AVEN_HUMAN
ID AVEN_HUMAN Reviewed; 362 AA.
AC Q9NQS1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cell death regulator Aven;
GN Name=AVEN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10949025; DOI=10.1016/s1097-2765(05)00021-3;
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-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 project:
RT 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-230, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 protein.
CC 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.
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DR EMBL; AF283508; AAF91470.1; -; mRNA.
DR EMBL; BC010488; AAH10488.1; -; mRNA.
DR EMBL; BC063533; AAH63533.1; -; mRNA.
DR CCDS; CCDS10030.1; -.
DR RefSeq; NP_065104.1; NM_020371.2.
DR AlphaFoldDB; Q9NQS1; -.
DR BioGRID; 121366; 19.
DR IntAct; Q9NQS1; 5.
DR MINT; Q9NQS1; -.
DR STRING; 9606.ENSP00000306822; -.
DR GlyGen; Q9NQS1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQS1; -.
DR PhosphoSitePlus; Q9NQS1; -.
DR BioMuta; AVEN; -.
DR DMDM; 20454834; -.
DR EPD; Q9NQS1; -.
DR jPOST; Q9NQS1; -.
DR MassIVE; Q9NQS1; -.
DR MaxQB; Q9NQS1; -.
DR PaxDb; Q9NQS1; -.
DR PeptideAtlas; Q9NQS1; -.
DR PRIDE; Q9NQS1; -.
DR ProteomicsDB; 82177; -.
DR Antibodypedia; 9528; 365 antibodies from 32 providers.
DR DNASU; 57099; -.
DR Ensembl; ENST00000306730.8; ENSP00000306822.3; ENSG00000169857.9.
DR GeneID; 57099; -.
DR KEGG; hsa:57099; -.
DR MANE-Select; ENST00000306730.8; ENSP00000306822.3; NM_020371.3; NP_065104.1.
DR UCSC; uc001zhj.4; human.
DR CTD; 57099; -.
DR DisGeNET; 57099; -.
DR GeneCards; AVEN; -.
DR HGNC; HGNC:13509; AVEN.
DR HPA; ENSG00000169857; Low tissue specificity.
DR MIM; 605265; gene.
DR neXtProt; NX_Q9NQS1; -.
DR OpenTargets; ENSG00000169857; -.
DR PharmGKB; PA134874337; -.
DR VEuPathDB; HostDB:ENSG00000169857; -.
DR eggNOG; ENOG502S0YI; Eukaryota.
DR GeneTree; ENSGT00390000003299; -.
DR HOGENOM; CLU_074829_0_0_1; -.
DR InParanoid; Q9NQS1; -.
DR OMA; WDRYQDI; -.
DR OrthoDB; 1340211at2759; -.
DR PhylomeDB; Q9NQS1; -.
DR TreeFam; TF332067; -.
DR PathwayCommons; Q9NQS1; -.
DR Reactome; R-HSA-111458; Formation of apoptosome.
DR Reactome; R-HSA-9627069; Regulation of the apoptosome activity.
DR SignaLink; Q9NQS1; -.
DR SIGNOR; Q9NQS1; -.
DR BioGRID-ORCS; 57099; 31 hits in 1076 CRISPR screens.
DR ChiTaRS; AVEN; human.
DR GenomeRNAi; 57099; -.
DR Pharos; Q9NQS1; Tbio.
DR PRO; PR:Q9NQS1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9NQS1; protein.
DR Bgee; ENSG00000169857; Expressed in heart right ventricle and 166 other tissues.
DR ExpressionAtlas; Q9NQS1; baseline and differential.
DR Genevisible; Q9NQS1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
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 GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR InterPro; IPR026187; Aven.
DR PANTHER; PTHR16524; PTHR16524; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Membrane; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..362
FT /note="Cell death regulator Aven"
FT /id="PRO_0000064768"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 230
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VARIANT 228
FT /note="Q -> R (in dbSNP:rs2241647)"
FT /id="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