AP2B1_HUMAN
ID AP2B1_HUMAN Reviewed; 937 AA.
AC P63010; A6NJP3; P21851; Q7Z451; Q96J19;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=AP-2 complex subunit beta;
DE AltName: Full=AP105B;
DE AltName: Full=Adaptor protein complex AP-2 subunit beta;
DE AltName: Full=Adaptor-related protein complex 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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=1969413; DOI=10.1016/s0021-9258(19)34045-1;
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 human
RT 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., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., 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 the
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 beta 2-
RT 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 the
RT 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., Traub L.M.;
RT "Functional dissection of an AP-2 beta2 appendage-binding sequence within
RT 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., Al-Hasani H.;
RT "Endocytosis of the glucose transporter GLUT8 is mediated by interaction of
RT a dileucine motif with the beta2-adaptin subunit of the AP-2 adaptor
RT 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 controlling
RT 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., Wiseman P.W.,
RA 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 the
RT 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 the
RT 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 for
RT receptors internalizing through the clathrin pathway.";
RL Cell. Signal. 21:103-110(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP INTERACTION WITH DENND1B, AND MUTAGENESIS OF TRP-841; GLU-849; TYR-888 AND
RP 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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [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, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP FUNCTION, INTERACTION WITH ADAM10, AND TISSUE SPECIFICITY.
RX PubMed=23676497; DOI=10.1172/jci65401;
RA Marcello E., Saraceno C., Musardo S., Vara H., de la Fuente A.G.,
RA Pelucchi S., Di Marino D., Borroni B., Tramontano A., Perez-Otano I.,
RA Padovani A., Giustetto M., Gardoni F., Di Luca M.;
RT "Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's
RT disease.";
RL J. Clin. Invest. 123:2523-2538(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [28]
RP INTERACTION WITH RFTN1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27022195; DOI=10.4049/jimmunol.1501734;
RA Tatematsu M., Yoshida R., Morioka Y., Ishii N., Funami K., Watanabe A.,
RA Saeki K., Seya T., Matsumoto M.;
RT "Raftlin controls lipopolysaccharide-induced TLR4 internalization and
RT TICAM-1 signaling in a cell type-specific manner.";
RL J. Immunol. 196:3865-3876(2016).
RN [29]
RP INTERACTION WITH KIAA1107.
RX PubMed=29262337; DOI=10.1016/j.celrep.2017.11.073;
RA Piccini A., Castroflorio E., Valente P., Guarnieri F.C., Aprile D.,
RA Michetti C., Bramini M., Giansante G., Pinto B., Savardi A., Cesca F.,
RA Bachi A., Cattaneo A., Wren J.D., Fassio A., Valtorta F., Benfenati F.,
RA Giovedi S.;
RT "APache is an AP2-interacting protein involved in synaptic vesicle
RT trafficking and neuronal development.";
RL Cell Rep. 21:3596-3611(2017).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 701-937, MUTAGENESIS OF ARG-879;
RP TYR-888 AND LYS-917, AND INTERACTION WITH EPN1; EPS15; SNAP91 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 [31]
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 [32]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 701-937 IN COMPLEX WITH LDLRAP1,
RP INTERACTION WITH ARRB1; EPN1; SNAP91; AMPH AND BIN1, AND MUTAGENESIS OF
RP 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 endocytic
RT cargo selection and clathrin coat assembly.";
RL Dev. Cell 10:329-342(2006).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 700-937 IN COMPLEX WITH EPS15,
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 700-937 IN COMPLEX WITH ARRB1,
RP INTERACTION WITH SCYL1; SCYL2; EPS15; AMPH; SNAP91; ARRB1 AND LDLRAP1, AND
RP MUTAGENESIS OF TYR-815; TRP-841; LYS-842; GLN-851; 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 clathrin-
RT coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-591 IN COMPLEX WITH AP2A2;
RP AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL.
RX PubMed=19140243; DOI=10.1038/nature07422;
RA Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R., Hoening S.,
RA Owen D.J.;
RT "A structural explanation for the binding of endocytic dileucine motifs by
RT the AP2 complex.";
RL Nature 456:976-979(2008).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor
CC protein complexes function in protein transport via transport vesicles
CC in different membrane traffic pathways. Adaptor protein complexes are
CC vesicle coat components and appear to be involved in cargo selection
CC and vesicle formation. AP-2 is involved in clathrin-dependent
CC endocytosis in which cargo proteins are incorporated into vesicles
CC surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC destined for fusion with the early endosome. The clathrin lattice
CC serves as a mechanical scaffold but is itself unable to bind directly
CC to membrane components. Clathrin-associated adaptor protein (AP)
CC complexes which can bind directly to both the clathrin lattice and to
CC the 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 proteins
CC involved in receptor-mediated endocytosis. AP-2 seems to play a role in
CC the recycling of synaptic vesicle membranes from the presynaptic
CC surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-
CC [LI] endocytosis signal motifs within the cytosolic tails of
CC transmembrane cargo molecules. AP-2 may also play a role in maintaining
CC normal post-endocytic trafficking through the ARF6-regulated, non-
CC clathrin pathway. During long-term potentiation in hippocampal neurons,
CC AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497).
CC The AP-2 beta subunit acts via its C-terminal appendage domain as a
CC scaffolding platform for endocytic accessory proteins; at least some
CC clathrin-associated sorting proteins (CLASPs) are recognized by their
CC [DE]-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; clathrin
CC displaces at least some CLASPs from AP2B1 which probably then can be
CC positioned for further coat assembly. {ECO:0000269|PubMed:14745134,
CC ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838,
CC ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23676497}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type
CC subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small
CC adaptin (sigma-type subunit AP2S1) (PubMed:12086608, PubMed:19140243).
CC Interacts with EPN1 (PubMed:10944104, PubMed:16516836). Interacts with
CC EPS15; clathrin competes with EPS15 (PubMed:10944104, PubMed:16903783).
CC Interacts with SNAP91; clathrin competes with SNAP91 (PubMed:10944104,
CC PubMed:16516836, PubMed:16903783). Interacts with CLTC; clathrin
CC competes with EPS15, SNAP91 and PIP5K1C (PubMed:10944104). Interacts
CC with LDLRAP1 (PubMed:15728179, PubMed:16516836, PubMed:16903783).
CC Interacts with AMPH and BIN1 (PubMed:16516836, PubMed:16903783).
CC Interacts with ARF6 (GDP-bound) (PubMed:17719203). Interacts
CC (dephosphorylated at Tyr-737) with ARRB1; phosphorylation of AP2B1 at
CC Tyr-737 disrupts the interaction (PubMed:11777907, PubMed:17456551,
CC PubMed:16516836, PubMed:16903783). Interacts with SLC2A8
CC (PubMed:16723738). Interacts with SCYL1 and SCYL2 (PubMed:16903783).
CC Interacts with TGFBR1 and TGFBR2 (PubMed:12429842). Interacts with
CC PIP5K1C; clathrin competes with PIP5K1C (By similarity). Interacts with
CC DENND1B, but not with DENND1A, nor DENND1C (PubMed:20154091). Interacts
CC with FCHO1 (PubMed:22484487). Interacts with RFTN1 (PubMed:27022195).
CC Interacts with KIAA1107 (PubMed:29262337). Together with AP2A1 or AP2A2
CC and AP2M1, it interacts with ADAM10; this interaction facilitates
CC ADAM10 endocytosis from the plasma membrane during long-term
CC potentiation in hippocampal neurons (PubMed:23676497).
CC {ECO:0000250|UniProtKB:P62944, ECO:0000269|PubMed:10944104,
CC ECO:0000269|PubMed:11777907, ECO:0000269|PubMed:12086608,
CC ECO:0000269|PubMed:12429842, ECO:0000269|PubMed:15728179,
CC ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:16723738,
CC ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:17456551,
CC ECO:0000269|PubMed:17719203, ECO:0000269|PubMed:19140243,
CC ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:22484487,
CC ECO:0000269|PubMed:23676497, ECO:0000269|PubMed:27022195,
CC ECO:0000269|PubMed:29262337}.
CC -!- INTERACTION:
CC P63010; Q9UHB7: AFF4; NbExp=3; IntAct=EBI-432924, EBI-395282;
CC P63010; Q9UHB7-2: AFF4; NbExp=3; IntAct=EBI-432924, EBI-10261324;
CC P63010; Q6ULP2: AFTPH; NbExp=2; IntAct=EBI-432924, EBI-2848714;
CC P63010; P52594: AGFG1; NbExp=2; IntAct=EBI-432924, EBI-996560;
CC P63010; Q9Y6Q5: AP1M2; NbExp=4; IntAct=EBI-432924, EBI-752250;
CC P63010; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-432924, EBI-297683;
CC P63010; Q14677: CLINT1; NbExp=2; IntAct=EBI-432924, EBI-1171113;
CC P63010; P42566: EPS15; NbExp=2; IntAct=EBI-432924, EBI-396684;
CC P63010; Q15811: ITSN1; NbExp=3; IntAct=EBI-432924, EBI-602041;
CC P63010; P52292: KPNA2; NbExp=3; IntAct=EBI-432924, EBI-349938;
CC P63010; Q5SW96: LDLRAP1; NbExp=5; IntAct=EBI-432924, EBI-747813;
CC P63010; Q9UJ55: MAGEL2; NbExp=2; IntAct=EBI-432924, EBI-5668174;
CC P63010; Q16626: MEA1; NbExp=2; IntAct=EBI-432924, EBI-744921;
CC P63010; Q8WWR8-2: NEU4; NbExp=3; IntAct=EBI-432924, EBI-10277551;
CC P63010; P50542: PEX5; NbExp=2; IntAct=EBI-432924, EBI-597835;
CC P63010; Q96KG9: SCYL1; NbExp=2; IntAct=EBI-432924, EBI-949287;
CC P63010; P12236: SLC25A6; NbExp=4; IntAct=EBI-432924, EBI-356254;
CC P63010; A8MWV9: SMIM34; NbExp=2; IntAct=EBI-432924, EBI-30815092;
CC P63010; Q9NVV9: THAP1; NbExp=4; IntAct=EBI-432924, EBI-741515;
CC P63010; O95153: TSPOAP1; NbExp=2; IntAct=EBI-432924, EBI-5915931;
CC P63010; Q99757: TXN2; NbExp=3; IntAct=EBI-432924, EBI-2932492;
CC P63010; Q01081: U2AF1; NbExp=3; IntAct=EBI-432924, EBI-632461;
CC P63010; Q8N4L5: XRCC6BP1; NbExp=3; IntAct=EBI-432924, EBI-10265517;
CC P63010; P84092: Ap2m1; Xeno; NbExp=4; IntAct=EBI-432924, EBI-297693;
CC P63010; Q9CR95: Necap1; Xeno; NbExp=2; IntAct=EBI-432924, EBI-7592476;
CC P63010; Q64729: Tgfbr1; Xeno; NbExp=3; IntAct=EBI-432924, EBI-2899393;
CC P63010-2; P01023: A2M; NbExp=3; IntAct=EBI-11529439, EBI-640741;
CC P63010-2; Q92870-2: APBB2; NbExp=3; IntAct=EBI-11529439, EBI-21535880;
CC P63010-2; P05067: APP; NbExp=3; IntAct=EBI-11529439, EBI-77613;
CC P63010-2; P05067-2: APP; NbExp=3; IntAct=EBI-11529439, EBI-17264467;
CC P63010-2; P49407: ARRB1; NbExp=3; IntAct=EBI-11529439, EBI-743313;
CC P63010-2; P54253: ATXN1; NbExp=6; IntAct=EBI-11529439, EBI-930964;
CC P63010-2; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-11529439, EBI-702390;
