ID AP3B1_HUMAN Reviewed; 1094 AA. AC O00203; E5RJ68; O00580; Q7Z393; Q9HD66; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 3. DT 27-MAR-2024, entry version 212. DE RecName: Full=AP-3 complex subunit beta-1; DE AltName: Full=Adaptor protein complex AP-3 subunit beta-1; DE AltName: Full=Adaptor-related protein complex 3 subunit beta-1; DE AltName: Full=Beta-3A-adaptin; DE AltName: Full=Clathrin assembly protein complex 3 beta-1 large chain; GN Name=AP3B1; Synonyms=ADTB3A; 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, IDENTIFICATION IN THE RP AP-3 COMPLEX, TISSUE SPECIFICITY, AND VARIANT GLU-585. RC TISSUE=Heart; RX PubMed=9151686; DOI=10.1083/jcb.137.4.835; RA Simpson F., Peden A.A., Christopoulou L., Robinson M.S.; RT "Characterization of the adaptor-related protein complex, AP-3."; RL J. Cell Biol. 137:835-845(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, TISSUE RP SPECIFICITY, AND VARIANT GLU-585. RC TISSUE=Pancreas; RX PubMed=9182526; DOI=10.1074/jbc.272.24.15078; RA Dell'Angelica E.C., Ooi C.E., Bonifacino J.S.; RT "Beta3A-adaptin, a subunit of the adaptor-like complex AP-3."; RL J. Biol. Chem. 272:15078-15084(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLU-585. RC TISSUE=Colon; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-585. RC TISSUE=Uterus; 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. RC TISSUE=Cervix; RA Kisseljov F., Petrenko A., Eshilev E., Kisseljova N.; RT "Identification of CpG islands hypermethylated in human tumors by the RT arbitrarily primed-PCR method."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-609; SER-750 AND RP SER-752, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-609, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] 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). RN [15] RP PYROPHOSPHORYLATION, AND INTERACTION WITH KIF3A. RX PubMed=19934039; DOI=10.1073/pnas.0909176106; RA Azevedo C., Burton A., Ruiz-Mateos E., Marsh M., Saiardi A.; RT "Inositol pyrophosphate mediated pyrophosphorylation of AP3B1 regulates RT HIV-1 Gag release."; RL Proc. Natl. Acad. Sci. U.S.A. 106:21161-21166(2009). RN [16] RP VARIANTS HPS2 390-LEU--GLN-410 DEL AND ARG-580. RX PubMed=10024875; DOI=10.1016/s1097-2765(00)80170-7; RA Dell'Angelica E.C., Shotelersuk V., Aguilar R.C., Gahl W.A., RA Bonifacino J.S.; RT "Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due RT to mutations in the beta 3A subunit of the AP-3 adaptor."; RL Mol. Cell 3:11-21(1999). RN [17] RP VARIANT [LARGE SCALE ANALYSIS] GLU-585, AND IDENTIFICATION BY MASS RP 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). CC -!- FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor CC protein complex 3 (AP-3) that plays a role in protein sorting in the CC late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes CC mediate both the recruitment of clathrin to membranes and the CC recognition of sorting signals within the cytosolic tails of CC transmembrane cargo molecules. AP-3 appears to be involved in the CC sorting of a subset of transmembrane proteins targeted to lysosomes and CC lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 CC is required to target cargos into vesicles assembled at cell bodies for CC delivery into neurites and nerve terminals. CC {ECO:0000305|PubMed:9151686}. CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed CC of two large adaptins (delta-type subunit AP3D1 and beta-type subunit CC AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and CC a small adaptin (sigma-type subunit APS1 or AP3S2) (Probable). AP-3 CC associates with the BLOC-1 complex (By similarity). Interacts with CC KIF3A; interaction is direct; interaction is impaired by CC pyrophosphorylation of AP3B1 (PubMed:19934039). CC {ECO:0000250|UniProtKB:Q9Z1T1, ECO:0000269|PubMed:19934039, CC ECO:0000305|PubMed:9151686}. CC -!