CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020176
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleoporin NDC1 
Protein Synonyms/Alias
 hNDC1; Transmembrane protein 48 
Gene Name
 NDC1 
Gene Synonyms/Alias
 TMEM48 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
403SYPVEPKKLNSPEETubiquitination[1, 2]
430PSVPPLVKTSLFSSKubiquitination[2, 3, 4, 5]
437KTSLFSSKLSTPDVVubiquitination[1, 2, 3, 5, 6]
510TSISAEGKTMRQPSVubiquitination[1]
628SLVDTSYKTLRFAFRubiquitination[1, 3, 5]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572
Functional Description
 Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane. 
Sequence Annotation
 MOD_RES 406 406 Phosphoserine.
 MOD_RES 414 414 Phosphothreonine.
 MOD_RES 439 439 Phosphoserine.
 MOD_RES 440 440 Phosphothreonine.
 MOD_RES 445 445 Phosphoserine.
 MOD_RES 449 449 Phosphothreonine.
 MOD_RES 471 471 Phosphoserine.
 MOD_RES 474 474 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Translocation; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 674 AA 
Protein Sequence
MATAVSRPCA GRSRDILWRV LGWRIVASIV WSVLFLPICT TVFIIFSRID LFHPIQWLSD 60
SFSDLYSSYV IFYFLLLSVV IIIISIFNVE FYAVVPSIPC SRLALIGKII HPQQLMHSFI 120
HAAMGMVMAW CAAVITQGQY SFLVVPCTGT NSFGSPAAQT CLNEYHLFFL LTGAFMGYSY 180
SLLYFVNNMN YLPFPIIQQY KFLRFRRSLL LLVKHSCVES LFLVRNFCIL YYFLGYIPKA 240
WISTAMNLHI DEQVHRPLDT VSGLLNLSLL YHVWLCGVFL LTTWYVSWIL FKIYATEAHV 300
FPVQPPFAEG SDECLPKVLN SNPPPIIKYL ALQDLMLLSQ YSPSRRQEVF SLSQPGGHPH 360
NWTAISRECL NLLNGMTQKL ILYQEAAATN GRVSSSYPVE PKKLNSPEET AFQTPKSSQM 420
PRPSVPPLVK TSLFSSKLST PDVVSPFGTP FGSSVMNRMA GIFDVNTCYG SPQSPQLIRR 480
GPRLWTSASD QQMTEFSNPS PSTSISAEGK TMRQPSVIYS WIQNKREQIK NFLSKRVLIM 540
YFFSKHPEAS IQAVFSDAQM HIWALEGLSH LVAASFTEDR FGVVQTTLPA ILNTLLTLQE 600
AVDKYFKLPH ASSKPPRISG SLVDTSYKTL RFAFRASLKT AIYRITTTFG EHLNAVQASA 660
EHQKRLQQFL EFKE 674 
Gene Ontology
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0005643; C:nuclear pore; IDA:UniProtKB.
 GO:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
 GO:0031081; P:nuclear pore distribution; IMP:UniProtKB.
 GO:0015031; P:protein transport; NAS:UniProtKB. 
Interpro
 IPR019049; Nucleoporin_prot_Ndc1/Nup. 
Pfam
 PF09531; Ndc1_Nup 
SMART
  
PROSITE
  
PRINTS