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Protein

Cyclic AMP-dependent transcription factor ATF-6 beta

Gene

ATF6B

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

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei410 – 4101Important for cleavage by PS2By similarity
Sitei413 – 4131Important for cleavage by PS2By similarity
Sitei440 – 4412Cleavage; by PS1By similarity

GO - Molecular functioni

GO - Biological processi

  • ATF6-mediated unfolded protein response Source: ParkinsonsUK-UCL
  • positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Unfolded protein response

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following chain:
Gene namesi
Name:ATF6B
Synonyms:CREBL1, G13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:2349. ATF6B.

Subcellular locationi

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

  • Note: Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 396395CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei397 – 41721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini418 – 703286LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  • Golgi apparatus Source: ParkinsonsUK-UCL
  • integral component of endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  • intracellular Source: MGI
  • nucleus Source: ParkinsonsUK-UCL
  • protein-DNA complex Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164716250.

Polymorphism and mutation databases

BioMutaiATF6B.
DMDMi20137431.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 703702Cyclic AMP-dependent transcription factor ATF-6 betaPRO_0000076590Add
BLAST
Chaini2 – ?Processed cyclic AMP-dependent transcription factor ATF-6 betaPRO_0000296201

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi505 – 5051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi627 – 6271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi676 – 6761N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiQ99941.
PaxDbiQ99941.
PRIDEiQ99941.

PTM databases

PhosphoSiteiQ99941.

Miscellaneous databases

PMAP-CutDBQ99941.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ99941.
ExpressionAtlasiQ99941. baseline and differential.
GenevisibleiQ99941. HS.

Organism-specific databases

HPAiHPA046871.

Interactioni

Subunit structurei

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).

Binary interactionsi

WithEntry#Exp.IntActNotes
P279585EBI-2841031,EBI-8763498From a different organism.

Protein-protein interaction databases

BioGridi107778. 27 interactions.
IntActiQ99941. 5 interactions.
STRINGi9606.ENSP00000364349.

Structurei

3D structure databases

ProteinModelPortaliQ99941.
SMRiQ99941. Positions 327-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini325 – 38864bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 8685Transcription activationAdd
BLAST
Regioni327 – 34721Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni350 – 3578Leucine-zipperPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi96 – 10510Poly-Ser

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.
HOVERGENiHBG050608.
InParanoidiQ99941.
KOiK09049.
OMAiEMMQIEC.
PhylomeDBiQ99941.
TreeFamiTF316079.

Family and domain databases

InterProiIPR029809. ATF6B.
IPR004827. bZIP.
[Graphical view]
PANTHERiPTHR22952:SF107. PTHR22952:SF107. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q99941-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAELMLLSEI ADPTRFFTDN LLSPEDWGLQ NSTLYSGLDE VAEEQTQLFR
60 70 80 90 100
CPEQDVPFDG SSLDVGMDVS PSEPPWELLP IFPDLQVKSE PSSPCSSSSL
110 120 130 140 150
SSESSRLSTE PSSEALGVGE VLHVKTESLA PPLCLLGDDP TSSFETVQIN
160 170 180 190 200
VIPTSDDSSD VQTKIEPVSP CSSVNSEASL LSADSSSQAF IGEEVLEVKT
210 220 230 240 250
ESLSPSGCLL WDVPAPSLGA VQISMGPSLD GSSGKALPTR KPPLQPKPVV
260 270 280 290 300
LTTVPMPSRA VPPSTTVLLQ SLVQPPPVSP VVLIQGAIRV QPEGPAPSLP
310 320 330 340 350
RPERKSIVPA PMPGNSCPPE VDAKLLKRQQ RMIKNRESAC QSRRKKKEYL
360 370 380 390 400
QGLEARLQAV LADNQQLRRE NAALRRRLEA LLAENSELKL GSGNRKVVCI
410 420 430 440 450
MVFLLFIAFN FGPVSISEPP SAPISPRMNK GEPQPRRHLL GFSEQEPVQG
460 470 480 490 500
VEPLQGSSQG PKEPQPSPTD QPSFSNLTAF PGGAKELLLR DLDQLFLSSD
510 520 530 540 550
CRHFNRTESL RLADELSGWV QRHQRGRRKI PQRAQERQKS QPRKKSPPVK
560 570 580 590 600
AVPIQPPGPP ERDSVGQLQL YRHPDRSQPA FLDAIDRRED TFYVVSFRRD
610 620 630 640 650
HLLLPAISHN KTSRPKMSLV MPAMAPNETL SGRGAPGDYE EMMQIECEVM
660 670 680 690 700
DTRVIHIKTS TVPPSLRKQP SPTPGNATGG PLPVSAASQA HQASHQPLYL

NHP
Length:703
Mass (Da):76,709
Last modified:January 23, 2002 - v2
Checksum:iB04C7B23E7D83F82
GO
Isoform 1 (identifier: Q99941-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     28-31: GLQN → D

Note: No experimental confirmation available.
Show »
Length:700
Mass (Da):76,412
Checksum:i54C077BF95309216
GO

Sequence cautioni

The sequence AAC50888.1 differs from that shown. Reason: Frameshift at position 600. Curated
The sequence AAG14898.1 differs from that shown. Reason: Frameshift at position 600. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31E → D in CAA66664 (PubMed:8870652).Curated
Sequence conflicti329 – 3302QQ → HE in CAA66664 (PubMed:8870652).Curated
Sequence conflicti520 – 5201V → D in AAC50888 (PubMed:8923003).Curated
Sequence conflicti600 – 6001D → G in AAA97438 (PubMed:8586413).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei28 – 314GLQN → D in isoform 1. 1 PublicationVSP_000593

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4737.1. [Q99941-1]
CCDS47408.1. [Q99941-2]
RefSeqiNP_001129625.1. NM_001136153.1. [Q99941-2]
NP_004372.3. NM_004381.4. [Q99941-1]
UniGeneiHs.42853.

Genome annotation databases

EnsembliENST00000293709; ENSP00000293709; ENSG00000168468.
ENST00000375201; ENSP00000364347; ENSG00000213676. [Q99941-2]
ENST00000375203; ENSP00000364349; ENSG00000213676.
ENST00000383156; ENSP00000372642; ENSG00000168468. [Q99941-2]
ENST00000425571; ENSP00000404814; ENSG00000228628.
ENST00000427136; ENSP00000404725; ENSG00000234539.
ENST00000435768; ENSP00000399764; ENSG00000228628. [Q99941-2]
ENST00000439240; ENSP00000391131; ENSG00000234539. [Q99941-2]
GeneIDi1388.
KEGGihsa:1388.
UCSCiuc003nzn.3. human. [Q99941-1]
uc003nzo.3. human. [Q99941-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4737.1. [Q99941-1]
CCDS47408.1. [Q99941-2]
RefSeqiNP_001129625.1. NM_001136153.1. [Q99941-2]
NP_004372.3. NM_004381.4. [Q99941-1]
UniGeneiHs.42853.

3D structure databases

ProteinModelPortaliQ99941.
SMRiQ99941. Positions 327-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107778. 27 interactions.
IntActiQ99941. 5 interactions.
STRINGi9606.ENSP00000364349.

PTM databases

PhosphoSiteiQ99941.

Polymorphism and mutation databases

BioMutaiATF6B.
DMDMi20137431.

Proteomic databases

MaxQBiQ99941.
PaxDbiQ99941.
PRIDEiQ99941.

Protocols and materials databases

DNASUi1388.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000293709; ENSP00000293709; ENSG00000168468.
ENST00000375201; ENSP00000364347; ENSG00000213676. [Q99941-2]
ENST00000375203; ENSP00000364349; ENSG00000213676.
ENST00000383156; ENSP00000372642; ENSG00000168468. [Q99941-2]
ENST00000425571; ENSP00000404814; ENSG00000228628.
ENST00000427136; ENSP00000404725; ENSG00000234539.
ENST00000435768; ENSP00000399764; ENSG00000228628. [Q99941-2]
ENST00000439240; ENSP00000391131; ENSG00000234539. [Q99941-2]
GeneIDi1388.
KEGGihsa:1388.
UCSCiuc003nzn.3. human. [Q99941-1]
uc003nzo.3. human. [Q99941-2]

Organism-specific databases

CTDi1388.
GeneCardsiGC06M032065.
GC06Mj32014.
GC06Mk32041.
GC06Mm32142.
H-InvDBHIX0166896.
HIX0207573.
HGNCiHGNC:2349. ATF6B.
HPAiHPA046871.
MIMi600984. gene.
neXtProtiNX_Q99941.
PharmGKBiPA164716250.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG236121.
GeneTreeiENSGT00530000063762.
HOVERGENiHBG050608.
InParanoidiQ99941.
KOiK09049.
OMAiEMMQIEC.
PhylomeDBiQ99941.
TreeFamiTF316079.

Miscellaneous databases

ChiTaRSiATF6B. human.
GeneWikiiCREBL1.
GenomeRNAii1388.
NextBioi5641.
PMAP-CutDBQ99941.
PROiQ99941.
SOURCEiSearch...

Gene expression databases

BgeeiQ99941.
ExpressionAtlasiQ99941. baseline and differential.
GenevisibleiQ99941. HS.

Family and domain databases

InterProiIPR029809. ATF6B.
IPR004827. bZIP.
[Graphical view]
PANTHERiPTHR22952:SF107. PTHR22952:SF107. 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. "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.
    , 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATF6B_HUMAN
AccessioniPrimary (citable) accession number: Q99941
Secondary accession number(s): B0UYX6
, Q13269, Q14343, Q14345, Q5SSW7, Q99635, Q99637, Q9H3V9, Q9H3W1, Q9NPL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: July 22, 2015
This is version 157 of the entry and version 2 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.