CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012414
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleolar and coiled-body phosphoprotein 1 
Protein Synonyms/Alias
 140 kDa nucleolar phosphoprotein; Nopp140; Hepatitis C virus NS5A-transactivated protein 13; HCV NS5A-transactivated protein 13; Nucleolar 130 kDa protein; Nucleolar phosphoprotein p130 
Gene Name
 NOLC1 
Gene Synonyms/Alias
 KIAA0035; NS5ATP13 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33QLSEVANKFAKATGAubiquitination[1, 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] 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
 Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I. 
Sequence Annotation
 DOMAIN 10 42 LisH.
 REPEAT 84 95 Acidic serine cluster 1.
 REPEAT 125 136 Acidic serine cluster 2.
 REPEAT 167 178 Acidic serine cluster 3.
 REPEAT 221 232 Acidic serine cluster 4.
 REPEAT 264 275 Acidic serine cluster 5.
 REPEAT 325 336 Acidic serine cluster 6.
 REPEAT 363 375 Acidic serine cluster 7.
 REPEAT 425 436 Acidic serine cluster 8.
 REPEAT 470 481 Acidic serine cluster 9.
 REPEAT 519 529 Acidic serine cluster 10.
 REPEAT 555 566 Acidic serine cluster 11.
 REGION 84 566 11 X 12 AA approximate repeats of an
 REGION 204 382 Interacts with RPA194.
 MOTIF 68 82 Nuclear localization signal (Potential).
 MOTIF 384 587 Nuclear localization signal (Potential).
 MOTIF 601 617 Nuclear localization signal (Potential).
 MOD_RES 33 33 N6-acetyllysine.
 MOD_RES 87 87 Phosphoserine.
 MOD_RES 90 90 Phosphoserine.
 MOD_RES 91 91 Phosphoserine.
 MOD_RES 366 366 Phosphoserine.
 MOD_RES 397 397 Phosphoserine.
 MOD_RES 415 415 N6-acetyllysine.
 MOD_RES 508 508 Phosphoserine.
 MOD_RES 538 538 Phosphoserine.
 MOD_RES 563 563 Phosphoserine.
 MOD_RES 580 580 Phosphoserine.
 MOD_RES 582 582 Phosphoserine.
 MOD_RES 607 607 Phosphothreonine.
 MOD_RES 610 610 Phosphothreonine.
 MOD_RES 622 622 Phosphoserine.
 MOD_RES 643 643 Phosphoserine.
 MOD_RES 663 663 N6-acetyllysine.
 MOD_RES 686 686 Phosphoserine.
 MOD_RES 698 698 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 699 AA 
Protein Sequence
MADAGIRRVV PSDLYPLVLG FLRDNQLSEV ANKFAKATGA TQQDANASSL LDIYSFWLKS 60
AKVPERKLQA NGPVAKKAKK KASSSDSEDS SEEEEEVQGP PAKKAAVPAK RVGLPPGKAA 120
AKASESSSSE ESSDDDDEED QKKQPVQKGV KPQAKAAKAP PKKAKSSDSD SDSSSEDEPP 180
KNQKPKITPV TVKAQTKAPP KPARAAPKIA NGKAASSSSS SSSSSSSDDS EEEKAAATPK 240
KVWTITSVRA ETVPKKQVVA KAPVKAATTP TRKSSSSEDS SSDEEEEQKK PMKNKPGPYS 300
SVPPPSAPPP KKSLGTQPPK KAVEKQQPVE SSEDSSDESD SSSEEEKKPP TKAVVSKATT 360
KPPPAKKAAE SSSDSSDSDS SEDDEAPSKP AGTTKNSSNK PAVTTKSPAV KPAAAPKQPV 420
GGGQKLLTRK ADSSSSEEES SSSEEEKTKK MVATTKPKAT AKAALSLPAK QAPQGSRDSS 480
SDSDSSSSEE EEEKTSKSAV KKKPQKVAGG AAPSKPASAK KGKAESSNSS SSDDSSEEEE 540
EKLKGKGSPR PQAPKANGTS ALTAQNGKAA KNSEEEEEEK KKAAVVVSKS GSLKKRKQNE 600
AAKEAETPQA KKIKLQTPNT FPKRKKGEKR ASSPFRRVRE EEIEVDSRVA DNSFDAKRGA 660
AGDWGERANQ VLKFTKGKSF RHEKTKKKRG SYRGGSISVQ VNSIKFDSE 709 
Gene Ontology
 GO:0015030; C:Cajal body; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; TAS:ProtInc.
 GO:0007000; P:nucleolus organization; IEA:Compara.
 GO:0006364; P:rRNA processing; TAS:ProtInc. 
Interpro
 IPR006594; LisH_dimerisation.
 IPR007718; SRP40_C. 
Pfam
 PF05022; SRP40_C 
SMART
 SM00667; LisH 
PROSITE
 PS50896; LISH 
PRINTS