CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008963
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleosome assembly protein 1-like 1 
Protein Synonyms/Alias
 NAP-1-related protein; hNRP 
Gene Name
 NAP1L1 
Gene Synonyms/Alias
 NRP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32EETGEETKLKARQLTubiquitination[1, 2, 3]
82KRRVNALKNLQVKCAubiquitination[1, 3, 4, 5, 6]
87ALKNLQVKCAQIEAKubiquitination[5]
105EVHDLERKYAVLYQPubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
116LYQPLFDKRFEIINAacetylation[9]
116LYQPLFDKRFEIINAubiquitination[1, 3, 4, 5, 6, 8]
165DEEKEDPKGIPEFWLacetylation[10]
165DEEKEDPKGIPEFWLubiquitination[4, 5, 6]
194EHDEPILKHLKDIKVacetylation[9]
194EHDEPILKHLKDIKVubiquitination[1]
381DPDYDPKKDQNPAECubiquitination[1]
389DQNPAECKQQ*****ubiquitination[1]
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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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] 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]
 [6] 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]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] 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]
 [10] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 May be involved in modulating chromatin formation and contribute to regulation of cell proliferation. 
Sequence Annotation
 MOTIF 273 279 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 62 62 Phosphothreonine.
 MOD_RES 69 69 Phosphoserine.
 MOD_RES 116 116 N6-acetyllysine.
 MOD_RES 143 143 Phosphoserine.
 MOD_RES 388 388 Cysteine methyl ester (Probable).
 LIPID 388 388 S-farnesyl cysteine.  
Keyword
 Acetylation; Complete proteome; Lipoprotein; Methylation; Nucleus; Phosphoprotein; Prenylation; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 391 AA 
Protein Sequence
MADIDNKEQS ELDQDLDDVE EVEEEETGEE TKLKARQLTV QMMQNPQILA ALQERLDGLV 60
ETPTGYIESL PRVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI 120
INAIYEPTEE ECEWKPDEED EISEELKEKA KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL 180
LSDMVQEHDE PILKHLKDIK VKFSDAGQPM SFVLEFHFEP NEYFTNEVLT KTYRMRSEPD 240
DSDPFSFDGP EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF 300
FAPPEVPESG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE 360
ADEEGEEEGD EENDPDYDPK KDQNPAECKQ Q 391 
Gene Ontology
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0006260; P:DNA replication; TAS:ProtInc.
 GO:0006334; P:nucleosome assembly; TAS:ProtInc.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc. 
Interpro
 IPR002164; NAP_family. 
Pfam
 PF00956; NAP 
SMART
  
PROSITE
  
PRINTS