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Reviewed, UniProtKB/Swiss-Prot P45880 (VDAC2_HUMAN)

Last modified October 13, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Voltage-dependent anion-selective channel protein 2
      Short name=VDAC-2
      Short name=hVDAC2
Alternative name(s):
    Outer mitochondrial membrane protein porin 2
Gene names
Name: VDAC2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective.

Subunit structure

Interacts with hexokinases By similarity.

Subcellular location

Mitochondrion outer membrane. Ref.9

Tissue specificity

Expressed in all tissues examined.

Domain

Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands By similarity.

Sequence similarities

Belongs to the eukaryotic mitochondrial porin family.

Sequence caution

The sequence CAH73106.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40910.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BAK1Q166111EBI-354022,EBI-519866
SERINC3Q135301EBI-354022,EBI-1045571

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: P45880-3)

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.
Isoform 1 (identifier: P45880-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MATHGQTCARP → MSWCNELRLPALKQHSIGRGLESHIT
Note: Ref.1 (AAA60144) sequence differs from that shown due to a frameshift in position 303.
Isoform 2 (identifier: P45880-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.
Note: Ref.1 (AAA60145) sequence differs from that shown due to a frameshift in position 277.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Voltage-dependent anion-selective channel protein 2
PRO_0000050505

Regions

Transmembrane37 – 4610Transmembrane beta-strand By similarity
Transmembrane50 – 589Transmembrane beta-strand By similarity
Transmembrane65 – 7511Transmembrane beta-strand By similarity
Transmembrane80 – 878Transmembrane beta-strand By similarity
Transmembrane91 – 10010Transmembrane beta-strand By similarity
Transmembrane106 – 11510Transmembrane beta-strand By similarity
Transmembrane122 – 13110Transmembrane beta-strand By similarity
Transmembrane134 – 1418Transmembrane beta-strand By similarity
Transmembrane148 – 1569Transmembrane beta-strand By similarity
Transmembrane161 – 1699Transmembrane beta-strand By similarity
Transmembrane174 – 18613Transmembrane beta-strand By similarity
Transmembrane189 – 1968Transmembrane beta-strand By similarity
Transmembrane200 – 20910Transmembrane beta-strand By similarity
Transmembrane213 – 22210Transmembrane beta-strand By similarity
Transmembrane229 – 23810Transmembrane beta-strand By similarity
Transmembrane242 – 2498Transmembrane beta-strand By similarity
Transmembrane253 – 26210Transmembrane beta-strand By similarity
Transmembrane265 – 27410Transmembrane beta-strand By similarity
Transmembrane284 – 29310Transmembrane beta-strand By similarity
Nucleotide binding253 – 2553NAD By similarity
Nucleotide binding271 – 2755NAD By similarity

Sites

Site841Involved in hexokinase binding By similarity

Amino acid modifications

Modified residue311N6-acetyllysine Ref.14
Modified residue391N6-acetyllysine Ref.14
Modified residue721N6-acetyllysine Ref.14
Modified residue741N6-acetyllysine Ref.14
Modified residue1151Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13
Modified residue2061Phosphotyrosine By similarity
Modified residue2361Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 1111MATHGQTCARP → MSWCNELRLPALKQHSIGRG LESHIT in isoform 1.
VSP_005077
Alternative sequence1 – 1111Missing in isoform 2.
VSP_005076
Natural variant241A → V
VAR_006380

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: F4EAE732E653637E

FASTA29431,567
        10         20         30         40         50         60 
MATHGQTCAR PMCIPPSYAD LGKAARDIFN KGFGFGLVKL DVKTKSCSGV EFSTSGSSNT 

        70         80         90        100        110        120 
DTGKVTGTLE TKYKWCEYGL TFTEKWNTDN TLGTEIAIED QICQGLKLTF DTTFSPNTGK 

       130        140        150        160        170        180 
KSGKIKSSYK RECINLGCDV DFDFAGPAIH GSAVFGYEGW LAGYQMTFDS AKSKLTRNNF 

       190        200        210        220        230        240 
AVGYRTGDFQ LHTNVNDGTE FGGSIYQKVC EDLDTSVNLA WTSGTNCTRF GIAAKYQLDP 

       250        260        270        280        290 
TASISAKVNN SSLIGVGYTQ TLRPGVKLTL SALVDGKSIN AGGHKVGLAL ELEA 

« Hide

Isoform 1.

Checksum: 7A94C18F1C07DEBA
Show »

FASTA30933,372
Isoform 2.

Checksum: 9A66CDF9CF0542B9
Show »

FASTA28330,412

References

« Hide 'large scale' references
[1]"A mitochondrial porin cDNA predicts the existence of multiple human porins."
Ha H., Hajek P., Bedwell D.M., Burrows P.D.
J. Biol. Chem. 268:12143-12149(1993) [PubMed: 7685033] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: B-cell.
[2]"Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel."
Blachly-Dyson E., Zambronicz E.B., Yu W.H., Adams V., McCabe E.R., Adelman J.P., Colombini M., Forte M.A.
J. Biol. Chem. 268:1835-1841(1993) [PubMed: 8420959] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT VAL-24.
Tissue: Liver.
[3]"Revised fine mapping of the human voltage-dependent anion channel loci by radiation hybrid analysis."
Decker W.K., Bowles K.R., Schatte E.C., Towbin J.A., Craigen W.J.
Mamm. Genome 10:1041-1042(1999) [PubMed: 10501981] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed: 15164054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Cervix and Eye.
[7]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 86-120; 178-229 AND 248-267, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-23 (ISOFORM 3), PROTEIN SEQUENCE OF 46-64; 75-85; 108-120; 178-185; 236-263 AND 268-277 (ISOFORMS 1/2/3), MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[9]"Subcellular localization of human voltage-dependent anion channel isoforms."
Yu W.H., Wolfgang W., Forte M.A.
J. Biol. Chem. 270:13998-14006(1995) [PubMed: 7539795] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, MASS SPECTROMETRY.
Tissue: Platelet.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, MASS SPECTROMETRY.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, MASS SPECTROMETRY.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-39; LYS-72 AND LYS-74, MASS SPECTROMETRY.

Cross-references

Sequence databases

L08666 mRNA. Translation: AAA60144.1. Frameshift.
L08666 mRNA. Translation: AAA60145.1. Frameshift.
L06328 mRNA. Translation: AAB59457.1.
AF152227 expand/collapse EMBL AC list , AF152220, AF152221, AF152222, AF152223, AF152224, AF152225, AF152226 Genomic DNA. Translation: AAD40241.1.
CR456964 mRNA. Translation: CAG33245.1.
AL390034, AL392111 Genomic DNA. Translation: CAH73108.1.
AL392111, AL390034 Genomic DNA. Translation: CAI40914.1.
AL390034, AL392111 Genomic DNA. Translation: CAH73107.1.
AL392111, AL390034 Genomic DNA. Translation: CAI40911.1.
AL390034, AL392111 Genomic DNA. Translation: CAH73106.1. Sequence problems.
AL392111, AL390034 Genomic DNA. Translation: CAI40910.1. Sequence problems.
BC000165 mRNA. Translation: AAH00165.2.
BC012883 mRNA. Translation: AAH12883.2.
BC072407 mRNA. Translation: AAH72407.1.
IPIIPI00024145.
IPI00216026.
IPI00902560.
PIRA45972.
B44422.
RefSeqNP_003366.2.
UniGeneHs.355927

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP45880. 6 interactions.
STRINGP45880.

PTM databases

PhosphoSiteP45880.

2-D gel databases

SWISS-2DPAGEP45880.
DOSAC-COBS-2DPAGEP45880.
OGPP45880.
REPRODUCTION-2DPAGEP45880.

Proteomic databases

PRIDEP45880.

Genome annotation databases

EnsemblENST00000298468; ENSP00000298468; ENSG00000165637; Homo sapiens. [Genome view]
ENST00000313132; ENSP00000361635; ENSG00000165637; Homo sapiens. [Genome view]
ENST00000332211; ENSP00000361686; ENSG00000165637; Homo sapiens. [Genome view]
ENST00000344036; ENSP00000344876; ENSG00000165637; Homo sapiens. [Genome view]
ENST00000413289; ENSP00000389551; ENSG00000165637; Homo sapiens. [Genome view]
ENST00000447677; ENSP00000401492; ENSG00000165637; Homo sapiens. [Genome view]
GeneID7417.
KEGGhsa:7417.
UCSCuc001jwz.1. human.
uc001jxa.1. human.

Organism-specific databases

CTD7417.
GeneCardsGC10P076640.
H-InvDBHIX0008945.
HIX0029994.
HGNCHGNC:12672. VDAC2.
MIM193245. gene.
PharmGKBPA37295.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP45880.

Gene expression databases

ArrayExpressP45880.
BgeeP45880.
CleanExHS_VDAC2.
GenevestigatorP45880.
GermOnlineENSG00000165637. Homo sapiens.

Family and domain databases

InterProIPR001925. Porin_Euk.
[Graphical view]
PfamPF01459. Porin_3. 1 hit.
[Graphical view]
PRINTSPR00185. EUKARYTPORIN.
PROSITEPS00558. EUKARYOTIC_PORIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01375. Dihydroxyaluminium.
NextBio29042.
SOURCESearch...

Entry information

Entry nameVDAC2_HUMAN
AccessionPrimary (citable) accession number: P45880
Secondary accession number(s): Q5VWK1 expand/collapse secondary AC list , Q5VWK3, Q6IB40, Q7L3J5, Q9BWK8, Q9Y5I6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 11, 2007
Last modified: October 13, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents