| Tag | Content |
|---|
| CPLM ID | CPLM-006118 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Transcription factor SFP1 |
Protein Synonyms/Alias | Split finger protein 1 |
Gene Name | SFP1 |
Gene Synonyms/Alias | YLR403W; L8084.4 |
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 |
|---|
| 655 | GDGMGSAKDKPYRCE | 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 | Transcription factor that regulates ribosomal protein (RP) and ribosome biogenesis (Ribi) gene expression in response to nutrients and stress. Promotes RP gene expression under optimal growth conditions. Leaves the nucleus upon environmental challenges, resulting in a down-regulation of RP gene transcription. The effect of the environmental cues on SFP1 localization is mediated through the TOR pathway. Also regulates the expression of genes involved in the G2/M transition during the mitotic cell cycle and the DNA-damage response. Required for carbon-source modulation of cell size. |
Sequence Annotation | ZN_FING 598 623 C2H2-type 1.
ZN_FING 659 683 C2H2-type 2.
REGION 230 458 Prion domain (PrD). |
Keyword | Amyloid; Complete proteome; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Prion; Reference proteome; Repeat; Stress response; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 683 AA |
Protein Sequence | MDFTTMTMAS NMATSTTTTA TSAHASINSS SNFNIDIDSN QNTPSILINN NSDSSNGKNT 60
DFNGVNNIHQ KNIMNNTNNV HLYSPNIMDQ TLLTPQDIAK LRRESIAHSQ GMGGVSWGSI 120
SVGSWLRDEI ISRRNSIVPA SANGAASAAA SATTTATNTL QIQQPTKRPS VSNPPYHRGY 180
SISPQIAYTA YLPNLEKQYC KDYSCCGLSL PGLHDLLRHY EEAHISTSPN TTNMSQIPMN 240
SAGNTSSSVR MTNNTSSANY NLQNNMAANT KNAGHKTNTM QAHSSNATNN TSINNMHANL 300
QSNMDSNSTI RQSQHPHHQQ NIIQQQLQSN SVNHTSGAVP TPSVMGSATA SSTTANPNVI 360
SITGAPNSGL SMANHSQQLH LNGNLVDAVS TNDVFLRTSN SPSRHVPHNK QINSNNNSGI 420
NINNNTSHNS NINMGSKNAM VNRPHTFNNY SLNKTSRNPI QHQSRKIDPH QTDLSPLVLV 480
QDIDLSFMDD DILGPSNHNS MNSVVNPTTG SHNYNTFHSS VHAKSSQNMV EDQDIDDIDD 540
DDDVDDDDDD DDDDDTENGS SSNGKSVHNN NYKMPQQAYI DDPARRLYVM DHEEQKPFKC 600
PVIGCEKTYK NQNGLKYHRL HGHQNQKLHE NPDGTFSVID PDSTDSFGDG MGSAKDKPYR 660
CEVCGKRYKN LNGLKYHRGH STH 683 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:SGD. GO:0005634; C:nucleus; IDA:SGD. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0060963; P:positive regulation of ribosomal protein gene transcription from RNA polymerase II promoter; IMP:SGD. GO:0008361; P:regulation of cell size; IMP:SGD. GO:0006950; P:response to stress; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |