CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013296
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Paraspeckle component 1 
Protein Synonyms/Alias
  
Gene Name
 Pspc1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
379RRQQEGFKPNYMENRacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Together with NONO, required for the formation of nuclear paraspeckles. Regulates, cooperatively with NONO and SFPQ, androgen receptor-mediated gene transcription activity in Sertoli cell line. Binds to poly(A), poly(G) and poly(U) RNA homopolymers (By similarity). 
Sequence Annotation
 DOMAIN 81 153 RRM 1.
 DOMAIN 155 236 RRM 2.
 REGION 124 357 Sufficient for paraspeckles localization
 REGION 230 357 Sufficient for perinucleolar caps
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 408 408 Phosphoserine (By similarity).
 MOD_RES 472 472 Phosphoserine (By similarity).
 MOD_RES 476 476 Phosphoserine (By similarity).
 MOD_RES 508 508 Phosphoserine (By similarity).  
Keyword
 Acetylation; Activator; Coiled coil; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 522 AA 
Protein Sequence
MMLRGNLKQV RIEKNPARLR ALESAAGESE PVAAAAMALT LAGEQPPPPA PSEEHPDEEM 60
GFTIDIKSFL KPGEKTYTQR CRLFVGNLPT DITEEDFKRL FERYGEPSEV FINRDRGFGF 120
IRLESRTLAE IAKAELDGTI LKSRPLRIRF ATHGAALTVK NLSPVVSNEL LEQAFSQFGP 180
VEKAVVVVDD RGRATGKGFV EFAAKPPARK ALERCGDGAF LLTTTPRPVI VEPMEQFDDE 240
DGLPEKLMQK TQQYHKEREQ PPRFAQPGTF EFEYASRWKA LDEMEKQQRE QVDRNIREAK 300
EKLEAEMEAA RHEHQLMLMR QDLMRRQEEL RRLEELRNQE LQKRKQIQLR HEEEHRRREE 360
EMIRHREQEE LRRQQEGFKP NYMENREQEM RMGDMGPRGA INMGDAFSPA PAGTQGPPPM 420
MGMNMNNRGT IPGPPMGPGP AMGPEGAANM GTPMIPDNGA VHNDRFPQGP PSQMGSPMGN 480
RTGSETPQAP MSAVGPVSGG PGGFGRGSQG GNFEGPNKRR RY 522 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0042382; C:paraspeckles; IEA:Compara.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR012975; NOPS.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF08075; NOPS
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS