Full text data of AVEN
AVEN
[Confidence: low (only semi-automatic identification from reviews)]
Cell death regulator Aven
Cell death regulator Aven
UniProt
Q9NQS1
ID AVEN_HUMAN Reviewed; 362 AA.
AC Q9NQS1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=Cell death regulator Aven;
GN Name=AVEN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10949025; DOI=10.1016/S1097-2765(00)00005-8;
RA Chau B.N., Cheng E.H.-Y., Kerr D.A., Hardwick J.M.;
RT "Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-
RT 1.";
RL Mol. Cell 6:31-40(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Protects against apoptosis mediated by Apaf-1.
CC -!- SUBUNIT: Binds Apaf-1, BCL-2 and BAD (Bcl-xl).
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC protein. Note=Associated with intracellular membranes.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, ovary, thymus,
CC prostate, spleen, small intestine, colon, heart, skeletal muscle,
CC liver, kidney and pancreas.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF283508; AAF91470.1; -; mRNA.
DR EMBL; BC010488; AAH10488.1; -; mRNA.
DR EMBL; BC063533; AAH63533.1; -; mRNA.
DR RefSeq; NP_065104.1; NM_020371.2.
DR UniGene; Hs.555966; -.
DR ProteinModelPortal; Q9NQS1; -.
DR MINT; MINT-143075; -.
DR STRING; 9606.ENSP00000306822; -.
DR PhosphoSite; Q9NQS1; -.
DR DMDM; 20454834; -.
DR PaxDb; Q9NQS1; -.
DR PeptideAtlas; Q9NQS1; -.
DR PRIDE; Q9NQS1; -.
DR Ensembl; ENST00000306730; ENSP00000306822; ENSG00000169857.
DR GeneID; 57099; -.
DR KEGG; hsa:57099; -.
DR UCSC; uc001zhj.3; human.
DR CTD; 57099; -.
DR GeneCards; GC15M034158; -.
DR HGNC; HGNC:13509; AVEN.
DR HPA; HPA020863; -.
DR MIM; 605265; gene.
DR neXtProt; NX_Q9NQS1; -.
DR PharmGKB; PA134874337; -.
DR eggNOG; NOG46616; -.
DR HOGENOM; HOG000231429; -.
DR HOVERGEN; HBG024370; -.
DR InParanoid; Q9NQS1; -.
DR OMA; WDRYQDI; -.
DR OrthoDB; EOG74XS8Q; -.
DR PhylomeDB; Q9NQS1; -.
DR ChiTaRS; AVEN; human.
DR GenomeRNAi; 57099; -.
DR NextBio; 62925; -.
DR PMAP-CutDB; Q9NQS1; -.
DR PRO; PR:Q9NQS1; -.
DR Bgee; Q9NQS1; -.
DR CleanEx; HS_AVEN; -.
DR Genevestigator; Q9NQS1; -.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005622; C:intracellular; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR InterPro; IPR026187; Aven.
DR PANTHER; PTHR16524; PTHR16524; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Complete proteome; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 362 Cell death regulator Aven.
FT /FTId=PRO_0000064768.
FT COMPBIAS 5 85 Ala/Gly-rich.
FT MOD_RES 94 94 Phosphoserine.
FT VARIANT 228 228 Q -> R (in dbSNP:rs2241647).
FT /FTId=VAR_020144.
SQ SEQUENCE 362 AA; 38506 MW; D86517BA087232D4 CRC64;
MQAERGARGG RGRRPGRGRP GGDRHSERPG AAAAVARGGG GGGGGDGGGR RGRGRGRGFR
GARGGRGGGG APRGSRREPG GWGAGASAPV EDDSDAETYG EENDEQGNYS KRKIVSNWDR
YQDIEKEVNN ESGESQRGTD FSVLLSSAGD SFSQFRFAEE KEWDSEASCP KQNSAFYVDS
ELLVRALQEL PLCLRLNVAA ELVQGTVPLE VPQVKPKRTD DGKGLGMQLK GPLGPGGRGP
IFELKSVAAG CPVLLGKDNP SPGPSRDSQK PTSPLQSAGD HLEEELDLLL NLDAPIKEGD
NILPDQTSQD LKSKEDGEVV QEEEVCAKPS VTEEKNMEPE QPSTSKNVTE EELEDWLDSM
IS
//
ID AVEN_HUMAN Reviewed; 362 AA.
