| Tag | Content |
|---|
| CPLM ID | CPLM-011191 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Pumilio homology domain family member 6 |
Protein Synonyms/Alias | |
Gene Name | PUF6 |
Gene Synonyms/Alias | YDR496C; D9719.2 |
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 |
|---|
| 450 | KYFSPIVKNELLRYI | 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 | RNA-binding protein involved in post-transcriptional regulation. Component of the ASH1 mRNP which transports the ASH1 mRNA to the distal tip of the bud, where the ASH1 protein is translated and targeted to the daughter cell nucleus. Binds to the ASH1 3'-UTR containing the PUF consensus UUGU segment and represses its translation. This silencing of ASH1 mRNA is critical for asymmetric seggregation of ASH1 to the daughter cell nucleus. |
Sequence Annotation | DOMAIN 133 483 PUM-HD.
REPEAT 155 191 Pumilio 1.
REPEAT 192 227 Pumilio 2.
REPEAT 228 264 Pumilio 3.
REPEAT 340 376 Pumilio 4.
REPEAT 377 413 Pumilio 5.
REPEAT 415 450 Pumilio 6.
MOD_RES 31 31 Phosphoserine; by CK2.
MOD_RES 34 34 Phosphoserine; alternate.
MOD_RES 34 34 Phosphoserine; by CK2; alternate.
MOD_RES 35 35 Phosphoserine; alternate.
MOD_RES 35 35 Phosphoserine; by CK2; alternate. |
Keyword | Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding; Translation regulation; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 656 AA |
Protein Sequence | MAPLTKKTNG KRSAKEVSHS EKKLAKKPRI SIDSSDEESE LSKKEDAVSS SSDDDDLDDL 60
STSDSEAEEE ADELDISDDS EEHENENEEK EGKDKSEGGE NGNHTEQRKL LKERKMQRKS 120
GTQVQQIKSV WERLRVKTPP LPKQIREKLS NEIWELSKDC ISDLVLKHDA SRIVQTLVKY 180
SSKDRREQIV DALKGKFYVL ATSAYGKYLL VKLLHYGSRS SRQTIINELH GSLRKLMRHR 240
EGAYVVEDLF VLYATHEQRQ QMIKEFWGSE YAVFRETHKD LTIEKVCESS IEKRNIIARN 300
LIGTITASVE KGSTGFQILH AAMREYVKIA NEKEISEMIE LLHEQFAELV HTPEGSDVAC 360
TLVARANAKE RKLILKALKN HAEKLIKNEY GNIVFITILN CVDDTVLVFK TFSPTVKEHL 420
QEFIIDKFGR RPWLYILLGL DGKYFSPIVK NELLRYIELS KATSKKDPLQ RRHELLSKFA 480
PMFLSTISKD YSSILTENLG CQFIAEVLIN DELYAQLNEK DQEKYQQVLN NILTTFKGDI 540
TEEEHPIHRA FSTRLLKALI QGGKWNNKEK KVIPLKNVQG LGVPFAEKLY DEIIDSSNLL 600
EWINNADSSF TIVALYETLK DQKEGKPFLK DLRGVQSKIT TDESNKGSQL LAKLLK 656 |
Gene Ontology | GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell. GO:0015934; C:large ribosomal subunit; IDA:SGD. GO:0005730; C:nucleolus; IDA:SGD. GO:0003730; F:mRNA 3'-UTR binding; IDA:SGD. GO:0000900; F:translation repressor activity, nucleic acid binding; IDA:SGD. GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD. GO:0006810; P:transport; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |