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Protein

Adenylate kinase isoenzyme 6 homolog FAP7

Gene

FAP7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity (By similarity). Involved in 18S rRNA maturation. Required for cleavage of the 20S pre-rRNA at site D in the cytoplasm. Involved in oxidative stress response. Required for POS9-dependent target gene transcription upon oxidative stress.UniRule annotation3 Publications

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441AMPUniRule annotation
Binding sitei84 – 841ATPUniRule annotation
Binding sitei110 – 1101ATPUniRule annotation
Binding sitei114 – 1141ATPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 226ATPUniRule annotation

GO - Molecular functioni

  • adenylate kinase activity Source: UniProtKB-HAMAP
  • ATPase activity Source: UniProtKB-HAMAP
  • ATP binding Source: UniProtKB-KW
  • nucleoside-triphosphatase activity Source: SGD

GO - Biological processi

  • cellular response to oxidative stress Source: SGD
  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Ribosome biogenesis, rRNA processing, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29558-MONOMER.
ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase isoenzyme 6 homolog FAP7UniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AK6UniRule annotation
Alternative name(s):
Dual activity adenylate kinase/ATPaseUniRule annotation
Short name:
AK/ATPaseUniRule annotation
POS9-activating factor 7
Gene namesi
Name:FAP7
Ordered Locus Names:YDL166C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL166C.
SGDiS000002325. FAP7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191G → S: Sensitive to hydrogen peroxide. 1 Publication
Mutagenesisi20 – 201K → R: Decreases the processing of 20S rRNA. 1 Publication
Mutagenesisi21 – 211S → G: Sensitive to hydrogen peroxide. 1 Publication
Mutagenesisi82 – 821D → A: Decreases the processing of 20S rRNA; when associated with A-84. 1 Publication
Mutagenesisi84 – 841H → A: Decreases the processing of 20S rRNA; when associated with A-82. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 197197Adenylate kinase isoenzyme 6 homolog FAP7PRO_0000153902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831PhosphotyrosineCombined sources
Modified residuei188 – 1881PhosphoserineCombined sources
Modified residuei196 – 1961PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12055.
PeptideAtlasiQ12055.

PTM databases

iPTMnetiQ12055.

Interactioni

Subunit structurei

Interacts with RPS14B. Not a structural component of 43S pre-ribosomes, but transiently interacts with them with them by binding to RPS14.1 Publication

Protein-protein interaction databases

BioGridi31899. 44 interactions.
DIPiDIP-4793N.
IntActiQ12055. 22 interactions.
MINTiMINT-501278.

Structurei

3D structure databases

ProteinModelPortaliQ12055.
SMRiQ12055. Positions 8-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 6124NMPbindUniRule annotationAdd
BLAST
Regioni113 – 12311LIDUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi28 – 358Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the adenylate kinase family. AK6 subfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000015930.
HOGENOMiHOG000224472.
InParanoidiQ12055.
KOiK18532.
OMAiDNVQCEI.
OrthoDBiEOG72C5C8.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00039. Adenylate_kinase_AK6.
InterProiIPR020618. Adenyl_kinase_AK6.
IPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12055-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEARRYGPNI IVTGTPGCGK SSTCEFLKNK LKDYKYYNIS DFAKDNDCFE
60 70 80 90 100
GYDEGRKSHI VDEDKLLDML EPLLRQGNSI VDWHVNDVFP ERLIDLVVVL
110 120 130 140 150
RCDNSNLYSR LHARGYHDSK IEENLDAEIM GVVKQDAVES YEPHIVVELQ
160 170 180 190
SDTKEDMVSN VSRIVAWEKM WLEQHPDGVT NEYQGPRSDD EDDEDSE
Length:197
Mass (Da):22,723
Last modified:November 1, 1996 - v1
Checksum:i836A25B0D7E2633C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801I → V in AAS56894 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z67750 Genomic DNA. Translation: CAA91580.1.
Z74214 Genomic DNA. Translation: CAA98740.1.
AY558568 Genomic DNA. Translation: AAS56894.1.
BK006938 Genomic DNA. Translation: DAA11695.1.
PIRiS61047.
RefSeqiNP_010115.1. NM_001180226.1.

Genome annotation databases

EnsemblFungiiYDL166C; YDL166C; YDL166C.
GeneIDi851388.
KEGGisce:YDL166C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z67750 Genomic DNA. Translation: CAA91580.1.
Z74214 Genomic DNA. Translation: CAA98740.1.
AY558568 Genomic DNA. Translation: AAS56894.1.
BK006938 Genomic DNA. Translation: DAA11695.1.
PIRiS61047.
RefSeqiNP_010115.1. NM_001180226.1.

3D structure databases

ProteinModelPortaliQ12055.
SMRiQ12055. Positions 8-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31899. 44 interactions.
DIPiDIP-4793N.
IntActiQ12055. 22 interactions.
MINTiMINT-501278.

PTM databases

iPTMnetiQ12055.

Proteomic databases

MaxQBiQ12055.
PeptideAtlasiQ12055.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL166C; YDL166C; YDL166C.
GeneIDi851388.
KEGGisce:YDL166C.

Organism-specific databases

EuPathDBiFungiDB:YDL166C.
SGDiS000002325. FAP7.

Phylogenomic databases

GeneTreeiENSGT00390000015930.
HOGENOMiHOG000224472.
InParanoidiQ12055.
KOiK18532.
OMAiDNVQCEI.
OrthoDBiEOG72C5C8.

Enzyme and pathway databases

BioCyciYEAST:G3O-29558-MONOMER.
ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

PROiQ12055.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00039. Adenylate_kinase_AK6.
InterProiIPR020618. Adenyl_kinase_AK6.
IPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    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.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The essential protein fap7 is involved in the oxidative stress response of Saccharomyces cerevisiae."
    Juhnke H., Charizanis C., Latifi F., Krems B., Entian K.-D.
    Mol. Microbiol. 35:936-948(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-19 AND SER-21.
  5. Cited for: FUNCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "The putative NTPase Fap7 mediates cytoplasmic 20S pre-rRNA processing through a direct interaction with Rps14."
    Granneman S., Nandineni M.R., Baserga S.J.
    Mol. Cell. Biol. 25:10352-10364(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPS14B, MUTAGENESIS OF LYS-20; ASP-82 AND HIS-84.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-183; SER-188 AND SER-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKAD6_YEAST
AccessioniPrimary (citable) accession number: Q12055
Secondary accession number(s): D6VRI5, E9P8W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8350 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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 one 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.