CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005182
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear autoantigen Sp-100 
Protein Synonyms/Alias
 Nuclear dot-associated Sp100 protein; Speckled 100 kDa 
Gene Name
 SP100 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
87DRDLITNKMFEDSQDubiquitination[1]
151FENVIHDKLPLQESEubiquitination[1, 2]
225RKDTTSDKDDSLGSQubiquitination[2]
297SVRLVDIKKEKPFSNsumoylation[3, 4, 5, 6]
300LVDIKKEKPFSNSKVubiquitination[1]
306EKPFSNSKVECQAQAubiquitination[1]
739GKFEDMAKADKAHYEubiquitination[2]
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] 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] The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers.
 Sternsdorf T, Jensen K, Reich B, Will H.
 J Biol Chem. 1999 Apr 30;274(18):12555-66. [PMID: 10212234]
 [4] The nucleoporin RanBP2 has SUMO1 E3 ligase activity.
 Pichler A, Gast A, Seeler JS, Dejean A, Melchior F.
 Cell. 2002 Jan 11;108(1):109-20. [PMID: 11792325]
 [5] "ChopNSpice," a mass spectrometric approach that allows identification of endogenous small ubiquitin-like modifier-conjugated peptides.
 Hsiao HH, Meulmeester E, Frank BT, Melchior F, Urlaub H.
 Mol Cell Proteomics. 2009 Dec;8(12):2664-75. [PMID: 19721078]
 [6] SUMO pathway dependent recruitment of cellular repressors to herpes simplex virus type 1 genomes.
 Cuchet-Lourenço D, Boutell C, Lukashchuk V, Grant K, Sykes A, Murray J, Orr A, Everett RD.
 PLoS Pathog. 2011 Jul;7(7):e1002123. [PMID: 21779164] 
Functional Description
 Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53- mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation. 
Sequence Annotation
 DOMAIN 33 149 HSR.
 DOMAIN 595 676 SAND.
 DNA_BIND 677 753 HMG box 1.
 DNA_BIND 769 837 HMG box 2.
 REGION 333 478 Sufficient to mediate interaction with
 MOTIF 165 168 D-box; recognition signal for CDC20-
 MOTIF 284 297 PxVxL motif.
 MOTIF 536 553 Nuclear localization signal (Potential).
 MOTIF 568 592 Nuclear localization signal (Potential).
 MOTIF 717 734 Nuclear localization signal (Potential).
 MOD_RES 18 18 Phosphoserine.
 MOD_RES 157 157 Phosphoserine.
 MOD_RES 171 171 Phosphoserine.
 MOD_RES 331 331 Phosphoserine.
 MOD_RES 362 362 Phosphoserine.
 MOD_RES 407 407 Phosphoserine.
 MOD_RES 409 409 Phosphoserine.
 MOD_RES 410 410 Phosphoserine.
 CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 879 AA 
Protein Sequence
MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY DIVFKHFKRN 60
KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV PVQRVVYNVL SELEKTFNLP 120
VLEALFSDVN MQEYPDLIHI YKGFENVIHD KLPLQESEEE EREERSGLQL SLEQGTGENS 180
FRSLTWPPSG SPSHAGTTPP ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ 240
KAEPTESCEQ IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK 300
PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS EPVINNDNPL 360
ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI GQDHDFSESS EEEAPAEASS 420
GALRSKHGEK APMTSRSTST WRIPSRKRRF SSSDFSDLSN GEELQETCSS SLRRGSGSQP 480
QEPENKKCSC VMCFPKGVPR SQEARTESSQ ASDMMDTMDV ENNSTLEKHS GKRRKKRRHR 540
SKVNGLQRGR KKDRPRKHLT LNNKVQKKRW QQRGRKANTR PLKRRRKRGP RIPKDENINF 600
KQSELPVTCG EVKGTLYKER FKQGTSKKCI QSEDKKWFTP REFEIEGDRG ASKNWKLSIR 660
CGGYTLKVLM ENKFLPEPPS TRKKRILESH NNTLVDPCEE HKKKNPDASV KFSEFLKKCS 720
ETWKTIFAKE KGKFEDMAKA DKAHYEREMK TYIPPKGEKK KKFKDPNAPK RPPLAFFLFC 780
SEYRPKIKGE HPGLSIDDVV KKLAGMWNNT AAADKQFYEK KAAKLKEKYK KDIAAYRAKG 840
KPNSAKKRVV KAEKSKKKKE EEEDEEDEQE EENEEDDDK 879 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:BHF-UCL.
 GO:0034399; C:nuclear periphery; IDA:BHF-UCL.
 GO:0005730; C:nucleolus; IDA:BHF-UCL.
 GO:0016605; C:PML body; IDA:BHF-UCL.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL.
 GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
 GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:BHF-UCL.
 GO:0060333; P:interferon-gamma-mediated signaling pathway; IC:BHF-UCL.
 GO:0043392; P:negative regulation of DNA binding; IDA:BHF-UCL.
 GO:0010596; P:negative regulation of endothelial cell migration; IMP:UniProtKB.
 GO:0046826; P:negative regulation of protein export from nucleus; IMP:UniProtKB.
 GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:BHF-UCL.
 GO:0032897; P:negative regulation of viral transcription; IDA:BHF-UCL.
 GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:BHF-UCL.
 GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB.
 GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
 GO:1902044; P:regulation of Fas signaling pathway; IMP:UniProtKB.
 GO:0034097; P:response to cytokine stimulus; IDA:BHF-UCL.
 GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
 GO:0034340; P:response to type I interferon; IDA:BHF-UCL.
 GO:0048384; P:retinoic acid receptor signaling pathway; IC:BHF-UCL.
 GO:0000723; P:telomere maintenance; IMP:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0060337; P:type I interferon-mediated signaling pathway; IC:BHF-UCL.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR009071; HMG_box_dom.
 IPR000770; SAND_dom.
 IPR010919; SAND_dom-like.
 IPR004865; Sp100. 
Pfam
 PF09011; DUF1898
 PF00505; HMG_box
 PF01342; SAND
 PF03172; Sp100 
SMART
 SM00398; HMG
 SM00258; SAND 
PROSITE
 PS50118; HMG_BOX_2
 PS51414; HSR
 PS50864; SAND 
PRINTS