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AP-2 complex subunit alpha-1 (100 kDa coated vesicle protein A) (Adaptor protein complex AP-2 subunit alpha-1) (Adaptor-related protein complex 2 subunit alpha-1) (Alpha-adaptin A) (Alpha1-adaptin) (Clathrin assembly protein complex 2 alpha-A large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit)

 AP2A1_HUMAN             Reviewed;         977 AA.
O95782; Q96CI7; Q96PP6; Q96PP7; Q9H070;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 3.
25-OCT-2017, entry version 167.
RecName: Full=AP-2 complex subunit alpha-1;
AltName: Full=100 kDa coated vesicle protein A;
AltName: Full=Adaptor protein complex AP-2 subunit alpha-1;
AltName: Full=Adaptor-related protein complex 2 subunit alpha-1;
AltName: Full=Alpha-adaptin A;
AltName: Full=Alpha1-adaptin;
AltName: Full=Clathrin assembly protein complex 2 alpha-A large chain;
AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit;
Name=AP2A1; Synonyms=ADTAA, CLAPA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
PubMed=12036598; DOI=10.1016/S0378-1119(02)00504-8;
Scorilas A., Levesque M.A., Ashworth L.K., Diamandis E.P.;
"Cloning, physical mapping and structural characterization of the
human alpha(A)-adaptin gene.";
Gene 289:191-199(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Uterus;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND VARIANT
LEU-270.
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH HIP1.
PubMed=11532990; DOI=10.1093/hmg/10.17.1807;
Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R.,
Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H.,
Wanker E.E.;
"The huntingtin interacting protein HIP1 is a clathrin and alpha-
adaptin-binding protein involved in receptor-mediated endocytosis.";
Hum. Mol. Genet. 10:1807-1817(2001).
[6]
INTERACTION WITH RAB11FIP2.
PubMed=12364336; DOI=10.1074/jbc.M206316200;
Cullis D.N., Philip B., Baleja J.D., Feig L.A.;
"Rab11-FIP2, an adaptor protein connecting cellular components
involved in internalization and recycling of epidermal growth factor
receptors.";
J. Biol. Chem. 277:49158-49166(2002).
[7]
FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
PubMed=14745134; DOI=10.1247/csf.28.419;
Nakatsu F., Ohno H.;
"Adaptor protein complexes as the key regulators of protein sorting in
the post-Golgi network.";
Cell Struct. Funct. 28:419-429(2003).
[8]
FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
Owen D.J., Collins B.M., Evans P.R.;
"Adaptors for clathrin coats: structure and function.";
Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
[9]
FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
PubMed=19033387; DOI=10.1242/jcs.033522;
Lau A.W., Chou M.M.;
"The adaptor complex AP-2 regulates post-endocytic trafficking through
the non-clathrin Arf6-dependent endocytic pathway.";
J. Cell Sci. 121:4008-4017(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652; THR-653 AND
SER-655, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-653, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
Adaptor protein complexes function in protein transport via
transport vesicles in different membrane traffic pathways. Adaptor
protein complexes are vesicle coat components and appear to be
involved in cargo selection and vesicle formation. AP-2 is
involved in clathrin-dependent endocytosis in which cargo proteins
are incorporated into vesicles surrounded by clathrin (clathrin-
coated vesicles, CCVs) which are destined for fusion with the
early endosome. The clathrin lattice serves as a mechanical
scaffold but is itself unable to bind directly to membrane
components. Clathrin-associated adaptor protein (AP) complexes
which can bind directly to both the clathrin lattice and to the
lipid and protein components of membranes are considered to be the
major clathrin adaptors contributing the CCV formation. AP-2 also
serves as a cargo receptor to selectively sort the membrane
proteins involved in receptor-mediated endocytosis. AP-2 seems to
play a role in the recycling of synaptic vesicle membranes from
the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
cytosolic tails of transmembrane cargo molecules. AP-2 may also
play a role in maintaining normal post-endocytic trafficking
through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha
subunit binds polyphosphoinositide-containing lipids, positioning
AP-2 on the membrane. The AP-2 alpha subunit acts via its C-
terminal appendage domain as a scaffolding platform for endocytic
accessory proteins. The AP-2 alpha and AP-2 sigma subunits are
thought to contribute to the recognition of the [ED]-X-X-X-L-[LI]
motif (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134,
ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387}.
-!- SUBUNIT: 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). Interacts
with SGIP1 (By similarity). Interacts with HIP1 and RAB11FIP2.
Interacts with SLC12A5. Interacts with clathrin. {ECO:0000250,
ECO:0000269|PubMed:11532990, ECO:0000269|PubMed:12364336}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane,
coated pit {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=AP-2 appears
to be excluded from internalizing CCVs and to disengage from sites
of endocytosis seconds before internalization of the nascent CCV.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=O95782-1; Sequence=Displayed;
Name=B;
IsoId=O95782-2; Sequence=VSP_000161;
-!- TISSUE SPECIFICITY: Isoform A expressed in forebrain, skeletal
muscle, spinal cord, cerebellum, salivary gland, heart and colon.
Isoform B is widely expressed in tissues and also in breast cancer
and in prostate carcinoma cells.
-!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD15564.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF289221; AAL11039.1; -; Genomic_DNA.
EMBL; AF289221; AAL11040.1; -; Genomic_DNA.
EMBL; AL136925; CAB66859.1; -; mRNA.
EMBL; AC006942; AAD15564.1; ALT_SEQ; Genomic_DNA.
EMBL; AC011495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC098783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014214; AAH14214.1; -; mRNA.
CCDS; CCDS46148.1; -. [O95782-1]
CCDS; CCDS46149.1; -. [O95782-2]
RefSeq; NP_055018.2; NM_014203.2. [O95782-1]
RefSeq; NP_570603.2; NM_130787.2. [O95782-2]
UniGene; Hs.467125; -.
ProteinModelPortal; O95782; -.
SMR; O95782; -.
BioGrid; 106669; 128.
CORUM; O95782; -.
DIP; DIP-33164N; -.
ELM; O95782; -.
IntAct; O95782; 70.
MINT; MINT-5002322; -.
STRING; 9606.ENSP00000351926; -.
iPTMnet; O95782; -.
PhosphoSitePlus; O95782; -.
SwissPalm; O95782; -.
BioMuta; AP2A1; -.
EPD; O95782; -.
MaxQB; O95782; -.
PaxDb; O95782; -.
PeptideAtlas; O95782; -.
PRIDE; O95782; -.
DNASU; 160; -.
Ensembl; ENST00000354293; ENSP00000346246; ENSG00000196961. [O95782-2]
Ensembl; ENST00000359032; ENSP00000351926; ENSG00000196961. [O95782-1]
GeneID; 160; -.
KEGG; hsa:160; -.
UCSC; uc002ppn.4; human. [O95782-1]
CTD; 160; -.
DisGeNET; 160; -.
EuPathDB; HostDB:ENSG00000196961.12; -.
GeneCards; AP2A1; -.
HGNC; HGNC:561; AP2A1.
HPA; CAB004306; -.
MIM; 601026; gene.
neXtProt; NX_O95782; -.
OpenTargets; ENSG00000196961; -.
PharmGKB; PA24852; -.
eggNOG; KOG1077; Eukaryota.
eggNOG; ENOG410XNQE; LUCA.
GeneTree; ENSGT00550000074757; -.
HOGENOM; HOG000170596; -.
HOVERGEN; HBG050518; -.
InParanoid; O95782; -.
KO; K11824; -.
OMA; DFKTCIS; -.
OrthoDB; EOG091G01JZ; -.
PhylomeDB; O95782; -.
TreeFam; TF300308; -.
Reactome; R-HSA-167590; Nef Mediated CD4 Down-regulation.
Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
Reactome; R-HSA-182218; Nef Mediated CD8 Down-regulation.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
Reactome; R-HSA-8964038; LDL clearance.
SignaLink; O95782; -.
ChiTaRS; AP2A1; human.
GeneWiki; Adaptor-related_protein_complex_2,_alpha_1; -.
GenomeRNAi; 160; -.
PRO; PR:O95782; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000196961; -.
CleanEx; HS_AP2A1; -.
ExpressionAtlas; O95782; baseline and differential.
Genevisible; O95782; HS.
GO; GO:0030122; C:AP-2 adaptor complex; TAS:BHF-UCL.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; NAS:UniProtKB.
GO; GO:0045334; C:clathrin-coated endocytic vesicle; NAS:ARUK-UCL.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:ARUK-UCL.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0072583; P:clathrin-dependent endocytosis; TAS:BHF-UCL.
GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0006895; P:Golgi to endosome transport; NAS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0032802; P:low-density lipoprotein particle receptor catabolic process; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007018; P:microtubule-based movement; TAS:Reactome.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR017104; AP2_complex_asu.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
InterPro; IPR013041; Clathrin_app_Ig-like_sf.
InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF02296; Alpha_adaptin_C; 1.
Pfam; PF02883; Alpha_adaptinC2; 1.
PIRSF; PIRSF037091; AP2_complex_alpha; 1.
SMART; SM00809; Alpha_adaptinC2; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
SUPFAM; SSF55711; SSF55711; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Coated pit; Complete proteome;
Endocytosis; Membrane; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Transport.
CHAIN 1 977 AP-2 complex subunit alpha-1.
/FTId=PRO_0000193730.
MOD_RES 626 626 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 653 653 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 655 655 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 706 727 Missing (in isoform B).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_000161.
VARIANT 270 270 P -> L (in dbSNP:rs17851121).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_060544.
CONFLICT 804 804 Q -> H (in Ref. 1; AAL11039/AAL11040).
{ECO:0000305}.
CONFLICT 924 977 ENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEP
VSRHLCELLAQQF -> GDREDTRVWGMPGTFLRPFVFLFL
FICCCLHSGGLGGVPLPPFPPQAQRGEGPGKWMSPPLPPHP
VVAPPTPSPSRGCVLL (in Ref. 4; AAH14214).
{ECO:0000305}.
SEQUENCE 977 AA; 107546 MW; D9FB569E7EDDF6ED CRC64;
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
ASRNPTFMCL ALHCIANVGS REMGEAFAAD IPRILVAGDS MDSVKQSAAL CLLRLYKASP
DLVPMGEWTA RVVHLLNDQH MGVVTAAVSL ITCLCKKNPD DFKTCVSLAV SRLSRIVSSA
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDAAVKGRL VECLETVLNK AQEPPKSKKV
QHSNAKNAIL FETISLIIHY DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE
FSHEAVKTHI DTVINALKTE RDVSVRQRAA DLLYAMCDRS NAKQIVSEML RYLETADYAI
REEIVLKVAI LAEKYAVDYS WYVDTILNLI RIAGDYVSEE VWYRVLQIVT NRDDVQGYAA
KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDPRSSPP VQFSLLHSKF HLCSVATRAL
LLSTYIKFIN LFPETKATIQ GVLRAGSQLR NADVELQQRA VEYLTLSSVA STDVLATVLE
EMPPFPERES SILAKLKRKK GPGAGSALDD GRRDPSSNDI NGGMEPTPST VSTPSPSADL
LGLRAAPPPA APPASAGAGN LLVDVFDGPA AQPSLGPTPE EAFLSELEPP APESPMALLA
DPAPAADPGP EDIGPPIPEA DELLNKFVCK NNGVLFENQL LQIGVKSEFR QNLGRMYLFY
GNKTSVQFQN FSPTVVHPGD LQTQLAVQTK RVAAQVDGGA QVQQVLNIEC LRDFLTPPLL
SVRFRYGGAP QALTLKLPVT INKFFQPTEM AAQDFFQRWK QLSLPQQEAQ KIFKANHPMD
AEVTKAKLLG FGSALLDNVD PNPENFVGAG IIQTKALQVG CLLRLEPNAQ AQMYRLTLRT
SKEPVSRHLC ELLAQQF


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15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.1 mg
20-272-190455 beta 1 + 2 Adaptin - Mouse monoclonal [100 _ 1] to beta 1 + 2 Adaptin; Adapter-related protein complex 1 beta-1 subunit; Beta-adaptin 1; Adaptor protein complex AP-1 beta-1 subunit; Golgi adaptor HA1_ 0.1 ml
15-288-22275 AP-2 complex subunit mu-1 - Adaptin mu-1; AP-2 mu-2 chain; Clathrin coat assembly protein AP50; Clathrin coat-associated protein AP50; Plasma membrane adaptor AP-2 50 kDa protein; HA2 50 kDa subunit; 0.05 mg
15-288-22275 AP-2 complex subunit mu-1 - Adaptin mu-1; AP-2 mu-2 chain; Clathrin coat assembly protein AP50; Clathrin coat-associated protein AP50; Plasma membrane adaptor AP-2 50 kDa protein; HA2 50 kDa subunit; 0.1 mg
10-288-22275F AP-2 complex subunit mu-1 - Adaptin mu-1; AP-2 mu-2 chain; Clathrin coat assembly protein AP50; Clathrin coat-associated protein AP50; Plasma membrane adaptor AP-2 50 kDa protein; HA2 50 kDa subunit; 0.05 mg
10-288-22275F AP-2 complex subunit mu-1 - Adaptin mu-1; AP-2 mu-2 chain; Clathrin coat assembly protein AP50; Clathrin coat-associated protein AP50; Plasma membrane adaptor AP-2 50 kDa protein; HA2 50 kDa subunit; 0.1 mg
20-272-191029 Clathrin - Membrane Vesicle Marker - Mouse monoclonal [1.BB.763] to Clathrin - Membrane Vesicle Marker; Adapter-related protein complex 1 beta-1 subunit; Beta-adaptin 1; Adaptor protein complex AP-1 b 0.025 mg
AP2M1 AP2A2 Gene adaptor-related protein complex 2, alpha 2 subunit
AP2B1 AP2A1 Gene adaptor-related protein complex 2, alpha 1 subunit
201-20-0354 AP2A1{adaptor-related protein complex 2, alpha 1 subunit}rabbit.pAb 0.1ml
abx110826 Polyclonal Rabbit Adaptor-Related Protein Complex 2, Alpha 1 Subunit Antibody 50 μl
CSB-EL001870RA Rat adaptor-related protein complex 2, alpha 2 subunit (AP2A2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
GS-0098a adaptor-related protein complex 2, alpha 1 subunit primary antibody, Host: Rabbit 200ul
15-288-22217F AP-3 complex subunit sigma-2 - Adapter-related protein complex 3 sigma-2 subunit; Sigma-adaptin 3b; AP-3 complex sigma-3B subunit; Sigma-3B-adaptin Polyclonal 0.1 mg
15-288-22217F AP-3 complex subunit sigma-2 - Adapter-related protein complex 3 sigma-2 subunit; Sigma-adaptin 3b; AP-3 complex sigma-3B subunit; Sigma-3B-adaptin Polyclonal 0.05 mg
CSB-EL001870BO Bovine adaptor-related protein complex 2, alpha 2 subunit (AP2A2) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL001869MO Mouse adaptor-related protein complex 2, alpha 1 subunit (AP2A1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL001870HU Human adaptor-related protein complex 2, alpha 2 subunit (AP2A2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL001869HU Human adaptor-related protein complex 2, alpha 1 subunit (AP2A1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL001870MO Mouse adaptor-related protein complex 2, alpha 2 subunit (AP2A2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
10-288-22217F AP-3 complex subunit sigma-2 - Adapter-related protein complex 3 sigma-2 subunit; Sigma-adaptin 3b; AP-3 complex sigma-3B subunit; Sigma-3B-adaptin 0.05 mg
10-288-22217F AP-3 complex subunit sigma-2 - Adapter-related protein complex 3 sigma-2 subunit; Sigma-adaptin 3b; AP-3 complex sigma-3B subunit; Sigma-3B-adaptin 0.1 mg
EIAAB41743 Cct1,Ccta,CCT-alpha,Mouse,Mus musculus,Tailless complex polypeptide 1A,Tailless complex polypeptide 1B,T-complex protein 1 subunit alpha,Tcp1,TCP-1-A,TCP-1-alpha,TCP-1-B
EIAAB26250 Alpha-NAC-like,Hom s 2.01,Homo sapiens,Human,NACA2,NACAL,NAC-alpha-like,Nascent polypeptide-associated complex subunit alpha-2,Nascent polypeptide-associated complex subunit alpha-like


 

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