SEC20_HUMAN
ID SEC20_HUMAN Reviewed; 228 AA.
AC Q12981; D3DQM3; D3DQM4; D3DQM5; D3DQM6; O75622; O75623; O75624; Q6K044;
AC Q96FG4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 174.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH BCL2,
RP AND INTERACTION WITH ADENOVIRUS PROTEIN E1B 19K (MICROBIAL INFECTION).
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 of
RT cellular proteins.";
RL Cell 79:341-351(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND TISSUE 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 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, INTERACTION WITH NAPA; RINT1; STX18; USE1L AND ZW10, SUBCELLULAR
RP LOCATION, AND 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., Buerckstuemmer T.,
RA 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, INTERACTION WITH RNF185 AND SQSTM1, SUBCELLULAR
RP LOCATION, AND UBIQUITINATION BY 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., Tang J.;
RT "RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy
RT through interaction with BNIP1.";
RL PLoS ONE 6:E24367-E24367(2011).
RN [10]
RP FUNCTION, INTERACTION WITH RNF186, SUBCELLULAR LOCATION, AND UBIQUITINATION
RP BY RNF186.
RX PubMed=23896122; DOI=10.1016/j.cellsig.2013.07.016;
RA Wang P., Wu Y., Li Y., Zheng J., Tang J.;
RT "A novel RING finger E3 ligase RNF186 regulate ER stress-mediated apoptosis
RT through interaction with BNip1.";
RL Cell. Signal. 25:2320-2333(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: As part of a SNARE complex may be involved in endoplasmic
CC reticulum membranes fusion and be required for the maintenance of
CC endoplasmic reticulum organization (PubMed:15272311). Also plays a role
CC in apoptosis (PubMed:7954800, PubMed:15272311, PubMed:23896122). It is
CC for instance required for endoplasmic reticulum stress-induced
CC apoptosis (PubMed:23896122). As a substrate of RNF185 interacting with
CC SQSTM1, might also be involved in mitochondrial autophagy (Probable).
CC {ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:23896122,
CC ECO:0000269|PubMed:7954800, ECO:0000305|PubMed:21931693}.
CC -!- SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L,
CC BNIP1/SEC20L and SEC22B (PubMed:15272311). Interacts directly with
CC STX18, RINT1/TIP20L and NAPA (PubMed:15272311). Interacts with ZW10
CC through RINT1 (PubMed:15272311). Interacts with BCL2 (PubMed:7954800).
CC Interacts with RNF186 (PubMed:23896122). Interacts with RNF185
CC (PubMed:21931693). Interacts with SQSTM1; increased by 'Lys-63'-linked
CC polyubiquitination of BNIP1 (PubMed:21931693).
CC {ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:21931693,
CC ECO:0000269|PubMed:23896122, ECO:0000269|PubMed:7954800}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus E1B 19K
CC protein; plays a role in the suppression of cell apoptosis by the viral
CC protein. {ECO:0000269|PubMed:7954800}.
CC -!- INTERACTION:
CC Q12981; P49447: CYB561; NbExp=3; IntAct=EBI-4402847, EBI-8646596;
CC Q12981; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-4402847, EBI-18535450;
CC Q12981; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-4402847, EBI-18636064;
CC Q12981; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-4402847, EBI-1052304;
CC Q12981; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-4402847, EBI-10266796;
CC Q12981; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-4402847, EBI-2341610;
CC Q12981; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-4402847, EBI-10192441;
CC Q12981; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-4402847, EBI-17247926;
CC Q12981; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-4402847, EBI-5235586;
CC Q12981; P27105: STOM; NbExp=3; IntAct=EBI-4402847, EBI-1211440;
CC Q12981; Q16623: STX1A; NbExp=3; IntAct=EBI-4402847, EBI-712466;
CC Q12981; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-4402847, EBI-6448756;
CC Q12981; Q9Y320: TMX2; NbExp=3; IntAct=EBI-4402847, EBI-6447886;
CC Q12981; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-4402847, EBI-1055364;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:23896122}; Single-pass
CC type IV membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:23896122}; Single-pass
CC type IV membrane protein {ECO:0000255}. Note=Localization to the
CC mitochondrion is regulated by RNF186. {ECO:0000269|PubMed:23896122}.
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 expressed
CC in placenta, lung and kidney. Isoform 4 is highly expressed in testis
CC and small intestine. {ECO:0000269|PubMed:10217402}.
CC -!- PTM: Polyubiquitinated (PubMed:21931693, PubMed:23896122). 'Lys-63'-
CC linked polyubiquitination by RNF185 increases the interaction with the
CC autophagy receptor SQSTM1 (PubMed:21931693). Undergoes 'Lys-29'- and
CC 'Lys-63'-linked polyubiquitination by RNF186 that may regulate BNIP1
CC localization to the mitochondrion (PubMed:23896122).
CC {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:23896122}.
CC -!- SIMILARITY: Belongs to the SEC20 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/bnip1/";
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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 CCDS; CCDS43400.1; -. [Q12981-2]
DR CCDS; CCDS4384.1; -. [Q12981-4]
DR CCDS; CCDS4385.1; -. [Q12981-1]
DR CCDS; CCDS4386.1; -. [Q12981-3]
DR PIR; I38863; I38863.
DR RefSeq; NP_001196.2; NM_001205.2. [Q12981-4]
DR RefSeq; NP_053581.2; NM_013978.2. [Q12981-2]
DR RefSeq; NP_053582.2; NM_013979.2. [Q12981-1]
DR RefSeq; NP_053583.2; NM_013980.2. [Q12981-3]
DR AlphaFoldDB; Q12981; -.
DR SMR; Q12981; -.
DR BioGRID; 107130; 127.
DR IntAct; Q12981; 41.
DR MINT; Q12981; -.
DR iPTMnet; Q12981; -.
DR MetOSite; Q12981; -.
DR PhosphoSitePlus; Q12981; -.
DR BioMuta; BNIP1; -.
DR DMDM; 93141310; -.
DR EPD; Q12981; -.
DR jPOST; Q12981; -.
DR MassIVE; Q12981; -.
DR MaxQB; Q12981; -.
DR PeptideAtlas; Q12981; -.
DR PRIDE; Q12981; -.
DR ProteomicsDB; 59075; -. [Q12981-4]
DR ProteomicsDB; 59076; -. [Q12981-1]
DR ProteomicsDB; 59077; -. [Q12981-2]
DR ProteomicsDB; 59078; -. [Q12981-3]
DR Antibodypedia; 2356; 546 antibodies from 35 providers.
DR DNASU; 662; -.
DR Ensembl; ENST00000231668.13; ENSP00000231668.9; ENSG00000113734.18. [Q12981-1]
DR Ensembl; ENST00000351486.10; ENSP00000239215.7; ENSG00000113734.18. [Q12981-4]
DR Ensembl; ENST00000352523.10; ENSP00000239214.8; ENSG00000113734.18. [Q12981-3]
DR Ensembl; ENST00000393770.4; ENSP00000377365.4; ENSG00000113734.18. [Q12981-2]
DR GeneID; 662; -.
DR KEGG; hsa:662; -.
DR MANE-Select; ENST00000351486.10; ENSP00000239215.7; NM_001205.3; NP_001196.2.
DR UCSC; uc003mci.5; human. [Q12981-4]
DR CTD; 662; -.
DR DisGeNET; 662; -.
DR GeneCards; BNIP1; -.
DR HGNC; HGNC:1082; BNIP1.
DR HPA; ENSG00000113734; Low tissue specificity.
DR MIM; 603291; gene.
DR neXtProt; NX_Q12981; -.
DR OpenTargets; ENSG00000113734; -.
DR PharmGKB; PA25392; -.
DR VEuPathDB; HostDB:ENSG00000113734; -.
DR GeneTree; ENSGT00390000014412; -.
DR HOGENOM; CLU_105902_0_0_1; -.
DR InParanoid; Q12981; -.
DR OMA; DDWARDT; -.
DR OrthoDB; 1328108at2759; -.
DR PhylomeDB; Q12981; -.
DR TreeFam; TF324339; -.
DR PathwayCommons; Q12981; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; Q12981; -.
DR BioGRID-ORCS; 662; 396 hits in 1082 CRISPR screens.
DR ChiTaRS; BNIP1; human.
DR GenomeRNAi; 662; -.
DR Pharos; Q12981; Tbio.
DR PRO; PR:Q12981; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q12981; protein.
DR Bgee; ENSG00000113734; Expressed in secondary oocyte and 153 other tissues.
DR ExpressionAtlas; Q12981; baseline and differential.
DR Genevisible; Q12981; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; TAS:HGNC-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:HGNC-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IPI:MGI.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IMP:HGNC-UCL.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:HGNC-UCL.
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:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR InterPro; IPR005606; Sec20.
DR PANTHER; PTHR12825; PTHR12825; 1.
DR Pfam; PF03908; Sec20; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Coiled coil; Endoplasmic reticulum;
KW ER-Golgi transport; Host-virus interaction; Membrane; Mitochondrion;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..228
FT /note="Vesicle transport protein SEC20"
FT /id="PRO_0000064960"
FT TOPO_DOM 1..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..228
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 37..90
FT /evidence="ECO:0000255"
FT VAR_SEQ 59
FT /note="Q -> QPVLYQRAFIWTASTFFFKLTYSLTDFSSTQHDFNSPTTPVTFS
FT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10217402"
FT /id="VSP_017901"
FT VAR_SEQ 90..123
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10217402"
FT /id="VSP_004330"
FT VARIANT 14
FT /note="Q -> H (in dbSNP:rs5745100)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019169"
FT MUTAGEN 114
FT /note="L->A: Loss of proapoptotic effect. No effect on
FT interaction with RINT1."
FT /evidence="ECO:0000269|PubMed:15272311"
FT CONFLICT 14
FT /note="Q -> R (in Ref. 3; AAO91805)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="K -> E (in Ref. 3; AAO91805)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
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
