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P32597

- STH1_YEAST

UniProt

P32597 - STH1_YEAST

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Protein

Nuclear protein STH1/NPS1

Gene

STH1

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

Functioni

Catalytic component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is the essential ATPase of the complex. It is a DNA translocase capable of nucleosome remodeling. Required for full expression of early meiotic genes. Essential for mitotic growth and repression of CHA1 expression. Also involved in G2 phase control.8 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi495 – 5028ATPCurated

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. DNA binding Source: InterPro
  4. DNA-dependent ATPase activity Source: SGD
  5. DNA translocase activity Source: SGD
  6. helicase activity Source: UniProtKB
  7. lysine-acetylated histone binding Source: SGD

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. ATP-dependent chromatin remodeling Source: UniProtKB
  3. base-excision repair Source: SGD
  4. chromatin remodeling at centromere Source: SGD
  5. chromosome segregation Source: SGD
  6. cytoskeleton organization Source: UniProtKB
  7. double-strand break repair Source: SGD
  8. G2/M transition of mitotic cell cycle Source: UniProtKB
  9. meiotic nuclear division Source: UniProtKB
  10. nucleosome disassembly Source: SGD
  11. nucleosome positioning Source: SGD
  12. regulation of transcription, DNA-templated Source: UniProtKB
  13. transcription elongation from RNA polymerase II promoter Source: SGD
  14. transfer RNA gene-mediated silencing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31377-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear protein STH1/NPS1 (EC:3.6.4.12)
Alternative name(s):
ATP-dependent helicase STH1
Chromatin structure-remodeling complex protein STH1
SNF2 homolog
Gene namesi
Name:STH1
Synonyms:NPS1
Ordered Locus Names:YIL126W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IX

Organism-specific databases

CYGDiYIL126w.
SGDiS000001388. STH1.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation
Note: Localizes to centromeric and flanking chromatin. Association of the RSC complex with these loci is dependent on this subunit.

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB
  2. nucleus Source: SGD
  3. RSC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi505 – 5051S → F: Temperature-sensitive. 1 Publication
Mutagenesisi646 – 6461P → L: Temperature-sensitive. 1 Publication
Mutagenesisi763 – 7631C → Y: Temperature-sensitive. Reduced sporulation efficiency. 1 Publication
Mutagenesisi792 – 7921K → E: Complete inactivation.
Mutagenesisi806 – 8061S → L: Temperature-sensitive; when associated with M-881. Altered cell cycle distribution. 1 Publication
Mutagenesisi881 – 8811T → M: Temperature-sensitive; when associated with L-806. Altered cell cycle distribution. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13591359Nuclear protein STH1/NPS1PRO_0000074361Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32597.
PaxDbiP32597.
PeptideAtlasiP32597.

Expressioni

Gene expression databases

GenevestigatoriP32597.

Interactioni

Subunit structurei

Interacts directly with SFH1, CSE4, histones H3, H4 and H2B, and via its N-terminus, with RSC8. Interacts with LDB7, NPL6 and RTT102. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HHF2P023094EBI-18410,EBI-8113
HHT2P618304EBI-18410,EBI-8098
HTB1P022933EBI-18410,EBI-8088
HTL1Q9URQ53EBI-18410,EBI-8717
LDB7P382102EBI-18410,EBI-21189
NHP6AP116323EBI-18410,EBI-12019
NUP170P381813EBI-18410,EBI-11756
RSC58Q079796EBI-18410,EBI-36549
RTT102P533305EBI-18410,EBI-23637

Protein-protein interaction databases

BioGridi34865. 91 interactions.
DIPiDIP-5889N.
IntActiP32597. 65 interactions.
MINTiMINT-615490.
STRINGi4932.YIL126W.

Structurei

3D structure databases

ProteinModelPortaliP32597.
SMRiP32597. Positions 456-990, 1259-1356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini307 – 38377HSAPROSITE-ProRule annotationAdd
BLAST
Domaini482 – 647166Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini795 – 956162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini1270 – 134071BromoPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi597 – 6004DEGH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1198 – 124750Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 HSA domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00550000074659.
HOGENOMiHOG000172362.
InParanoidiP32597.
KOiK11786.
OMAiDYLQTIC.
OrthoDBiEOG7M98QM.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32597-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLQEQSELMS TVMNNTPTTV AALAAVAAAS ETNGKLGSEE QPEITIPKPR
60 70 80 90 100
SSAQLEQLLY RYRAIQNHPK ENKLEIKAIE DTFRNISRDQ DIYETKLDTL
110 120 130 140 150
RKSIDKGFQY DEDLLNKHLV ALQLLEKDTD VPDYFLDLPD TKNDNTTAIE
160 170 180 190 200
VDYSEKKPIK ISADFNAKAK SLGLESKFSN ATKTALGDPD TEIRISARIS
210 220 230 240 250
NRINELERLP ANLGTYSLDD CLEFITKDDL SSRMDTFKIK ALVELKSLKL
260 270 280 290 300
LTKQKSIRQK LINNVASQAH HNIPYLRDSP FTAAAQRSVQ IRSKVIVPQT
310 320 330 340 350
VRLAEELERQ QLLEKRKKER NLHLQKINSI IDFIKERQSE QWSRQERCFQ
360 370 380 390 400
FGRLGASLHN QMEKDEQKRI ERTAKQRLAA LKSNDEEAYL KLLDQTKDTR
410 420 430 440 450
ITQLLRQTNS FLDSLSEAVR AQQNEAKILH GEEVQPITDE EREKTDYYEV
460 470 480 490 500
AHRIKEKIDK QPSILVGGTL KEYQLRGLEW MVSLYNNHLN GILADEMGLG
510 520 530 540 550
KTIQSISLIT YLYEVKKDIG PFLVIVPLST ITNWTLEFEK WAPSLNTIIY
560 570 580 590 600
KGTPNQRHSL QHQIRVGNFD VLLTTYEYII KDKSLLSKHD WAHMIIDEGH
610 620 630 640 650
RMKNAQSKLS FTISHYYRTR NRLILTGTPL QNNLPELWAL LNFVLPKIFN
660 670 680 690 700
SAKTFEDWFN TPFANTGTQE KLELTEEETL LIIRRLHKVL RPFLLRRLKK
710 720 730 740 750
EVEKDLPDKV EKVIKCKLSG LQQQLYQQML KHNALFVGAG TEGATKGGIK
760 770 780 790 800
GLNNKIMQLR KICNHPFVFD EVEGVVNPSR GNSDLLFRVA GKFELLDRVL
810 820 830 840 850
PKFKASGHRV LMFFQMTQVM DIMEDFLRMK DLKYMRLDGS TKTEERTEML
860 870 880 890 900
NAFNAPDSDY FCFLLSTRAG GLGLNLQTAD TVIIFDTDWN PHQDLQAQDR
910 920 930 940 950
AHRIGQKNEV RILRLITTDS VEEVILERAM QKLDIDGKVI QAGKFDNKST
960 970 980 990 1000
AEEQEAFLRR LIESETNRDD DDKAELDDDE LNDTLARSAD EKILFDKIDK
1010 1020 1030 1040 1050
ERMNQERADA KAQGLRVPPP RLIQLDELPK VFREDIEEHF KKEDSEPLGR
1060 1070 1080 1090 1100
IRQKKRVYYD DGLTEEQFLE AVEDDNMSLE DAIKKRREAR ERRRLRQNGT
1110 1120 1130 1140 1150
KENEIETLEN TPEASETSLI ENNSFTAAVD EETNADKETT ASRSKRRSSR
1160 1170 1180 1190 1200
KKRTISIVTA EDKENTQEES TSQENGGAKV EEEVKSSSVE IINGSESKKK
1210 1220 1230 1240 1250
KPKLTVKIKL NKTTVLENND GKRAEEKPES KSPAKKTAAK KTKTKSKSLG
1260 1270 1280 1290 1300
IFPTVEKLVE EMREQLDEVD SHPRTSIFEK LPSKRDYPDY FKVIEKPMAI
1310 1320 1330 1340 1350
DIILKNCKNG TYKTLEEVRQ ALQTMFENAR FYNEEGSWVY VDADKLNEFT

DEWFKEHSS
Length:1,359
Mass (Da):156,743
Last modified:October 1, 1993 - v1
Checksum:i269A91BD853C20D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1062DK → NE in AAZ22501. (PubMed:16273108)Curated
Sequence conflicti144 – 1441D → N in AAZ22501. (PubMed:16273108)Curated
Sequence conflicti227 – 2271K → R in AAZ22501. (PubMed:16273108)Curated
Sequence conflicti546 – 5461N → T in AAA35120. (PubMed:1549132)Curated
Sequence conflicti566 – 5661V → I in AAZ22501. (PubMed:16273108)Curated
Sequence conflicti1010 – 10101A → R in AAA35120. (PubMed:1549132)Curated
Sequence conflicti1074 – 10807Missing(PubMed:1549132)Curated
Sequence conflicti1114 – 11141A → V in AAZ22501. (PubMed:16273108)Curated
Sequence conflicti1157 – 11571I → V in AAZ22501. (PubMed:16273108)Curated
Sequence conflicti1221 – 12211G → S in AAZ22501. (PubMed:16273108)Curated
Sequence conflicti1246 – 12461S → P in AAZ22501. (PubMed:16273108)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10595 Genomic DNA. Translation: BAA01446.1.
M83755 Genomic DNA. Translation: AAA35120.1.
DQ115392 Genomic DNA. Translation: AAZ22501.1.
Z46833 Genomic DNA. Translation: CAA86866.1.
BK006942 Genomic DNA. Translation: DAA08427.1.
PIRiS49883.
RefSeqiNP_012140.1. NM_001179474.1.

Genome annotation databases

EnsemblFungiiYIL126W; YIL126W; YIL126W.
GeneIDi854680.
KEGGisce:YIL126W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10595 Genomic DNA. Translation: BAA01446.1 .
M83755 Genomic DNA. Translation: AAA35120.1 .
DQ115392 Genomic DNA. Translation: AAZ22501.1 .
Z46833 Genomic DNA. Translation: CAA86866.1 .
BK006942 Genomic DNA. Translation: DAA08427.1 .
PIRi S49883.
RefSeqi NP_012140.1. NM_001179474.1.