- INTERACTION: CC O00203; A0A0S2Z5Q7: ALS2; NbExp=3; IntAct=EBI-1044383, EBI-25928834; CC O00203; P46379-2: BAG6; NbExp=3; IntAct=EBI-1044383, EBI-10988864; CC O00203; O14645: DNALI1; NbExp=3; IntAct=EBI-1044383, EBI-395638; CC O00203; P42858: HTT; NbExp=6; IntAct=EBI-1044383, EBI-466029; CC O00203; Q5S007: LRRK2; NbExp=2; IntAct=EBI-1044383, EBI-5323863; CC O00203; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1044383, EBI-748974; CC O00203; P37840: SNCA; NbExp=3; IntAct=EBI-1044383, EBI-985879; CC O00203-1; Q12955: ANK3; NbExp=2; IntAct=EBI-15816315, EBI-2691178; CC O00203-1; Q9Y496: KIF3A; NbExp=5; IntAct=EBI-15816315, EBI-1104844; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle CC membrane {ECO:0000305|PubMed:9151686}; Peripheral membrane protein CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus CC {ECO:0000305|PubMed:9151686}. Note=Component of the coat surrounding CC the cytoplasmic face of coated vesicles located at the Golgi complex. CC {ECO:0000305|PubMed:9151686}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O00203-1; Sequence=Displayed; CC Name=2; CC IsoId=O00203-3; Sequence=VSP_054708; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:9151686, ECO:0000269|PubMed:9182526}. CC -!- PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:9182526}. CC -!- PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5- CC IP7) impairs interaction with KIF3A (PubMed:19934039). Serine CC pyrophosphorylation is achieved by Mg(2+)-dependent, but enzyme CC independent transfer of a beta-phosphate from a inositol pyrophosphate CC to a pre-phosphorylated serine residue (PubMed:19934039). CC {ECO:0000269|PubMed:19934039}. CC -!- DISEASE: Hermansky-Pudlak syndrome 2 (HPS2) [MIM:608233]: A form of CC Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal CC recessive disorder characterized by oculocutaneous albinism, bleeding CC due to platelet storage pool deficiency, and lysosomal storage defects. CC This syndrome results from defects of diverse cytoplasmic organelles CC including melanosomes, platelet dense granules and lysosomes. Ceroid CC storage in the lungs is associated with pulmonary fibrosis, a common CC cause of premature death in individuals with HPS. HPS2 differs from the CC other forms of HPS in that it includes immunodeficiency in its CC phenotype and patients with HPS2 have an increased susceptibility to CC infections. {ECO:0000269|PubMed:10024875}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAD97982.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAD97982.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=AP3B1base; Note=AP3B1 mutation db; CC URL="http://structure.bmc.lu.se/idbase/AP3B1base/"; CC -!- WEB RESOURCE: Name=Mutations of the ADTB3A gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/adtb3mut.htm"; CC -!- WEB RESOURCE: Name=Albinism database (ADB); Note=AP3B1 mutations; CC URL="http://www.ifpcs.org/albinism/hps2mut.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U91931; AAD03778.1; -; mRNA. DR EMBL; U81504; AAB61638.1; -; mRNA. DR EMBL; BX538041; CAD97982.1; ALT_SEQ; mRNA. DR EMBL; AC024568; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC024578; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104108; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112197; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC038444; AAH38444.1; -; mRNA. DR EMBL; AF247736; AAG01739.1; -; Genomic_DNA. DR CCDS; CCDS4041.1; -. [O00203-1] DR CCDS; CCDS64186.1; -. [O00203-3] DR PIR; T50651; T50651. DR PIR; T50652; T50652. DR RefSeq; NP_001258698.1; NM_001271769.1. [O00203-3] DR RefSeq; NP_003655.3; NM_003664.4. [O00203-1] DR AlphaFoldDB; O00203; -. DR SMR; O00203; -. DR BioGRID; 114116; 185. DR ComplexPortal; CPX-5051; Ubiquitous AP-3 Adaptor complex, sigma3a variant. DR ComplexPortal; CPX-5052; Ubiquitous