Ap2a2

Functionⁱ

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.3 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	43	Phosphatidylinositol lipid headgroup	1
Binding siteⁱ	53	Phosphatidylinositol lipid headgroup	1
Binding siteⁱ	57	Phosphatidylinositol lipid headgroup	1
Binding siteⁱ	58	Phosphatidylinositol lipid headgroup	1
Binding siteⁱ	61	Phosphatidylinositol lipid headgroup	1

GO - Molecular functionⁱ

clathrin adaptor activity Source: InterPro
disordered domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 11756460
- 12732633
phosphatidylinositol binding Source: MGI
protein-containing complex binding Source: MGI
protein domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 12732633
protein kinase binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 21307259

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

clathrin-dependent endocytosis Source: InterPro
intracellular protein transport
Source: MGI
Traceable author statementⁱ
- 9714600
regulation of hematopoietic stem cell differentiation
Source: BHF-UCL
Non-traceable author statementⁱ
- 22174158
vesicle-mediated transport
Source: MGI
Traceable author statementⁱ
- 9714600

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Endocytosis, Protein transport, Transport
Ligand	Lipid-binding

Enzyme and pathway databases

Reactomeⁱ	R-MMU-177504 Retrograde neurotrophin signalling R-MMU-2132295 MHC class II antigen presentation R-MMU-416993 Trafficking of GluR2-containing AMPA receptors R-MMU-437239 Recycling pathway of L1 R-MMU-5099900 WNT5A-dependent internalization of FZD4 R-MMU-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2 R-MMU-6798695 Neutrophil degranulation R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis R-MMU-8856828 Clathrin-mediated endocytosis R-MMU-8866427 VLDLR internalisation and degradation R-MMU-8964038 LDL clearance

Reactomeⁱ

R-MMU-177504 Retrograde neurotrophin signalling
R-MMU-2132295 MHC class II antigen presentation
R-MMU-416993 Trafficking of GluR2-containing AMPA receptors
R-MMU-437239 Recycling pathway of L1
R-MMU-5099900 WNT5A-dependent internalization of FZD4
R-MMU-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2
R-MMU-6798695 Neutrophil degranulation
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8866427 VLDLR internalisation and degradation
R-MMU-8964038 LDL clearance

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: AP-2 complex subunit alpha-2 Alternative name(s): 100 kDa coated vesicle protein C Adaptor protein complex AP-2 subunit alpha-2 Adaptor-related protein complex 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 namesⁱ	Name:Ap2a2 Synonyms:Adtab
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 7

Organism-specific databases

MGIⁱ	MGI:101920 Ap2a2

Keywords - Cellular componentⁱ

Cell membrane, Coated pit, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	21	R → E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15. 1 Publication	1
Mutagenesisⁱ	31	K → Q: Reduces phosphatidylinositol binding. 1 Publication	1
Mutagenesisⁱ	32	R → Q: Reduces phosphatidylinositol binding. 1 Publication	1
Mutagenesisⁱ	35	K → Q: Reduces phosphatidylinositol binding. 1 Publication	1
Mutagenesisⁱ	45	K → Q: Reduces phosphatidylinositol binding. 1 Publication	1
Mutagenesisⁱ	55	K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. 1 Publication	1
Mutagenesisⁱ	56	K → E: Strongly reduces phosphatidylinositol binding. 1 Publication	1
Mutagenesisⁱ	56	K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57. 1 Publication	1
Mutagenesisⁱ	57	K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56. 1 Publication	1
Mutagenesisⁱ	61	K → Q: Reduces phosphatidylinositol binding. 1 Publication	1
Mutagenesisⁱ	727	K → A: No effect on DENND1A-,DENND1B- nor DENND1C-binding.	1
Mutagenesisⁱ	782	Q → A: Reduces DENND1A- and DENND1C-binding. 1 Publication	1
Mutagenesisⁱ	837	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. 2 Publications	1
Mutagenesisⁱ	840	W → A: Abolishes AMPH, BIN1, EPS15, EPN1, auxilin and SNAP91 binding. Abolishes interaction with DGKD. 2 Publications	1
Mutagenesisⁱ	849	E → A: No effect. 1 Publication	1
Mutagenesisⁱ	905	R → A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837. 2 Publications	1
Mutagenesisⁱ	907	E → A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding. 1 Publication	1
Mutagenesisⁱ	916	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. 2 Publications	1
Mutagenesisⁱ	920	R → A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000193733	1 – 938	AP-2 complex subunit alpha-2Add BLAST		938

Proteomic databases

EPDⁱ	P17427
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P17427
PaxDbⁱ	P17427
PeptideAtlas More...PeptideAtlasⁱ	P17427
PRIDEⁱ	P17427

PTM databases

iPTMnetⁱ	P17427
PhosphoSitePlusⁱ	P17427
SwissPalmⁱ	P17427

Miscellaneous databases

PMAP-CutDBⁱ	P17427

PMAP-CutDBⁱ

P17427

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000002957 Expressed in 295 organ(s), highest expression level in embryo
CleanExⁱ	MM_AP2A2
ExpressionAtlasⁱ	P17427 baseline and differential
Genevisibleⁱ	P17427 MM

Interactionⁱ

Subunit structureⁱ

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. Interacts with ATAT1; this interaction is required for efficient alpha-tubulin acetylation by ATAT1. Interacts with KIAA1107 (PubMed:29262337).By similarity12 Publications

GO - Molecular functionⁱ

clathrin adaptor activity Source: InterPro
disordered domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 11756460
- 12732633
protein domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 12732633
protein kinase binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 21307259

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	198130, 17 interactors
CORUMⁱ	P17427
Database of interacting proteins More...DIPⁱ	DIP-32160N
IntActⁱ	P17427, 24 interactors
Molecular INTeraction database More...MINTⁱ	P17427
STRINGⁱ	10090.ENSMUSP00000003038

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	11 – 22	Combined sources	12
Helixⁱ	28 – 40	Combined sources	13
Turnⁱ	41 – 43	Combined sources	3
Beta strandⁱ	44 – 48	Combined sources	5
Helixⁱ	52 – 66	Combined sources	15
Turnⁱ	67 – 69	Combined sources	3
Helixⁱ	76 – 82	Combined sources	7
Helixⁱ	88 – 100	Combined sources	13
Helixⁱ	106 – 121	Combined sources	16
Helixⁱ	125 – 138	Combined sources	14
Helixⁱ	141 – 147	Combined sources	7
Helixⁱ	150 – 156	Combined sources	7
Helixⁱ	162 – 178	Combined sources	17
Helixⁱ	180 – 182	Combined sources	3
Helixⁱ	188 – 193	Combined sources	6
Helixⁱ	194 – 197	Combined sources	4
Helixⁱ	201 – 214	Combined sources	14
Turnⁱ	215 – 217	Combined sources	3
Helixⁱ	219 – 222	Combined sources	4
Helixⁱ	225 – 238	Combined sources	14
Beta strandⁱ	241 – 244	Combined sources	4
Turnⁱ	245 – 247	Combined sources	3
Beta strandⁱ	252 – 254	Combined sources	3
Helixⁱ	255 – 265	Combined sources	11
Helixⁱ	273 – 291	Combined sources	19
Helixⁱ	299 – 319	Combined sources	21
Helixⁱ	323 – 338	Combined sources	16
Helixⁱ	343 – 355	Combined sources	13
Beta strandⁱ	359 – 361	Combined sources	3
Helixⁱ	364 – 368	Combined sources	5
Helixⁱ	386 – 394	Combined sources	9
Helixⁱ	398 – 405	Combined sources	8
Helixⁱ	407 – 410	Combined sources	4
Turnⁱ	417 – 419	Combined sources	3
Helixⁱ	420 – 424	Combined sources	5
Helixⁱ	427 – 434	Combined sources	8
Helixⁱ	438 – 453	Combined sources	16
Helixⁱ	459 – 471	Combined sources	13
Turnⁱ	473 – 475	Combined sources	3
Helixⁱ	480 – 485	Combined sources	6
Beta strandⁱ	488 – 490	Combined sources	3
Helixⁱ	493 – 505	Combined sources	13
Helixⁱ	508 – 510	Combined sources	3
Helixⁱ	514 – 516	Combined sources	3
Helixⁱ	518 – 529	Combined sources	12
Helixⁱ	534 – 550	Combined sources	17
Turnⁱ	552 – 554	Combined sources	3
Helixⁱ	555 – 562	Combined sources	8
Helixⁱ	565 – 568	Combined sources	4
Helixⁱ	573 – 588	Combined sources	16
Helixⁱ	591 – 597	Combined sources	7
Beta strandⁱ	610 – 613	Combined sources	4
Beta strandⁱ	617 – 620	Combined sources	4
Beta strandⁱ	698 – 700	Combined sources	3
Turnⁱ	701 – 704	Combined sources	4
Helixⁱ	705 – 708	Combined sources	4
Beta strandⁱ	714 – 718	Combined sources	5
Beta strandⁱ	720 – 731	Combined sources	12
Beta strandⁱ	734 – 743	Combined sources	10
Beta strandⁱ	745 – 747	Combined sources	3
Beta strandⁱ	749 – 757	Combined sources	9
Helixⁱ	760 – 765	Combined sources	6
Beta strandⁱ	766 – 770	Combined sources	5
Beta strandⁱ	782 – 791	Combined sources	10
Beta strandⁱ	800 – 807	Combined sources	8
Beta strandⁱ	810 – 817	Combined sources	8
Helixⁱ	822 – 825	Combined sources	4
Beta strandⁱ	826 – 828	Combined sources	3
Helixⁱ	833 – 840	Combined sources	8
Helixⁱ	846 – 848	Combined sources	3
Beta strandⁱ	849 – 855	Combined sources	7
Helixⁱ	862 – 872	Combined sources	11
Beta strandⁱ	874 – 877	Combined sources	4
Beta strandⁱ	879 – 883	Combined sources	5
Beta strandⁱ	886 – 894	Combined sources	9
Beta strandⁱ	899 – 909	Combined sources	11
Turnⁱ	910 – 913	Combined sources	4
Beta strandⁱ	914 – 923	Combined sources	10
Helixⁱ	924 – 935	Combined sources	12

Show more details

3D structure databases

ProteinModelPortalⁱ	P17427
SMRⁱ	P17427
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P17427

EvolutionaryTraceⁱ

P17427

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	5 – 80	Lipid-bindingAdd BLAST		76

Sequence similaritiesⁱ

Belongs to the adaptor complexes large subunit family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1077 Eukaryota ENOG410XNQE LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074757
HOVERGENⁱ	HBG050518
InParanoidⁱ	P17427
KEGG Orthology (KO) More...KOⁱ	K11824
OMAⁱ	FMNLALH
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G01JZ
TreeFamⁱ	TF300308

Family and domain databases

Gene3Dⁱ	1.25.10.10, 1 hit 3.30.310.10, 1 hit
InterProⁱ	View protein in InterPro IPR017104 AP2_complex_asu IPR011989 ARM-like IPR016024 ARM-type_fold IPR002553 Clathrin/coatomer_adapt-like_N IPR003164 Clathrin_a-adaptin_app_sub_C IPR008152 Clathrin_a/b/g-adaptin_app_Ig IPR013041 Clathrin_app_Ig-like_sf IPR009028 Coatomer/calthrin_app_sub_C IPR012295 TBP_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01602 Adaptin_N, 1 hit PF02296 Alpha_adaptin_C, 1 hit PF02883 Alpha_adaptinC2, 1 hit
PIRSFⁱ	PIRSF037091 AP2_complex_alpha, 1 hit
SMARTⁱ	View protein in SMART SM00809 Alpha_adaptinC2, 1 hit
SUPFAMⁱ	SSF48371 SSF48371, 1 hit SSF49348 SSF49348, 1 hit SSF55711 SSF55711, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

P17427-1 [UniParc]FASTA Add to basket

« Hide

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

Length:938

Mass (Da):104,017

Last modified:July 27, 2011 - v2

Checksum:ⁱ183FE8DFE199DBCA

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A0J9YUA7	A0A0J9YUA7_MOUSE		AP-2 complex subunit alpha-2 AP-2 complex subunit alpha-2	Ap2a2	131	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	858 – 859	HP → LE in AAH10597 (PubMed:15489334).Curated	2
Sequence conflictⁱ	889 – 890	GA → VL in CAA33097 (PubMed:2564002).Curated	2
Sequence conflictⁱ	889 – 890	GA → VL in AAB62703 (PubMed:9618202).Curated	2

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS40188.1
PIRⁱ	B30111 S12471
NCBI Reference Sequences More...RefSeqⁱ	NP_031485.3, NM_007459.3
UniGeneⁱ	Mm.253090

Genome annotation databases

Ensemblⁱ	ENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957
GeneIDⁱ	11772
KEGGⁱ	mmu:11772
UCSC genome browser More...UCSCⁱ	uc009kls.2 mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P17427	MKIAA0899 protein (Fragment)		MOUSE		967	UniRef100_P17427
UPI0003D785B4		MOUSE		544

Protein	Similar proteins		Species	Score	Length	Source
P17427	AP-2 complex subunit alpha-2		HUMAN		939	UniRef90_P17427
AP-2 complex subunit alpha-2		BOVIN		938
AP-2 complex subunit alpha-2	)	RAT		938
MKIAA0899 protein (Fragment)		MOUSE		967
AP-2 complex subunit alpha		FELCA		977
+371

Protein	Similar proteins		Species	Score	Length	Source
P17427	AP-2 complex subunit alpha-2		HUMAN		939	UniRef50_P17427
AP-2 complex subunit alpha-2		BOVIN		938
AP-2 complex subunit alpha-2	)	RAT		938
MKIAA0899 protein (Fragment)		MOUSE		967
AP-2 complex subunit alpha		FELCA		977
+497

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
CCDSⁱ	CCDS40188.1
PIRⁱ	B30111 S12471
RefSeqⁱ	NP_031485.3, NM_007459.3
UniGeneⁱ	Mm.253090

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
ProteinModelPortalⁱ	P17427
SMRⁱ	P17427
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	198130, 17 interactors
CORUMⁱ	P17427
DIPⁱ	DIP-32160N
IntActⁱ	P17427, 24 interactors
MINTⁱ	P17427
STRINGⁱ	10090.ENSMUSP00000003038

PTM databases

iPTMnetⁱ	P17427
PhosphoSitePlusⁱ	P17427
SwissPalmⁱ	P17427

Proteomic databases

EPDⁱ	P17427
MaxQBⁱ	P17427
PaxDbⁱ	P17427
PeptideAtlasⁱ	P17427
PRIDEⁱ	P17427

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957
GeneIDⁱ	11772
KEGGⁱ	mmu:11772
UCSCⁱ	uc009kls.2 mouse

Organism-specific databases

CTDⁱ	161
MGIⁱ	MGI:101920 Ap2a2

Phylogenomic databases

eggNOGⁱ	KOG1077 Eukaryota ENOG410XNQE LUCA
GeneTreeⁱ	ENSGT00550000074757
HOVERGENⁱ	HBG050518
InParanoidⁱ	P17427
KOⁱ	K11824
OMAⁱ	FMNLALH
OrthoDBⁱ	EOG091G01JZ
TreeFamⁱ	TF300308

Enzyme and pathway databases

Reactomeⁱ	R-MMU-177504 Retrograde neurotrophin signalling R-MMU-2132295 MHC class II antigen presentation R-MMU-416993 Trafficking of GluR2-containing AMPA receptors R-MMU-437239 Recycling pathway of L1 R-MMU-5099900 WNT5A-dependent internalization of FZD4 R-MMU-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2 R-MMU-6798695 Neutrophil degranulation R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis R-MMU-8856828 Clathrin-mediated endocytosis R-MMU-8866427 VLDLR internalisation and degradation R-MMU-8964038 LDL clearance

Reactomeⁱ

R-MMU-177504 Retrograde neurotrophin signalling
R-MMU-2132295 MHC class II antigen presentation
R-MMU-416993 Trafficking of GluR2-containing AMPA receptors
R-MMU-437239 Recycling pathway of L1
R-MMU-5099900 WNT5A-dependent internalization of FZD4
R-MMU-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2
R-MMU-6798695 Neutrophil degranulation
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8866427 VLDLR internalisation and degradation
R-MMU-8964038 LDL clearance

Miscellaneous databases

ChiTaRSⁱ	Ap2a2 mouse
EvolutionaryTraceⁱ	P17427
PMAP-CutDBⁱ	P17427
Protein Ontology More...PROⁱ	PR:P17427
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000002957 Expressed in 295 organ(s), highest expression level in embryo
CleanExⁱ	MM_AP2A2
ExpressionAtlasⁱ	P17427 baseline and differential
Genevisibleⁱ	P17427 MM

Family and domain databases

Gene3Dⁱ	1.25.10.10, 1 hit 3.30.310.10, 1 hit
InterProⁱ	View protein in InterPro IPR017104 AP2_complex_asu IPR011989 ARM-like IPR016024 ARM-type_fold IPR002553 Clathrin/coatomer_adapt-like_N IPR003164 Clathrin_a-adaptin_app_sub_C IPR008152 Clathrin_a/b/g-adaptin_app_Ig IPR013041 Clathrin_app_Ig-like_sf IPR009028 Coatomer/calthrin_app_sub_C IPR012295 TBP_dom_sf
Pfamⁱ	View protein in Pfam PF01602 Adaptin_N, 1 hit PF02296 Alpha_adaptin_C, 1 hit PF02883 Alpha_adaptinC2, 1 hit
PIRSFⁱ	PIRSF037091 AP2_complex_alpha, 1 hit
SMARTⁱ	View protein in SMART SM00809 Alpha_adaptinC2, 1 hit
SUPFAMⁱ	SSF48371 SSF48371, 1 hit SSF49348 SSF49348, 1 hit SSF55711 SSF55711, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AP2A2_MOUSE
Accessionⁱ	P17427Primary (citable) accession number: P17427 Secondary accession number(s): Q8C2J5, Q921V0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
	Last sequence update:	July 27, 2011
	Last modified:	September 12, 2018
	This is version 187 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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UniProtKB - P17427 (AP2A2_MOUSE)

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AP-2 complex subunit alpha-2

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