| Tag | Content |
|---|
| CPLM ID | CPLM-011378 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Endoribonuclease YSH1 |
Protein Synonyms/Alias | Yeast 73 kDa homolog 1; mRNA 3'-end-processing protein YSH1 |
Gene Name | YSH1 |
Gene Synonyms/Alias | BRR5; YLR277C |
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 |
|---|
| 521 | NLDSQAEKGLVDEEE | acetylation | [1] |
|
Reference | [1] 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 | Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Has endonuclease activity. |
Sequence Annotation | ACT_SITE 408 408 Proton donor (Potential).
METAL 68 68 Zinc 1 (By similarity).
METAL 70 70 Zinc 1 (By similarity).
METAL 72 72 Zinc 2 (By similarity).
METAL 73 73 Zinc 2 (By similarity).
METAL 163 163 Zinc 1 (By similarity).
METAL 184 184 Zinc 1 (By similarity).
METAL 184 184 Zinc 2 (By similarity).
METAL 430 430 Zinc 2 (By similarity).
MOD_RES 517 517 Phosphoserine; by ATM or ATR. |
Keyword | Complete proteome; Endonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleus; Phosphoprotein; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 779 AA |
Protein Sequence | MERTNTTTFK FFSLGGSNEV GRSCHILQYK GKTVMLDAGI HPAYQGLASL PFYDEFDLSK 60
VDILLISHFH LDHAASLPYV MQRTNFQGRV FMTHPTKAIY RWLLRDFVRV TSIGSSSSSM 120
GTKDEGLFSD EDLVDSFDKI ETVDYHSTVD VNGIKFTAFH AGHVLGAAMF QIEIAGLRVL 180
FTGDYSREVD RHLNSAEVPP LSSNVLIVES TFGTATHEPR LNRERKLTQL IHSTVMRGGR 240
VLLPVFALGR AQEIMLILDE YWSQHADELG GGQVPIFYAS NLAKKCMSVF QTYVNMMNDD 300
IRKKFRDSQT NPFIFKNISY LRNLEDFQDF GPSVMLASPG MLQSGLSRDL LERWCPEDKN 360
LVLITGYSIE GTMAKFIMLE PDTIPSINNP EITIPRRCQV EEISFAAHVD FQENLEFIEK 420
ISAPNIILVH GEANPMGRLK SALLSNFASL KGTDNEVHVF NPRNCVEVDL EFQGVKVAKA 480
VGNIVNEIYK EENVEIKEEI AAKIEPIKEE NEDNLDSQAE KGLVDEEEHK DIVVSGILVS 540
DDKNFELDFL SLSDLREHHP DLSTTILRER QSVRVNCKKE LIYWHILQMF GEAEVLQDDD 600
RVTNQEPKVK EESKDNLTNT GKLILQIMGD IKLTIVNTLA VVEWTQDLMN DTVADSIIAI 660
LMNVDSAPAS VKLSSHSCDD HDHNNVQSNA QGKIDEVERV KQISRLFKEQ FGDCFTLFLN 720
KDEYASNKEE TITGVVTIGK STAKIDFNNM KILECNSNPL KGRVESLLNI GGNLVTPLC 779 |
Gene Ontology | GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD. GO:0004521; F:endoribonuclease activity; IMP:SGD. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006379; P:mRNA cleavage; IMP:SGD. GO:0006378; P:mRNA polyadenylation; IMP:SGD. GO:0031126; P:snoRNA 3'-end processing; IMP:SGD. GO:0034247; P:snoRNA splicing; IMP:SGD. GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |