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UniProtKB/Swiss-Prot entry P53309


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AP18B_YEAST
Primary accession number P53309
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 61)
Name and origin of the protein
Protein name Clathrin coat assembly protein AP180B
Synonyms None
Gene name
Name: YAP1802
OrderedLocusNames: YGR241C
ORFNames: G8610
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/(SICI)1097-0061(19970315)13:3<275::AID-YEA73>3.3.CO;2-7; PubMed=9090057 [NCBI, ExPASy, EBI, Israel, Japan]
Guerreiro P., Azevedo D., Barreiros T., Rodrigues-Pousada C.;
"Sequencing of a 9.9 kb segment on the right arm of yeast chromosome VII reveals four open reading frames, including PFK1, the gene coding for succinyl-CoA synthetase (beta-chain) and two ORFs sharing homology with ORFs of the yeast chromosome VIII.";
Yeast 13:275-280(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
FUNCTION, AND INTERACTION WITH CHC1; CLC1 AND PAN1.
DOI=10.1083/jcb.141.1.71; PubMed=9531549 [NCBI, ExPASy, EBI, Israel, Japan]
Wendland B., Emr S.D.;
"Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis.";
J. Cell Biol. 141:71-84(1998).
[4]
FUNCTION.
PubMed=14704157 [NCBI, ExPASy, EBI, Israel, Japan]
Baggett J.J., D'Aquino K.E., Wendland B.;
"The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae.";
Genetics 165:1661-1674(2003).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z73026; CAA97270.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64567; S64567.
RefSeq NP_011757.1; -.
3D structure databases
HSSP O96528; 1HX8. [HSSP ENTRY / PDB]
ModBase P53309.
Protein-protein interaction databases
DIP DIP:2751N; -.
IntAct P53309; 12.
Organism-specific databases
CYGD YGR241c; -.
SGD S000003473; YAP1802.
Yeast-GFP YGR241C.
Gene expression databases
ArrayExpress P53309; -.
GermOnline YGR241C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0030479; Cellular component: actin cortical patch (traceable author statement from SGD).
GO:0005935; Cellular component: cellular bud neck (inferred from electronic annotation from UniProtKB-SubCell).
GO:0030118; Cellular component: clathrin coat (inferred from electronic annotation from InterPro).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0030276; Molecular function: clathrin binding (inferred from electronic annotation from InterPro).
GO:0005545; Molecular function: phosphatidylinositol binding (inferred from electronic annotation from InterPro).
GO:0048268; Biological process: clathrin coat assembly (inferred from electronic annotation from InterPro).
GO:0006897; Biological process: endocytosis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR011417; ANTH.
IPR014712; Clathrin_Pinositid-bd_GAT-like.
IPR008942; ENTH_VHS.
IPR013809; Epsin-like_N.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.90; ENTH_VHS; 1.
G3DSA:1.20.58.150; Pinositid-bd_clathrin_GAT-like; 1.
Pfam PF07651; ANTH; 1.
Pfam graphical view of domain structure.
SMART SM00273; ENTH; 1.
SMART graphical view of domain structure.
PROSITE PS50942; ENTH; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl YGR241C; Saccharomyces cerevisiae. [Contig view]
GeneID 853157; -.
GenomeReviews Y13135_GR; YGR241C.
KEGG sce:YGR241C; -.
NMPDR fig|4932.3.peg.2886; -.
Phylogenomic databases
HOGENOM P53309; -.
Other
LinkHub P53309; -.
NextBio 973252; -.
ProtoNet P53309.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Cytoplasm; Endocytosis; Membrane; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   568  568     Clathrin coat assembly protein AP180B. PRO_0000202856
DOMAIN   1   127  127     ENTH. 
COMPBIAS   379   383  5     Poly-Gln. 
COMPBIAS   464   467  4     Poly-Gln. 
COMPBIAS   551   560  10     Poly-Gln. 
MOD_RES   133   133        Phosphoserine. 
Sequence information
Length: 568 AA [This is the length of the unprocessed precursor] Molecular weight: 64328 Da [This is the MW of the unprocessed precursor] CRC64: C5B5FD733739C3CD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSLYTKLVK GATKIKMAPP KQKYVDPILS GTSSARGLQE ITHALDIRLS DTAWTIVYKA 

        70         80         90        100        110        120 
LIVLHLMIQQ GEKDVTLRHY SHNLDVFQLR KISHTTKWSS NDMRALQRYD EYLKTRCEEY 

       130        140        150        160        170        180 
GRLGMDHLRD NYSSLKLGSK NQLSMDEELD HVESLEIQIN ALIRNKYSVS DLENHLLLYA 

       190        200        210        220        230        240 
FQLLVQDLLG LYNALNEGVI TLLESFFELS IEHAKRTLDL YKDFVDMTEY VVRYLKIGKA 

       250        260        270        280        290        300 
VGLKIPVIKH ITTKLINSLE EHLREETKRQ RGEPSEPQQD RKPSTAISST SSHNNNSNDK 

       310        320        330        340        350        360 
NKSIAQKKLE QIREQKRLLE QQLQNQQLLI SPTVPQDAYN PFGSQQQDLN NDTFSFEPTQ 

       370        380        390        400        410        420 
PQMTAQVPQP TANPFLIPQQ QQQALQLTSA STMPQPSEIQ ITPNLNNQQT GMYASNLQYT 

       430        440        450        460        470        480 
PNFTGSGFGG YTTTENNAIM TGTLDPTKTG SNNPFSLENI AREQQQQNFQ NSPNPFTLQQ 

       490        500        510        520        530        540 
AQTTPILAHS QTGNPFQAQN VVTSPMGTYM TNPVAGQLQY ASTGAQQQPQ MMQGQQTGYV 

       550        560 
MVPTAFVPIN QQQQQQQHQQ ENPNLIDI 

P53309 in FASTA format

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