CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008131
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear autoantigenic sperm protein 
Protein Synonyms/Alias
 NASP 
Gene Name
 NASP 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33APSTSADKVESLDVDacetylation[1]
33APSTSADKVESLDVDubiquitination[2]
45DVDSEAKKLLGLGQKubiquitination[3, 4]
52KLLGLGQKHLVMGDIubiquitination[2]
93EAFFFYGKSLLELARubiquitination[2, 5]
231EAEVTSGKPEQEVPDubiquitination[2]
417LEEKVRAKLVPSQEEacetylation[6, 7]
426VPSQEETKLSVEESEubiquitination[2, 8]
442AGDGVDTKVAQGATEubiquitination[2, 8]
450VAQGATEKSPEDKVQacetylation[9]
535IFKRQETKEAQLYAAubiquitination[2, 3, 4, 10]
626AVLNEQVKEAEGSSAubiquitination[2]
637GSSAEYKKEIEELKEubiquitination[3, 4]
643KKEIEELKELLPEIRubiquitination[2, 3, 4]
652LLPEIREKIEDAKESubiquitination[2]
657REKIEDAKESQRSGNubiquitination[2]
671NVAELALKATLVESSubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] 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]
 [8] 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]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [10] 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] 
Functional Description
 Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA (By similarity). 
Sequence Annotation
 REPEAT 43 76 TPR 1.
 REPEAT 542 575 TPR 2.
 REPEAT 584 617 TPR 3.
 REGION 116 127 Histone-binding.
 REGION 211 244 Histone-binding.
 REGION 469 512 Histone-binding.
 MOTIF 716 722 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 33 33 N6-acetyllysine.
 MOD_RES 123 123 Phosphothreonine.
 MOD_RES 127 127 Phosphoserine.
 MOD_RES 189 189 Phosphoserine.
 MOD_RES 244 244 Phosphoserine.
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 321 321 Phosphoserine.
 MOD_RES 390 390 Phosphothreonine.
 MOD_RES 408 408 Phosphoserine.
 MOD_RES 421 421 Phosphoserine.
 MOD_RES 451 451 Phosphoserine.
 MOD_RES 464 464 Phosphothreonine.
 MOD_RES 477 477 Phosphothreonine.
 MOD_RES 480 480 Phosphoserine.
 MOD_RES 490 490 Phosphothreonine.
 MOD_RES 497 497 Phosphoserine.
 MOD_RES 503 503 Phosphoserine.
 MOD_RES 683 683 Phosphothreonine.
 MOD_RES 726 726 Phosphoserine.
 MOD_RES 751 751 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Coiled coil; Complete proteome; Cytoplasm; DNA replication; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; TPR repeat; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 788 AA 
Protein Sequence
MAMESTATAA VAAELVSADK IEDVPAPSTS ADKVESLDVD SEAKKLLGLG QKHLVMGDIP 60
AAVNAFQEAA SLLGKKYGET ANECGEAFFF YGKSLLELAR MENGVLGNAL EGVHVEEEEG 120
EKTEDESLVE NNDNIDEEAR EELREQVYDA MGEKEEAKKT EDKSLAKPET DKEQDSEMEK 180
GGREDMDISK SAEEPQEKVD LTLDWLTETS EEAKGGAAPE GPNEAEVTSG KPEQEVPDAE 240
EEKSVSGTDV QEECREKGGQ EKQGEVIVSI EEKPKEVSEE QPVVTLEKQG TAVEVEAESL 300
DPTVKPVDVG GDEPEEKVVT SENEAGKAVL EQLVGQEVPP AEESPEVTTE AAEASAVEAG 360
SEVSEKPGQE APVLPKDGAV NGPSVVGDQT PIEPQTSIER LTETKDGSGL EEKVRAKLVP 420
SQEETKLSVE ESEAAGDGVD TKVAQGATEK SPEDKVQIAA NEETQEREEQ MKEGEETEGS 480
EEDDKENDKT EEMPNDSVLE NKSLQENEEE EIGNLELAWD MLDLAKIIFK RQETKEAQLY 540
AAQAHLKLGE VSVESENYVQ AVEEFQSCLN LQEQYLEAHD RLLAETHYQL GLAYGYNSQY 600
DEAVAQFSKS IEVIENRMAV LNEQVKEAEG SSAEYKKEIE ELKELLPEIR EKIEDAKESQ 660
RSGNVAELAL KATLVESSTS GFTPGGGGSS VSMIASRKPT DGASSSNCVT DISHLVRKKR 720
KPEEESPRKD DAKKAKQEPE VNGGSGDAVP SGNEVSENME EEAENQAESR AAVEGTVEAG 780
ATVESTAC 788 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
 GO:0001824; P:blastocyst development; ISS:UniProtKB.
 GO:0007049; P:cell cycle; ISS:UniProtKB.
 GO:0008283; P:cell proliferation; ISS:UniProtKB.
 GO:0006260; P:DNA replication; ISS:UniProtKB.
 GO:0043486; P:histone exchange; ISS:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR019544; Tetratricopeptide_SHNi-TPR_dom.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF10516; SHNi-TPR
 PF00515; TPR_1 
SMART
 SM00028; TPR 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS