ID   AP1B1_HUMAN             Reviewed;         949 AA.
AC   Q10567; P78436;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   09-FEB-2010, entry version 86.
DE   RecName: Full=AP-1 complex subunit beta-1;
DE   AltName: Full=Adapter-related protein complex 1 subunit beta-1;
DE   AltName: Full=Adaptor protein complex AP-1 subunit beta-1;
DE   AltName: Full=Beta-adaptin 1;
DE   AltName: Full=Beta1-adaptin;
DE   AltName: Full=Golgi adaptor HA1/AP1 adaptin beta subunit;
DE   AltName: Full=Clathrin assembly protein complex 1 beta large chain;
GN   Name=AP1B1; Synonyms=ADTB1, BAM22, CLAPB2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC   TISSUE=Brain;
RX   MEDLINE=95078847; PubMed=7987321; DOI=10.1093/hmg/3.8.1393;
RA   Peyrard M., Fransson I., Xie Y.-G., Han F.-Y., Ruttledge M.H.,
RA   Swahn S., Collins J.E., Dunham I., Collins V.P., Dumanski J.P.;
RT   "Characterization of a new member of the human beta-adaptin gene
RT   family from chromosome 22q12, a candidate meningioma gene.";
RL   Hum. Mol. Genet. 3:1393-1399(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-922.
RX   MEDLINE=96411653; 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
RT   beta'-adaptin gene (BAM22) from chromosome 22q12.";
RL   Genomics 36:112-117(1996).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-897, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Lung;
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [4]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
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).
CC   -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
CC       that plays a role in protein sorting in the late-Golgi/trans-Golgi
CC       network (TGN) and/or endosomes. The AP complexes mediate both the
CC       recruitment of clathrin to membranes and the recognition of
CC       sorting signals within the cytosolic tails of transmembrane cargo
CC       molecules.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is an heterotetramer
CC       composed of two large adaptins (gamma-type subunit AP1G1 and beta-
CC       type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or
CC       AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or
CC       AP1S3).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle,
CC       clathrin-coated vesicle membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Note=Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles located at the Golgi complex.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q10567-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q10567-2; Sequence=VSP_000163;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
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DR   EMBL; L13939; AAC98702.1; -; 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   IPI; IPI00328257; -.
DR   IPI; IPI00413947; -.
DR   PIR; I54360; I54360.
DR   RefSeq; NP_001118.3; -.
DR   UniGene; Hs.368794; -.
DR   SMR; Q10567; 2-583, 714-949.
DR   DIP; DIP-24207N; -.
DR   STRING; Q10567; -.
DR   PhosphoSite; Q10567; -.
DR   PRIDE; Q10567; -.
DR   Ensembl; ENST00000357586; ENSP00000350199; ENSG00000100280; Homo sapiens.
DR   Ensembl; ENST00000405198; ENSP00000384194; ENSG00000100280; Homo sapiens.
DR   GeneID; 162; -.
DR   KEGG; hsa:162; -.
DR   UCSC; uc003afj.1; human.
DR   UCSC; uc003afk.1; human.
DR   CTD; 162; -.
DR   GeneCards; GC22M028048; -.
DR   H-InvDB; HIX0027860; -.
DR   HGNC; HGNC:554; AP1B1.
DR   MIM; 600157; gene.
DR   PharmGKB; PA24844; -.
DR   eggNOG; prNOG09855; -.
DR   HOGENOM; HBG718694; -.
DR   HOVERGEN; Q10567; -.
DR   InParanoid; Q10567; -.
DR   PhylomeDB; Q10567; -.
DR   Pathway_Interaction_DB; hnf3apathway; FOXA1 transcription factor network.
DR   Reactome; REACT_11123; Membrane Trafficking.
DR   Reactome; REACT_6185; HIV Infection.
DR   NextBio; 647; -.
DR   ArrayExpress; Q10567; -.
DR   Bgee; Q10567; -.
DR   CleanEx; HS_AP1B1; -.
DR   Genevestigator; Q10567; -.
DR   GermOnline; ENSG00000100280; Homo sapiens.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; EXP:Reactome.
DR   InterPro; IPR016342; AP_complex_bsu.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012295; b_Adaptin_TBP_C.
DR   InterPro; IPR009028; Calthrin/coatomer_app_sub_C.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin/coatomer_app_Ig-like.
DR   InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR   InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR   InterPro; IPR015151; Clathrin_b-adaptin_app_sub_C.
DR   Gene3D; G3DSA:3.30.310.10; b_Adaptin_TBP_C; 1.
DR   Gene3D; G3DSA:2.60.40.1150; Clathrin_b-adaptin_app_Ig-like; 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.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Complete proteome;
KW   Cytoplasmic vesicle; Endocytosis; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    949       AP-1 complex subunit beta-1.
FT                                /FTId=PRO_0000193738.
FT   COMPBIAS    576    725       Pro-rich (stalk region).
FT   MOD_RES     318    318       N6-acetyllysine.
FT   MOD_RES     897    897       Phosphotyrosine.
FT   VAR_SEQ     667    673       Missing (in isoform B).
FT                                /FTId=VSP_000163.
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
//