CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019304
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear envelope pore membrane protein POM 121 
Protein Synonyms/Alias
 Nuclear envelope pore membrane protein POM 121A; Nucleoporin Nup121; Pore membrane protein of 121 kDa 
Gene Name
 POM121 
Gene Synonyms/Alias
 KIAA0618; NUP121; POM121A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
112LFASPLAKSTANGNLubiquitination[1, 2]
143LMGSYLGKPGPPQPAubiquitination[3]
317ETVLSALKEKEKKRTubiquitination[2]
319VLSALKEKEKKRTVEubiquitination[2]
339FLDGQENKRRRHDSSubiquitination[2]
387SSDDHLNKRSRSSSMubiquitination[2]
428RGISQLWKRNGPSSSubiquitination[4, 5]
541EDLDLEKKASLQWFNubiquitination[2]
689LQAETATKPQATSAPubiquitination[2]
Reference
 [1] 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]
 [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] 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] 
Functional Description
 Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). 
Sequence Annotation
 REGION 1 285 Required for targeting to the nucleus and
 REGION 1 34 Cisternal side (Potential).
 REGION 56 1249 Pore side (Potential).
 MOD_RES 345 345 Phosphoserine (By similarity).
 MOD_RES 351 351 Phosphoserine.
 MOD_RES 371 371 Phosphoserine.
 MOD_RES 393 393 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Endoplasmic reticulum; Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; Translocation; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1249 AA 
Protein Sequence
MSPAAAAAGA GERRRPIASV RDGRGRGCGG PARAVLLGLS LVGLLLYLVP AAAALAWLTV 60
GATAAWWGLS REPRGSRPLS SFVRKARHRR PLSSFVRKAR HRRTLFASPL AKSTANGNLL 120
EPRTLLEGPD PAELLLMGSY LGKPGPPQPA AAPEGQDLRD RPGRRPPARP APRSPPPRSP 180
PPRSPPPSPP THRAHHVYPS LPTPLLRPSR RPSPRDCGTL PNRFVITPRR RYPIHQAQYS 240
CLGVLPTVCW NGYHKKAVLS PRNSRMVCSP VTVRIAPPDR RFSRSAIPEQ IISSTLSSPS 300
SNAPDPCAKE TVLSALKEKE KKRTVEEEDQ IFLDGQENKR RRHDSSGSGH SAFEPLVANG 360
VPASFVPKPG SLKRGLNSQS SDDHLNKRSR SSSMSSLTGA YASGIPSSSR NAITSSYSST 420
RGISQLWKRN GPSSSPFSSP ASSRSQTPER PAKKIREEEL CHHSSSSTPL AADRESQGEK 480
AADTTPRKKQ NSNSQSTPGS SGQRKRKVQL LPSRRGEQLT LPPPPQLGYS ITAEDLDLEK 540
KASLQWFNQA LEDKSDAASN SVTETPPITQ PSFTFTLPAA APASPPTSLL APSTNPLLES 600
LKKMQTPPSL PPCPESAGAA TTEALSPPKT PSLLPPLGLS QSGPPGLLPS PSFDSKPPTT 660
LLGLIPAPSM VPATDTKAPP TLQAETATKP QATSAPSPAP KQSFLFGTQN TSPSSPAAPA 720
ASSAPPMFKP IFTAPPKSEK EGPTPPGPSV TATAPSSSSL PTTTSTTAPT FQPVFSSMGP 780
PASVPLPAPF FKQTTTPATA PTTTAPLFTG LASATSAVAP ITSASPSTDS ASKPAFGFGI 840
NSVSSSSVST TTSTATAASQ PFLFGAPQAS AASFTPAMGS IFQFGKPPAL PTTTTVTTFS 900
QSLHTAVPTA TSSSAADFSG FGSTLATSAP ATSSQPTLTF SNTSTPTFNI PFGSSAKSPL 960
PSYPGANPQP AFGAAEGQPP GAAKPALAPS FGSSFTFGNS AAPAAAPTPA PPSMIKVVPA 1020
YVPTPIHPIF GGATHSAFGL KATASAFGAP ASSQPAFGGS TAVFFGAATS SGFGATTQTA 1080
SSGSSSSVFG STTPSPFTFG GSAAPAGSGS FGINVATPGS STTTGAFSFG AGQSGSTATS 1140
TPFAGGLGQN ALGTTGQSTP FAFNVSSTTE SKPVFGGTAT PTFGLNTPAP GVGTSGSSLS 1200
FGASSAPAQG FVGVAPFGSA ALSFSIGAGS KTPGARQRLQ ARRQHTRKK 1249 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005635; C:nuclear envelope; TAS:Reactome.
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
 GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO:0015758; P:glucose transport; TAS:Reactome.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0010827; P:regulation of glucose transport; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 
Interpro
 IPR026054; Nucleoporin.
 IPR026090; POM121. 
Pfam
  
SMART
  
PROSITE
  
PRINTS