CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007388
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphatidylinositol 4,5-bisphosphate 5-phosphatase INP51 
Protein Synonyms/Alias
 Synaptojanin-like protein 1 
Gene Name
 INP51 
Gene Synonyms/Alias
 SJL1; YIL002C; YIA2C 
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
384YSSSVLTKSPHKLLYacetylation[1]
780KNYDTSEKMRIPAWTubiquitination[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
 Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5- bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth. 
Sequence Annotation
 DOMAIN 151 480 SAC.  
Keyword
 Complete proteome; Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Lipid metabolism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 946 AA 
Protein Sequence
MRLFIGRRSR SIVISSNNYC LSFQRLRSIP GASSQQRQLS KTPSVTIKSY PDTDLSSDSN 60
YLEVKSCIFN GLLGLVCLNG DIYVAVISGV QNVGFPRWKL IDHQVRPSES IYKVLDVDFY 120
SLENDVFDYL LCERSEQNYD KLIHEHPCGP LKKLFSDGTF YYSRDFDISN IVKNHGLSHN 180
LEYTVDNQDL SFIWNANLAS EVINWRSKIS NEEKQLFANA GFLTFVIRGY CKTALIEDGP 240
NTASITIISR ISTESKQDTL ELEGISEDGR VSLFVETEIV VTTEKFIFSY TQVNGSIPLF 300
WESVESQLLY GKKIKVTKDS IEAQGAFDRH FDNLTSKYGV VSIVNIIKPK SESQEKLALT 360
YKDCAESKGI KITNIEYSSS VLTKSPHKLL YLLKQDIYEF GAFAYDISRG IYFAKQTGVL 420
RISAFDSIEK PNTVERLVSK EVLELTTNEI DVFELTSPFL DAHDKLWSEN YYWLDRTYTK 480
HTKNSGKYTK VYSKLFGSRV RLYDPLHIYI SQYLKQLRSK YTFEKDISIF AGTFNISGKI 540
PKDDIKDWIF PKSMSKEDEM ADLYVIGLEE VVELTPGHML ATDPYVRQFW EKKILTLLNG 600
PGRKKKYIRL WSTQLGGILL LLFMNETEYS KVKHIEGDVK KTGFGGMASN KGAVAVSFKY 660
SATRFCVLVS HLAAGLENVE QRHNDYKTIA KSIRFSKGLR IKDHDAIIWM GDFNYRILMS 720
NEDVRRKIVS KEYASLFEKD QLNQQMIAGE SFPYFHEMAI DFPPTYKFDP GTKNYDTSEK 780
MRIPAWTDRI LSRGEVLEQL EYKCCEDILF SDHRPVYAIF RARVTVVDEQ KKTTLGTQIY 840
EKIMERLEGL DDDEKIAVLS DDAFVIESFE GSDSIAGPTH SPTPIPEPKR GRKLPPPSSD 900
LKKWWIGSGK QVKVVLDVDP AVYMINPKRD PNPFVENEDE PLFIER 946 
Gene Ontology
 GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0016020; C:membrane; IDA:SGD.
 GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:SGD.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:SGD.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR005135; Endo/exonuclease/phosphatase.
 IPR000300; IPPc.
 IPR002013; Syja_N. 
Pfam
 PF03372; Exo_endo_phos
 PF02383; Syja_N 
SMART
 SM00128; IPPc 
PROSITE
 PS50275; SAC 
PRINTS