Full text data of AP2B1
AP2B1
(ADTB2, CLAPB1)
[Confidence: high (present in two of the MS resources)]
AP-2 complex subunit beta (AP105B; Adapter-related protein complex 2 subunit beta; Adaptor protein complex AP-2 subunit beta; Beta-2-adaptin; Beta-adaptin; Clathrin assembly protein complex 2 beta large chain; Plasma membrane adaptor HA2/AP2 adaptin beta subunit)
AP-2 complex subunit beta (AP105B; Adapter-related protein complex 2 subunit beta; Adaptor protein complex AP-2 subunit beta; Beta-2-adaptin; Beta-adaptin; Clathrin assembly protein complex 2 beta large chain; Plasma membrane adaptor HA2/AP2 adaptin beta subunit)
hRBCD
IPI00220991
IPI00220991 Splice Isoform 2 Of Adapter-related protein complex 2 beta 1 subunit Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection, The complex binds polyphosphoinositides soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic face of coated vesicles in plasma membrane. Isoform 1 or 2 found at its expected molecular weight found at molecular weight
IPI00220991 Splice Isoform 2 Of Adapter-related protein complex 2 beta 1 subunit Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection, The complex binds polyphosphoinositides soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic face of coated vesicles in plasma membrane. Isoform 1 or 2 found at its expected molecular weight found at molecular weight
Comments
Isoform P63010-2 was detected.
Isoform P63010-2 was detected.
UniProt
P63010
ID AP2B1_HUMAN Reviewed; 937 AA.
AC P63010; A6NJP3; P21851; Q7Z451; Q96J19;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=AP-2 complex subunit beta;
DE AltName: Full=AP105B;
DE AltName: Full=Adapter-related protein complex 2 subunit beta;
DE AltName: Full=Adaptor protein complex AP-2 subunit beta;
DE AltName: Full=Beta-2-adaptin;
DE AltName: Full=Beta-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 beta large chain;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin beta subunit;
GN Name=AP2B1; Synonyms=ADTB2, CLAPB1;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=1969413;
RA Ponnambalam S., Robinson M.S., Jackson A.P., Peiperl L., Parham P.;
RT "Conservation and diversity in families of coated vesicle adaptins.";
RL J. Biol. Chem. 265:4814-4820(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RC TISSUE=Testis;
RX PubMed=15897975; DOI=10.1111/j.1745-7262.2005.00025.x;
RA Zhang X.D., Yin L.L., Zheng Y., Lu L., Zhou Z.M., Sha J.H.;
RT "Expression of a novel beta adaptin subunit mRNA splice variant in
RT human testes.";
RL Asian J. Androl. 7:179-188(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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 [6]
RP INTERACTION WITH ARRB1, AND MUTAGENESIS OF GLU-849 AND GLU-902.
RX PubMed=11777907; DOI=10.1074/jbc.M108490200;
RA Laporte S.A., Miller W.E., Kim K.-M., Caron M.G.;
RT "beta-Arrestin/AP-2 interaction in G protein-coupled receptor
RT internalization: identification of a beta-arrestin binding site in
RT beta 2-adaptin.";
RL J. Biol. Chem. 277:9247-9254(2002).
RN [7]
RP INTERACTION WITH TGFBR1 AND TGFBR2.
RX PubMed=12429842; DOI=10.1091/mbc.02-07-0104;
RA Yao D., Ehrlich M., Henis Y.I., Leof E.B.;
RT "Transforming growth factor-beta receptors interact with AP2 by direct
RT binding to beta2 subunit.";
RL Mol. Biol. Cell 13:4001-4012(2002).
RN [8]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14745134; DOI=10.1247/csf.28.419;
RA Nakatsu F., Ohno H.;
RT "Adaptor protein complexes as the key regulators of protein sorting in
RT the post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=14530274; DOI=10.1074/jbc.C300390200;
RA Rappoport J.Z., Taha B.W., Lemeer S., Benmerah A., Simon S.M.;
RT "The AP-2 complex is excluded from the dynamic population of plasma
RT membrane-associated clathrin.";
RL J. Biol. Chem. 278:47357-47360(2003).
RN [10]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA Owen D.J., Collins B.M., Evans P.R.;
RT "Adaptors for clathrin coats: structure and function.";
RL Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN [11]
RP FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14985334; DOI=10.1074/jbc.C400046200;
RA Huang F., Khvorova A., Marshall W., Sorkin A.;
RT "Analysis of clathrin-mediated endocytosis of epidermal growth factor
RT receptor by RNA interference.";
RL J. Biol. Chem. 279:16657-16661(2004).
RN [12]
RP INTERACTION WITH LDLRAP1, AND MUTAGENESIS OF TRP-841 AND TYR-888.
RX PubMed=15728179; DOI=10.1074/jbc.M501029200;
RA Mishra S.K., Keyel P.A., Edeling M.A., Dupin A.L., Owen D.J.,
RA Traub L.M.;
RT "Functional dissection of an AP-2 beta2 appendage-binding sequence
RT within the autosomal recessive hypercholesterolemia protein.";
RL J. Biol. Chem. 280:19270-19280(2005).
RN [13]
RP INTERACTION WITH SLC2A8.
RX PubMed=16723738; DOI=10.1242/jcs.02943;
RA Schmidt U., Briese S., Leicht K., Schuermann A., Joost H.-G.,
RA Al-Hasani H.;
RT "Endocytosis of the glucose transporter GLUT8 is mediated by
RT interaction of a dileucine motif with the beta2-adaptin subunit of the
RT AP-2 adaptor complex.";
RL J. Cell Sci. 119:2321-2331(2006).
RN [14]
RP INTERACTION WITH ARF6.
RX PubMed=17719203; DOI=10.1016/j.cellsig.2007.07.015;
RA Poupart M.-E., Fessart D., Cotton M., Laporte S.A., Claing A.;
RT "ARF6 regulates angiotensin II type 1 receptor endocytosis by
RT controlling the recruitment of AP-2 and clathrin.";
RL Cell. Signal. 19:2370-2378(2007).
RN [15]
RP PHOSPHORYLATION AT TYR-737, AND INTERACTION WITH ARRB1.
RX PubMed=17456551; DOI=10.1242/jcs.03444;
RA Fessart D., Simaan M., Zimmerman B., Comeau J., Hamdan F.F.,
RA Wiseman P.W., Bouvier M., Laporte S.A.;
RT "Src-dependent phosphorylation of beta2-adaptin dissociates the beta-
RT arrestin-AP-2 complex.";
RL J. Cell Sci. 120:1723-1732(2007).
RN [16]
RP FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
RX PubMed=19033387; DOI=10.1242/jcs.033522;
RA Lau A.W., Chou M.M.;
RT "The adaptor complex AP-2 regulates post-endocytic trafficking through
RT the non-clathrin Arf6-dependent endocytic pathway.";
RL J. Cell Sci. 121:4008-4017(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP PHOSPHORYLATION AT TYR-737.
RX PubMed=18938240; DOI=10.1016/j.cellsig.2008.09.013;
RA Zimmerman B., Simaan M., Lee M.-H., Luttrell L.M., Laporte S.A.;
RT "c-Src-mediated phosphorylation of AP-2 reveals a general mechanism
RT for receptors internalizing through the clathrin pathway.";
RL Cell. Signal. 21:103-110(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265, 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 [20]
RP INTERACTION WITH DENND1B, AND MUTAGENESIS OF TRP-841; GLU-849; TYR-888
RP AND GLU-902.
RX PubMed=20154091; DOI=10.1074/jbc.M109.050930;
RA Marat A.L., McPherson P.S.;
RT "The connecdenn family, Rab35 guanine nucleotide exchange factors
RT interfacing with the clathrin machinery.";
RL J. Biol. Chem. 285:10627-10637(2010).
RN [21]
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).
RN [22]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 701-937, MUTAGENESIS OF
RP ARG-879; TYR-888 AND LYS-917, AND INTERACTION WITH EPN1; EPS15; SNAP91
RP AND CLTC.
RX PubMed=10944104; DOI=10.1093/emboj/19.16.4216;
RA Owen D.J., Vallis Y., Pearse B.M.F., McMahon H.T., Evans P.R.;
RT "The structure and function of the beta 2-adaptin appendage domain.";
RL EMBO J. 19:4216-4227(2000).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-591 IN COMPLEX WITH AP2A2;
RP AP2M1; AP2S1 AND AN INOSITOL POLYPHOSPHATE HEADGROUP.
RX PubMed=12086608; DOI=10.1016/S0092-8674(02)00735-3;
RA Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.;
RT "Molecular architecture and functional model of the endocytic AP2
RT complex.";
RL Cell 109:523-535(2002).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 701-937 IN COMPLEX WITH
RP LDLRAP1, INTERACTION WITH ARRB1; EPN1; SNAP91; AMPH AND BIN1, AND
RP MUTAGENESIS OF TYR-815; TRP-841; GLU-849; TYR-888 AND GLU-902.
RX PubMed=16516836; DOI=10.1016/j.devcel.2006.01.016;
RA Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M.,
RA Roth R., Heuser J.E., Owen D.J., Traub L.M.;
RT "Molecular switches involving the AP-2 beta2 appendage regulate
RT endocytic cargo selection and clathrin coat assembly.";
RL Dev. Cell 10:329-342(2006).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 700-937 IN COMPLEX WITH
RP EPS15, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 700-937 IN COMPLEX
RP WITH ARRB1, INTERACTION WITH SCYL1; SCYL2; EPS15; AMPH; SNAP91; ARRB1
RP AND LDLRAP1, AND MUTAGENESIS OF TYR-815; TRP-841; LYS-842; GLN-851;
RP ARG-879 AND TYR-888.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for
RT clathrin-coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-591 IN COMPLEX WITH AP2A2;
RP AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL.
RX PubMed=18978775; DOI=10.1038/nature07422;
RA Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R.,
RA Hoening S., Owen D.J.;
RT "A structural explanation for the binding of endocytic dileucine
RT motifs by the AP2 complex.";
RL Nature 456:976-979(2008).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
CC Adaptor protein complexes function in protein transport via
CC transport vesicles in different membrane traffic pathways. Adaptor
CC protein complexes are vesicle coat components and appear to be
CC involved in cargo selection and vesicle formation. AP-2 is
CC involved in clathrin-dependent endocytosis in which cargo proteins
CC are incorporated into vesicles surrounded by clathrin (clathrin-
CC coated vesicles, CCVs) which are destined for fusion with the
CC early endosome. The clathrin lattice serves as a mechanical
CC scaffold but is itself unable to bind directly to membrane
CC components. Clathrin-associated adaptor protein (AP) complexes
CC which can bind directly to both the clathrin lattice and to the
CC lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane
CC proteins involved in receptor-mediated endocytosis. AP-2 seems to
CC play a role in the recycling of synaptic vesicle membranes from
CC the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
CC and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
CC cytosolic tails of transmembrane cargo molecules. AP-2 may also
CC play a role in maintaining normal post-endocytic trafficking
CC through the ARF6-regulated, non-clathrin pathway. The AP-2 beta
CC subunit acts via its C-terminal appendage domain as a scaffolding
CC platform for endocytic accessory proteins; at least some clathrin-
CC associated sorting proteins (CLASPs) are recognized by their [DE]-
CC X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to
CC clathrin heavy chain, promoting clathrin lattice assembly;
CC clathrin displaces at least some CLASPs from AP2B1 which probably
CC then can be positioned for further coat assembly.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
CC composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
CC and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
CC AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts
CC with EPN1. Interacts with EPS15; clathrin competes with EPS15.
CC Interacts with SNAP91; clathrin competes with SNAP91. Interacts
CC with CLTC; clathrin competes with EPS15, SNAP91 and PIP5K1C.
CC Interacts with LDLRAP1. Interacts with AMPH and BIN1. Interacts
CC with ARF6 (GDP-bound). Interacts (dephosphorylated at Tyr-737)
CC with ARRB1; phosphorylation of AP2B1 at Tyr-737 disrupts the
CC interaction. Interacts with SLC2A8. Interacts with SCYL1 and
CC SCYL2. Interacts with TGFBR1 and TGFBR2. Interacts with PIP5K1C;
CC clathrin competes with PIP5K1C (By similarity). Interacts with
CC DENND1B, but not with DENND1A, nor DENND1C. Interacts with FCHO1.
CC -!- INTERACTION:
CC P84092:Ap2m1 (xeno); NbExp=2; IntAct=EBI-432924, EBI-297693;
CC Q16626:MEA1; NbExp=2; IntAct=EBI-432924, EBI-744921;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit;
CC Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears
CC to be excluded from internalizing CCVs and to disengage from sites
CC of endocytosis seconds before internalization of the nascent CCV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P63010-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P63010-2; Sequence=VSP_011490;
CC Name=3; Synonyms=Ap2beta-NY;
CC IsoId=P63010-3; Sequence=VSP_047805;
CC Note=Highly expressed in the testis, spleen, thymus, prostate,
CC ovary, blood leukocyte and brain, but not in the heart,
CC placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC Testis expression is restricted to germ cells and is about
CC 3-fold higher in adults than in embryos;
CC -!- PTM: Phosphorylation at Tyr-737 by SRC occurs at the plasma
CC membrane in clathrin-coated vesicles (CCVs).
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
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DR EMBL; M34175; AAA35583.1; -; mRNA.
DR EMBL; AY341427; AAQ20044.1; -; mRNA.
DR EMBL; AC004134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80133.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80139.1; -; Genomic_DNA.
DR EMBL; BC006201; AAH06201.1; -; mRNA.
DR PIR; A35553; A35553.
DR RefSeq; NP_001025177.1; NM_001030006.1.
DR RefSeq; NP_001273.1; NM_001282.2.
DR RefSeq; XP_005257994.1; XM_005257937.1.
DR RefSeq; XP_005257995.1; XM_005257938.1.
DR RefSeq; XP_005257997.1; XM_005257940.1.
DR UniGene; Hs.514819; -.
DR PDB; 1E42; X-ray; 1.70 A; A/B=701-937.
DR PDB; 2G30; X-ray; 1.60 A; A=701-937.
DR PDB; 2IV8; X-ray; 2.80 A; A=700-937.
DR PDB; 2IV9; X-ray; 1.90 A; A/B=700-937.
DR PDB; 2JKR; X-ray; 2.98 A; B/E=1-591.
DR PDB; 2JKT; X-ray; 3.40 A; B/E=1-591.
DR PDB; 2VGL; X-ray; 2.59 A; B=1-591.
DR PDB; 2XA7; X-ray; 3.10 A; B=1-592.
DR PDBsum; 1E42; -.
DR PDBsum; 2G30; -.
DR PDBsum; 2IV8; -.
DR PDBsum; 2IV9; -.
DR PDBsum; 2JKR; -.
DR PDBsum; 2JKT; -.
DR PDBsum; 2VGL; -.
DR PDBsum; 2XA7; -.
DR ProteinModelPortal; P63010; -.
DR SMR; P63010; 4-582, 705-937.
DR DIP; DIP-33098N; -.
DR IntAct; P63010; 38.
DR MINT; MINT-256705; -.
DR STRING; 9606.ENSP00000314414; -.
DR PhosphoSite; P63010; -.
DR DMDM; 51702211; -.
DR PaxDb; P63010; -.
DR PRIDE; P63010; -.
DR DNASU; 163; -.
DR Ensembl; ENST00000262325; ENSP00000262325; ENSG00000006125.
DR Ensembl; ENST00000312678; ENSP00000314414; ENSG00000006125.
DR Ensembl; ENST00000537622; ENSP00000437413; ENSG00000006125.
DR Ensembl; ENST00000538556; ENSP00000440563; ENSG00000006125.
DR Ensembl; ENST00000589344; ENSP00000467883; ENSG00000006125.
DR Ensembl; ENST00000603960; ENSP00000474789; ENSG00000270478.
DR Ensembl; ENST00000604032; ENSP00000474511; ENSG00000270478.
DR Ensembl; ENST00000604035; ENSP00000474943; ENSG00000270478.
DR Ensembl; ENST00000604623; ENSP00000474435; ENSG00000270478.
DR Ensembl; ENST00000605645; ENSP00000474277; ENSG00000270478.
DR GeneID; 163; -.
DR KEGG; hsa:163; -.
DR UCSC; uc002hjr.3; human.
DR CTD; 163; -.
DR GeneCards; GC17P033914; -.
DR HGNC; HGNC:563; AP2B1.
DR HPA; CAB017631; -.
DR MIM; 601025; gene.
DR neXtProt; NX_P63010; -.
DR PharmGKB; PA24854; -.
DR eggNOG; COG5096; -.
DR HOGENOM; HOG000163270; -.
DR HOVERGEN; HBG050515; -.
DR KO; K11825; -.
DR OMA; YMDMTFT; -.
DR OrthoDB; EOG7BGHK0; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P63010; -.
DR ChiTaRS; AP2B1; human.
DR EvolutionaryTrace; P63010; -.
DR GeneWiki; AP2B1; -.
DR GenomeRNAi; 163; -.
DR NextBio; 653; -.
DR PRO; PR:P63010; -.
DR ArrayExpress; P63010; -.
DR Bgee; P63010; -.
DR CleanEx; HS_AP2B1; -.
DR Genevestigator; P63010; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR GO; GO:0007268; P:synaptic transmission; 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; Cell membrane;
KW Coated pit; Complete proteome; Endocytosis; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 937 AP-2 complex subunit beta.
FT /FTId=PRO_0000193742.
FT REGION 841 937 Interaction with ARRB1.
FT COMPBIAS 576 716 Pro-rich (stalk region).
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 265 265 N6-acetyllysine.
FT MOD_RES 737 737 Phosphotyrosine; by SRC.
FT VAR_SEQ 1 57 Missing (in isoform 3).
FT /FTId=VSP_047805.
FT VAR_SEQ 663 663 L -> LLGSDLGGGIGGSPA (in isoform 2).
FT /FTId=VSP_011490.
FT MUTAGEN 815 815 Y->A: Strongly reduces interaction with
FT SNAP91, EPS15, AMPH and BIN1 and clathrin
FT heavy chain.
FT MUTAGEN 841 841 W->A: Abolishes interaction with LDLRAP1
FT and ARRB1. Greatly reduces DENND1B-
FT binding.
FT MUTAGEN 842 842 K->E: Strongly reduces interaction with
FT ARRB1.
FT MUTAGEN 849 849 E->A: Strongly reduces interaction with
FT LDLRAP1, ARRB1 and EPN1. No effect on
FT DENND1B-binding.
FT MUTAGEN 851 851 Q->A: Strongly reduces interaction with
FT ARRB1.
FT MUTAGEN 879 879 R->A: No effect on interaction with
FT ARRB1.
FT MUTAGEN 879 879 R->E: Strongly reduces interaction with
FT EPN1. Reduces interaction with SNAP91 and
FT clathrin. No effect on EPS15 binding.
FT MUTAGEN 888 888 Y->V: Strongly reduces interaction with
FT SNAP91, EPN1 and clathrin. No effect on
FT EPS15 binding. Abolishes interaction with
FT ARRB1 and with DENND1B.
FT MUTAGEN 902 902 E->A: Strongly reduces interaction with
FT LDLRAP1 and ARRB1. No effect on DENND1B-
FT binding.
FT MUTAGEN 917 917 K->Q: Strongly reduces interaction with
FT LDLRAP1. SNAP91 and clathrin. Reduces
FT interaction with EPN1. No effect on EPS15
FT binding.
FT STRAND 11 13
FT HELIX 14 21
FT HELIX 27 42
FT HELIX 48 50
FT HELIX 51 56
FT STRAND 59 61
FT HELIX 63 79
FT HELIX 81 85
FT HELIX 88 91
FT HELIX 92 94
FT STRAND 95 99
FT HELIX 100 111
FT HELIX 116 118
FT HELIX 119 129
FT HELIX 135 150
FT HELIX 156 167
FT HELIX 174 177
FT HELIX 180 187
FT TURN 192 195
FT HELIX 200 213
FT HELIX 216 227
FT HELIX 234 244
FT HELIX 245 247
FT HELIX 254 265
FT STRAND 267 270
FT TURN 272 275
FT HELIX 277 283
FT HELIX 285 291
FT HELIX 296 312
FT TURN 316 319
FT TURN 321 324
FT HELIX 332 344
FT TURN 348 350
FT HELIX 351 361
FT HELIX 367 381
FT HELIX 385 400
FT HELIX 404 420
FT TURN 422 424
FT HELIX 425 428
FT HELIX 429 434
FT TURN 435 438
FT HELIX 442 453
FT HELIX 456 458
FT HELIX 462 469
FT TURN 470 472
FT STRAND 474 476
FT HELIX 478 492
FT STRAND 495 497
FT HELIX 500 511
FT HELIX 517 527
FT TURN 528 532
FT HELIX 536 541
FT HELIX 557 564
FT TURN 565 568
FT HELIX 571 574
FT HELIX 578 580
FT STRAND 712 715
FT HELIX 717 719
FT TURN 720 722
FT STRAND 723 732
FT STRAND 735 744
FT STRAND 746 748
FT STRAND 754 757
FT STRAND 765 768
FT STRAND 781 790
FT STRAND 802 808
FT STRAND 813 819
FT HELIX 822 825
FT HELIX 834 843
FT HELIX 846 848
FT STRAND 850 854
FT HELIX 861 870
FT STRAND 874 881
FT STRAND 884 893
FT STRAND 898 905
FT STRAND 910 920
FT HELIX 921 923
FT HELIX 924 936
SQ SEQUENCE 937 AA; 104553 MW; B472EE5B2AE176DF CRC64;
MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA
VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI
CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK
YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV
QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV
VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST
DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL
DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI GMAPGGYVAP KAVWLPAVKA
KGLEISGTFT HRQGHIYMEM NFTNKALQHM TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ
SIDVSLPLNT LGPVMKMEPL NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT
WKDIPNENEL QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN
//
ID AP2B1_HUMAN Reviewed; 937 AA.
AC P63010; A6NJP3; P21851; Q7Z451; Q96J19;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=AP-2 complex subunit beta;
DE AltName: Full=AP105B;
DE AltName: Full=Adapter-related protein complex 2 subunit beta;
DE AltName: Full=Adaptor protein complex AP-2 subunit beta;
DE AltName: Full=Beta-2-adaptin;
DE AltName: Full=Beta-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 beta large chain;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin beta subunit;
GN Name=AP2B1; Synonyms=ADTB2, CLAPB1;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=1969413;
RA Ponnambalam S., Robinson M.S., Jackson A.P., Peiperl L., Parham P.;
RT "Conservation and diversity in families of coated vesicle adaptins.";
RL J. Biol. Chem. 265:4814-4820(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RC TISSUE=Testis;
RX PubMed=15897975; DOI=10.1111/j.1745-7262.2005.00025.x;
RA Zhang X.D., Yin L.L., Zheng Y., Lu L., Zhou Z.M., Sha J.H.;
RT "Expression of a novel beta adaptin subunit mRNA splice variant in
RT human testes.";
RL Asian J. Androl. 7:179-188(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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 [6]
RP INTERACTION WITH ARRB1, AND MUTAGENESIS OF GLU-849 AND GLU-902.
RX PubMed=11777907; DOI=10.1074/jbc.M108490200;
RA Laporte S.A., Miller W.E., Kim K.-M., Caron M.G.;
RT "beta-Arrestin/AP-2 interaction in G protein-coupled receptor
RT internalization: identification of a beta-arrestin binding site in
RT beta 2-adaptin.";
RL J. Biol. Chem. 277:9247-9254(2002).
RN [7]
RP INTERACTION WITH TGFBR1 AND TGFBR2.
RX PubMed=12429842; DOI=10.1091/mbc.02-07-0104;
RA Yao D., Ehrlich M., Henis Y.I., Leof E.B.;
RT "Transforming growth factor-beta receptors interact with AP2 by direct
RT binding to beta2 subunit.";
RL Mol. Biol. Cell 13:4001-4012(2002).
RN [8]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14745134; DOI=10.1247/csf.28.419;
RA Nakatsu F., Ohno H.;
RT "Adaptor protein complexes as the key regulators of protein sorting in
RT the post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=14530274; DOI=10.1074/jbc.C300390200;
RA Rappoport J.Z., Taha B.W., Lemeer S., Benmerah A., Simon S.M.;
RT "The AP-2 complex is excluded from the dynamic population of plasma
RT membrane-associated clathrin.";
RL J. Biol. Chem. 278:47357-47360(2003).
RN [10]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA Owen D.J., Collins B.M., Evans P.R.;
RT "Adaptors for clathrin coats: structure and function.";
RL Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN [11]
RP FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14985334; DOI=10.1074/jbc.C400046200;
RA Huang F., Khvorova A., Marshall W., Sorkin A.;
RT "Analysis of clathrin-mediated endocytosis of epidermal growth factor
RT receptor by RNA interference.";
RL J. Biol. Chem. 279:16657-16661(2004).
RN [12]
RP INTERACTION WITH LDLRAP1, AND MUTAGENESIS OF TRP-841 AND TYR-888.
RX PubMed=15728179; DOI=10.1074/jbc.M501029200;
RA Mishra S.K., Keyel P.A., Edeling M.A., Dupin A.L., Owen D.J.,
RA Traub L.M.;
RT "Functional dissection of an AP-2 beta2 appendage-binding sequence
RT within the autosomal recessive hypercholesterolemia protein.";
RL J. Biol. Chem. 280:19270-19280(2005).
RN [13]
RP INTERACTION WITH SLC2A8.
RX PubMed=16723738; DOI=10.1242/jcs.02943;
RA Schmidt U., Briese S., Leicht K., Schuermann A., Joost H.-G.,
RA Al-Hasani H.;
RT "Endocytosis of the glucose transporter GLUT8 is mediated by
RT interaction of a dileucine motif with the beta2-adaptin subunit of the
RT AP-2 adaptor complex.";
RL J. Cell Sci. 119:2321-2331(2006).
RN [14]
RP INTERACTION WITH ARF6.
RX PubMed=17719203; DOI=10.1016/j.cellsig.2007.07.015;
RA Poupart M.-E., Fessart D., Cotton M., Laporte S.A., Claing A.;
RT "ARF6 regulates angiotensin II type 1 receptor endocytosis by
RT controlling the recruitment of AP-2 and clathrin.";
RL Cell. Signal. 19:2370-2378(2007).
RN [15]
RP PHOSPHORYLATION AT TYR-737, AND INTERACTION WITH ARRB1.
RX PubMed=17456551; DOI=10.1242/jcs.03444;
RA Fessart D., Simaan M., Zimmerman B., Comeau J., Hamdan F.F.,
RA Wiseman P.W., Bouvier M., Laporte S.A.;
RT "Src-dependent phosphorylation of beta2-adaptin dissociates the beta-
RT arrestin-AP-2 complex.";
RL J. Cell Sci. 120:1723-1732(2007).
RN [16]
RP FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
RX PubMed=19033387; DOI=10.1242/jcs.033522;
RA Lau A.W., Chou M.M.;
RT "The adaptor complex AP-2 regulates post-endocytic trafficking through
RT the non-clathrin Arf6-dependent endocytic pathway.";
RL J. Cell Sci. 121:4008-4017(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP PHOSPHORYLATION AT TYR-737.
RX PubMed=18938240; DOI=10.1016/j.cellsig.2008.09.013;
RA Zimmerman B., Simaan M., Lee M.-H., Luttrell L.M., Laporte S.A.;
RT "c-Src-mediated phosphorylation of AP-2 reveals a general mechanism
RT for receptors internalizing through the clathrin pathway.";
RL Cell. Signal. 21:103-110(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265, 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 [20]
RP INTERACTION WITH DENND1B, AND MUTAGENESIS OF TRP-841; GLU-849; TYR-888
RP AND GLU-902.
RX PubMed=20154091; DOI=10.1074/jbc.M109.050930;
RA Marat A.L., McPherson P.S.;
RT "The connecdenn family, Rab35 guanine nucleotide exchange factors
RT interfacing with the clathrin machinery.";
RL J. Biol. Chem. 285:10627-10637(2010).
RN [21]
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).
RN [22]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 701-937, MUTAGENESIS OF
RP ARG-879; TYR-888 AND LYS-917, AND INTERACTION WITH EPN1; EPS15; SNAP91
RP AND CLTC.
RX PubMed=10944104; DOI=10.1093/emboj/19.16.4216;
RA Owen D.J., Vallis Y., Pearse B.M.F., McMahon H.T., Evans P.R.;
RT "The structure and function of the beta 2-adaptin appendage domain.";
RL EMBO J. 19:4216-4227(2000).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-591 IN COMPLEX WITH AP2A2;
RP AP2M1; AP2S1 AND AN INOSITOL POLYPHOSPHATE HEADGROUP.
RX PubMed=12086608; DOI=10.1016/S0092-8674(02)00735-3;
RA Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.;
RT "Molecular architecture and functional model of the endocytic AP2
RT complex.";
RL Cell 109:523-535(2002).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 701-937 IN COMPLEX WITH
RP LDLRAP1, INTERACTION WITH ARRB1; EPN1; SNAP91; AMPH AND BIN1, AND
RP MUTAGENESIS OF TYR-815; TRP-841; GLU-849; TYR-888 AND GLU-902.
RX PubMed=16516836; DOI=10.1016/j.devcel.2006.01.016;
RA Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M.,
RA Roth R., Heuser J.E., Owen D.J., Traub L.M.;
RT "Molecular switches involving the AP-2 beta2 appendage regulate
RT endocytic cargo selection and clathrin coat assembly.";
RL Dev. Cell 10:329-342(2006).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 700-937 IN COMPLEX WITH
RP EPS15, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 700-937 IN COMPLEX
RP WITH ARRB1, INTERACTION WITH SCYL1; SCYL2; EPS15; AMPH; SNAP91; ARRB1
RP AND LDLRAP1, AND MUTAGENESIS OF TYR-815; TRP-841; LYS-842; GLN-851;
RP ARG-879 AND TYR-888.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for
RT clathrin-coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-591 IN COMPLEX WITH AP2A2;
RP AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL.
RX PubMed=18978775; DOI=10.1038/nature07422;
RA Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R.,
RA Hoening S., Owen D.J.;
RT "A structural explanation for the binding of endocytic dileucine
RT motifs by the AP2 complex.";
RL Nature 456:976-979(2008).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
CC Adaptor protein complexes function in protein transport via
CC transport vesicles in different membrane traffic pathways. Adaptor
CC protein complexes are vesicle coat components and appear to be
CC involved in cargo selection and vesicle formation. AP-2 is
CC involved in clathrin-dependent endocytosis in which cargo proteins
CC are incorporated into vesicles surrounded by clathrin (clathrin-
CC coated vesicles, CCVs) which are destined for fusion with the
CC early endosome. The clathrin lattice serves as a mechanical
CC scaffold but is itself unable to bind directly to membrane
CC components. Clathrin-associated adaptor protein (AP) complexes
CC which can bind directly to both the clathrin lattice and to the
CC lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane
CC proteins involved in receptor-mediated endocytosis. AP-2 seems to
CC play a role in the recycling of synaptic vesicle membranes from
CC the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
CC and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
CC cytosolic tails of transmembrane cargo molecules. AP-2 may also
CC play a role in maintaining normal post-endocytic trafficking
CC through the ARF6-regulated, non-clathrin pathway. The AP-2 beta
CC subunit acts via its C-terminal appendage domain as a scaffolding
CC platform for endocytic accessory proteins; at least some clathrin-
CC associated sorting proteins (CLASPs) are recognized by their [DE]-
CC X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to
CC clathrin heavy chain, promoting clathrin lattice assembly;
CC clathrin displaces at least some CLASPs from AP2B1 which probably
CC then can be positioned for further coat assembly.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
CC composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
CC and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
CC AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts
CC with EPN1. Interacts with EPS15; clathrin competes with EPS15.
CC Interacts with SNAP91; clathrin competes with SNAP91. Interacts
CC with CLTC; clathrin competes with EPS15, SNAP91 and PIP5K1C.
CC Interacts with LDLRAP1. Interacts with AMPH and BIN1. Interacts
CC with ARF6 (GDP-bound). Interacts (dephosphorylated at Tyr-737)
CC with ARRB1; phosphorylation of AP2B1 at Tyr-737 disrupts the
CC interaction. Interacts with SLC2A8. Interacts with SCYL1 and
CC SCYL2. Interacts with TGFBR1 and TGFBR2. Interacts with PIP5K1C;
CC clathrin competes with PIP5K1C (By similarity). Interacts with
CC DENND1B, but not with DENND1A, nor DENND1C. Interacts with FCHO1.
CC -!- INTERACTION:
CC P84092:Ap2m1 (xeno); NbExp=2; IntAct=EBI-432924, EBI-297693;
CC Q16626:MEA1; NbExp=2; IntAct=EBI-432924, EBI-744921;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit;
CC Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears
CC to be excluded from internalizing CCVs and to disengage from sites
CC of endocytosis seconds before internalization of the nascent CCV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P63010-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P63010-2; Sequence=VSP_011490;
CC Name=3; Synonyms=Ap2beta-NY;
CC IsoId=P63010-3; Sequence=VSP_047805;
CC Note=Highly expressed in the testis, spleen, thymus, prostate,
CC ovary, blood leukocyte and brain, but not in the heart,
CC placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC Testis expression is restricted to germ cells and is about
CC 3-fold higher in adults than in embryos;
CC -!- PTM: Phosphorylation at Tyr-737 by SRC occurs at the plasma
CC membrane in clathrin-coated vesicles (CCVs).
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
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DR EMBL; M34175; AAA35583.1; -; mRNA.
DR EMBL; AY341427; AAQ20044.1; -; mRNA.
DR EMBL; AC004134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80133.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80139.1; -; Genomic_DNA.
DR EMBL; BC006201; AAH06201.1; -; mRNA.
DR PIR; A35553; A35553.
DR RefSeq; NP_001025177.1; NM_001030006.1.
DR RefSeq; NP_001273.1; NM_001282.2.
DR RefSeq; XP_005257994.1; XM_005257937.1.
DR RefSeq; XP_005257995.1; XM_005257938.1.
DR RefSeq; XP_005257997.1; XM_005257940.1.
DR UniGene; Hs.514819; -.
DR PDB; 1E42; X-ray; 1.70 A; A/B=701-937.
DR PDB; 2G30; X-ray; 1.60 A; A=701-937.
DR PDB; 2IV8; X-ray; 2.80 A; A=700-937.
DR PDB; 2IV9; X-ray; 1.90 A; A/B=700-937.
DR PDB; 2JKR; X-ray; 2.98 A; B/E=1-591.
DR PDB; 2JKT; X-ray; 3.40 A; B/E=1-591.
DR PDB; 2VGL; X-ray; 2.59 A; B=1-591.
DR PDB; 2XA7; X-ray; 3.10 A; B=1-592.
DR PDBsum; 1E42; -.
DR PDBsum; 2G30; -.
DR PDBsum; 2IV8; -.
DR PDBsum; 2IV9; -.
DR PDBsum; 2JKR; -.
DR PDBsum; 2JKT; -.
DR PDBsum; 2VGL; -.
DR PDBsum; 2XA7; -.
DR ProteinModelPortal; P63010; -.
DR SMR; P63010; 4-582, 705-937.
DR DIP; DIP-33098N; -.
DR IntAct; P63010; 38.
DR MINT; MINT-256705; -.
DR STRING; 9606.ENSP00000314414; -.
DR PhosphoSite; P63010; -.
DR DMDM; 51702211; -.
DR PaxDb; P63010; -.
DR PRIDE; P63010; -.
DR DNASU; 163; -.
DR Ensembl; ENST00000262325; ENSP00000262325; ENSG00000006125.
DR Ensembl; ENST00000312678; ENSP00000314414; ENSG00000006125.
DR Ensembl; ENST00000537622; ENSP00000437413; ENSG00000006125.
DR Ensembl; ENST00000538556; ENSP00000440563; ENSG00000006125.
DR Ensembl; ENST00000589344; ENSP00000467883; ENSG00000006125.
DR Ensembl; ENST00000603960; ENSP00000474789; ENSG00000270478.
DR Ensembl; ENST00000604032; ENSP00000474511; ENSG00000270478.
DR Ensembl; ENST00000604035; ENSP00000474943; ENSG00000270478.
DR Ensembl; ENST00000604623; ENSP00000474435; ENSG00000270478.
DR Ensembl; ENST00000605645; ENSP00000474277; ENSG00000270478.
DR GeneID; 163; -.
DR KEGG; hsa:163; -.
DR UCSC; uc002hjr.3; human.
DR CTD; 163; -.
DR GeneCards; GC17P033914; -.
DR HGNC; HGNC:563; AP2B1.
DR HPA; CAB017631; -.
DR MIM; 601025; gene.
DR neXtProt; NX_P63010; -.
DR PharmGKB; PA24854; -.
DR eggNOG; COG5096; -.
DR HOGENOM; HOG000163270; -.
DR HOVERGEN; HBG050515; -.
DR KO; K11825; -.
DR OMA; YMDMTFT; -.
DR OrthoDB; EOG7BGHK0; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P63010; -.
DR ChiTaRS; AP2B1; human.
DR EvolutionaryTrace; P63010; -.
DR GeneWiki; AP2B1; -.
DR GenomeRNAi; 163; -.
DR NextBio; 653; -.
DR PRO; PR:P63010; -.
DR ArrayExpress; P63010; -.
DR Bgee; P63010; -.
DR CleanEx; HS_AP2B1; -.
DR Genevestigator; P63010; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR GO; GO:0007268; P:synaptic transmission; 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; Cell membrane;
KW Coated pit; Complete proteome; Endocytosis; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 937 AP-2 complex subunit beta.
FT /FTId=PRO_0000193742.
FT REGION 841 937 Interaction with ARRB1.
FT COMPBIAS 576 716 Pro-rich (stalk region).
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 265 265 N6-acetyllysine.
FT MOD_RES 737 737 Phosphotyrosine; by SRC.
FT VAR_SEQ 1 57 Missing (in isoform 3).
FT /FTId=VSP_047805.
FT VAR_SEQ 663 663 L -> LLGSDLGGGIGGSPA (in isoform 2).
FT /FTId=VSP_011490.
FT MUTAGEN 815 815 Y->A: Strongly reduces interaction with
FT SNAP91, EPS15, AMPH and BIN1 and clathrin
FT heavy chain.
FT MUTAGEN 841 841 W->A: Abolishes interaction with LDLRAP1
FT and ARRB1. Greatly reduces DENND1B-
FT binding.
FT MUTAGEN 842 842 K->E: Strongly reduces interaction with
FT ARRB1.
FT MUTAGEN 849 849 E->A: Strongly reduces interaction with
FT LDLRAP1, ARRB1 and EPN1. No effect on
FT DENND1B-binding.
FT MUTAGEN 851 851 Q->A: Strongly reduces interaction with
FT ARRB1.
FT MUTAGEN 879 879 R->A: No effect on interaction with
FT ARRB1.
FT MUTAGEN 879 879 R->E: Strongly reduces interaction with
FT EPN1. Reduces interaction with SNAP91 and
FT clathrin. No effect on EPS15 binding.
FT MUTAGEN 888 888 Y->V: Strongly reduces interaction with
FT SNAP91, EPN1 and clathrin. No effect on
FT EPS15 binding. Abolishes interaction with
FT ARRB1 and with DENND1B.
FT MUTAGEN 902 902 E->A: Strongly reduces interaction with
FT LDLRAP1 and ARRB1. No effect on DENND1B-
FT binding.
FT MUTAGEN 917 917 K->Q: Strongly reduces interaction with
FT LDLRAP1. SNAP91 and clathrin. Reduces
FT interaction with EPN1. No effect on EPS15
FT binding.
FT STRAND 11 13
FT HELIX 14 21
FT HELIX 27 42
FT HELIX 48 50
FT HELIX 51 56
FT STRAND 59 61
FT HELIX 63 79
FT HELIX 81 85
FT HELIX 88 91
FT HELIX 92 94
FT STRAND 95 99
FT HELIX 100 111
FT HELIX 116 118
FT HELIX 119 129
FT HELIX 135 150
FT HELIX 156 167
FT HELIX 174 177
FT HELIX 180 187
FT TURN 192 195
FT HELIX 200 213
FT HELIX 216 227
FT HELIX 234 244
FT HELIX 245 247
FT HELIX 254 265
FT STRAND 267 270
FT TURN 272 275
FT HELIX 277 283
FT HELIX 285 291
FT HELIX 296 312
FT TURN 316 319
FT TURN 321 324
FT HELIX 332 344
FT TURN 348 350
FT HELIX 351 361
FT HELIX 367 381
FT HELIX 385 400
FT HELIX 404 420
FT TURN 422 424
FT HELIX 425 428
FT HELIX 429 434
FT TURN 435 438
FT HELIX 442 453
FT HELIX 456 458
FT HELIX 462 469
FT TURN 470 472
FT STRAND 474 476
FT HELIX 478 492
FT STRAND 495 497
FT HELIX 500 511
FT HELIX 517 527
FT TURN 528 532
FT HELIX 536 541
FT HELIX 557 564
FT TURN 565 568
FT HELIX 571 574
FT HELIX 578 580
FT STRAND 712 715
FT HELIX 717 719
FT TURN 720 722
FT STRAND 723 732
FT STRAND 735 744
FT STRAND 746 748
FT STRAND 754 757
FT STRAND 765 768
FT STRAND 781 790
FT STRAND 802 808
FT STRAND 813 819
FT HELIX 822 825
FT HELIX 834 843
FT HELIX 846 848
FT STRAND 850 854
FT HELIX 861 870
FT STRAND 874 881
FT STRAND 884 893
FT STRAND 898 905
FT STRAND 910 920
FT HELIX 921 923
FT HELIX 924 936
SQ SEQUENCE 937 AA; 104553 MW; B472EE5B2AE176DF CRC64;
MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA
VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI
CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK
YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV
QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV
VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST
DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL
DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI GMAPGGYVAP KAVWLPAVKA
KGLEISGTFT HRQGHIYMEM NFTNKALQHM TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ
SIDVSLPLNT LGPVMKMEPL NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT
WKDIPNENEL QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN
//
MIM
601025
*RECORD*
*FIELD* NO
601025
*FIELD* TI
*601025 ADAPTOR-RELATED PROTEIN COMPLEX 2, BETA-1 SUBUNIT; AP2B1
;;CLATHRIN-ASSOCIATED/ASSEMBLY/ADAPTOR PROTEIN, LARGE, BETA-1; CLAPB1;;
read moreCLATHRIN ADAPTOR COMPLEX AP2, BETA SUBUNIT;;
AP2-BETA;;
ADAPTIN, BETA-2
*FIELD* TX
DESCRIPTION
The AP2B1 protein is part of the AP2 coat assembly protein complex (see
601024) and links clathrin (118960) to receptors in the coated vesicles
(summary by Ponnambalam et al., 1990).
CLONING
The beta adaptin subunit of the clathrin coat assembly complex, also
referred to as AP2-beta, was cloned from human, rat and bovine cDNA
libraries by Ponnambalam et al. (1990), who found that the predicted
937-amino acid proteins are totally conserved between species.
MAPPING
Druck et al. (1995) used a probe from the 3-prime UTR of the human cDNA
to map the gene to chromosome 17. Hybrids with portions of chromosome 17
were then used to localize CLAPB1 to 17q11.2-q12.
*FIELD* RF
1. Druck, T.; Gu, Y.; Prabhala. G.; Cannizzaro, L. A.; Park, S.-H.;
Huebner, K.; Keen, J. H.: Chromosome localization of human genes
for clathrin adaptor polypeptides AP2-beta and AP50 and the clathrin-binding
protein, VCP. Genomics 30: 94-97, 1995.
2. Ponnambalam, S.; Robinson, M. S.; Jackson, A. P.; Peiperl, L.;
Parham, P.: Conservation and diversity in families of coated vesicle
adaptins. J. Biol. Chem. 265: 4814-4820, 1990.
*FIELD* CD
Alan F. Scott: 1/30/1996
*FIELD* ED
alopez: 03/08/2012
alopez: 3/30/2010
carol: 9/19/2000
carol: 3/22/1999
psherman: 1/6/1999
psherman: 1/5/1999
mark: 7/3/1997
mark: 1/30/1996
*RECORD*
*FIELD* NO
601025
*FIELD* TI
*601025 ADAPTOR-RELATED PROTEIN COMPLEX 2, BETA-1 SUBUNIT; AP2B1
;;CLATHRIN-ASSOCIATED/ASSEMBLY/ADAPTOR PROTEIN, LARGE, BETA-1; CLAPB1;;
read moreCLATHRIN ADAPTOR COMPLEX AP2, BETA SUBUNIT;;
AP2-BETA;;
ADAPTIN, BETA-2
*FIELD* TX
DESCRIPTION
The AP2B1 protein is part of the AP2 coat assembly protein complex (see
601024) and links clathrin (118960) to receptors in the coated vesicles
(summary by Ponnambalam et al., 1990).
CLONING
The beta adaptin subunit of the clathrin coat assembly complex, also
referred to as AP2-beta, was cloned from human, rat and bovine cDNA
libraries by Ponnambalam et al. (1990), who found that the predicted
937-amino acid proteins are totally conserved between species.
MAPPING
Druck et al. (1995) used a probe from the 3-prime UTR of the human cDNA
to map the gene to chromosome 17. Hybrids with portions of chromosome 17
were then used to localize CLAPB1 to 17q11.2-q12.
*FIELD* RF
1. Druck, T.; Gu, Y.; Prabhala. G.; Cannizzaro, L. A.; Park, S.-H.;
Huebner, K.; Keen, J. H.: Chromosome localization of human genes
for clathrin adaptor polypeptides AP2-beta and AP50 and the clathrin-binding
protein, VCP. Genomics 30: 94-97, 1995.
2. Ponnambalam, S.; Robinson, M. S.; Jackson, A. P.; Peiperl, L.;
Parham, P.: Conservation and diversity in families of coated vesicle
adaptins. J. Biol. Chem. 265: 4814-4820, 1990.
*FIELD* CD
Alan F. Scott: 1/30/1996
*FIELD* ED
alopez: 03/08/2012
alopez: 3/30/2010
carol: 9/19/2000
carol: 3/22/1999
psherman: 1/6/1999
psherman: 1/5/1999
mark: 7/3/1997
mark: 1/30/1996