CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006309
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein SLA2 
Protein Synonyms/Alias
 Transmembrane protein MOP2 
Gene Name
 SLA2 
Gene Synonyms/Alias
 END4; MOP2; UFG1; YNL243W; N1102 
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
225DAALQPLKERYELQHubiquitination[1]
274INDVDESKEIKFKKRubiquitination[1]
739LLNIQSVKSNKETNPubiquitination[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
 Required for cellular morphogenesis and polarization of the cortical cytoskeleton. It might act in concert with proteins such as CDC42 and CDC43 to limit the region of cortical patch formation to the cortex of the bud. Required for the accumulation and/or maintenance of plasma membrane H(+)-ATPase on the cell surface. 
Sequence Annotation
 DOMAIN 1 127 ENTH.
 DOMAIN 717 965 I/LWEQ.
 MOD_RES 294 294 Phosphothreonine.
 MOD_RES 298 298 Phosphothreonine.
 MOD_RES 308 308 Phosphoserine.
 MOD_RES 555 555 Phosphoserine.  
Keyword
 Actin-binding; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 968 AA 
Protein Sequence
MSRIDSDLQK ALKKACSVEE TAPKRKHVRA CIVYTWDHQS SKAVFTTLKT LPLANDEVQL 60
FKMLIVLHKI IQEGHPSALA EAIRDRDWIR SLGRVHSGGS SYSKLIREYV RYLVLKLDFH 120
AHHRGFNNGT FEYEEYVSLV SVSDPDEGYE TILDLMSLQD SLDEFSQIIF ASIQSERRNT 180
ECKISALIPL IAESYGIYKF ITSMLRAMHR QLNDAEGDAA LQPLKERYEL QHARLFEFYA 240
DCSSVKYLTT LVTIPKLPVD APDVFLINDV DESKEIKFKK REPSVTPART PARTPTPTPP 300
VVAEPAISPR PVSQRTTSTP TGYLQTMPTG ATTGMMIPTA TGAANAIFPQ ATAQMQPDFW 360
ANQQAQFANE QNRLEQERVQ QLQQQQAQQE LFQQQLQKAQ QDMMNMQLQQ QNQHQNDLIA 420
LTNQYEKDQA LLQQYDQRVQ QLESEITTMD STASKQLANK DEQLTALQDQ LDVWERKYES 480
LAKLYSQLRQ EHLNLLPRFK KLQLKVNSAQ ESIQKKEQLE HKLKQKDLQM AELVKDRDRA 540
RLELERSINN AEADSAAATA AAETMTQDKM NPILDAILES GINTIQESVY NLDSPLSWSG 600
PLTPPTFLLS LLESTSENAT EFATSFNNLI VDGLAHGDQT EVIHCVSDFS TSMATLVTNS 660
KAYAVTTLPQ EQSDQILTLV KRCAREAQYF FEDLMSENLN QVGDEEKTDI VINANVDMQE 720
KLQELSLAIE PLLNIQSVKS NKETNPHSEL VATADKIVKS SEHLRVDVPK PLLSLALMII 780
DAVVALVKAA IQCQNEIATT TSIPLNQFYL KNSRWTEGLI SAAKAVAGAT NVLITTASKL 840
ITSEDNENTS PEQFIVASKE VAASTIQLVA ASRVKTSIHS KAQDKLEHCS KDVTDACRSL 900
GNHVMGMIED DHSTSQQQQP LDFTSEHTLK TAEMEQQVEI LKLEQSLSNA RKRLGEIRRH 960
AYYNQDDD 968 
Gene Ontology
 GO:0030479; C:actin cortical patch; IDA:SGD.
 GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
 GO:0000131; C:incipient cellular bud site; IDA:SGD.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0043332; C:mating projection tip; IDA:SGD.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0007015; P:actin filament organization; IMP:SGD.
 GO:0007121; P:bipolar cellular bud site selection; TAS:SGD.
 GO:0006897; P:endocytosis; IMP:SGD.
 GO:0006887; P:exocytosis; TAS:SGD.
 GO:0031505; P:fungal-type cell wall organization; TAS:SGD. 
Interpro
 IPR011417; ANTH_dom.
 IPR008942; ENTH_VHS.
 IPR013809; Epsin-like_N.
 IPR002558; ILWEQ_dom. 
Pfam
 PF07651; ANTH
 PF01608; I_LWEQ 
SMART
 SM00273; ENTH
 SM00307; ILWEQ 
PROSITE
 PS50942; ENTH
 PS50945; I_LWEQ 
PRINTS