BL1S2_HUMAN
ID BL1S2_HUMAN Reviewed; 142 AA.
AC Q6QNY1; B4DQV2; Q5W040; Q8WUI8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 2;
DE Short=BLOC-1 subunit 2;
DE AltName: Full=Centrosome-associated protein;
GN Name=BLOC1S2; Synonyms=BLOS2, CEAP;
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), IDENTIFICATION IN THE BLOC-1
RP COMPLEX, FUNCTION, AND INTERACTION WITH BLOC1S1; BLOC1S3; BLOC1S4; BLOC1S5
RP AND SNAPIN.
RC TISSUE=Cervix carcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INTERACTION WITH GAMMA-TUBULIN, AND ALTERNATIVE
RP SPLICING (ISOFORM 1).
RC TISSUE=Fetal liver;
RX PubMed=15381421; DOI=10.1016/j.jmb.2004.08.034;
RA Wang Z., Wei H., Yu Y., Sun J., Yang Y., Xing G., Wu S., Zhou Y., Zhu Y.,
RA Zhang C., Zhou T., Zhao X., Sun Q., He F.;
RT "Characterization of Ceap-11 and Ceap-16, two novel splicing-variant-
RT proteins, associated with centrosome, microtubule aggregation and cell
RT proliferation.";
RL J. Mol. Biol. 343:71-82(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
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] OF 27-142 (ISOFORM 1).
RC TISSUE=Pancreas;
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.
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 [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 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: 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 (PubMed:15102850,
CC PubMed:17182842). In concert with the AP-3 complex, the BLOC-1 complex
CC is required to target membrane protein cargos into vesicles assembled
CC at cell bodies for delivery into neurites and nerve terminals. The
CC BLOC-1 complex, in association with SNARE proteins, is also proposed to
CC be involved in neurite extension (By similarity). As part of the BORC
CC complex may play a role in lysosomes movement and localization at the
CC cell periphery. Associated with the cytosolic face of lysosomes, the
CC BORC complex may recruit ARL8B and couple lysosomes to microtubule
CC plus-end-directed kinesin motor (PubMed:25898167). May play a role in
CC cell proliferation (PubMed:15381421). {ECO:0000250|UniProtKB:Q9CWG9,
CC ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:15381421,
CC ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:25898167}.
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. Interacts directly with BLOC1S1,
CC BLOC1S3, BLOC1S4, BLOC1S5 and SNAPIN (PubMed:15102850,
CC PubMed:22203680). The BLOC-1 complex associates with the AP-3 protein
CC complex and membrane protein cargos (By similarity). Component of the
CC BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2,
CC BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN (PubMed:25898167).
CC Interacts with gamma-tubulin (PubMed:15381421). Interacts with IFT57
CC (By similarity). {ECO:0000250|UniProtKB:Q9CWG9,
CC ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:15381421,
CC ECO:0000269|PubMed:22203680, ECO:0000269|PubMed:25898167}.
CC -!- INTERACTION:
CC Q6QNY1; P53365: ARFIP2; NbExp=3; IntAct=EBI-465872, EBI-638194;
CC Q6QNY1; Q13515: BFSP2; NbExp=3; IntAct=EBI-465872, EBI-10229433;
CC Q6QNY1; P78537: BLOC1S1; NbExp=3; IntAct=EBI-465872, EBI-348630;
CC Q6QNY1; Q6QNY0: BLOC1S3; NbExp=3; IntAct=EBI-465872, EBI-465930;
CC Q6QNY1; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-465872, EBI-10749669;
CC Q6QNY1; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-465872, EBI-10175300;
CC Q6QNY1; P24863: CCNC; NbExp=3; IntAct=EBI-465872, EBI-395261;
CC Q6QNY1; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-465872, EBI-11962928;
CC Q6QNY1; Q13561: DCTN2; NbExp=3; IntAct=EBI-465872, EBI-715074;
CC Q6QNY1; Q96DN0: ERP27; NbExp=3; IntAct=EBI-465872, EBI-953772;
CC Q6QNY1; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-465872, EBI-742102;
CC Q6QNY1; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-465872, EBI-7225287;
CC Q6QNY1; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-465872, EBI-10175124;
CC Q6QNY1; O95257: GADD45G; NbExp=3; IntAct=EBI-465872, EBI-448202;
CC Q6QNY1; P55040: GEM; NbExp=3; IntAct=EBI-465872, EBI-744104;
CC Q6QNY1; Q9NWB7: IFT57; NbExp=3; IntAct=EBI-465872, EBI-725672;
CC Q6QNY1; Q7Z3Y9: KRT26; NbExp=3; IntAct=EBI-465872, EBI-12084444;
CC Q6QNY1; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-465872, EBI-10181968;
CC Q6QNY1; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-465872, EBI-79165;
CC Q6QNY1; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-465872, EBI-747035;
CC Q6QNY1; O95295: SNAPIN; NbExp=10; IntAct=EBI-465872, EBI-296723;
CC Q6QNY1; A1L4H1: SSC5D; NbExp=3; IntAct=EBI-465872, EBI-10172867;
CC Q6QNY1; P32856-2: STX2; NbExp=3; IntAct=EBI-465872, EBI-11956649;
CC Q6QNY1; Q8N7C3: TRIML2; NbExp=4; IntAct=EBI-465872, EBI-11059915;
CC Q6QNY1; Q9Y3C0: WASHC3; NbExp=4; IntAct=EBI-465872, EBI-712969;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:15381421}. Lysosome membrane
CC {ECO:0000305|PubMed:25898167}. Note=Localizes to the centrosomes in a
CC microtubule-dependent manner. {ECO:0000269|PubMed:15381421}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ceap-16;
CC IsoId=Q6QNY1-1; Sequence=Displayed;
CC Name=2; Synonyms=Ceap-11;
CC IsoId=Q6QNY1-2; Sequence=VSP_018350;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed.
CC Expressed in various malignant tumor tissues (at protein level).
CC {ECO:0000269|PubMed:15381421}.
CC -!- SIMILARITY: Belongs to the BLOC1S2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20494.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY531265; AAT00461.1; -; mRNA.
DR EMBL; AY278457; AAQ19606.1; -; mRNA.
DR EMBL; AK298969; BAG61064.1; -; mRNA.
DR EMBL; AL138921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49836.1; -; Genomic_DNA.
DR EMBL; BC020494; AAH20494.1; ALT_INIT; mRNA.
DR CCDS; CCDS7490.1; -. [Q6QNY1-1]
DR RefSeq; NP_001001342.1; NM_001001342.2. [Q6QNY1-2]
DR RefSeq; NP_001269366.1; NM_001282437.1. [Q6QNY1-2]
DR RefSeq; NP_001269367.1; NM_001282438.1. [Q6QNY1-2]
DR RefSeq; NP_776170.2; NM_173809.4. [Q6QNY1-1]
DR AlphaFoldDB; Q6QNY1; -.
DR SMR; Q6QNY1; -.
DR BioGRID; 129431; 68.
DR ComplexPortal; CPX-1910; BLOC-1 complex.
DR ComplexPortal; CPX-5029; BORC complex.
DR CORUM; Q6QNY1; -.
DR IntAct; Q6QNY1; 52.
DR MINT; Q6QNY1; -.
DR STRING; 9606.ENSP00000359398; -.
DR iPTMnet; Q6QNY1; -.
DR PhosphoSitePlus; Q6QNY1; -.
DR BioMuta; BLOC1S2; -.
DR DMDM; 74749300; -.
DR EPD; Q6QNY1; -.
DR jPOST; Q6QNY1; -.
DR MassIVE; Q6QNY1; -.
DR MaxQB; Q6QNY1; -.
DR PaxDb; Q6QNY1; -.
DR PeptideAtlas; Q6QNY1; -.
DR PRIDE; Q6QNY1; -.
DR ProteomicsDB; 67307; -. [Q6QNY1-1]
DR ProteomicsDB; 67308; -. [Q6QNY1-2]
DR TopDownProteomics; Q6QNY1-1; -. [Q6QNY1-1]
DR TopDownProteomics; Q6QNY1-2; -. [Q6QNY1-2]
DR Antibodypedia; 55739; 109 antibodies from 21 providers.
DR DNASU; 282991; -.
DR Ensembl; ENST00000370372.7; ENSP00000359398.2; ENSG00000196072.12. [Q6QNY1-1]
DR Ensembl; ENST00000441611.5; ENSP00000410865.1; ENSG00000196072.12. [Q6QNY1-2]
DR Ensembl; ENST00000614731.4; ENSP00000481847.1; ENSG00000196072.12. [Q6QNY1-2]
DR GeneID; 282991; -.
DR KEGG; hsa:282991; -.
DR MANE-Select; ENST00000370372.7; ENSP00000359398.2; NM_173809.5; NP_776170.2.
DR UCSC; uc001kqv.4; human. [Q6QNY1-1]
DR CTD; 282991; -.
DR DisGeNET; 282991; -.
DR GeneCards; BLOC1S2; -.
DR HGNC; HGNC:20984; BLOC1S2.
DR HPA; ENSG00000196072; Low tissue specificity.
DR MIM; 609768; gene.
DR neXtProt; NX_Q6QNY1; -.
DR OpenTargets; ENSG00000196072; -.
DR PharmGKB; PA134936108; -.
DR VEuPathDB; HostDB:ENSG00000196072; -.
DR eggNOG; KOG4559; Eukaryota.
DR GeneTree; ENSGT00390000005889; -.
DR HOGENOM; CLU_110820_2_1_1; -.
DR InParanoid; Q6QNY1; -.
DR OMA; CSDMFEK; -.
DR PhylomeDB; Q6QNY1; -.
DR TreeFam; TF313861; -.
DR PathwayCommons; Q6QNY1; -.
DR SignaLink; Q6QNY1; -.
DR SIGNOR; Q6QNY1; -.
DR BioGRID-ORCS; 282991; 30 hits in 1083 CRISPR screens.
DR ChiTaRS; BLOC1S2; human.
DR GeneWiki; BLOC1S2; -.
DR GenomeRNAi; 282991; -.
DR Pharos; Q6QNY1; Tbio.
DR PRO; PR:Q6QNY1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q6QNY1; protein.
DR Bgee; ENSG00000196072; Expressed in tibialis anterior and 187 other tissues.
DR ExpressionAtlas; Q6QNY1; baseline and differential.
DR Genevisible; Q6QNY1; 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:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0000930; C:gamma-tubulin complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI: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:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; NAS:UniProtKB.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IDA: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:0060155; P:platelet dense granule organization; NAS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA: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; IPR019269; BLOC1_su2.
DR PANTHER; PTHR46479; PTHR46479; 1.
DR Pfam; PF10046; BLOC1_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Lysosome; Membrane; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..142
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 2"
FT /id="PRO_0000234543"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 79..127
FT /evidence="ECO:0000255"
FT COMPBIAS 12..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15381421"
FT /id="VSP_018350"
FT VARIANT 13
FT /note="S -> R (in dbSNP:rs33965491)"
FT /id="VAR_054068"
SQ SEQUENCE 142 AA; 15961 MW; 023DDBAC66E1912B CRC64;
MAAAAEGVLA TRSDEPARDD AAVETAEEAK EPAEADITEL CRDMFSKMAT YLTGELTATS
EDYKLLENMN KLTSLKYLEM KDIAINISRN LKDLNQKYAG LQPYLDQINV IEEQVAALEQ
AAYKLDAYSK KLEAKYKKLE KR