CC P63010-2; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-11529439, EBI-739879;
CC P63010-2; P02461-2: COL3A1; NbExp=3; IntAct=EBI-11529439, EBI-12214501;
CC P63010-2; P09172: DBH; NbExp=3; IntAct=EBI-11529439, EBI-8589586;
CC P63010-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-11529439, EBI-25840379;
CC P63010-2; P14136: GFAP; NbExp=3; IntAct=EBI-11529439, EBI-744302;
CC P63010-2; O95872: GPANK1; NbExp=3; IntAct=EBI-11529439, EBI-751540;
CC P63010-2; P78347-2: GTF2I; NbExp=4; IntAct=EBI-11529439, EBI-12033200;
CC P63010-2; P42858: HTT; NbExp=18; IntAct=EBI-11529439, EBI-466029;
CC P63010-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-11529439, EBI-1055254;
CC P63010-2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-11529439, EBI-2556193;
CC P63010-2; Q5SW96: LDLRAP1; NbExp=5; IntAct=EBI-11529439, EBI-747813;
CC P63010-2; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-11529439, EBI-2341787;
CC P63010-2; P51608: MECP2; NbExp=3; IntAct=EBI-11529439, EBI-1189067;
CC P63010-2; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-11529439, EBI-14086479;
CC P63010-2; P40692: MLH1; NbExp=8; IntAct=EBI-11529439, EBI-744248;
CC P63010-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-11529439, EBI-713665;
CC P63010-2; Q8WWR8-2: NEU4; NbExp=3; IntAct=EBI-11529439, EBI-10277551;
CC P63010-2; P29474: NOS3; NbExp=3; IntAct=EBI-11529439, EBI-1391623;
CC P63010-2; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-11529439, EBI-741048;
CC P63010-2; Q99497: PARK7; NbExp=3; IntAct=EBI-11529439, EBI-1164361;
CC P63010-2; Q7Z412: PEX26; NbExp=3; IntAct=EBI-11529439, EBI-752057;
CC P63010-2; Q9BXM7: PINK1; NbExp=3; IntAct=EBI-11529439, EBI-2846068;
CC P63010-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-11529439, EBI-25882629;
CC P63010-2; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-11529439, EBI-11956563;
CC P63010-2; O60260-5: PRKN; NbExp=6; IntAct=EBI-11529439, EBI-21251460;
CC P63010-2; P49768-2: PSEN1; NbExp=6; IntAct=EBI-11529439, EBI-11047108;
CC P63010-2; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-11529439, EBI-11974061;
CC P63010-2; P37840: SNCA; NbExp=3; IntAct=EBI-11529439, EBI-985879;
CC P63010-2; P00441: SOD1; NbExp=3; IntAct=EBI-11529439, EBI-990792;
CC P63010-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-11529439, EBI-372899;
CC P63010-2; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-11529439, EBI-12090309;
CC P63010-2; O14656-2: TOR1A; NbExp=3; IntAct=EBI-11529439, EBI-25847109;
CC P63010-2; Q99757: TXN2; NbExp=3; IntAct=EBI-11529439, EBI-2932492;
CC P63010-2; Q01081: U2AF1; NbExp=3; IntAct=EBI-11529439, EBI-632461;
CC P63010-2; P09936: UCHL1; NbExp=3; IntAct=EBI-11529439, EBI-714860;
CC P63010-2; O95292: VAPB; NbExp=3; IntAct=EBI-11529439, EBI-1188298;
CC P63010-2; Q6ZN96; NbExp=3; IntAct=EBI-11529439, EBI-10255097;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14530274}.
CC Membrane, coated pit {ECO:0000269|PubMed:14530274}; Peripheral membrane
CC protein {ECO:0000269|PubMed:14530274}; Cytoplasmic side
CC {ECO:0000269|PubMed:14530274}. Note=AP-2 appears to be excluded from
CC internalizing CCVs and to disengage from sites of endocytosis seconds
CC 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 -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:23676497}.
CC -!- PTM: Phosphorylation at Tyr-737 by SRC occurs at the plasma membrane in
CC clathrin-coated vesicles (CCVs). {ECO:0000269|PubMed:17456551,
CC ECO:0000269|PubMed:18938240}.
CC -!- MISCELLANEOUS: [Isoform 3]: Highly expressed in the testis, spleen,
CC thymus, prostate, ovary, blood leukocyte and brain, but not in the
CC heart, placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC Testis expression is restricted to germ cells and is about 3-fold
CC higher in adults than in embryos. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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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 CCDS; CCDS32621.1; -. [P63010-2]
DR CCDS; CCDS32622.1; -. [P63010-1]
DR PIR; A35553; A35553.
DR RefSeq; NP_001025177.1; NM_001030006.1. [P63010-2]
DR RefSeq; NP_001273.1; NM_001282.2. [P63010-1]
DR RefSeq; XP_005257994.1; XM_005257937.3. [P63010-2]
DR RefSeq; XP_005257995.1; XM_005257938.2. [P63010-2]
DR RefSeq; XP_011522757.1; XM_011524455.2. [P63010-3]
DR RefSeq; XP_016879773.1; XM_017024284.1. [P63010-1]
DR RefSeq; XP_016879775.1; XM_017024286.1. [P63010-3]
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 PDB; 4UQI; X-ray; 2.79 A; B=1-651.
DR PDB; 5M5R; X-ray; 1.76 A; C/D=628-637.
DR PDB; 6QH5; X-ray; 2.56 A; B=1-592.
DR PDB; 6QH6; X-ray; 5.00 A; B=1-592.
DR PDB; 6QH7; X-ray; 3.40 A; B=1-592.
DR PDB; 6URI; X-ray; 3.00 A; B=1-591.
DR PDB; 6YAE; EM; 3.90 A; B=1-591.
DR PDB; 6YAF; EM; 9.10 A; B=1-937.
DR PDB; 6YAH; EM; 10.20 A; B=1-937.
DR PDB; 6YAI; EM; 9.20 A; F=705-937.
DR PDB; 7OM8; EM; 10.50 A; B=705-937.
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 PDBsum; 4UQI; -.
DR PDBsum; 5M5R; -.
DR PDBsum; 6QH5; -.
DR PDBsum; 6QH6; -.
DR PDBsum; 6QH7; -.
DR PDBsum; 6URI; -.
DR PDBsum; 6YAE; -.
DR PDBsum; 6YAF; -.
DR PDBsum; 6YAH; -.
DR PDBsum; 6YAI; -.
DR PDBsum; 7OM8; -.
DR AlphaFoldDB; P63010; -.
DR SMR; P63010; -.
DR BioGRID; 106672; 320.
DR ComplexPortal; CPX-5149; AP-2 Adaptor complex, alpha1 variant.
DR ComplexPortal; CPX-5150; AP-2 Adaptor complex, alpha2 variant.
DR CORUM; P63010; -.
DR DIP; DIP-33098N; -.
DR IntAct; P63010; 318.
DR MINT; P63010; -.
DR STRING; 9606.ENSP00000482835; -.
DR TCDB; 9.B.278.1.4; the organellar-targeting adaptor protein complex (o-apc) family.
DR GlyGen; P63010; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P63010; -.
DR MetOSite; P63010; -.
DR PhosphoSitePlus; P63010; -.
DR SwissPalm; P63010; -.
DR BioMuta; AP2B1; -.
DR DMDM; 51702211; -.
DR EPD; P63010; -.
DR jPOST; P63010; -.
DR MassIVE; P63010; -.
DR MaxQB; P63010; -.
DR PaxDb; P63010; -.
DR PeptideAtlas; P63010; -.
DR PRIDE; P63010; -.
DR ProteomicsDB; 57469; -. [P63010-1]
DR ProteomicsDB; 57470; -. [P63010-2]
DR ProteomicsDB; 69151; -.
DR Antibodypedia; 4320; 267 antibodies from 30 providers.
DR DNASU; 163; -.
DR Ensembl; ENST00000610402.5; ENSP00000483185.1; ENSG00000006125.18. [P63010-2]
DR Ensembl; ENST00000618940.4; ENSP00000482835.1; ENSG00000006125.18. [P63010-2]
DR Ensembl; ENST00000621914.4; ENSP00000482315.1; ENSG00000006125.18. [P63010-1]
DR GeneID; 163; -.
DR KEGG; hsa:163; -.
DR MANE-Select; ENST00000610402.5; ENSP00000483185.1; NM_001030006.2; NP_001025177.1. [P63010-2]
DR UCSC; uc002hjq.4; human. [P63010-1]
DR CTD; 163; -.
DR DisGeNET; 163; -.
DR GeneCards; AP2B1; -.
DR HGNC; HGNC:563; AP2B1.
DR HPA; ENSG00000006125; Low tissue specificity.
DR MIM; 601025; gene.
DR neXtProt; NX_P63010; -.
DR OpenTargets; ENSG00000006125; -.
DR PharmGKB; PA24854; -.
DR VEuPathDB; HostDB:ENSG00000006125; -.
DR eggNOG; KOG1061; Eukaryota.
DR GeneTree; ENSGT00940000155206; -.
DR InParanoid; P63010; -.
DR OMA; ASIYHKS; -.
DR OrthoDB; 323029at2759; -.
DR PhylomeDB; P63010; -.
DR TreeFam; TF300318; -.
DR PathwayCommons; P63010; -.
DR Reactome; R-HSA-167590; Nef Mediated CD4 Down-regulation.
DR Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
DR Reactome; R-HSA-182218; Nef Mediated CD8 Down-regulation.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors. [P63010-1]
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
DR Reactome; R-HSA-8964038; LDL clearance.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; P63010; -.
DR SIGNOR; P63010; -.
DR BioGRID-ORCS; 163; 29 hits in 1078 CRISPR screens.
DR ChiTaRS; AP2B1; human.
DR EvolutionaryTrace; P63010; -.
DR GeneWiki; AP2B1; -.
DR GenomeRNAi; 163; -.
DR Pharos; P63010; Tbio.
DR PRO; PR:P63010; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P63010; protein.
DR Bgee; ENSG00000006125; Expressed in cortical plate and 203 other tissues.
DR ExpressionAtlas; P63010; baseline and differential.
DR Genevisible; P63010; HS.
DR GO; GO:0030122; C:AP-2 adaptor complex; IDA:UniProtKB.
DR GO; GO:0030131; C:clathrin adaptor complex; IDA:MGI.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; NAS:ARUK-UCL.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0030276; F:clathrin binding; IDA:MGI.
DR GO; GO:0005048; F:signal sequence binding; TAS:BHF-UCL.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:UniProtKB.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IC:ComplexPortal.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1150; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF09066; B2-adapt-app_C; 1.
DR PIRSF; PIRSF002291; AP_complex_beta; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SMART; SM00185; ARM; 2.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Coated pit;
KW Endocytosis; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..937
FT /note="AP-2 complex subunit beta"
FT /id="PRO_0000193742"
FT REGION 841..937
FT /note="Interaction with ARRB1"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 737
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:17456551,
FT ECO:0000269|PubMed:18938240"
FT MOD_RES 928
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62944"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15897975"
FT /id="VSP_047805"
FT VAR_SEQ 663
FT /note="L -> LLGSDLGGGIGGSPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011490"
FT MUTAGEN 815
FT /note="Y->A: Strongly reduces interaction with SNAP91,
FT EPS15, AMPH and BIN1 and clathrin heavy chain."
FT /evidence="ECO:0000269|PubMed:16516836,
FT ECO:0000269|PubMed:16903783"
FT MUTAGEN 841
FT /note="W->A: Abolishes interaction with LDLRAP1 and ARRB1.
FT Greatly reduces DENND1B-binding."
FT /evidence="ECO:0000269|PubMed:15728179,
FT ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:16903783,
FT ECO:0000269|PubMed:20154091"
FT MUTAGEN 842
FT /note="K->E: Strongly reduces interaction with ARRB1."
FT /evidence="ECO:0000269|PubMed:16903783"
FT MUTAGEN 849
FT /note="E->A: Strongly reduces interaction with LDLRAP1,
FT ARRB1 and EPN1. No effect on DENND1B-binding."
FT /evidence="ECO:0000269|PubMed:11777907,
FT ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:20154091"
FT MUTAGEN 851
FT /note="Q->A: Strongly reduces interaction with ARRB1."
FT /evidence="ECO:0000269|PubMed:16903783"
FT MUTAGEN 879
FT /note="R->A: No effect on interaction with ARRB1."
FT /evidence="ECO:0000269|PubMed:10944104,
FT ECO:0000269|PubMed:16903783"
FT MUTAGEN 879
FT /note="R->E: Strongly reduces interaction with EPN1.
FT Reduces interaction with SNAP91 and clathrin. No effect on
FT EPS15 binding."
FT /evidence="ECO:0000269|PubMed:10944104,
FT ECO:0000269|PubMed:16903783"
FT MUTAGEN 888
FT /note="Y->V: Strongly reduces interaction with SNAP91, EPN1
FT and clathrin. No effect on EPS15 binding. Abolishes
FT interaction with ARRB1 and with DENND1B."
FT /evidence="ECO:0000269|PubMed:10944104,
FT ECO:0000269|PubMed:15728179, ECO:0000269|PubMed:16516836,
FT ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:20154091"
FT MUTAGEN 902
FT /note="E->A: Strongly reduces interaction with LDLRAP1 and
FT ARRB1. No effect on DENND1B-binding."
FT /evidence="ECO:0000269|PubMed:11777907,
FT ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:20154091"
FT MUTAGEN 917
FT /note="K->Q: Strongly reduces interaction with LDLRAP1.
FT SNAP91 and clathrin. Reduces interaction with EPN1. No
FT effect on EPS15 binding."
FT /evidence="ECO:0000269|PubMed:10944104"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2VGL"
FT HELIX 63..79
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 81..86
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2VGL"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:2JKR"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2JKR"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2JKR"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 296..312
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 314..319
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 404..420
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 427..433
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 478..494
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 496..499
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 517..530
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 536..542
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:4UQI"
FT HELIX 559..564
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 565..568
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:4UQI"
FT HELIX 624..630
FT /evidence="ECO:0007829|PDB:4UQI"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:2G30"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:2G30"
FT TURN 720..722
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 723..732
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 735..744
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 754..757
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 765..768
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 781..790
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 802..808
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 813..819
FT /evidence="ECO:0007829|PDB:2G30"
FT HELIX 822..825
FT /evidence="ECO:0007829|PDB:2G30"
FT HELIX 834..843
FT /evidence="ECO:0007829|PDB:2G30"
FT HELIX 846..848
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 850..854
FT /evidence="ECO:0007829|PDB:2G30"
FT HELIX 861..870
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 874..881
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 884..893
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 898..905
FT /evidence="ECO:0007829|PDB:2G30"
FT STRAND 910..920
FT /evidence="ECO:0007829|PDB:2G30"
FT HELIX 921..923
FT /evidence="ECO:0007829|PDB:2G30"
FT HELIX 924..936
FT /evidence="ECO:0007829|PDB:2G30"
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
