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Q9JME5 (AP3B2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP-3 complex subunit beta-2
Alternative name(s):
Adapter-related protein complex 3 subunit beta-2
Adaptor protein complex AP-3 subunit beta-2
Beta-3B-adaptin
Clathrin assembly protein complex 3 beta-2 large chain
Gene names
Name:Ap3b2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1082 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. Ref.6

Subunit structure

Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2) By similarity. AP-3 associates with the BLOC-1 complex.

Subcellular location

Golgi apparatus. Cytoplasmic vesicleclathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Golgi apparatus By similarity. Note: Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex By similarity.

Sequence similarities

Belongs to the adaptor complexes large subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10821082AP-3 complex subunit beta-2
PRO_0000193749

Regions

Compositional bias646 – 798153Glu/Ser-rich

Amino acid modifications

Modified residue2721Phosphoserine By similarity

Experimental info

Sequence conflict7341E → D in BAA92765. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9JME5 [UniParc].

Last modified October 25, 2004. Version 2.
Checksum: A2FEB20E83E16A52

FASTA1,082119,193
        10         20         30         40         50         60 
MSAAPAYSED KGGSAGPGEP EYGHDPASGG IFSSDYKRHD DLKEMLDTNK DSLKLEAMKR 

        70         80         90        100        110        120 
IVAMIARGKN ASDLFPAVVK NVACKNIEVK KLVYVYLVRY AEEQQDLALL SISTFQRGLK 

       130        140        150        160        170        180 
DPNQLIRASA LRVLSSIRVP IIVPIMMLAI KEAASDMSPY VRKTAAHAIP KLYSLDSDQK 

       190        200        210        220        230        240 
DQLIEVIEKL LADKTTLVAG SVVMAFEEVC PERIDLIHKN YRKLCNLLID VEEWGQVVII 

       250        260        270        280        290        300 
SMLTRYARTQ FLSPTQNESL LEENPEKAFY GSEEDEAKGP GSEEAATAAL PARKPYVMDP 

       310        320        330        340        350        360 
DHRLLLRNTK PLLQSRSAAV VMAVAQLYFH LAPKAEVGVI AKALVRLLRS HSEVQYVVLQ 

       370        380        390        400        410        420 
NVATMSIKRR GMFEPYLKSF YIRSTDPTQI KILKLEVLTN LANETNIPTV LREFQTYIRS 

       430        440        450        460        470        480 
MDKDFVAATI QAIGRCATNI GRVRDTCLNG LVQLLSNRDE LVVAESVVVI KKLLQMQPAQ 

       490        500        510        520        530        540 
HGEIIKHLAK LTDNIQVPMA RASILWLIGE YCEHVPKIAP DVLRKMAKSF TAEEDIVKLQ 

       550        560        570        580        590        600 
VINLAAKLYL TNSKQTKLLT QYVLSLAKYD QNYDIRDRAR FTRQLIVPSE QGGALSRHAK 

       610        620        630        640        650        660 
KLFLAPKPAP ILESSFKDRD HFQLGSLSHL LNAKATGYQE LPDWPEEAPD PSVRNVEVPE 

       670        680        690        700        710        720 
WTKCSNREKR KEKEKPFYSD SEGESGPTES ADSEPESESE SESKSSSGSG SGESSSESDN 

       730        740        750        760        770        780 
EEEDEEKGGG SESEQSEEED EKKKKTKKKK ASEGHREGSS SEEGSDSSSS SESEVTSESE 

       790        800        810        820        830        840 
EEQVEPASWR KKTPPGSKSA PVAKEISLLD LEDFTPPSVQ PVSPPMVVST SLAADLEGLT 

       850        860        870        880        890        900 
LTDSSLVPSL LSPVSSIGRQ ELLHRVAGEG LSVDYAFSRQ PFSGDPHMVS LHIYFSNNSE 

       910        920        930        940        950        960 
TPIKGLHVGT PKLPAGISIQ EFPEIESLAP GESTTTVMGI NFCDSTQAAN FQLCTQTRQF 

       970        980        990       1000       1010       1020 
YVSIQPPVGE LMAPVFMSEN EFKKEQGKLT GMNEITEKLT LPDTCRSDHM VVQKVTATAN 

      1030       1040       1050       1060       1070       1080 
LGRVPCGTSD EYRFAGRTLT SGSLVLLTLD ARAAGAAQLT VNSEKMVIGT MLVKDVIQAL 


TQ 

« Hide

References

« Hide 'large scale' references
[1]"Ap3b2, a neuron specific subunit of adaptor protein complex 3 (AP-3)."
Seong E., Burmeister M.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[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].
[3]"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. expand/collapse author list , 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] OF 1-738.
Strain: C57BL/6J.
Tissue: Embryonic head.
[4]"Growth suppression of Escherichia coli by induction of expression of mammalian genes with transmembrane or ATPase domains."
Inoue S., Sano H., Ohta M.
Biochem. Biophys. Res. Commun. 268:553-561(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 608-1082.
Tissue: Brain.
[5]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[6]"The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse."
Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.
Mol. Biol. Cell 22:4854-4867(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH THE BLOC-1 COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY528675 mRNA. Translation: AAS18679.1.
BC139378 mRNA. Translation: AAI39379.1.
BC139379 mRNA. Translation: AAI39380.1.
AK134504 mRNA. Translation: BAE22164.1.
AB030202 mRNA. Translation: BAA92765.1.
RefSeqNP_067467.2. NM_021492.3.
UniGeneMm.322894.

3D structure databases

ProteinModelPortalQ9JME5.
SMRQ9JME5. Positions 41-628.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198133. 1 interaction.
IntActQ9JME5. 2 interactions.
MINTMINT-4087974.

PTM databases

PhosphoSiteQ9JME5.

Proteomic databases

PaxDbQ9JME5.
PRIDEQ9JME5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000082090; ENSMUSP00000080739; ENSMUSG00000062444.
GeneID11775.
KEGGmmu:11775.
UCSCuc009iby.1. mouse.

Organism-specific databases

CTD8120.
MGIMGI:1100869. Ap3b2.

Phylogenomic databases

eggNOGCOG5096.
GeneTreeENSGT00530000063546.
HOGENOMHOG000033978.
HOVERGENHBG050519.
InParanoidQ3UYP8.
KOK12397.
OMANLGRVPC.
OrthoDBEOG74R1QG.
PhylomeDBQ9JME5.
TreeFamTF314605.

Gene expression databases

ArrayExpressQ9JME5.
BgeeQ9JME5.
CleanExMM_AP3B2.
GenevestigatorQ9JME5.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR026740. AP3_beta.
IPR026739. AP_beta.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PANTHERPTHR11134. PTHR11134. 1 hit.
PTHR11134:SF1. PTHR11134:SF1. 1 hit.
PfamPF01602. Adaptin_N. 1 hit.
[Graphical view]
PIRSFPIRSF037096. AP3_complex_beta. 1 hit.
SUPFAMSSF48371. SSF48371. 2 hits.
SSF49348. SSF49348. 1 hit.
ProtoNetSearch...

Other

NextBio279567.
PROQ9JME5.
SOURCESearch...

Entry information

Entry nameAP3B2_MOUSE
AccessionPrimary (citable) accession number: Q9JME5
Secondary accession number(s): B2RTK2 expand/collapse secondary AC list , Q3UYP8, Q6QR53, Q8R1E5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 25, 2004
Last modified: April 16, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot