O94973 (AP2A2_HUMAN) 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
Huntingtin yeast partner J
Huntingtin-interacting protein 9
Short name=HIP-9
Huntingtin-interacting protein J
Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit

Gene names

Name:	AP2A2
Synonyms:	ADTAB, CLAPA2, HIP9, HYPJ, KIAA0899

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	939 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 By similarity. Ref.8 Ref.9 Ref.10 Ref.11
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. Interacts with DGKD isoform 2 By similarity. Interacts with DENND1A, DENND1B and DENND1C By similarity. Interacts with FCHO1 and DAB2. Ref.7 Ref.13
Subcellular location	Cell membrane By similarity. Membrane › coated pit; Peripheral membrane protein; Cytoplasmic side By similarity. Note: AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV By similarity.
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
Coding sequence diversity	Alternative splicing
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome axon guidance Traceable author statement. Source: Reactome endocytosis Inferred from electronic annotation. Source: UniProtKB-KW epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome intracellular protein transport Non-traceable author statement. Source: UniProtKB negative regulation of epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome regulation of defense response to virus by virus Traceable author statement. Source: Reactome synaptic transmission Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	AP-2 adaptor complex Non-traceable author statement. Source: UniProtKB cytosol Traceable author statement. Source: Reactome
Molecular_function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW protein transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dab2	P98078	2	EBI-1642835,EBI-1391846	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O94973-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O94973-2)

The sequence of this isoform differs from the canonical sequence as follows:
     271-271: P → PE

Note: No experimental confirmation available.

Isoform 3 (identifier: O94973-3)

The sequence of this isoform differs from the canonical sequence as follows:
     271-271: P → PE
     653-655: STP → VCL
     656-939: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 939	938	AP-2 complex subunit alpha-2		PRO_0000193732
Regions
	Region	5 – 80	76	Lipid-binding
Sites
	Binding site	43	1	Phosphatidylinositol lipid headgroup By similarity
	Binding site	53	1	Phosphatidylinositol lipid headgroup By similarity
	Binding site	57	1	Phosphatidylinositol lipid headgroup By similarity
	Binding site	58	1	Phosphatidylinositol lipid headgroup By similarity
	Binding site	61	1	Phosphatidylinositol lipid headgroup By similarity
Amino acid modifications
	Modified residue	808	1	Phosphotyrosine By similarity
Natural variations
	Alternative sequence	271	1	P → PE in isoform 2 and isoform 3.		VSP_035762
	Alternative sequence	653 – 655	3	STP → VCL in isoform 3.		VSP_035763
	Alternative sequence	656 – 939	284	Missing in isoform 3.		VSP_035764
Experimental info
	Sequence conflict	20	1	I → T in BAB55435. Ref.4
	Sequence conflict	450	1	R → Q in AAC27505. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 24, 2001. Version 2. Checksum: A8D3CC1B15B8C6BF	FASTA	939	103,960
	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 ALHCIASVGS REMAEAFAGE IPKVLVAGDT 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 APQIVAEMLS YLETADYSIR 430 440 450 460 470 480 EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK 490 500 510 520 530 540 TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFHLLHSKFH LCSVPTRALL 550 560 570 580 590 600 LSTYIKFVNL FPEVKPTIQD VLRSDSQLRN ADVELQQRAV EYLRLSTVAS TDILATVLEE 610 620 630 640 650 660 MPPFPERESS ILAKLKKKKG PSTVTDLEDT KRDRSVDVNG GPEPAPASTS AVSTPSPSAD 670 680 690 700 710 720 LLGLGAAPPA PAGPPPSSGG SGLLVDVFSD SASVVAPLAP GSEDNFARFV CKNNGVLFEN 730 740 750 760 770 780 QLLQIGLKSE FRQNLGRMFI FYGNKTSTQF LNFTPTLICS DDLQPNLNLQ TKPVDPTVEG 790 800 810 820 830 840 GAQVQQVVNI ECVSDFTEAP VLNIQFRYGG TFQNVSVQLP ITLNKFFQPT EMASQDFFQR 850 860 870 880 890 900 WKQLSNPQQE VQNIFKAKHP MDTEVTKAKI IGFGSALLEE VDPNPANFVG AGIIHTKTTQ 910 920 930 IGCLLRLEPN LQAQMYRLTL RTSKEAVSQR LCELLSAQF
	Isoform 2 [UniParc]. Checksum: 98F8345F9BBB149C	FASTA	940	104,090
	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 ALHCIASVGS REMAEAFAGE IPKVLVAGDT MDSVKQSAAL CLLRLYRTSP 190 200 210 220 230 240 DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA 250 260 270 280 290 300 STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDPAVRGRL TECLETILNK AQEPPKSKKV 310 320 330 340 350 360 QHSNAKNAVL FEAISLIIHH DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE 370 380 390 400 410 420 FSHEAVKTHI ETVINALKTE RDVSVRQRAV DLLYAMCDRS NAPQIVAEML SYLETADYSI 430 440 450 460 470 480 REEIVLKVAI LAEKYAVDYT WYVDTILNLI RIAGDYVSEE VWYRVIQIVI NRDDVQGYAA 490 500 510 520 530 540 KTVFEALQAP ACHENLVKVG GYILGEFGNL IAGDPRSSPL IQFHLLHSKF HLCSVPTRAL 550 560 570 580 590 600 LLSTYIKFVN LFPEVKPTIQ DVLRSDSQLR NADVELQQRA VEYLRLSTVA STDILATVLE 610 620 630 640 650 660 EMPPFPERES SILAKLKKKK GPSTVTDLED TKRDRSVDVN GGPEPAPAST SAVSTPSPSA 670 680 690 700 710 720 DLLGLGAAPP APAGPPPSSG GSGLLVDVFS DSASVVAPLA PGSEDNFARF VCKNNGVLFE 730 740 750 760 770 780 NQLLQIGLKS EFRQNLGRMF IFYGNKTSTQ FLNFTPTLIC SDDLQPNLNL QTKPVDPTVE 790 800 810 820 830 840 GGAQVQQVVN IECVSDFTEA PVLNIQFRYG GTFQNVSVQL PITLNKFFQP TEMASQDFFQ 850 860 870 880 890 900 RWKQLSNPQQ EVQNIFKAKH PMDTEVTKAK IIGFGSALLE EVDPNPANFV GAGIIHTKTT 910 920 930 940 QIGCLLRLEP NLQAQMYRLT LRTSKEAVSQ RLCELLSAQF
	Isoform 3 [UniParc]. Checksum: 98E2FE160BFAC0AC	FASTA	656	73,128
	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 ALHCIASVGS REMAEAFAGE IPKVLVAGDT MDSVKQSAAL CLLRLYRTSP 190 200 210 220 230 240 DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA 250 260 270 280 290 300 STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDPAVRGRL TECLETILNK AQEPPKSKKV 310 320 330 340 350 360 QHSNAKNAVL FEAISLIIHH DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE 370 380 390 400 410 420 FSHEAVKTHI ETVINALKTE RDVSVRQRAV DLLYAMCDRS NAPQIVAEML SYLETADYSI 430 440 450 460 470 480 REEIVLKVAI LAEKYAVDYT WYVDTILNLI RIAGDYVSEE VWYRVIQIVI NRDDVQGYAA 490 500 510 520 530 540 KTVFEALQAP ACHENLVKVG GYILGEFGNL IAGDPRSSPL IQFHLLHSKF HLCSVPTRAL 550 560 570 580 590 600 LLSTYIKFVN LFPEVKPTIQ DVLRSDSQLR NADVELQQRA VEYLRLSTVA STDILATVLE 610 620 630 640 650 EMPPFPERES SILAKLKKKK GPSTVTDLED TKRDRSVDVN GGPEPAPAST SAVVCL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]	"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] (ISOFORM 1). Tissue: Brain.
[6]	"Huntingtin interacts with a family of WW domain proteins." Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F., MacDonald M.E. Hum. Mol. Genet. 7:1463-1474(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 318-476. Tissue: Testis.
[7]	"The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis." Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R., Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H., Wanker E.E. Hum. Mol. Genet. 10:1807-1817(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIP1.
[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]	"Effect of clathrin heavy chain- and alpha-adaptin-specific small inhibitory RNAs on endocytic accessory proteins and receptor trafficking in HeLa cells." Hinrichsen L., Harborth J., Andrees L., Weber K., Ungewickell E.J. J. Biol. Chem. 278:45160-45170(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[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]	"The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway." Lau A.W., Chou M.M. J. Cell Sci. 121:4008-4017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB020706 mRNA. Translation: BAA74922.2. AK223558 mRNA. Translation: BAD97278.1. AK027891 mRNA. Translation: BAB55435.1. BC006155 mRNA. Translation: AAH06155.1. AF049527 mRNA. Translation: AAC27505.1.
IPI	IPI00016621. IPI00914938. IPI00914952.
RefSeq	NP_001229766.1. NM_001242837.1. NP_036437.1. NM_012305.3.
UniGene	Hs.19121.
3D structure databases
ProteinModelPortal	O94973.
ModBase	Search...
Protein-protein interaction databases
IntAct	O94973. 13 interactions.
MINT	MINT-1198502.
STRING	9606.ENSP00000413234.
PTM databases
PhosphoSite	O94973.
Proteomic databases
PaxDb	O94973.
PRIDE	O94973.
Protocols and materials databases
DNASU	161.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000332231; ENSP00000327694; ENSG00000183020. ENST00000448903; ENSP00000413234; ENSG00000183020. ENST00000528815; ENSP00000431630; ENSG00000183020.
GeneID	161.
KEGG	hsa:161.
UCSC	uc001lss.3. human. uc001lst.2. human.
Organism-specific databases
CTD	161.
GeneCards	GC11P000915.
HGNC	HGNC:562. AP2A2.
HPA	CAB017514.
MIM	607242. gene.
neXtProt	NX_O94973.
PharmGKB	PA24853.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5096.
HOGENOM	HOG000170596.
HOVERGEN	HBG050518.
InParanoid	O94973.
KO	K11824.
OMA	PNKQAQM.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_13685. Neuronal System. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	O94973.
Bgee	O94973.
CleanEx	HS_AP2A2.
Genevestigator	O94973.
GermOnline	ENSG00000183020. Homo sapiens.
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. human.
GenomeRNAi	161.
NextBio	643.
PMAP-CutDB	O94973.
SOURCE	Search...

Entry information

Entry name

AP2A2_HUMAN

Accession

Primary (citable) accession number: O94973
Secondary accession number(s): O75403, Q53ET1, Q96SI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 24, 2001
Last modified:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.