BL1S1_HUMAN
ID BL1S1_HUMAN Reviewed; 153 AA.
AC P78537; A1L4Q9; Q6NZ45;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 1;
DE Short=BLOC-1 subunit 1;
DE AltName: Full=GCN5-like protein 1;
DE AltName: Full=Protein RT14;
GN Name=BLOC1S1; Synonyms=BLOS1, GCN5L1, RT14;
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 2).
RC TISSUE=Fetal brain;
RX PubMed=8770567; DOI=10.1093/dnares/2.5.235;
RA Watanabe T.K., Fujiwara T., Shinomiya H., Kuga Y., Hishigaki H.,
RA Nakamura Y., Hirai Y.;
RT "Molecular cloning of a novel human cDNA, RT14, containing a putative ORF
RT highly conserved between human, fruit fly, and nematode.";
RL DNA Res. 2:235-237(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-153 (ISOFORM 1).
RX PubMed=8646881; DOI=10.1159/000134324;
RA Inoue M., Isomura M., Ikegawa S., Fujiwara T., Shin S., Moriya H.,
RA Nakamura Y.;
RT "Isolation and characterization of a human cDNA clone (GCN5L1) homologous
RT to GCN5, a yeast transcription activator.";
RL Cytogenet. Cell Genet. 73:134-136(1996).
RN [5]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX.
RX PubMed=15102850; DOI=10.1074/jbc.m402513200;
RA Starcevic M., Dell'Angelica E.C.;
RT "Identification of snapin and three novel proteins (BLOS1, BLOS2, and
RT BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related
RT organelles complex-1 (BLOC-1).";
RL J. Biol. Chem. 279:28393-28401(2004).
RN [6]
RP FUNCTION.
RX PubMed=17182842; DOI=10.1091/mbc.e06-12-1066;
RA Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C.,
RA Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C.,
RA Dell'Angelica E.C., Raposo G., Marks M.S.;
RT "BLOC-1 is required for cargo-specific sorting from vacuolar early
RT endosomes toward lysosome-related organelles.";
RL Mol. Biol. Cell 18:768-780(2007).
RN [7]
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 [8]
RP FUNCTION IN MITOCHONDRIAL PROTEIN ACETYLATION, FUNCTION IN AEROBIC
RP RESPIRATION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP5F1A AND NDUFA9.
RX PubMed=22309213; DOI=10.1042/bj20120118;
RA Scott I., Webster B.R., Li J.H., Sack M.N.;
RT "Identification of a molecular component of the mitochondrial acetyl
RT transferase program; a novel role for GCN5L1.";
RL Biochem. J. 443:655-661(2012).
RN [9]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND COMPOSITION OF THE BLOC-1
RP COMPLEX.
RX PubMed=22203680; DOI=10.1074/jbc.m111.325746;
RA Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R., Steven A.C.,
RA Bonifacino J.S., Hurley J.H.;
RT "Assembly and architecture of biogenesis of lysosome-related organelles
RT complex-1 (BLOC-1).";
RL J. Biol. Chem. 287:5882-5890(2012).
RN [10]
RP FUNCTION, IDENTIFICATION OF THE BORC COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=25898167; DOI=10.1016/j.devcel.2015.02.011;
RA Pu J., Schindler C., Jia R., Jarnik M., Backlund P., Bonifacino J.S.;
RT "BORC, a multisubunit complex that regulates lysosome positioning.";
RL Dev. Cell 33:176-188(2015).
CC -!- FUNCTION: Component of the BLOC-1 complex, a complex that is required
CC for normal biogenesis of lysosome-related organelles (LRO), such as
CC platelet dense granules and melanosomes. In concert with the AP-3
CC complex, the BLOC-1 complex is required to target membrane protein
CC cargos into vesicles assembled at cell bodies for delivery into
CC neurites and nerve terminals. The BLOC-1 complex, in association with
CC SNARE proteins, is also proposed to be involved in neurite extension
CC (PubMed:17182842). As part of the BORC complex may play a role in
CC lysosomes movement and localization at the cell periphery. Associated
CC with the cytosolic face of lysosomes, the BORC complex may recruit
CC ARL8B and couple lysosomes to microtubule plus-end-directed kinesin
CC motor (PubMed:25898167). {ECO:0000269|PubMed:17182842,
CC ECO:0000269|PubMed:25898167}.
CC -!- FUNCTION: May negatively regulate aerobic respiration through
CC mitochondrial protein lysine-acetylation. May counteract the action of
CC the deacetylase SIRT3 by acetylating and regulating proteins of the
CC mitochondrial respiratory chain including ATP5F1A and NDUFA9.
CC {ECO:0000269|PubMed:22309213}.
CC -!- SUBUNIT: Component of the biogenesis of lysosome-related organelles
CC complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4,
CC BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed
CC of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6,
CC DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8 (PubMed:15102850, PubMed:22203680).
CC The BLOC-1 complex associates with the AP-3 protein complex and
CC membrane protein cargos (By similarity). Component of the BLOC-one-
CC related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5,
CC BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN (PubMed:25898167). Interacts
CC with ATP5F1A and NDUFA9; involved in their acetylation on lysine
CC residues (PubMed:22309213). Interacts with KXD1 (By similarity).
CC {ECO:0000250|UniProtKB:O55102, ECO:0000269|PubMed:15102850,
CC ECO:0000269|PubMed:22203680, ECO:0000269|PubMed:22309213,
CC ECO:0000269|PubMed:25898167}.
CC -!- INTERACTION:
CC P78537; P25705: ATP5F1A; NbExp=2; IntAct=EBI-348630, EBI-351437;
CC P78537; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-348630, EBI-465872;
CC P78537; Q9UL45: BLOC1S6; NbExp=17; IntAct=EBI-348630, EBI-465781;
CC P78537; Q13561: DCTN2; NbExp=3; IntAct=EBI-348630, EBI-715074;
CC P78537; Q9H4M3-2: FBXO44; NbExp=3; IntAct=EBI-348630, EBI-12104696;
CC P78537; O14964: HGS; NbExp=3; IntAct=EBI-348630, EBI-740220;
CC P78537; O15481: MAGEB4; NbExp=3; IntAct=EBI-348630, EBI-751857;
CC P78537; Q16795: NDUFA9; NbExp=3; IntAct=EBI-348630, EBI-1045087;
CC P78537; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-348630, EBI-12004298;
CC P78537; O95295: SNAPIN; NbExp=6; IntAct=EBI-348630, EBI-296723;
CC P78537; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-348630, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22309213}. Mitochondrion matrix
CC {ECO:0000269|PubMed:22309213}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:22309213}. Lysosome membrane
CC {ECO:0000305|PubMed:25898167}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P78537-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78537-2; Sequence=VSP_040954;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced by alternative initiation
CC at Met-27 of isoform 1. A polymorphism at position 9 leads to the
CC creation of a stop codon. Isoform 2 is the only form that exists in
CC orthologs (except primates). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BLOC1S1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB37682.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D64007; BAA10887.1; -; mRNA.
DR EMBL; AC009779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130640; AAI30641.1; -; mRNA.
DR EMBL; BC132795; AAI32796.1; -; mRNA.
DR EMBL; S82447; AAB37682.1; ALT_INIT; mRNA.
DR CCDS; CCDS8889.2; -. [P78537-1]
DR PIR; JC4392; JC4392.
DR RefSeq; NP_001478.2; NM_001487.3. [P78537-1]
DR AlphaFoldDB; P78537; -.
DR SMR; P78537; -.
DR BioGRID; 108917; 45.
DR ComplexPortal; CPX-1910; BLOC-1 complex.
DR ComplexPortal; CPX-5029; BORC complex.
DR CORUM; P78537; -.
DR IntAct; P78537; 26.
DR MINT; P78537; -.
