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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)DescriptionActionsGraphical viewLength
Binding sitei43Phosphatidylinositol lipid headgroup1
Binding sitei53Phosphatidylinositol lipid headgroup1
Binding sitei57Phosphatidylinositol lipid headgroup1
Binding sitei58Phosphatidylinositol lipid headgroup1
Binding sitei61Phosphatidylinositol lipid headgroup1

GO - Molecular functioni

  • lipid binding Source: UniProtKB-KW
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein transporter activity Source: InterPro

GO - Biological processi

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

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-171052. LDL-mediated lipid transport.
R-MMU-177504. Retrograde neurotrophin signalling.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-416993. Trafficking of GluR2-containing AMPA receptors.
R-MMU-437239. Recycling pathway of L1.
R-MMU-5099900. WNT5A-dependent internalization of FZD4.
R-MMU-5140745. WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.
R-MMU-8866427. VLDLR internalisation and degradation.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:101920. Ap2a2.

Subcellular locationi

GO - Cellular componenti

  • clathrin adaptor complex Source: InterPro
  • clathrin-coated pit Source: UniProtKB-SubCell
  • cytoplasmic, membrane-bounded vesicle Source: BHF-UCL
  • membrane coat Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
  • secretory granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21R → E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15. 1 Publication1
Mutagenesisi31K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi32R → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi35K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi45K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi55K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. 1 Publication1
Mutagenesisi56K → E: Strongly reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi56K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57. 1 Publication1
Mutagenesisi57K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56. 1 Publication1
Mutagenesisi61K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi727K → A: No effect on DENND1A-,DENND1B- nor DENND1C-binding. 1
Mutagenesisi782Q → A: Reduces DENND1A- and DENND1C-binding. 1 Publication1
Mutagenesisi837F → 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 Publications1
Mutagenesisi840W → A: Abolishes AMPH, BIN1, EPS15, EPN1, auxilin and SNAP91 binding. Abolishes interaction with DGKD. 2 Publications1
Mutagenesisi849E → A: No effect. 1 Publication1
Mutagenesisi905R → A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837. 2 Publications1
Mutagenesisi907E → A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding. 1 Publication1
Mutagenesisi916R → 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 Publications1
Mutagenesisi920R → A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001937332 – 938AP-2 complex subunit alpha-2Add BLAST937

Proteomic databases

EPDiP17427.
MaxQBiP17427.
PaxDbiP17427.
PeptideAtlasiP17427.
PRIDEiP17427.

PTM databases

iPTMnetiP17427.
PhosphoSitePlusiP17427.
SwissPalmiP17427.

Miscellaneous databases

PMAP-CutDBP17427.

Expressioni

Gene expression databases

BgeeiENSMUSG00000002957.
CleanExiMM_AP2A2.
ExpressionAtlasiP17427. baseline and differential.
GenevisibleiP17427. MM.

Interactioni

Subunit structurei

Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Binds EPN1, EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1 (By similarity). Interacts with DGKD isoform 2. Interacts with DENND1A, DENND1B and DENND1C. Interacts with FCHO1 and DAB2. Interacts with ATAT1; this interaction is required for efficient alpha-tubulin acetylation by ATAT1.By similarity11 Publications

GO - Molecular functioni

  • protein kinase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi198130. 12 interactors.
DIPiDIP-32160N.
IntActiP17427. 17 interactors.
MINTiMINT-101068.
STRINGi10090.ENSMUSP00000003038.

Structurei

Secondary structure

1938
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 22Combined sources12
Helixi28 – 40Combined sources13
Turni41 – 43Combined sources3
Beta strandi44 – 48Combined sources5
Helixi52 – 66Combined sources15
Turni67 – 69Combined sources3
Helixi76 – 82Combined sources7
Helixi88 – 100Combined sources13
Helixi106 – 121Combined sources16
Helixi125 – 138Combined sources14
Helixi141 – 147Combined sources7
Helixi150 – 156Combined sources7
Helixi162 – 178Combined sources17
Helixi180 – 182Combined sources3
Helixi188 – 193Combined sources6
Helixi194 – 197Combined sources4
Helixi201 – 214Combined sources14
Turni215 – 217Combined sources3
Helixi219 – 222Combined sources4
Helixi225 – 238Combined sources14
Beta strandi241 – 244Combined sources4
Turni245 – 247Combined sources3
Beta strandi252 – 254Combined sources3
Helixi255 – 265Combined sources11
Helixi273 – 291Combined sources19
Helixi299 – 319Combined sources21
Helixi323 – 338Combined sources16
Helixi343 – 355Combined sources13
Beta strandi359 – 361Combined sources3
Helixi364 – 368Combined sources5
Helixi369 – 378Combined sources10
Helixi382 – 393Combined sources12
Turni398 – 400Combined sources3
Helixi401 – 413Combined sources13
Helixi417 – 434Combined sources18
Helixi438 – 450Combined sources13
Helixi453 – 455Combined sources3
Helixi458 – 470Combined sources13
Helixi475 – 485Combined sources11
Beta strandi488 – 490Combined sources3
Helixi493 – 505Combined sources13
Helixi508 – 510Combined sources3
Helixi514 – 516Combined sources3
Helixi518 – 529Combined sources12
Helixi534 – 550Combined sources17
Turni552 – 554Combined sources3
Helixi555 – 562Combined sources8
Helixi565 – 568Combined sources4
Helixi573 – 588Combined sources16
Helixi591 – 597Combined sources7
Beta strandi610 – 613Combined sources4
Beta strandi617 – 620Combined sources4
Turni701 – 704Combined sources4
Helixi705 – 708Combined sources4
Beta strandi714 – 718Combined sources5
Beta strandi720 – 731Combined sources12
Beta strandi734 – 743Combined sources10
Beta strandi745 – 747Combined sources3
Beta strandi749 – 757Combined sources9
Helixi760 – 765Combined sources6
Beta strandi766 – 770Combined sources5
Beta strandi782 – 791Combined sources10
Beta strandi800 – 807Combined sources8
Beta strandi810 – 817Combined sources8
Helixi822 – 825Combined sources4
Beta strandi826 – 828Combined sources3
Helixi833 – 840Combined sources8
Helixi846 – 848Combined sources3
Beta strandi849 – 855Combined sources7
Helixi862 – 872Combined sources11
Beta strandi874 – 877Combined sources4
Beta strandi879 – 883Combined sources5
Beta strandi886 – 894Combined sources9
Beta strandi899 – 909Combined sources11
Turni910 – 913Combined sources4
Beta strandi914 – 923Combined sources10
Helixi924 – 935Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17427.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni5 – 80Lipid-bindingAdd BLAST76

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1077. Eukaryota.
ENOG410XNQE. LUCA.
GeneTreeiENSGT00550000074757.
HOVERGENiHBG050518.
InParanoidiP17427.
KOiK11824.
OMAiPPFSERT.
OrthoDBiEOG091G01JZ.
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)DescriptionActionsGraphical viewLength
Sequence conflicti858 – 859HP → LE in AAH10597 (PubMed:15489334).Curated2
Sequence conflicti889 – 890GA → VL in CAA33097 (PubMed:2564002).Curated2
Sequence conflicti889 – 890GA → VL in AAB62703 (PubMed:9618202).Curated2

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198130. 12 interactors.
DIPiDIP-32160N.
IntActiP17427. 17 interactors.
MINTiMINT-101068.
STRINGi10090.ENSMUSP00000003038.

PTM databases

iPTMnetiP17427.
PhosphoSitePlusiP17427.
SwissPalmiP17427.

Proteomic databases

EPDiP17427.
MaxQBiP17427.
PaxDbiP17427.
PeptideAtlasiP17427.
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

eggNOGiKOG1077. Eukaryota.
ENOG410XNQE. LUCA.
GeneTreeiENSGT00550000074757.
HOVERGENiHBG050518.
InParanoidiP17427.
KOiK11824.
OMAiPPFSERT.
OrthoDBiEOG091G01JZ.
TreeFamiTF300308.

Enzyme and pathway databases

ReactomeiR-MMU-171052. LDL-mediated lipid transport.
R-MMU-177504. Retrograde neurotrophin signalling.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-416993. Trafficking of GluR2-containing AMPA receptors.
R-MMU-437239. Recycling pathway of L1.
R-MMU-5099900. WNT5A-dependent internalization of FZD4.
R-MMU-5140745. WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.
R-MMU-8866427. VLDLR internalisation and degradation.

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000002957.
CleanExiMM_AP2A2.
ExpressionAtlasiP17427. baseline and differential.
GenevisibleiP17427. MM.

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...

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: November 30, 2016
This is version 170 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

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 one 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.