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P17427 (AP2A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP-2 complex subunit alpha-2
Alternative name(s):
100 kDa coated vesicle protein C
Adapter-related protein complex 2 subunit alpha-2
Adaptor protein complex AP-2 subunit alpha-2
Alpha-adaptin C
Alpha2-adaptin
Clathrin assembly protein complex 2 alpha-C large chain
Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit
Gene names
Name:Ap2a2
Synonyms:Adtab
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length938 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. Ref.6 Ref.8 Ref.10

Subunit structure

Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Binds EPN1, EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1 By similarity. Interacts with DGKD isoform 2 Interacts with DENND1A, DENND1B and DENND1C. Interacts with FCHO1 and DAB2. Interacts with ATAT1; this interaction is required for efficient alpha-tubulin acetylation by ATAT1. Ref.6 Ref.7 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19

Subcellular location

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. Ref.9 Ref.11

Sequence similarities

Belongs to the adaptor complexes large subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 938937AP-2 complex subunit alpha-2
PRO_0000193733

Regions

Region5 – 8076Lipid-binding

Sites

Binding site431Phosphatidylinositol lipid headgroup
Binding site531Phosphatidylinositol lipid headgroup
Binding site571Phosphatidylinositol lipid headgroup
Binding site581Phosphatidylinositol lipid headgroup
Binding site611Phosphatidylinositol lipid headgroup

Experimental info

Mutagenesis211R → E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15. Ref.20
Mutagenesis311K → Q: Reduces phosphatidylinositol binding. Ref.6
Mutagenesis321R → Q: Reduces phosphatidylinositol binding. Ref.6
Mutagenesis351K → Q: Reduces phosphatidylinositol binding. Ref.6
Mutagenesis451K → Q: Reduces phosphatidylinositol binding. Ref.6
Mutagenesis551K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. Ref.6
Mutagenesis561K → E: Strongly reduces phosphatidylinositol binding. Ref.6
Mutagenesis561K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57. Ref.6
Mutagenesis571K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56. Ref.6
Mutagenesis611K → Q: Reduces phosphatidylinositol binding. Ref.6
Mutagenesis7271K → A: No effect on DENND1A-,DENND1B- nor DENND1C-binding.
Mutagenesis7821Q → A: Reduces DENND1A- and DENND1C-binding. Ref.13
Mutagenesis8371F → A: Reduces SNAP91, AMPH and BIN1 binding. Abolishes AMPH and SNAP91 binding; when associated with A-916. Abolishes EPN1 and EPS15 binding; when associated with A-905. Ref.16 Ref.19
Mutagenesis8401W → A: Abolishes AMPH, BIN1, EPS15, EPN1, auxilin and SNAP91 binding. Abolishes interaction with DGKD. Ref.12 Ref.16
Mutagenesis8491E → A: No effect. Ref.16
Mutagenesis9051R → A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837. Ref.16 Ref.19
Mutagenesis9071E → A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding. Ref.16
Mutagenesis9161R → A: Strongly reduces AMPH and SNAP91 binding. Abolishes DENND1B-binding; no effect on DENND1A-, nor DENND1C-binding. Abolishes AMPH and SNAP91 binding; when associated with A-837. Ref.13 Ref.19
Mutagenesis9201R → A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding. Ref.16
Sequence conflict858 – 8592HP → LE in AAH10597. Ref.4
Sequence conflict889 – 8902GA → VL in CAA33097. Ref.1
Sequence conflict889 – 8902GA → VL in AAB62703. Ref.5

Secondary structure

.......................................................................................................................................... 938
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17427 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 183FE8DFE199DBCA

FASTA938104,017
        10         20         30         40         50         60 
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC 

        70         80         90        100        110        120 
KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL 

       130        140        150        160        170        180 
ASRNPTFMGL ALHCIANVGS REMAEAFAGE IPKILVAGDT MDSVKQSAAL CLLRLYRTSP 

       190        200        210        220        230        240 
DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA 

       250        260        270        280        290        300 
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ 

       310        320        330        340        350        360 
HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF 

       370        380        390        400        410        420 
SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN AQQIVAEMLS YLETADYSIR 

       430        440        450        460        470        480 
EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK 

       490        500        510        520        530        540 
TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL 

       550        560        570        580        590        600 
LSTYIKFVNL FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE 

       610        620        630        640        650        660 
MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS AASTPSPSAD 

       670        680        690        700        710        720 
LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG SEDNFARFVC KNNGVLFENQ 

       730        740        750        760        770        780 
LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL NFTPTLICAD DLQTNLNLQT KPVDPTVDGG 

       790        800        810        820        830        840 
AQVQQVVNIE CISDFTEAPV LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW 

       850        860        870        880        890        900 
KQLSNPQQEV QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI 

       910        920        930 
GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins)."
Robinson M.S.
J. Cell Biol. 108:833-842(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-859.
Tissue: Mammary tumor.
[5]"Identification and cloning of differentially expressed genes by long-distance differential display."
Jurecic R., Nachtman R.G., Colicos S.M., Belmont J.W.
Anal. Biochem. 259:235-244(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 379-938.
Tissue: Fetal liver.
[6]"Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits."
Gaidarov I., Keen J.H.
J. Cell Biol. 146:755-764(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CLATHRIN, MUTAGENESIS OF LYS-31; ARG-32; LYS-35; LYS-45; LYS-55; LYS-56; LYS-57 AND LYS-61.
[7]"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2."
Morris S.M., Cooper J.A.
Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[8]"Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network."
Nakatsu F., Ohno H.
Cell Struct. Funct. 28:419-429(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[9]"The AP-2 complex is excluded from the dynamic population of plasma membrane-associated clathrin."
Rappoport J.Z., Taha B.W., Lemeer S., Benmerah A., Simon S.M.
J. Biol. Chem. 278:47357-47360(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Adaptors for clathrin coats: structure and function."
Owen D.J., Collins B.M., Evans P.R.
Annu. Rev. Cell Dev. Biol. 20:153-191(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[11]"Dynamics of clathrin and adaptor proteins during endocytosis."
Rappoport J.Z., Kemal S., Benmerah A., Simon S.M.
Am. J. Physiol. 291:C1072-C1081(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"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]"alphaTAT1 catalyses microtubule acetylation at clathrin-coated pits."
Montagnac G., Meas-Yedid V., Irondelle M., Castro-Castro A., Franco M., Shida T., Nachury M.V., Benmerah A., Olivo-Marin J.C., Chavrier P.
Nature 502:567-570(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14972 mRNA. Translation: CAA33097.1.
AK088500 mRNA. Translation: BAC40392.1.
AC158224 Genomic DNA. No translation available.
AC102524 Genomic DNA. No translation available.
BC010597 mRNA. Translation: AAH10597.1.
AF006990 mRNA. Translation: AAB62703.1.
PIRB30111.
S12471.
RefSeqNP_031485.3. NM_007459.3.
UniGeneMm.253090.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP17427.
SMRP17427. Positions 9-607, 701-938.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198130. 10 interactions.
DIPDIP-32160N.
IntActP17427. 17 interactions.
MINTMINT-101068.

PTM databases

PhosphoSiteP17427.

Proteomic databases

PaxDbP17427.
PRIDEP17427.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957.
GeneID11772.
KEGGmmu:11772.
UCSCuc009kls.2. mouse.

Organism-specific databases

CTD161.
MGIMGI:101920. Ap2a2.

Phylogenomic databases

eggNOGCOG5096.
GeneTreeENSGT00550000074757.
HOVERGENHBG050518.
InParanoidQ8C2J5.
KOK11824.
OMAPNKQAQM.
OrthoDBEOG7GQXV2.
TreeFamTF300308.

Gene expression databases

ArrayExpressP17427.
BgeeP17427.
CleanExMM_AP2A2.
GenevestigatorP17427.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
2.60.40.1030. 1 hit.
3.30.310.30. 1 hit.
InterProIPR017104. 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]
PfamPF01602. Adaptin_N. 1 hit.
PF02296. Alpha_adaptin_C. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFPIRSF037091. AP2_complex_alpha. 1 hit.
SMARTSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAP2A2. mouse.
EvolutionaryTraceP17427.
NextBio279555.
PMAP-CutDBP17427.
PROP17427.
SOURCESearch...

Entry information

Entry nameAP2A2_MOUSE
AccessionPrimary (citable) accession number: P17427
Secondary accession number(s): Q8C2J5, Q921V0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot