CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037031
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear body protein SP140 
Protein Synonyms/Alias
 SP140 nuclear body protein, isoform CRA_c 
Gene Name
 SP140 
Gene Synonyms/Alias
 hCG_1811427 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
380ANNSTLGKPKRKRRKubiquitination[1, 2, 3, 4]
382NSTLGKPKRKRRKKRubiquitination[2, 4]
562RKKKRILKSQNNSSVubiquitination[2, 4]
622NCIFCRMKESPGSQQubiquitination[2, 4]
682REACQGLKEPMWLDKubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [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] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 753 AA 
Protein Sequence
MAQQGQQGQM ASGDSNLNFR MVAEIQNVEG QNLQEQVCPE PIFRFFRENK VEIASAITRP 60
FPFLMGLRDR SFISEQMYEH FQEAFRNLVP VTRVMYCVLS ELEKTFGWSH LEALFSRINL 120
MAYPDLNEIY RSFQNVCYEH SPLQMNNVND LEDRPRLLPY GKQENSNACH EMDDIAVPQE 180
ALSSSPRCEP GFSSESCEQL ALPKAGGGDA EDAPSLLPVS CKLAIQIDEG ESEEMPKLLP 240
YDTEETFDLK TPQVTNEGEP EKGLCLLPGE GEEGSDDCSE MCDGEERQEA SSSLARRGSV 300
SSELENHPMN EEGESEELAS SLLYDNVPGA EQSAYENEKC SCVMCFSEEV PGSPEARTES 360
DQACGTMDTV DIANNSTLGK PKRKRRKKRG HGWSRMRMRR QENSQQNDNS KADGQVVSSE 420
KKANVNLKDL SKIRGRKRGK PGTRFTQSDR AAQKRVRSRA SRKHKDETVD FKAPLLPVTC 480
GGVKGILHKK KLQQGILVKC IQTEDGKWFT PTEFEIKGGH ARSKNWRLSV RCGGWPLRWL 540
MENGFLPDPP RIRYRKKKRI LKSQNNSSVD PCMRNLDECE VCRDGGELFC CDTCSRVFHE 600
DCHIPPVEAE RTPWNCIFCR MKESPGSQQC CQESEVLERQ MCPEEQLKCE FLLLKVYCCS 660
ESSFFAKIPY YYYIREACQG LKEPMWLDKI KKRLNEHGYP QVEGFVQDMR LIFQNHRASY 720
KYKDFGQMGF RLEAEFEKNF KEVFAIQETN GNN 753 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001487; Bromodomain.
 IPR000770; SAND_dom.
 IPR010919; SAND_dom-like.
 IPR004865; Sp100.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF00628; PHD
 PF01342; SAND
 PF03172; Sp100 
SMART
 SM00297; BROMO
 SM00249; PHD
 SM00258; SAND 
PROSITE
 PS50014; BROMODOMAIN_2
 PS51414; HSR
 PS50864; SAND
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS