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 10-JUN-2026, entry version 224. DE RecName: Full=Non-selective voltage-gated ion channel VDAC2 {ECO:0000305}; DE Short=VDAC-2; DE Short=hVDAC2 {ECO:0000303|PubMed:8420959}; DE AltName: Full=Outer mitochondrial membrane protein porin 2; GN Name=VDAC2 {ECO:0000312|HGNC:HGNC:12672}; 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), FUNCTION, TRANSPORTER ACTIVITY, RP TISSUE SPECIFICITY, AND VARIANT 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). RN [25] RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBUNIT. RX PubMed=38065946; DOI=10.1038/s41467-023-43570-y; RA Jahn H., Bartos L., Dearden G.I., Dittman J.S., Holthuis J.C.M., Vacha R., RA Menon A.K.; RT "Phospholipids are imported into mitochondria by VDAC, a dimeric beta RT barrel scramblase."; RL Nat. Commun. 14:8115-8115(2023). RN [26] {ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, ECO:0007744|PDB:9EIJ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.75 ANGSTROMS) IN COMPLEX WITH PINK1 AND RP THE TOM COMPLEX, FUNCTION, INTERACTION WITH PINK1 AND THE TOM COMPLEX, RP SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=40080546; DOI=10.1126/science.adu6445; RA Callegari S., Kirk N.S., Gan Z.Y., Dite T., Cobbold S.A., Leis A., RA Dagley L.F., Glukhova A., Komander D.; RT "Structure of human PINK1 at a mitochondrial TOM-VDAC array."; RL Science 0:0-0(2025). CC -!- FUNCTION: Non-selective voltage-gated ion channel that mediates the CC transport of anions and cations through the mitochondrion outer CC membrane and plasma membrane (PubMed:8420959). The channel adopts an CC open conformation at zero mV and a closed conformation at both positive CC and negative potentials (PubMed:8420959). There are two populations of CC channels; the main that functions in a lower open-state conductance CC with lower ion selectivity, that switch, in a voltage-dependent manner, CC from the open to a low-conducting 'closed' state and the other that has CC a normal ion selectivity in the typical high conductance, 'open' state CC (PubMed:8420959). Binds various lipids, including the sphingolipid CC ceramide, the phospholipid phosphatidylcholine, and the sterols CC cholesterol and oxysterol (PubMed:31015432). Binding of ceramide CC promotes the mitochondrial outer membrane permeabilization (MOMP) CC apoptotic pathway (PubMed:31015432). Associates with the translocase of CC the outer mitochondrial membrane (TOM) complex and PINK1 kinase at CC depolarized mitochondria, this interaction stabilizes PINK1 at the CC outer mitochondrial membrane and triggers downstream mitophagy by the CC recruitment of the E3 ubiquitin ligase PRKN (PubMed:40080546). CC {ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:40080546, CC ECO:0000269|PubMed:8420959}. CC -!- FUNCTION: Catalyzes the scrambling of phospholipids across the outer CC mitochondrial membrane; the mechanism is unrelated to channel activity CC and is capable of translocating both anionic and zwitterionic CC phospholipids. {ECO:0000269|PubMed:38065946}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:8420959}; CC -!- CATALYTIC ACTIVITY: CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:8420959}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl- CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, CC ChEBI:CHEBI:57262; Evidence={ECO:0000305|PubMed:38065946}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl- CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, CC ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:38065946}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out); CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880; CC Evidence={ECO:0000269|PubMed:38065946}; CC -!- SUBUNIT: Monomer, homodimer and higher order oligomers; formation of CC higher order structures is necessary for scramblase activity CC (PubMed:38065946). Interacts with ARMC12 in a TBC1D21-dependent manner CC (By similarity). Interacts with KLC3 (By similarity). Interacts with CC SPATA33 (By similarity). Interacts with PPP3CC in a SPATA33-dependent CC manner (By similarity). As a homodimer, interacts with the TOM complex CC (PubMed:40080546). Upon mitochondrial depolarization, the TOM-VDAC CC assembly interacts with PINK1; the interaction stabilizes PINK1 at the CC outer mitochondrial membrane and triggers downstream mitophagy CC (PubMed:40080546). {ECO:0000250|UniProtKB:Q60930, CC ECO:0000269|PubMed:38065946, ECO:0000269|PubMed:40080546}. 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; P13569: CFTR; NbExp=10; IntAct=EBI-354022, EBI-349854; 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; A0A6Q8PF08: PMP22; NbExp=3; IntAct=EBI-354022, EBI-50433196; 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=6; IntAct=EBI-354022, EBI-354158; CC P45880; Q9Y277: VDAC3; NbExp=2; IntAct=EBI-354022, EBI-354196; 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}; Multi-pass CC membrane protein {ECO:0000269|PubMed:40080546}. 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|UniProtKB:P21796}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001184783.3. [P45880-1] DR RefSeq; NP_001171752.1; NM_001184823.2. [P45880-3] DR RefSeq; NP_001311017.1; NM_001324088.2. [P45880-3] DR RefSeq; NP_001378892.1; NM_001391963.1. [P45880-3] DR RefSeq; NP_003366.2; NM_003375.4. [P45880-3] DR PDB; 9EIH; EM; 3.10 A; E/F=1-294. DR PDB; 9EII; EM; 2.75 A; F=1-294. DR PDB; 9EIJ; EM; 3.30 A; E/F=1-294. DR PDBsum; 9EIH; -. DR PDBsum; 9EII; -. DR PDBsum; 9EIJ; -. DR AlphaFoldDB; P45880; -. DR EMDB; EMD-48083; -. DR EMDB; EMD-48084; -. DR EMDB; EMD-48085; -. DR SMR; P45880; -. DR BioGRID; 113260; 480. DR CORUM; P45880; -. DR FunCoup; P45880; 2876. DR IntAct; P45880; 196. DR MINT; P45880; -. DR NDEx; IQUERY-CP-VDAC2; 4 NDEx IQuery Curated Pathways. 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 GlyCosmos; P45880; 2 sites, 1 glycan. DR GlyGen; P45880; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (3 sites). DR iPTMnet; P45880; -. DR PhosphoSitePlus; P45880; -. DR SwissPalm; P45880; -. DR BioMuta; VDAC2; -. DR DMDM; 158518391; -. DR OGP; P45880; -. DR REPRODUCTION-2DPAGE; P45880; -. DR jPOST; P45880; -. DR MassIVE; P45880; -. DR PaxDb; 9606-ENSP00000361635; -. DR PeptideAtlas; P45880; -. DR ProteomicsDB; 55687; -. [P45880-3] DR ProteomicsDB; 55688; -. [P45880-1] DR ProteomicsDB; 55689; -. [P45880-2] DR Pumba; P45880; -. DR TopDownProteomics; P45880-3; -. [P45880-3] DR Antibodypedia; 29670; 306 antibodies from 32 providers. DR DNASU; 7417; -. DR Ensembl; ENST00000313132.8; ENSP00000361635.1; ENSG00000165637.15. [P45880-1] DR Ensembl; ENST00000332211.11; ENSP00000361686.3; ENSG00000165637.15. [P45880-3] DR Ensembl; ENST00000543351.5; ENSP00000443092.1; ENSG00000165637.15. [P45880-3] DR Ensembl; ENST00000880919.1; ENSP00000550978.1; ENSG00000165637.15. [P45880-3] DR Ensembl; ENST00000880920.1; ENSP00000550979.1; ENSG00000165637.15. [P45880-3] DR Ensembl; ENST00000880921.1; ENSP00000550980.1; ENSG00000165637.15. [P45880-3] DR Ensembl; ENST00000880922.1; ENSP00000550981.1; ENSG00000165637.15. [P45880-3] DR Ensembl; ENST00000880923.1; ENSP00000550982.1; ENSG00000165637.15. [P45880-3] DR Ensembl; ENST00000880924.1; ENSP00000550983.1; ENSG00000165637.15. [P45880-3] DR Ensembl; ENST00000958957.1; ENSP00000629016.1; ENSG00000165637.15. [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 AGR; HGNC:12672; -. DR ClinPGx; PA37295; -. 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 OpenTargets; ENSG00000165637; -. DR VEuPathDB; HostDB:ENSG00000165637; -. DR eggNOG; KOG3126; Eukaryota. DR GeneTree; ENSGT00950000182869; -. DR HOGENOM; CLU_044399_2_0_1; -. DR InParanoid; P45880; -. DR OMA; FKQPAFH; -. DR OrthoDB; 7827681at2759; -. DR PAN-GO; P45880; 2 GO annotations based on evolutionary models. DR PhylomeDB; P45880; -. DR PathwayCommons; P45880; -. DR Reactome; R-HSA-5205685; PINK1-PRKN Mediated Mitophagy. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-8949215; Mitochondrial calcium ion transport. DR SignaLink; P45880; -. DR Agora; ENSG00000165637; -. DR BioGRID-ORCS; 7417; 144 hits in 1167 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. 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 116 other cell types or tissues. DR ExpressionAtlas; P45880; baseline and differential. 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:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0097001; F:ceramide binding; IDA:UniProtKB. DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB. DR GO; GO:0008142; F:oxysterol binding; ISS:UniProtKB. DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB. DR GO; GO:0017128; F:phospholipid scramblase activity; IDA:UniProtKB. DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW. DR GO; GO:0008308; F:voltage-gated monoatomic anion channel activity; IDA:UniProtKB. DR GO; GO:0005244; F:voltage-gated monoatomic ion channel activity; 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:1990542; P:mitochondrial transmembrane transport; IDA:UniProtKB. DR GO; GO:0006820; P:monoatomic anion transport; IDA:UniProtKB. DR GO; GO:0045332; P:phospholipid translocation; IDA:UniProtKB. DR CDD; cd07306; Porin3_VDAC; 1. DR FunFam; 2.40.160.10:FF:000001; Voltage-dependent anion-selective channel protein 2; 1. DR Gene3D; 2.40.160.10; Porin; 1. DR InterPro; IPR023614; Porin_dom_sf. DR InterPro; IPR001925; Porin_Euk. DR InterPro; IPR027246; Porin_Euk/Tom40. DR PANTHER; PTHR11743; VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL; 1. DR PANTHER; PTHR11743:SF12; VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL PROTEIN 2; 1. DR Pfam; PF01459; Porin_3; 1. DR PRINTS; PR00185; EUKARYTPORIN. DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Direct protein sequencing; Ion transport; Isopeptide bond; Lipid transport; KW Lipid-binding; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD; KW Nucleotide-binding; Phosphoprotein; Porin; Proteomics identification; KW Reference proteome; Transmembrane; Transmembrane beta strand; Transport; KW 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="Non-selective voltage-gated ion channel VDAC2" FT /id="PRO_0000050505" FT TOPO_DOM 2..12 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT INTRAMEM 13..36 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 37..46 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 47..49 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 50..58 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 59..64 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 65..75 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 76..79 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 80..87 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 88..90 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 91..100 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 101..105 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 106..115 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 116..121 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 122..131 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 132..133 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 134..141 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 142..147 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 148..156 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 157..160 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 161..169 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 170..173 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 174..186 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 187..188 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, ECO:0000305, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 189..196 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 197..199 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 200..209 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 210..212 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 213..222 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 223..228 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 229..238 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 239..241 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 242..249 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 250..252 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 253..262 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 263..264 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 265..274 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 275..283 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TRANSMEM 284..293 FT /note="Beta stranded" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT TOPO_DOM 294 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:40080546, FT ECO:0007744|PDB:9EIH, ECO:0007744|PDB:9EII, FT ECO:0007744|PDB:9EIJ" FT MOTIF 244..248 FT /note="Mitochondrial localization signal" FT /evidence="ECO:0000250|UniProtKB:J5JPV3" FT MOTIF 266..276 FT /note="C-terminal beta-signal" FT /evidence="ECO:0000250|UniProtKB:J5JPV3" FT BINDING 23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q60932" FT BINDING 31 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q60932" FT BINDING 253 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P21796" FT BINDING 254 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P21796" FT BINDING 255 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P21796" FT BINDING 272 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P21796" FT BINDING 275 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" 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" FT HELIX 14..17 FT /evidence="ECO:0007829|PDB:9EII" FT HELIX 18..20 FT /evidence="ECO:0007829|PDB:9EII" FT HELIX 23..30 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 37..59 FT /evidence="ECO:0007829|PDB:9EII" FT TURN 60..63 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 64..75 FT /evidence="ECO:0007829|PDB:9EII" FT TURN 76..79 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 80..87 FT /evidence="ECO:0007829|PDB:9EII" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 91..98 FT /evidence="ECO:0007829|PDB:9EII" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 103..115 FT /evidence="ECO:0007829|PDB:9EII" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 120..131 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 134..141 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 148..155 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 157..169 FT /evidence="ECO:0007829|PDB:9EII" FT TURN 170..173 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 174..185 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 187..196 FT /evidence="ECO:0007829|PDB:9EII" FT TURN 197..199 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 200..207 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 210..222 FT /evidence="ECO:0007829|PDB:9EII" FT TURN 223..226 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 227..239 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 242..249 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 253..263 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 266..275 FT /evidence="ECO:0007829|PDB:9EII" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:9EII" FT STRAND 285..293 FT /evidence="ECO:0007829|PDB:9EII" 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 //