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AP-2 complex subunit beta (AP105B) (Adaptor protein complex AP-2 subunit beta) (Adaptor-related protein complex 2 subunit beta) (Beta-2-adaptin) (Beta-adaptin) (Clathrin assembly protein complex 2 beta large chain) (Plasma membrane adaptor HA2/AP2 adaptin beta subunit)

 AP2B1_MOUSE             Reviewed;         937 AA.
Q9DBG3; Q80XJ4;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
22-NOV-2017, entry version 138.
RecName: Full=AP-2 complex subunit beta;
AltName: Full=AP105B;
AltName: Full=Adaptor protein complex AP-2 subunit beta;
AltName: Full=Adaptor-related protein complex 2 subunit beta;
AltName: Full=Beta-2-adaptin;
AltName: Full=Beta-adaptin;
AltName: Full=Clathrin assembly protein complex 2 beta large chain;
AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin beta subunit;
Name=Ap2b1; Synonyms=Clapb1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
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).
[4]
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 beta
subunit acts via its C-terminal appendage domain as a scaffolding
platform for endocytic accessory proteins; at least some clathrin-
associated sorting proteins (CLASPs) are recognized by their [DE]-
X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to
clathrin heavy chain, promoting clathrin lattice assembly;
clathrin displaces at least some CLASPs from AP2B1 which probably
then can be positioned for further coat assembly (By similarity).
{ECO:0000250, ECO:0000269|PubMed:14745134,
ECO:0000269|PubMed:15473838}.
-!- 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 EPN1. Interacts with EPS15; clathrin competes with EPS15.
Interacts with SNAP91; clathrin competes with SNAP91. Interacts
with CLTC; clathrin competes with EPS15, SNAP91 and PIP5K1C.
Interacts with LDLRAP1. Interacts with AMPH and BIN1. Interacts
with ARF6 (GDP-bound). Interacts (dephosphorylated at Tyr-737)
with ARRB1; phosphorylation of AP2B1 at Tyr-737 disrupts the
interaction. Interacts with SLC2A8. Interacts with SCYL1 and
SCYL2. Interacts with TGFBR1 and TGFBR2. Interacts with PIP5K1C;
clathrin competes with PIP5K1C (By similarity). Interacts with
DENND1B (By similarity). Interacts with FCHO1 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
P48023:FASLG (xeno); NbExp=2; IntAct=EBI-775229, EBI-495538;
O70161:Pip5k1c; NbExp=8; IntAct=EBI-7257021, EBI-773657;
Q64729:Tgfbr1; NbExp=2; IntAct=EBI-775229, EBI-2899393;
-!- 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=1;
IsoId=Q9DBG3-1; Sequence=Displayed;
Name=2;
IsoId=Q9DBG3-2; Sequence=VSP_011491;
-!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK004975; BAB23711.1; -; mRNA.
EMBL; BC046772; AAH46772.1; -; mRNA.
CCDS; CCDS25161.1; -. [Q9DBG3-2]
CCDS; CCDS25162.1; -. [Q9DBG3-1]
RefSeq; NP_001030931.1; NM_001035854.2. [Q9DBG3-2]
RefSeq; NP_082191.1; NM_027915.3. [Q9DBG3-1]
RefSeq; XP_006534321.1; XM_006534258.3. [Q9DBG3-2]
RefSeq; XP_017170261.1; XM_017314772.1. [Q9DBG3-2]
UniGene; Mm.39053; -.
ProteinModelPortal; Q9DBG3; -.
SMR; Q9DBG3; -.
BioGrid; 214914; 15.
DIP; DIP-32161N; -.
IntAct; Q9DBG3; 11.
MINT; MINT-1870047; -.
STRING; 10090.ENSMUSP00000018875; -.
iPTMnet; Q9DBG3; -.
PhosphoSitePlus; Q9DBG3; -.
SwissPalm; Q9DBG3; -.
EPD; Q9DBG3; -.
PaxDb; Q9DBG3; -.
PRIDE; Q9DBG3; -.
