P17427 (AP2A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AP-2 complex subunit alpha-2

Alternative name(s):
100 kDa coated vesicle protein C
Adapter-related protein complex 2 alpha-2 subunit
Adaptor protein complex AP-2 subunit alpha-2
Alpha-adaptin C
Alpha2-adaptin
Clathrin assembly protein complex 2 alpha-C large chain
Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit

Gene names

Name:	Ap2a2
Synonyms:	Adtab

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	938 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. Ref.6 Ref.8 Ref.10
Subunit structure	Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Binds EPN1, EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1 By similarity. Interacts with DGKD isoform 2. Interacts with DENND1A, DENND1B and DENND1C. Interacts with FCHO1 and DAB2. Ref.6 Ref.7 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19
Subcellular location	Cell membrane. Membrane › coated pit; Peripheral membrane protein; Cytoplasmic side. Note: AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. Ref.9 Ref.11
Sequence similarities	Belongs to the adaptor complexes large subunit family.

Ontologies

Keywords
Biological process	Endocytosis Protein transport Transport
Cellular component	Cell membrane Coated pit Membrane
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW intracellular protein transport Traceable author statement PubMed 9714600. Source: MGI vesicle-mediated transport Traceable author statement PubMed 9714600. Source: MGI
Cellular_component	clathrin adaptor complex Inferred from electronic annotation. Source: InterPro coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell membrane coat Inferred from direct assay PubMed 11879655. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell secretory granule Traceable author statement PubMed 9714600. Source: MGI
Molecular_function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW protein transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 938

937

AP-2 complex subunit alpha-2

PRO_0000193733

Regions

Region

5 – 80

76

Lipid-binding

Sites

Binding site

43

1

Phosphatidylinositol lipid headgroup

Binding site

53

1

Phosphatidylinositol lipid headgroup

Binding site

57

1

Phosphatidylinositol lipid headgroup

Binding site

58

1

Phosphatidylinositol lipid headgroup

Binding site

61

1

Phosphatidylinositol lipid headgroup

Amino acid modifications

Modified residue

807

1

Phosphotyrosine Ref.12

Experimental info

Mutagenesis

21

1

R → E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15. Ref.20

Mutagenesis

31

1

K → Q: Reduces phosphatidylinositol binding. Ref.6

Mutagenesis

32

1

R → Q: Reduces phosphatidylinositol binding. Ref.6

Mutagenesis

35

1

K → Q: Reduces phosphatidylinositol binding. Ref.6

Mutagenesis

45

1

K → Q: Reduces phosphatidylinositol binding. Ref.6

Mutagenesis

55

1

K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. Ref.6

Mutagenesis

56

1

K → E: Strongly reduces phosphatidylinositol binding. Ref.6

Mutagenesis

56

1

K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57. Ref.6

Mutagenesis

57

1

K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56. Ref.6

Mutagenesis

61

1

K → Q: Reduces phosphatidylinositol binding. Ref.6

Mutagenesis

727

1

K → A: No effect on DENND1A-,DENND1B- nor DENND1C-binding.

Mutagenesis

782

1

Q → A: Reduces DENND1A- and DENND1C-binding. Ref.14

Mutagenesis

837

1

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. Ref.16 Ref.19

Mutagenesis

840

1

W → A: Abolishes AMPH, BIN1, EPS15, EPN1, auxilin and SNAP91 binding. Abolishes interaction with DGKD. Ref.13 Ref.16

Mutagenesis

849

1

E → A: No effect. Ref.16

Mutagenesis

905

1

R → A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837. Ref.16 Ref.19

Mutagenesis

907

1

E → A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding. Ref.16

Mutagenesis

916

1

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. Ref.14 Ref.19

Mutagenesis

920

1

R → A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding. Ref.16

Sequence conflict

858 – 859

2

HP → LE in AAH10597. Ref.4

Sequence conflict

889 – 890

2

GA → VL in CAA33097. Ref.1

Sequence conflict

889 – 890

2

GA → VL in AAB62703. Ref.5

Secondary structure

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938

Helix Strand Turn

Details...

Helix

11 – 22

12

Helix

28 – 40

13

Turn

41 – 43

3

Beta strand

44 – 48

5

Helix

52 – 66

15

Turn

67 – 69

3

Helix

76 – 82

7

Helix

88 – 100

13

Helix

106 – 121

16

Helix

125 – 138

14

Helix

141 – 147

7

Helix

150 – 156

7

Helix

162 – 178

17

Helix

180 – 182

3

Helix

188 – 193

6

Helix

194 – 197

4

Helix

201 – 214

14

Turn

215 – 217

3

Helix

219 – 222

4

Helix

225 – 238

14

Beta strand

241 – 244

4

Turn

245 – 247

3

Beta strand

252 – 254

3

Helix

255 – 265

11

Helix

273 – 291

19

Helix

299 – 319

21

Helix

323 – 338

16

Helix

343 – 355

13

Beta strand

359 – 361

3

Helix

364 – 368

5

Helix

369 – 378

10

Helix

382 – 393

12

Turn

398 – 400

3

Helix

401 – 413

13

Helix

417 – 434

18

Helix

438 – 450

13

Helix

453 – 455

3

Helix

458 – 470

13

Helix

475 – 485

11

Beta strand

488 – 490

3

Helix

493 – 505

13

Helix

508 – 510

3

Helix

514 – 516

3

Helix

518 – 529

12

Helix

534 – 550

17

Turn

552 – 554

3

Helix

555 – 562

8

Helix

565 – 568

4

Helix

573 – 588

16

Helix

591 – 597

7

Beta strand

610 – 613

4

Beta strand

617 – 620

4

Turn

701 – 704

4

Helix

705 – 708

4

Beta strand

714 – 718

5

Beta strand

720 – 731

12

Beta strand

734 – 743

10

Beta strand

745 – 747

3

Beta strand

749 – 757

9

Helix

760 – 765

6

Beta strand

766 – 770

5

Beta strand

782 – 791

10

Beta strand

800 – 807

8

Beta strand

810 – 817

8

Helix

822 – 825

4

Beta strand

826 – 828

3

Helix

833 – 840

8

Helix

846 – 848

3

Beta strand

849 – 855

7

Helix

862 – 872

11

Beta strand

874 – 877

4

Beta strand

879 – 883

5

Beta strand

886 – 894

9

Beta strand

899 – 909

11

Turn

910 – 913

4

Beta strand

914 – 923

10

Helix

924 – 935

12

Sequences

	Sequence		Length	Mass (Da)
	P17427 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 183FE8DFE199DBCA	FASTA	938	104,017
	10 20 30 40 50 60 MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC 70 80 90 100 110 120 KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL 130 140 150 160 170 180 ASRNPTFMGL ALHCIANVGS REMAEAFAGE IPKILVAGDT MDSVKQSAAL CLLRLYRTSP 190 200 210 220 230 240 DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA 250 260 270 280 290 300 STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ 310 320 330 340 350 360 HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF 370 380 390 400 410 420 SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN AQQIVAEMLS YLETADYSIR 430 440 450 460 470 480 EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK 490 500 510 520 530 540 TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL 550 560 570 580 590 600 LSTYIKFVNL FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE 610 620 630 640 650 660 MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS AASTPSPSAD 670 680 690 700 710 720 LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG SEDNFARFVC KNNGVLFENQ 730 740 750 760 770 780 LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL NFTPTLICAD DLQTNLNLQT KPVDPTVDGG 790 800 810 820 830 840 AQVQQVVNIE CISDFTEAPV LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW 850 860 870 880 890 900 KQLSNPQQEV QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI 910 920 930 GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins)." Robinson M.S. J. Cell Biol. 108:833-842(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD. Tissue: Thymus.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-859. Tissue: Mammary tumor.
[5]	"Identification and cloning of differentially expressed genes by long-distance differential display." Jurecic R., Nachtman R.G., Colicos S.M., Belmont J.W. Anal. Biochem. 259:235-244(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 379-938. Tissue: Fetal liver.
[6]	"Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits." Gaidarov I., Keen J.H. J. Cell Biol. 146:755-764(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CLATHRIN, MUTAGENESIS OF LYS-31; ARG-32; LYS-35; LYS-45; LYS-55; LYS-56; LYS-57 AND LYS-61.
[7]	"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2." Morris S.M., Cooper J.A. Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAB2.
[8]	"Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network." Nakatsu F., Ohno H. Cell Struct. Funct. 28:419-429(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[9]	"The AP-2 complex is excluded from the dynamic population of plasma membrane-associated clathrin." Rappoport J.Z., Taha B.W., Lemeer S., Benmerah A., Simon S.M. J. Biol. Chem. 278:47357-47360(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"Adaptors for clathrin coats: structure and function." Owen D.J., Collins B.M., Evans P.R. Annu. Rev. Cell Dev. Biol. 20:153-191(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[11]	"Dynamics of clathrin and adaptor proteins during endocytosis." Rappoport J.Z., Kemal S., Benmerah A., Simon S.M. Am. J. Physiol. 291:C1072-C1081(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-807, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Regulation of clathrin-dependent endocytosis by diacylglycerol kinase delta: importance of kinase activity and binding to AP2alpha." Kawasaki T., Kobayashi T., Ueyama T., Shirai Y., Saito N. Biochem. J. 409:471-479(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DKGD, MUTAGENESIS OF TRP-840.
[14]	"The connecdenn family, Rab35 guanine nucleotide exchange factors interfacing with the clathrin machinery." Marat A.L., McPherson P.S. J. Biol. Chem. 285:10627-10637(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DENND1A; DENND1B AND DENND1C, MUTAGENESIS OF GLN-782 AND ARG-916.
[15]	"Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning." Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M. Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FCHO1.
[16]	"A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain." Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R., Evans P.R., McMahon H.T. Cell 97:805-815(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 701-938, MUTAGENESIS OF PHE-837; TRP-840; GLU-849; ARG-905; GLU-907 AND ARG-920, INTERACTION WITH AMPH; EPS15; EPN1; SNAP91; BIN1 AND AUXILIN.
[17]	"Molecular architecture and functional model of the endocytic AP2 complex." Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J. Cell 109:523-535(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 9-592 IN COMPLEX WITH AP2B1; AP2M1; AP2S1 AND AN INOSITOL POLYPHOSPHATE HEADGROUP.
[18]	"Accessory protein recruitment motifs in clathrin-mediated endocytosis." Brett T.J., Traub L.M., Fremont D.H. Structure 10:797-809(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 701-938 IN COMPLEX WITH EPS15; EPN1 OR AMPH.
[19]	"Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly." Traub L.M., Downs M.A., Westrich J.L., Fremont D.H. Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 692-938, MUTAGENESIS OF PHE-837; ARG-905 AND ARG-916, INTERACTION WITH EPN1; EPS15; AMPH; SNAP91 AND BIN1.
[20]	"A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex." Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R., Hoening S., Owen D.J. Nature 456:976-979(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-620 IN COMPLEX WITH AP2B1; AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL, MUTAGENESIS OF ARG-21.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14972 mRNA. Translation: CAA33097.1.
AK088500 mRNA. Translation: BAC40392.1.
AC158224 Genomic DNA. No translation available.
AC102524 Genomic DNA. No translation available.
BC010597 mRNA. Translation: AAH10597.1.
AF006990 mRNA. Translation: AAB62703.1.

IPI

IPI00310131.

PIR

B30111.
S12471.

RefSeq

NP_031485.3. NM_007459.3.

UniGene

Mm.253090.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B9K	X-ray	1.90	A	701-938	[»]
1KY6	X-ray	2.00	A	701-938	[»]
1KY7	X-ray	2.15	A	701-938	[»]
1KYD	X-ray	2.00	A	701-938	[»]
1KYF	X-ray	1.22	A	701-938	[»]
1KYU	X-ray	1.80	A	701-938	[»]
1QTP	X-ray	1.60	A	701-938	[»]
1QTS	X-ray	1.40	A	701-938	[»]
1W80	X-ray	1.90	A	695-938	[»]
2JKR	X-ray	2.98	A/L	1-620	[»]
2JKT	X-ray	3.40	A/L	1-620	[»]
2VJ0	X-ray	1.60	A	695-938	[»]
3HS8	X-ray	1.90	A	702-938	[»]

ProteinModelPortal

P17427.

SMR

P17427. Positions 9-607, 701-938.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32160N.

IntAct

P17427. 6 interactions.

MINT

MINT-101068.

PTM databases

PhosphoSite

P17427.

Proteomic databases

PaxDb

P17427.

PRIDE

P17427.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957.

GeneID

11772.

KEGG

mmu:11772.

Organism-specific databases

CTD

161.

MGI

MGI:101920. Ap2a2.

Phylogenomic databases

eggNOG

COG5096.

GeneTree

ENSGT00550000074757.

HOVERGEN

HBG050518.

InParanoid

Q8C2J5.

KO

K11824.

OMA

PNKQAQM.

OrthoDB

EOG4HMJ8J.

Gene expression databases

ArrayExpress

P17427.

Bgee

P17427.

CleanEx

MM_AP2A2.

Genevestigator

P17427.

GermOnline

ENSMUSG00000002957. Mus musculus.

Family and domain databases

Gene3D

1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.

InterPro

IPR017104. AP2_complex_asu.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR013038. Clathrin_a-adaptin_app_Ig-like.
IPR003164. Clathrin_a-adaptin_app_sub_C.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR015873. Clathrin_a/coatomer_app_sub_C.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]

Pfam

PF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]

PIRSF

PIRSF037091. AP2_complex_alpha. 1 hit.

SMART

SM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]

SUPFAM

SSF55711. AP2_adap_app. 1 hit.
SSF48371. ARM-type_fold. 1 hit.
SSF49348. Clath_adapt. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

AP2A2. mouse.

EvolutionaryTrace

P17427.

NextBio

279555.

PMAP-CutDB

P17427.

SOURCE

Search...

Entry information

Entry name

AP2A2_MOUSE

Accession

Primary (citable) accession number: P17427
Secondary accession number(s): Q8C2J5, Q921V0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program