CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024551
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear envelope pore membrane protein POM 121C 
Protein Synonyms/Alias
 Nuclear pore membrane protein 121-2; POM121-2; Pore membrane protein of 121 kDa C 
Gene Name
 POM121C 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
99LFASPPAKSTANGNLubiquitination[1]
286NAPDPCAKETVLSALubiquitination[2]
294ETVLSALKEKKKKRTubiquitination[3]
316FLDGQENKRRRHDSSubiquitination[2, 3, 4, 5]
364SSDDHLNKRSRSSSMubiquitination[2, 3]
405RGISQLWKRNGPSSSubiquitination[6]
666LQAETATKPQATSAPubiquitination[3]
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] 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] 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]
 [4] 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]
 [5] 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]
 [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] 
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 1 398 Required for targeting to the nucleus and
 REGION 1 40 Cisternal side (Potential).
 REGION 62 1229 Pore side (Potential).
 MOD_RES 322 322 Phosphoserine.
 MOD_RES 328 328 Phosphoserine (By similarity).
 MOD_RES 348 348 Phosphoserine.
 MOD_RES 370 370 Phosphoserine.  
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
 1229 AA 
Protein Sequence
MSPAAAAAGA GERRRPIASV RDGRGRGCGG PAGAALLGLS LVGLLLYLVP AAAALAWLAV 60
GTTAAWWGLS REPRGSRPLS SFVQKARHRR TLFASPPAKS TANGNLLEPR TLLEGPDPAE 120
LLLMGSYLGK PGPPQPAPAP EGQDLRNRPG RRPPARPAPR STPPSPPTHR VHHFYPSLPT 180
PLLRPSGRPS PRDRGTLPDR FVITPRRRYP IHQTQYSCPG VLPTVCWNGY HKKAVLSPRN 240
SRMVCSPVTV RIAPPDRRFS RSAIPEQIIS STLSSPSSNA PDPCAKETVL SALKEKKKKR 300
TVEEEDQIFL DGQENKRRRH DSSGSGHSAF EPLVASGVPA SFVPKPGSLK RGLNSQSSDD 360
HLNKRSRSSS MSSLTGAYTS GIPSSSRNAI TSSYSSTRGI SQLWKRNGPS SSPFSSPASS 420
RSQTPERPAK KIREEELCHH SSSSTPLAAD KESQGEKAAD TTPRKKQNSN SQSTPGSSGQ 480
RKRKVQLLPS RRGEQLTLPP PPQLGYSITA EDLDLEKKAS LQWFNQALED KSDAASNSVT 540
ETPPTTQPSF TFTLPAAATA SPPTSLLAPS TNPLLESLKK MQTPPSLPPC PESAGAATTE 600
ALSPPKTPSL LPPLGLSQSG PPGLLPSPSF DSKPPTTLLG LIPAPSMVPA TDTKAPPTLQ 660
AETATKPQAT SAPSPAPKQS FLFGTQNTSP SSPAAPAASS ASPMFKPIFT APPKSEKEGP 720
TPPGPSVTAT APSSSSLPTT TSTTAPTFQP VFSSMGPPAS VPLPAPFFKQ TTTPATAPTT 780
TAPLFTGLAS ATSAVAPITS ASPSTDSASK PAFGFGINSV SSSSVSTTTS TATAASQPFL 840
FGAPQASAAS FTPAMGSIFQ FGKPPALPTT TTVTTFSQSL PTAVPTATSS SAADFSGFGS 900
TLATSAPATS SQPTLTFSNT STPTFNIPFG SSAKSPLPSY PGANPQPAFG AAEGQPPGAA 960
KPALTPSFGS SFTFGNSAAP APATAPTPAP ASTIKIVPAH VPTPIQPTFG GATHSAFGLK 1020
ATASAFGAPA SSQPAFGGST AVFSFGAATS SGFGATTQTA SSGSSSSVFG STTPSPFTFG 1080
GSAAPAGSGS FGINVATPGS SATTGAFSFG AGQSGSTATS TPFTGGLGQN ALGTTGQSTP 1140
FAFNVGSTTE SKPVFGGTAT PTFGQNTPAP GVGTSGSSLS FGASSAPAQG FVGVGPFGSA 1200
APSFSIGAGS KTPGARQRLQ ARRQHTRKK 1229 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR026054; Nucleoporin.
 IPR026090; POM121. 
Pfam
  
SMART
  
PROSITE
  
PRINTS