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Protein

AP-2 complex subunit beta

Gene

Ap2b1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_299462. WNT5A-dependent internalization of FZD4.
REACT_304279. Retrograde neurotrophin signalling.
REACT_316383. MHC class II antigen presentation.
REACT_322343. Trafficking of GluR2-containing AMPA receptors.
REACT_350802. EGFR downregulation.
REACT_353475. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-2 complex subunit beta
Alternative name(s):
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
Gene namesi
Name:Ap2b1
Synonyms:Clapb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1919020. Ap2b1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 937936AP-2 complex subunit betaPRO_0000193743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei265 – 2651N6-acetyllysineBy similarity
Modified residuei737 – 7371PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9DBG3.
PaxDbiQ9DBG3.
PRIDEiQ9DBG3.

PTM databases

PhosphoSiteiQ9DBG3.

Expressioni

Gene expression databases

BgeeiQ9DBG3.
CleanExiMM_AP2B1.
ExpressionAtlasiQ9DBG3. baseline and differential.
GenevisibleiQ9DBG3. 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). 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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FASLGP480232EBI-775229,EBI-495538From a different organism.
Pip5k1cO701618EBI-7257021,EBI-773657

Protein-protein interaction databases

BioGridi214914. 13 interactions.
IntActiQ9DBG3. 10 interactions.
MINTiMINT-1870047.
STRINGi10090.ENSMUSP00000018875.

Structurei

3D structure databases

ProteinModelPortaliQ9DBG3.
SMRiQ9DBG3. Positions 4-582, 705-937.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi576 – 716141Pro-rich (stalk region)Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5096.
GeneTreeiENSGT00530000063138.
HOGENOMiHOG000163270.
HOVERGENiHBG050515.
InParanoidiQ9DBG3.
KOiK11825.
OMAiCHLNADA.
OrthoDBiEOG7BGHK0.
TreeFamiTF300318.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1150. 1 hit.
3.30.310.10. 1 hit.
InterProiIPR026739. AP_beta.
IPR016342. AP_complex_bsu_1_2_4.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015151. B-adaptin_app_sub_C.
IPR012295. Beta2_adaptin/TBP_C_dom.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR013037. Clathrin_b-adaptin_app_Ig-like.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PANTHERiPTHR11134. PTHR11134. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
PF09066. B2-adapt-app_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002291. AP_complex_beta. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
SM01020. B2-adapt-app_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9DBG3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL
60 70 80 90 100
FPDVVNCMQT DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP
110 120 130 140 150
LIRALAVRTM GCIRVDKITE YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD
160 170 180 190 200
INAQMVEDQG FLDSLRDLIA DSNPMVVANA VAALSEISES HPNSNLLDLN
210 220 230 240 250
PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI CERVTPRLSH
260 270 280 290 300
ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY
310 320 330 340 350
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN
360 370 380 390 400
IAQVLAELKE YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ
410 420 430 440 450
TKVNYVVQEA IVVIRDIFRK YPNKYESIIA TLCENLDSLD EPDARAAMIW
460 470 480 490 500
IVGEYAERID NADELLESFL EGFHDESTQV QLTLLTAIVK LFLKKPSETQ
510 520 530 540 550
ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV VLSEKPLISE
560 570 580 590 600
ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST
610 620 630 640 650
DAGDSPVGTT TTTNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM
660 670 680 690 700
GAVDLLGGGL DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI
710 720 730 740 750
GMAPGGYVAP KAVWLPAVKA KGLEISGTFT HRQGHIYMEM NFTNKALQHM
760 770 780 790 800
TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ SIDVSLPLNT LGPVMKMEPL
810 820 830 840 850
NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT WKDIPNENEL
860 870 880 890 900
QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL
910 920 930
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN
Length:937
Mass (Da):104,583
Last modified:June 1, 2001 - v1
Checksum:i452DF0AE91EDB0AE
GO
Isoform 2 (identifier: Q9DBG3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     663-663: L → LLGSDLGGGIGGSPA

Show »
Length:951
Mass (Da):105,722
Checksum:iEBB43F600FC24A3C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei663 – 6631L → LLGSDLGGGIGGSPA in isoform 2. 1 PublicationVSP_011491

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004975 mRNA. Translation: BAB23711.1.
BC046772 mRNA. Translation: AAH46772.1.
CCDSiCCDS25161.1. [Q9DBG3-2]
CCDS25162.1. [Q9DBG3-1]
RefSeqiNP_001030931.1. NM_001035854.2. [Q9DBG3-2]
NP_082191.1. NM_027915.3. [Q9DBG3-1]
XP_006534321.1. XM_006534258.2. [Q9DBG3-2]
UniGeneiMm.39053.

Genome annotation databases

EnsembliENSMUST00000065692; ENSMUSP00000070714; ENSMUSG00000035152. [Q9DBG3-1]
GeneIDi71770.
KEGGimmu:71770.
UCSCiuc007kor.1. mouse. [Q9DBG3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004975 mRNA. Translation: BAB23711.1.
BC046772 mRNA. Translation: AAH46772.1.
CCDSiCCDS25161.1. [Q9DBG3-2]
CCDS25162.1. [Q9DBG3-1]
RefSeqiNP_001030931.1. NM_001035854.2. [Q9DBG3-2]
NP_082191.1. NM_027915.3. [Q9DBG3-1]
XP_006534321.1. XM_006534258.2. [Q9DBG3-2]
UniGeneiMm.39053.

3D structure databases

ProteinModelPortaliQ9DBG3.
SMRiQ9DBG3. Positions 4-582, 705-937.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214914. 13 interactions.
IntActiQ9DBG3. 10 interactions.
MINTiMINT-1870047.
STRINGi10090.ENSMUSP00000018875.

PTM databases

PhosphoSiteiQ9DBG3.

Proteomic databases

MaxQBiQ9DBG3.
PaxDbiQ9DBG3.
PRIDEiQ9DBG3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065692; ENSMUSP00000070714; ENSMUSG00000035152. [Q9DBG3-1]
GeneIDi71770.
KEGGimmu:71770.
UCSCiuc007kor.1. mouse. [Q9DBG3-1]

Organism-specific databases

CTDi163.
MGIiMGI:1919020. Ap2b1.

Phylogenomic databases

eggNOGiCOG5096.
GeneTreeiENSGT00530000063138.
HOGENOMiHOG000163270.
HOVERGENiHBG050515.
InParanoidiQ9DBG3.
KOiK11825.
OMAiCHLNADA.
OrthoDBiEOG7BGHK0.
TreeFamiTF300318.

Enzyme and pathway databases

ReactomeiREACT_299462. WNT5A-dependent internalization of FZD4.
REACT_304279. Retrograde neurotrophin signalling.
REACT_316383. MHC class II antigen presentation.
REACT_322343. Trafficking of GluR2-containing AMPA receptors.
REACT_350802. EGFR downregulation.
REACT_353475. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSiAp2b1. mouse.
NextBioi334467.
PROiQ9DBG3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBG3.
CleanExiMM_AP2B1.
ExpressionAtlasiQ9DBG3. baseline and differential.
GenevisibleiQ9DBG3. MM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1150. 1 hit.
3.30.310.10. 1 hit.
InterProiIPR026739. AP_beta.
IPR016342. AP_complex_bsu_1_2_4.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015151. B-adaptin_app_sub_C.
IPR012295. Beta2_adaptin/TBP_C_dom.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR013037. Clathrin_b-adaptin_app_Ig-like.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PANTHERiPTHR11134. PTHR11134. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
PF09066. B2-adapt-app_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002291. AP_complex_beta. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
SM01020. B2-adapt-app_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "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] (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Brain.
  3. "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.
  4. "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.

Entry informationi

Entry nameiAP2B1_MOUSE
AccessioniPrimary (citable) accession number: Q9DBG3
Secondary accession number(s): Q80XJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.