Saccharomyces cerevisiae (S288c)

HST3

L000003042, YOR025W

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

GO Process (3)

GO Function (1)

GO Component (1)

Gene Ontology Biological Process

chromatin silencing at telomere [IGI]

histone deacetylation [IGI, IMP]

short-chain fatty acid metabolic process [IMP]

Gene Ontology Molecular Function

NAD-dependent histone deacetylase activity [IDA, IMP]

Gene Ontology Cellular Component

nucleus [IC]

SGD Alliance of Genome Resources Entrez Gene RefSeq UniprotKB

Download Curated Data for this Protein

34428

559292

Interactor Statistics

Proteins/Genes

133

Publications

Interactors w/ Physical (HTP) Evidence (31)
Interactors w/ Physical (LTP) Evidence (5)
Interactors w/ Genetic (HTP) Evidence (90)
Interactors w/ Genetic (LTP) Evidence (4)
Interactors w/ More than One Evidence Type (3)

Interactors 307
Interactions 627
Network
PTM Sites 7

Sites with Multi-PTMs

Displaying 1 protein 1 non-assigned with 7 total post translational modifications

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NP_014668

Hst3p

Length: 447

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

Location	PTM	Residue	Source(s)	Note(s)
128	Ubiquitination	K	Mayor T (2007)	-
131	Ubiquitination	K	Mayor T (2007)	-
229	Ubiquitination	K	Mayor T (2007)	-
406	Phosphorylation	S	Helbig AO (2010)	eyJOT1RFUyI6WyJQTUlEIDIxMTI2MzM2OiBQcmVkaWN0ZWQgcHJvdGVpbiBraW5hc2UgPSBUUEsxIl19
420	Phosphorylation	S	Gnad F (2009)	eyJOT1RFUyI6WyJQTUlEIDE5ODIzNzUwOiA1LDIwIG1pbiAwLjRNIE5hQ2wgcmF0aW8gKGxvZzIpOyAtMC4zMDQsLTEuMzE3IiwiUE1JRCAxOTgyMzc1MDogYmVzdCBwcmVkaWN0ZWQgbW90aWYgPSBDSzIuIl19
420	Phosphorylation	S	Soufi B (2009)	eyJOT1RFUyI6WyJQTUlEIDE5ODIzNzUwOiA1LDIwIG1pbiAwLjRNIE5hQ2wgcmF0aW8gKGxvZzIpOyAtMC4zMDQsLTEuMzE3IiwiUE1JRCAxOTgyMzc1MDogYmVzdCBwcmVkaWN0ZWQgbW90aWYgPSBDSzIuIl19
421	Phosphorylation	S	Gnad F (2009)	eyJOT1RFUyI6WyJQTUlEIDE5ODIzNzUwOiA1LDIwIG1pbiAwLjRNIE5hQ2wgcmF0aW8gKGxvZzIpOyAtMC4zMDQsLTEuMzE3LiJdfQ==
421	Phosphorylation	S	Soufi B (2009)	eyJOT1RFUyI6WyJQTUlEIDE5ODIzNzUwOiA1LDIwIG1pbiAwLjRNIE5hQ2wgcmF0aW8gKGxvZzIpOyAtMC4zMDQsLTEuMzE3LiJdfQ==

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Non-Assigned PTMs

Post translational modifications that are currently unassigned to a specific residue location.

Location	PTM	Residue	Source(s)	Note(s)
-	Ubiquitination	K	Mayor T (2007)	eyJOT1RFUyI6WyJsaWtlbHkgdWJpcXVpdGluIGNvbmp1Z2F0ZSJdLCJSRUxBVElPTlNISVBTIjp7IlVCSTQiOiI8c3Bhbj48YSBocmVmPSdodHRwczpcL1wvdGhlYmlvZ3JpZC5vcmdcLzMxMjE1XC9zdW1tYXJ5XC9zYWNjaGFyb215Y2VzLWNlcmV2aXNpYWVcL3ViaTQuaHRtbCcgYWx0PSdVQkk0Jz5VQkk0PFwvYT48XC9zcGFuPiJ9fQ==

Relationships

Protein	Relationship	Location	PTM	Residue	Identity	Source(s)
UBI4	Conjugate	-	Ubiquitination	K	PTM	Mayor T (2007)

Result Summary