UniProt Accession

 DDI1_YEAST; P40087; D3DM50 

Genbank Protein ID

 U14002; AF034895; U18917; AY692945; BK006939 

Genbank Nucleotide ID

 AAB82066.1; AAC18522.1; AAB64670.1; AAT92964.1; DAA07804.1 

Protein Name

 DNA damage-inducible protein 1 

Protein Synonyms/Alias

 v-SNARE-master 1 

Gene Name

 DDI1 

Gene Synonyms/Alias

 VSM1; YER143W 

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
42	DCGFDKTKHDLYYNM	ubiquitination	[1]
61	SNRTQSLKELGLKTD	ubiquitination	[1]
171	NPDDPDNKKRIAELL	ubiquitination	[2, 3, 4]
257	ARGVGTGKIIGRIHQ	ubiquitination	[1, 3, 5]
325	LSEAEIPKSFQEGLP	ubiquitination	[1]
343	SVTTSSDKPLTPTKT	ubiquitination	[1, 6]
349	DKPLTPTKTSSTLPP	ubiquitination	[1]
410	FPRDAVVKALKQTNG	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] A proteomics approach to understanding protein ubiquitination.
 Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
 Nat Biotechnol. 2003 Aug;21(8):921-6. [PMID: 12872131]
 [3] Computational identification of ubiquitylation sites from protein sequences.
 Tung CW, Ho SY.
 BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
 [4] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [5] A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.
 Hitchcock AL, Auld K, Gygi SP, Silver PA.
 Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12735-40. [PMID: 14557538]
 [6] 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] 

Functional Description

 Acts as a linker between the 19S proteasome and polyubiquitinated proteins like the HO endonuclease and UFO1 via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control. Appears to act as negative regulator of constitutive exocytosis. May act at the level of secretory vesicle docking and fusion as a competitive inhibitor of SNARE assembly. 

Sequence Annotation

 DOMAIN 1 80 Ubiquitin-like.
 DOMAIN 389 428 UBA.
 MOD_RES 346 346 Phosphothreonine.
 CROSSLNK 171 171 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 257 257 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Cell membrane; Complete proteome; Cytoplasm; Isopeptide bond; Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 428 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0004190; F:aspartic-type endopeptidase activity; ISA:SGD.
 GO:0000149; F:SNARE binding; IDA:SGD.
 GO:0043130; F:ubiquitin binding; IDA:SGD.
 GO:0009306; P:protein secretion; IMP:SGD.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
 GO:0016192; P:vesicle-mediated transport; IMP:SGD. 

Interpro

 IPR001995; Peptidase_A2_cat.
 IPR021109; Peptidase_aspartic.
 IPR019103; Peptidase_aspartic_DDI1-type.
 IPR009060; UBA-like.
 IPR000449; UBA/transl_elong_EF1B_N.
 IPR015940; UBA/transl_elong_EF1B_N_euk. 

Pfam

 PF09668; Asp_protease
 PF00627; UBA 

SMART

 SM00165; UBA 

PROSITE

 PS50030; UBA
 PS50053; UBIQUITIN_2 

PRINTS