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Protein

AP-2 complex subunit alpha-2

Gene

Ap2a2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431Phosphatidylinositol lipid headgroup
Binding sitei53 – 531Phosphatidylinositol lipid headgroup
Binding sitei57 – 571Phosphatidylinositol lipid headgroup
Binding sitei58 – 581Phosphatidylinositol lipid headgroup
Binding sitei61 – 611Phosphatidylinositol lipid headgroup

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW
  2. protein kinase binding Source: ParkinsonsUK-UCL
  3. protein transporter activity Source: InterPro

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. intracellular protein transport Source: MGI
  3. regulation of hematopoietic stem cell differentiation Source: BHF-UCL
  4. vesicle-mediated transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_299462. WNT5A-dependent internalization of FZD4.
REACT_304279. Retrograde neurotrophin signalling.
REACT_316383. MHC class II antigen presentation.
REACT_322343. Trafficking of GluR2-containing AMPA receptors.
REACT_350802. EGFR downregulation.
REACT_353475. Recycling pathway of L1.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:101920. Ap2a2.

Subcellular locationi

Cell membrane. Membranecoated 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.

GO - Cellular componenti

  1. clathrin adaptor complex Source: InterPro
  2. coated pit Source: UniProtKB-SubCell
  3. cytoplasmic membrane-bounded vesicle Source: BHF-UCL
  4. membrane coat Source: MGI
  5. plasma membrane Source: UniProtKB-SubCell
  6. secretory granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211R → E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15. 1 Publication
Mutagenesisi31 – 311K → Q: Reduces phosphatidylinositol binding. 1 Publication
Mutagenesisi32 – 321R → Q: Reduces phosphatidylinositol binding. 1 Publication
Mutagenesisi35 – 351K → Q: Reduces phosphatidylinositol binding. 1 Publication
Mutagenesisi45 – 451K → Q: Reduces phosphatidylinositol binding. 1 Publication
Mutagenesisi55 – 551K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. 1 Publication
Mutagenesisi56 – 561K → E: Strongly reduces phosphatidylinositol binding. 1 Publication
Mutagenesisi56 – 561K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57. 1 Publication
Mutagenesisi57 – 571K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56. 1 Publication
Mutagenesisi61 – 611K → Q: Reduces phosphatidylinositol binding. 1 Publication
Mutagenesisi727 – 7271K → A: No effect on DENND1A-,DENND1B- nor DENND1C-binding.
Mutagenesisi782 – 7821Q → A: Reduces DENND1A- and DENND1C-binding. 1 Publication
Mutagenesisi837 – 8371F → 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
Mutagenesisi840 – 8401W → A: Abolishes AMPH, BIN1, EPS15, EPN1, auxilin and SNAP91 binding. Abolishes interaction with DGKD. 2 Publications
Mutagenesisi849 – 8491E → A: No effect. 1 Publication
Mutagenesisi905 – 9051R → A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837. 2 Publications
Mutagenesisi907 – 9071E → A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding. 1 Publication
Mutagenesisi916 – 9161R → 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
Mutagenesisi920 – 9201R → A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 938937AP-2 complex subunit alpha-2PRO_0000193733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei653 – 6531PhosphoserineBy similarity
Modified residuei654 – 6541PhosphothreonineBy similarity
Modified residuei656 – 6561PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP17427.
PaxDbiP17427.
PRIDEiP17427.

PTM databases

PhosphoSiteiP17427.

Miscellaneous databases

PMAP-CutDBP17427.

Expressioni

Gene expression databases

BgeeiP17427.
CleanExiMM_AP2A2.
ExpressionAtlasiP17427. baseline and differential.
GenevestigatoriP17427.

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.By similarity11 Publications

Protein-protein interaction databases

BioGridi198130. 12 interactions.
DIPiDIP-32160N.
IntActiP17427. 17 interactions.
MINTiMINT-101068.

Structurei

Secondary structure

1
938
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2212Combined sources
Helixi28 – 4013Combined sources
Turni41 – 433Combined sources
Beta strandi44 – 485Combined sources
Helixi52 – 6615Combined sources
Turni67 – 693Combined sources
Helixi76 – 827Combined sources
Helixi88 – 10013Combined sources
Helixi106 – 12116Combined sources
Helixi125 – 13814Combined sources
Helixi141 – 1477Combined sources
Helixi150 – 1567Combined sources
Helixi162 – 17817Combined sources
Helixi180 – 1823Combined sources
Helixi188 – 1936Combined sources
Helixi194 – 1974Combined sources
Helixi201 – 21414Combined sources
Turni215 – 2173Combined sources
Helixi219 – 2224Combined sources
Helixi225 – 23814Combined sources
Beta strandi241 – 2444Combined sources
Turni245 – 2473Combined sources
Beta strandi252 – 2543Combined sources
Helixi255 – 26511Combined sources
Helixi273 – 29119Combined sources
Helixi299 – 31921Combined sources
Helixi323 – 33816Combined sources
Helixi343 – 35513Combined sources
Beta strandi359 – 3613Combined sources
Helixi364 – 3685Combined sources
Helixi369 – 37810Combined sources
Helixi382 – 39312Combined sources
Turni398 – 4003Combined sources
Helixi401 – 41313Combined sources
Helixi417 – 43418Combined sources
Helixi438 – 45013Combined sources
Helixi453 – 4553Combined sources
Helixi458 – 47013Combined sources
Helixi475 – 48511Combined sources
Beta strandi488 – 4903Combined sources
Helixi493 – 50513Combined sources
Helixi508 – 5103Combined sources
Helixi514 – 5163Combined sources
Helixi518 – 52912Combined sources
Helixi534 – 55017Combined sources
Turni552 – 5543Combined sources
Helixi555 – 5628Combined sources
Helixi565 – 5684Combined sources
Helixi573 – 58816Combined sources
Helixi591 – 5977Combined sources
Beta strandi610 – 6134Combined sources
Beta strandi617 – 6204Combined sources
Turni701 – 7044Combined sources
Helixi705 – 7084Combined sources
Beta strandi714 – 7185Combined sources
Beta strandi720 – 73112Combined sources
Beta strandi734 – 74310Combined sources
Beta strandi745 – 7473Combined sources
Beta strandi749 – 7579Combined sources
Helixi760 – 7656Combined sources
Beta strandi766 – 7705Combined sources
Beta strandi782 – 79110Combined sources
Beta strandi800 – 8078Combined sources
Beta strandi810 – 8178Combined sources
Helixi822 – 8254Combined sources
Beta strandi826 – 8283Combined sources
Helixi833 – 8408Combined sources
Helixi846 – 8483Combined sources
Beta strandi849 – 8557Combined sources
Helixi862 – 87211Combined sources
Beta strandi874 – 8774Combined sources
Beta strandi879 – 8835Combined sources
Beta strandi886 – 8949Combined sources
Beta strandi899 – 90911Combined sources
Turni910 – 9134Combined sources
Beta strandi914 – 92310Combined sources
Helixi924 – 93512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9KX-ray1.90A701-938[»]
1KY6X-ray2.00A701-938[»]
1KY7X-ray2.15A701-938[»]
1KYDX-ray2.00A701-938[»]
1KYFX-ray1.22A701-938[»]
1KYUX-ray1.80A701-938[»]
1QTPX-ray1.60A701-938[»]
1QTSX-ray1.40A701-938[»]
1W80X-ray1.90A695-938[»]
2JKRX-ray2.98A/L1-620[»]
2JKTX-ray3.40A/L1-620[»]
2VJ0X-ray1.60A695-938[»]
3HS8X-ray1.90A702-938[»]
ProteinModelPortaliP17427.
SMRiP17427. Positions 9-607, 701-938.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17427.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 8076Lipid-bindingAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5096.
GeneTreeiENSGT00550000074757.
HOVERGENiHBG050518.
InParanoidiP17427.
KOiK11824.
OMAiFMEAPIL.
OrthoDBiEOG7GQXV2.
TreeFamiTF300308.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProiIPR017104. 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]
PfamiPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17427-1 [UniParc]FASTAAdd 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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti858 – 8592HP → LE in AAH10597 (PubMed:15489334).Curated
Sequence conflicti889 – 8902GA → VL in CAA33097 (PubMed:2564002).Curated
Sequence conflicti889 – 8902GA → VL in AAB62703 (PubMed:9618202).Curated

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.
CCDSiCCDS40188.1.
PIRiB30111.
S12471.
RefSeqiNP_031485.3. NM_007459.3.
UniGeneiMm.253090.

Genome annotation databases

EnsembliENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957.
GeneIDi11772.
KEGGimmu:11772.
UCSCiuc009kls.2. mouse.

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.
CCDSiCCDS40188.1.
PIRiB30111.
S12471.
RefSeqiNP_031485.3. NM_007459.3.
UniGeneiMm.253090.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9KX-ray1.90A701-938[»]
1KY6X-ray2.00A701-938[»]
1KY7X-ray2.15A701-938[»]
1KYDX-ray2.00A701-938[»]
1KYFX-ray1.22A701-938[»]
1KYUX-ray1.80A701-938[»]
1QTPX-ray1.60A701-938[»]
1QTSX-ray1.40A701-938[»]
1W80X-ray1.90A695-938[»]
2JKRX-ray2.98A/L1-620[»]
2JKTX-ray3.40A/L1-620[»]
2VJ0X-ray1.60A695-938[»]
3HS8X-ray1.90A702-938[»]
ProteinModelPortaliP17427.
SMRiP17427. Positions 9-607, 701-938.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198130. 12 interactions.
DIPiDIP-32160N.
IntActiP17427. 17 interactions.
MINTiMINT-101068.

PTM databases

PhosphoSiteiP17427.

Proteomic databases

MaxQBiP17427.
PaxDbiP17427.
PRIDEiP17427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957.
GeneIDi11772.
KEGGimmu:11772.
UCSCiuc009kls.2. mouse.

Organism-specific databases

CTDi161.
MGIiMGI:101920. Ap2a2.

Phylogenomic databases

eggNOGiCOG5096.
GeneTreeiENSGT00550000074757.
HOVERGENiHBG050518.
InParanoidiP17427.
KOiK11824.
OMAiFMEAPIL.
OrthoDBiEOG7GQXV2.
TreeFamiTF300308.

Enzyme and pathway databases

ReactomeiREACT_299462. WNT5A-dependent internalization of FZD4.
REACT_304279. Retrograde neurotrophin signalling.
REACT_316383. MHC class II antigen presentation.
REACT_322343. Trafficking of GluR2-containing AMPA receptors.
REACT_350802. EGFR downregulation.
REACT_353475. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSiAp2a2. mouse.
EvolutionaryTraceiP17427.
NextBioi279555.
PMAP-CutDBP17427.
PROiP17427.
SOURCEiSearch...

Gene expression databases

BgeeiP17427.
CleanExiMM_AP2A2.
ExpressionAtlasiP17427. baseline and differential.
GenevestigatoriP17427.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProiIPR017104. 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]
PfamiPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins)."
    Robinson M.S.
    J. Cell Biol. 108:833-842(1988) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Thymus.
  3. 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(2003) [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(1997) [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(1998) [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(2000) [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(2002) [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(2002) [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(2003) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DKGD, MUTAGENESIS OF TRP-840.
  13. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DENND1A; DENND1B AND DENND1C, MUTAGENESIS OF GLN-782 AND ARG-916.
  14. "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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO1.
  15. Cited for: INTERACTION WITH ATAT1.
  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(1998) [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(2001) [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(2001) [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(1998) [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(2007) [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.

Entry informationi

Entry nameiAP2A2_MOUSE
AccessioniPrimary (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: April 1, 2015
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.