P21796 (VDAC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.30
Subunit structure	Interacts with hexokinases By similarity. Interacts with BCL2L1. Interacts with BOP/C22orf29 (via BH3 domain). Interacts with influenza A virus PB1-F2 protein. Ref.19 Ref.28 Ref.30
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 Transmembrane beta strand
Molecular function	Porin
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Traceable author statement PubMed 10365962. Source: UniProtKB behavioral fear response Inferred from electronic annotation. Source: Compara learning Inferred from electronic annotation. Source: Compara neuron-neuron synaptic transmission Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial nucleoid Inferred from direct assay PubMed 18063578. Source: BHF-UCL mitochondrial outer membrane Traceable author statement Ref.1. Source: ProtInc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell pore complex Traceable author statement PubMed 9843949. Source: HGNC
Molecular_function	porin activity Inferred from electronic annotation. Source: UniProtKB-KW voltage-gated anion channel activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HK1	P19367	2	EBI-354158,EBI-713162

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

Beta stranded

Transmembrane

39 – 47

9

Beta stranded

Transmembrane

54 – 64

11

Beta stranded

Transmembrane

69 – 76

8

Beta stranded

Transmembrane

80 – 89

10

Beta stranded

Transmembrane

95 – 104

10

Beta stranded

Transmembrane

111 – 120

10

Beta stranded

Transmembrane

123 – 130

8

Beta stranded

Transmembrane

137 – 145

9

Beta stranded

Transmembrane

150 – 158

9

Beta stranded

Transmembrane

163 – 175

13

Beta stranded

Transmembrane

178 – 185

8

Beta stranded

Transmembrane

189 – 198

10

Beta stranded

Transmembrane

202 – 211

10

Beta stranded

Transmembrane

218 – 227

10

Beta stranded

Transmembrane

231 – 238

8

Beta stranded

Transmembrane

242 – 251

10

Beta stranded

Transmembrane

254 – 263

10

Beta stranded

Transmembrane

273 – 282

10

Beta stranded

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

Modified residue

13

1

Phosphoserine By similarity

Modified residue

20

1

N6-acetyllysine Ref.24

Modified residue

28

1

N6-acetyllysine Ref.24

Modified residue

61

1

N6-acetyllysine Ref.24

Modified residue

67

1

Phosphotyrosine By similarity

Modified residue

101

1

Phosphoserine Ref.23

Modified residue

104

1

Phosphoserine Ref.23 Ref.25 Ref.27

Modified residue

137

1

Phosphoserine By similarity

Modified residue

195

1

Phosphotyrosine By similarity

Modified residue

224

1

N6-acetyllysine Ref.24

Modified residue

266

1

N6-acetyllysine Ref.24

Experimental info

Sequence conflict

225

1

Y → L in CAB58127. Ref.4

Secondary structure

1

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283

Helix Strand Turn

Details...

Turn

7 – 10

4

Beta strand

26 – 33

8

Turn

36 – 38

3

Beta strand

40 – 51

12

Beta strand

55 – 62

8

Beta strand

66 – 76

11

Turn

77 – 79

3

Beta strand

80 – 88

9

Beta strand

95 – 103

9

Turn

105 – 107

3

Beta strand

110 – 119

10

Beta strand

124 – 135

12

Beta strand

137 – 146

10

Beta strand

149 – 158

10

Turn

159 – 162

4

Beta strand

167 – 174

8

Beta strand

176 – 185

10

Turn

186 – 188

3

Beta strand

189 – 196

8

Beta strand

203 – 211

9

Beta strand

217 – 228

12

Beta strand

231 – 241

11

Beta strand

243 – 250

8

Beta strand

252 – 254

3

Beta strand

256 – 264

9

Helix

268 – 270

3

Beta strand

274 – 282

9

Sequences

	Sequence		Length	Mass (Da)
	P21796 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOPTOSIS.
[19]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INFLUENZA A VIRUS PB1-F2.
[20]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[21]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[22]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[23]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-28; LYS-61; LYS-224 AND LYS-266, MASS SPECTROMETRY.
[25]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, MASS SPECTROMETRY.
[28]	"Human Bop is a novel BH3-only member of the Bcl-2 protein family." Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q., Pan L., Tang H. Protein Cell 3:790-801(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BOP/C22ORF29.
[29]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF 2-283, STRUCTURE BY NMR.
[30]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR, FUNCTION, INTERACTION WITH BCL2L1, NADH-BINDING.
+	Additional computationally mapped references.

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.
CH471062 Genomic DNA. Translation: EAW62282.1.
CH471062 Genomic DNA. Translation: EAW62283.1.
CH471062 Genomic DNA. Translation: EAW62285.1.
CH471062 Genomic DNA. Translation: EAW62286.1.
BC008482 mRNA. Translation: AAH08482.1.
BC071168 mRNA. Translation: AAH71168.1.
BC090042 mRNA. Translation: AAH90042.1.

IPI

IPI00216308.

PIR

MMHUP3. A44422.

RefSeq

NP_003365.1. NM_003374.2.

UniGene

Hs.519320.

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	[»]

ProteinModelPortal

P21796.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32862N.

IntAct

P21796. 10 interactions.

MINT

MINT-5002499.

STRING

9606.ENSP00000265333.

PTM databases

PhosphoSite

P21796.

Polymorphism databases

DMDM

130683.

2D gel databases

DOSAC-COBS-2DPAGE

P21796.

OGP

P21796.

REPRODUCTION-2DPAGE

IPI00216308.
P21796.

UCD-2DPAGE

P21796.

Proteomic databases

PaxDb

P21796.

PeptideAtlas

P21796.

PRIDE

P21796.

Protocols and materials databases

DNASU

7416.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265333; ENSP00000265333; ENSG00000213585.
ENST00000395044; ENSP00000378484; ENSG00000213585.
ENST00000395047; ENSP00000378487; ENSG00000213585.

GeneID

7416.

KEGG

hsa:7416.

UCSC

uc003kyp.2. human.

Organism-specific databases

CTD

7416.

GeneCards

GC05M133307.

H-InvDB

HIX0056260.

HGNC

HGNC:12669. VDAC1.

HPA

CAB005885.

MIM

604492. gene+phenotype.

neXtProt

NX_P21796.

PharmGKB

PA37292.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG243169.

HOGENOM

HOG000188277.

HOVERGEN

HBG054036.

InParanoid

P21796.

KO

K05862.

OMA

QKMAVPP.

OrthoDB

EOG4T4CVZ.

PhylomeDB

P21796.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpress

P21796.

Bgee

P21796.

CleanEx

HS_VDAC1.

Genevestigator

P21796.

GermOnline

ENSG00000073905. Homo sapiens.

Family and domain databases

Gene3D

2.40.160.10. 1 hit.

InterPro

IPR023614. Porin_dom.
IPR001925. Porin_Euk.
IPR027246. Porin_Euk/Tom40.
[Graphical view]

Pfam

PF01459. Porin_3. 1 hit.
[Graphical view]

PRINTS

PR00185. EUKARYTPORIN.

PROSITE

PS00558. EUKARYOTIC_PORIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01375. Dihydroxyaluminium.

EvolutionaryTrace

P21796.

GenomeRNAi

7416.

NextBio

29038.

SOURCE

Search...

Entry information

Entry name

VDAC1_HUMAN

Accession

Primary (citable) accession number: P21796
Secondary accession number(s): B3KVK4 , D3DQ93, Q5FVE7, Q9UIQ5, Q9UPL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 151 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.