref.14
	Mutagenesis	156	1	T → A: No effect on transactivation; when associated with A-158. Ref.11
	Mutagenesis	158	1	T → A: No effect on transactivation; when associated with A-156. Ref.11
	Sequence conflict	12	1	P → T in AAH42363. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 (ATF-A1) [UniParc]. Last modified January 24, 2001. Version 2. Checksum: 511EAF79C6503300	FASTA	494	52,967
	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
	Isoform 1 (ATF-A) [UniParc]. Checksum: 92AB6DF8D2A954CD	FASTA	462	49,650
	10 20 30 40 50 60 MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN 70 80 90 100 110 120 CEEVGLFNEL ASSFEHEFKK AADEDEKKAA AGPLDMSLPS TPDIKIKEEE PVEEVTPKPV 130 140 150 160 170 180 LISTPTPTIV RPGSLPLHLG YDPLHPTLPS PTSVITQAPP SNRQMGSPTG SLPLVMHLAN 190 200 210 220 230 240 GQTMPVLPGP PVQMPSVISL ARPVSMVPNI PGIPGPPVNS SGSISPSGHP IPSEAKMRLK 250 260 270 280 290 300 ATLTHQVSSI NGGCGMVVGT ASTMVTARPE QSQILIQHPD APSPAQPQVS PAQPTPSTGG 310 320 330 340 350 360 RRRRTVDEDP DERRQRFLER NRAAASRCRQ KRKLWVSSLE KKAEELTSQN IQLSNEVTLL 370 380 390 400 410 420 RNEVAQLKQL LLAHKDCPVT ALQKKTQGYL ESPKESSEPT GSPAPVIQHS SATAPSNGLS 430 440 450 460 VRSAAEAVAT SVLTQMASQR TELSMPIQSH VIMTPQSQSA GR
	Isoform 2 (ATF-A-delta) [UniParc]. Checksum: 6CB9C4D7A0128AA9	FASTA	473	50,860
	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 EPVEEVTPKP VLISTPTPTI VRPGSLPLHL GYDPLHPTLP SPTSVITQAP PSNRQMGSPT 190 200 210 220 230 240 GSLPLVMHLA NGQTMPVLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN SSGSISPSGH 250 260 270 280 290 300 PIPSEAKMRL KATLTHQVSS INGGCGMVVG TASTMVTARP EQSQILIQHP DAPSPAQPQV 310 320 330 340 350 360 SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR QKRKLWVSSL EKKAEELTSQ 370 380 390 400 410 420 NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV TALQKKTQGY LESPKESSEP TGSPAPVIQH 430 440 450 460 470 SSATAPSNGL SVRSAAEAVA TSVLTQMASQ RTELSMPIQS HVIMTPQSQS AGR
	Isoform 4 (ATF-A0) [UniParc]. Checksum: 01665BFA649C6CA1	FASTA	307	33,681
	10 20 30 40 50 60 MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN 70 80 90 100 110 120 CEEVGLFNEL ASSFEHEFKK AADEDEKKAA AGPLDMSLPS TPDIKIKEEE PVEVDSSPPD 130 140 150 160 170 180 SPASSPCSPP LKEKSPAQPT PSTGGRRRRT VDEDPDERRQ RFLERNRAAA SRCRQKRKLW 190 200 210 220 230 240 VSSLEKKAEE LTSQNIQLSN EVTLLRNEVA QLKQLLLAHK DCPVTALQKK TQGYLESPKE 250 260 270 280 290 300 SSEPTGSPAP VIQHSSATAP SNGLSVRSAA EAVATSVLTQ MASQRTELSM PIQSHVIMTP QSQSAGR
	Isoform 5 (ATF-4) [UniParc]. Checksum: 15298D193695ACED	FASTA	117	13,278
	10 20 30 40 50 60 MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN 70 80 90 100 110 CEEVGLFNEL ASSFEHEFKK AADEDEKKAR SRTVAKKLVV FRPRLFLLCF GIIFLIG
	Isoform 6 [UniParc]. Checksum: 07080BC24FED635B	FASTA	483	51,757
	10 20 30 40 50 60 MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN 70 80 90 100 110 120 CEEVGLFNEL ASSFEHEFKK AADEDEKKAA AGPLDMSLPS TPDIKIKEEE PVEVDSSPPD 130 140 150 160 170 180 SPASSPCSPP LKEKEVTPKP VLISTPTPTI VRPGSLPLHL GYDPLHPTLP SPTSVITQAP 190 200 210 220 230 240 PSNRQMGSPT GSLPLVMHLA NGQTMPVLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN 250 260 270 280 290 300 SSGSISPSGH PIPSEAKMRL KATLTHQVSS INGGCGMVVG TASTMVTARP EQSQILIQHP 310 320 330 340 350 360 DAPSPAQPQV SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR QKRKLWVSSL 370 380 390 400 410 420 EKKAEELTSQ NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV TALQKKTQGY LESPKESSEP 430 440 450 460 470 480 TGSPAPVIQH SSATAPSNGL SVRSAAEAVA TSVLTQMASQ RTELSMPIQS HVIMTPQSQS AGR

References

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[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] [Europe PMC] [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] [Europe PMC] [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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 5 AND 6). Tissue: Brain and Colon.
[8]	"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] [Europe PMC] [Abstract] Cited for: SUBUNIT, FUNCTION.
[9]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN ADENOVIRUS 2 E1A, ZINC-BINDING, MUTAGENESIS OF ASP-22 AND HIS-27.
[10]	"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] [Europe PMC] [Abstract] Cited for: SUBUNIT, FUNCTION.
[11]	"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] [Europe PMC] [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.
[12]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TAF4 AND TAF12, FUNCTION, TRANSACTIVATION DOMAIN, MUTAGENESIS OF CYS-9; MET-33; LEU-35; THR-51 AND THR-53.
[13]	"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] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-118, SUBCELLULAR LOCATION, INTERACTION WITH TAF12, FUNCTION.
[14]	"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] [Europe PMC] [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.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"A cytoplasmic negative regulator isoform of ATF7 impairs ATF7 and ATF2 phosphorylation and transcriptional activity." Diring J., Camuzeaux B., Donzeau M., Vigneron M., Rosa-Calatrava M., Kedinger C., Chatton B. PLoS ONE 6:E23351-E23351(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION (ISOFORM 5), SUBCELLULAR LOCATION (ISOFORM 5).
[17]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	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. AC023509 Genomic DNA. No translation available. AC073594 Genomic DNA. No translation available. CH471054 Genomic DNA. Translation: EAW96723.1. CH471054 Genomic DNA. Translation: EAW96724.1. BC042363 mRNA. Translation: AAH42363.1. BC136302 mRNA. Translation: AAI36303.1. BC140006 mRNA. Translation: AAI40007.1.
IPI	IPI00009975. IPI00015147. IPI00218344. IPI00641268. IPI00909393.
PIR	S12741.
RefSeq	NP_001123532.1. NM_001130060.1. NP_001193611.1. NM_001206682.1. NP_001193612.1. NM_001206683.1. NP_006847.1. NM_006856.2.
UniGene	Hs.12286. Hs.633602.
3D structure databases
ProteinModelPortal	P17544.
ModBase	Search...
Protein-protein interaction databases
IntAct	P17544. 7 interactions.
STRING	9606.ENSP00000329212.
PTM databases
PhosphoSite	P17544.
Polymorphism databases
DMDM	12643393.
Proteomic databases
PaxDb	P17544.
PRIDE	P17544.
Protocols and materials databases
DNASU	11016.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000328463; ENSP00000329212; ENSG00000170653. ENST00000415113; ENSP00000404880; ENSG00000170653. ENST00000420353; ENSP00000399465; ENSG00000170653. ENST00000456903; ENSP00000387406; ENSG00000170653. ENST00000548118; ENSP00000456858; ENSG00000170653. ENST00000548446; ENSP00000449938; ENSG00000170653. ENST00000591397; ENSP00000465192; ENSG00000170653.
GeneID	11016.
KEGG	hsa:11016.
UCSC	uc001sdy.3. human. uc010sol.2. human.
Organism-specific databases
CTD	11016.
GeneCards	GC12M053905.
H-InvDB	HIX0201838.
HGNC	HGNC:792. ATF7.
HPA	HPA003384.
MIM	606371. gene.
neXtProt	NX_P17544.
PharmGKB	PA25092.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG306955.
HOGENOM	HOG000220894.
HOVERGEN	HBG004300.
InParanoid	P17544.
KO	K09045.
OMA	CMVPNIP.
OrthoDB	EOG4QFWDQ.
PhylomeDB	P17544.
Gene expression databases
Bgee	P17544.
CleanEx	HS_ATF7.
Genevestigator	P17544.
GermOnline	ENSG00000170653. 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	ATF7. human.
GenomeRNAi	11016.
NextBio	41853.
SOURCE	Search...

Entry information

Entry name

ATF7_HUMAN

Accession

Primary (citable) accession number: P17544
Secondary accession number(s): A5D6Y4 , B2RMP1, B4DQL4, Q13814, Q8IVR8, Q9UD83

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 24, 2001
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 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.