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Protein

Cyclic AMP-dependent transcription factor ATF-6 alpha

Gene

ATF6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that acts during endoplasmic reticulum stress by activating unfolded protein response target genes. Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3'). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei419 – 4202Cleavage; by PS1By similarity

GO - Molecular functioni

  • cAMP response element binding Source: InterPro
  • protein heterodimerization activity Source: ParkinsonsUK-UCL
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: ParkinsonsUK-UCL
  • transcription coactivator activity Source: ProtInc

GO - Biological processi

  • ATF6-mediated unfolded protein response Source: ParkinsonsUK-UCL
  • cellular protein metabolic process Source: Reactome
  • endoplasmic reticulum unfolded protein response Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response Source: ProtInc
  • protein folding Source: ProtInc
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • response to stress Source: ProtInc
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Unfolded protein response

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_18348. ATF6-alpha activates chaperones.
REACT_18355. ATF4 activates genes.
REACT_18423. ATF6-alpha activates chaperone genes.
SignaLinkiP18850.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic AMP-dependent transcription factor ATF-6 alpha
Short name:
cAMP-dependent transcription factor ATF-6 alpha
Alternative name(s):
Activating transcription factor 6 alpha
Short name:
ATF6-alpha
Cleaved into the following chain:
Gene namesi
Name:ATF6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:791. ATF6.

Subcellular locationi

Processed cyclic AMP-dependent transcription factor ATF-6 alpha :
  • Nucleus

  • Note: Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. THBS4 promotes its nuclear shuttling.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 377377CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei378 – 39821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini399 – 670272LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: ParkinsonsUK-UCL
  • endoplasmic reticulum membrane Source: Reactome
  • Golgi apparatus Source: ParkinsonsUK-UCL
  • Golgi membrane Source: Reactome
  • integral component of endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  • membrane Source: ParkinsonsUK-UCL
  • nuclear envelope Source: ProtInc
  • nucleoplasm Source: Reactome
  • nucleus Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi391 – 3911N → F: Loss of proteolytic cleavage; when associated with L-394. 1 Publication
Mutagenesisi394 – 3941P → L: Loss of proteolytic cleavage; when associated with F-391. 1 Publication
Mutagenesisi415 – 4162RR → AA: Reduces proteolytic cleavage. 1 Publication
Mutagenesisi419 – 4191L → V: Reduces proteolytic cleavage. 1 Publication
Mutagenesisi474 – 4741T → I: Loss of glycosylation at Asn-472 and increase of Golgi translocation rate. 1 Publication
Mutagenesisi586 – 5861T → I: Loss of glycosylation at Asn-584 and increase of Golgi translocation rate. Higher increase in Golgi translocation rate; when associated with Ile-645. 1 Publication
Mutagenesisi645 – 6451T → I: Loss of glycosylation at Asn-643 and increase of Golgi translocation rate. Higher increase in Golgi translocation rate; when associated with Ile-586. 1 Publication

Organism-specific databases

PharmGKBiPA25091.

Chemistry

DrugBankiDB00852. Pseudoephedrine.

Polymorphism and mutation databases

BioMutaiATF6.
DMDMi66774203.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 670670Cyclic AMP-dependent transcription factor ATF-6 alphaPRO_0000076589Add
BLAST
Chaini1 – ?Processed cyclic AMP-dependent transcription factor ATF-6 alphaPRO_0000296200

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi472 – 4721N-linked (GlcNAc...)1 Publication
Glycosylationi584 – 5841N-linked (GlcNAc...)1 Publication
Glycosylationi643 – 6431N-linked (GlcNAc...)1 Publication

Post-translational modificationi

During unfolded protein response an approximative 50 kDa fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 and site-2 proteases.1 Publication
N-glycosylated. The glycosylation status may serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the unfolded protein response (UPR).1 Publication
Phosphorylated in vitro by MAPK14/P38MAPK.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP18850.
PaxDbiP18850.
PRIDEiP18850.

PTM databases

PhosphoSiteiP18850.

Miscellaneous databases

PMAP-CutDBP18850.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP18850.
CleanExiHS_ATF6.
GenevisibleiP18850. HS.

