Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

AP-2 complex subunit mu (AP-2 mu chain) (Adaptin-mu2) (Adaptor protein complex AP-2 subunit mu) (Adaptor-related protein complex 2 subunit mu) (Clathrin assembly protein complex 2 mu medium chain) (Clathrin coat assembly protein AP50) (Clathrin coat-associated protein AP50) (HA2 50 kDa subunit) (Plasma membrane adaptor AP-2 50 kDa protein)

 AP2M1_HUMAN             Reviewed;         435 AA.
Q96CW1; A6NE12; D3DNT1; P20172; P53679;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
27-SEP-2017, entry version 156.
RecName: Full=AP-2 complex subunit mu;
AltName: Full=AP-2 mu chain;
AltName: Full=Adaptin-mu2;
AltName: Full=Adaptor protein complex AP-2 subunit mu;
AltName: Full=Adaptor-related protein complex 2 subunit mu;
AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
AltName: Full=Clathrin coat assembly protein AP50;
AltName: Full=Clathrin coat-associated protein AP50;
AltName: Full=HA2 50 kDa subunit;
AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
Name=AP2M1; Synonyms=CLAPM1, KIAA0109;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
Tsui S.K.W., Waye M.M.Y., Liew C.C., Fung K., Lee C.Y.;
"Molecular cloning and sequence analysis of the cDNA for human 50 kDa
subunit of the clathrin assembly complex AP-2 (AP50).";
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, Placenta, and Skin;
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).
[7]
INTERACTION WITH ATP6V1H.
PubMed=12032142; DOI=10.1074/jbc.M200522200;
Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.-H., Fackler O.T.,
Peterlin B.M.;
"Subunit H of the V-ATPase binds to the medium chain of adaptor
protein complex 2 and connects Nef to the endocytic machinery.";
J. Biol. Chem. 277:28521-28529(2002).
[8]
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).
[9]
FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
PubMed=12952941; DOI=10.1083/jcb.200305145;
Motley A., Bright N.A., Seaman M.N.J., Robinson M.S.;
"Clathrin-mediated endocytosis in AP-2-depleted cells.";
J. Cell Biol. 162:909-918(2003).
[10]
FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
PubMed=12694563; DOI=10.1034/j.1600-0854.2003.00079.x;
Fraile-Ramos A., Kohout T.A., Waldhoer M., Marsh M.;
"Endocytosis of the viral chemokine receptor US28 does not require
beta-arrestins but is dependent on the clathrin-mediated pathway.";
Traffic 4:243-253(2003).
[11]
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).
[12]
FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
PubMed=14985334; DOI=10.1074/jbc.C400046200;
Huang F., Khvorova A., Marshall W., Sorkin A.;
"Analysis of clathrin-mediated endocytosis of epidermal growth factor
receptor by RNA interference.";
J. Biol. Chem. 279:16657-16661(2004).
[13]
FUNCTION IN RECEPTOR INTERNALIZATION, AND INTERACTION WITH F2R.
PubMed=16581796; DOI=10.1128/MCB.26.8.3231-3242.2006;
Paing M.M., Johnston C.A., Siderovski D.P., Trejo J.;
"Clathrin adaptor AP2 regulates thrombin receptor constitutive
internalization and endothelial cell resensitization.";
Mol. Cell. Biol. 26:3231-3242(2006).
[14]
INTERACTION WITH MEGF10.
PubMed=17643423; DOI=10.1016/j.yexcr.2007.06.015;
Suzuki E., Nakayama M.;
"MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin
assembly protein complex 2 medium chain and induces large vacuole
formation.";
Exp. Cell Res. 313:3729-3742(2007).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-156, 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).
[17]
INTERACTION WITH KIAA0319.
PubMed=19419997; DOI=10.1152/ajpcell.00630.2008;
Levecque C., Velayos-Baeza A., Holloway Z.G., Monaco A.P.;
"The dyslexia-associated protein KIAA0319 interacts with adaptor
protein 2 and follows the classical clathrin-mediated endocytosis
pathway.";
Am. J. Physiol. 297:C160-C168(2009).
[18]
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).
[19]
INTERACTION WITH KCNQ1.
PubMed=23529131; DOI=10.1113/jphysiol.2013.251678;
Rapetti-Mauss R., O'Mahony F., Sepulveda F.V., Urbach V., Harvey B.J.;
"Oestrogen promotes KCNQ1 potassium channel endocytosis and
postendocytic trafficking in colonic epithelium.";
J. Physiol. (Lond.) 591:2813-2831(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156, AND 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).
[22]
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).
[23]
X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 167-435 IN COMPLEX WITH CTLA4
INTERNALIZATION SIGNAL.
PubMed=11583591; DOI=10.1042/0264-6021:3590427;
Follows E.R., McPheat J.C., Minshull C., Moore N.C., Pauptit R.A.,
Rowsell S., Stacey C.L., Stanway J.J., Taylor I.W.F., Abbott W.M.;
"Study of the interaction of the medium chain mu 2 subunit of the
clathrin-associated adapter protein complex 2 with cytotoxic T-
lymphocyte antigen 4 and CD28.";
Biochem. J. 359:427-434(2001).
-!- 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 mu
subunit binds to transmembrane cargo proteins; it recognizes the
Y-X-X-Phi motifs. The surface region interacting with to the Y-X-
X-Phi motif is inaccessible in cytosolic AP-2, but becomes
accessible through a conformational change following
phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-
associated AP-2. The membrane-specific phosphorylation event
appears to involve assembled clathrin which activates the AP-2 mu
kinase AAK1 (By similarity). Plays a role in endocytosis of
frizzled family members upon Wnt signaling (By similarity).
{ECO:0000250, ECO:0000269|PubMed:12694563,
ECO:0000269|PubMed:12952941, ECO:0000269|PubMed:14745134,
ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838,
ECO:0000269|PubMed:16581796, 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 ATP6V1H and MEGF10. Interacts with EGFR. Interacts with F2R.
Interacts with PIP5K1C; tyrosine phosphorylation of PIP5K1C
weakens the interaction (By similarity). Interacts with KIAA0319;
required for clathrin-mediated endocytosis of KIAA0319. Interacts
with DVL2 (via DEP domain) (By similarity). Interacts with KCNQ1;
mediates estrogen-induced internalization via clathrin-coated
vesicles (PubMed:23529131). {ECO:0000250,
ECO:0000269|PubMed:23529131}.
-!- INTERACTION:
P27958:- (xeno); NbExp=4; IntAct=EBI-297683, EBI-6377335;
P00533:EGFR; NbExp=4; IntAct=EBI-297683, EBI-297353;
P62807:HIST1H2BI; NbExp=4; IntAct=EBI-297683, EBI-354552;
Q16778:HIST2H2BE; NbExp=4; IntAct=EBI-297683, EBI-1056125;
Q00013:MPP1; NbExp=4; IntAct=EBI-297683, EBI-711788;
Q15311:RALBP1; NbExp=3; IntAct=EBI-297683, EBI-749285;
Q9UHP6:RSPH14; NbExp=3; IntAct=EBI-297683, EBI-748350;
Q92609:TBC1D5; NbExp=3; IntAct=EBI-297683, EBI-742381;
-!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated 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.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96CW1-1; Sequence=Displayed;
Name=2;
IsoId=Q96CW1-2; Sequence=VSP_034599;
-!- SIMILARITY: Belongs to the adaptor complexes medium subunit
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA09762.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U36188; AAA93254.1; -; mRNA.
EMBL; D63475; BAA09762.2; ALT_INIT; mRNA.
EMBL; BT007308; AAP35972.1; -; mRNA.
EMBL; AC131235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78290.1; -; Genomic_DNA.
EMBL; CH471052; EAW78291.1; -; Genomic_DNA.
EMBL; BC004996; AAH04996.1; -; mRNA.
EMBL; BC013796; AAH13796.1; -; mRNA.
EMBL; BC014030; AAH14030.1; -; mRNA.
CCDS; CCDS43177.1; -. [Q96CW1-1]
CCDS; CCDS43178.1; -. [Q96CW1-2]
PIR; G02088; G02088.
RefSeq; NP_001020376.1; NM_001025205.1. [Q96CW1-2]
RefSeq; NP_001298127.1; NM_001311198.1.
RefSeq; NP_004059.2; NM_004068.3. [Q96CW1-1]
UniGene; Hs.518460; -.
PDB; 1H6E; X-ray; 3.60 A; A=164-435.
PDBsum; 1H6E; -.
ProteinModelPortal; Q96CW1; -.
SMR; Q96CW1; -.
BioGrid; 107587; 237.
CORUM; Q96CW1; -.
IntAct; Q96CW1; 116.
MINT; MINT-140451; -.
STRING; 9606.ENSP00000292807; -.
iPTMnet; Q96CW1; -.
PhosphoSitePlus; Q96CW1; -.
SwissPalm; Q96CW1; -.
BioMuta; AP2M1; -.
DMDM; 51316978; -.
EPD; Q96CW1; -.
MaxQB; Q96CW1; -.
PaxDb; Q96CW1; -.
PeptideAtlas; Q96CW1; -.
PRIDE; Q96CW1; -.
DNASU; 1173; -.
Ensembl; ENST00000292807; ENSP00000292807; ENSG00000161203. [Q96CW1-1]
Ensembl; ENST00000382456; ENSP00000371894; ENSG00000161203. [Q96CW1-2]
Ensembl; ENST00000439647; ENSP00000409081; ENSG00000161203. [Q96CW1-2]
GeneID; 1173; -.
KEGG; hsa:1173; -.
UCSC; uc003fmw.4; human. [Q96CW1-1]
CTD; 1173; -.
DisGeNET; 1173; -.
EuPathDB; HostDB:ENSG00000161203.13; -.
GeneCards; AP2M1; -.
HGNC; HGNC:564; AP2M1.
HPA; HPA036849; -.
HPA; HPA069870; -.
MIM; 601024; gene.
neXtProt; NX_Q96CW1; -.
OpenTargets; ENSG00000161203; -.
PharmGKB; PA24855; -.
eggNOG; KOG0937; Eukaryota.
eggNOG; ENOG410XPFS; LUCA.
GeneTree; ENSGT00530000062779; -.
HOGENOM; HOG000173246; -.
HOVERGEN; HBG050516; -.
InParanoid; Q96CW1; -.
KO; K11826; -.
PhylomeDB; Q96CW1; -.
TreeFam; TF300722; -.
Reactome; R-HSA-164939; Nef mediated downregulation of CD28 cell surface expression.
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-190873; Gap junction degradation.
Reactome; R-HSA-196025; Formation of annular gap junctions.
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; Q96CW1; -.
SIGNOR; Q96CW1; -.
ChiTaRS; AP2M1; human.
EvolutionaryTrace; Q96CW1; -.
GeneWiki; AP2M1; -.
GenomeRNAi; 1173; -.
PRO; PR:Q96CW1; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000161203; -.
CleanEx; HS_AP2M1; -.
ExpressionAtlas; Q96CW1; baseline and differential.
Genevisible; Q96CW1; HS.
GO; GO:0030122; C:AP-2 adaptor complex; TAS:BHF-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:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISS:BHF-UCL.
GO; GO:0005048; F:signal sequence binding; IDA:BHF-UCL.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
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:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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:1903077; P:negative regulation of protein localization to plasma membrane; IMP: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.
InterPro; IPR022775; AP_mu_sigma_su.
InterPro; IPR001392; Clathrin_mu.
InterPro; IPR018240; Clathrin_mu_CS.
InterPro; IPR011012; Longin-like_dom.
InterPro; IPR028565; MHD.
Pfam; PF00928; Adap_comp_sub; 1.
Pfam; PF01217; Clat_adaptor_s; 1.
PIRSF; PIRSF005992; Clathrin_mu; 1.
PRINTS; PR00314; CLATHRINADPT.
SUPFAM; SSF49447; SSF49447; 1.
SUPFAM; SSF64356; SSF64356; 1.
PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
PROSITE; PS51072; MHD; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Coated pit;
Complete proteome; Endocytosis; Lipid-binding; Membrane;
Phosphoprotein; Protein transport; Reference proteome; Transport.
CHAIN 1 435 AP-2 complex subunit mu.
/FTId=PRO_0000193774.
DOMAIN 170 434 MHD. {ECO:0000255|PROSITE-
ProRule:PRU00404}.
BINDING 341 341 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
BINDING 343 343 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
BINDING 345 345 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
BINDING 354 354 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
BINDING 356 356 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 156 156 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 141 142 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034599.
CONFLICT 106 106 V -> L (in Ref. 1; AAA93254).
{ECO:0000305}.
SEQUENCE 435 AA; 49655 MW; 82803219BA279954 CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMA AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKS QHQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIEKQGKGTA DETSKSGKQS
IAIDDCTFHQ CVRLSKFDSE RSISFIPPDG EFELMRYRTT KDIILPFRVI PLVREVGRTK
LEVKVVIKSN FKPSLLAQKI EVRIPTPLNT SGVQVICMKG KAKYKASENA IVWKIKRMAG
MKESQISAEI ELLPTNDKKK WARPPISMNF EVPFAPSGLK VRYLKVFEPK LNYSDHDVIK
WVRYIGRSGI YETRC


Related products :

Catalog number Product name Quantity
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; 0.1 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
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
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 0.05 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
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
26-638 AP3M2 is part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates th 0.05 mg
26-951 EPN1 is an endocytic accessory protein that interacts with EPS15 (MIM 600051), the alpha subunit of the clathrin adaptor AP2 (AP2A1; MIM 601026), and clathrin (see MIM 118960), as well as with other a 0.05 mg
201-20-0353 AP1M2{adaptor-related protein complex 1, mu 2 subunit}rabbit.pAb 0.1ml
201-20-0352 AP1M1{adaptor-related protein complex 1, mu 1 subunit}rabbit.pAb 0.1ml
AP3B1 AP2M1 Gene adaptor-related protein complex 2, mu 1 subunit
201-20-0358 AP3M1{adaptor-related protein complex 3, mu 1 subunit}rabbit.pAb 0.1ml
AP1S1 AP1M1 Gene adaptor-related protein complex 1, mu 1 subunit
201-20-0361 AP4M1{adaptor-related protein complex 4, mu 1 subunit}rabbit.pAb 0.1ml
APAF1 AP4M1 Gene adaptor-related protein complex 4, mu 1 subunit
201-20-0359 AP3M2{adaptor-related protein complex 3, mu 2 subunit}rabbit.pAb 0.1ml
AP3S2 AP3M2 Gene adaptor-related protein complex 3, mu 2 subunit
AP3S1 AP3M1 Gene adaptor-related protein complex 3, mu 1 subunit
AP1S2 AP1M2 Gene adaptor-related protein complex 1, mu 2 subunit
CSB-EL001877RA Rat adaptor-related protein complex 3, mu 1 subunit (AP3M1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001864RA Rat adaptor-related protein complex 1, mu 1 subunit (AP1M1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001883RA Rat adaptor-related protein complex 4, mu 1 subunit (AP4M1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001878RA Rat adaptor-related protein complex 3, mu 2 subunit (AP3M2) ELISA kit, Species Rat, Sample Type serum, plasma 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur