Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

J domain-containing protein APJ1

Gene

APJ1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Putative chaperone involved in protein folding. Interferes with propagation of [PSI+] prion when overproduced.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri193 – 27482CR-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ATPase activator activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • unfolded protein binding Source: SGD

GO - Biological processi

  • positive regulation of ATPase activity Source: GOC
  • protein folding Source: InterPro
  • protein sumoylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33106-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
J domain-containing protein APJ1
Gene namesi
Name:APJ1
Ordered Locus Names:YNL077W
ORF Names:N2342
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL077W.
SGDiS000005021. APJ1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nuclear periphery Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528J domain-containing protein APJ1PRO_0000071155Add
BLAST

Proteomic databases

MaxQBiP53940.

PTM databases

iPTMnetiP53940.

Interactioni

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi35746. 36 interactions.
DIPiDIP-7817N.
IntActiP53940. 1 interaction.
MINTiMINT-4499575.

Structurei

3D structure databases

ProteinModelPortaliP53940.
SMRiP53940. Positions 1-100, 175-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 7370JPROSITE-ProRule annotationAdd
BLAST
Repeati206 – 2138CXXCXGXG motif
Repeati218 – 2258CXXCXGXG motif
Repeati246 – 2538CXXCXGXG motif
Repeati262 – 2698CXXCXGXG motif

Sequence similaritiesi

Contains 1 CR-type zinc finger.PROSITE-ProRule annotation
Contains 1 J domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri193 – 27482CR-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00840000129903.
HOGENOMiHOG000226718.
InParanoidiP53940.
OMAiAQFFNSS.
OrthoDBiEOG77M90H.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
InterProiIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53940-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQNTSLYDS LNVTAAASTS EIKKAYRNAA LKYHPDKNNH TEESKRKFQE
60 70 80 90 100
ICQAYEILKD NRLRALYDQY GTTDEVLIQE QQAQAQRQQA GPFSSSSNFD
110 120 130 140 150
TEAMSFPDLS PGDLFAQFFN SSATPSSNGS KSSFNFSFNN SSTPSFSFVN
160 170 180 190 200
GSGVNNLYSS SAKYNSNDED HHLDRGPDIK HNLKCTLKEL YMGKTAKLGL
210 220 230 240 250
NRTRICSVCD GHGGLKKCTC KTCKGQGIQT QTRRMGPLVQ SWSQTCADCG
260 270 280 290 300
GAGVFVKNKD ICQQCQGLGF IKERKILQVT VQPGSCHNQL IVLTGEGDEV
310 320 330 340 350
ISTKGGGHEK VIPGDVVITI LRLKDPNFQV INYSNLICKK CKIDFMTSLC
360 370 380 390 400
GGVVYIEGHP SGKLIKLDII PGEILKPGCF KTVEDMGMPK FINGVRSGFG
410 420 430 440 450
HLYVKFDVTY PERLEPENAK KIQNILANDK YIKAERSTME TADSDCYCDL
460 470 480 490 500
EKSYDSVEEH VLSSFEAPNL NNEVIEDDDL GDLINERDSR KRNNRRFDES
510 520
NINNNNETKR NKYSSPVSGF YDHDINGY
Length:528
Mass (Da):58,889
Last modified:October 1, 1996 - v1
Checksum:iAD6038F5B4768F9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71353 Genomic DNA. Translation: CAA95951.1.
AY723859 Genomic DNA. Translation: AAU09776.1.
BK006947 Genomic DNA. Translation: DAA10468.1.
PIRiS63009.
RefSeqiNP_014322.1. NM_001182915.1.

Genome annotation databases

EnsemblFungiiYNL077W; YNL077W; YNL077W.
GeneIDi855647.
KEGGisce:YNL077W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71353 Genomic DNA. Translation: CAA95951.1.
AY723859 Genomic DNA. Translation: AAU09776.1.
BK006947 Genomic DNA. Translation: DAA10468.1.
PIRiS63009.
RefSeqiNP_014322.1. NM_001182915.1.

3D structure databases

ProteinModelPortaliP53940.
SMRiP53940. Positions 1-100, 175-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35746. 36 interactions.
DIPiDIP-7817N.
IntActiP53940. 1 interaction.
MINTiMINT-4499575.

PTM databases

iPTMnetiP53940.

Proteomic databases

MaxQBiP53940.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL077W; YNL077W; YNL077W.
GeneIDi855647.
KEGGisce:YNL077W.

Organism-specific databases

EuPathDBiFungiDB:YNL077W.
SGDiS000005021. APJ1.

Phylogenomic databases

GeneTreeiENSGT00840000129903.
HOGENOMiHOG000226718.
InParanoidiP53940.
OMAiAQFFNSS.
OrthoDBiEOG77M90H.

Enzyme and pathway databases

BioCyciYEAST:G3O-33106-MONOMER.

Miscellaneous databases

PROiP53940.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
InterProiIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs."
    Poehlmann R., Philippsen P.
    Yeast 12:391-402(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "The J-protein family: modulating protein assembly, disassembly and translocation."
    Walsh P., Bursac D., Law Y.C., Cyr D., Lithgow T.
    EMBO Rep. 5:567-571(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  8. "Network of general and specialty J protein chaperones of the yeast cytosol."
    Sahi C., Craig E.A.
    Proc. Natl. Acad. Sci. U.S.A. 104:7163-7168(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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: 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAPJ1_YEAST
AccessioniPrimary (citable) accession number: P53940
Secondary accession number(s): D6W1A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 137 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 125 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.