Tag | Content |
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CPLM ID | CPLM-005290 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein SSD1 |
Protein Synonyms/Alias | Protein SRK1 |
Gene Name | SSD1 |
Gene Synonyms/Alias | CLA1; RLD1; SRK1; YDR293C; D9819.4 |
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 |
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667 | SNEYLDQKNPQKEKP | ubiquitination | [1] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | Can suppress the lethality due to deletion of SIT4, and partially the defects due to BCY1 disruption. Is implicated in the control of the cell cycle G1 phase. |
Sequence Annotation | MOD_RES 40 40 Phosphoserine. MOD_RES 164 164 Phosphoserine. MOD_RES 183 183 Phosphoserine. MOD_RES 227 227 Phosphothreonine. MOD_RES 286 286 Phosphoserine. MOD_RES 322 322 Phosphoserine. MOD_RES 491 491 Phosphoserine. MOD_RES 492 492 Phosphoserine. MOD_RES 688 688 Phosphotyrosine. |
Keyword | Cell cycle; Cell division; Complete proteome; Mitosis; Phosphoprotein; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1250 AA |
Protein Sequence | MSKNSNVNNN RSQEPNNMFV QTTGGGKNAP KQIHVAHRRS QSELTNLMIE QFTLQKQLEQ 60 VQAQQQQLMA QQQQLAQQTG QYLSGNSGSN NHFTPQPPHP HYNSNGNSPG MSAGGSRSRT 120 HSRNNSGYYH NSYDNNNNSN NPGSNSHRKT SSQSSIYGHS RRHSLGLNEA KKAAAEEQAK 180 RISGGEAGVT VKIDSVQADS GSNSTTEQSD FKFPPPPNAH QGHRRATSNL SPPSFKFPPN 240 SHGDNDDEFI ATSSTHRRSK TRNNEYSPGI NSNWRNQSQQ PQQQLSPFRH RGSNSRDYNS 300 FNTLEPPAIF QQGHKHRASN SSVHSFSSQG NNNGGGRKSL FAPYLPQANI PELIQEGRLV 360 AGILRVNKKN RSDAWVSTDG ALDADIYICG SKDRNRALEG DLVAVELLVV DDVWESKKEK 420 EEKKRRKDAS MQHDLIPLNS SDDYHNDASV TAATSNNFLS SPSSSDSLSK DDLSVRRKRS 480 STINNDSDSL SSPTKSGVRR RSSLKQRPTQ KKNDDVEVEG QSLLLVEEEE INDKYKPLYA 540 GHVVAVLDRI PGQLFSGTLG LLRPSQQANS DNNKPPQSPK IAWFKPTDKK VPLIAIPTEL 600 APKDFVENAD KYSEKLFVAS IKRWPITSLH PFGILVSELG DIHDPDTEID SILRDNNFLS 660 NEYLDQKNPQ KEKPSFQPLP LTAESLEYRR NFTDTNEYNI FAISELGWVS EFALHVRNNG 720 NGTLELGCHV VDVTSHIEEG SSVDRRARKR SSAVFMPQKL VNLLPQSFND ELSLAPGKES 780 ATLSVVYTLD SSTLRIKSTW VGESTISPSN ILSLEQLDEK LSTGSPTSYL STVQEIARSF 840 YARRINDPEA TLLPTLSLLE SLDDEKVKVD LNILDRTLGF VVINEIKRKV NSTVAEKIYT 900 KLGDLALLRR QMQPIATKMA SFRKKIQNFG YNFDTNTADE LIKGVLKIKD DDVRVGIEIL 960 LFKTMPRARY FIAGKVDPDQ YGHYALNLPI YTHFTAPMRR YADHVVHRQL KAVIHDTPYT 1020 EDMEALKITS EYCNFKKDCA YQAQEQAIHL LLCKTINDMG NTTGQLLTMA TVLQVYESSF 1080 DVFIPEFGIE KRVHGDQLPL IKAEFDGTNR VLELHWQPGV DSATFIPADE KNPKSYRNSI 1140 KNKFRSTAAE IANIELDKEA ESEPLISDPL SKELSDLHLT VPNLRLPSAS DNKQNALEKF 1200 ISTTETRIEN DNYIQEIHEL QKIPILLRAE VGMALPCLTV RALNPFMKRV 1250 |
Gene Ontology | GO:0005935; C:cellular bud neck; IDA:SGD. GO:0000932; C:cytoplasmic mRNA processing body; IDA:SGD. GO:0010494; C:cytoplasmic stress granule; IDA:SGD. GO:0005634; C:nucleus; IDA:SGD. GO:0048027; F:mRNA 5'-UTR binding; IDA:SGD. GO:0004540; F:ribonuclease activity; IEA:InterPro. GO:0000900; F:translation repressor activity, nucleic acid binding; IGI:SGD. GO:0051301; P:cell division; IEA:UniProtKB-KW. GO:0008298; P:intracellular mRNA localization; IMP:SGD. GO:0007067; P:mitosis; IEA:UniProtKB-KW. GO:0060237; P:regulation of fungal-type cell wall organization; IGI:SGD. |
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Pfam | |
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PRINTS | |