Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-559292-00660
Entry Name
UniProt Accession
Theoretical PI
5.03
Molecular Weight
40748.6
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Serine/threonine-protein kinase ENV7
Protein Synonyms/Alias
2.7.11.1; Late endosome and vacuole interface protein 7;
Gene Name
ENV7
Gene Synonyms/Alias
YPL236C;
Created Date
31-OCT-2006
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
13
Canonical
LELFQNLCCCRGFSD
[1][2]
S-Palmitoylation
14
Canonical
ELFQNLCCCRGFSDA
[1][2]
S-Palmitoylation
15
Canonical
LFQNLCCCRGFSDAT
[1][2]
S-Palmitoylation
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
NCBI Taxa ID
559292
Reference
[1] Roth AF, Wan J, Bailey AO, Sun B, Kuchar JA, Green WN, Phinney BS, Yates JR3rd, Davis NG. Global analysis of protein palmitoylation in yeast. Cell. 2006 Jun2;125(5):1003-13.[PMID:16751107]
[2] Manandhar SP, Calle EN, Gharakhanian E. Distinct palmitoylation events at the amino-terminal conserved cysteines of Env7 direct its stability, localization,and vacuolar fusion regulation in S. cerevisiae. J Biol Chem. 2014 Apr18;289(16):11431-42. doi: 10.1074/jbc.M113.524082. Epub 2014 Mar 7.[PMID:24610781]
Functional Description
Serine/threonine-protein kinase involved in vacuolar processing and morphology.
Sequence Annotation
Domain: 30 364 Protein kinase.
Nucleotide-binding: 36 44 ATP.
Active site: 215 215 Proton acceptor.
Binding site: 69 69 ATP.
Protein Length
364 AA.
Protein Sequence
(Canonical)
MISIVLELFQ NLCCCRGFSD ATIRVNDKRY RIQRLLGEGG MSFVYLVQLS KNSLIIDNGI  60
ATPELYALKK IICPSVESIS NGMREIENYK RFQSPYVIKS IDSQVMQEKD GSKTIYIVLP  120
YYSLGSLQDS INRRLLEGTF VSEAECVRIM LGVTRGLLCL HDPASRQDNA TSRVNVDAVS  180
MTYSDETAML LEDTPLEMDM LSSNSAGSIA YAHRDITPSN ILFSSDGLPV IGDLGSCSQA  240
DITIENRHQL SELQEWVNDN CTLPYTPPEL LNLKLNQVLS SKVDIWSLGC TFYTLMFGIS  300
PFEREEQIHG ASLTYAINTG KYSFPRNSRF SEGLLSVIKK CIQVDPIQRP TTSQLLNLLQ  360
DLDT                                                               364
FASTA
(Canonical)
>LipidDB-559292-00660|Q12003
MISIVLELFQNLCCCRGFSDATIRVNDKRYRIQRLLGEGGMSFVYLVQLSKNSLIIDNGI
ATPELYALKKIICPSVESISNGMREIENYKRFQSPYVIKSIDSQVMQEKDGSKTIYIVLP
YYSLGSLQDSINRRLLEGTFVSEAECVRIMLGVTRGLLCLHDPASRQDNATSRVNVDAVS
MTYSDETAMLLEDTPLEMDMLSSNSAGSIAYAHRDITPSNILFSSDGLPVIGDLGSCSQA
DITIENRHQLSELQEWVNDNCTLPYTPPELLNLKLNQVLSSKVDIWSLGCTFYTLMFGIS
PFEREEQIHGASLTYAINTGKYSFPRNSRFSEGLLSVIKKCIQVDPIQRPTTSQLLNLLQ
DLDT
Gene Ontology
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005773; C:vacuole; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0004674; F:protein serine/threonine kinase activity; ISS:SGD
GO:0032889; P:regulation of vacuole fusion, non-autophagic; IMP:SGD
GO:0006624; P:vacuolar protein processing; IMP:SGD
Interpro
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
Pfam
Pfam; PF00069; Pkinase;
SMART
PROSITE
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PRINTS