| Tag | Content |
|---|
| CPLM ID | CPLM-011464 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Uncharacterized PH domain-containing protein YPR091C |
Protein Synonyms/Alias | |
Gene Name | YPR091C |
Gene Synonyms/Alias | |
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 |
|---|
| 55 | TADEIDEKTRLLARD | ubiquitination | [1] | | 475 | VTNAIKSKFAEAVKE | ubiquitination | [1] | | 598 | SSSENSTKSRKYFKN | ubiquitination | [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 | |
Sequence Annotation | DOMAIN 114 266 PH.
MOD_RES 640 640 Phosphoserine.
MOD_RES 669 669 Phosphoserine.
MOD_RES 717 717 Phosphoserine.
MOD_RES 720 720 Phosphoserine.
MOD_RES 723 723 Phosphoserine.
CARBOHYD 228 228 N-linked (GlcNAc...) (Potential).
CARBOHYD 263 263 N-linked (GlcNAc...) (Potential).
CARBOHYD 279 279 N-linked (GlcNAc...) (Potential).
CARBOHYD 300 300 N-linked (GlcNAc...) (Potential).
CARBOHYD 391 391 N-linked (GlcNAc...) (Potential).
CARBOHYD 528 528 N-linked (GlcNAc...) (Potential).
CARBOHYD 529 529 N-linked (GlcNAc...) (Potential).
CARBOHYD 595 595 N-linked (GlcNAc...) (Potential).
CARBOHYD 620 620 N-linked (GlcNAc...) (Potential).
CARBOHYD 700 700 N-linked (GlcNAc...) (Potential).
CARBOHYD 718 718 N-linked (GlcNAc...) (Potential). |
Keyword | Complete proteome; Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 770 AA |
Protein Sequence | MASLKVFLAV YLLGGITFLP LVLFTLYKIH LLYSNLKSAS KKELDHDTAD EIDEKTRLLA 60
RDIDPEFKAR KLEEQLGVKV FNKGWITVTK QYYYHSSEVA VILKNSNNNK DSDTALQEQI 120
LQRTDLKKKQ RFFAVLRHGN LFLYKDDSQN ANLVHAISLQ NRFITIWPRF DELGKEELPD 180
ASLFTKRTCI AIFKNDLVSI DSKNHNVILP HFDPLTSAES NNGDISTNDT THEYQSQFHS 240
SNQFFLYFDN NMDKEDWYYQ LINASKNSNS LSTGLLDPNV SANAAHLKTK DMLQLIQDIN 300
STENQLTTKW LNALLGRLFL SLQQTDTLNK FIHEKICKKL NKIKTPGFLD DLVVEKVDVG 360
DSAPLFTSPE LLELSPEGST KIAIDVQYRG NLTIIIATKA SINLGSRFKQ REVSLQLSIK 420
IKEFSGPLLF LIKPPPSNRI WYAFRTEPIM DFEIEPIVSS SKLSYNVVTN AIKSKFAEAV 480
KESLVVPFMD DIVFYPTPNE VYRGGIWEEQ DPEAAARART AAAASDMNNT SAKEHLEALQ 540
EGGMKTQSRI KKALRPERKK ENLKDLVDAS GVATKTTTQT TVTTATNDDV SSSENSTKSR 600
KYFKNSIKKI GRWYKDNVGN SSDTEDMDEI DVQDKKNDDS ADERESDNPI LTSNPKMISN 660
RRPVPRRPSQ PLNTLSPKLE GRKEKDTENF PVPPSASNMN ASKMFANKEN RKFSVSSNDS 720
QNSLKNGDPH VKASKLESSQ AFVKKTSQNR FNDGFFKQDL EFEEQREPKL 770 |
Gene Ontology | GO:0005783; C:endoplasmic reticulum; IDA:SGD. GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0071561; C:nucleus-vacuole junction; IDA:SGD. GO:0008289; F:lipid binding; IDA:SGD. GO:0005543; F:phospholipid binding; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |