CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
667SNEYLDQKNPQKEKPubiquitination[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, VillĂ©n 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. 
Interpro
 IPR001900; RNase_II/R.
 IPR022966; RNase_II/R_CS. 
Pfam
 PF00773; RNB 
SMART
 SM00955; RNB 
PROSITE
 PS01175; RIBONUCLEASE_II 
PRINTS