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UniProtKB/Swiss-Prot entry P43633


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

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Entry information
Entry name ALK1_YEAST
Primary accession number P43633
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 55)
Name and origin of the protein
Protein name Serine/threonine-protein kinase Haspin homolog ALK1
Synonyms EC 2.7.11.1
DNA damage-responsive protein ALK1
Gene name
Name: ALK1
OrderedLocusNames: YGL021W
ORFNames: G3686
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].
Moen C., Lindstedt B.A., Berdal K.G., Rognes T., Seeberg E.C.;
"A novel DNA damage-response gene from Saccharomyces cerevisiae with homology to protein kinase.";
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
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]
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).
[4]
FUNCTION, INDUCTION, DOMAINS, AND MUTAGENESIS OF 606-E--L-610.
PubMed=16855400 [NCBI, ExPASy, EBI, Israel, Japan]
Nespoli A., Vercillo R., di Nola L., Diani L., Giannattasio M., Plevani P., Muzi-Falconi M.;
"Alk1 and Alk2 are two new cell cycle-regulated haspin-like proteins in budding yeast.";
Cell Cycle 5:1464-1471(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172 AND SER-318, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND THR-439, 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
X87672; CAA61012.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72543; CAA96721.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64023; S64023.
RefSeq NP_011494.1; -.
3D structure databases
ModBase P43633.
Protein-protein interaction databases
DIP DIP:4816N; -.
IntAct P43633; -.
Organism-specific databases
CYGD YGL021w; -.
SGD S000002989; ALK1.
Yeast-GFP YGL021W.
Gene expression databases
ArrayExpress P43633; -.
GermOnline YGL021W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0007067; Biological process: mitosis (inferred from expression pattern from SGD).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from SGD).
GO:0006974; Biological process: response to DNA damage stimulus (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
Graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS50011; PROTEIN_KINASE_DOM; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
ProtoNet P43633.
Genome annotation databases
Ensembl YGL021W; Saccharomyces cerevisiae. [Contig view]
GeneID 852863; -.
GenomeReviews Y13135_GR; YGL021W.
KEGG sce:YGL021W; -.
NMPDR fig|4932.3.peg.2601; -.
Phylogenomic databases
HOGENOM P43633; -.
Other
LinkHub P43633; -.
NextBio 972475; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell cycle; Complete proteome; DNA damage; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   760  760     Serine/threonine-protein kinase Haspin homolog ALK1. PRO_0000064557
DOMAIN   468   760  293     Protein kinase. 
NP_BIND   474   482  9     ATP (By similarity). 
MOTIF   200   202  3     KEN box. 
MOTIF   224   232  9     D box. 
COMPBIAS   94   449  356     Ser-rich. 
COMPBIAS   240   245  6     Poly-Gln. 
COMPBIAS   264   269  6     Poly-Ser. 
COMPBIAS   351   356  6     Poly-Ser. 
BINDING   510   510        ATP (By similarity). 
MOD_RES   172   172        Phosphothreonine. 
MOD_RES   318   318        Phosphoserine. 
MOD_RES   351   351        Phosphoserine. 
MOD_RES   439   439        Phosphothreonine. 
MUTAGEN   606   610        EHRNL->AAAAA: Reduces strongly kinase activity. 
CONFLICT   758   760        LYK -> AL (in Ref. 1; CAA61012). 
Sequence information
Length: 760 AA [This is the length of the unprocessed precursor] Molecular weight: 86087 Da [This is the MW of the unprocessed precursor] CRC64: 3FD169AD789ED60A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLLHFDIVIQ LLSSHTLKSH QVEPPMDFET SFEEFVEDKR FIALEVSDND DDCDTDLTAD 

        70         80         90        100        110        120 
TADELESSAI LKMRESDASL NVTTGNNTSR KTTSNSKKRW SLLSNHSAVS SSKSKKRWSV 

       130        140        150        160        170        180 
LSSSFTSESH KDRESRNVLQ QKRKSLQSYS SLDTVASNSS ISASSSLKRS STGLSLRQLF 

       190        200        210        220        230        240 
TKIGINDDIS QPGIGIPQGK ENLPPTMGKK NSSIASTSSE NRLRTPLKPL VNHSKRPTSQ 

       250        260        270        280        290        300 
PQQQQPLYNA SLSSRRSSIS STVSSSSSSK WRFWKRNKNQ TPALLQPDHH SLKTFPAVNR 

       310        320        330        340        350        360 
RDSMTPVEPR NMVKHKTSFS DFHKTIFSSN TYSESSDTIS SMEITLKNKA SSSSLSLNVL 

       370        380        390        400        410        420 
KKRNSQSSLK HKSSHASLQK FKRNKGKSSM IAPSTATNSS NDDSCSYSSK NSTLSHRISL 

       430        440        450        460        470        480 
PVPDQVSRDK IQNKLRYSTS LLSLNSKSSL PMNKNDHDET LLRQILLNCD IKRILNPAKG 

       490        500        510        520        530        540 
DVLPLINDVN HLSSIQLTSN VWQIGEVICK KVSLGTIDDI TWDRKFLSLQ ELEKLKIMQQ 

       550        560        570        580        590        600 
KFDGIPQLLK SFVVKEANGG LYLYLLFKDH GTPISLISLK NWKQILKIFW SCAGIIHGLE 

       610        620        630        640        650        660 
KNLKFEHRNL TLDNILIDGN GNITIIDFKC SRLQTPQDDV LYLRLDHPLF FLNGKDKSKI 

       670        680        690        700        710        720 
NEYQYQFEFE IYQSMRILLN MDASAFEPMT NLYWLYYLSR VLLKFGDRKL GKNDANRDKM 

       730        740        750        760 
ARVINHLEMN LAVHKRGGQL FKRLETEDIK NTGDLLKLYK 

P43633 in FASTA format

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