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Reviewed, UniProtKB/Swiss-Prot Q99941 (ATF6B_HUMAN)

Last modified December 15, 2009. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cyclic AMP-dependent transcription factor ATF-6 beta
      Short name=cAMP-dependent transcription factor ATF-6 beta
Alternative name(s):
    Activating transcription factor 6 beta
      Short name=ATF6-beta
    cAMP-responsive element-binding protein-like 1
    cAMP response element-binding protein-related protein
      Short name=Creb-rp
    Protein G13
Cleaved into the following chain:
    1- Recommended name:
            Processed cyclic AMP-dependent transcription factor ATF-6 beta
Gene names
Name: ATF6B
Synonyms: CREBL1, G13
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length703 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Transcriptional factor that acts in the unfolded protein response (UPR) pathway by activating UPR target genes induced during ER stress. Binds DNA on the 5'-CCAC[GA]-3' half of the ER stress response element (ERSE) (5'-CCAATN9CCAC[GA]-3') when NF-Y is bound to ERSE.

Subunit structure

Homodimer and heterodimer with ATF6-alpha. The dimer interacts with the nuclear transcription factor Y (NF-Y) trimer through direct binding to NF-Y subunit C (NF-YC).

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein.

Processed cyclic AMP-dependent transcription factor ATF-6 beta: Nucleus. Note: Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus.

Tissue specificity

Ubiquitous.

Domain

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.

Post-translational modification

N-glycosylated.

During unfolded protein response an approximative 60 kDa fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage is probably performed sequentially by site-1 and site-2 proteases.

Sequence similarities

Belongs to the bZIP family. ATF subfamily.

Contains 1 bZIP domain.

Sequence caution

The sequence AAC50888.1 differs from that shown. Reason: Frameshift at position 600.

The sequence AAG14898.1 differs from that shown. Reason: Frameshift at position 600.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q99941-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: Q99941-2)

The sequence of this isoform differs from the canonical sequence as follows:
     28-31: GLQN → D
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 703703Cyclic AMP-dependent transcription factor ATF-6 beta
PRO_0000076590
Chain1 – ?Processed cyclic AMP-dependent transcription factor ATF-6 betaPRO_0000296201

Regions

Topological domain1 – 396396Cytoplasmic Potential
Transmembrane397 – 41721Signal-anchor for type II membrane protein Potential
Topological domain418 – 703286Lumenal Potential
Domain367 – 38822Leucine-zipper
DNA binding327 – 34721Basic motif
Region1 – 8686Transcription activation
Compositional bias96 – 10510Poly-Ser

Sites

Site4101Important for cleavage by PS2 By similarity
Site4131Important for cleavage by PS2 By similarity
Site440 – 4412Cleavage; by PS1 By similarity

Amino acid modifications

Glycosylation4761N-linked (GlcNAc...) Potential
Glycosylation5051N-linked (GlcNAc...) Potential
Glycosylation6101N-linked (GlcNAc...) Potential
Glycosylation6271N-linked (GlcNAc...) Potential
Glycosylation6761N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence28 – 314GLQN → D in isoform 1.
VSP_000593

Experimental info

Sequence conflict31E → D in CAA66664. Ref.2
Sequence conflict329 – 3302QQ → HE in CAA66664. Ref.2
Sequence conflict5201V → D in AAC50888. Ref.6
Sequence conflict6001D → G in AAA97438. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: B04C7B23E7D83F82

FASTA70376,709
        10         20         30         40         50         60 
MAELMLLSEI ADPTRFFTDN LLSPEDWGLQ NSTLYSGLDE VAEEQTQLFR CPEQDVPFDG 

        70         80         90        100        110        120 
SSLDVGMDVS PSEPPWELLP IFPDLQVKSE PSSPCSSSSL SSESSRLSTE PSSEALGVGE 

       130        140        150        160        170        180 
VLHVKTESLA PPLCLLGDDP TSSFETVQIN VIPTSDDSSD VQTKIEPVSP CSSVNSEASL 

       190        200        210        220        230        240 
LSADSSSQAF IGEEVLEVKT ESLSPSGCLL WDVPAPSLGA VQISMGPSLD GSSGKALPTR 

       250        260        270        280        290        300 
KPPLQPKPVV LTTVPMPSRA VPPSTTVLLQ SLVQPPPVSP VVLIQGAIRV QPEGPAPSLP 

       310        320        330        340        350        360 
RPERKSIVPA PMPGNSCPPE VDAKLLKRQQ RMIKNRESAC QSRRKKKEYL QGLEARLQAV 

       370        380        390        400        410        420 
LADNQQLRRE NAALRRRLEA LLAENSELKL GSGNRKVVCI MVFLLFIAFN FGPVSISEPP 

       430        440        450        460        470        480 
SAPISPRMNK GEPQPRRHLL GFSEQEPVQG VEPLQGSSQG PKEPQPSPTD QPSFSNLTAF 

       490        500        510        520        530        540 
PGGAKELLLR DLDQLFLSSD CRHFNRTESL RLADELSGWV QRHQRGRRKI PQRAQERQKS 

       550        560        570        580        590        600 
QPRKKSPPVK AVPIQPPGPP ERDSVGQLQL YRHPDRSQPA FLDAIDRRED TFYVVSFRRD 

       610        620        630        640        650        660 
HLLLPAISHN KTSRPKMSLV MPAMAPNETL SGRGAPGDYE EMMQIECEVM DTRVIHIKTS 

       670        680        690        700 
TVPPSLRKQP SPTPGNATGG PLPVSAASQA HQASHQPLYL NHP 

« Hide

Isoform 1.

Checksum: 54C077BF95309216
Show »

FASTA70076,412

References

« Hide 'large scale' references
[1]"A novel Creb family gene telomeric of HLA-DRA in the HLA complex."
Min J., Shukla H., Kozono H., Bronson S.K., Weissman S.M., Chaplin D.D.
Genomics 30:149-156(1995) [PubMed: 8586413] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Tonsil.
[2]"The gene G13 in the class III region of the human MHC encodes a potential DNA-binding protein."
Khanna A., Campbell R.D.
Biochem. J. 319:81-89(1996) [PubMed: 8870652] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
[3]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed: 14656967] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]"Alternate promoters and alternate splicing of human tenascin-X, a gene with 5' and 3' ends buried in other genes."
Speek M., Barry F., Miller W.L.
Hum. Mol. Genet. 5:1749-1758(1996) [PubMed: 8923003] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]"Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response."
Haze K., Okada T., Yoshida H., Yanagi H., Yura T., Negishi M., Mori K.
Biochem. J. 355:19-28(2001) [PubMed: 11256944] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

U31903 mRNA. Translation: AAA97438.1.
X98053 Genomic DNA. Translation: CAA66663.1.
X98054 mRNA. Translation: CAA66664.1.
U89337 Genomic DNA. Translation: AAB47487.1.
AL049547 Genomic DNA. Translation: CAB89295.1.
AL662828 Genomic DNA. Translation: CAI17416.1.
AL662828 Genomic DNA. Translation: CAI17419.1.
AL662884 Genomic DNA. Translation: CAI18334.1.
AL662884 Genomic DNA. Translation: CAI18336.2.
CR753803 Genomic DNA. Translation: CAQ09553.1.
CR925796 Genomic DNA. Translation: CAQ10264.1.
CH471081 Genomic DNA. Translation: EAX03581.1.
U52694 Genomic DNA. Translation: AAG14900.1.
U52696 mRNA. Translation: AAC50888.1. Frameshift.
U52693 Genomic DNA. Translation: AAG14898.1. Frameshift.
U52701 mRNA. Translation: AAC50883.1. Sequence problems.
IPIIPI00004084.
IPI00221087.
RefSeqNP_001129625.1.
NP_004372.3.
UniGeneHs.42853

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ99941.

Proteomic databases

PRIDEQ99941.

Genome annotation databases

EnsemblENST00000293709; ENSP00000293709; ENSG00000168468; Homo sapiens. [Genome view]
ENST00000375203; ENSP00000364349; ENSG00000213676; Homo sapiens. [Genome view]
ENST00000425571; ENSP00000404814; ENSG00000228628; Homo sapiens. [Genome view]
ENST00000427136; ENSP00000404725; ENSG00000234539; Homo sapiens. [Genome view]
GeneID1388.
KEGGhsa:1388.
NMPDRfig|9606.3.peg.26896.
UCSCuc003nzn.1. human.
uc003nzo.1. human.

Organism-specific databases

CTD1388.
GeneCardsGC06M032194.
H-InvDBHIX0019631.
HIX0057941.
HGNCHGNC:2349. ATF6B.
MIM600984. gene.
PharmGKBPA26867.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ99941.
InParanoidQ99941.
OMARPERKSI.
OrthoDBEOG9HQH3H.

Gene expression databases

GenevestigatorQ99941.
GermOnlineENSG00000168477. Homo sapiens.

Family and domain databases

InterProIPR011616. bZIP_1.
IPR004827. TF_bZIP.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio5641.
PMAP-CutDBQ99941.
SOURCESearch...

Entry information

Entry nameATF6B_HUMAN
AccessionPrimary (citable) accession number: Q99941
Secondary accession number(s): Q13269 expand/collapse secondary AC list , Q14343, Q14345, Q5SSW7, Q99635, Q99637, Q9H3V9, Q9H3W1, Q9NPL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: December 15, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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 6

Human chromosome 6: 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents