HST3/YOR025W Protein Information

Standard Name	Hst3p
Systematic Name	Yor025wp
ORF Classification	Verified
Description	Member of the Sir2 family of NAD(+)-dependent protein deacetylases; involved along with Hst4p in telomeric silencing, cell cycle progression, radiation resistance, genomic stability and short-chain fatty acid metabolism (1, 2, 3, 4)
Name Description	Homolog of SIR Two (SIR2) 2, 5

Experimental Data
Molecules/cell	319 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	447
Molecular Weight (Da)	50,523
Isoelectric Point (pI)	9.72

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Hst3p (InterPro)
Physical Interactions	There are 5 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000012CDAD \| P53687 MIPS: YOR025W NCBI: 1055022 \| 1420135 \| 1708327 \| 51830520 \| 6324599 \| 829135 \| NP_014668.1 GenBank/EMBL/DDBJ: DAA10807.1 \| AY723866 \| U39062 \| X87331 \| Z74933
External Classifications	EC: 3.5.1.- [Hydrolases, Acting on Carbon-Nitrogen Bonds In Linear Amides]

Amino Acid Sequence (or in FASTA format)
1 MTSVSPSPPA SRSGSMCSDL PSSLQTEKLA HIIGLDADDE VLRRVTKQLS 51 RSRRIACLTG AGISCNAGIP DFRSSDGLYD LVKKDCSQYW SIKSGREMFD 101 ISLFRDDFKI SIFAKFMERL YSNVQLAKPT KTHKFIAHLK DRNKLLRCYT 151 QNIDGLEESI GLTLSNRKLP LTSFSSHWKN LDVVQLHGDL KTLSCTKCFQ 201 TFPWSRYWSR CLRRGELPLC PDCEALINKR LNEGKRTLGS NVGILRPNIV 251 LYGENHPSCE IITQGLNLDI IKGNPDFLII MGTSLKVDGV KQLVKKLSKK 301 IHDRGGLIIL VNKTPIGESS WHGIIDYQIH SDCDNWVTFL ESQIPDFFKT 351 QDQIKKLRQL KREASDLRKQ MKAQKDSIGT PPTTPLRTAQ GIDIQGNNEL 401 NTKIKSLNTV KRKILSPENS SEEDEEENLD TRKRAKIRPT FGDNQAS*

Amino Acid Sequence (or in FASTA format)

       1  MTSVSPSPPA SRSGSMCSDL PSSLQTEKLA HIIGLDADDE VLRRVTKQLS
      51  RSRRIACLTG AGISCNAGIP DFRSSDGLYD LVKKDCSQYW SIKSGREMFD
     101  ISLFRDDFKI SIFAKFMERL YSNVQLAKPT KTHKFIAHLK DRNKLLRCYT
     151  QNIDGLEESI GLTLSNRKLP LTSFSSHWKN LDVVQLHGDL KTLSCTKCFQ
     201  TFPWSRYWSR CLRRGELPLC PDCEALINKR LNEGKRTLGS NVGILRPNIV
     251  LYGENHPSCE IITQGLNLDI IKGNPDFLII MGTSLKVDGV KQLVKKLSKK
     301  IHDRGGLIIL VNKTPIGESS WHGIIDYQIH SDCDNWVTFL ESQIPDFFKT
     351  QDQIKKLRQL KREASDLRKQ MKAQKDSIGT PPTTPLRTAQ GIDIQGNNEL
     401  NTKIKSLNTV KRKILSPENS SEEDEEENLD TRKRAKIRPT FGDNQAS*

external links for Hst3p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Hst3p

1)	Smith JS, et al. (2000) A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci U S A 97(12):6658-63
2)	Brachmann CB, et al. (1995) The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev 9(23):2888-902
3)	Grunweller A and Ehrenhofer-Murray AE (2002) A novel yeast silencer. the 2mu origin of Saccharomyces cerevisiae has HST3-, MIG1- and SIR-dependent silencing activity. Genetics 162(1):59-71
4)	Starai VJ, et al. (2003) Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae. Genetics 163(2):545-55
5)	Derbyshire MK, et al. (1996) HST1, a new member of the SIR2 family of genes. Yeast 12(7):631-40
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41