CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004982
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vacuolar protein sorting-associated protein 1 
Protein Synonyms/Alias
  
Gene Name
 VPS1 
Gene Synonyms/Alias
 LAM1; SPO15; YKR001C 
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
132FLHLPGKKFYNFDEIacetylation[1]
423LDPFDQIKDSDIRTIubiquitination[2]
561AVDPKTGKPLPTQPSubiquitination[2]
571PTQPSSSKAPVMEEKubiquitination[2]
578KAPVMEEKSGFFGGFubiquitination[2]
667LLEKLYGKQDIEELTacetylation[1]
667LLEKLYGKQDIEELTubiquitination[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
 Essential for protein sorting in meiotic cell division of Saccharomyces cerevisiae; it binds microtubules. Could also be involved in microtubule-associated motility. Necessary for membrane protein retention in a late Golgi compartment. Interacts with the MVP1 protein. 
Sequence Annotation
 DOMAIN 618 704 GED.
 NP_BIND 36 43 GTP (Potential).
 NP_BIND 178 182 GTP (Potential).
 NP_BIND 247 250 GTP (Potential).
 MOD_RES 579 579 Phosphoserine.
 MOD_RES 599 599 Phosphoserine.  
Keyword
 Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding; Meiosis; Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 704 AA 
Protein Sequence
MDEHLISTIN KLQDALAPLG GGSQSPIDLP QITVVGSQSS GKSSVLENIV GRDFLPRGTG 60
IVTRRPLVLQ LINRRPKKSE HAKVNQTANE LIDLNINDDD KKKDESGKHQ NEGQSEDNKE 120
EWGEFLHLPG KKFYNFDEIR KEIVKETDKV TGANSGISSV PINLRIYSPH VLTLTLVDLP 180
GLTKVPVGDQ PPDIERQIKD MLLKYISKPN AIILSVNAAN TDLANSDGLK LAREVDPEGT 240
RTIGVLTKVD LMDQGTDVID ILAGRVIPLR YGYIPVINRG QKDIEHKKTI REALENERKF 300
FENHPSYSSK AHYCGTPYLA KKLNSILLHH IRQTLPEIKA KIEATLKKYQ NELINLGPET 360
MDSASSVVLS MITDFSNEYA GILDGEAKEL SSQELSGGAR ISYVFHETFK NGVDSLDPFD 420
QIKDSDIRTI MYNSSGSAPS LFVGTEAFEV LVKQQIRRFE EPSLRLVTLV FDELVRMLKQ 480
IISQPKYSRY PALREAISNQ FIQFLKDATI PTNEFVVDII KAEQTYINTA HPDLLKGSQA 540
MVMVEEKLHP RQVAVDPKTG KPLPTQPSSS KAPVMEEKSG FFGGFFSTKN KKKLAALESP 600
PPVLKATGQM TERETMETEV IKLLISSYFS IVKRTIADII PKALMLKLIV KSKTDIQKVL 660
LEKLYGKQDI EELTKENDIT IQRRKECKKM VEILRNASQI VSSV 704 
Gene Ontology
 GO:0030479; C:actin cortical patch; IDA:SGD.
 GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
 GO:0005777; C:peroxisome; IDA:SGD.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IDA:SGD.
 GO:0030036; P:actin cytoskeleton organization; IGI:SGD.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0006897; P:endocytosis; IMP:SGD.
 GO:0060988; P:lipid tube assembly; IDA:SGD.
 GO:0007126; P:meiosis; IEA:UniProtKB-KW.
 GO:0016559; P:peroxisome fission; IMP:SGD.
 GO:0045053; P:protein retention in Golgi apparatus; IMP:SGD.
 GO:0006623; P:protein targeting to vacuole; IMP:SGD. 
Interpro
 IPR022812; Dynamin.
 IPR000375; Dynamin_central.
 IPR001401; Dynamin_GTPase.
 IPR019762; Dynamin_GTPase_CS.
 IPR003130; GED.
 IPR020850; GTPase_effector_domain_GED.
 IPR027417; P-loop_NTPase. 
Pfam
 PF01031; Dynamin_M
 PF00350; Dynamin_N
 PF02212; GED 
SMART
 SM00053; DYNc
 SM00302; GED 
PROSITE
 PS00410; DYNAMIN
 PS51388; GED 
PRINTS
 PR00195; DYNAMIN.