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Q16611 (BAK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bcl-2 homologous antagonist/killer
Alternative name(s):
Apoptosis regulator BAK
Bcl-2-like protein 7
Short name=Bcl2-L-7
Gene names
Name:BAK1
Synonyms:BAK, BCL2L7, CDN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis. Ref.10 Ref.15

Subunit structure

Interacts with BCL2A1 By similarity. Homodimer. Formation of the homodimer is zinc-dependent. Forms heterodimers with BCL2, E1B 19k protein, and BCL2L1 isoform Bcl-X(L) Interacts with myxoma virus protein M11L. Interacts with BOP/C22orf29. Ref.13 Ref.15

Subcellular location

Mitochondrion membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in a wide variety of tissues, with highest levels in the heart and skeletal muscle.

Domain

Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.

Sequence similarities

Belongs to the Bcl-2 family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentMembrane
Mitochondrion
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

B cell homeostasis

Inferred from electronic annotation. Source: Ensembl

B cell negative selection

Inferred from electronic annotation. Source: Ensembl

activation of cysteine-type endopeptidase activity

Inferred from direct assay PubMed 18387192. Source: BHF-UCL

activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

apoptotic process involved in patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

apoptotic signaling pathway

Inferred from mutant phenotype PubMed 15901672. Source: UniProtKB

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to UV

Inferred from mutant phenotype PubMed 15901672. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

endocrine pancreas development

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum calcium ion homeostasis

Traceable author statement PubMed 18309324. Source: UniProtKB

establishment or maintenance of transmembrane electrochemical gradient

Inferred from direct assay PubMed 9843949. Source: HGNC

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from Biological aspect of Ancestor. Source: RefGenome

fibroblast apoptotic process

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from Biological aspect of Ancestor. Source: RefGenome

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from electronic annotation. Source: Ensembl

limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

mitochondrial fusion

Inferred from electronic annotation. Source: Ensembl

myeloid cell homeostasis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of endoplasmic reticulum calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 17289999. Source: UniProtKB

positive regulation of calcium ion transport into cytosol

Inferred from electronic annotation. Source: Ensembl

positive regulation of endoplasmic reticulum unfolded protein response

Inferred from mutant phenotype PubMed 16645094. Source: UniProtKB

positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of proteolysis

Inferred from direct assay PubMed 18387192. Source: BHF-UCL

positive regulation of release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

post-embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial membrane permeability

Inferred from direct assay PubMed 21041309. Source: BHF-UCL

regulation of mitochondrial membrane potential

Inferred from direct assay PubMed 9843949. Source: HGNC

regulation of protein heterodimerization activity

Inferred from direct assay PubMed 9111042. Source: HGNC

regulation of protein homodimerization activity

Inferred from direct assay PubMed 9111042. Source: HGNC

release of cytochrome c from mitochondria

Inferred from direct assay PubMed 16199525. Source: BHF-UCL

response to UV-C

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to fungus

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to mycotoxin

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

thymocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

vagina development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

integral component of mitochondrial outer membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

mitochondrial outer membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrion

Inferred from direct assay PubMed 9843949. Source: HGNC

pore complex

Inferred from direct assay PubMed 9843949. Source: HGNC

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 15901672PubMed 16439990PubMed 17446862PubMed 23782464. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10381623PubMed 15901672. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 10837489. Source: UniProtKB

protein homodimerization activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 211210Bcl-2 homologous antagonist/killer
PRO_0000143059

Regions

Transmembrane188 – 20518Helical; Potential
Motif74 – 8815BH3
Motif117 – 13620BH1
Motif169 – 18416BH2

Sites

Metal binding1601Zinc; shared with dimeric partner
Metal binding1641Zinc; shared with dimeric partner

Amino acid modifications

Modified residue21N-acetylalanine Ref.11

Natural variations

Natural variant281A → V. Ref.4
Corresponds to variant rs4987115 [ dbSNP | Ensembl ].
VAR_018829
Natural variant421R → H.
Corresponds to variant rs1051911 [ dbSNP | Ensembl ].
VAR_048417
Natural variant691S → R. Ref.4
Corresponds to variant rs5745592 [ dbSNP | Ensembl ].
VAR_018830

Experimental info

Mutagenesis1641H → A: Strongly reduced zinc binding and homodimerization. Ref.15

Secondary structure

...................... 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16611 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A2200FE72A46D04E

FASTA21123,409
        10         20         30         40         50         60 
MASGQGPGPP RQECGEPALP SASEEQVAQD TEEVFRSYVF YRHQQEQEAE GVAAPADPEM 

        70         80         90        100        110        120 
VTLPLQPSST MGQVGRQLAI IGDDINRRYD SEFQTMLQHL QPTAENAYEY FTKIATSLFE 

       130        140        150        160        170        180 
SGINWGRVVA LLGFGYRLAL HVYQHGLTGF LGQVTRFVVD FMLHHCIARW IAQRGGWVAA 

