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Q99941 (ATF6B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. 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

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
Protein G13
cAMP response element-binding protein-related protein
Short name=Creb-rp
cAMP-responsive element-binding protein-like 1
Gene names
Name:ATF6B
Synonyms:CREBL1, G13
OrganismHomo sapiens (Human) [Reference 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 (basic-leucine zipper) 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P279585EBI-2841031,EBI-8763498From a different organism.

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

Initiator methionine11Removed Ref.8
Chain2 – 703702Cyclic AMP-dependent transcription factor ATF-6 beta
PRO_0000076590
Chain2 – ?Processed cyclic AMP-dependent transcription factor ATF-6 betaPRO_0000296201

Regions

Topological domain2 – 396395Cytoplasmic Potential
Transmembrane397 – 41721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain418 – 703286Lumenal Potential
Domain325 – 38864bZIP
Region2 – 8685Transcription activation
Region327 – 34721Basic motif By similarity
Region350 – 3578Leucine-zipper By similarity
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

Modified residue21N-acetylalanine Ref.8 Ref.9
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 [UniParc].

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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: CAQ09552.1.
CR753803 Genomic DNA. Translation: CAQ09553.1.
CR925796 Genomic DNA. Translation: CAQ10263.1.
CR925796 Genomic DNA. Translation: CAQ10264.1.
CH471081 Genomic DNA. Translation: EAX03581.1.
CH471081 Genomic DNA. Translation: EAX03583.1.
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.
RefSeqNP_001129625.1. NM_001136153.1.
NP_004372.3. NM_004381.4.
UniGeneHs.42853.

3D structure databases

ProteinModelPortalQ99941.
SMRQ99941. Positions 327-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107778. 10 interactions.
IntActQ99941. 5 interactions.

PTM databases

PhosphoSiteQ99941.

Polymorphism databases

DMDM20137431.

Proteomic databases

PaxDbQ99941.
PRIDEQ99941.

Protocols and materials databases

DNASU1388.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000293709; ENSP00000293709; ENSG00000168468. [Q99941-1]
ENST00000375201; ENSP00000364347; ENSG00000213676. [Q99941-2]
ENST00000375203; ENSP00000364349; ENSG00000213676. [Q99941-1]
ENST00000383156; ENSP00000372642; ENSG00000168468. [Q99941-2]
ENST00000425571; ENSP00000404814; ENSG00000228628. [Q99941-1]
ENST00000427136; ENSP00000404725; ENSG00000234539. [Q99941-1]
ENST00000435768; ENSP00000399764; ENSG00000228628. [Q99941-2]
ENST00000439240; ENSP00000391131; ENSG00000234539. [Q99941-2]
GeneID1388.
KEGGhsa:1388.
UCSCuc003nzn.3. human. [Q99941-1]
uc003nzo.3. human. [Q99941-2]

Organism-specific databases

CTD1388.
GeneCardsGC06M032065.
GC06Mj32014.
GC06Mk32041.
GC06Mm32142.
H-InvDBHIX0166896.
HIX0207573.
HGNCHGNC:2349. ATF6B.
HPAHPA046871.
MIM600984. gene.
neXtProtNX_Q99941.
PharmGKBPA164716250.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236121.
HOVERGENHBG050608.
InParanoidQ99941.
KOK09049.
OMAEMMQIEC.
PhylomeDBQ99941.
TreeFamTF316079.

Gene expression databases

BgeeQ99941.
GenevestigatorQ99941.

Family and domain databases

InterProIPR004827. 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

ChiTaRSATF6B. human.
GeneWikiCREBL1.
GenomeRNAi1388.
NextBio5641.
PMAP-CutDBQ99941.
PROQ99941.
SOURCESearch...

Entry information

Entry nameATF6B_HUMAN
AccessionPrimary (citable) accession number: Q99941
Secondary accession number(s): B0UYX6 expand/collapse secondary AC list , Q13269, 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: April 16, 2014
This is version 144 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM