Full text data of AP1B1
AP1B1
(ADTB1, BAM22, CLAPB2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
AP-1 complex subunit beta-1 (Adapter-related protein complex 1 subunit beta-1; Adaptor protein complex AP-1 subunit beta-1; Beta-1-adaptin; Beta-adaptin 1; Clathrin assembly protein complex 1 beta large chain; Golgi adaptor HA1/AP1 adaptin beta subunit)
AP-1 complex subunit beta-1 (Adapter-related protein complex 1 subunit beta-1; Adaptor protein complex AP-1 subunit beta-1; Beta-1-adaptin; Beta-adaptin 1; Clathrin assembly protein complex 1 beta large chain; Golgi adaptor HA1/AP1 adaptin beta subunit)
UniProt
Q10567
ID AP1B1_HUMAN Reviewed; 949 AA.
AC Q10567; C9JRD1; F8WDL0; P78436; Q20WL3; Q86X54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAR-2010, sequence version 2.
DT 22-JAN-2014, entry version 124.
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-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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND VARIANT ALA-777.
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.,
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 [LARGE SCALE MRNA] (ISOFORM C), AND VARIANT
RP ALA-777.
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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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), AND VARIANT
RP ALA-777.
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-922, AND VARIANT ALA-777.
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
RT beta'-adaptin gene (BAM22) from chromosome 22q12.";
RL Genomics 36:112-117(1996).
RN [6]
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.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 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 a 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 -!- INTERACTION:
CC P35585:Ap1m1 (xeno); NbExp=3; IntAct=EBI-1171303, EBI-1040251;
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=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 Note=No experimental confirmation available;
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; 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 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 RefSeq; XP_005261438.1; XM_005261381.1.
DR UniGene; Hs.368794; -.
DR PDB; 4HMY; X-ray; 7.00 A; B=1-584.
DR PDBsum; 4HMY; -.
DR ProteinModelPortal; Q10567; -.
DR SMR; Q10567; 12-574, 714-949.
DR DIP; DIP-24207N; -.
DR IntAct; Q10567; 26.
DR MINT; MINT-1540570; -.
DR STRING; 9606.ENSP00000350199; -.
DR PhosphoSite; Q10567; -.
DR DMDM; 290457628; -.
DR PaxDb; Q10567; -.
DR PRIDE; Q10567; -.
DR DNASU; 162; -.
DR Ensembl; ENST00000317368; ENSP00000319361; ENSG00000100280.
DR Ensembl; ENST00000356015; ENSP00000348297; ENSG00000100280.
DR Ensembl; ENST00000357586; ENSP00000350199; ENSG00000100280.
DR Ensembl; ENST00000402502; ENSP00000386071; ENSG00000100280.
DR Ensembl; ENST00000405198; ENSP00000384194; ENSG00000100280.
DR Ensembl; ENST00000415447; ENSP00000387612; ENSG00000100280.
DR Ensembl; ENST00000432560; ENSP00000400065; ENSG00000100280.
DR GeneID; 162; -.
DR KEGG; hsa:162; -.
DR UCSC; uc003afj.3; human.
DR CTD; 162; -.
DR GeneCards; GC22M029723; -.
DR HGNC; HGNC:554; AP1B1.
DR MIM; 600157; gene.
DR neXtProt; NX_Q10567; -.
DR PharmGKB; PA24844; -.
DR eggNOG; COG5096; -.
DR HOGENOM; HOG000163270; -.
DR HOVERGEN; HBG050515; -.
DR InParanoid; Q10567; -.
DR KO; K12392; -.
DR OMA; QPGNPSC; -.
DR OrthoDB; EOG7BGHK0; -.
DR PhylomeDB; Q10567; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; AP1B1; human.
DR GeneWiki; AP1B1; -.
DR GenomeRNAi; 162; -.
DR NextBio; 35514080; -.
DR PRO; PR:Q10567; -.
DR ArrayExpress; Q10567; -.
DR Bgee; Q10567; -.
DR CleanEx; HS_AP1B1; -.
DR Genevestigator; Q10567; -.
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:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
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; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR012295; Beta2_adaptin/TBP_C_dom.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
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; 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; Complete proteome;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Nitration;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 949 AP-1 complex subunit beta-1.
FT /FTId=PRO_0000193738.
FT COMPBIAS 576 725 Pro-rich (stalk region).
FT MOD_RES 2 2 N-acetylthreonine (By similarity).
FT MOD_RES 265 265 N6-acetyllysine (By similarity).
FT MOD_RES 318 318 N6-acetyllysine.
FT MOD_RES 574 574 Nitrated tyrosine (By similarity).
FT VAR_SEQ 667 673 Missing (in isoform B, isoform C and
FT isoform 4).
FT /FTId=VSP_000163.
FT VAR_SEQ 722 741 Missing (in isoform 4).
FT /FTId=VSP_044928.
FT VAR_SEQ 923 925 Missing (in isoform C and isoform 4).
FT /FTId=VSP_038753.
FT VARIANT 777 777 T -> A (in dbSNP:rs2857465).
FT /FTId=VAR_062816.
SQ SEQUENCE 949 AA; 104637 MW; FE1BA762F9318585 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 FGLAPATPLQ
VHAPLSPNQT VEISLPLSTV GSVMKMEPLN NLQVAVKNNI DVFYFSTLYP LHILFVEDGK
MDRQMFLATW KDIPNENEAQ FQIRDCPLNA EAASSKLQSS NIFTVAKRNV EGQDMLYQSL
KLTNGIWVLA ELRIQPGNPS CTDLELSLKC RAPEVSQHVY QAYETILKN
//
ID AP1B1_HUMAN Reviewed; 949 AA.
AC Q10567; C9JRD1; F8WDL0; P78436; Q20WL3; Q86X54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAR-2010, sequence version 2.
DT 22-JAN-2014, entry version 124.
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-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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND VARIANT ALA-777.
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.,
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 [LARGE SCALE MRNA] (ISOFORM C), AND VARIANT
RP ALA-777.
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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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), AND VARIANT
RP ALA-777.
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-922, AND VARIANT ALA-777.
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
RT beta'-adaptin gene (BAM22) from chromosome 22q12.";
RL Genomics 36:112-117(1996).
RN [6]
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.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 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 a 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 -!- INTERACTION:
CC P35585:Ap1m1 (xeno); NbExp=3; IntAct=EBI-1171303, EBI-1040251;
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=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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC -----------------------------------------------------------------------
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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 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 RefSeq; XP_005261438.1; XM_005261381.1.
DR UniGene; Hs.368794; -.
DR PDB; 4HMY; X-ray; 7.00 A; B=1-584.
DR PDBsum; 4HMY; -.
DR ProteinModelPortal; Q10567; -.
DR SMR; Q10567; 12-574, 714-949.
DR DIP; DIP-24207N; -.
DR IntAct; Q10567; 26.
DR MINT; MINT-1540570; -.
DR STRING; 9606.ENSP00000350199; -.
DR PhosphoSite; Q10567; -.
DR DMDM; 290457628; -.
DR PaxDb; Q10567; -.
DR PRIDE; Q10567; -.
DR DNASU; 162; -.
DR Ensembl; ENST00000317368; ENSP00000319361; ENSG00000100280.
DR Ensembl; ENST00000356015; ENSP00000348297; ENSG00000100280.
DR Ensembl; ENST00000357586; ENSP00000350199; ENSG00000100280.
DR Ensembl; ENST00000402502; ENSP00000386071; ENSG00000100280.
DR Ensembl; ENST00000405198; ENSP00000384194; ENSG00000100280.
DR Ensembl; ENST00000415447; ENSP00000387612; ENSG00000100280.
DR Ensembl; ENST00000432560; ENSP00000400065; ENSG00000100280.
DR GeneID; 162; -.
DR KEGG; hsa:162; -.
DR UCSC; uc003afj.3; human.
DR CTD; 162; -.
DR GeneCards; GC22M029723; -.
DR HGNC; HGNC:554; AP1B1.
DR MIM; 600157; gene.
DR neXtProt; NX_Q10567; -.
DR PharmGKB; PA24844; -.
DR eggNOG; COG5096; -.
DR HOGENOM; HOG000163270; -.
DR HOVERGEN; HBG050515; -.
DR InParanoid; Q10567; -.
DR KO; K12392; -.
DR OMA; QPGNPSC; -.
DR OrthoDB; EOG7BGHK0; -.
DR PhylomeDB; Q10567; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; AP1B1; human.
DR GeneWiki; AP1B1; -.
DR GenomeRNAi; 162; -.
DR NextBio; 35514080; -.
DR PRO; PR:Q10567; -.
DR ArrayExpress; Q10567; -.
DR Bgee; Q10567; -.
DR CleanEx; HS_AP1B1; -.
DR Genevestigator; Q10567; -.
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:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
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; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR012295; Beta2_adaptin/TBP_C_dom.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
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; 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; Complete proteome;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Nitration;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 949 AP-1 complex subunit beta-1.
FT /FTId=PRO_0000193738.
FT COMPBIAS 576 725 Pro-rich (stalk region).
FT MOD_RES 2 2 N-acetylthreonine (By similarity).
FT MOD_RES 265 265 N6-acetyllysine (By similarity).
FT MOD_RES 318 318 N6-acetyllysine.
FT MOD_RES 574 574 Nitrated tyrosine (By similarity).
FT VAR_SEQ 667 673 Missing (in isoform B, isoform C and
FT isoform 4).
FT /FTId=VSP_000163.
FT VAR_SEQ 722 741 Missing (in isoform 4).
FT /FTId=VSP_044928.
FT VAR_SEQ 923 925 Missing (in isoform C and isoform 4).
FT /FTId=VSP_038753.
FT VARIANT 777 777 T -> A (in dbSNP:rs2857465).
FT /FTId=VAR_062816.
SQ SEQUENCE 949 AA; 104637 MW; FE1BA762F9318585 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 FGLAPATPLQ
VHAPLSPNQT VEISLPLSTV GSVMKMEPLN NLQVAVKNNI DVFYFSTLYP LHILFVEDGK
MDRQMFLATW KDIPNENEAQ FQIRDCPLNA EAASSKLQSS NIFTVAKRNV EGQDMLYQSL
KLTNGIWVLA ELRIQPGNPS CTDLELSLKC RAPEVSQHVY QAYETILKN
//
MIM
600157
*RECORD*
*FIELD* NO
600157
*FIELD* TI
*600157 ADAPTOR-RELATED PROTEIN COMPLEX 1, BETA-1 SUBUNIT; AP1B1
;;ADAPTIN, BETA-1; ADTB1;;
read moreADAPTIN, BETA-PRIME;;
BETA-ADAPTIN-MENINGIOMA GENE ON CHROMOSOME 22; BAM22
*FIELD* TX
GENE FAMILY
Adaptins are essential for the formation of adaptor complexes of
clathrin-coded vesicles. Adaptins interact with the cytoplasmic domains
of membrane-spanning receptors in the course of their endocytic/exocytic
transport. They represent 1 of at least 4 components of intracellular
transport and receptor downregulation pathways, the others being
alpha/gamma-adaptins, receptors, and ligand molecules. Beta-adaptins
have a bipartite structure with invariant N-terminal and variable
C-terminal domains. The former interact with the uniform component of
coded vesicles, the clathrin lattice. In contrast, the C-terminal domain
provides a set of recognition sequences for other proteins and therefore
functions as part of a selector domain responsible for the specific
entrapment of membrane-bound proteins in vesicles.
CLONING
A 140-kb homozygous deletion in 22q12 in a sporadic meningioma directed
Peyrard et al. (1994) to the cloning and characterization of a new
member of the human beta-adaptin gene family, which was named BAM22 for
'beta-adaptin-meningioma-chromosome 22.' The BAM22 gene was totally
inactivated in the tumor with homozygous deletion. Northern blot
analysis of 70 sporadic meningiomas showed specific loss of expression
in 8 tumors, suggesting inactivation of BAM22. Based on this, Peyrard et
al. (1994) suggested that BAM22 is a second chromosome 22 locus
important in meningioma development and second in importance to the NF2
gene (607379), which is mutant in neurofibromatosis type II (101000).
The likelihood that multiple loci on chromosome 22 are involved in the
oncogenesis of meningioma is suggested by the facts that monosomy 22 is
observed in as many as 65% of tumors (Zankl and Zang, 1980); some
meningiomas have chromosome 22 deletions not encompassing the NF2 gene
region and do not show mutations in the NF2 gene; and constitutional
ring chromosome 22 has been observed in young patients with multiple
tumors (Arinami et al., 1986; Petrella et al., 1993).
GENE STRUCTURE
Peyrard et al. (1996) described the genomic structure of the human
beta-adaptin gene BAM22. The gene consists of 22 exons spanning over 100
kb. They analyzed 7 exons for sporadic mutations in 110 sporadic
meningiomas and failed to detect point mutations. Peyrard et al. (1996)
suggested that mutations in the promoter region of the gene may be
important in generating meningiomas. They also considered the
possibility that the 140-kb region involved in homozygous deletions in
meningiomas may contain another candidate tumor suppressor gene.