AP-3 Adaptor complex, sigma3b variant. DR CORUM; O00203; -. DR DIP; DIP-24208N; -. DR ELM; O00203; -. DR IntAct; O00203; 61. DR MINT; O00203; -. DR STRING; 9606.ENSP00000255194; -. DR GlyGen; O00203; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O00203; -. DR MetOSite; O00203; -. DR PhosphoSitePlus; O00203; -. DR SwissPalm; O00203; -. DR BioMuta; AP3B1; -. DR EPD; O00203; -. DR jPOST; O00203; -. DR MassIVE; O00203; -. DR MaxQB; O00203; -. DR PaxDb; 9606-ENSP00000255194; -. DR PeptideAtlas; O00203; -. DR ProteomicsDB; 16507; -. DR ProteomicsDB; 47775; -. [O00203-1] DR Pumba; O00203; -. DR Antibodypedia; 24502; 173 antibodies from 30 providers. DR DNASU; 8546; -. DR Ensembl; ENST00000255194.11; ENSP00000255194.7; ENSG00000132842.15. [O00203-1] DR Ensembl; ENST00000519295.6; ENSP00000430597.1; ENSG00000132842.15. [O00203-3] DR GeneID; 8546; -. DR KEGG; hsa:8546; -. DR MANE-Select; ENST00000255194.11; ENSP00000255194.7; NM_003664.5; NP_003655.3. DR UCSC; uc003kfj.5; human. [O00203-1] DR AGR; HGNC:566; -. DR CTD; 8546; -. DR DisGeNET; 8546; -. DR GeneCards; AP3B1; -. DR GeneReviews; AP3B1; -. DR HGNC; HGNC:566; AP3B1. DR HPA; ENSG00000132842; Low tissue specificity. DR MalaCards; AP3B1; -. DR MIM; 203300; phenotype. DR MIM; 603401; gene. DR MIM; 608233; phenotype. DR neXtProt; NX_O00203; -. DR OpenTargets; ENSG00000132842; -. DR Orphanet; 183678; Hermansky-Pudlak syndrome due to AP-3 deficiency. DR PharmGKB; PA24857; -. DR VEuPathDB; HostDB:ENSG00000132842; -. DR eggNOG; KOG1060; Eukaryota. DR GeneTree; ENSGT00940000157603; -. DR HOGENOM; CLU_006320_3_1_1; -. DR InParanoid; O00203; -. DR OMA; XLEILTN; -. DR OrthoDB; 7857at2759; -. DR PhylomeDB; O00203; -. DR TreeFam; TF314605; -. DR PathwayCommons; O00203; -. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions. DR SignaLink; O00203; -. DR SIGNOR; O00203; -. DR BioGRID-ORCS; 8546; 63 hits in 1166 CRISPR screens. DR ChiTaRS; AP3B1; human. DR GeneWiki; AP3B1; -. DR GenomeRNAi; 8546; -. DR Pharos; O00203; Tbio. DR PRO; PR:O00203; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; O00203; Protein. DR Bgee; ENSG00000132842; Expressed in tendon of biceps brachii and 202 other cell types or tissues. DR ExpressionAtlas; O00203; baseline and differential. DR GO; GO:0030123; C:AP-3 adaptor complex; NAS:ComplexPortal. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro. DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005769; C:early endosome; NAS:ComplexPortal. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0019903; F:protein phosphatase 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:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IEA:Ensembl. DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. DR GO; GO:0035654; P:clathrin-coated vesicle cargo loading, AP-3-mediated; NAS:ComplexPortal. DR GO; GO:0090152; P:establishment of protein localization to mitochondrial membrane involved in mitochondrial fission; IEA:Ensembl. DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl. DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl. DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc. DR GO; GO:0046907; P:intracellular transport; NAS:ComplexPortal. DR GO; GO:0006882; P:intracellular zinc ion homeostasis; IEA:Ensembl. DR GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl. DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl. DR GO; GO:1903232; P:melanosome assembly; NAS:ComplexPortal. DR GO; GO:0032438; P:melanosome organization; IMP:UniProtKB. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0060155; P:platelet dense granule organization; NAS:ComplexPortal. DR GO; GO:0051138; P:positive regulation of NK T cell differentiation; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl. DR GO; GO:0036211; P:protein modification process; IEA:Ensembl. DR GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl. DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl. DR GO; GO:0007338; P:single fertilization; IEA:Ensembl. DR GO; GO:0098773; P:skin epidermis development; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:Ensembl. DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR026740; AP3_beta. DR InterPro; IPR029394; AP3B1_Ser. DR InterPro; IPR029390; AP3B_C. DR InterPro; IPR026739; AP_beta. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR015151; B-adaptin_app_sub_C. DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N. DR PANTHER; PTHR11134; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1. DR PANTHER; PTHR11134:SF10; AP-3 COMPLEX SUBUNIT BETA-1; 1. DR Pfam; PF01602; Adaptin_N; 1. DR Pfam; PF14796; AP3B1_C; 1. DR Pfam; PF14797; SEEEED; 1. DR PIRSF; PIRSF037096; AP3_complex_beta; 1. DR SMART; SM01355; AP3B1_C; 1. DR SMART; SM01020; B2-adapt-app_C; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; O00203; HS. PE 1: Evidence at protein level; KW Albinism; Alternative splicing; Cytoplasmic vesicle; Disease variant; KW Golgi apparatus; Hermansky-Pudlak syndrome; Membrane; Phosphoprotein; KW Protein transport; Reference proteome; Transport. FT CHAIN 1..1094 FT /note="AP-3 complex subunit beta-1" FT /id="PRO_0000193746" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 268..292 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 662..811 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 702..722 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 723..767 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 789..811 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 609 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 750 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 752 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT VAR_SEQ 1..49 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_054708" FT VARIANT 390..410 FT /note="Missing (in HPS2)" FT /evidence="ECO:0000269|PubMed:10024875" FT /id="VAR_011595" FT VARIANT 580 FT /note="L -> R (in HPS2; dbSNP:rs121908904)" FT /evidence="ECO:0000269|PubMed:10024875" FT /id="VAR_011596" FT VARIANT 585 FT /note="V -> E (in dbSNP:rs6453373)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:9151686, FT ECO:0000269|PubMed:9182526, ECO:0007744|PubMed:21269460" FT /id="VAR_058404" FT CONFLICT 168 FT /note="K -> R (in Ref. 3; CAD97982)" FT /evidence="ECO:0000305" FT CONFLICT 379 FT /note="S -> P (in Ref. 3; CAD97982)" FT /evidence="ECO:0000305" FT CONFLICT 804 FT /note="Missing (in Ref. 1; AAD03778)" FT /evidence="ECO:0000305" SQ SEQUENCE 1094 AA; 121320 MW; AC683CE18EF90555 CRC64; MSSNSFPYNE QSGGGEATEL GQEATSTISP SGAFGLFSSD LKKNEDLKQM LESNKDSAKL DAMKRIVGMI AKGKNASELF PAVVKNVASK NIEIKKLVYV YLVRYAEEQQ DLALLSISTF QRALKDPNQL IRASALRVLS SIRVPIIVPI MMLAIKEASA DLSPYVRKNA AHAIQKLYSL DPEQKEMLIE VIEKLLKDKS TLVAGSVVMA FEEVCPDRID LIHKNYRKLC NLLVDVEEWG QVVIIHMLTR YARTQFVSPW KEGDELEDNG KNFYESDDDQ KEKTDKKKKP YTMDPDHRLL IRNTKPLLQS RNAAVVMAVA QLYWHISPKS EAGIISKSLV RLLRSNREVQ YIVLQNIATM SIQRKGMFEP YLKSFYVRST DPTMIKTLKL EILTNLANEA NISTLLREFQ TYVKSQDKQF AAATIQTIGR CATNILEVTD TCLNGLVCLL SNRDEIVVAE SVVVIKKLLQ MQPAQHGEII KHMAKLLDSI TVPVARASIL WLIGENCERV PKIAPDVLRK MAKSFTSEDD LVKLQILNLG AKLYLTNSKQ TKLLTQYILN LGKYDQNYDI RDRTRFIRQL IVPNVKSGAL SKYAKKIFLA QKPAPLLESP FKDRDHFQLG TLSHTLNIKA TGYLELSNWP EVAPDPSVRN VEVIELAKEW TPAGKAKQEN SAKKFYSESE EEEDSSDSSS DSESESGSES GEQGESGEEG DSNEDSSEDS SSEQDSESGR ESGLENKRTA KRNSKAKGKS DSEDGEKENE KSKTSDSSND ESSSIEDSSS DSESESEPES ESESRRVTKE KEKKTKQDRT PLTKDVSLLD LDDFNPVSTP VALPTPALSP SLMADLEGLH LSTSSSVISV STPAFVPTKT HVLLHRMSGK GLAAHYFFPR QPCIFGDKMV SIQITLNNTT DRKIENIHIG EKKLPIGMKM HVFNPIDSLE PEGSITVSMG IDFCDSTQTA SFQLCTKDDC FNVNIQPPVG ELLLPVAMSE KDFKKEQGVL TGMNETSAVI IAAPQNFTPS VIFQKVVNVA NVGAVPSGQD NIHRFAAKTV HSGSLMLVTV ELKEGSTAQL IINTEKTVIG SVLLRELKPV LSQG //