CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011129
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sporulation-specific protein 71 
Protein Synonyms/Alias
  
Gene Name
 SPO71 
Gene Synonyms/Alias
 YDR104C; YD8557.13c 
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
30SPQNANVKVFTIPRHacetylation[1]
348MLWKTSQKYGTYLDEubiquitination[2]
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]
 [2] 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
 Required for spore wall formation during sporulation. 
Sequence Annotation
 DOMAIN 1030 1229 PH.  
Keyword
 Complete proteome; Reference proteome; Sporulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1245 AA 
Protein Sequence
MDSIVNVVED DVKYAQRVTS FSSPQNANVK VFTIPRHSFT AFRLSYVSPT ELSACSQVTL 60
LGGIPKQWYA DQNNQVWKLL TKISLRKVRK QSDMLRRYGY GTIYKKRVGK IPTALYLRKH 120
FTWSYEDNTS IHNGHRLKEA EMEMKRTRSS PVQKSEYKLS LPRRCRSSSD QNFMRQELLK 180
EKKSELSRNN SLPLIDTAQA VDIHPVLHEE DQENTNKRNK SLLSNLKRKD LGESKSISRK 240
DYSHFDRIPS PSSARSVGET DFNYNREPSE DTLRYPDSII EVTNRTSPAP NSILSRSGQF 300
VNSNDLSDGF STSNTINNVG LNANEKIFFN ALQSMEKENL MLWKTSQKYG TYLDERRKSA 360
DAFQKRERGS CVDIGKLHSS HLPFINILPP WPTELTEEER IIHDRLASKH SHHIRKHVHN 420
ARNKTSCKIK DSVGTFLGMT NSLTNKATVK KRTGQILKKE KMLVMVKEAI QNKVPLPNFS 480
ENECFDTRVS ERWKEYIVIA RSTGRFDPPI LLQFYRHRHI PEIEDISSIA TKYHRNPLDF 540
FLSRNCIVKF YSSLDKTISI QKPDKRLGGF IDESIEKKDE LKHYSPIKIF ILRCSSIRSS 600
GRWYKFLLES LDRQLFTPAI NLKIPLTEIS IKINLNEIIF QKLIDLGKQE KDRLKICFLQ 660
RGYKIFQHPI LRYFTVAILE KLKLAHYDYL IRKWDTENPV LGCALKRYDR LEWIPCDEDS 720
LVTGIFAFCQ SHLIQYRPIA NRLRETKSLE GKCLKEPTPI EGFLIRLTDK YGSARTNFGK 780
YSISTAYFFT CENLLFSMKA YRANPPLPID SMIDDTSTEI EKEEIWKQWK KIPEVYEQQP 840
YPLDTNDHIE WMNCQTTQSE YDSRDFYAFH CFHRRIDQIL KTDNVIDLTE VKDIYQGTRT 900
DYEADKIKYG VYKEASEIFW HRNYEIDDVS RSVINIETSN GLLLKLLATS ATVAEEWVIK 960
LKQMISYWKN KQREDTERLL KIRRSNAGLL MLNGEEETKI GENTLRWIVE HGRADEQTFN 1020
ANGISLSRPL IQKGPLYQKP HKHSVFSKYY VVLISGFIVL FHCFHRSTTG FAKEVLEYAH 1080
YVTIPIDDCY LYSGTTTELD LLQRDRTFDE INYGSHALPR VYGDGWRSVE DESSRCFTLW 1140
FGTRRALSSN RLQKKGNEKQ YTQDYGRQDN NIDPPSAPEA DLNNSNVPSN TDKIHFTKKL 1200
GVSGKSMVFM ARSRQERDLW VMSIYYELER LRRTASTSNS RNQTM 1245 
Gene Ontology
 GO:0005619; C:ascospore wall; IMP:SGD.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0030476; P:ascospore wall assembly; IMP:SGD. 
Interpro
 IPR001849; Pleckstrin_homology. 
Pfam
  
SMART
 SM00233; PH 
PROSITE
 PS50003; PH_DOMAIN 
PRINTS