Reviewed, UniProtKB/Swiss-Prot P21796 (VDAC1_HUMAN)

Names and origin

Protein names

Recommended name:
    Voltage-dependent anion-selective channel protein 1
      Short name=VDAC-1
      Short name=hVDAC1
Alternative name(s):
    Outer mitochondrial membrane protein porin 1
    Plasmalemmal porin
    Porin 31HL
    Porin 31HM

Gene names

Name:	VDAC1
Synonyms:	VDAC

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It 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. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. Ref.17 Ref.18 Ref.33
Subunit structure	Interacts with hexokinases By similarity. Interacts with BCL2L1. Interacts with influenza A virus PB1-F2 protein. Ref.33 Ref.21
Subcellular location	Mitochondrion outer membrane. Cell membrane Ref.15.
Tissue specificity	Heart, liver and skeletal muscle.
Domain	Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands. The helical N-terminus folds back into the pore opening and plays a role in voltage-gated channel activity.
Sequence similarities	Belongs to the eukaryotic mitochondrial porin family.

Ontologies

Keywords
Biological process	Apoptosis Host-virus interaction Ion transport Transport
Cellular component	Cell membrane Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Molecular function	Porin
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anion transport Ref.1 Traceable author statement. Source: ProtInc apoptosis Traceable author statement. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW transmembrane transport Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial nucleoid Inferred from direct assay. Source: UniProtKB mitochondrial outer membrane Ref.1 Traceable author statement. Source: ProtInc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell pore complex Traceable author statement. Source: HGNC
Molecular function	protein binding Inferred from physical interaction. Source: IntAct voltage-gated anion channel activity Ref.1 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DCD	P81605	1	EBI-354158,EBI-395625
GABARAPL2	P60520	1	EBI-354158,EBI-720116
KIF5B	P33176	1	EBI-354158,EBI-355878
MCC	P23508	1	EBI-354158,EBI-307531
PANK2	Q9BZ23	1	EBI-354158,EBI-1058434
TRAF6	Q9Y4K3	1	EBI-354158,EBI-359276

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9 Ref.10 Ref.11 Ref.12

Chain

2 – 283

282

Voltage-dependent anion-selective channel protein 1

PRO_0000050499

Regions

Transmembrane

26 – 35

10

Transmembrane beta-strand

Transmembrane

39 – 47

9

Transmembrane beta-strand

Transmembrane

54 – 64

11

Transmembrane beta-strand

Transmembrane

69 – 76

8

Transmembrane beta-strand

Transmembrane

80 – 89

10

Transmembrane beta-strand

Transmembrane

95 – 104

10

Transmembrane beta-strand

Transmembrane

111 – 120

10

Transmembrane beta-strand

Transmembrane

123 – 130

8

Transmembrane beta-strand

Transmembrane

137 – 145

9

Transmembrane beta-strand

Transmembrane

150 – 158

9

Transmembrane beta-strand

Transmembrane

163 – 175

13

Transmembrane beta-strand

Transmembrane

178 – 185

8

Transmembrane beta-strand

Transmembrane

189 – 198

10

Transmembrane beta-strand

Transmembrane

202 – 211

10

Transmembrane beta-strand

Transmembrane

218 – 227

10

Transmembrane beta-strand

Transmembrane

231 – 238

8

Transmembrane beta-strand

Transmembrane

242 – 251

10

Transmembrane beta-strand

Transmembrane

254 – 263

10

Transmembrane beta-strand

Transmembrane

273 – 282

10

Transmembrane beta-strand

Nucleotide binding

242 – 244

3

NAD

Nucleotide binding

260 – 264

5

NAD

Sites

Site

73

1

Involved in hexokinase binding By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.9 Ref.12 Ref.30

Modified residue

13

1

Phosphoserine By similarity

Modified residue

20

1

N6-acetyllysine Ref.31

Modified residue

28

1

N6-acetyllysine Ref.31

Modified residue

61

1

N6-acetyllysine Ref.31

Modified residue

67

1

Phosphotyrosine Ref.24

Modified residue

101

1

Phosphoserine Ref.28

Modified residue

104

1

Phosphoserine Ref.30 Ref.28 Ref.19 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27

Modified residue

107

1

Phosphothreonine Ref.25

Modified residue

137

1

Phosphoserine By similarity

Modified residue

195

1

Phosphotyrosine Ref.20

Modified residue

224

1

N6-acetyllysine Ref.31

Modified residue

266

1

N6-acetyllysine Ref.31

Experimental info

Sequence conflict

225

1

Y → L in CAB58127. Ref.4

Secondary structure

1

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283

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Helix

15 – 18

4

Beta strand

30 – 34

5

Beta strand

40 – 43

4

Turn

49 – 52

4

Beta strand

59 – 63

5

Beta strand

70 – 73

4

Beta strand

77 – 79

3

Beta strand

84 – 86

3

Beta strand

98 – 100

3

Beta strand

113 – 115

3

Beta strand

157 – 161

5

Beta strand

173 – 175

3

Beta strand

178 – 182

5

Beta strand

193 – 196

4

Beta strand

203 – 211

9

Beta strand

222 – 224

3

Beta strand

228 – 232

5

Beta strand

239 – 241

3

Sequences

	Sequence		Length	Mass (Da)
	P21796-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 89BA3378B04020D5	FASTA	283	30,773
	10 20 30 40 50 60 MAVPPTYADL GKSARDVFTK GYGFGLIKLD LKTKSENGLE FTSSGSANTE TTKVTGSLET 70 80 90 100 110 120 KYRWTEYGLT FTEKWNTDNT LGTEITVEDQ LARGLKLTFD SSFSPNTGKK NAKIKTGYKR 130 140 150 160 170 180 EHINLGCDMD FDIAGPSIRG ALVLGYEGWL AGYQMNFETA KSRVTQSNFA VGYKTDEFQL 190 200 210 220 230 240 HTNVNDGTEF GGSIYQKVNK KLETAVNLAW TAGNSNTRFG IAAKYQIDPD ACFSAKVNNS 250 260 270 280 SLIGLGYTQT LKPGIKLTLS ALLDGKNVNA GGHKLGLGLE FQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"Cloning of human VDAC cDNA." Blachly-Dyson E., Forte M.A. Biophys. J. 59:216A-216A(1991) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pituitary.
[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].
[4]	"Characterization of the human porin isoform 1 (HVDAC1) gene by amplification on the whole human genome: a tool for porin deficiency analysis." Messina A., Guarino F., Oliva M., van den Heuvel L.P., Smeitink J., De Pinto V. Biochem. Biophys. Res. Commun. 270:787-792(2000) [PubMed: 10772903] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
[6]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed: 15372022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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]. Tissue: Lung and Skin.
[9]	"Identification of human porins. II. Characterization and primary structure of a 31-lDa porin from human B lymphocytes (Porin 31HL)." Kayser H., Kratzin H.D., Thinnes F.P., Goetz H., Schmidt W.E., Eckart K., Hilschmann N. Biol. Chem. Hoppe-Seyler 370:1265-1278(1989) [PubMed: 2559745] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-283. Tissue: Lymphocyte.
[10]	"Studies on human porin. IV. The primary structures of 'Porin 31HM' purified from human skeletal muscle membranes and of 'Porin 31HL' derived from human B lymphocyte membranes are identical." Juergens L., Ilsemann P., Kratzin H.D., Hesse D., Eckart K., Thinnes F.P., Hilschmann N. Biol. Chem. Hoppe-Seyler 372:455-463(1991) [PubMed: 1657034] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-283. Tissue: Skeletal muscle.
[11]	Hein A., Kiafard Z., Hesse D., Hesse J.-O., Zimmermann B., Kratzin H.D., Schulz H., Reiss J., Thinnes F.P., Goetz H., Hilschmann N. Submitted (DEC-1997) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-283. Tissue: B-cell.
[12]	Bienvenut W.V. Submitted (MAR-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12; 21-61; 64-74; 94-110; 121-139; 162-174; 225-236 AND 257-274, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[13]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 75-93; 175-197 AND 201-218, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[14]	"Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel." Thomas L., Blachly-Dyson E., Colombini M., Forte M.A. Proc. Natl. Acad. Sci. U.S.A. 90:5446-5449(1993) [PubMed: 7685903] [Abstract] Cited for: MUTAGENESIS.
[15]	"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.
[16]	"Mitochondria-derived and extra-mitochondrial human type-1 porin are identical as revealed by amino acid sequencing and electrophysiological characterisation." Stadtmueller U., Eben-Brunnen J., Schmid A., Hesse D., Klebert S., Kratzin H.D., Hesse J., Zimmermann B., Reymann S., Thinnes F.P., Benz R., Goetz H., Hilschmann N. Biol. Chem. 380:1461-1466(1999) [PubMed: 10661876] [Abstract] Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
[17]	"Gadolinium as an opener of the outwardly rectifying Cl(-) channel (ORCC). Is there relevance for cystic fibrosis therapy?" Thinnes F.P., Walter G., Hellmann K.P., Hellmann T., Merker R., Kiafard Z., Eben-Brunnen J., Schwarzer C., Goetz H., Hilschmann N. Pflugers Arch. 443:S111-S116(2001) [PubMed: 11845315] [Abstract] Cited for: FUNCTION.
[18]	"Study of PTPC composition during apoptosis for identification of viral protein target." Verrier F., Mignotte B., Jan G., Brenner C. Ann. N. Y. Acad. Sci. 1010:126-142(2003) [PubMed: 15033708] [Abstract] Cited for: FUNCTION IN APOPTOSIS.
[19]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY. Tissue: Epithelium.
[20]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, MASS SPECTROMETRY.
[21]	"Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1." Zamarin D., Garcia-Sastre A., Xiao X., Wang R., Palese P. PLoS Pathog. 1:40-54(2005) [PubMed: 16201016] [Abstract] Cited for: INTERACTION WITH INFLUENZA A VIRUS PB1-F2.
[22]	"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-104, MASS SPECTROMETRY. Tissue: Epithelium.
[23]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY. Tissue: Epithelium.
[24]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, MASS SPECTROMETRY.
[25]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND THR-107, MASS SPECTROMETRY.
[26]	"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-104, MASS SPECTROMETRY. Tissue: Platelet.
[27]	"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-104, MASS SPECTROMETRY.
[28]	"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-101 AND SER-104, MASS SPECTROMETRY.
[29]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[30]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY.
[31]	"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-20; LYS-28; LYS-61; LYS-224 AND LYS-266, MASS SPECTROMETRY.
[32]	"Structure of the human voltage-dependent anion channel." Bayrhuber M., Meins T., Habeck M., Becker S., Giller K., Villinger S., Vonrhein C., Griesinger C., Zweckstetter M., Zeth K. Proc. Natl. Acad. Sci. U.S.A. 105:15370-15375(2008) [PubMed: 18832158] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF 2-283, STRUCTURE BY NMR.
[33]	"Solution structure of the integral human membrane protein VDAC-1 in detergent micelles." Hiller S., Garces R.G., Malia T.J., Orekhov V.Y., Colombini M., Wagner G. Science 321:1206-1210(2008) [PubMed: 18755977] [Abstract] Cited for: STRUCTURE BY NMR, FUNCTION, INTERACTION WITH BCL2L1, NADH BINDING.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L06132 mRNA. Translation: AAA61272.1.
AJ250032 , AJ250033, AJ250034, AJ250035, AJ250036, AJ250037, AJ250038, AJ250039 Genomic DNA. Translation: CAB58127.1.
AF151097 , AF151093, AF151094, AF151095, AF151096 Genomic DNA. Translation: AAD54939.1.
AC005200 Genomic DNA. Translation: AAC24723.1.
AK122953 mRNA. Translation: BAG53816.1.
AC008608 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62281.1.
BC008482 mRNA. Translation: AAH08482.1.
BC071168 mRNA. Translation: AAH71168.1.
BC090042 mRNA. Translation: AAH90042.1.

IPI

IPI00216308.

PIR

MMHUP3. A44422.

RefSeq

NP_003365.1.

UniGene

Hs.519320
Hs.709372

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JK4	X-ray	4.10	A	2-283	[»]
2K4T	NMR	-	A	1-283	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32862N.

IntAct

P21796. 27 interactions.

STRING

P21796.

PTM databases

PhosphoSite

P21796.

2-D gel databases

DOSAC-COBS-2DPAGE

P21796.

OGP

P21796.

REPRODUCTION-2DPAGE

IPI00216308.
P21796.

Proteomic databases

PeptideAtlas

P21796.

PRIDE

P21796.

Genome annotation databases

Ensembl

ENST00000265333; ENSP00000265333; ENSG00000213585; Homo sapiens. [Genome view]
ENST00000395044; ENSP00000378484; ENSG00000213585; Homo sapiens. [Genome view]
ENST00000395047; ENSP00000378487; ENSG00000213585; Homo sapiens. [Genome view]

GeneID

7416.

KEGG

hsa:7416.

UCSC

uc003kyp.1. human.

Organism-specific databases

CTD

7416.

GeneCards

GC05M133336.

H-InvDB

HIX0005171.

HGNC

HGNC:12669. VDAC1.

HPA

CAB005885.

MIM

604492. gene+phenotype.

PharmGKB

PA37292.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG10452.

HOGENOM

HBG396026.

HOVERGEN

P21796.

InParanoid

P21796.

OMA

QKMAVPP.

OrthoDB

EOG92FW36.

PhylomeDB

P21796.

Gene expression databases

ArrayExpress

P21796.

Bgee

P21796.

CleanEx

HS_VDAC1.

Genevestigator

P21796.

GermOnline

ENSG00000073905. Homo sapiens.

Family and domain databases

InterPro

IPR001925. Porin_Euk.
[Graphical view]

Pfam

PF01459. Porin_3. 1 hit.
[Graphical view]

PRINTS

PR00185. EUKARYTPORIN.

PROSITE

PS00558. EUKARYOTIC_PORIN. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

DrugBank

DB01375. Dihydroxyaluminium.

NextBio

29038.

SOURCE

Search...

Entry information

Entry name

VDAC1_HUMAN

Accession

Primary (citable) accession number: P21796
Secondary accession number(s): B3KVK4 , Q5FVE7, Q9UIQ5, Q9UPL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.