CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010951
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription factor Sp3 
Protein Synonyms/Alias
 SPR-2 
Gene Name
 SP3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
120SATPTTIKDEAGNLVsumoylation[1, 2]
551SPADIRIKEEEPDPEacetylation[3]
551SPADIRIKEEEPDPEsumoylation[1, 2, 4, 5, 6]
593DQQHQEGKRLRRVACubiquitination[7, 8]
606ACTCPNCKEGGGRGTubiquitination[8]
Reference
 [1] Transcription factor Sp3 is silenced through SUMO modification by PIAS1.
 Sapetschnig A, Rischitor G, Braun H, Doll A, Schergaut M, Melchior F, Suske G.
 EMBO J. 2002 Oct 1;21(19):5206-15. [PMID: 12356736]
 [2] SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization.
 Ross S, Best JL, Zon LI, Gill G.
 Mol Cell. 2002 Oct;10(4):831-42. [PMID: 12419227]
 [3] Transcription factor Sp3 is regulated by acetylation.
 Braun H, Koop R, Ertmer A, Nacht S, Suske G.
 Nucleic Acids Res. 2001 Dec 15;29(24):4994-5000. [PMID: 11812829]
 [4] Complexity of translationally controlled transcription factor Sp3 isoform expression.
 Sapetschnig A, Koch F, Rischitor G, Mennenga T, Suske G.
 J Biol Chem. 2004 Oct 1;279(40):42095-105. [PMID: 15247228]
 [5] Sumoylation of internally initiated Sp3 isoforms regulates transcriptional repression via a Trichostatin A-insensitive mechanism.
 Spengler ML, Kennett SB, Moorefield KS, Simmons SO, Brattain MG, Horowitz JM.
 Cell Signal. 2005 Feb;17(2):153-66. [PMID: 15494207]
 [6] Epigenetic silencing of spermatocyte-specific and neuronal genes by SUMO modification of the transcription factor Sp3.
 Stielow B, Krüger I, Diezko R, Finkernagel F, Gillemans N, Kong-a-San J, Philipsen S, Suske G.
 PLoS Genet. 2010 Nov 11;6(11):e1001203. [PMID: 21085687]
 [7] 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]
 [8] 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
 Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone- induction and house-keeping. 
Sequence Annotation
 ZN_FING 621 645 C2H2-type 1.
 ZN_FING 651 675 C2H2-type 2.
 ZN_FING 681 703 C2H2-type 3.
 REGION 138 237 Transactivation domain (Gln-rich).
 REGION 350 499 Transactivation domain (Gln-rich).
 REGION 534 620 Repressor domain.
 MOD_RES 73 73 Phosphoserine.
 MOD_RES 551 551 N6-acetyllysine; alternate.
 MOD_RES 563 563 Phosphoserine.
 MOD_RES 646 646 Phosphoserine.
 CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 551 551 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Activator; Alternative initiation; Alternative splicing; Complete proteome; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 781 AA 
Protein Sequence
MTAPEKPVKQ EEMAALDVDS GGGGGGGGGH GEYLQQQQQH GNGAVAAAAA AQDTQPSPLA 60
LLAATCSKIG PPSPGDDEEE AAAAAGAPAA AGATGDLASA QLGGAPNRWE VLSATPTTIK 120
DEAGNLVQIP SAATSSGQYV LPLQNLQNQQ IFSVAPGSDS SNGTVSSVQY QVIPQIQSAD 180
GQQVQIGFTG SSDNGGINQE SSQIQIIPGS NQTLLASGTP SANIQNLIPQ TGQVQVQGVA 240
IGGSSFPGQT QVVANVPLGL PGNITFVPIN SVDLDSLGLS GSSQTMTAGI NADGHLINTG 300
QAMDSSDNSE RTGERVSPDI NETNTDTDLF VPTSSSSQLP VTIDSTGILQ QNTNSLTTSS 360
GQVHSSDLQG NYIQSPVSEE TQAQNIQVST AQPVVQHLQL QESQQPTSQA QIVQGITPQT 420
IHGVQASGQN ISQQALQNLQ LQLNPGTFLI QAQTVTPSGQ VTWQTFQVQG VQNLQNLQIQ 480
NTAAQQITLT PVQTLTLGQV AAGGAFTSTP VSLSTGQLPN LQTVTVNSID SAGIQLHPGE 540
NADSPADIRI KEEEPDPEEW QLSGDSTLNT NDLTHLRVQV VDEEGDQQHQ EGKRLRRVAC 600
TCPNCKEGGG RGTNLGKKKQ HICHIPGCGK VYGKTSHLRA HLRWHSGERP FVCNWMYCGK 660
RFTRSDELQR HRRTHTGEKK FVCPECSKRF MRSDHLAKHI KTHQNKKGIH SSSTVLASVE 720
AARDDTLITA GGTTLILANI QQGSVSGIGT VNTSATSNQD ILTNTEIPLQ LVTVSGNETM 780
E 781 
Gene Ontology
 GO:0005634; C:nucleus; IC:UniProtKB.
 GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
 GO:0017053; C:transcriptional repressor complex; IEA:Compara.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IEA:Compara.
 GO:0003690; F:double-stranded DNA binding; IEA:Compara.
 GO:0001078; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription; IEA:Compara.
 GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030183; P:B cell differentiation; IEA:Compara.
 GO:0060216; P:definitive hemopoiesis; IEA:Compara.
 GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Compara.
 GO:0001892; P:embryonic placenta development; IEA:Compara.
 GO:0060136; P:embryonic process involved in female pregnancy; IEA:Compara.
 GO:0048706; P:embryonic skeletal system development; IEA:Compara.
 GO:0043353; P:enucleate erythrocyte differentiation; IEA:Compara.
 GO:0030851; P:granulocyte differentiation; IEA:Compara.
 GO:0001889; P:liver development; IEA:Compara.
 GO:0030324; P:lung development; IEA:Compara.
 GO:0030219; P:megakaryocyte differentiation; IEA:Compara.
 GO:0030224; P:monocyte differentiation; IEA:Compara.
 GO:0001779; P:natural killer cell differentiation; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
 GO:0001503; P:ossification; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0030217; P:T cell differentiation; IEA:Compara.
 GO:0001829; P:trophectodermal cell differentiation; IEA:Compara. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
  
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS