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UniProtKB/Swiss-Prot entry P07170


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

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Entry information
Entry name KAD1_YEAST
Primary accession number P07170
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on July 1, 1989 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 104)
Name and origin of the protein
Protein name Adenylate kinase cytosolic
Synonyms EC 2.7.4.3
AK 1
ATP-AMP transphosphorylase 1
Gene name
Name: ADK1
Synonyms: AKY, AKY1, AKY2
OrderedLocusNames: YDR226W
ORFNames: YD9934.11
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].
DOI=10.1007/BF00434817; PubMed=2834097 [NCBI, ExPASy, EBI, Israel, Japan]
Magdolen V., Oechsner U., Bandlow W.;
"The complete nucleotide sequence of the gene coding for yeast adenylate kinase.";
Curr. Genet. 12:405-411(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/15.17.7187; PubMed=2821496 [NCBI, ExPASy, EBI, Israel, Japan]
Proba K., Tomasselli A.G., Nielsen P., Schulz G.E.;
"The cDNA sequence encoding cytosolic adenylate kinase from baker's yeast (Saccharomyces cerevisiae).";
Nucleic Acids Res. 15:7187-7187(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2848829 [NCBI, ExPASy, EBI, Israel, Japan]
Konrad M.;
"Analysis and in vivo disruption of the gene coding for adenylate kinase (ADK1) in the yeast Saccharomyces cerevisiae.";
J. Biol. Chem. 263:19468-19474(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/23.3.507; PubMed=7885847 [NCBI, ExPASy, EBI, Israel, Japan]
Davies C.J., Hutchison C.A. III;
"Insertion site specificity of the transposon Tn3.";
Nucleic Acids Res. 23:507-514(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[6]
PROTEIN SEQUENCE OF 3-222.
PubMed=3004985 [NCBI, ExPASy, EBI, Israel, Japan]
Tomasselli A.G., Mast E., Janes W., Schiltz E.;
"The complete amino acid sequence of adenylate kinase from baker's yeast.";
Eur. J. Biochem. 155:111-119(1986).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[9]
X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS).
PubMed=7670369 [NCBI, ExPASy, EBI, Israel, Japan]
Abele U., Schulz G.E.;
"High-resolution structures of adenylate kinase from yeast ligated with inhibitor Ap5A, showing the pathway of phosphoryl transfer.";
Protein Sci. 4:1262-1271(1995).
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
X06304; CAA29624.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00413; CAA68471.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18455; AAA66319.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13239; AAC33143.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z48612; CAA88506.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S05799; KIBYA.
RefSeq NP_010512.1; -.
3D structure databases
PDB
1AKY; X-ray; 1.63 A; A=3-221.[ExPASy / RCSB / EBI]
1DVR; X-ray; 2.36 A; A/B=3-221.[ExPASy / RCSB / EBI]
2AKY; X-ray; 1.96 A; A=3-221.[ExPASy / RCSB / EBI]
3AKY; X-ray; 2.23 A; A=3-221.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AKY; -.
1DVR; -.
2AKY; -.
3AKY; -.
ModBase P07170.
Protein-protein interaction databases
DIP DIP:5129N; -.
IntAct P07170; -.
2D gel databases
SWISS-2DPAGE P07170; -.
Organism-specific databases
CYGD YDR226w; -.
SGD S000002634; ADK1.
Yeast-GFP YDR226W.
Gene expression databases
GermOnline YDR226W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from direct assay from SGD).
GO:0004017; Molecular function: adenylate kinase activity (inferred from direct assay from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0006172; Biological process: ADP biosynthetic process (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR006259; Adenyl_kin_sub.
IPR000850; Adenylate_kin.
IPR007862; Adenylate_kinase_Znf_lid.
Graphical view of domain structure.
PANTHER PTHR23359; Adenylate_kin; 1.
Pfam PF00406; ADK; 1.
PF05191; ADK_lid; 1.
Pfam graphical view of domain structure.
PRINTS PR00094; ADENYLTKNASE.
ProDom PD000657; Adenylate_kin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01351; adk; 1.
PROSITE PS00113; ADENYLATE_KINASE; 1.
BLOCKS P07170.
ProtoNet P07170.
Proteomic databases
PeptideAtlas P07170; -.
Genome annotation databases
Ensembl YDR226W; Saccharomyces cerevisiae. [Contig view]
GeneID 851812; -.
GenomeReviews Z71256_GR; YDR226W.
KEGG sce:YDR226W; -.
NMPDR fig|4932.3.peg.1269; -.
Phylogenomic databases
HOGENOM P07170; -.
Other
LinkHub P07170; -.
NextBio 969668; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
PROPEP   1     2  2     Removed in mature form. PRO_0000016550
CHAIN   3   222  220     Adenylate kinase cytosolic. PRO_0000016551
NP_BIND   13    21  9     ATP (By similarity). 
MOD_RES   3     3        N-acetylserine. 
MOD_RES   140   140        Phosphoserine. 
CONFLICT   139   139        A -> R (in Ref. 2; CAA68471). 
CONFLICT   222   222        D -> N (in Ref. 6; AA sequence). 
STRAND   8    12  5      
HELIX   19    30  12      
STRAND   33    36  4      
HELIX   37    46  10      
HELIX   50    58  9      
HELIX   59    61  3      
HELIX   68    80  13      
HELIX   82    85  4      
STRAND   88    92  5      
HELIX   97   110  14      
STRAND   115   121  7      
HELIX   124   132  9      
STRAND   134   137  4      
TURN   138   141  4      
STRAND   142   145  4      
TURN   146   148  3      
TURN   158   160  3      
HELIX   172   195  24      
STRAND   199   203  5      
HELIX   208   218  11      
Sequence information
Length: 222 AA [This is the length of the unprocessed precursor] Molecular weight: 24255 Da [This is the MW of the unprocessed precursor] CRC64: FE566FD8015907CE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSSESIRMV LIGPPGAGKG TQAPNLQERF HAAHLATGDM LRSQIAKGTQ LGLEAKKIMD 

        70         80         90        100        110        120 
QGGLVSDDIM VNMIKDELTN NPACKNGFIL DGFPRTIPQA EKLDQMLKEQ GTPLEKAIEL 

       130        140        150        160        170        180 
KVDDELLVAR ITGRLIHPAS GRSYHKIFNP PKEDMKDDVT GEALVQRSDD NADALKKRLA 

       190        200        210        220 
AYHAQTEPIV DFYKKTGIWA GVDASQPPAT VWADILNKLG KD 

P07170 in FASTA format

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View entry in raw text format (no links)
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