VDAC2_HUMAN
ID VDAC2_HUMAN Reviewed; 294 AA.
AC P45880; Q5VWK1; Q5VWK3; Q6IB40; Q7L3J5; Q9BWK8; Q9Y5I6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Voltage-dependent anion-selective channel protein 2;
DE Short=VDAC-2;
DE Short=hVDAC2;
DE AltName: Full=Outer mitochondrial membrane protein porin 2;
GN Name=VDAC2;
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] (ISOFORMS 1 AND 2).
RC TISSUE=B-cell;
RX PubMed=7685033; DOI=10.1016/s0021-9258(19)50319-2;
RA Ha H., Hajek P., Bedwell D.M., Burrows P.D.;
RT "A mitochondrial porin cDNA predicts the existence of multiple human
RT porins.";
RL J. Biol. Chem. 268:12143-12149(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND VARIANT
RP VAL-24.
RC TISSUE=Liver;
RX PubMed=8420959; DOI=10.1016/s0021-9258(18)53930-2;
RA Blachly-Dyson E., Zambronicz E.B., Yu W.H., Adams V., McCabe E.R.,
RA Adelman J.P., Colombini M., Forte M.A.;
RT "Cloning and functional expression in yeast of two human isoforms of the
RT outer mitochondrial membrane channel, the voltage-dependent anion
RT channel.";
RL J. Biol. Chem. 268:1835-1841(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RX PubMed=10501981; DOI=10.1007/s003359901158;
RA Decker W.K., Bowles K.R., Schatte E.C., Towbin J.A., Craigen W.J.;
RT "Revised fine mapping of the human voltage-dependent anion channel loci by
RT radiation hybrid analysis.";
RL Mamm. Genome 10:1041-1042(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Cervix, and Eye;
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 [7]
RP PROTEIN SEQUENCE OF 86-120; 178-229 AND 248-267, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 11-23 (ISOFORM 3), PROTEIN SEQUENCE OF 46-64; 75-85;
RP 108-120; 178-185; 236-263 AND 268-277 (ISOFORMS 1/2/3), AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=7539795; DOI=10.1074/jbc.270.23.13998;
RA Yu W.H., Wolfgang W., Forte M.A.;
RT "Subcellular localization of human voltage-dependent anion channel
RT isoforms.";
RL J. Biol. Chem. 270:13998-14006(1995).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-31, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP IDENTIFICATION BY 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 [20]
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 [21]
RP UBIQUITINATION AT LYS-31; LYS-64; LYS-72; LYS-120; LYS-121; LYS-124;
RP LYS-277 AND LYS-285.
RX PubMed=25621951; DOI=10.1038/ncb3097;
RA Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
RA Kirkpatrick D.S., Bingol B., Corn J.E.;
RT "USP30 and parkin homeostatically regulate atypical ubiquitin chains on
RT mitochondria.";
RL Nat. Cell Biol. 17:160-169(2015).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=27641616; DOI=10.1038/srep33516;
RA Marginedas-Freixa I., Hattab C., Bouyer G., Halle F., Chene A.,
RA Lefevre S.D., Cambot M., Cueff A., Schmitt M., Gamain B., Lacapere J.J.,
RA Egee S., Bihel F., Le Van Kim C., Ostuni M.A.;
RT "TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to
RT the inhibition of P. falciparum growth in human blood.";
RL Sci. Rep. 6:33516-33516(2016).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF GLU-84.
RX PubMed=31015432; DOI=10.1038/s41467-019-09654-4;
RA Dadsena S., Bockelmann S., Mina J.G.M., Hassan D.G., Korneev S.,
RA Razzera G., Jahn H., Niekamp P., Mueller D., Schneider M., Tafesse F.G.,
RA Marrink S.J., Melo M.N., Holthuis J.C.M.;
RT "Ceramides bind VDAC2 to trigger mitochondrial apoptosis.";
RL Nat. Commun. 10:1832-1832(2019).
CC -!- FUNCTION: Forms a channel through the mitochondrial outer membrane that
CC allows diffusion of small hydrophilic molecules (By similarity). The
CC channel adopts an open conformation at low or zero membrane potential
CC and a closed conformation at potentials above 30-40 mV (By similarity).
CC The open state has a weak anion selectivity whereas the closed state is
CC cation-selective (By similarity). Binds various lipids, including the
CC sphingolipid ceramide, the phospholipid phosphatidylcholine, and the
CC sterol cholesterol (PubMed:31015432). Binding of ceramide promotes the
CC mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway
CC (PubMed:31015432). {ECO:0000250|UniProtKB:P21796,
CC ECO:0000269|PubMed:31015432}.
CC -!- SUBUNIT: Interacts with hexokinases (By similarity). Interacts with
CC ARMC12 in a TBC1D21-dependent manner (By similarity). Interacts with
CC KLC3 (By similarity). Interacts with SPATA33 (By similarity). Interacts
CC with PPP3CC in a SPATA33-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P21796, ECO:0000250|UniProtKB:Q60930}.
CC -!- INTERACTION:
CC P45880; Q6NUP5: AGTR1; NbExp=3; IntAct=EBI-354022, EBI-10232010;
CC P45880; Q92870-2: APBB2; NbExp=3; IntAct=EBI-354022, EBI-21535880;
CC P45880; P42331-2: ARHGAP25; NbExp=3; IntAct=EBI-354022, EBI-21499901;
CC P45880; P46379-2: BAG6; NbExp=3; IntAct=EBI-354022, EBI-10988864;
CC P45880; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-354022, EBI-2837444;
CC P45880; P48643: CCT5; NbExp=3; IntAct=EBI-354022, EBI-355710;
CC P45880; P07339: CTSD; NbExp=3; IntAct=EBI-354022, EBI-2115097;
CC P45880; P29692-2: EEF1D; NbExp=3; IntAct=EBI-354022, EBI-5280572;
CC P45880; Q96A26: FAM162A; NbExp=2; IntAct=EBI-354022, EBI-6123466;
CC P45880; Q06787-7: FMR1; NbExp=3; IntAct=EBI-354022, EBI-25856644;
CC P45880; P28799: GRN; NbExp=3; IntAct=EBI-354022, EBI-747754;
CC P45880; P04792: HSPB1; NbExp=3; IntAct=EBI-354022, EBI-352682;
CC P45880; P42858: HTT; NbExp=22; IntAct=EBI-354022, EBI-466029;
CC P45880; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-354022, EBI-6398041;
CC P45880; O60333-2: KIF1B; NbExp=3; IntAct=EBI-354022, EBI-10975473;
CC P45880; O14901: KLF11; NbExp=3; IntAct=EBI-354022, EBI-948266;
CC P45880; P49821: NDUFV1; NbExp=3; IntAct=EBI-354022, EBI-748312;
CC P45880; P07196: NEFL; NbExp=3; IntAct=EBI-354022, EBI-475646;
CC P45880; O43933: PEX1; NbExp=3; IntAct=EBI-354022, EBI-988601;
CC P45880; D3DTS7: PMP22; NbExp=3; IntAct=EBI-354022, EBI-25882629;
CC P45880; O60260-5: PRKN; NbExp=6; IntAct=EBI-354022, EBI-21251460;
CC P45880; P60891: PRPS1; NbExp=3; IntAct=EBI-354022, EBI-749195;
CC P45880; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-354022, EBI-396669;
CC P45880; O94811: TPPP; NbExp=3; IntAct=EBI-354022, EBI-3927802;
CC P45880; P02766: TTR; NbExp=3; IntAct=EBI-354022, EBI-711909;
CC P45880; P21796: VDAC1; NbExp=5; IntAct=EBI-354022, EBI-354158;
CC P45880; O76024: WFS1; NbExp=3; IntAct=EBI-354022, EBI-720609;
CC P45880-3; Q05996: ZP2; NbExp=2; IntAct=EBI-11614013, EBI-1755919;
CC P45880-3; P21754: ZP3; NbExp=2; IntAct=EBI-11614013, EBI-11783624;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:7539795}. Membrane
CC {ECO:0000269|PubMed:27641616}. Note=May localize to non-mitochondrial
CC membranes. {ECO:0000269|PubMed:27641616}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=P45880-3; Sequence=Displayed;
CC Name=1;
CC IsoId=P45880-1; Sequence=VSP_005077;
CC Name=2;
CC IsoId=P45880-2; Sequence=VSP_005076;
CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes (at protein level)
CC (PubMed:27641616). Expressed in all tissues examined (PubMed:8420959).
CC {ECO:0000269|PubMed:27641616, ECO:0000269|PubMed:8420959}.
CC -!- DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19
CC beta-strands. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000269|PubMed:25621951}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION: [Isoform 1]:
CC Sequence=AAA60144.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAA60145.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L08666; AAA60144.1; ALT_FRAME; mRNA.
DR EMBL; L08666; AAA60145.1; ALT_FRAME; mRNA.
DR EMBL; L06328; AAB59457.1; -; mRNA.
DR EMBL; AF152227; AAD40241.1; -; Genomic_DNA.
DR EMBL; AF152220; AAD40241.1; JOINED; Genomic_DNA.
DR EMBL; AF152221; AAD40241.1; JOINED; Genomic_DNA.
DR EMBL; AF152222; AAD40241.1; JOINED; Genomic_DNA.
DR EMBL; AF152223; AAD40241.1; JOINED; Genomic_DNA.
DR EMBL; AF152224; AAD40241.1; JOINED; Genomic_DNA.
DR EMBL; AF152225; AAD40241.1; JOINED; Genomic_DNA.
DR EMBL; AF152226; AAD40241.1; JOINED; Genomic_DNA.
DR EMBL; CR456964; CAG33245.1; -; mRNA.
DR EMBL; AL390034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL392111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000165; AAH00165.2; -; mRNA.
DR EMBL; BC012883; AAH12883.2; -; mRNA.
DR EMBL; BC072407; AAH72407.1; -; mRNA.
DR CCDS; CCDS53544.1; -. [P45880-1]
DR CCDS; CCDS7348.1; -. [P45880-3]
DR PIR; A45972; A45972.
DR PIR; B44422; B44422.
DR RefSeq; NP_001171712.1; NM_001184783.2. [P45880-1]
DR RefSeq; NP_001171752.1; NM_001184823.1. [P45880-3]
DR RefSeq; NP_001311017.1; NM_001324088.1. [P45880-3]
DR RefSeq; NP_003366.2; NM_003375.4. [P45880-3]
DR AlphaFoldDB; P45880; -.
DR SMR; P45880; -.
DR BioGRID; 113260; 372.
DR CORUM; P45880; -.
DR IntAct; P45880; 135.
DR MINT; P45880; -.
DR STRING; 9606.ENSP00000361635; -.
DR BindingDB; P45880; -.
DR ChEMBL; CHEMBL6190; -.
DR DrugBank; DB01375; Aluminium monostearate.
DR DrugBank; DB06098; PRLX 93936.
DR MoonProt; P45880; -.
DR TCDB; 1.B.8.1.12; the mitochondrial and plastid porin (mpp) family.
DR CarbonylDB; P45880; -.
DR GlyGen; P45880; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P45880; -.
DR PhosphoSitePlus; P45880; -.
DR SwissPalm; P45880; -.
DR BioMuta; VDAC2; -.
DR DMDM; 158518391; -.
DR DOSAC-COBS-2DPAGE; P45880; -.
DR OGP; P45880; -.
DR REPRODUCTION-2DPAGE; P45880; -.
DR SWISS-2DPAGE; P45880; -.
DR UCD-2DPAGE; P45880; -.
DR EPD; P45880; -.
DR jPOST; P45880; -.
DR MassIVE; P45880; -.
DR MaxQB; P45880; -.
DR PaxDb; P45880; -.
DR PeptideAtlas; P45880; -.
DR PRIDE; P45880; -.
DR ProteomicsDB; 55687; -. [P45880-3]
DR ProteomicsDB; 55688; -. [P45880-1]
DR ProteomicsDB; 55689; -. [P45880-2]
DR TopDownProteomics; P45880-3; -. [P45880-3]
DR Antibodypedia; 29670; 306 antibodies from 32 providers.
DR DNASU; 7417; -.
DR Ensembl; ENST00000313132.8; ENSP00000361635.1; ENSG00000165637.14. [P45880-1]
DR Ensembl; ENST00000332211.11; ENSP00000361686.3; ENSG00000165637.14. [P45880-3]
DR Ensembl; ENST00000543351.5; ENSP00000443092.1; ENSG00000165637.14. [P45880-3]
DR GeneID; 7417; -.
DR KEGG; hsa:7417; -.
DR MANE-Select; ENST00000332211.11; ENSP00000361686.3; NM_001391963.1; NP_001378892.1.
DR UCSC; uc001jwz.5; human. [P45880-3]
DR CTD; 7417; -.
DR DisGeNET; 7417; -.
DR GeneCards; VDAC2; -.
DR HGNC; HGNC:12672; VDAC2.
DR HPA; ENSG00000165637; Low tissue specificity.
DR MIM; 193245; gene.
DR neXtProt; NX_P45880; -.
DR OpenTargets; ENSG00000165637; -.
DR PharmGKB; PA37295; -.
DR VEuPathDB; HostDB:ENSG00000165637; -.
DR eggNOG; KOG3126; Eukaryota.
DR GeneTree; ENSGT00950000182869; -.
DR HOGENOM; CLU_044399_2_0_1; -.
DR InParanoid; P45880; -.
DR OMA; PWSWRLN; -.
DR OrthoDB; 938262at2759; -.
DR PhylomeDB; P45880; -.
DR TreeFam; TF315091; -.
DR PathwayCommons; P45880; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-8949215; Mitochondrial calcium ion transport.
DR SignaLink; P45880; -.
DR BioGRID-ORCS; 7417; 128 hits in 1082 CRISPR screens.
DR ChiTaRS; VDAC2; human.
DR GeneWiki; VDAC2; -.
DR GenomeRNAi; 7417; -.
DR Pharos; P45880; Tchem.
DR PRO; PR:P45880; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P45880; protein.
DR Bgee; ENSG00000165637; Expressed in esophagus mucosa and 114 other tissues.
DR ExpressionAtlas; P45880; baseline and differential.
DR Genevisible; P45880; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:CAFA.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0097001; F:ceramide binding; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IDA:UniProtKB.
DR GO; GO:0006820; P:anion transport; IDA:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:CAFA.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IMP:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0032272; P:negative regulation of protein polymerization; IEA:Ensembl.
DR CDD; cd07306; Porin3_VDAC; 1.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR001925; Porin_Euk.
DR InterPro; IPR027246; Porin_Euk/Tom40.
DR InterPro; IPR030277; VDAC2.
DR PANTHER; PTHR11743; PTHR11743; 1.
DR PANTHER; PTHR11743:SF12; PTHR11743:SF12; 1.
DR Pfam; PF01459; Porin_3; 1.
DR PRINTS; PR00185; EUKARYTPORIN.
DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Ion transport; Isopeptide bond; Lipid-binding; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; NAD; Nucleotide-binding; Phosphoprotein;
KW Porin; Reference proteome; Transmembrane; Transmembrane beta strand;
KW Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..294
FT /note="Voltage-dependent anion-selective channel protein 2"
FT /id="PRO_0000050505"
FT TRANSMEM 37..46
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 50..58
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 65..75
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 80..87
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 91..100
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 106..115
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 122..131
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 134..141
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 148..156
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 161..169
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 174..186
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 189..196
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 200..209
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 213..222
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 229..238
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 242..249
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 253..262
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 265..274
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 284..293
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 253..255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 271..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT SITE 84
FT /note="Involved in ceramide and phosphatidylcholine
FT binding"
FT /evidence="ECO:0000269|PubMed:31015432"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 31
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 31
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60930"
FT MOD_RES 78
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 120
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60930"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 277
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT VAR_SEQ 1..11
FT /note="MATHGQTCARP -> MSWCNELRLPALKQHSIGRGLESHIT (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:7685033"
FT /id="VSP_005077"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7685033, ECO:0000303|Ref.4"
FT /id="VSP_005076"
FT VARIANT 24
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:8420959"
FT /id="VAR_006380"
FT MUTAGEN 84
FT /note="E->Q: Abolishes ceramide and phosphatidylcholine
FT binding. Decreases apoptosis frequency following
FT mitochondrial targeting of ceramide."
FT /evidence="ECO:0000269|PubMed:31015432"
SQ SEQUENCE 294 AA; 31567 MW; F4EAE732E653637E CRC64;
MATHGQTCAR PMCIPPSYAD LGKAARDIFN KGFGFGLVKL DVKTKSCSGV EFSTSGSSNT
DTGKVTGTLE TKYKWCEYGL TFTEKWNTDN TLGTEIAIED QICQGLKLTF DTTFSPNTGK
KSGKIKSSYK RECINLGCDV DFDFAGPAIH GSAVFGYEGW LAGYQMTFDS AKSKLTRNNF
AVGYRTGDFQ LHTNVNDGTE FGGSIYQKVC EDLDTSVNLA WTSGTNCTRF GIAAKYQLDP
TASISAKVNN SSLIGVGYTQ TLRPGVKLTL SALVDGKSIN AGGHKVGLAL ELEA
