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P18850

- ATF6A_HUMAN

UniProt

P18850 - ATF6A_HUMAN

Protein

Cyclic AMP-dependent transcription factor ATF-6 alpha

Gene

ATF6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (24 May 2005)
      Previous versions | rss
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    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.1 Publication

    Sites

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

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. sequence-specific DNA binding Source: InterPro
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc
    4. transcription coactivator activity Source: ProtInc

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. endoplasmic reticulum unfolded protein response Source: BHF-UCL
    4. positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response Source: ProtInc
    5. protein folding Source: ProtInc
    6. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    7. response to stress Source: ProtInc
    8. signal transduction Source: ProtInc
    9. transcription, DNA-templated Source: UniProtKB-KW

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:791. ATF6.

    Subcellular locationi

    Chain 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.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. Golgi membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB-KW
    4. nuclear envelope Source: ProtInc
    5. nucleoplasm Source: Reactome
    6. nucleus Source: ProtInc

    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.
    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.

    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.
    GenevestigatoriP18850.

    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.By similarity1 Publication

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi116586. 22 interactions.
    DIPiDIP-29304N.
    IntActiP18850. 15 interactions.
    MINTiMINT-268075.
    STRINGi9606.ENSP00000356919.

    Structurei

    3D structure databases

    ProteinModelPortaliP18850.
    SMRiP18850. Positions 314-357.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 377377CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini399 – 670272LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei378 – 39821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

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

    Family and domain databases

    InterProiIPR004827. bZIP.
    [Graphical view]
    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

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    MGEPAGVAGT MESPFSPGLF HRLDEDWDSA LFAELGYFTD TDELQLEAAN    50
    ETYENNFDNL DFDLDLMPWE SDIWDINNQI CTVKDIKAEP QPLSPASSSY 100
    SVSSPRSVDS YSSTQHVPEE LDLSSSSQMS PLSLYGENSN SLSSAEPLKE 150
    DKPVTGPRNK TENGLTPKKK IQVNSKPSIQ PKPLLLPAAP KTQTNSSVPA 200
    KTIIIQTVPT LMPLAKQQPI ISLQPAPTKG QTVLLSQPTV VQLQAPGVLP 250
    SAQPVLAVAG GVTQLPNHVV NVVPAPSANS PVNGKLSVTK PVLQSTMRNV 300
    GSDIAVLRRQ QRMIKNRESA CQSRKKKKEY MLGLEARLKA ALSENEQLKK 350
    ENGTLKRQLD EVVSENQRLK VPSPKRRVVC VMIVLAFIIL NYGPMSMLEQ 400
    DSRRMNPSVS PANQRRHLLG FSAKEAQDTS DGIIQKNSYR YDHSVSNDKA 450
    LMVLTEEPLL YIPPPPCQPL INTTESLRLN HELRGWVHRH EVERTKSRRM 500
    TNNQQKTRIL QGALEQGSNS QLMAVQYTET TSSISRNSGS ELQVYYASPR 550
    SYQDFFEAIR RRGDTFYVVS FRRDHLLLPA TTHNKTTRPK MSIVLPAINI 600
    NENVINGQDY EVMMQIDCQV MDTRILHIKS SSVPPYLRDQ QRNQTNTFFG 650
    SPPAATEATH VVSTIPESLQ 670
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi66774203.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1235.1.
    PIRi F34223.
    RefSeqi NP_031374.2. NM_007348.3.
    UniGenei Hs.492740.
    Hs.617868.

    3D structure databases

    ProteinModelPortali P18850.
    SMRi P18850. Positions 314-357.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116586. 22 interactions.
    DIPi DIP-29304N.
    IntActi P18850. 15 interactions.
    MINTi MINT-268075.
    STRINGi 9606.ENSP00000356919.

    Chemistry

    DrugBanki DB00852. Pseudoephedrine.

    PTM databases

    PhosphoSitei P18850.

    Polymorphism databases

    DMDMi 66774203.

    Proteomic databases

    MaxQBi P18850.
    PaxDbi P18850.
    PRIDEi P18850.

    Protocols and materials databases

    DNASUi 22926.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367942 ; ENSP00000356919 ; ENSG00000118217 .
    GeneIDi 22926.
    KEGGi hsa:22926.
    UCSCi uc001gbq.2. human.

    Organism-specific databases

    CTDi 22926.
    GeneCardsi GC01P161736.
    H-InvDB HIX0001253.
    HGNCi HGNC:791. ATF6.
    HPAi HPA005935.
    MIMi 605537. gene.
    neXtProti NX_P18850.
    PharmGKBi PA25091.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236121.
    HOGENOMi HOG000253938.
    HOVERGENi HBG108357.
    InParanoidi P18850.
    KOi K09054.
    OMAi MDTRILH.
    OrthoDBi EOG7GBFWN.
    PhylomeDBi P18850.
    TreeFami TF316079.

    Enzyme and pathway databases

    Reactomei REACT_18348. ATF6-alpha activates chaperones.
    REACT_18355. ATF4 activates genes.
    REACT_18423. ATF6-alpha activates chaperone genes.
    SignaLinki P18850.

    Miscellaneous databases

    ChiTaRSi ATF6. human.
    GeneWikii ATF6.
    GenomeRNAii 22926.
    NextBioi 43639.
    PMAP-CutDB P18850.
    PROi P18850.
    SOURCEi Search...

    Gene expression databases

    Bgeei P18850.
    CleanExi HS_ATF6.
    Genevestigatori P18850.

    Family and domain databases

    InterProi IPR004827. bZIP.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    10. "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.
    11. "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.
    12. 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: October 1, 2014
    This is version 157 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