MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
Description | RecName: Full=AP-2 complex subunit alpha-2; AltName: Full=100 kDa coated vesicle protein C; AltName: Full=Adaptor protein complex AP-2 subunit alpha-2; AltName: Full=Adaptor-related protein complex 2 subunit alpha-2; AltName: Full=Alpha-adaptin C; AltName: Full=Alpha2-adaptin; AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain; AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit; |
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MyHits synonyms | AP2A2_MOUSE , P17427 , Q8C2J5 , Q921V0 , 183FE8DFE199DBCA |
![]() Legends: 1, INIT_MET Removed. {ECO:0000250|UniProtKB:P18484}; 2, BINDING Phosphatidylinositol lipid headgroup; 3, MUTAGEN R->E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15. {ECO:0000269|PubMed:19140243}; 4, MUTAGEN K->Q: Reduces phosphatidylinositol binding. {ECO:0000269|PubMed:10459011}; 5, MUTAGEN R->Q: Reduces phosphatidylinositol binding. {ECO:0000269|PubMed:10459011}; 6, MUTAGEN K->Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. {ECO:0000269|PubMed:10459011}; 7, MUTAGEN K->E: Strongly reduces phosphatidylinositol binding. {ECO:0000269|PubMed:10459011}; 8, MUTAGEN K->Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57. {ECO:0000269|PubMed:10459011}; 9, MUTAGEN K->Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56. {ECO:0000269|PubMed:10459011}; 10, MUTAGEN K->A: No effect on DENND1A-,DENND1B- nor DENND1C-binding; 11, MUTAGEN Q->A: Reduces DENND1A- and DENND1C- binding. {ECO:0000269|PubMed:20154091}; 12, MUTAGEN F->A: Reduces SNAP91, AMPH and BIN1 binding. Abolishes AMPH and SNAP91 binding; when associated with A-916. Abolishes EPN1 and EPS15 binding; when associated with A-905. {ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:10430869}; 13, MUTAGEN W->A: Abolishes AMPH, BIN1, EPS15, EPN1, auxilin and SNAP91 binding. Abolishes interaction with DGKD. {ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:17880279}; 14, MUTAGEN E->A: No effect. {ECO:0000269|PubMed:10380931}; 15, MUTAGEN R->A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837. {ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:10430869}; 16, MUTAGEN E->A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding. {ECO:0000269|PubMed:10380931}; 17, MUTAGEN R->A: Strongly reduces AMPH and SNAP91 binding. Abolishes DENND1B-binding; no effect on DENND1A-, nor DENND1C-binding. Abolishes AMPH and SNAP91 binding; when associated with A-837. {ECO:0000269|PubMed:10430869, ECO:0000269|PubMed:20154091}; 18, MUTAGEN R->A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding. {ECO:0000269|PubMed:10380931}; 19, REGION Lipid-binding; 20, CONFLICT HP -> LE (in Ref. 4; AAH10597). {ECO:0000305}; 21, CONFLICT GA -> VL (in Ref. 1; CAA33097 and 5; AAB62703). {ECO:0000305}; 22, ismart:Alpha_adaptinC2 [T]; 23, ipfam:Alpha_adaptinC2 [T]; 24, ipfam:Alpha_adaptin_C [T]; 25, HELIX {ECO:0000244|PDB:2JKR}; 26, TURN {ECO:0000244|PDB:2JKR}; 27, STRAND {ECO:0000244|PDB:2JKR}; 28, TURN {ECO:0000244|PDB:1QTS}; 29, HELIX {ECO:0000244|PDB:1KYF}; 30, STRAND {ECO:0000244|PDB:1KYF}; 31, TURN {ECO:0000244|PDB:1KYF}.
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ID AP2A2_MOUSE Reviewed; 938 AA. AC P17427; Q8C2J5; Q921V0; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 10-MAY-2017, entry version 173. DE RecName: Full=AP-2 complex subunit alpha-2; DE AltName: Full=100 kDa coated vesicle protein C; DE AltName: Full=Adaptor protein complex AP-2 subunit alpha-2; DE AltName: Full=Adaptor-related protein complex 2 subunit alpha-2; DE AltName: Full=Alpha-adaptin C; DE AltName: Full=Alpha2-adaptin; DE AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain; DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit; GN Name=Ap2a2; Synonyms=Adtab; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=2564002; DOI=10.1083/jcb.108.3.833; RA Robinson M.S.; RT "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins RT (alpha-adaptins)."; RL J. Cell Biol. 108:833-842(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-859. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 379-938. RC TISSUE=Fetal liver; RX PubMed=9618202; DOI=10.1006/abio.1998.2653; RA Jurecic R., Nachtman R.G., Colicos S.M., Belmont J.W.; RT "Identification and cloning of differentially expressed genes by long- RT distance differential display."; RL Anal. Biochem. 259:235-244(1998). RN [6] RP FUNCTION, SUBUNIT, INTERACTION WITH CLATHRIN, AND MUTAGENESIS OF RP LYS-31; ARG-32; LYS-35; LYS-45; LYS-55; LYS-56; LYS-57 AND LYS-61. RX PubMed=10459011; DOI=10.1083/jcb.146.4.755; RA Gaidarov I., Keen J.H.; RT "Phosphoinositide-AP-2 interactions required for targeting to plasma RT membrane clathrin-coated pits."; RL J. Cell Biol. 146:755-764(1999). RN [7] RP INTERACTION WITH DAB2. RX PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x; RA Morris S.M., Cooper J.A.; RT "Disabled-2 colocalizes with the LDLR in clathrin-coated pits and RT interacts with AP-2."; RL Traffic 2:111-123(2001). 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 SUBCELLULAR LOCATION. RX PubMed=17035303; DOI=10.1152/ajpcell.00160.2006; RA Rappoport J.Z., Kemal S., Benmerah A., Simon S.M.; RT "Dynamics of clathrin and adaptor proteins during endocytosis."; RL Am. J. Physiol. 291:C1072-C1081(2006). RN [12] RP INTERACTION WITH DKGD, AND MUTAGENESIS OF TRP-840. RX PubMed=17880279; DOI=10.1042/BJ20070755; RA Kawasaki T., Kobayashi T., Ueyama T., Shirai Y., Saito N.; RT "Regulation of clathrin-dependent endocytosis by diacylglycerol kinase RT delta: importance of kinase activity and binding to AP2alpha."; RL Biochem. J. 409:471-479(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [14] RP INTERACTION WITH DENND1A; DENND1B AND DENND1C, AND MUTAGENESIS OF RP GLN-782 AND ARG-916. 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 [15] 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 [16] RP INTERACTION WITH ATAT1. RX PubMed=24097348; DOI=10.1038/nature12571; RA Montagnac G., Meas-Yedid V., Irondelle M., Castro-Castro A., RA Franco M., Shida T., Nachury M.V., Benmerah A., Olivo-Marin J.C., RA Chavrier P.; RT "alphaTAT1 catalyses microtubule acetylation at clathrin-coated RT pits."; RL Nature 502:567-570(2013). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 701-938, MUTAGENESIS OF RP PHE-837; TRP-840; GLU-849; ARG-905; GLU-907 AND ARG-920, AND RP INTERACTION WITH AMPH; EPS15; EPN1; SNAP91; BIN1 AND AUXILIN. RX PubMed=10380931; DOI=10.1016/S0092-8674(00)80791-6; RA Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R., RA Evans P.R., McMahon H.T.; RT "A structural explanation for the binding of multiple ligands by the RT alpha-adaptin appendage domain."; RL Cell 97:805-815(1999). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 9-592 IN COMPLEX WITH AP2B1; 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 [19] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 701-938 IN COMPLEX WITH RP EPS15; EPN1 OR AMPH. RX PubMed=12057195; DOI=10.1016/S0969-2126(02)00784-0; RA Brett T.J., Traub L.M., Fremont D.H.; RT "Accessory protein recruitment motifs in clathrin-mediated RT endocytosis."; RL Structure 10:797-809(2002). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 692-938, MUTAGENESIS OF RP PHE-837; ARG-905 AND ARG-916, AND INTERACTION WITH EPN1; EPS15; AMPH; RP SNAP91 AND BIN1. RX PubMed=10430869; DOI=10.1073/pnas.96.16.8907; RA Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.; RT "Crystal structure of the alpha appendage of AP-2 reveals a RT recruitment platform for clathrin-coat assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-620 IN COMPLEX WITH AP2B1; RP AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL, AND MUTAGENESIS OF RP ARG-21. RX PubMed=19140243; 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 alpha CC subunit binds polyphosphoinositide-containing lipids, positioning CC AP-2 on the membrane. The AP-2 alpha subunit acts via its C- CC terminal appendage domain as a scaffolding platform for endocytic CC accessory proteins. The AP-2 alpha and AP-2 sigma subunits are CC thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] CC motif. {ECO:0000269|PubMed:10459011, ECO:0000269|PubMed:14745134, CC ECO:0000269|PubMed:15473838}. 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). Binds EPN1, CC EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1 (By similarity). CC Interacts with DGKD isoform 2. Interacts with DENND1A, DENND1B and CC DENND1C. Interacts with FCHO1 and DAB2. Interacts with ATAT1; this CC interaction is required for efficient alpha-tubulin acetylation by CC ATAT1. {ECO:0000250, ECO:0000269|PubMed:10380931, CC ECO:0000269|PubMed:10430869, ECO:0000269|PubMed:10459011, CC ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:12057195, CC ECO:0000269|PubMed:12086608, ECO:0000269|PubMed:17880279, CC ECO:0000269|PubMed:19140243, ECO:0000269|PubMed:20154091, CC ECO:0000269|PubMed:22484487, ECO:0000269|PubMed:24097348}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14530274, CC ECO:0000269|PubMed:17035303}; Peripheral membrane protein CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane, coated CC pit {ECO:0000269|PubMed:17035303}; Peripheral membrane protein CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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 {ECO:0000269|PubMed:17035303}. CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14972; CAA33097.1; -; mRNA. DR EMBL; AK088500; BAC40392.1; -; mRNA. DR EMBL; AC158224; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC102524; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC010597; AAH10597.1; -; mRNA. DR EMBL; AF006990; AAB62703.1; -; mRNA. DR CCDS; CCDS40188.1; -. DR PIR; B30111; B30111. DR PIR; S12471; S12471. DR RefSeq; NP_031485.3; NM_007459.3. DR UniGene; Mm.253090; -. DR PDB; 1B9K; X-ray; 1.90 A; A=701-938. DR PDB; 1KY6; X-ray; 2.00 A; A=701-938. DR PDB; 1KY7; X-ray; 2.15 A; A=701-938. DR PDB; 1KYD; X-ray; 2.00 A; A=701-938. DR PDB; 1KYF; X-ray; 1.22 A; A=701-938. DR PDB; 1KYU; X-ray; 1.80 A; A=701-938. DR PDB; 1QTP; X-ray; 1.60 A; A=701-938. DR PDB; 1QTS; X-ray; 1.40 A; A=701-938. DR PDB; 1W80; X-ray; 1.90 A; A=695-938. DR PDB; 2JKR; X-ray; 2.98 A; A/L=1-620. DR PDB; 2JKT; X-ray; 3.40 A; A/L=1-620. DR PDB; 2VJ0; X-ray; 1.60 A; A=695-938. DR PDB; 3HS8; X-ray; 1.90 A; A=702-938. DR PDBsum; 1B9K; -. DR PDBsum; 1KY6; -. DR PDBsum; 1KY7; -. DR PDBsum; 1KYD; -. DR PDBsum; 1KYF; -. DR PDBsum; 1KYU; -. DR PDBsum; 1QTP; -. DR PDBsum; 1QTS; -. DR PDBsum; 1W80; -. DR PDBsum; 2JKR; -. DR PDBsum; 2JKT; -. DR PDBsum; 2VJ0; -. DR PDBsum; 3HS8; -. DR ProteinModelPortal; P17427; -. DR SMR; P17427; -. DR BioGrid; 198130; 12. DR DIP; DIP-32160N; -. DR IntAct; P17427; 17. DR MINT; MINT-101068; -. DR STRING; 10090.ENSMUSP00000003038; -. DR iPTMnet; P17427; -. DR PhosphoSitePlus; P17427; -. DR SwissPalm; P17427; -. DR EPD; P17427; -. DR MaxQB; P17427; -. DR PaxDb; P17427; -. DR PeptideAtlas; P17427; -. DR PRIDE; P17427; -. DR Ensembl; ENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957. DR GeneID; 11772; -. DR KEGG; mmu:11772; -. DR UCSC; uc009kls.2; mouse. DR CTD; 161; -. DR MGI; MGI:101920; Ap2a2. DR eggNOG; KOG1077; Eukaryota. DR eggNOG; ENOG410XNQE; LUCA. DR GeneTree; ENSGT00550000074757; -. DR HOVERGEN; HBG050518; -. DR InParanoid; P17427; -. DR KO; K11824; -. DR OMA; PPFSERT; -. DR OrthoDB; EOG091G01JZ; -. DR TreeFam; TF300308; -. DR Reactome; R-MMU-171052; LDL-mediated lipid transport. DR Reactome; R-MMU-177504; Retrograde neurotrophin signalling. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors. DR Reactome; R-MMU-437239; Recycling pathway of L1. DR Reactome; R-MMU-5099900; WNT5A-dependent internalization of FZD4. DR Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR Reactome; R-MMU-8866427; VLDLR internalisation and degradation. DR ChiTaRS; Ap2a2; mouse. DR EvolutionaryTrace; P17427; -. DR PMAP-CutDB; P17427; -. DR PRO; PR:P17427; -. DR Proteomes; UP000000589; Chromosome 7. DR Bgee; ENSMUSG00000002957; -. DR CleanEx; MM_AP2A2; -. DR ExpressionAtlas; P17427; baseline and differential. DR Genevisible; P17427; MM. DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro. DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL. DR GO; GO:0030117; C:membrane coat; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030141; C:secretory granule; TAS:MGI. DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA. DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI. DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; NAS:BHF-UCL. DR GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR017104; AP2_complex_asu. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N. DR InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C. DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig. DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C. DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like. DR Pfam; PF01602; Adaptin_N; 1. DR Pfam; PF02296; Alpha_adaptin_C; 1. DR Pfam; PF02883; Alpha_adaptinC2; 1. DR PIRSF; PIRSF037091; AP2_complex_alpha; 1. DR SMART; SM00809; Alpha_adaptinC2; 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; Cell membrane; Coated pit; Complete proteome; KW Endocytosis; Lipid-binding; Membrane; Protein transport; KW Reference proteome; Transport. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P18484}. FT CHAIN 2 938 AP-2 complex subunit alpha-2. FT /FTId=PRO_0000193733. FT REGION 5 80 Lipid-binding. FT BINDING 43 43 Phosphatidylinositol lipid headgroup. FT BINDING 53 53 Phosphatidylinositol lipid headgroup. FT BINDING 57 57 Phosphatidylinositol lipid headgroup. FT BINDING 58 58 Phosphatidylinositol lipid headgroup. FT BINDING 61 61 Phosphatidylinositol lipid headgroup. FT MUTAGEN 21 21 R->E: Reduces interaction with CD4 FT endocytosis signal motif; when associated FT with AP2S1 S-15. FT {ECO:0000269|PubMed:19140243}. FT MUTAGEN 31 31 K->Q: Reduces phosphatidylinositol FT binding. {ECO:0000269|PubMed:10459011}. FT MUTAGEN 32 32 R->Q: Reduces phosphatidylinositol FT binding. {ECO:0000269|PubMed:10459011}. FT MUTAGEN 35 35 K->Q: Reduces phosphatidylinositol FT binding. {ECO:0000269|PubMed:10459011}. FT MUTAGEN 45 45 K->Q: Reduces phosphatidylinositol FT binding. {ECO:0000269|PubMed:10459011}. FT MUTAGEN 55 55 K->Q: Strongly reduces FT phosphatidylinositol binding. Abolishes FT phosphatidylinositol binding; when FT associated with Q-56 and Q-57. FT {ECO:0000269|PubMed:10459011}. FT MUTAGEN 56 56 K->E: Strongly reduces FT phosphatidylinositol binding. FT {ECO:0000269|PubMed:10459011}. FT MUTAGEN 56 56 K->Q: Strongly reduces FT phosphatidylinositol binding. Abolishes FT phosphatidylinositol binding; when FT associated with Q-55 and Q-57. FT {ECO:0000269|PubMed:10459011}. FT MUTAGEN 57 57 K->Q: Strongly reduces FT phosphatidylinositol binding. Abolishes FT phosphatidylinositol binding; when FT associated with Q-55 and Q-56. FT {ECO:0000269|PubMed:10459011}. FT MUTAGEN 61 61 K->Q: Reduces phosphatidylinositol FT binding. {ECO:0000269|PubMed:10459011}. FT MUTAGEN 727 727 K->A: No effect on DENND1A-,DENND1B- nor FT DENND1C-binding. FT MUTAGEN 782 782 Q->A: Reduces DENND1A- and DENND1C- FT binding. {ECO:0000269|PubMed:20154091}. FT MUTAGEN 837 837 F->A: Reduces SNAP91, AMPH and BIN1 FT binding. Abolishes AMPH and SNAP91 FT binding; when associated with A-916. FT Abolishes EPN1 and EPS15 binding; when FT associated with A-905. FT {ECO:0000269|PubMed:10380931, FT ECO:0000269|PubMed:10430869}. FT MUTAGEN 840 840 W->A: Abolishes AMPH, BIN1, EPS15, EPN1, FT auxilin and SNAP91 binding. Abolishes FT interaction with DGKD. FT {ECO:0000269|PubMed:10380931, FT ECO:0000269|PubMed:17880279}. FT MUTAGEN 849 849 E->A: No effect. FT {ECO:0000269|PubMed:10380931}. FT MUTAGEN 905 905 R->A: Strongly reduces AMPH, SNAP91, FT auxilin and BIN1 binding. Abolishes EPN1 FT and EPS15 binding; when associated with FT A-837. {ECO:0000269|PubMed:10380931, FT ECO:0000269|PubMed:10430869}. FT MUTAGEN 907 907 E->A: Strongly reduces AMPH, SNAP91 and FT BIN1 binding. Slightly reduces EPS15 and FT auxilin binding. FT {ECO:0000269|PubMed:10380931}. FT MUTAGEN 916 916 R->A: Strongly reduces AMPH and SNAP91 FT binding. Abolishes DENND1B-binding; no FT effect on DENND1A-, nor DENND1C-binding. FT Abolishes AMPH and SNAP91 binding; when FT associated with A-837. FT {ECO:0000269|PubMed:10430869, FT ECO:0000269|PubMed:20154091}. FT MUTAGEN 920 920 R->A: Abolishes AMPH and BIN1 binding. FT Reduces EPS15, SNAP91 and auxilin FT binding. {ECO:0000269|PubMed:10380931}. FT CONFLICT 858 859 HP -> LE (in Ref. 4; AAH10597). FT {ECO:0000305}. FT CONFLICT 889 890 GA -> VL (in Ref. 1; CAA33097 and 5; FT AAB62703). {ECO:0000305}. FT HELIX 11 22 {ECO:0000244|PDB:2JKR}. FT HELIX 28 40 {ECO:0000244|PDB:2JKR}. FT TURN 41 43 {ECO:0000244|PDB:2JKR}. FT STRAND 44 48 {ECO:0000244|PDB:2JKR}. FT HELIX 52 66 {ECO:0000244|PDB:2JKR}. FT TURN 67 69 {ECO:0000244|PDB:2JKR}. FT HELIX 76 82 {ECO:0000244|PDB:2JKR}. FT HELIX 88 100 {ECO:0000244|PDB:2JKR}. FT HELIX 106 121 {ECO:0000244|PDB:2JKR}. FT HELIX 125 138 {ECO:0000244|PDB:2JKR}. FT HELIX 141 147 {ECO:0000244|PDB:2JKR}. FT HELIX 150 156 {ECO:0000244|PDB:2JKR}. FT HELIX 162 178 {ECO:0000244|PDB:2JKR}. FT HELIX 180 182 {ECO:0000244|PDB:2JKR}. FT HELIX 188 193 {ECO:0000244|PDB:2JKR}. FT HELIX 194 197 {ECO:0000244|PDB:2JKR}. FT HELIX 201 214 {ECO:0000244|PDB:2JKR}. FT TURN 215 217 {ECO:0000244|PDB:2JKR}. FT HELIX 219 222 {ECO:0000244|PDB:2JKR}. FT HELIX 225 238 {ECO:0000244|PDB:2JKR}. FT STRAND 241 244 {ECO:0000244|PDB:2JKR}. FT TURN 245 247 {ECO:0000244|PDB:2JKR}. FT STRAND 252 254 {ECO:0000244|PDB:2JKR}. FT HELIX 255 265 {ECO:0000244|PDB:2JKR}. FT HELIX 273 291 {ECO:0000244|PDB:2JKR}. FT HELIX 299 319 {ECO:0000244|PDB:2JKR}. FT HELIX 323 338 {ECO:0000244|PDB:2JKR}. FT HELIX 343 355 {ECO:0000244|PDB:2JKR}. FT STRAND 359 361 {ECO:0000244|PDB:2JKR}. FT HELIX 364 368 {ECO:0000244|PDB:2JKR}. FT HELIX 369 378 {ECO:0000244|PDB:2JKR}. FT HELIX 382 393 {ECO:0000244|PDB:2JKR}. FT TURN 398 400 {ECO:0000244|PDB:2JKR}. FT HELIX 401 413 {ECO:0000244|PDB:2JKR}. FT HELIX 417 434 {ECO:0000244|PDB:2JKR}. FT HELIX 438 450 {ECO:0000244|PDB:2JKR}. FT HELIX 453 455 {ECO:0000244|PDB:2JKR}. FT HELIX 458 470 {ECO:0000244|PDB:2JKR}. FT HELIX 475 485 {ECO:0000244|PDB:2JKR}. FT STRAND 488 490 {ECO:0000244|PDB:2JKR}. FT HELIX 493 505 {ECO:0000244|PDB:2JKR}. FT HELIX 508 510 {ECO:0000244|PDB:2JKR}. FT HELIX 514 516 {ECO:0000244|PDB:2JKR}. FT HELIX 518 529 {ECO:0000244|PDB:2JKR}. FT HELIX 534 550 {ECO:0000244|PDB:2JKR}. FT TURN 552 554 {ECO:0000244|PDB:2JKR}. FT HELIX 555 562 {ECO:0000244|PDB:2JKR}. FT HELIX 565 568 {ECO:0000244|PDB:2JKR}. FT HELIX 573 588 {ECO:0000244|PDB:2JKR}. FT HELIX 591 597 {ECO:0000244|PDB:2JKR}. FT STRAND 610 613 {ECO:0000244|PDB:2JKR}. FT STRAND 617 620 {ECO:0000244|PDB:2JKR}. FT TURN 701 704 {ECO:0000244|PDB:1QTS}. FT HELIX 705 708 {ECO:0000244|PDB:1KYF}. FT STRAND 714 718 {ECO:0000244|PDB:1KYF}. FT STRAND 720 731 {ECO:0000244|PDB:1KYF}. FT STRAND 734 743 {ECO:0000244|PDB:1KYF}. FT STRAND 745 747 {ECO:0000244|PDB:1KYF}. FT STRAND 749 757 {ECO:0000244|PDB:1KYF}. FT HELIX 760 765 {ECO:0000244|PDB:1KYF}. FT STRAND 766 770 {ECO:0000244|PDB:1KYF}. FT STRAND 782 791 {ECO:0000244|PDB:1KYF}. FT STRAND 800 807 {ECO:0000244|PDB:1KYF}. FT STRAND 810 817 {ECO:0000244|PDB:1KYF}. FT HELIX 822 825 {ECO:0000244|PDB:1KYF}. FT STRAND 826 828 {ECO:0000244|PDB:1KYF}. FT HELIX 833 840 {ECO:0000244|PDB:1KYF}. FT HELIX 846 848 {ECO:0000244|PDB:1KYF}. FT STRAND 849 855 {ECO:0000244|PDB:1KYF}. FT HELIX 862 872 {ECO:0000244|PDB:1KYF}. FT STRAND 874 877 {ECO:0000244|PDB:1KYF}. FT STRAND 879 883 {ECO:0000244|PDB:1KYF}. FT STRAND 886 894 {ECO:0000244|PDB:1KYF}. FT STRAND 899 909 {ECO:0000244|PDB:1KYF}. FT TURN 910 913 {ECO:0000244|PDB:1KYF}. FT STRAND 914 923 {ECO:0000244|PDB:1KYF}. FT HELIX 924 935 {ECO:0000244|PDB:1KYF}. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 706 819 ismart:Alpha_adaptinC2 [T] FT MYHIT 712 816 ipfam:Alpha_adaptinC2 [T] FT MYHIT 31 587 ipfam:Adaptin_N [T] FT MYHIT 825 933 ipfam:Alpha_adaptin_C [T] SQ SEQUENCE 938 AA; 104017 MW; 183FE8DFE199DBCA CRC64; MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL ASRNPTFMGL ALHCIANVGS REMAEAFAGE IPKILVAGDT MDSVKQSAAL CLLRLYRTSP DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN AQQIVAEMLS YLETADYSIR EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL LSTYIKFVNL FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS AASTPSPSAD LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG SEDNFARFVC KNNGVLFENQ LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL NFTPTLICAD DLQTNLNLQT KPVDPTVDGG AQVQQVVNIE CISDFTEAPV LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW KQLSNPQQEV QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF // |