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Protein

Bcl-2-interacting killer

Gene

BIK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Accelerates programmed cell death. Association to the apoptosis repressors Bcl-X(L), BHRF1, Bcl-2 or its adenovirus homolog E1B 19k protein suppresses this death-promoting activity. Does not interact with BAX.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei153 – 1542Cleavage; by RHBDL4/RHBDD1Curated

GO - Biological processi

  1. apoptotic mitochondrial changes Source: Ensembl
  2. apoptotic process Source: UniProtKB
  3. male gonad development Source: GO_Central
  4. positive regulation of protein homooligomerization Source: BHF-UCL
  5. positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
  6. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Bcl-2-interacting killer
Alternative name(s):
Apoptosis inducer NBK
BIP1
BP4
Gene namesi
Name:BIK
Synonyms:NBK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:1051. BIK.

Subcellular locationi

Endomembrane system; Single-pass membrane protein. Mitochondrion membrane By similarity; Single-pass membrane protein By similarity
Note: Around the nuclear envelope, and in cytoplasmic membranes.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei136 – 15621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endomembrane system Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi153 – 1542GG → FF: Inhibits RHBDL4/RHBDD1-induced cleavage. 1 Publication

Organism-specific databases

PharmGKBiPA25354.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 160160Bcl-2-interacting killerPRO_0000143100Add
BLAST

Post-translational modificationi

Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage is a necessary step prior its degradation by the proteosome-dependent mechanism.1 Publication

Proteomic databases

PaxDbiQ13323.
PRIDEiQ13323.

PTM databases

PhosphoSiteiQ13323.

Expressioni

Gene expression databases

BgeeiQ13323.
CleanExiHS_BIK.
ExpressionAtlasiQ13323. baseline and differential.
GenevestigatoriQ13323.

Organism-specific databases

HPAiHPA051360.

Interactioni

Subunit structurei

Interacts with RHBDL4/RHBDD1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL2P104153EBI-700794,EBI-77694
BCL2L1Q078172EBI-700794,EBI-78035
BCL2L1Q07817-13EBI-700794,EBI-287195
BCL2L2Q928432EBI-700794,EBI-707714

Protein-protein interaction databases

BioGridi107107. 13 interactions.
DIPiDIP-928N.
IntActiQ13323. 11 interactions.
MINTiMINT-1457938.
STRINGi9606.ENSP00000216115.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IPEmodel-@1-160[»]
ProteinModelPortaliQ13323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni137 – 15822Leucine-zipperSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 7115BH3Add
BLAST

Domaini

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.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG39366.
GeneTreeiENSGT00530000064453.
HOGENOMiHOG000095229.
HOVERGENiHBG001515.
InParanoidiQ13323.
KOiK18452.
OMAiLECMEGS.
OrthoDBiEOG7NKKN5.
PhylomeDBiQ13323.
TreeFamiTF338339.

Family and domain databases

InterProiIPR024579. Bcl2-int_killer.
IPR020728. Bcl2_BH3_motif_CS.
[Graphical view]
PANTHERiPTHR15018. PTHR15018. 1 hit.
PfamiPF12201. bcl-2I13. 1 hit.
[Graphical view]
ProDomiPD032623. PD032623. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS01259. BH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEVRPLSRD ILMETLLYEQ LLEPPTMEVL GMTDSEEDLD PMEDFDSLEC
60 70 80 90 100
MEGSDALALR LACIGDEMDV SLRAPRLAQL SEVAMHSLGL AFIYDQTEDI
110 120 130 140 150
RDVLRSFMDG FTTLKENIMR FWRSPNPGSW VSCEQVLLAL LLLLALLLPL
160
LSGGLHLLLK
Length:160
Mass (Da):18,016
Last modified:November 1, 1997 - v2
Checksum:i89034F4443F5A136
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191E → K.1 Publication
Corresponds to variant rs4988415 [ dbSNP | Ensembl ].
VAR_029179
Natural varianti26 – 261T → I.
Corresponds to variant rs11090143 [ dbSNP | Ensembl ].
VAR_048420
Natural varianti148 – 1481L → P.
Corresponds to variant rs11574527 [ dbSNP | Ensembl ].
VAR_029180

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34584 mRNA. Translation: AAC50413.1.
U49730 mRNA. Translation: AAC79124.1.
X89986 mRNA. Translation: CAA62013.1.
AF174424
, AF174421, AF174422, AF174423 Genomic DNA. Translation: AAF01156.1.
CR456390 mRNA. Translation: CAG30276.1.
BT006728 mRNA. Translation: AAP35374.1.
AY245248 Genomic DNA. Translation: AAO61089.1.
CR541863 mRNA. Translation: CAG46661.1.
CR541883 mRNA. Translation: CAG46681.1.
AL022237 Genomic DNA. Translation: CAA18260.2.
CH471138 Genomic DNA. Translation: EAW73282.1.
BC001599 mRNA. Translation: AAH01599.1.
CCDSiCCDS14044.1.
PIRiS58214.
RefSeqiNP_001188.1. NM_001197.4.
UniGeneiHs.475055.

Genome annotation databases

EnsembliENST00000216115; ENSP00000216115; ENSG00000100290.
GeneIDi638.
KEGGihsa:638.
UCSCiuc003bdk.3. human.

Polymorphism databases

DMDMi2493284.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34584 mRNA. Translation: AAC50413.1.
U49730 mRNA. Translation: AAC79124.1.
X89986 mRNA. Translation: CAA62013.1.
AF174424
, AF174421, AF174422, AF174423 Genomic DNA. Translation: AAF01156.1.
CR456390 mRNA. Translation: CAG30276.1.
BT006728 mRNA. Translation: AAP35374.1.
AY245248 Genomic DNA. Translation: AAO61089.1.
CR541863 mRNA. Translation: CAG46661.1.
CR541883 mRNA. Translation: CAG46681.1.
AL022237 Genomic DNA. Translation: CAA18260.2.
CH471138 Genomic DNA. Translation: EAW73282.1.
BC001599 mRNA. Translation: AAH01599.1.
CCDSiCCDS14044.1.
PIRiS58214.
RefSeqiNP_001188.1. NM_001197.4.
UniGeneiHs.475055.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IPEmodel-@1-160[»]
ProteinModelPortaliQ13323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107107. 13 interactions.
DIPiDIP-928N.
IntActiQ13323. 11 interactions.
MINTiMINT-1457938.
STRINGi9606.ENSP00000216115.

PTM databases

PhosphoSiteiQ13323.

Polymorphism databases

DMDMi2493284.

Proteomic databases

PaxDbiQ13323.
PRIDEiQ13323.

Protocols and materials databases

DNASUi638.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216115; ENSP00000216115; ENSG00000100290.
GeneIDi638.
KEGGihsa:638.
UCSCiuc003bdk.3. human.

Organism-specific databases

CTDi638.
GeneCardsiGC22P043506.
HGNCiHGNC:1051. BIK.
HPAiHPA051360.
MIMi603392. gene.
neXtProtiNX_Q13323.
PharmGKBiPA25354.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39366.
GeneTreeiENSGT00530000064453.
HOGENOMiHOG000095229.
HOVERGENiHBG001515.
InParanoidiQ13323.
KOiK18452.
OMAiLECMEGS.
OrthoDBiEOG7NKKN5.
PhylomeDBiQ13323.
TreeFamiTF338339.

Miscellaneous databases

GeneWikiiBcl-2-interacting_killer.
GenomeRNAii638.
NextBioi2586.
PROiQ13323.
SOURCEiSearch...

Gene expression databases

BgeeiQ13323.
CleanExiHS_BIK.
ExpressionAtlasiQ13323. baseline and differential.
GenevestigatoriQ13323.

Family and domain databases

InterProiIPR024579. Bcl2-int_killer.
IPR020728. Bcl2_BH3_motif_CS.
[Graphical view]
PANTHERiPTHR15018. PTHR15018. 1 hit.
PfamiPF12201. bcl-2I13. 1 hit.
[Graphical view]
ProDomiPD032623. PD032623. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS01259. BH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins."
    Boyd J.M., Gallo G.J., Elangovan B., Houghton A.B., Malstrom S., Avery B.J., Ebb R.G., Subramanian T., Chittenden T., Lutz R.J., Chinnadurai G.
    Oncogene 11:1921-1928(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: B-cell.
  2. "Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K."
    Han J., Sabbatini P., White E.
    Mol. Cell. Biol. 16:5857-5864(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "E1B-19K interacts with a novel apoptotic inducer, NBK."
    Pun K.-T., Farrow S.N., Raven T., Wride C.J., White J.H.M., Brown R.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoid tissue.
  4. "Mapping of a target region of allelic loss to a 0.5-cM interval on chromosome 22q13 in human colorectal cancer."
    Castells A., Ino Y., Louis D.N., Ramesh V., Gusella J.F., Rustgi A.K.
    Gastroenterology 117:831-837(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. NIEHS SNPs program
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-19.
  8. "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].
  9. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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: Lymph.
  12. "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.
  13. "A novel member of the Rhomboid family, RHBDD1, regulates BIK-mediated apoptosis."
    Wang Y., Guan X., Fok K.L., Li S., Zhang X., Miao S., Zong S., Koide S.S., Chan H.C., Wang L.
    Cell. Mol. Life Sci. 65:3822-3829(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY RHBDD1, INTERACTION WITH RHBDD1, MUTAGENESIS OF 153-GLY-PHE-154.

Entry informationi

Entry nameiBIK_HUMAN
AccessioniPrimary (citable) accession number: Q13323
Secondary accession number(s): Q16582, Q6FH93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 4, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.