3D structure databases

ProteinModelPortali P32597.
SMRi P32597. Positions 456-990, 1259-1356.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34865. 91 interactions.
DIPi DIP-5889N.
IntActi P32597. 65 interactions.
MINTi MINT-615490.
STRINGi 4932.YIL126W.

Proteomic databases

MaxQBi P32597.
PaxDbi P32597.
PeptideAtlasi P32597.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YIL126W ; YIL126W ; YIL126W .
GeneIDi 854680.
KEGGi sce:YIL126W.

Organism-specific databases

CYGDi YIL126w.
SGDi S000001388. STH1.

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00550000074659.
HOGENOMi HOG000172362.
InParanoidi P32597.
KOi K11786.
OMAi DYLQTIC.
OrthoDBi EOG7M98QM.

Enzyme and pathway databases

BioCyci YEAST:G3O-31377-MONOMER.

Miscellaneous databases

NextBioi 977286.

Gene expression databases

Genevestigatori P32597.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view ]
Pfami PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Saccharomyces cerevisiae NPS1 gene, a novel CDC gene which encodes a 160 kDa nuclear protein involved in G2 phase control."
    Tsuchiya E., Uno M., Kiguchi A., Masuoka K., Kanemori Y., Okabe S., Miyakawa T.
    EMBO J. 11:4017-4026(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "An essential Saccharomyces cerevisiae gene homologous to SNF2 encodes a helicase-related protein in a new family."
    Laurent B.C., Yang X., Carlson M.
    Mol. Cell. Biol. 12:1893-1902(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Quantitative trait loci mapped to single-nucleotide resolution in yeast."
    Deutschbauer A.M., Davis R.W.
    Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SK1.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: PROTEIN SEQUENCE OF 961-987 AND 993-1002, IDENTIFICATION IN THE RSC COMPLEX, FUNCTION OF THE RSC COMPLEX.
  7. "Interaction of a Swi3 homolog with Sth1 provides evidence for a Swi/Snf-related complex with an essential function in Saccharomyces cerevisiae."
    Treich I., Carlson M.
    Mol. Cell. Biol. 17:1768-1775(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RSC8.
  8. "Sfh1p, a component of a novel chromatin-remodeling complex, is required for cell cycle progression."
    Cao Y., Cairns B.R., Kornberg R.D., Laurent B.C.
    Mol. Cell. Biol. 17:3323-3334(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFH1.
  9. "Sth1p, a Saccharomyces cerevisiae Snf2p/Swi2p homolog, is an essential ATPase in RSC and differs from Snf/Swi in its interactions with histones and chromatin-associated proteins."
    Du J., Nasir I., Benton B.K., Kladde M.P., Laurent B.C.
    Genetics 150:987-1005(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-505; PRO-646; SER-806 AND THR-881.
  10. "Histone octamer transfer by a chromatin-remodeling complex."
    Lorch Y., Zhang M., Kornberg R.D.
    Cell 96:389-392(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  11. "Transcriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex RSC."
    Moreira J.M.A., Holmberg S.
    EMBO J. 18:2836-2844(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Nps1/Sth1p, a component of an essential chromatin-remodeling complex of Saccharomyces cerevisiae, is required for the maximal expression of early meiotic genes."
    Yukawa M., Katoh S., Miyakawa T., Tsuchiya E.
    Genes Cells 4:99-110(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-763.
  13. "Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains."
    Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D., Winston F.
    Mol. Cell 4:715-723(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPOSITION OF THE RSC COMPLEX.
  14. "Chromatin remodeling by RSC involves ATP-dependent DNA translocation."
    Saha A., Wittmeyer J., Cairns B.R.
    Genes Dev. 16:2120-2134(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Yeast RSC function is required for organization of the cellular cytoskeleton via an alternative PKC1 pathway."
    Chai B., Hsu J.-M., Du J., Laurent B.C.
    Genetics 161:575-584(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  16. "The yeast RSC chromatin-remodeling complex is required for kinetochore function in chromosome segregation."
    Hsu J.-M., Huang J., Meluh P.B., Laurent B.C.
    Mol. Cell. Biol. 23:3202-3215(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX, INTERACTION WITH CSE4 AND HISTONES H3; H4 AND H2B, SUBCELLULAR LOCATION.
  17. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  18. "Proteomic analysis of chromatin-modifying complexes in Saccharomyces cerevisiae identifies novel subunits."
    Lee K.K., Prochasson P., Florens L., Swanson S.K., Washburn M.P., Workman J.L.
    Biochem. Soc. Trans. 32:899-903(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RTT102.
  19. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  20. "The RSC chromatin remodeling complex bears an essential fungal-specific protein module with broad functional roles."
    Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R.
    Genetics 172:795-809(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LDB7 AND NPL6.
  21. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  22. "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-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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 nameiSTH1_YEAST
AccessioniPrimary (citable) accession number: P32597
Secondary accession number(s): D6VVG1, Q45U09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 156 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 1990 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3