GENE FUNCTION
Doray et al. (2002) demonstrated that the Golgi-localized,
gamma-ear-containing adenosine diphosphate ribosylation factor-binding
proteins (GGA1, 606004 and GGA3, 606006) and the coat protein adaptor
protein-1 (AP-1) complex (see AP1G2, 603534) colocalize in
clathrin-coated buds of the trans-Golgi networks of mouse L cells and
human HeLa cells. Binding studies revealed a direct interaction between
the hinge domains of the GGAs and the gamma-ear domain of AP-1. Further,
AP-1 contained bound casein kinase-2 (see CSNK2A1, 115440) that
phosphorylated GGA1 and GGA3, thereby causing autoinhibition. Doray et
al. (2002) demonstrated that this autoinhibition could induce the
directed transfer of mannose 6-phosphate receptors (see 154540) from the
GGAs to AP-1. Mannose 6-phosphate receptors that were defective in
binding to GGAs were poorly incorporated into adaptor protein complex
containing clathrin coated vesicles. Thus, Doray et al. (2002) concluded
that GGAs and the AP-1 complex interact to package mannose 6-phosphate
receptors into AP-1-containing coated vesicles.
MAPPING
Peyrard et al. (1994) identified the BAM22 gene within chromosome 22q12.
*FIELD* RF
1. Arinami, T.; Kondo, I.; Hamaguchi, H.; Nakajima, S.: Multifocal
meningiomas in a patient with a constitutional ring chromosome 22. J.
Med. Genet. 23: 178-180, 1986.
2. Doray, B.; Ghosh, P.; Griffith, J.; Geuze, H. J.; Kornfeld, S.
: Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi
network. Science 297: 1700-1703, 2002.
3. Petrella, R.; Levine, S.; Wilmot, P. L.; Ashar, K. D.; Casamassima,
A. C.; Shapiro, L. R.: Multiple meningiomas in a patient with constitutional
ring chromosome 22. Am. J. Med. Genet. 47: 184-186, 1993.
4. Peyrard, M.; Fransson, I.; Xie, Y.-G.; Han, F.-Y.; Ruttledge, M.
H.; Swahn, S.; Collins, J. E.; Dunham, I.; Collins, V. P.; Dumanski,
J. P.: Characterization of a new member of the human beta-adaptin
gene family from chromosome 22q12, a candidate meningioma gene. Hum.
Molec. Genet. 3: 1393-1399, 1994.
5. Peyrard, M.; Pan, H.-Q.; Kedra, D.; Fransson, I.; Swahn, S.; Hartman,
K.; Clifton, S. W.; Roe, B. A.; Dumanski, J. P.: Structure of the
promoter and genomic organization of the human beta-prime-adaptin
gene (BAM22) from chromosome 22q12. Genomics 36: 112-117, 1996.
6. Zankl, H.; Zang, K. D.: Correlations between clinical and cytogenetical
data in 180 human meningiomas. Cancer Genet. Cytogenet. 1: 351-356,
1980.
*FIELD* CN
Ada Hamosh - updated: 10/22/2002
Moyra Smith - updated: 12/18/1996
*FIELD* CD
Victor A. McKusick: 10/19/1994
*FIELD* ED
carol: 01/28/2003
alopez: 10/23/2002
alopez: 10/22/2002
carol: 9/19/2000
psherman: 1/5/1999
dkim: 6/26/1998
alopez: 7/30/1997
alopez: 7/8/1997
mark: 12/18/1996
jamie: 12/17/1996
mimadm: 9/23/1995
carol: 11/2/1994
terry: 10/19/1994
*RECORD*
*FIELD* NO
600157
*FIELD* TI
*600157 ADAPTOR-RELATED PROTEIN COMPLEX 1, BETA-1 SUBUNIT; AP1B1
;;ADAPTIN, BETA-1; ADTB1;;
read moreADAPTIN, BETA-PRIME;;
BETA-ADAPTIN-MENINGIOMA GENE ON CHROMOSOME 22; BAM22
*FIELD* TX
GENE FAMILY
Adaptins are essential for the formation of adaptor complexes of
clathrin-coded vesicles. Adaptins interact with the cytoplasmic domains
of membrane-spanning receptors in the course of their endocytic/exocytic
transport. They represent 1 of at least 4 components of intracellular
transport and receptor downregulation pathways, the others being
alpha/gamma-adaptins, receptors, and ligand molecules. Beta-adaptins
have a bipartite structure with invariant N-terminal and variable
C-terminal domains. The former interact with the uniform component of
coded vesicles, the clathrin lattice. In contrast, the C-terminal domain
provides a set of recognition sequences for other proteins and therefore
functions as part of a selector domain responsible for the specific
entrapment of membrane-bound proteins in vesicles.
CLONING
A 140-kb homozygous deletion in 22q12 in a sporadic meningioma directed
Peyrard et al. (1994) to the cloning and characterization of a new
member of the human beta-adaptin gene family, which was named BAM22 for
'beta-adaptin-meningioma-chromosome 22.' The BAM22 gene was totally
inactivated in the tumor with homozygous deletion. Northern blot
analysis of 70 sporadic meningiomas showed specific loss of expression
in 8 tumors, suggesting inactivation of BAM22. Based on this, Peyrard et
al. (1994) suggested that BAM22 is a second chromosome 22 locus
important in meningioma development and second in importance to the NF2
gene (607379), which is mutant in neurofibromatosis type II (101000).
The likelihood that multiple loci on chromosome 22 are involved in the
oncogenesis of meningioma is suggested by the facts that monosomy 22 is
observed in as many as 65% of tumors (Zankl and Zang, 1980); some
meningiomas have chromosome 22 deletions not encompassing the NF2 gene
region and do not show mutations in the NF2 gene; and constitutional
ring chromosome 22 has been observed in young patients with multiple
tumors (Arinami et al., 1986; Petrella et al., 1993).
GENE STRUCTURE
Peyrard et al. (1996) described the genomic structure of the human
beta-adaptin gene BAM22. The gene consists of 22 exons spanning over 100
kb. They analyzed 7 exons for sporadic mutations in 110 sporadic
meningiomas and failed to detect point mutations. Peyrard et al. (1996)
suggested that mutations in the promoter region of the gene may be
important in generating meningiomas. They also considered the
possibility that the 140-kb region involved in homozygous deletions in
meningiomas may contain another candidate tumor suppressor gene.
GENE FUNCTION
Doray et al. (2002) demonstrated that the Golgi-localized,
gamma-ear-containing adenosine diphosphate ribosylation factor-binding
proteins (GGA1, 606004 and GGA3, 606006) and the coat protein adaptor
protein-1 (AP-1) complex (see AP1G2, 603534) colocalize in
clathrin-coated buds of the trans-Golgi networks of mouse L cells and
human HeLa cells. Binding studies revealed a direct interaction between
the hinge domains of the GGAs and the gamma-ear domain of AP-1. Further,
AP-1 contained bound casein kinase-2 (see CSNK2A1, 115440) that
phosphorylated GGA1 and GGA3, thereby causing autoinhibition. Doray et
al. (2002) demonstrated that this autoinhibition could induce the
directed transfer of mannose 6-phosphate receptors (see 154540) from the
GGAs to AP-1. Mannose 6-phosphate receptors that were defective in
binding to GGAs were poorly incorporated into adaptor protein complex
containing clathrin coated vesicles. Thus, Doray et al. (2002) concluded
that GGAs and the AP-1 complex interact to package mannose 6-phosphate
receptors into AP-1-containing coated vesicles.
MAPPING
Peyrard et al. (1994) identified the BAM22 gene within chromosome 22q12.
*FIELD* RF
1. Arinami, T.; Kondo, I.; Hamaguchi, H.; Nakajima, S.: Multifocal
meningiomas in a patient with a constitutional ring chromosome 22. J.
Med. Genet. 23: 178-180, 1986.
2. Doray, B.; Ghosh, P.; Griffith, J.; Geuze, H. J.; Kornfeld, S.
: Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi
network. Science 297: 1700-1703, 2002.
3. Petrella, R.; Levine, S.; Wilmot, P. L.; Ashar, K. D.; Casamassima,
A. C.; Shapiro, L. R.: Multiple meningiomas in a patient with constitutional
ring chromosome 22. Am. J. Med. Genet. 47: 184-186, 1993.
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*FIELD* CN
Ada Hamosh - updated: 10/22/2002
Moyra Smith - updated: 12/18/1996
*FIELD* CD
Victor A. McKusick: 10/19/1994
*FIELD* ED
carol: 01/28/2003
alopez: 10/23/2002
alopez: 10/22/2002
carol: 9/19/2000
psherman: 1/5/1999
dkim: 6/26/1998
alopez: 7/30/1997
alopez: 7/8/1997
mark: 12/18/1996
jamie: 12/17/1996
mimadm: 9/23/1995
carol: 11/2/1994
terry: 10/19/1994