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Protein

Oxysterol-binding protein homolog 4

Gene

KES1

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

Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1 phosphatase in the endoplasmic reticulum (PubMed:16136145, PubMed:22162133). Displays a similar affinity for PI4P and sterols (PubMed:22162133). Binds sterol and PI4P in a mutually exclusive manner (Probable).Curated2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei96SterolCombined sources2 Publications1
Binding sitei336Phosphatidylinositol 4-phosphateCombined sources1 Publication1
Binding sitei340Phosphatidylinositol 4-phosphateCombined sources1 Publication1
Binding sitei344Phosphatidylinositol 4-phosphateCombined sources1 Publication1

GO - Molecular functioni

  • lipid binding Source: SGD
  • oxysterol binding Source: SGD
  • phosphatidic acid binding Source: SGD
  • phosphatidylinositol-4,5-bisphosphate binding Source: SGD
  • phosphatidylinositol-4-phosphate binding Source: UniProtKB
  • sterol transporter activity Source: UniProtKB

GO - Biological processi

  • endocytosis Source: SGD
  • ER to Golgi ceramide transport Source: SGD
  • exocytosis Source: SGD
  • maintenance of cell polarity Source: SGD
  • piecemeal microautophagy of nucleus Source: SGD
  • positive regulation of phosphatase activity Source: SGD
  • post-Golgi vesicle-mediated transport Source: SGD
  • sphingolipid metabolic process Source: SGD
  • sterol biosynthetic process Source: UniProtKB-KW
  • sterol transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Lipid transport, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34042-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein homolog 4
Alternative name(s):
Protein KES1
Gene namesi
Name:KES1Imported
Synonyms:OSH4
Ordered Locus Names:YPL145C
ORF Names:LPI3C, P2614
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL145C.
SGDiS000006066. KES1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • extrinsic component of membrane Source: SGD
  • Golgi membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi97Y → F: Abolishes both cholesterol binding and biological function. 1 Publication1
Mutagenesisi109K → A: Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 2 Publications1
Mutagenesisi111L → D: Abolishes both cholesterol binding and biological function. 1 Publication1
Mutagenesisi112N → E: Abolishes binding to phosphatidylinositol 4-phosphate. 1 Publication1
Mutagenesisi117E → A: Abolishes both cholesterol binding and biological function. 1 Publication1
Mutagenesisi143 – 144HH → AA: Reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 3 Publications2
Mutagenesisi168K → A: Slight reduction in cholesterol transport. 1 Publication1
Mutagenesisi168K → A: Strong reduction in cholesterol transport. 1 Publication1
Mutagenesisi202 – 204HIE → AIA: Strong reduction in cholesterol binding without affecting phosphatidylinositol 4-phosphate binding. 1 Publication3
Mutagenesisi336K → A: Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 2 Publications1
Mutagenesisi340E → A: Abolishes binding to phosphatidylinositol 4-phosphate. 1 Publication1
Mutagenesisi344R → A: Slight reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001003861 – 434Oxysterol-binding protein homolog 4Add BLAST434

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei370PhosphothreonineCombined sources1
Modified residuei389PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP35844.
PRIDEiP35844.

PTM databases

iPTMnetiP35844.

Interactioni

Protein-protein interaction databases

BioGridi36038. 176 interactors.
DIPiDIP-2867N.
IntActiP35844. 10 interactors.
MINTiMINT-1678684.

Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 6Combined sources3
Helixi8 – 15Combined sources8
Turni16 – 19Combined sources4
Helixi24 – 26Combined sources3
Helixi31 – 33Combined sources3
Beta strandi34 – 38Combined sources5
Helixi39 – 46Combined sources8
Beta strandi47 – 49Combined sources3
Helixi50 – 54Combined sources5
Helixi55 – 58Combined sources4
Turni61 – 63Combined sources3
Helixi64 – 66Combined sources3
Helixi77 – 104Combined sources28
Beta strandi109 – 111Combined sources3
Beta strandi118 – 123Combined sources6
Turni129 – 131Combined sources3
Beta strandi134 – 142Combined sources9
Turni143 – 146Combined sources4
Beta strandi147 – 154Combined sources8
Turni155 – 158Combined sources4
Beta strandi159 – 171Combined sources13
Beta strandi173 – 175Combined sources3
Beta strandi177 – 182Combined sources6
Beta strandi185 – 189Combined sources5
Beta strandi192 – 197Combined sources6
Beta strandi201 – 204Combined sources4
Turni206 – 209Combined sources4
Beta strandi212 – 215Combined sources4
Beta strandi217 – 223Combined sources7
Beta strandi228 – 234Combined sources7
Beta strandi236 – 239Combined sources4
Beta strandi241 – 253Combined sources13
Helixi256 – 258Combined sources3
Helixi260 – 262Combined sources3
Beta strandi264 – 270Combined sources7
Beta strandi273 – 279Combined sources7
Helixi283 – 285Combined sources3
Beta strandi287 – 291Combined sources5
Turni292 – 294Combined sources3
Helixi305 – 307Combined sources3
Helixi313 – 316Combined sources4
Helixi318 – 326Combined sources9
Helixi329 – 353Combined sources25
Helixi357 – 359Combined sources3
Beta strandi360 – 366Combined sources7
Beta strandi368 – 370Combined sources3
Helixi383 – 391Combined sources9
Beta strandi396 – 399Combined sources4
Helixi407 – 410Combined sources4
Beta strandi417 – 421Combined sources5
Helixi423 – 427Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZHTX-ray1.90A2-434[»]
1ZHWX-ray1.70A2-434[»]
1ZHXX-ray1.50A2-434[»]
1ZHYX-ray1.60A2-434[»]
1ZHZX-ray1.90A2-434[»]
1ZI7X-ray2.50A/B/C30-434[»]
3SPWX-ray2.60A/B1-434[»]
4F4BX-ray1.87A/B2-434[»]
4FESX-ray2.00A/B2-434[»]
4JCHX-ray1.70A/B2-434[»]
ProteinModelPortaliP35844.
SMRiP35844.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35844.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 29Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication6
Regioni109 – 112Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication4
Regioni143 – 144Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication2

Domaini

Consists of a beta-barrel forming a sterol-binding pocket. When empty, the N-terminal lid (29 residues) is unfolded and leaves the pocket open. Upon sterol binding, this segment forms a lid that blocks the sterol molecule in the pocket (PubMed:16136145). Phosphatidylinositol 4-phosphate (PI4P) binding sites are roughly the same as for sterol. First, the sterol-binding pocket accommodates the PI4P acyl chains. Second, a shallow pocket at the entrance of the tunnel, which contains critical residues such as Lys-336, His-143 and His-144, selects the polar head of PI4P with high specificity. This interaction is probably essential for compensating loose binding of the PI4P acyl chains. Third, the N-terminal lid secures the bound PI4P molecule by wrapping its glycerol moiety (PubMed:22162133).2 Publications

Sequence similaritiesi

Belongs to the OSBP family.Curated

Phylogenomic databases

HOGENOMiHOG000197950.
InParanoidiP35844.
KOiK20465.
OMAiYTAKIDY.
OrthoDBiEOG092C2RAT.

Family and domain databases

InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 2 hits.
PfamiPF01237. Oxysterol_BP. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQYASSSSW TSFLKSIASF NGDLSSLSAP PFILSPISLT EFSQYWAEHP
60 70 80 90 100
ELFLEPSFIN DDNYKEHCLI DPEVESPELA RMLAVTKWFI STLKSQYCSR
110 120 130 140 150
NESLGSEKKP LNPFLGELFV GKWENKEHPE FGETVLLSEQ VSHHPPVTAF
160 170 180 190 200
SIFNDKNKVK LQGYNQIKAS FTKSLMLTVK QFGHTMLDIK DESYLVTPPP
210 220 230 240 250
LHIEGILVAS PFVELEGKSY IQSSTGLLCV IEFSGRGYFS GKKNSFKARI
260 270 280 290 300
YKDSKDSKDK EKALYTISGQ WSGSSKIIKA NKKEESRLFY DAARIPAEHL
310 320 330 340 350
NVKPLEEQHP LESRKAWYDV AGAIKLGDFN LIAKTKTELE ETQRELRKEE
360 370 380 390 400
EAKGISWQRR WFKDFDYSVT PEEGALVPEK DDTFLKLASA LNLSTKNAPS
410 420 430
GTLVGDKEDR KEDLSSIHWR FQRELWDEEK EIVL
Length:434
Mass (Da):49,492
Last modified:June 1, 1994 - v1
Checksum:i360E4A46ABE2D87B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti355I → T in AAS56373 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03913 Unassigned DNA. Translation: AAA17736.1.
U43703 Genomic DNA. Translation: AAB68217.1.
X96770 Genomic DNA. Translation: CAA65548.1.
Z73501 Genomic DNA. Translation: CAA97849.1.
AY558047 Genomic DNA. Translation: AAS56373.1.
BK006949 Genomic DNA. Translation: DAA11290.1.
PIRiS42676.
RefSeqiNP_015180.1. NM_001183959.1.

Genome annotation databases

EnsemblFungiiYPL145C; YPL145C; YPL145C.
GeneIDi855958.
KEGGisce:YPL145C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03913 Unassigned DNA. Translation: AAA17736.1.
U43703 Genomic DNA. Translation: AAB68217.1.
X96770 Genomic DNA. Translation: CAA65548.1.
Z73501 Genomic DNA. Translation: CAA97849.1.
AY558047 Genomic DNA. Translation: AAS56373.1.
BK006949 Genomic DNA. Translation: DAA11290.1.
PIRiS42676.
RefSeqiNP_015180.1. NM_001183959.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZHTX-ray1.90A2-434[»]
1ZHWX-ray1.70A2-434[»]
1ZHXX-ray1.50A2-434[»]
1ZHYX-ray1.60A2-434[»]
1ZHZX-ray1.90A2-434[»]
1ZI7X-ray2.50A/B/C30-434[»]
3SPWX-ray2.60A/B1-434[»]
4F4BX-ray1.87A/B2-434[»]
4FESX-ray2.00A/B2-434[»]
4JCHX-ray1.70A/B2-434[»]
ProteinModelPortaliP35844.
SMRiP35844.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36038. 176 interactors.
DIPiDIP-2867N.
IntActiP35844. 10 interactors.
MINTiMINT-1678684.

PTM databases

iPTMnetiP35844.

Proteomic databases

MaxQBiP35844.
PRIDEiP35844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL145C; YPL145C; YPL145C.
GeneIDi855958.
KEGGisce:YPL145C.

Organism-specific databases

EuPathDBiFungiDB:YPL145C.
SGDiS000006066. KES1.

Phylogenomic databases

HOGENOMiHOG000197950.
InParanoidiP35844.
KOiK20465.
OMAiYTAKIDY.
OrthoDBiEOG092C2RAT.

Enzyme and pathway databases

BioCyciYEAST:G3O-34042-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP35844.
PROiP35844.

Family and domain databases

InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 2 hits.
PfamiPF01237. Oxysterol_BP. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKES1_YEAST
AccessioniPrimary (citable) accession number: P35844
Secondary accession number(s): D6W3M4, E9P8U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 151 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 32200 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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