UBP3/YER151C Protein Information Help

Standard Name Ubp3p 1
Systematic Name Yer151cp
Alias Blm3p 2
ORF Classification Verified
Description Ubiquitin-specific protease involved in transport and osmotic response; interacts with Bre5p to co-regulate anterograde and retrograde transport between the ER and Golgi; involved in transcription elongation in response to osmostress through phosphorylation at Ser695 by Hog1p; inhibitor of gene silencing; cleaves ubiquitin fusions but not polyubiquitin; also has mRNA binding activity; protein abundance increases in response to DNA replication stress (1, 3, 4, 5, 6, 7, 8)
Name Description UBiquitin-specific Protease 1
Experimental Data
Molecules/cell 2210 9
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 912
Molecular Weight (Da) 101,916
Isoelectric Point (pI) 7.92

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Ubp3p (InterPro)
Physical Interactions There are 483 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI00001379DE | Q01477
MIPS: YER151C
NCBI: 159795228 | 159795230 | 173130 | 398364935 | 401244 | 603391 | NP_011078.3 | NM_001179041.3
GenBank/EMBL/DDBJ: DAA07812.1 | M94917 | U18917
External Classifications EC: 3.1.2.15 [Ubiquitin thiolesterase]
EC: 3.4.19.12 [Ubiquitinyl hydrolase 1]
Amino Acid Sequence (or in FASTA format)
       1  MNMQDANKEE SYSMYPKTSS PPPPTPTNMQ IPIYQAPLQM YGYTQAPYLY
      51  PTQIPAYSFN MVNQNQPIYH QSGSPHHLPP QNNINGGSTT NNNNINKKKW
     101  HSNGITNNNG SSGNQGANSS GSGMSYNKSH TYHHNYSNNH IPMMASPNSG
     151  SNAGMKKQTN SSNGNGSSAT SPSYSSYNSS SQYDLYKFDV TKLKNLKENS
     201  SNLIQLPLFI NTTEAEFAAA SVQRYELNMK ALNLNSESLE NSSVEKSSAH
     251  HHTKSHSIPK HNEEVKTETH GEEEDAHDKK PHASKDAHEL KKKTEVKKED
     301  AKQDRNEKVI QEPQATVLPV VDKKEPEESV EENTSKTSSP SPSPPAAKSW
     351  SAIASDAIKS RQASNKTVSG SMVTKTPISG TTAGVSSTNM AAATIGKSSS
     401  PLLSKQPQKK DKKYVPPSTK GIEPLGSIAL RMCFDPDFIS YVLRNKDVEN
     451  KIPVHSIIPR GIINRANICF MSSVLQVLLY CKPFIDVINV LSTRNTNSRV
     501  GTSSCKLLDA CLTMYKQFDK ETYEKKFLEN ADDAEKTTES DAKKSSKSKS
     551  FQHCATADAV KPDEFYKTLS TIPKFKDLQW GHQEDAEEFL THLLDQLHEE
     601  LISAIDGLTD NEIQNMLQSI NDEQLKVFFI RNLSRYGKAE FIKNASPRLK
     651  ELIEKYGVIN DDSTEENGWH EVSGSSKRGK KTKTAAKRTV EIVPSPISKL
     701  FGGQFRSVLD IPNNKESQSI TLDPFQTIQL DISDAGVNDL ETAFKKFSEY
     751  ELLPFKSSSG NDVEAKKQTF IDKLPQVLLI QFKRFSFINN VNKDNAMTNY
     801  NAYNGRIEKI RKKIKYGHEL IIPEESMSSI TLKNNTSGID DRRYKLTGVI
     851  YHHGVSSDGG HYTADVYHSE HNKWYRIDDV NITELEDDDV LKGGEEASDS
     901  RTAYILMYQK RN*                                        

external links for Ubp3p
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


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Ubp3p
1) Baker RT, et al.  (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J Biol Chem 267(32):23364-75
2) McCullock S, et al.  (2006) blm3-1 Is an Allele of UBP3, a Ubiquitin Protease that Appears to Act During Transcription of Damaged DNA. J Mol Biol 363(3):660-72
3) Moazed D and Johnson D  (1996) A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Cell 86(4):667-77
4) Cohen M, et al.  (2003) Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nat Cell Biol 5(7):661-7
5) Cohen M, et al.  (2003) Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport. J Biol Chem 278(52):51989-92
6) Tsvetanova NG, et al.  (2010) Proteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae.LID - e12671 [pii] PLoS One 5(9)
7) Sole C, et al.  (2011) Control of Ubp3 ubiquitin protease activity by the Hog1 SAPK modulates transcription upon osmostress.LID - 10.1038/emboj.2011.227 [doi] EMBO J ()
8) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
9) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41