| Tag | Content |
|---|
| CPLM ID | CPLM-010843 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Pre-tRNA-processing protein PTA1 |
Protein Synonyms/Alias | |
Gene Name | PTA1 |
Gene Synonyms/Alias | YAL043C; FUN39 |
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 |
|---|
| 403 | DQLKILQKYTLNKAS | acetylation | [1] | | 569 | NKSTSAIKEIAPPFE | 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 | Essential in pre-tRNA processing. 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. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. |
Sequence Annotation | MOD_RES 500 500 Phosphoserine. |
Keyword | Complete proteome; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; tRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 785 AA |
Protein Sequence | MSSAEMEQLL QAKTLAMHNN PTEMLPKVLE TTASMYHNGN LSKLKLPLAK FFTQLVLDVV 60
SMDSPIANTE RPFIAAQYLP LLLAMAQSTA DVLVYKNIVL IMCASYPLVL DLVAKTSNQE 120
MFDQLCMLKK FVLSHWRTAY PLRATVDDET DVEQWLAQID QNIGVKLATI KFISEVVLSQ 180
TKSPSGNEIN SSTIPDNHPV LNKPALESEA KRLLDMLLNY LIEEQYMVSS VFIGIINSLS 240
FVIKRRPQTT IRILSGLLRF NVDAKFPLEG KSDLNYKLSK RFVERAYKNF VQFGLKNQII 300
TKSLSSGSGS SIYSKLTKIS QTLHVIGEET KSKGILNFDP SKGNSKKTLS RQDKLKYISL 360
WKRQLSALLS TLGVSTKTPT PVSAPATGSS TENMLDQLKI LQKYTLNKAS HQGNTFFNNS 420
PKPISNTYSS VYSLMNSSNS NQDVTQLPND ILIKLSTEAI LQMDSTKLIT GLSIVASRYT 480
DLMNTYINSV PSSSSSKRKS DDDDDGNDNE EVGNDGPTAN SKKIKMETEP LAEEPEEPED 540
DDRMQKMLQE EESAQEISGD ANKSTSAIKE IAPPFEPDSL TQDEKLKYLS KLTKKLFELS 600
GRQDTTRAKS SSSSSILLDD DDSSSWLHVL IRLVTRGIEA QEASDLIREE LLGFFIQDFE 660
QRVSLIIEWL NEEWFFQTSL HQDPSNYKKW SLRVLESLGP FLENKHRRFF IRLMSELPSL 720
QSDHLEALKP ICLDPARSSL GFQTLKFLIM FRPPVQDTVR DLLHQLKQED EGLHKQCDSL 780
LDRLK 785 |
Gene Ontology | GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD. GO:0006379; P:mRNA cleavage; IMP:SGD. GO:0006378; P:mRNA polyadenylation; IMP:SGD. GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IPI:SGD. GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IPI:SGD. GO:0008033; P:tRNA processing; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |