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   24-JAN-2024, entry version 160.
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; 75.
DR   ComplexPortal; CPX-1910; BLOC-1 complex.
DR   ComplexPortal; CPX-5029; BORC complex.
DR   CORUM; Q6QNY1; -.
DR   IntAct; Q6QNY1; 53.
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; 9606-ENSP00000359398; -.
DR   PeptideAtlas; Q6QNY1; -.
DR   ProteomicsDB; 67307; -. [Q6QNY1-1]
DR   ProteomicsDB; 67308; -. [Q6QNY1-2]
DR   Pumba; Q6QNY1; -.
DR   TopDownProteomics; Q6QNY1-1; -. [Q6QNY1-1]
DR   TopDownProteomics; Q6QNY1-2; -. [Q6QNY1-2]
DR   Antibodypedia; 55739; 118 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   AGR; HGNC:20984; -.
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   OrthoDB; 9322at2759; -.
DR   PhylomeDB; Q6QNY1; -.
DR   TreeFam; TF313861; -.
DR   PathwayCommons; Q6QNY1; -.
DR   SignaLink; Q6QNY1; -.
DR   SIGNOR; Q6QNY1; -.
DR   BioGRID-ORCS; 282991; 31 hits in 1159 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 188 other cell types or tissues.
DR   ExpressionAtlas; Q6QNY1; baseline and differential.
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; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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: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; NAS: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 DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0051036; P:regulation of endosome size; NAS:ComplexPortal.
DR   GO; GO:0062196; P:regulation of lysosome size; NAS:ComplexPortal.
DR   InterPro; IPR019269; BLOC1_su2.
DR   PANTHER; PTHR46479; BIOGENESIS OF LYSOSOME-RELATED ORGANELLES COMPLEX 1 SUBUNIT 2; 1.
DR   PANTHER; PTHR46479:SF1; BIOGENESIS OF LYSOSOME-RELATED ORGANELLES COMPLEX 1 SUBUNIT 2; 1.
DR   Pfam; PF10046; BLOC1_2; 1.
DR   Genevisible; Q6QNY1; HS.
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
//