Full text data of BNIP1
BNIP1
(NIP1, SEC20L)
[Confidence: high (present in two of the MS resources)]
Vesicle transport protein SEC20 (BCL2/adenovirus E1B 19 kDa protein-interacting protein 1; Transformation-related gene 8 protein; TRG-8)
Vesicle transport protein SEC20 (BCL2/adenovirus E1B 19 kDa protein-interacting protein 1; Transformation-related gene 8 protein; TRG-8)
Comments
Isoform Q12981-1 was detected.
Isoform Q12981-1 was detected.
UniProt
Q12981
ID SEC20_HUMAN Reviewed; 228 AA.
AC Q12981; D3DQM3; D3DQM4; D3DQM5; D3DQM6; O75622; O75623; O75624;
read moreAC Q6K044; Q96FG4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Vesicle transport protein SEC20;
DE AltName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 1;
DE AltName: Full=Transformation-related gene 8 protein;
DE Short=TRG-8;
GN Name=BNIP1; Synonyms=NIP1, SEC20L; ORFNames=TRG8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7954800; DOI=10.1016/0092-8674(94)90202-X;
RA Boyd J.M., Malstrom S., Subramanian T., Venkatesh L.K., Schaeper U.,
RA Elangovan B., D'Sa-Eipper C., Chinnadurai G.;
RT "Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set
RT of cellular proteins.";
RL Cell 79:341-351(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
RX PubMed=10217402; DOI=10.1016/S0014-5793(99)00335-X;
RA Zhang H., Heim J., Meyhack B.;
RT "Novel BNIP1 variants and their interaction with BCL2 family
RT members.";
RL FEBS Lett. 448:23-27(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of human transformation-related gene.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-14.
RG NIEHS SNPs program;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STX18 AND RINT1, AND
RP MUTAGENESIS OF LEU-114.
RX PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT fusion.";
RL EMBO J. 23:3216-3226(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION IN AUTOPHAGY, SUBCELLULAR LOCATION, AND UBIQUITINATION BY
RP RNF185.
RX PubMed=21931693; DOI=10.1371/journal.pone.0024367;
RA Tang F., Wang B., Li N., Wu Y., Jia J., Suo T., Chen Q., Liu Y.J.,
RA Tang J.;
RT "RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates
RT autophagy through interaction with BNIP1.";
RL PLoS ONE 6:E24367-E24367(2011).
CC -!- FUNCTION: SNARE that may be involved in targeting and fusion of
CC Golgi-derived retrograde transport vesicles with the ER. Required
CC for maintenance of ER network. Implicated in the suppression of
CC cell death. May be involved in mitochondrial autophagy.
CC -!- SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L,
CC BNIP1/SEC20L and SEC22B. Interacts directly with STX18,
CC RINT1/TIP20L and NAPA. Interacts with ZW10 through RINT1.
CC Interacts with BCL2 and adenovirus E1B 19 kDa protein.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Endoplasmic reticulum
CC membrane; Single-pass type IV membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist;
CC Name=1; Synonyms=BNIP1, S4;
CC IsoId=Q12981-4; Sequence=Displayed;
CC Name=2; Synonyms=BNIP1-a, S1;
CC IsoId=Q12981-2; Sequence=VSP_004330;
CC Name=3; Synonyms=BNIP1-b, S2;
CC IsoId=Q12981-1; Sequence=VSP_017901;
CC Name=4; Synonyms=BNIP1-c, S3;
CC IsoId=Q12981-3; Sequence=VSP_017901, VSP_004330;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in heart, brain,
CC liver skeletal muscle and pancreas. Isoform 3 is moderately
CC expressed in placenta, lung and kidney. Isoform 4 is highly
CC expressed in testis and small intestine.
CC -!- PTM: 'Lys-63'-linked polyubiquitination by RNF185 allows
CC recruiting of autophagy receptor SQSTM1, which simultaneously
CC binds both ubiquitin and LC3 to link ubiquitination and autophagy.
CC -!- MISCELLANEOUS: Silencing of BNIP1 disrupts ER morphology.
CC -!- SIMILARITY: Belongs to the SEC20 family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/bnip1/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U15172; AAC00020.1; -; mRNA.
DR EMBL; AF083956; AAC33124.1; -; mRNA.
DR EMBL; AF083957; AAC33125.1; -; mRNA.
DR EMBL; AF083958; AAC33126.1; -; mRNA.
DR EMBL; AY216799; AAO91805.1; -; mRNA.
DR EMBL; AY246554; AAO61090.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61405.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61406.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61408.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61409.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61410.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61411.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61412.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61413.1; -; Genomic_DNA.
DR EMBL; BC010959; AAH10959.1; -; mRNA.
DR PIR; I38863; I38863.
DR RefSeq; NP_001196.2; NM_001205.2.
DR RefSeq; NP_053581.2; NM_013978.2.
DR RefSeq; NP_053582.2; NM_013979.2.
DR RefSeq; NP_053583.2; NM_013980.2.
DR UniGene; Hs.145726; -.
DR ProteinModelPortal; Q12981; -.
DR MINT; MINT-1957109; -.
DR STRING; 9606.ENSP00000231668; -.
DR PhosphoSite; Q12981; -.
DR PaxDb; Q12981; -.
DR PRIDE; Q12981; -.
DR DNASU; 662; -.
DR Ensembl; ENST00000231668; ENSP00000231668; ENSG00000113734.
DR Ensembl; ENST00000351486; ENSP00000239215; ENSG00000113734.
DR Ensembl; ENST00000352523; ENSP00000239214; ENSG00000113734.
DR Ensembl; ENST00000393770; ENSP00000377365; ENSG00000113734.
DR GeneID; 662; -.
DR KEGG; hsa:662; -.
DR UCSC; uc003mcj.4; human.
DR CTD; 662; -.
DR GeneCards; GC05P172504; -.
DR HGNC; HGNC:1082; BNIP1.
DR HPA; HPA008009; -.
DR MIM; 603291; gene.
DR neXtProt; NX_Q12981; -.
DR PharmGKB; PA25392; -.
DR eggNOG; NOG73997; -.
DR HOVERGEN; HBG050708; -.
DR KO; K08497; -.
DR OMA; AMTGTIQ; -.
DR OrthoDB; EOG7D2FG0; -.
DR ChiTaRS; BNIP1; human.
DR GenomeRNAi; 662; -.
DR NextBio; 2694; -.
DR PRO; PR:Q12981; -.
DR ArrayExpress; Q12981; -.
DR Bgee; Q12981; -.
DR CleanEx; HS_BNIP1; -.
DR Genevestigator; Q12981; -.
DR GO; GO:0030176; C:integral to endoplasmic reticulum membrane; TAS:HGNC.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:HGNC.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IMP:HGNC.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:HGNC.
DR GO; GO:0097194; P:execution phase of apoptosis; IC:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR005606; Sec20.
DR Pfam; PF03908; Sec20; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Autophagy; Coiled coil;
KW Complete proteome; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Mitochondrion; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1 228 Vesicle transport protein SEC20.
FT /FTId=PRO_0000064960.
FT TOPO_DOM 1 199 Cytoplasmic (Potential).
FT TRANSMEM 200 220 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 221 228 Lumenal (Potential).
FT COILED 37 90 Potential.
FT VAR_SEQ 59 59 Q -> QPVLYQRAFIWTASTFFFKLTYSLTDFSSTQHDFNS
FT PTTPVTFS (in isoform 3 and isoform 4).
FT /FTId=VSP_017901.
FT VAR_SEQ 90 123 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_004330.
FT VARIANT 14 14 Q -> H (in dbSNP:rs5745100).
FT /FTId=VAR_019169.
FT MUTAGEN 114 114 L->A: Loss of proapoptotic effect. No
FT effect on interaction with RINT1.
FT CONFLICT 14 14 Q -> R (in Ref. 3; AAO91805).
FT CONFLICT 66 66 K -> E (in Ref. 3; AAO91805).
FT CONFLICT 210 210 A -> R (in Ref. 1 and 2).
SQ SEQUENCE 228 AA; 26132 MW; 23F4C21E7327DE3D CRC64;
MAAPQDVHVR ICNQEIVKFD LEVKALIQDI RDCSGPLSAL TELNTKVKEK FQQLRHRIQD
LEQLAKEQDK ESEKQLLLQE VENHKKQMLS NQASWRKANL TCKIAIDNLE KAELLQGGDL
LRQRKTTKES LAQTSSTITE SLMGISRMMA QQVQQSEEAM QSLVTSSRTI LDANEEFKSM
SGTIQLGRKL ITKYNRRELT DKLLIFLALA LFLATVLYIV KKRLFPFL
//
ID SEC20_HUMAN Reviewed; 228 AA.
AC Q12981; D3DQM3; D3DQM4; D3DQM5; D3DQM6; O75622; O75623; O75624;
read moreAC Q6K044; Q96FG4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Vesicle transport protein SEC20;
DE AltName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 1;
DE AltName: Full=Transformation-related gene 8 protein;
DE Short=TRG-8;
GN Name=BNIP1; Synonyms=NIP1, SEC20L; ORFNames=TRG8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7954800; DOI=10.1016/0092-8674(94)90202-X;
RA Boyd J.M., Malstrom S., Subramanian T., Venkatesh L.K., Schaeper U.,
RA Elangovan B., D'Sa-Eipper C., Chinnadurai G.;
RT "Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set
RT of cellular proteins.";
RL Cell 79:341-351(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
RX PubMed=10217402; DOI=10.1016/S0014-5793(99)00335-X;
RA Zhang H., Heim J., Meyhack B.;
RT "Novel BNIP1 variants and their interaction with BCL2 family
RT members.";
RL FEBS Lett. 448:23-27(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of human transformation-related gene.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-14.
RG NIEHS SNPs program;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STX18 AND RINT1, AND
RP MUTAGENESIS OF LEU-114.
RX PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT fusion.";
RL EMBO J. 23:3216-3226(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION IN AUTOPHAGY, SUBCELLULAR LOCATION, AND UBIQUITINATION BY
RP RNF185.
RX PubMed=21931693; DOI=10.1371/journal.pone.0024367;
RA Tang F., Wang B., Li N., Wu Y., Jia J., Suo T., Chen Q., Liu Y.J.,
RA Tang J.;
RT "RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates
RT autophagy through interaction with BNIP1.";
RL PLoS ONE 6:E24367-E24367(2011).
CC -!- FUNCTION: SNARE that may be involved in targeting and fusion of
CC Golgi-derived retrograde transport vesicles with the ER. Required
CC for maintenance of ER network. Implicated in the suppression of
CC cell death. May be involved in mitochondrial autophagy.
CC -!- SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L,
CC BNIP1/SEC20L and SEC22B. Interacts directly with STX18,
CC RINT1/TIP20L and NAPA. Interacts with ZW10 through RINT1.
CC Interacts with BCL2 and adenovirus E1B 19 kDa protein.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Endoplasmic reticulum
CC membrane; Single-pass type IV membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist;
CC Name=1; Synonyms=BNIP1, S4;
CC IsoId=Q12981-4; Sequence=Displayed;
CC Name=2; Synonyms=BNIP1-a, S1;
CC IsoId=Q12981-2; Sequence=VSP_004330;
CC Name=3; Synonyms=BNIP1-b, S2;
CC IsoId=Q12981-1; Sequence=VSP_017901;
CC Name=4; Synonyms=BNIP1-c, S3;
CC IsoId=Q12981-3; Sequence=VSP_017901, VSP_004330;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in heart, brain,
CC liver skeletal muscle and pancreas. Isoform 3 is moderately
CC expressed in placenta, lung and kidney. Isoform 4 is highly
CC expressed in testis and small intestine.
CC -!- PTM: 'Lys-63'-linked polyubiquitination by RNF185 allows
CC recruiting of autophagy receptor SQSTM1, which simultaneously
CC binds both ubiquitin and LC3 to link ubiquitination and autophagy.
CC -!- MISCELLANEOUS: Silencing of BNIP1 disrupts ER morphology.
CC -!- SIMILARITY: Belongs to the SEC20 family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/bnip1/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U15172; AAC00020.1; -; mRNA.
DR EMBL; AF083956; AAC33124.1; -; mRNA.
DR EMBL; AF083957; AAC33125.1; -; mRNA.
DR EMBL; AF083958; AAC33126.1; -; mRNA.
DR EMBL; AY216799; AAO91805.1; -; mRNA.
DR EMBL; AY246554; AAO61090.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61405.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61406.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61408.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61409.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61410.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61411.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61412.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61413.1; -; Genomic_DNA.
DR EMBL; BC010959; AAH10959.1; -; mRNA.
DR PIR; I38863; I38863.
DR RefSeq; NP_001196.2; NM_001205.2.
DR RefSeq; NP_053581.2; NM_013978.2.
DR RefSeq; NP_053582.2; NM_013979.2.
DR RefSeq; NP_053583.2; NM_013980.2.
DR UniGene; Hs.145726; -.
DR ProteinModelPortal; Q12981; -.
DR MINT; MINT-1957109; -.
DR STRING; 9606.ENSP00000231668; -.
DR PhosphoSite; Q12981; -.
DR PaxDb; Q12981; -.
DR PRIDE; Q12981; -.
DR DNASU; 662; -.
DR Ensembl; ENST00000231668; ENSP00000231668; ENSG00000113734.
DR Ensembl; ENST00000351486; ENSP00000239215; ENSG00000113734.
DR Ensembl; ENST00000352523; ENSP00000239214; ENSG00000113734.
DR Ensembl; ENST00000393770; ENSP00000377365; ENSG00000113734.
DR GeneID; 662; -.
DR KEGG; hsa:662; -.
DR UCSC; uc003mcj.4; human.
DR CTD; 662; -.
DR GeneCards; GC05P172504; -.
DR HGNC; HGNC:1082; BNIP1.
DR HPA; HPA008009; -.
DR MIM; 603291; gene.
DR neXtProt; NX_Q12981; -.
DR PharmGKB; PA25392; -.
DR eggNOG; NOG73997; -.
DR HOVERGEN; HBG050708; -.
DR KO; K08497; -.
DR OMA; AMTGTIQ; -.
DR OrthoDB; EOG7D2FG0; -.
DR ChiTaRS; BNIP1; human.
DR GenomeRNAi; 662; -.
DR NextBio; 2694; -.
DR PRO; PR:Q12981; -.
DR ArrayExpress; Q12981; -.
DR Bgee; Q12981; -.
DR CleanEx; HS_BNIP1; -.
DR Genevestigator; Q12981; -.
DR GO; GO:0030176; C:integral to endoplasmic reticulum membrane; TAS:HGNC.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:HGNC.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IMP:HGNC.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:HGNC.
DR GO; GO:0097194; P:execution phase of apoptosis; IC:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR005606; Sec20.
DR Pfam; PF03908; Sec20; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Autophagy; Coiled coil;
KW Complete proteome; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Mitochondrion; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1 228 Vesicle transport protein SEC20.
FT /FTId=PRO_0000064960.
FT TOPO_DOM 1 199 Cytoplasmic (Potential).
FT TRANSMEM 200 220 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 221 228 Lumenal (Potential).
FT COILED 37 90 Potential.
FT VAR_SEQ 59 59 Q -> QPVLYQRAFIWTASTFFFKLTYSLTDFSSTQHDFNS
FT PTTPVTFS (in isoform 3 and isoform 4).
FT /FTId=VSP_017901.
FT VAR_SEQ 90 123 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_004330.
FT VARIANT 14 14 Q -> H (in dbSNP:rs5745100).
FT /FTId=VAR_019169.
FT MUTAGEN 114 114 L->A: Loss of proapoptotic effect. No
FT effect on interaction with RINT1.
FT CONFLICT 14 14 Q -> R (in Ref. 3; AAO91805).
FT CONFLICT 66 66 K -> E (in Ref. 3; AAO91805).
FT CONFLICT 210 210 A -> R (in Ref. 1 and 2).
SQ SEQUENCE 228 AA; 26132 MW; 23F4C21E7327DE3D CRC64;
MAAPQDVHVR ICNQEIVKFD LEVKALIQDI RDCSGPLSAL TELNTKVKEK FQQLRHRIQD
LEQLAKEQDK ESEKQLLLQE VENHKKQMLS NQASWRKANL TCKIAIDNLE KAELLQGGDL
LRQRKTTKES LAQTSSTITE SLMGISRMMA QQVQQSEEAM QSLVTSSRTI LDANEEFKSM
SGTIQLGRKL ITKYNRRELT DKLLIFLALA LFLATVLYIV KKRLFPFL
//
MIM
603291
*RECORD*
*FIELD* NO
603291
*FIELD* TI
*603291 BCL2/ADENOVIRUS E1B 19-KD PROTEIN-INTERACTING PROTEIN 1; BNIP1
;;NIP1
*FIELD* TX
read more
CLONING
Using a yeast 2-hybrid system to identify proteins that interact with
discrete domains of the E1B 19-kD protein, which is involved in
suppression of cell death, Boyd et al. (1994) cloned human B-cell cDNAs
encoding NIP1, NIP2 (603292), and NIP3 (603293). The deduced NIP1
protein has 228 amino acids and contains a putative membrane-spanning
hydrophobic domain. Although the authors found no significant sequence
homology between NIP1 and other proteins, they identified a 59- to
83-amino acid region of NIP1 that shows 29% to 36% identity to a
conserved region within the catalytic domain of 3 mammalian
3-prime-5-prime-cyclic nucleotide phosphodiesterases. Boyd et al. (1994)
localized NIP1 to the nuclear envelope region and to other cytoplasmic
structures.
GENE FUNCTION
Adenovirus E1B 19-kD protein protects against cell death induced by
viral infection and certain external stimuli. Using yeast 2-hybrid
analysis, Boyd et al. (1994) showed that NIP1, NIP2, and NIP3 interacted
with the adenovirus E1B 19-kD protein and with human BCL2 (151430),
which can functionally substitute for the 19-kD protein during
adenovirus infection. The interactions occurred at bipartite sequence
motifs common to both the E1B 19-kD and BCL2 proteins.
MAPPING
Gross (2012) mapped the BNIP1 gene to chromosome 5q35.1 based on an
alignment of the BNIP1 sequence (GenBank GENBANK AF083956) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Boyd, J. M.; Malstrom, S.; Subramanian, T.; Venkatesh, L. K.; Schaeper,
U.; Elangovan, B.; D'Sa-Eipper, C.; Chinnadurai, G.: Adenovirus E1B
19 kDa and Bcl-2 proteins interact with a common set of cellular proteins. Cell 79:
341-351, 1994. Note: Erratum: Cell 79: 1121 only, 1994.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 6/29/2012.
*FIELD* CN
Matthew B. Gross - updated: 6/29/2012
*FIELD* CD
Sheryl A. Jankowski: 11/17/1998
*FIELD* ED
terry: 03/15/2013
mgross: 6/29/2012
carol: 6/21/2012
psherman: 11/17/1998
*RECORD*
*FIELD* NO
603291
*FIELD* TI
*603291 BCL2/ADENOVIRUS E1B 19-KD PROTEIN-INTERACTING PROTEIN 1; BNIP1
;;NIP1
*FIELD* TX
read more
CLONING
Using a yeast 2-hybrid system to identify proteins that interact with
discrete domains of the E1B 19-kD protein, which is involved in
suppression of cell death, Boyd et al. (1994) cloned human B-cell cDNAs
encoding NIP1, NIP2 (603292), and NIP3 (603293). The deduced NIP1
protein has 228 amino acids and contains a putative membrane-spanning
hydrophobic domain. Although the authors found no significant sequence
homology between NIP1 and other proteins, they identified a 59- to
83-amino acid region of NIP1 that shows 29% to 36% identity to a
conserved region within the catalytic domain of 3 mammalian
3-prime-5-prime-cyclic nucleotide phosphodiesterases. Boyd et al. (1994)
localized NIP1 to the nuclear envelope region and to other cytoplasmic
structures.
GENE FUNCTION
Adenovirus E1B 19-kD protein protects against cell death induced by
viral infection and certain external stimuli. Using yeast 2-hybrid
analysis, Boyd et al. (1994) showed that NIP1, NIP2, and NIP3 interacted
with the adenovirus E1B 19-kD protein and with human BCL2 (151430),
which can functionally substitute for the 19-kD protein during
adenovirus infection. The interactions occurred at bipartite sequence
motifs common to both the E1B 19-kD and BCL2 proteins.
MAPPING
Gross (2012) mapped the BNIP1 gene to chromosome 5q35.1 based on an
alignment of the BNIP1 sequence (GenBank GENBANK AF083956) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Boyd, J. M.; Malstrom, S.; Subramanian, T.; Venkatesh, L. K.; Schaeper,
U.; Elangovan, B.; D'Sa-Eipper, C.; Chinnadurai, G.: Adenovirus E1B
19 kDa and Bcl-2 proteins interact with a common set of cellular proteins. Cell 79:
341-351, 1994. Note: Erratum: Cell 79: 1121 only, 1994.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 6/29/2012.
*FIELD* CN
Matthew B. Gross - updated: 6/29/2012
*FIELD* CD
Sheryl A. Jankowski: 11/17/1998
*FIELD* ED
terry: 03/15/2013
mgross: 6/29/2012
carol: 6/21/2012
psherman: 11/17/1998