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Protein

Palmitoyltransferase AKR1

Gene

AKR1

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

Palmitoyltransferase specific for casein kinase 1. Palmitoylates isoforms YCK1 and YCK2 at both C-terminal cysteine residues, which is required for their proper plasma membrane localization. Required for constitutive endocytosis of a-factor receptor STE3 and both constitutive and pheromone-induced endocytosis of alpha-factor receptor STE2.5 Publications

Catalytic activityi

Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei500 – 5001S-palmitoyl cysteine intermediate1 Publication

GO - Molecular functioni

GO - Biological processi

  • protein palmitoylation Source: UniProtKB
  • protein targeting to membrane Source: SGD
  • regulation of endocytosis Source: SGD
  • regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-29834-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Palmitoyltransferase AKR1 (EC:2.3.1.225)
Alternative name(s):
Ankyrin repeat-containing protein AKR1
Gene namesi
Name:AKR1
Ordered Locus Names:YDR264C
ORF Names:D9954.9, YD9230B.03C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR264C.
SGDiS000002672. AKR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 321321CytoplasmicAdd
BLAST
Transmembranei322 – 34120HelicalSequence analysisAdd
BLAST
Topological domaini342 – 3465Lumenal
Transmembranei347 – 36418HelicalSequence analysisAdd
BLAST
Topological domaini365 – 38420CytoplasmicAdd
BLAST
Transmembranei385 – 40521HelicalSequence analysisAdd
BLAST
Topological domaini406 – 41813LumenalAdd
BLAST
Transmembranei419 – 43921HelicalSequence analysisAdd
BLAST
Topological domaini440 – 51374CytoplasmicAdd
BLAST
Transmembranei514 – 53421HelicalSequence analysisAdd
BLAST
Topological domaini535 – 57036LumenalAdd
BLAST
Transmembranei571 – 59121HelicalSequence analysisAdd
BLAST
Topological domaini592 – 764173CytoplasmicAdd
BLAST

GO - Cellular componenti

  • early endosome membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: SGD
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi497 – 4982DH → AA: Abolishes YCK2 palmitoylation. 1 Publication
Mutagenesisi500 – 5001C → A: Abolishes YCK2 palmitoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 764764Palmitoyltransferase AKR1PRO_0000212934Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511PhosphoserineCombined sources
Modified residuei57 – 571PhosphoserineCombined sources

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP39010.

PTM databases

iPTMnetiP39010.
SwissPalmiP39010.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
STE4P188513EBI-2421,EBI-7390
YCK1P232913EBI-2421,EBI-4718

Protein-protein interaction databases

BioGridi32320. 142 interactions.
DIPiDIP-1145N.
IntActiP39010. 39 interactions.
MINTiMINT-544657.

Structurei

3D structure databases

ProteinModelPortaliP39010.
SMRiP39010. Positions 43-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati72 – 10231ANK 1Add
BLAST
Repeati108 – 13730ANK 2Add
BLAST
Repeati142 – 17130ANK 3Add
BLAST
Repeati175 – 20430ANK 4Add
BLAST
Repeati213 – 24230ANK 5Add
BLAST
Repeati246 – 27530ANK 6Add
BLAST
Domaini470 – 52051DHHCPROSITE-ProRule annotationAdd
BLAST

Domaini

The DHHC domain is required for palmitoyltransferase activity.

