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P17427

- AP2A2_MOUSE

UniProt

P17427 - AP2A2_MOUSE

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Protein

AP-2 complex subunit alpha-2

Gene

Ap2a2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. vesicle-mediated transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_202778. Retrograde neurotrophin signalling.
REACT_203917. EGFR downregulation.
REACT_222404. WNT5A-dependent internalization of FZD4.

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: 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-KW
  3. membrane coat Source: MGI
  4. plasma membrane Source: UniProtKB-KW
  5. 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

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. 11 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 – 2212
Helixi28 – 4013
Turni41 – 433
Beta strandi44 – 485
Helixi52 – 6615
Turni67 – 693
Helixi76 – 827
Helixi88 – 10013
Helixi106 – 12116
Helixi125 – 13814
Helixi141 – 1477
Helixi150 – 1567
Helixi162 – 17817
Helixi180 – 1823
Helixi188 – 1936
Helixi194 – 1974
Helixi201 – 21414
Turni215 – 2173
Helixi219 – 2224
Helixi225 – 23814
Beta strandi241 – 2444
Turni245 – 2473
Beta strandi252 – 2543
Helixi255 – 26511
Helixi273 – 29119
Helixi299 – 31921
Helixi323 – 33816
Helixi343 – 35513
Beta strandi359 – 3613
Helixi364 – 3685
Helixi369 – 37810
Helixi382 – 39312
Turni398 – 4003
Helixi401 – 41313
Helixi417 – 43418
Helixi438 – 45013
Helixi453 – 4553
Helixi458 – 47013
Helixi475 – 48511
Beta strandi488 – 4903
Helixi493 – 50513
Helixi508 – 5103
Helixi514 – 5163
Helixi518 – 52912
Helixi534 – 55017
Turni552 – 5543
Helixi555 – 5628
Helixi565 – 5684
Helixi573 – 58816
Helixi591 – 5977
Beta strandi610 – 6134
Beta strandi617 – 6204
Turni701 – 7044
Helixi705 – 7084
Beta strandi714 – 7185
Beta strandi720 – 73112
Beta strandi734 – 74310
Beta strandi745 – 7473
Beta strandi749 – 7579
Helixi760 – 7656
Beta strandi766 – 7705
Beta strandi782 – 79110
Beta strandi800 – 8078
Beta strandi810 – 8178
Helixi822 – 8254
Beta strandi826 – 8283
Helixi833 – 8408
Helixi846 – 8483
Beta strandi849 – 8557
Helixi862 – 87211
Beta strandi874 – 8774
Beta strandi879 – 8835
Beta strandi886 – 8949
Beta strandi899 – 90911
Turni910 – 9134
Beta strandi914 – 92310
Helixi924 – 93512

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiQDVFRQH.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 9-607, 701-938.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198130. 11 interactions.
DIPi DIP-32160N.
IntActi P17427. 17 interactions.
MINTi MINT-101068.

PTM databases

PhosphoSitei P17427.

Proteomic databases

MaxQBi P17427.
PaxDbi P17427.
PRIDEi P17427.

Protocols and materials databases

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 COG5096.
GeneTreei ENSGT00550000074757.
HOVERGENi HBG050518.
InParanoidi P17427.
KOi K11824.
OMAi QDVFRQH.
OrthoDBi EOG7GQXV2.
TreeFami TF300308.

Enzyme and pathway databases

Reactomei REACT_196550. MHC class II antigen presentation.
REACT_202778. Retrograde neurotrophin signalling.
REACT_203917. EGFR downregulation.
REACT_222404. WNT5A-dependent internalization of FZD4.

Miscellaneous databases

ChiTaRSi AP2A2. mouse.
EvolutionaryTracei P17427.
NextBioi 279555.
PMAP-CutDB P17427.
PROi P17427.
SOURCEi Search...

Gene expression databases

Bgeei P17427.
CleanExi MM_AP2A2.
ExpressionAtlasi P17427. baseline and differential.
Genevestigatori P17427.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProi 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 ]
Pfami PF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view ]
PIRSFi PIRSF037091. AP2_complex_alpha. 1 hit.
SMARTi SM00809. Alpha_adaptinC2. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNeti Search...

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(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. 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. "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.
  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(2010) [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(2012) [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(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.

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: October 29, 2014
This is version 151 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