CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021601
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sp110 nuclear body protein 
Protein Synonyms/Alias
 Interferon-induced protein 41/75; Speckled 110 kDa; Transcriptional coactivator Sp110 
Gene Name
 SP110 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
394EKLQVVDKVTQRKDDubiquitination[1]
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
Functional Description
 Transcription factor. May be a nuclear hormone receptor coactivator. Enhances transcription of genes with retinoic acid response elements (RARE). 
Sequence Annotation
 DOMAIN 1 108 HSR.
 DOMAIN 454 535 SAND.
 DOMAIN 581 676 Bromo.
 ZN_FING 534 580 PHD-type.
 REGION 525 529 Nuclear hormone receptor interaction
 MOTIF 281 294 Nuclear localization signal (Potential).
 MOTIF 428 444 Nuclear localization signal (Potential).
 MOD_RES 175 175 Phosphoserine (By similarity).
 MOD_RES 177 177 Phosphoserine (By similarity).
 MOD_RES 256 256 Phosphoserine.  
Keyword
 Alternative splicing; Bromodomain; Complete proteome; DNA-binding; Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 689 AA 
Protein Sequence
MFTMTRAMEE ALFQHFMHQK LGIAYAIHKP FPFFEGLLDN SIITKRMYME SLEACRNLIP 60
VSRVVHNILT QLERTFNLSL LVTLFSQINL REYPNLVTIY RSFKRVGASY EWQSRDTPIL 120
LEAPTGLAEG SSLHTPLALP PPQPPQPSCS PCAPRVSEPG TSSQQSDEIL SESPSPSDPV 180
LPLPALIQEG RSTSVTNDKL TSKMNAEEDS EEMPSLLTST VQVASDNLIP QIRDKEDPQE 240
MPHSPLGSMP EIRDNSPEPN DPEEPQEVSS TPSDKKGKKR KRCIWSTPKR RHKKKSLPGG 300
TASSRHGIQK KLKRVDQVPQ KKDDSTCNST VETRAQKART ECARKSRSEE IIDGTSEMNE 360
GKRSQKTPST PRRVTQGAAS PGHGIQEKLQ VVDKVTQRKD DSTWNSEVMM RVQKARTKCA 420
RKSRLKEKKK EKDICSSSKR RFQKNIHRRG KPKSDTVDFH CSKLPVTCGE AKGILYKKKM 480
KHGSSVKCIR NEDGTWLTPN EFEVEGKGRN AKNWKRNIRC EGMTLGELLK RKNSDECEVC 540
CQGGQLLCCG TCPRVFHEDC HIPPVEAKRM LWSCTFCRMK RSSGSQQCHH VSKTLERQMQ 600
PQDQLKCEFL LLKAYCHPQS SFFTGIPFNI RDYGEPFQEA MWLDLVKERL ITEMYTVAWF 660
VRDMRLMFRN HKTFYKASDF GQVGLDLEAE FEKDLKDVLG FHEANDGGFW TLP 713 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0004871; F:signal transducer activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR001487; Bromodomain.
 IPR000770; SAND_dom.
 IPR010919; SAND_dom-like.
 IPR004865; Sp100.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF01342; SAND
 PF03172; Sp100 
SMART
 SM00297; BROMO
 SM00249; PHD
 SM00258; SAND 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS51414; HSR
 PS50864; SAND
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS