CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008132
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
47DVDSEAKKLLGLGQKubiquitination[1]
54KLLGLGQKHLVMGDIubiquitination[1]
78AASLLGKKYGETANEubiquitination[1]
95EAFFFYGKSLLELARubiquitination[1, 2, 3]
169TEDKSLAKPETDKEQubiquitination[3]
428VPSQEETKLSVEESEubiquitination[3]
444AGDGVDTKVAQGATEubiquitination[3]
537IFKRQETKEAQLYAAubiquitination[1, 3, 4]
645KKEIEELKELLPEIRubiquitination[1, 3]
659REKIEDAKESQRSGNubiquitination[3]
673NVAELALKATLVESSubiquitination[3]
700VSMIASRKPTDGASSubiquitination[1, 2, 4]
Reference
 [1] 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]
 [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] 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
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
MFLLLLHLQI KWRATINLLS VTEDGLHFVE YYLNRIIHLD VDSEAKKLLG LGQKHLVMGD 60
IPAAVNAFQE AASLLGKKYG ETANECGEAF FFYGKSLLEL ARMENGVLGN ALEGVHVEEE 120
EGEKTEDESL VENNDNIDEE AREELREQVY DAMGEKEEAK KTEDKSLAKP ETDKEQDSEM 180
EKGGREDMDI SKSAEEPQEK VDLTLDWLTE TSEEAKGGAA PEGPNEAEVT SGKPEQEVPD 240
AEEEKSVSGT DVQEECREKG GQEKQGEVIV SIEEKPKEVS EEQPVVTLEK QGTAVEVEAE 300
SLDPTVKPVD VGGDEPEEKV VTSENEAGKA VLEQLVGQEV PPAEESPEVT TEAAEASAVE 360
AGSEVSEKPG QEAPVLPKDG AVNGPSVVGD QTPIEPQTSI ERLTETKDGS GLEEKVRAKL 420
VPSQEETKLS VEESEAAGDG VDTKVAQGAT EKSPEDKVQI AANEETQERE EQMKEGEETE 480
GSEEDDKEND KTEEMPNDSV LENKSLQENE EEEIGNLELA WDMLDLAKII FKRQETKEAQ 540
LYAAQAHLKL GEVSVESENY VQAVEEFQSC LNLQEQYLEA HDRLLAETHY QLGLAYGYNS 600
QYDEAVAQFS KSIEVIENRM AVLNEQVKEA EGSSAEYKKE IEELKELLPE IREKIEDAKE 660
SQRSGNVAEL ALKATLVESS TSGFTPGGGG SSVSMIASRK PTDGASSSNC VTDISHLVRK 720
KRKPEEESPR KDDAKKAKQE PEVNGGSGDA VPSGNEVSEN MEEEAENQAE SRAAVEGTVE 780
AGATVESTAC 790 
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