AP3B1_HUMAN
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 03-AUG-2022, entry version 203.
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";
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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; 144.
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; 56.
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; O00203; -.
DR PeptideAtlas; O00203; -.
DR PRIDE; O00203; -.
DR ProteomicsDB; 16507; -.
DR ProteomicsDB; 47775; -. [O00203-1]
DR Antibodypedia; 24502; 150 antibodies from 30 providers.
DR DNASU; 8546; -.
DR Ensembl; ENST00000255194.11; ENSP00000255194.7; ENSG00000132842.14. [O00203-1]
DR Ensembl; ENST00000519295.5; ENSP00000430597.1; ENSG00000132842.14. [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 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; ASSNEWK; -.
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; 62 hits in 1088 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 200 other tissues.
DR ExpressionAtlas; O00203; baseline and differential.
DR Genevisible; O00203; HS.
DR GO; GO:0030123; C:AP-3 adaptor complex; IC: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; IC: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:0045202; C:synapse; 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:0006882; P:cellular zinc ion homeostasis; IEA:Ensembl.
DR GO; GO:0035654; P:clathrin-coated vesicle cargo loading, AP-3-mediated; IC: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; IC:ComplexPortal.
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; IC: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; IC: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:0050790; P:regulation of catalytic activity; 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:0016182; P:synaptic vesicle budding from endosome; 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; -; 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; PTHR11134; 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; SSF48371; 1.
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
