CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-044964
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Glucosidase 2 subunit beta 
Protein Synonyms/Alias
  
Gene Name
 PRKCSH 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
142REGFRLKKILIEDWKubiquitination[1, 2]
167IELQAGKKSLEDQVEubiquitination[1, 2]
383AAQEARNKFEEAERSacetylation[2]
383AAQEARNKFEEAERSubiquitination[1]
392EEAERSLKDMEESIRubiquitination[1, 2]
445KLVSQKPKLGGSPTSubiquitination[3]
466WIGPDHDKFSAMKYEubiquitination[1]
471HDKFSAMKYEQGTGCubiquitination[1]
494TVRLLCGKETMVTSTubiquitination[1, 2, 3, 4]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
  
Sequence Annotation
  
Keyword
 Calcium; Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 535 AA 
Protein Sequence
MLLPLLLLLP MCWAVEVKRP RGVSLTNHHF YDESKPFTCL DGSATIPFDQ VNDDYCDCKD 60
GSDEPGTAAC PNGSFHCTNT GYKPLYIPSN RVNDGVCDCC DGTDEYNSGV ICENTCKEKG 120
RKERESLQQM AEVTREGFRL KKILIEDWKK AREEKQKKLI ELQAGKKSLE DQVEMLRTVK 180
EEAEKPEREA KEQHQKLWEE QLAAAKAQQE QELAADAFKE LDDDMDGTVS VTELQTHPEL 240
DTDGDGALSE AEAQALLSGD TQTDATSFYD RVWAAIRDKY RSEALPTDLP APSAPDLTEP 300
KEEQPPVPSS PTEEEEEEEE EEEEEAEEEE EEEDSEVQGE QPKEAPPPLS PPQPASPAEE 360
DKMPPYDEQT QAFIDAAQEA RNKFEEAERS LKDMEESIRN LEQEISFDFG PNGEFAYLYS 420
QCYELTTNEY VYRLCPFKLV SQKPKLGGSP TSLGTWGSWI GPDHDKFSAM KYEQGTGCWQ 480
GPNRSTTVRL LCGKETMVTS TTEPSRCEYL MELMTPAACP EPPPEAPTED DHDEL 535 
Gene Ontology
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0006491; P:N-glycan processing; IEA:InterPro. 
Interpro
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR026874; Glucosidase_2_bsu.
 IPR002172; LDrepeatLR_classA_rpt.
 IPR009011; Man6P_isomerase_rcpt-bd_dom. 
Pfam
 PF13202; EF_hand_3 
SMART
 SM00192; LDLa 
PROSITE
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2 
PRINTS