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation
Contains 1 DHHC domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063074.
HOGENOMiHOG000033883.
InParanoidiP39010.
KOiK20032.
OMAiFAATLFW.
OrthoDBiEOG72G1GX.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF01529. zf-DHHC. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS50216. DHHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNELENVPR ASTLTNEEQT VDPSNNDSQE DISLGDSNEI TSLASLKAIR
60 70 80 90 100
SGNEEESGNE QVNHNDEAEE DPLLTRYHTA CQRGDLATVK EMIHGKLLEV
110 120 130 140 150
NNDGDSTEHI TGLHWASINN RLSVVDFLVS QGADVNARAG ALHATPLHWA
160 170 180 190 200
ARYGYVYIVD FLLKHGADPT MTDDQGFNLL HLSVNSSNIM LVLYVLFNVV
210 220 230 240 250
SKGLLDIDCR DPKGRTSLLW AAYQGDSLTV AELLKFGASI KIADTEGFTP
260 270 280 290 300
LHWGTVKGQP HVLKYLIQDG ADFFQKTDTG KDCFAIAQEM NTVYSLREAL
310 320 330 340 350
THSGFDYHGY PIKKWFKKSQ HAKLVTFITP FLFLGIAFAL FSHINPLFVI
360 370 380 390 400
IVLFLLAIAT NKGLNKFVLP SYGRMGVHNV TLLRSPLLSG VFFGTLLWVT
410 420 430 440 450
IVWFFKVMPR TFSDEQYTNI LMLVILVSVF YLFGQLVIMD PGCLPEETDH
460 470 480 490 500
ENVRQTISNL LEIGKFDTKN FCIETWIRKP LRSKFSPLNN AVVARFDHYC
510 520 530 540 550
PWIFNDVGLK NHKAFIFFIT LMESGIFTFL ALCLEYFDEL EDAHEDTSQK
560 570 580 590 600
NGKCFILGAS DLCSGLIYDR FVFLILLWAL LQSIWVASLI FVQAFQICKG
610 620 630 640 650
MTNTEFNVLM KESKSIGPDG LSFNENFNTT PEGFAPSIDP GEESNDTVLA
660 670 680 690 700
PVPGSTIRKP RTCFGVCYAV TGMDQWLAVI KETIGIKDST GHNVYSITSR
710 720 730 740 750
IPTNYGWKRN VKDFWLTSDI NAPLWRRILY PPSGSKALLN GIEVDYFKLY
760
KLPNKDVEQG NDMV
Length:764
Mass (Da):85,840
Last modified:February 1, 1995 - v1
Checksum:i9C9759F0140CE3F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31407 Genomic DNA. Translation: AAC41676.1.
U51030 Genomic DNA. Translation: AAB64454.1.
Z70202 Genomic DNA. Translation: CAA94103.1.
Z68290 Genomic DNA. Translation: CAA92582.1.
BK006938 Genomic DNA. Translation: DAA12108.1.
PIRiS48521.
RefSeqiNP_010550.1. NM_001180572.1.

Genome annotation databases

EnsemblFungiiYDR264C; YDR264C; YDR264C.
GeneIDi851857.
KEGGisce:YDR264C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31407 Genomic DNA. Translation: AAC41676.1.
U51030 Genomic DNA. Translation: AAB64454.1.
Z70202 Genomic DNA. Translation: CAA94103.1.
Z68290 Genomic DNA. Translation: CAA92582.1.
BK006938 Genomic DNA. Translation: DAA12108.1.
PIRiS48521.
RefSeqiNP_010550.1. NM_001180572.1.

3D structure databases

ProteinModelPortaliP39010.
SMRiP39010. Positions 43-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32320. 142 interactions.
DIPiDIP-1145N.
IntActiP39010. 39 interactions.
MINTiMINT-544657.

PTM databases

iPTMnetiP39010.
SwissPalmiP39010.

Proteomic databases

MaxQBiP39010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR264C; YDR264C; YDR264C.
GeneIDi851857.
KEGGisce:YDR264C.

Organism-specific databases

EuPathDBiFungiDB:YDR264C.
SGDiS000002672. AKR1.

Phylogenomic databases

GeneTreeiENSGT00530000063074.
HOGENOMiHOG000033883.
InParanoidiP39010.
KOiK20032.
OMAiFAATLFW.
OrthoDBiEOG72G1GX.

Enzyme and pathway databases

BioCyciYEAST:G3O-29834-MONOMER.

Miscellaneous databases

PROiP39010.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF01529. zf-DHHC. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS50216. DHHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Interactions between the ankyrin repeat-containing protein Akr1p and the pheromone response pathway in Saccharomyces cerevisiae."
    Kao L.-R., Peterson J., Ji R., Bender L., Bender A.
    Mol. Cell. Biol. 16:168-178(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The ankyrin repeat-containing protein Akr1p is required for the endocytosis of yeast pheromone receptors."
    Givan S.A., Sprague G.F. Jr.
    Mol. Biol. Cell 8:1317-1327(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane."
    Feng Y., Davis N.G.
    Mol. Cell. Biol. 20:5350-5359(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase."
    Roth A.F., Feng Y., Chen L., Davis N.G.
    J. Cell Biol. 159:23-28(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ACTIVE SITE, MUTAGENESIS OF 497-ASP--HIS-498 AND CYS-500.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Akr1p-dependent palmitoylation of Yck2p yeast casein kinase 1 is necessary and sufficient for plasma membrane targeting."
    Babu P., Deschenes R.J., Robinson L.C.
    J. Biol. Chem. 279:27138-27147(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Transmembrane topology of the protein palmitoyl transferase Akr1."
    Politis E.G., Roth A.F., Davis N.G.
    J. Biol. Chem. 280:10156-10163(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  11. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  12. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  13. "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-51 AND SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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 SER-51 AND SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAKR1_YEAST
AccessioniPrimary (citable) accession number: P39010
Secondary accession number(s): D6VSP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 154 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 4072 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.