Ensembl; ENSMUST00000018875; ENSMUSP00000018875; ENSMUSG00000035152. [Q9DBG3-2]
Ensembl; ENSMUST00000065692; ENSMUSP00000070714; ENSMUSG00000035152. [Q9DBG3-1]
GeneID; 71770; -.
KEGG; mmu:71770; -.
UCSC; uc007kor.1; mouse. [Q9DBG3-1]
CTD; 163; -.
MGI; MGI:1919020; Ap2b1.
eggNOG; KOG1061; Eukaryota.
eggNOG; COG5096; LUCA.
GeneTree; ENSGT00530000063138; -.
HOGENOM; HOG000163270; -.
HOVERGEN; HBG050515; -.
InParanoid; Q9DBG3; -.
KO; K11825; -.
OMA; ARASMVW; -.
TreeFam; TF300318; -.
Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
Reactome; R-MMU-437239; Recycling pathway of L1.
Reactome; R-MMU-5099900; WNT5A-dependent internalization of FZD4.
Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
Reactome; R-MMU-8964038; LDL clearance.
ChiTaRS; Ap2b1; mouse.
PRO; PR:Q9DBG3; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000035152; -.
CleanEx; MM_AP2B1; -.
ExpressionAtlas; Q9DBG3; baseline and differential.
Genevisible; Q9DBG3; MM.
GO; GO:0030122; C:AP-2 adaptor complex; IEA:Ensembl.
GO; GO:0030131; C:clathrin adaptor complex; ISO:MGI.
GO; GO:0060076; C:excitatory synapse; IC:GOC-OWL.
GO; GO:0005887; C:integral component of plasma membrane; IC:GOC-OWL.
GO; GO:0098794; C:postsynapse; IC:GOC-OWL.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:0030276; F:clathrin binding; ISO:MGI.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
GO; GO:0035904; P:aorta development; IMP:MGI.
GO; GO:0003279; P:cardiac septum development; IMP:MGI.
GO; GO:0048268; P:clathrin coat assembly; IEA:Ensembl.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0099590; P:neurotransmitter receptor internalization; IMP:SynGO.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
GO; GO:0099003; P:vesicle-mediated transport in synapse; IC:GOC-OWL.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 2.60.40.1150; -; 1.
InterPro; IPR026739; AP_beta.
InterPro; IPR016342; AP_complex_bsu_1_2_4.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR015151; B-adaptin_app_sub_C.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
InterPro; IPR013041; Clathrin_app_Ig-like_sf.
InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
PANTHER; PTHR11134; PTHR11134; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF02883; Alpha_adaptinC2; 1.
Pfam; PF09066; B2-adapt-app_C; 1.
PIRSF; PIRSF002291; AP_complex_beta; 1.
SMART; SM00809; Alpha_adaptinC2; 1.
SMART; SM00185; ARM; 2.
SMART; SM01020; B2-adapt-app_C; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
SUPFAM; SSF55711; SSF55711; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Coated pit;
Complete proteome; Endocytosis; Membrane; Phosphoprotein;
Protein transport; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P63010}.
CHAIN 2 937 AP-2 complex subunit beta.
/FTId=PRO_0000193743.
COMPBIAS 576 716 Pro-rich (stalk region).
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000250|UniProtKB:P63010}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000250|UniProtKB:P63010}.
MOD_RES 265 265 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63010}.
MOD_RES 737 737 Phosphotyrosine.
{ECO:0000250|UniProtKB:P63010}.
MOD_RES 928 928 Phosphotyrosine.
{ECO:0000250|UniProtKB:P62944}.
VAR_SEQ 663 663 L -> LLGSDLGGGIGGSPA (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011491.
SEQUENCE 937 AA; 104583 MW; 452DF0AE91EDB0AE CRC64;
MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA
VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI
CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK
YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV
QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV
VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST
DAGDSPVGTT TTTNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL
DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI GMAPGGYVAP KAVWLPAVKA
KGLEISGTFT HRQGHIYMEM NFTNKALQHM TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ
SIDVSLPLNT LGPVMKMEPL NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT
WKDIPNENEL QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN


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