DR STRING; 9606.ENSP00000447537; -.
DR iPTMnet; P78537; -.
DR PhosphoSitePlus; P78537; -.
DR BioMuta; BLOC1S1; -.
DR DMDM; 332278161; -.
DR EPD; P78537; -.
DR jPOST; P78537; -.
DR MassIVE; P78537; -.
DR MaxQB; P78537; -.
DR PaxDb; P78537; -.
DR PeptideAtlas; P78537; -.
DR PRIDE; P78537; -.
DR ProteomicsDB; 57639; -. [P78537-1]
DR ProteomicsDB; 57640; -. [P78537-2]
DR Antibodypedia; 15519; 92 antibodies from 20 providers.
DR DNASU; 2647; -.
DR Ensembl; ENST00000548925.6; ENSP00000447537.1; ENSG00000135441.8. [P78537-1]
DR GeneID; 2647; -.
DR KEGG; hsa:2647; -.
DR MANE-Select; ENST00000548925.6; ENSP00000447537.1; NM_001487.4; NP_001478.2.
DR UCSC; uc001shi.5; human. [P78537-1]
DR CTD; 2647; -.
DR DisGeNET; 2647; -.
DR GeneCards; BLOC1S1; -.
DR HGNC; HGNC:4200; BLOC1S1.
DR HPA; ENSG00000135441; Low tissue specificity.
DR MIM; 601444; gene.
DR neXtProt; NX_P78537; -.
DR OpenTargets; ENSG00000135441; -.
DR PharmGKB; PA28617; -.
DR VEuPathDB; HostDB:ENSG00000135441; -.
DR eggNOG; KOG3390; Eukaryota.
DR GeneTree; ENSGT00390000002689; -.
DR HOGENOM; CLU_115602_3_0_1; -.
DR InParanoid; P78537; -.
DR OMA; HSATNFA; -.
DR OrthoDB; 1603359at2759; -.
DR PhylomeDB; P78537; -.
DR TreeFam; TF314443; -.
DR PathwayCommons; P78537; -.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; P78537; -.
DR SIGNOR; P78537; -.
DR BioGRID-ORCS; 2647; 17 hits in 1067 CRISPR screens.
DR GeneWiki; BLOC1S1; -.
DR GenomeRNAi; 2647; -.
DR Pharos; P78537; Tbio.
DR PRO; PR:P78537; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P78537; protein.
DR Bgee; ENSG00000135441; Expressed in mucosa of transverse colon and 98 other tissues.
DR ExpressionAtlas; P78537; baseline and differential.
DR Genevisible; P78537; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
DR GO; GO:0099078; C:BORC complex; IDA:UniProtKB.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IMP:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0072384; P:organelle transport along microtubule; IC:ComplexPortal.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; IMP:UniProtKB.
DR GO; GO:0060155; P:platelet dense granule organization; NAS:UniProtKB.
DR GO; GO:0051036; P:regulation of endosome size; IC:ComplexPortal.
DR GO; GO:0062196; P:regulation of lysosome size; IC:ComplexPortal.
DR InterPro; IPR009395; BLOC1S1.
DR PANTHER; PTHR13073; PTHR13073; 1.
DR Pfam; PF06320; GCN5L1; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Coiled coil; Cytoplasm; Lysosome; Membrane;
KW Mitochondrion; Reference proteome.
FT CHAIN 1..153
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 1"
FT /id="PRO_0000156331"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..59
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8770567"
FT /id="VSP_040954"
SQ SEQUENCE 153 AA; 17263 MW; B7D1FE64F242B25A CRC64;
MAPGSRGERS SFRSRRGPGV PSPQPDVTML SRLLKEHQAK QNERKELQEK RRREAITAAT
CLTEALVDHL NVGVAQAYMN QRKLDHEVKT LQVQAAQFAK QTGQWIGMVE NFNQALKEIG
DVENWARSIE LDMRTIATAL EYVYKGQLQS APS
