Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32597 (STH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:STH1
Synonyms:NPS1
Ordered Locus Names:YIL126W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.16 Ref.18 Ref.20

Subcellular location

Nucleus. Note: Localizes to centromeric and flanking chromatin. Association of the RSC complex with these loci is dependent on this subunit. Ref.16

Miscellaneous

Present with 1990 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 bromo domain.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 HSA domain.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainBromodomain
   LigandATP-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Helicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.14PubMed 16455496PubMed 17188033PubMed 17918861Ref.9. Source: GOC

ATP-dependent chromatin remodeling

Inferred from direct assay Ref.10Ref.14. Source: UniProtKB

G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.9. Source: UniProtKB

base-excision repair

Inferred from mutant phenotype PubMed 24674626. Source: SGD

chromatin remodeling at centromere

Inferred from mutant phenotype Ref.16. Source: SGD

chromosome segregation

Inferred from genetic interaction Ref.16. Source: SGD

cytoskeleton organization

Inferred from genetic interaction Ref.15. Source: UniProtKB

double-strand break repair

Inferred from mutant phenotype PubMed 16024655. Source: SGD

meiotic nuclear division

Inferred from mutant phenotype Ref.12. Source: UniProtKB

nucleosome disassembly

Inferred from direct assay PubMed 16492771. Source: SGD

nucleosome positioning

Inferred from mutant phenotype PubMed 21343911. Source: SGD

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.12Ref.11. Source: UniProtKB

transcription elongation from RNA polymerase II promoter

Inferred from direct assay PubMed 17081996. Source: SGD

transfer RNA gene-mediated silencing

Inferred from mutant phenotype PubMed 23707796. Source: SGD

   Cellular_componentRSC complex

Inferred from direct assay Ref.6. Source: UniProtKB

chromosome, centromeric region

Inferred from direct assay Ref.16. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1Ref.2. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay Ref.14Ref.9. Source: UniProtKB

DNA binding

Inferred from electronic annotation. Source: InterPro

DNA translocase activity

Inferred from direct assay Ref.14. Source: SGD

DNA-dependent ATPase activity

Inferred from direct assay Ref.14Ref.9. Source: SGD

helicase activity

Inferred from direct assay Ref.14. Source: UniProtKB

lysine-acetylated histone binding

Inferred from direct assay PubMed 20126658. Source: SGD

protein binding

Inferred from physical interaction Ref.16Ref.20Ref.6Ref.7Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13591359Nuclear protein STH1/NPS1
PRO_0000074361

Regions

Domain307 – 38377HSA
Domain482 – 647166Helicase ATP-binding
Domain795 – 956162Helicase C-terminal
Domain1270 – 134071Bromo
Nucleotide binding495 – 5028ATP Probable
Motif597 – 6004DEGH box
Compositional bias1198 – 124750Lys-rich

Amino acid modifications

Modified residue381Phosphoserine Ref.22

Experimental info

Mutagenesis5051S → F: Temperature-sensitive. Ref.9
Mutagenesis6461P → L: Temperature-sensitive. Ref.9
Mutagenesis7631C → Y: Temperature-sensitive. Reduced sporulation efficiency. Ref.12
Mutagenesis7921K → E: Complete inactivation.
Mutagenesis8061S → L: Temperature-sensitive; when associated with M-881. Altered cell cycle distribution. Ref.9
Mutagenesis8811T → M: Temperature-sensitive; when associated with L-806. Altered cell cycle distribution. Ref.9
Sequence conflict105 – 1062DK → NE in AAZ22501. Ref.3
Sequence conflict1441D → N in AAZ22501. Ref.3
Sequence conflict2271K → R in AAZ22501. Ref.3
Sequence conflict5461N → T in AAA35120. Ref.2
Sequence conflict5661V → I in AAZ22501. Ref.3
Sequence conflict10101A → R in AAA35120. Ref.2
Sequence conflict1074 – 10807Missing Ref.2
Sequence conflict11141A → V in AAZ22501. Ref.3
Sequence conflict11571I → V in AAZ22501. Ref.3
Sequence conflict12211G → S in AAZ22501. Ref.3
Sequence conflict12461S → P in AAZ22501. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P32597 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 269A91BD853C20D0

FASTA1,359156,743
        10         20         30         40         50         60 
MLQEQSELMS TVMNNTPTTV AALAAVAAAS ETNGKLGSEE QPEITIPKPR SSAQLEQLLY 

        70         80         90        100        110        120 
RYRAIQNHPK ENKLEIKAIE DTFRNISRDQ DIYETKLDTL RKSIDKGFQY DEDLLNKHLV 

       130        140        150        160        170        180 
ALQLLEKDTD VPDYFLDLPD TKNDNTTAIE VDYSEKKPIK ISADFNAKAK SLGLESKFSN 

       190        200        210        220        230        240 
ATKTALGDPD TEIRISARIS NRINELERLP ANLGTYSLDD CLEFITKDDL SSRMDTFKIK 

       250        260        270        280        290        300 
ALVELKSLKL LTKQKSIRQK LINNVASQAH HNIPYLRDSP FTAAAQRSVQ IRSKVIVPQT 

       310        320        330        340        350        360 
VRLAEELERQ QLLEKRKKER NLHLQKINSI IDFIKERQSE QWSRQERCFQ FGRLGASLHN 

       370        380        390        400        410        420 
QMEKDEQKRI ERTAKQRLAA LKSNDEEAYL KLLDQTKDTR ITQLLRQTNS FLDSLSEAVR 

       430        440        450        460        470        480 
AQQNEAKILH GEEVQPITDE EREKTDYYEV AHRIKEKIDK QPSILVGGTL KEYQLRGLEW 

       490        500        510        520        530        540 
MVSLYNNHLN GILADEMGLG KTIQSISLIT YLYEVKKDIG PFLVIVPLST ITNWTLEFEK 

       550        560        570        580        590        600 
WAPSLNTIIY KGTPNQRHSL QHQIRVGNFD VLLTTYEYII KDKSLLSKHD WAHMIIDEGH 

       610        620        630        640        650        660 
RMKNAQSKLS FTISHYYRTR NRLILTGTPL QNNLPELWAL LNFVLPKIFN SAKTFEDWFN 

       670        680        690        700        710        720 
TPFANTGTQE KLELTEEETL LIIRRLHKVL RPFLLRRLKK EVEKDLPDKV EKVIKCKLSG 

       730        740        750        760        770        780 
LQQQLYQQML KHNALFVGAG TEGATKGGIK GLNNKIMQLR KICNHPFVFD EVEGVVNPSR 

       790        800        810        820        830        840 
GNSDLLFRVA GKFELLDRVL PKFKASGHRV LMFFQMTQVM DIMEDFLRMK DLKYMRLDGS 

       850        860        870        880        890        900 
TKTEERTEML NAFNAPDSDY FCFLLSTRAG GLGLNLQTAD TVIIFDTDWN PHQDLQAQDR 

       910        920        930        940        950        960 
AHRIGQKNEV RILRLITTDS VEEVILERAM QKLDIDGKVI QAGKFDNKST AEEQEAFLRR 

       970        980        990       1000       1010       1020 
LIESETNRDD DDKAELDDDE LNDTLARSAD EKILFDKIDK ERMNQERADA KAQGLRVPPP 

      1030       1040       1050       1060       1070       1080 
RLIQLDELPK VFREDIEEHF KKEDSEPLGR IRQKKRVYYD DGLTEEQFLE AVEDDNMSLE 

      1090       1100       1110       1120       1130       1140 
DAIKKRREAR ERRRLRQNGT KENEIETLEN TPEASETSLI ENNSFTAAVD EETNADKETT 

      1150       1160       1170       1180       1190       1200 
ASRSKRRSSR KKRTISIVTA EDKENTQEES TSQENGGAKV EEEVKSSSVE IINGSESKKK 

      1210       1220       1230       1240       1250       1260 
KPKLTVKIKL NKTTVLENND GKRAEEKPES KSPAKKTAAK KTKTKSKSLG IFPTVEKLVE 

      1270       1280       1290       1300       1310       1320 
EMREQLDEVD SHPRTSIFEK LPSKRDYPDY FKVIEKPMAI DIILKNCKNG TYKTLEEVRQ 

      1330       1340       1350 
ALQTMFENAR FYNEEGSWVY VDADKLNEFT DEWFKEHSS 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"RSC, an essential, abundant chromatin-remodeling complex."
Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H., Tempst P., Du J., Laurent B.C., Kornberg R.D.
Cell 87:1249-1260(1996) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS49883.
RefSeqNP_012140.1. NM_001179474.1.

3D structure databases

ProteinModelPortalP32597.
SMRP32597. Positions 456-990, 1277-1356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34865. 91 interactions.
DIPDIP-5889N.
IntActP32597. 65 interactions.
MINTMINT-615490.
STRING4932.YIL126W.

Proteomic databases

MaxQBP32597.
PaxDbP32597.
PeptideAtlasP32597.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL126W; YIL126W; YIL126W.
GeneID854680.
KEGGsce:YIL126W.

Organism-specific databases

CYGDYIL126w.
SGDS000001388. STH1.

Phylogenomic databases

eggNOGCOG0553.
GeneTreeENSGT00550000074659.
HOGENOMHOG000172362.
KOK11786.
OMADYLQTIC.
OrthoDBEOG7M98QM.

Enzyme and pathway databases

BioCycYEAST:G3O-31377-MONOMER.

Gene expression databases

GenevestigatorP32597.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR001487. 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]
PfamPF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS00633. 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]
ProtoNetSearch...

Other

NextBio977286.

Entry information

Entry nameSTH1_YEAST
AccessionPrimary (citable) accession number: P32597
Secondary accession number(s): D6VVG1, Q45U09
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families