UniProt Accession

 STM1_YEAST; P39015; D6VYE5 

Genbank Protein ID

 D26183; D32208; U20616; Z73322; U53879; AY557944; BK006945 

Genbank Nucleotide ID

 BAA05171.1; BAA06907.1; AAA70169.1; CAA97722.1; AAB82384.1; AAS56270.1; DAA09461.1 

Protein Name

 Suppressor protein STM1 

Protein Synonyms/Alias

 3BP1; GU4 nucleic-binding protein 2; G4p2 protein; POP2 multicopy suppressor protein 4; Ribosomal subunits association factor; AF; TOM1 suppressor protein 1; Triplex-binding protein 1 

Gene Name

 STM1 

Gene Synonyms/Alias

 MPT4; STO1; YLR150W; L9634.1 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
34	KSNTSSKKADVPPPS	ubiquitination	[1]
46	PPSADPSKARKNRPR	ubiquitination	[2]
74	GRRNNRSKDVTDSAT	acetylation	[3]
74	GRRNNRSKDVTDSAT	ubiquitination	[1]
114	NQGWGDDKKELSAEK	acetylation	[4]
121	KKELSAEKEAQADAA	acetylation	[4]
121	KKELSAEKEAQADAA	ubiquitination	[2]
143	AEAEDAGKPKTAQLS	acetylation	[4]
143	AEAEDAGKPKTAQLS	ubiquitination	[2]
165	QANNQFNKVPEAKKV	ubiquitination	[1]
171	NKVPEAKKVELDAER	acetylation	[4]
171	NKVPEAKKVELDAER	ubiquitination	[1, 2]
184	ERIETAEKEAYVPAT	ubiquitination	[1, 2]
192	EAYVPATKVKNVKSK	ubiquitination	[1]
244	RGGRGARKGNNTANA	ubiquitination	[1]
260	NSANTVQKNRNIDVS	ubiquitination	[1]

Reference

 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
 [4] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 

Functional Description

 Binds specifically G4 quadruplex (these are four- stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs. Acts with CDC13 to control telomere length homeostasis. Involved in the control of the apoptosis-like cell death. 

Sequence Annotation

 MOD_RES 2 2 N-acetylserine.
 MOD_RES 55 55 Phosphoserine.
 MOD_RES 118 118 Phosphoserine.
 MOD_RES 229 229 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 273 AA 

Protein Sequence

Gene Ontology

 GO:0022626; C:cytosolic ribosome; IDA:SGD.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005844; C:polysome; IDA:SGD.
 GO:0042162; F:telomeric DNA binding; IDA:SGD.
 GO:0045142; F:triplex DNA binding; IDA:SGD.
 GO:0043066; P:negative regulation of apoptotic process; IDA:SGD.
 GO:0043558; P:regulation of translational initiation in response to stress; IMP:SGD.
 GO:0000723; P:telomere maintenance; IGI:SGD.
 GO:0031929; P:TOR signaling cascade; IMP:SGD.
 GO:0006414; P:translational elongation; IMP:SGD. 

Interpro

 IPR027204; Stm1.
 IPR019084; Stm1_N. 

Pfam

 PF09598; Stm1_N 

SMART

  

PROSITE

  

PRINTS