AC Q9NQS1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=Cell death regulator Aven;
GN Name=AVEN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10949025; DOI=10.1016/S1097-2765(00)00005-8;
RA Chau B.N., Cheng E.H.-Y., Kerr D.A., Hardwick J.M.;
RT "Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-
RT 1.";
RL Mol. Cell 6:31-40(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Protects against apoptosis mediated by Apaf-1.
CC -!- SUBUNIT: Binds Apaf-1, BCL-2 and BAD (Bcl-xl).
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC protein. Note=Associated with intracellular membranes.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, ovary, thymus,
CC prostate, spleen, small intestine, colon, heart, skeletal muscle,
CC liver, kidney and pancreas.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF283508; AAF91470.1; -; mRNA.
DR EMBL; BC010488; AAH10488.1; -; mRNA.
DR EMBL; BC063533; AAH63533.1; -; mRNA.
DR RefSeq; NP_065104.1; NM_020371.2.
DR UniGene; Hs.555966; -.
DR ProteinModelPortal; Q9NQS1; -.
DR MINT; MINT-143075; -.
DR STRING; 9606.ENSP00000306822; -.
DR PhosphoSite; Q9NQS1; -.
DR DMDM; 20454834; -.
DR PaxDb; Q9NQS1; -.
DR PeptideAtlas; Q9NQS1; -.
DR PRIDE; Q9NQS1; -.
DR Ensembl; ENST00000306730; ENSP00000306822; ENSG00000169857.
DR GeneID; 57099; -.
DR KEGG; hsa:57099; -.
DR UCSC; uc001zhj.3; human.
DR CTD; 57099; -.
DR GeneCards; GC15M034158; -.
DR HGNC; HGNC:13509; AVEN.
DR HPA; HPA020863; -.
DR MIM; 605265; gene.
DR neXtProt; NX_Q9NQS1; -.
DR PharmGKB; PA134874337; -.
DR eggNOG; NOG46616; -.
DR HOGENOM; HOG000231429; -.
DR HOVERGEN; HBG024370; -.
DR InParanoid; Q9NQS1; -.
DR OMA; WDRYQDI; -.
DR OrthoDB; EOG74XS8Q; -.
DR PhylomeDB; Q9NQS1; -.
DR ChiTaRS; AVEN; human.
DR GenomeRNAi; 57099; -.
DR NextBio; 62925; -.
DR PMAP-CutDB; Q9NQS1; -.
DR PRO; PR:Q9NQS1; -.
DR Bgee; Q9NQS1; -.
DR CleanEx; HS_AVEN; -.
DR Genevestigator; Q9NQS1; -.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005622; C:intracellular; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR InterPro; IPR026187; Aven.
DR PANTHER; PTHR16524; PTHR16524; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Complete proteome; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 362 Cell death regulator Aven.
FT /FTId=PRO_0000064768.
FT COMPBIAS 5 85 Ala/Gly-rich.
FT MOD_RES 94 94 Phosphoserine.
FT VARIANT 228 228 Q -> R (in dbSNP:rs2241647).
FT /FTId=VAR_020144.
SQ SEQUENCE 362 AA; 38506 MW; D86517BA087232D4 CRC64;
MQAERGARGG RGRRPGRGRP GGDRHSERPG AAAAVARGGG GGGGGDGGGR RGRGRGRGFR
GARGGRGGGG APRGSRREPG GWGAGASAPV EDDSDAETYG EENDEQGNYS KRKIVSNWDR
YQDIEKEVNN ESGESQRGTD FSVLLSSAGD SFSQFRFAEE KEWDSEASCP KQNSAFYVDS
ELLVRALQEL PLCLRLNVAA ELVQGTVPLE VPQVKPKRTD DGKGLGMQLK GPLGPGGRGP
IFELKSVAAG CPVLLGKDNP SPGPSRDSQK PTSPLQSAGD HLEEELDLLL NLDAPIKEGD
NILPDQTSQD LKSKEDGEVV QEEEVCAKPS VTEEKNMEPE QPSTSKNVTE EELEDWLDSM
IS
//
MIM
605265
*RECORD*
*FIELD* NO
605265
*FIELD* TI
*605265 CELL DEATH REGULATOR AVEN
;;AVEN
*FIELD* TX
BCLXL (600039), an antiapoptotic BCL2 family member, is postulated to
read morefunction at multiple stages in the cell death pathway. The possibility
that BCLXL inhibits cell death at a late (postmitochondrial) step in the
death pathway was supported by the study of Chau et al. (2000). Using a
yeast 2-hybrid screen of a B-cell cDNA library, they identified a novel
apoptosis inhibitor, which they termed AVEN (derived from 'Aventine,' a
Roman stronghold), that binds to both BCLXL and the caspase regulator
APAF1 (602233). The AVEN gene encodes a 362-amino acid protein and is
conserved in other mammalian species. Northern blot analysis detected a
1.7-kb AVEN transcript in all adult tissues tested, with highest
expression in heart, skeletal muscle, kidney, liver, pancreas, and
testis; a number of cell lines also expressed AVEN. Only those mutants
of BCLXL that retained their antiapoptotic activity were capable of
binding AVEN. AVEN was shown to interfere with the ability of APAF1 to
self-associate, suggesting that AVEN impairs APAF1-mediated activation
of caspases. Consistent with this idea, AVEN inhibited the proteolytic
activation of caspases in a cell-free extract and suppressed apoptosis
induced by APAF1 plus caspase-9 (CASP9; 602234). Thus, AVEN represents a
novel class of cell death regulator.
By genomic sequencing, Chau et al. (2000) mapped the AVEN gene to
chromosome 15.
*FIELD* RF
1. Chau, B. N.; Cheng, E. H.-Y.; Kerr, D. A.; Hardwick, J. M.: Aven,
a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1. Molec.
Cell 6: 31-40, 2000.
*FIELD* CD
Stylianos E. Antonarakis: 9/14/2000
*FIELD* ED
mgross: 09/14/2000
*RECORD*
*FIELD* NO
605265
*FIELD* TI
*605265 CELL DEATH REGULATOR AVEN
;;AVEN
*FIELD* TX
BCLXL (600039), an antiapoptotic BCL2 family member, is postulated to
read morefunction at multiple stages in the cell death pathway. The possibility
that BCLXL inhibits cell death at a late (postmitochondrial) step in the
death pathway was supported by the study of Chau et al. (2000). Using a
yeast 2-hybrid screen of a B-cell cDNA library, they identified a novel
apoptosis inhibitor, which they termed AVEN (derived from 'Aventine,' a
Roman stronghold), that binds to both BCLXL and the caspase regulator
APAF1 (602233). The AVEN gene encodes a 362-amino acid protein and is
conserved in other mammalian species. Northern blot analysis detected a
1.7-kb AVEN transcript in all adult tissues tested, with highest
expression in heart, skeletal muscle, kidney, liver, pancreas, and
testis; a number of cell lines also expressed AVEN. Only those mutants
of BCLXL that retained their antiapoptotic activity were capable of
binding AVEN. AVEN was shown to interfere with the ability of APAF1 to
self-associate, suggesting that AVEN impairs APAF1-mediated activation
of caspases. Consistent with this idea, AVEN inhibited the proteolytic
activation of caspases in a cell-free extract and suppressed apoptosis
induced by APAF1 plus caspase-9 (CASP9; 602234). Thus, AVEN represents a
novel class of cell death regulator.
By genomic sequencing, Chau et al. (2000) mapped the AVEN gene to
chromosome 15.
*FIELD* RF
1. Chau, B. N.; Cheng, E. H.-Y.; Kerr, D. A.; Hardwick, J. M.: Aven,
a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1. Molec.
Cell 6: 31-40, 2000.
*FIELD* CD
Stylianos E. Antonarakis: 9/14/2000
*FIELD* ED
mgross: 09/14/2000