       190        200        210 
LNLGNGPILN VLVVLGVVLL GQFVVRRFFK S 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K."
Farrow S.N., White J.H.M., Martinou I., Raven T., Pun K.-T., Grinham C.J., Martinou J.-C., Brown R.
Nature 374:731-733(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: B-cell.
[2]"Induction of apoptosis by the Bcl-2 homologue Bak."
Chittenden T., Harrington E.A., O'Connor R., Flemington C., Lutz R.J., Evan G.I., Guild B.C.
Nature 374:733-736(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak."
Kiefer M.C., Brauer M.J., Powers V.C., Wu J.J., Umansky S.R., Tomei L.D., Barr P.J.
Nature 374:736-739(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]NIEHS SNPs program
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-28 AND ARG-69.
[5]"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].
[6]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [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. expand/collapse author list , 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 (JUL-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.
[9]"Estrogen alters expression of apoptosis-regulators, Bcl-2, Bcl-xL and Bak, as well as susceptibility to therapeutic agents of human breast cancer cells."
Eguchi H., Hayashi S.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-206.
[10]"A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions."
Chittenden T., Flemington C., Houghton A.B., Ebb R.G., Gallo G.J., Elangovan B., Chinnadurai G., Lutz R.J.
EMBO J. 14:5589-5596(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, FUNCTION OF BH3 MOTIF.
[11]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"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].
[13]"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.
[14]"Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis."
Sattler M., Liang H., Nettesheim D., Meadows R.P., Harlan J.E., Eberstadt M., Yoon H.S., Shuker S.B., Chang B.S., Minn A.J., Thompson C.B., Fesik S.W.
Science 275:983-986(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 72-87 IN COMPLEX WITH BCL2L1 ISOFORM BCL-X(L).
[15]"The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site."
Moldoveanu T., Liu Q., Tocilj A., Watson M., Shore G., Gehring K.
Mol. Cell 24:677-688(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 16-186, FUNCTION, SUBUNIT, MUTAGENESIS OF HIS-164, ZINC-BINDING.
[16]"A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak."
Kvansakul M., van Delft M.F., Lee E.F., Gulbis J.M., Fairlie W.D., Huang D.C.S., Colman P.M.
Mol. Cell 25:933-942(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 67-92 IN COMPLEX WITH MYXOMA VIRUS PROTEIN M11L.
[17]"Crystal structure of MS0836."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84213 mRNA. Translation: CAA58997.1.
U23765 mRNA. Translation: AAA93066.1.
U16811 mRNA. Translation: AAA74466.1.
AY260471 Genomic DNA. Translation: AAO74828.1.
CR457419 mRNA. Translation: CAG33700.1.
Z93017 Genomic DNA. Translation: CAB65626.1.
CH471081 Genomic DNA. Translation: EAX03742.1.
BC004431 mRNA. Translation: AAH04431.1.
D88397 Genomic DNA. Translation: BAA13606.1.
CCDSCCDS4781.1.
PIRS58873.
RefSeqNP_001179.1. NM_001188.3.
UniGeneHs.485139.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXLNMR-B72-87[»]
2IMSX-ray1.48A16-186[»]
2IMTX-ray1.49A16-186[»]
2JBYX-ray2.41B67-92[»]
2JCNX-ray1.80A21-190[»]
2M5BNMR-A18-186[»]
2XPXX-ray2.05B67-92[»]
2YV6X-ray2.50A23-185[»]
3I1HX-ray2.20B72-87[»]
3QBRX-ray2.60B/Y63-96[»]
ProteinModelPortalQ16611.
SMRQ16611. Positions 19-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107054. 26 interactions.
DIPDIP-935N.
IntActQ16611. 16 interactions.
MINTMINT-96576.
STRING9606.ENSP00000363591.

Chemistry

BindingDBQ16611.
ChEMBLCHEMBL5609.

Protein family/group databases

TCDB1.A.21.1.3. the bcl-2 (bcl-2) family.

PTM databases

PhosphoSiteQ16611.

Polymorphism databases

DMDM2493274.

Proteomic databases

MaxQBQ16611.
PaxDbQ16611.
PRIDEQ16611.

Protocols and materials databases

DNASU578.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360661; ENSP00000353878; ENSG00000030110.
ENST00000374467; ENSP00000363591; ENSG00000030110.
GeneID578.
KEGGhsa:578.
UCSCuc003oer.3. human.

Organism-specific databases

CTD578.
GeneCardsGC06M033541.
HGNCHGNC:949. BAK1.
HPACAB005029.
MIM600516. gene.
neXtProtNX_Q16611.
PharmGKBPA25253.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145601.
HOGENOMHOG000006521.
HOVERGENHBG002674.
InParanoidQ16611.
KOK14021.
OMAGDDINQR.
OrthoDBEOG70GMGD.
PhylomeDBQ16611.
TreeFamTF315834.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ16611.
BgeeQ16611.
CleanExHS_BAK1.
GenevestigatorQ16611.

Family and domain databases

InterProIPR026308. BAK.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF41. PTHR11256:SF41. 1 hit.
PfamPF00452. Bcl-2. 1 hit.
[Graphical view]
PRINTSPR01862. BCL2FAMILY.
PROSITEPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16611.
GeneWikiBcl-2_homologous_antagonist_killer.
GenomeRNAi578.
NextBio2359.
PROQ16611.
SOURCESearch...

Entry information

Entry nameBAK_HUMAN
AccessionPrimary (citable) accession number: Q16611
Secondary accession number(s): Q6I9T6, Q92533
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM