CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008819
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein transport protein Sec24C 
Protein Synonyms/Alias
 SEC24-related protein C 
Gene Name
 SEC24C 
Gene Synonyms/Alias
 KIAA0079 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
364VTTNFLVKDQGNASPubiquitination[1]
389PCTSDMAKQAQVPLAubiquitination[1]
400VPLAAVIKPLARLPPubiquitination[1, 2]
638KAAECAGKLFLFHTSubiquitination[1]
654PIAEAPGKLKNRDDRubiquitination[1]
656AEAPGKLKNRDDRKLubiquitination[1]
670LINTDKEKTLFQPQTubiquitination[2, 3]
745DLRRDVQKVVGFDAVubiquitination[1]
853TLINYMAKFAYRGVLubiquitination[1]
865GVLNSPVKAVRDTLIubiquitination[1, 3]
884QILACYRKNCASPSSubiquitination[1]
913VYLNCVLKSDVLQPGubiquitination[1]
956PRLLPLTKSPVESTTubiquitination[1, 3]
1048AQRSRYMKLTVVKQEubiquitination[1, 2, 4, 5]
1057TVVKQEDKMEMLFKHubiquitination[1]
1087DFLCHMHKEIRQLLSacetylation[6]
1087DFLCHMHKEIRQLLSubiquitination[1]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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] 
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. 
Sequence Annotation
 REGION 425 450 Zinc finger-like.
 MOD_RES 214 214 Phosphothreonine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1094 AA 
Protein Sequence
MNVNQSVPPV PPFGQPQPIY PGYHQSSYGG QSGSTAPAIP YGAYNGPVPG YQQTPPQGMS 60
RAPPSSGAPP ASTAQAPCGQ AAYGQFGQGD VQNGPSSTVQ MQRLPGSQPF GSPLAPVGNQ 120
PPVLQPYGPP PTSAQVATQL SGMQISGAVA PAPPSSGLGF GPPTSLASAS GSFPNSGLYG 180
SYPQGQAPPL SQAQGHPGIQ TPQRSAPSQA SSFTPPASGG PRLPSMTGPL LPGQSFGGPS 240
VSQPNHVSSP PQALPPGTQM TGPLGPLPPM HSPQQPGYQP QQNGSFGPAR GPQSNYGGPY 300
PAAPTFGSQP GPPQPLPPKR LDPDAIPSPI QVIEDDRNNR GTEPFVTGVR GQVPPLVTTN 360
FLVKDQGNAS PRYIRCTSYN IPCTSDMAKQ AQVPLAAVIK PLARLPPEEA SPYVVDHGES 420
GPLRCNRCKA YMCPFMQFIE GGRRFQCCFC SCINDVPPQY FQHLDHTGKR VDAYDRPELS 480
LGSYEFLATV DYCKNNKFPS PPAFIFMIDV SYNAIRTGLV RLLCEELKSL LDFLPREGGA 540
EESAIRVGFV TYNKVLHFYN VKSSLAQPQM MVVSDVADMF VPLLDGFLVN VNESRAVITS 600
LLDQIPEMFA DTRETETVFV PVIQAGMEAL KAAECAGKLF LFHTSLPIAE APGKLKNRDD 660
RKLINTDKEK TLFQPQTGAY QTLAKECVAQ GCCVDLFLFP NQYVDVATLS VVPQLTGGSV 720
YKYASFQVEN DQERFLSDLR RDVQKVVGFD AVMRVRTSTG IRAVDFFGAF YMSNTTDVEL 780
AGLDGDKTVT VEFKHDDRLN EESGALLQCA LLYTSCAGQR RLRIHNLALN CCTQLADLYR 840
NCETDTLINY MAKFAYRGVL NSPVKAVRDT LITQCAQILA CYRKNCASPS SAGQLILPEC 900
MKLLPVYLNC VLKSDVLQPG AEVTTDDRAY VRQLVTSMDV TETNVFFYPR LLPLTKSPVE 960
STTEPPAVRA SEERLSNGDI YLLENGLNLF LWVGASVQQG VVQSLFSVSS FSQITSGLSV 1020
LPVLDNPLSK KVRGLIDSLR AQRSRYMKLT VVKQEDKMEM LFKHFLVEDK SLSGGASYVD 1080
FLCHMHKEIR QLLS 1094 
Gene Ontology
 GO:0030127; C:COPII vesicle coat; NAS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
 GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
 GO:0048208; P:COPII vesicle coating; TAS:Reactome.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
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