CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012567
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein transport protein Sec23B 
Protein Synonyms/Alias
 SEC23-related protein B 
Gene Name
 SEC23B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
81CQVDYRAKLWACNFCubiquitination[1]
185LSCEGISKSYVFRGTubiquitination[1]
208QDMLGLTKPAMPMQQubiquitination[1]
237RFLQPVHKIDMNLTDubiquitination[2]
260PWPVTQGKRPLRSTGubiquitination[2, 3]
309MVVGDELKIPIRSWHubiquitination[2, 3]
320RSWHDIEKDNARFMKacetylation[4, 5]
320RSWHDIEKDNARFMKubiquitination[1, 2, 3]
328DNARFMKKATKHYEMubiquitination[3]
331RFMKKATKHYEMLANubiquitination[3]
394TFQRIFTKDFNGDFRubiquitination[1, 2, 3, 5]
431PCVSLNVKGPCVSENubiquitination[2]
558QLIRLCQKFGQYNKEubiquitination[1]
564QKFGQYNKEDPTSFRubiquitination[1, 2, 3, 5]
671ETIAQWRKAGYQDMPubiquitination[2, 3, 6, 7, 8]
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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] 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]
 [6] 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]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex (By similarity). 
Sequence Annotation
  
Keyword
 Complete proteome; Congenital dyserythropoietic anemia; Disease mutation; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Hereditary hemolytic anemia; Membrane; Polymorphism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 767 AA 
Protein Sequence
MATYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPLAC LLTPLKERPD LPPVQYEPVL 60
CSRPTCKAVL NPLCQVDYRA KLWACNFCFQ RNQFPPAYGG ISEVNQPAEL MPQFSTIEYV 120
IQRGAQSPLI FLYVVDTCLE EDDLQALKES LQMSLSLLPP DALVGLITFG RMVQVHELSC 180
EGISKSYVFR GTKDLTAKQI QDMLGLTKPA MPMQQARPAQ PQEHPFASSR FLQPVHKIDM 240
NLTDLLGELQ RDPWPVTQGK RPLRSTGVAL SIAVGLLEGT FPNTGARIML FTGGPPTQGP 300
GMVVGDELKI PIRSWHDIEK DNARFMKKAT KHYEMLANRT AANGHCIDIY ACALDQTGLL 360
EMKCCANLTG GYMVMGDSFN TSLFKQTFQR IFTKDFNGDF RMAFGATLDV KTSRELKIAG 420
AIGPCVSLNV KGPCVSENEL GVGGTSQWKI CGLDPTSTLG IYFEVVNQHN TPIPQGGRGA 480
IQFVTHYQHS STQRRIRVTT IARNWADVQS QLRHIEAAFD QEAAAVLMAR LGVFRAESEE 540
GPDVLRWLDR QLIRLCQKFG QYNKEDPTSF RLSDSFSLYP QFMFHLRRSP FLQVFNNSPD 600
ESSYYRHHFA RQDLTQSLIM IQPILYSYSF HGPPEPVLLD SSSILADRIL LMDTFFQIVI 660
YLGETIAQWR KAGYQDMPEY ENFKHLLQAP LDDAQEILQA RFPMPRYINT EHGGSQARFL 720
LSKVNPSQTH NNLYAWGQET GAPILTDDVS LQVFMDHLKK LAVSSAC 767 
Gene Ontology
 GO:0030127; C:COPII vesicle coat; IEA:InterPro.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
 GO:0016020; C:membrane; TAS:ProtInc.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:InterPro.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0016192; P:vesicle-mediated transport; TAS:ProtInc. 
Interpro
 IPR007123; Gelsolin_dom.
 IPR006900; Sec23/24_helical_dom.
 IPR006896; Sec23/24_trunk_dom.
 IPR012990; Sec23_24_beta_S.
 IPR002035; VWF_A.
 IPR006895; Znf_Sec23_Sec24. 
Pfam
 PF00626; Gelsolin
 PF08033; Sec23_BS
 PF04815; Sec23_helical
 PF04811; Sec23_trunk
 PF04810; zf-Sec23_Sec24 
SMART
  
PROSITE
  
PRINTS