Organism-specific databases

HPAiHPA005935.

Interactioni

Subunit structurei

Homodimer and heterodimer with ATF6-beta. The dimer interacts with the nuclear transcription factor Y (NF-Y) trimer through direct binding to NF-Y subunit C (NF-YC). Interacts also with the transcription factors GTF2I, YY1 and SRF. Interacts (via lumenal domain) with THBS1 (By similarity). Interacts with THBS4 (via EGF-like 3; calcium-binding domain) which facilitates its processing, activation and nuclear translocation (PubMed:22682248). Interacts with XBP1 isoform 2; the interaction occurs in a ER stress-dependent manner (PubMed:17765680).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CREB3L3Q68CJ92EBI-852157,EBI-852194

Protein-protein interaction databases

BioGridi116586. 29 interactions.
DIPiDIP-29304N.
IntActiP18850. 15 interactions.
MINTiMINT-268075.
STRINGi9606.ENSP00000356919.

Structurei

3D structure databases

ProteinModelPortaliP18850.
SMRiP18850. Positions 312-357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini306 – 36964bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 150150Transcription activationAdd
BLAST
Regioni308 – 33932Basic motifAdd
BLAST
Regioni348 – 3558Leucine-zipper
Regioni468 – 589122Interaction with THBS4Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi124 – 1274Poly-Ser
Compositional biasi325 – 3284Poly-Lys
Compositional biasi463 – 4664Poly-Pro

Domaini

The basic domain functions as a nuclear localization signal.
The basic leucine-zipper domain is sufficient for association with the NF-Y trimer and binding to ERSE.

Sequence similaritiesi

Belongs to the bZIP family. ATF subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG236121.
GeneTreeiENSGT00530000063762.
HOGENOMiHOG000253938.
HOVERGENiHBG108357.
InParanoidiP18850.
KOiK09054.
OMAiMDTRILH.
OrthoDBiEOG7GBFWN.
PhylomeDBiP18850.
TreeFamiTF316079.

Family and domain databases

InterProiIPR029801. ATF6A.
IPR004827. bZIP.
[Graphical view]
PANTHERiPTHR22952:SF10. PTHR22952:SF10. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18850-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEPAGVAGT MESPFSPGLF HRLDEDWDSA LFAELGYFTD TDELQLEAAN
60 70 80 90 100
ETYENNFDNL DFDLDLMPWE SDIWDINNQI CTVKDIKAEP QPLSPASSSY
110 120 130 140 150
SVSSPRSVDS YSSTQHVPEE LDLSSSSQMS PLSLYGENSN SLSSAEPLKE
160 170 180 190 200
DKPVTGPRNK TENGLTPKKK IQVNSKPSIQ PKPLLLPAAP KTQTNSSVPA
210 220 230 240 250
KTIIIQTVPT LMPLAKQQPI ISLQPAPTKG QTVLLSQPTV VQLQAPGVLP
260 270 280 290 300
SAQPVLAVAG GVTQLPNHVV NVVPAPSANS PVNGKLSVTK PVLQSTMRNV
310 320 330 340 350
GSDIAVLRRQ QRMIKNRESA CQSRKKKKEY MLGLEARLKA ALSENEQLKK
360 370 380 390 400
ENGTLKRQLD EVVSENQRLK VPSPKRRVVC VMIVLAFIIL NYGPMSMLEQ
410 420 430 440 450
DSRRMNPSVS PANQRRHLLG FSAKEAQDTS DGIIQKNSYR YDHSVSNDKA
460 470 480 490 500
LMVLTEEPLL YIPPPPCQPL INTTESLRLN HELRGWVHRH EVERTKSRRM
510 520 530 540 550
TNNQQKTRIL QGALEQGSNS QLMAVQYTET TSSISRNSGS ELQVYYASPR
560 570 580 590 600
SYQDFFEAIR RRGDTFYVVS FRRDHLLLPA TTHNKTTRPK MSIVLPAINI
610 620 630 640 650
NENVINGQDY EVMMQIDCQV MDTRILHIKS SSVPPYLRDQ QRNQTNTFFG
660 670
SPPAATEATH VVSTIPESLQ
Length:670
Mass (Da):74,585
Last modified:May 24, 2005 - v3
Checksum:i5EBD08CF4121D41A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951N → I in AAH14969 (PubMed:15489334).Curated
Sequence conflicti195 – 1951N → I in AAH71997 (PubMed:15489334).Curated
Sequence conflicti198 – 2014VPAK → IPPQ in AAH14969 (PubMed:15489334).Curated
Sequence conflicti198 – 2014VPAK → IPPQ in AAH71997 (PubMed:15489334).Curated
Sequence conflicti307 – 3071L → I no nucleotide entry (PubMed:2516827).Curated
Sequence conflicti354 – 3541T → R no nucleotide entry (PubMed:2516827).Curated
Sequence conflicti366 – 3694NQRL → LRNS no nucleotide entry (PubMed:2516827).Curated
Sequence conflicti410 – 4101S → G in AAB64434 (PubMed:9271374).Curated
Sequence conflicti513 – 5142AL → VV in AAB64434 (PubMed:9271374).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671M → L.1 Publication
Corresponds to variant rs1058405 [ dbSNP | Ensembl ].
VAR_022455
Natural varianti67 – 671M → V.1 Publication
Corresponds to variant rs1058405 [ dbSNP | Ensembl ].
VAR_022456
Natural varianti145 – 1451A → P.2 Publications
Corresponds to variant rs2070150 [ dbSNP | Ensembl ].
VAR_022457
Natural varianti157 – 1571P → S.2 Publications
Corresponds to variant rs1135983 [ dbSNP | Ensembl ].
VAR_022458

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005887 mRNA. Translation: AAB64434.1.
AB015856 mRNA. Translation: BAA34722.1.
AL391825, AL359541, AL450995 Genomic DNA. Translation: CAH73985.1.
AL450995, AL359541, AL391825 Genomic DNA. Translation: CAH71144.1.
AL359541, AL391825, AL450995 Genomic DNA. Translation: CAH74152.1.
BC014969 mRNA. Translation: AAH14969.1.
BC071997 mRNA. Translation: AAH71997.1.
CCDSiCCDS1235.1.
PIRiF34223.
RefSeqiNP_031374.2. NM_007348.3.
UniGeneiHs.492740.
Hs.617868.

Genome annotation databases

EnsembliENST00000367942; ENSP00000356919; ENSG00000118217.
GeneIDi22926.
KEGGihsa:22926.
UCSCiuc001gbq.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005887 mRNA. Translation: AAB64434.1.
AB015856 mRNA. Translation: BAA34722.1.
AL391825, AL359541, AL450995 Genomic DNA. Translation: CAH73985.1.
AL450995, AL359541, AL391825 Genomic DNA. Translation: CAH71144.1.
AL359541, AL391825, AL450995 Genomic DNA. Translation: CAH74152.1.
BC014969 mRNA. Translation: AAH14969.1.
BC071997 mRNA. Translation: AAH71997.1.
CCDSiCCDS1235.1.
PIRiF34223.
RefSeqiNP_031374.2. NM_007348.3.
UniGeneiHs.492740.
Hs.617868.

3D structure databases

ProteinModelPortaliP18850.
SMRiP18850. Positions 312-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116586. 29 interactions.
DIPiDIP-29304N.
IntActiP18850. 15 interactions.
MINTiMINT-268075.
STRINGi9606.ENSP00000356919.

Chemistry

DrugBankiDB00852. Pseudoephedrine.

PTM databases

PhosphoSiteiP18850.

Polymorphism and mutation databases

BioMutaiATF6.
DMDMi66774203.

Proteomic databases

MaxQBiP18850.
PaxDbiP18850.
PRIDEiP18850.

Protocols and materials databases

DNASUi22926.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367942; ENSP00000356919; ENSG00000118217.
GeneIDi22926.
KEGGihsa:22926.
UCSCiuc001gbq.2. human.

Organism-specific databases

CTDi22926.
GeneCardsiGC01P161736.
H-InvDBHIX0001253.
HGNCiHGNC:791. ATF6.
HPAiHPA005935.
MIMi605537. gene.
neXtProtiNX_P18850.
PharmGKBiPA25091.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG236121.
GeneTreeiENSGT00530000063762.
HOGENOMiHOG000253938.
HOVERGENiHBG108357.
InParanoidiP18850.
KOiK09054.
OMAiMDTRILH.
OrthoDBiEOG7GBFWN.
PhylomeDBiP18850.
TreeFamiTF316079.

Enzyme and pathway databases

ReactomeiREACT_18348. ATF6-alpha activates chaperones.
REACT_18355. ATF4 activates genes.
REACT_18423. ATF6-alpha activates chaperone genes.
SignaLinkiP18850.

Miscellaneous databases

ChiTaRSiATF6. human.
GeneWikiiATF6.
GenomeRNAii22926.
NextBioi43639.
PMAP-CutDBP18850.
PROiP18850.
SOURCEiSearch...

Gene expression databases

BgeeiP18850.
CleanExiHS_ATF6.
GenevisibleiP18850. HS.

Family and domain databases

InterProiIPR029801. ATF6A.
IPR004827. bZIP.
[Graphical view]
PANTHERiPTHR22952:SF10. PTHR22952:SF10. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Interaction of ATF6 and serum response factor."
    Zhu C., Johansen F.E., Prywes R.
    Mol. Cell. Biol. 17:4957-4966(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-67; PRO-145 AND SER-157.
    Tissue: Cervix carcinoma.
  2. "Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins; involvement of basic-leucine zipper transcription factors."
    Yoshida H., Haze K., Yanagi H., Yura T., Mori K.
    J. Biol. Chem. 273:33741-33749(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PRO-145 AND SER-157.
    Tissue: Cervix carcinoma.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] OF 1-202, VARIANT VAL-67.
    Tissue: Pancreas.
  5. "Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers."
    Hai T., Liu F., Coukos W.J., Green M.R.
    Genes Dev. 3:2083-2090(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-369.
  6. Erratum
    Hai T., Liu F., Coukos W.J., Green M.R.
    Genes Dev. 4:682-682(1990)
  7. "Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress."
    Haze K., Yoshida H., Yanagi H., Yura T., Mori K.
    Mol. Biol. Cell 10:3787-3799(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs."
    Ye J., Rawson R.B., Komuro R., Chen X., Dave U.P., Prywes R., Brown M.S., Goldstein J.L.
    Mol. Cell 6:1355-1364(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING BY PS1 AND PS2, MUTAGENESIS OF ASN-391; PRO-394; 415-ARG-ARG-416 AND LEU-419.
  9. "XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor."
    Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K.
    Cell 107:881-891(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  10. "Endoplasmic reticulum stress-induced formation of transcription factor complex ERSF including NF-Y (CBF) and activating transcription factors 6alpha and 6beta that activates the mammalian unfolded protein response."
    Yoshida H., Okada T., Haze K., Yanagi H., Yura T., Negishi M., Mori K.
    Mol. Cell. Biol. 21:1239-1248(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The molecular biology and nomenclature of the activating transcription factor/cAMP responsive element binding family of transcription factors: activating transcription factor proteins and homeostasis."
    Hai T., Hartman M.G.
    Gene 273:1-11(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  12. "Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response."
    Hong M., Luo S., Baumeister P., Huang J.M., Gogia R.K., Li M., Lee A.S.
    J. Biol. Chem. 279:11354-11363(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-472; ASN-584 AND ASN-643, MUTAGENESIS OF THR-474; THR-586 AND THR-645.
  13. "Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1."
    Yamamoto K., Sato T., Matsui T., Sato M., Okada T., Yoshida H., Harada A., Mori K.
    Dev. Cell 13:365-376(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XBP1.
  14. Cited for: INTERACTION WITH THBS4.

Entry informationi

Entry nameiATF6A_HUMAN
AccessioniPrimary (citable) accession number: P18850
Secondary accession number(s): O15139
, Q5VW62, Q6IPB5, Q9UEC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 24, 2005
Last modified: June 24, 2015
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.