AP1B1_HUMAN
ID AP1B1_HUMAN Reviewed; 949 AA.
AC Q10567; C9JRD1; F8WDL0; P78436; Q20WL3; Q86X54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=AP-1 complex subunit beta-1;
DE AltName: Full=Adaptor protein complex AP-1 subunit beta-1;
DE AltName: Full=Adaptor-related protein complex 1 subunit beta-1;
DE AltName: Full=Beta-1-adaptin;
DE AltName: Full=Beta-adaptin 1;
DE AltName: Full=Clathrin assembly protein complex 1 beta large chain;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin beta subunit;
GN Name=AP1B1; Synonyms=ADTB1, BAM22, CLAPB2;
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] (ISOFORMS A AND B).
RC TISSUE=Brain;
RX PubMed=7987321; DOI=10.1093/hmg/3.8.1393;
RA Peyrard M., Fransson I., Xie Y.-G., Han F.-Y., Ruttledge M.H., Swahn S.,
RA Collins J.E., Dunham I., Collins V.P., Dumanski J.P.;
RT "Characterization of a new member of the human beta-adaptin gene family
RT from chromosome 22q12, a candidate meningioma gene.";
RL Hum. Mol. Genet. 3:1393-1399(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lymph;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8812422; DOI=10.1006/geno.1996.0431;
RA Peyrard M., Pan H.-Q., Kedra D., Fransson I., Swahn S., Hartman K.,
RA Clifton S.W., Roe B.A., Dumanski J.P.;
RT "Structure of the promoter and genomic organization of the human beta'-
RT adaptin gene (BAM22) from chromosome 22q12.";
RL Genomics 36:112-117(1996).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
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 [10]
RP FUNCTION, AND INVOLVEMENT IN KIDAR.
RX PubMed=31630791; DOI=10.1016/j.ajhg.2019.09.020;
RA Alsaif H.S., Al-Owain M., Barrios-Llerena M.E., Gosadi G., Binamer Y.,
RA Devadason D., Ravenscroft J., Suri M., Alkuraya F.S.;
RT "Homozygous loss-of-function mutations in AP1B1, encoding beta-1 subunit of
RT adaptor-related protein complex 1, cause MEDNIK-like syndrome.";
RL Am. J. Hum. Genet. 105:1016-1022(2019).
RN [11]
RP INVOLVEMENT IN KIDAR, VARIANTS KIDAR ARG-144 AND 792-GLU--ASN-949 DEL, AND
RP CHARACTERIZATION OF VARIANT KIDAR 792-GLU--ASN-949 DEL.
RX PubMed=31630788; DOI=10.1016/j.ajhg.2019.09.021;
RA Boyden L.M., Atzmony L., Hamilton C., Zhou J., Lim Y.H., Hu R., Pappas J.,
RA Rabin R., Ekstien J., Hirsch Y., Prendiville J., Lifton R.P., Ferguson S.,
RA Choate K.A.;
RT "Recessive mutations in AP1B1 cause ichthyosis, deafness, and
RT photophobia.";
RL Am. J. Hum. Genet. 105:1023-1029(2019).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the late-Golgi/trans-Golgi network
CC (TGN) and/or endosomes (PubMed:31630791). The AP complexes mediate both
CC the recruitment of clathrin to membranes and the recognition of sorting
CC signals within the cytosolic tails of transmembrane cargo molecules.
CC {ECO:0000269|PubMed:31630791}.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit
CC AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small
CC adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3).
CC -!- INTERACTION:
CC Q10567; P35585: Ap1m1; Xeno; NbExp=5; IntAct=EBI-1171303, EBI-1040251;
CC Q10567-3; Q8TD06: AGR3; NbExp=3; IntAct=EBI-11978055, EBI-3925742;
CC Q10567-3; P53674: CRYBB1; NbExp=3; IntAct=EBI-11978055, EBI-7519424;
CC Q10567-3; O95363: FARS2; NbExp=3; IntAct=EBI-11978055, EBI-2513774;
CC Q10567-3; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-11978055, EBI-744935;
CC Q10567-3; O95872: GPANK1; NbExp=3; IntAct=EBI-11978055, EBI-751540;
CC Q10567-3; P78347-2: GTF2I; NbExp=3; IntAct=EBI-11978055, EBI-12033200;
CC Q10567-3; Q9H1H9-2: KIF13A; NbExp=3; IntAct=EBI-11978055, EBI-12216695;
CC Q10567-3; Q5SW96: LDLRAP1; NbExp=3; IntAct=EBI-11978055, EBI-747813;
CC Q10567-3; P40692: MLH1; NbExp=3; IntAct=EBI-11978055, EBI-744248;
CC Q10567-3; A6NI15: MSGN1; NbExp=3; IntAct=EBI-11978055, EBI-11991020;
CC Q10567-3; Q9HB07: MYG1; NbExp=3; IntAct=EBI-11978055, EBI-709754;
CC Q10567-3; Q8NC96: NECAP1; NbExp=3; IntAct=EBI-11978055, EBI-2609792;
CC Q10567-3; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-11978055, EBI-741048;
CC Q10567-3; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-11978055, EBI-11956563;
CC Q10567-3; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-11978055, EBI-11974061;
CC Q10567-3; Q9H2S5: RNF39; NbExp=3; IntAct=EBI-11978055, EBI-12235180;
CC Q10567-3; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-11978055, EBI-8787464;
CC Q10567-3; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-11978055, EBI-10241197;
CC Q10567-3; Q01081: U2AF1; NbExp=3; IntAct=EBI-11978055, EBI-632461;
CC Q10567-3; Q6ZN96; NbExp=3; IntAct=EBI-11978055, EBI-10255097;
CC Q10567-3; Q86V28; NbExp=3; IntAct=EBI-11978055, EBI-10259496;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Component of the coat surrounding the cytoplasmic face of coated
CC vesicles located at the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=A;
CC IsoId=Q10567-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q10567-2; Sequence=VSP_000163;
CC Name=C;
CC IsoId=Q10567-3; Sequence=VSP_000163, VSP_038753;
CC Name=4;
CC IsoId=Q10567-4; Sequence=VSP_000163, VSP_044928, VSP_038753;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DISEASE: Keratitis-ichthyosis-deafness syndrome, autosomal recessive
CC (KIDAR) [MIM:242150]: An autosomal recessive form of keratitis-
CC ichthyosis-deafness syndrome, a disease characterized by the
CC association of hyperkeratotic skin lesions with vascularizing keratitis
CC and profound sensorineural hearing loss. KIDAR patients manifest
CC ichthyosis, failure to thrive and developmental delay in childhood,
CC thrombocytopenia, photophobia, and progressive hearing loss. Low plasma
CC copper and ceruloplasmin levels have been reported in some patients.
CC {ECO:0000269|PubMed:31630788, ECO:0000269|PubMed:31630791}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; L13939; AAC98702.1; -; mRNA.
DR EMBL; CT841508; CAJ86438.1; -; mRNA.
DR EMBL; AC000041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046242; AAH46242.1; -; mRNA.
DR EMBL; U36268; AAC50684.2; -; Genomic_DNA.
DR EMBL; U36250; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36251; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36252; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36253; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36254; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36255; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36256; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36257; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36258; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36259; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36260; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36261; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36262; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36263; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36264; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36265; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36266; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; U36267; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; AF379038; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; AF379039; AAC50684.2; JOINED; Genomic_DNA.
DR EMBL; L48038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS13855.1; -. [Q10567-1]
DR CCDS; CCDS13856.2; -. [Q10567-3]
DR CCDS; CCDS54515.1; -. [Q10567-4]
DR PIR; I54360; I54360.
DR RefSeq; NP_001118.3; NM_001127.3.
DR RefSeq; NP_001159491.1; NM_001166019.1.
DR RefSeq; NP_663782.2; NM_145730.2.
DR PDB; 4HMY; X-ray; 7.00 A; B=1-584.
DR PDB; 4P6Z; X-ray; 3.00 A; B=1-584.
DR PDB; 6CM9; EM; 3.73 A; B=1-584.
DR PDB; 6CRI; EM; 6.80 A; B/I/J=14-583.
DR PDB; 6D83; EM; 4.27 A; B=1-584.
DR PDB; 6D84; EM; 6.72 A; B/F=1-584.
DR PDB; 6DFF; EM; 3.90 A; B=1-584.
DR PDBsum; 4HMY; -.
DR PDBsum; 4P6Z; -.
DR PDBsum; 6CM9; -.
DR PDBsum; 6CRI; -.
DR PDBsum; 6D83; -.
DR PDBsum; 6D84; -.
DR PDBsum; 6DFF; -.
DR AlphaFoldDB; Q10567; -.
DR SMR; Q10567; -.
DR BioGRID; 106671; 207.
DR ComplexPortal; CPX-5047; Ubiquitous AP-1 Adaptor complex, sigma1a variant.
DR ComplexPortal; CPX-5048; Ubiquitous AP-1 Adaptor complex, sigma1b variant.
DR ComplexPortal; CPX-5049; Ubiquitous AP-1 Adaptor complex, sigma1c variant.
DR ComplexPortal; CPX-5050; Endothelial AP-1 Adaptor complex, sigma1a variant.
DR CORUM; Q10567; -.
DR DIP; DIP-24207N; -.
DR ELM; Q10567; -.
DR IntAct; Q10567; 91.
DR MINT; Q10567; -.
DR STRING; 9606.ENSP00000350199; -.
DR BindingDB; Q10567; -.
DR ChEMBL; CHEMBL4630824; -.
DR TCDB; 9.B.278.1.1; the organellar-targeting adaptor protein complex (o-apc) family.
DR GlyGen; Q10567; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q10567; -.
DR MetOSite; Q10567; -.
DR PhosphoSitePlus; Q10567; -.
DR SwissPalm; Q10567; -.
DR BioMuta; AP1B1; -.
DR DMDM; 290457628; -.
DR CPTAC; CPTAC-1596; -.
DR EPD; Q10567; -.
DR jPOST; Q10567; -.
DR MassIVE; Q10567; -.
DR MaxQB; Q10567; -.
DR PaxDb; Q10567; -.
DR PeptideAtlas; Q10567; -.
DR PRIDE; Q10567; -.
DR ProteomicsDB; 31533; -.
DR ProteomicsDB; 58857; -. [Q10567-1]
DR ProteomicsDB; 58858; -. [Q10567-2]
DR ProteomicsDB; 58859; -. [Q10567-3]
DR Antibodypedia; 10350; 112 antibodies from 24 providers.
DR DNASU; 162; -.
DR Ensembl; ENST00000317368.11; ENSP00000319361.7; ENSG00000100280.17. [Q10567-4]
DR Ensembl; ENST00000357586.7; ENSP00000350199.2; ENSG00000100280.17. [Q10567-1]
DR Ensembl; ENST00000405198.6; ENSP00000384194.2; ENSG00000100280.17. [Q10567-3]
DR Ensembl; ENST00000432560.6; ENSP00000400065.2; ENSG00000100280.17. [Q10567-3]
DR GeneID; 162; -.
DR KEGG; hsa:162; -.
DR MANE-Select; ENST00000357586.7; ENSP00000350199.2; NM_001127.4; NP_001118.3.
DR UCSC; uc003afi.4; human. [Q10567-1]
DR CTD; 162; -.
DR DisGeNET; 162; -.
DR GeneCards; AP1B1; -.
DR HGNC; HGNC:554; AP1B1.
DR HPA; ENSG00000100280; Low tissue specificity.
DR MalaCards; AP1B1; -.
DR MIM; 242150; phenotype.
DR MIM; 600157; gene.
DR neXtProt; NX_Q10567; -.
DR OpenTargets; ENSG00000100280; -.
DR Orphanet; 171851; MEDNIK syndrome.
DR PharmGKB; PA24844; -.
DR VEuPathDB; HostDB:ENSG00000100280; -.
DR eggNOG; KOG1061; Eukaryota.
DR GeneTree; ENSGT00940000155991; -.
DR HOGENOM; CLU_006320_1_1_1; -.
DR InParanoid; Q10567; -.
DR OrthoDB; 323029at2759; -.
DR PhylomeDB; Q10567; -.
DR TreeFam; TF300318; -.
DR PathwayCommons; Q10567; -.
DR Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; Q10567; -.
DR SIGNOR; Q10567; -.
DR BioGRID-ORCS; 162; 22 hits in 1076 CRISPR screens.
DR ChiTaRS; AP1B1; human.
DR GeneWiki; AP1B1; -.
DR GenomeRNAi; 162; -.
DR Pharos; Q10567; Tbio.
DR PRO; PR:Q10567; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q10567; protein.
DR Bgee; ENSG00000100280; Expressed in endometrium epithelium and 201 other tissues.
DR ExpressionAtlas; Q10567; baseline and differential.
DR Genevisible; Q10567; HS.
DR GO; GO:0030121; C:AP-1 adaptor complex; IC:ComplexPortal.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0110010; P:basolateral protein secretion; IC:ComplexPortal.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1150; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF09066; B2-adapt-app_C; 1.
DR PIRSF; PIRSF002291; AP_complex_beta; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SMART; SM00185; ARM; 2.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle;
KW Deafness; Disease variant; Golgi apparatus; Ichthyosis; Membrane;
KW Nitration; Protein transport; Reference proteome; Transport.
FT CHAIN 1..949
FT /note="AP-1 complex subunit beta-1"
FT /id="PRO_0000193738"
FT REGION 584..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 574
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35643"
FT VAR_SEQ 667..673
FT /note="Missing (in isoform B, isoform C and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15461802,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7987321"
FT /id="VSP_000163"
FT VAR_SEQ 722..741
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044928"
FT VAR_SEQ 923..925
FT /note="Missing (in isoform C and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15461802,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_038753"
FT VARIANT 144
FT /note="C -> R (in KIDAR)"
FT /evidence="ECO:0000269|PubMed:31630788"
FT /id="VAR_083524"
FT VARIANT 777
FT /note="A -> T (in dbSNP:rs2857465)"
FT /id="VAR_062816"
FT VARIANT 792..949
FT /note="Missing (in KIDAR; no protein detected by Western
FT blot in patient cells)"
FT /evidence="ECO:0000269|PubMed:31630788"
FT /id="VAR_083525"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 27..42
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 174..190
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 275..290
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 296..312
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 314..319
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 332..345
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 404..420
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 442..454
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 455..458
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 462..467
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 471..475
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 478..494
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 517..532
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 534..540
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 557..564
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 565..568
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 570..574
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:4P6Z"
SQ SEQUENCE 949 AA; 104607 MW; 0B010DD2F29B248E CRC64;
MTDSKYFTTT KKGEIFELKA ELNSDKKEKK KEAVKKVIAS MTVGKDVSAL FPDVVNCMQT
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNT FVKDCEDPNP LIRALAVRTM GCIRVDKITE
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQLVEDQG FLDTLKDLIS DSNPMVVANA
VAALSEIAES HPSSNLLDLN PQSINKLLTA LNECTEWGQI FILDCLANYM PKDDREAQSI
CERVTPRLSH ANSAVVLSAV KVLMKFMEML SKDLDYYGTL LKKLAPPLVT LLSAEPELQY
VALRNINLIV QKRPEILKHE MKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIKDIFRK
YPNKYESVIA TLCENLDSLD EPEARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV
QLQLLTAIVK LFLKKPTETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVAAKEV
VLAEKPLISE ETDLIEPTLL DELICYIGTL ASVYHKPPSA FVEGGRGVVH KSLPPRTASS
ESAESPETAP TGAPPGEQPD VIPAQGDLLG DLLNLDLGPP VSGPPLATSS VQMGAVDLLG
GGLDSLMGDE PEGIGGTNFV APPTAAVPAN LGAPIGSGLS DLFDLTSGVG TLSGSYVAPK
AVWLPAMKAK GLEISGTFTR QVGSISMDLQ LTNKALQVMT DFAIQFNRNS FGLAPAAPLQ
VHAPLSPNQT VEISLPLSTV GSVMKMEPLN NLQVAVKNNI DVFYFSTLYP LHILFVEDGK
MDRQMFLATW KDIPNENEAQ FQIRDCPLNA EAASSKLQSS NIFTVAKRNV EGQDMLYQSL
KLTNGIWVLA ELRIQPGNPS CTDLELSLKC RAPEVSQHVY QAYETILKN
