CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004474
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 78 kDa glucose-regulated protein homolog 
Protein Synonyms/Alias
 GRP-78; Immunoglobulin heavy chain-binding protein homolog; BiP 
Gene Name
 KAR2 
Gene Synonyms/Alias
 GRP78; SSD1; YJL034W; J1248 
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
71VAVMKNGKTEILANEubiquitination[1]
134RSVQKDIKHLPFNVVacetylation[2]
303IDVSDNNKALAKLKRacetylation[2]
346SETLTRAKFEELNLDacetylation[2]
374QDSGLEKKDVDDIVLacetylation[2]
584AKVESRNKLENYAHSacetylation[2]
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]
 [2] 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] 
Functional Description
 Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis. 
Sequence Annotation
 MOTIF 679 682 Prevents secretion from ER.  
Keyword
 3D-structure; ATP-binding; Complete proteome; Endoplasmic reticulum; Nucleotide-binding; Reference proteome; Signal; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 682 AA 
Protein Sequence
MFFNRLSAGK LLVPLSVVLY ALFVVILPLQ NSFHSSNVLV RGADDVENYG TVIGIDLGTT 60
YSCVAVMKNG KTEILANEQG NRITPSYVAF TDDERLIGDA AKNQVAANPQ NTIFDIKRLI 120
GLKYNDRSVQ KDIKHLPFNV VNKDGKPAVE VSVKGEKKVF TPEEISGMIL GKMKQIAEDY 180
LGTKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVLRIVN EPTAAAIAYG LDKSDKEHQI 240
IVYDLGGGTF DVSLLSIENG VFEVQATSGD THLGGEDFDY KIVRQLIKAF KKKHGIDVSD 300
NNKALAKLKR EAEKAKRALS SQMSTRIEID SFVDGIDLSE TLTRAKFEEL NLDLFKKTLK 360
PVEKVLQDSG LEKKDVDDIV LVGGSTRIPK VQQLLESYFD GKKASKGINP DEAVAYGAAV 420
QAGVLSGEEG VEDIVLLDVN ALTLGIETTG GVMTPLIKRN TAIPTKKSQI FSTAVDNQPT 480
VMIKVYEGER AMSKDNNLLG KFELTGIPPA PRGVPQIEVT FALDANGILK VSATDKGTGK 540
SESITITNDK GRLTQEEIDR MVEEAEKFAS EDASIKAKVE SRNKLENYAH SLKNQVNGDL 600
GEKLEEEDKE TLLDAANDVL EWLDDNFETA IAEDFDEKFE SLSKVAYPIT SKLYGGADGS 660
GAADYDDEDE DDDGDYFEHD EL 682 
Gene Ontology
 GO:0034099; C:luminal surveillance complex; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IDA:SGD.
 GO:0051082; F:unfolded protein binding; IMP:SGD.
 GO:0030433; P:ER-associated protein catabolic process; IMP:SGD.
 GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IGI:SGD.
 GO:0031204; P:posttranslational protein targeting to membrane, translocation; IDA:SGD.
 GO:0006986; P:response to unfolded protein; IMP:SGD.
 GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IMP:SGD. 
Interpro
 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 
Pfam
 PF00012; HSP70 
SMART
  
PROSITE
 PS00014; ER_TARGET
 PS00297; HSP70_1
 PS00329; HSP70_2
 PS01036; HSP70_3 
PRINTS
 PR00301; HEATSHOCK70.