CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002591
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription factor Sp1 
Protein Synonyms/Alias
  
Gene Name
 SP1 
Gene Synonyms/Alias
 TSFP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
16DEMTAVVKIEKGVGGsumoylation[1, 2]
610ACTCPYCKDSEGRGSubiquitination[3]
685RTHTGEKKFACPECPubiquitination[3]
703MRSDHLSKHIKTHQNacetylation[4]
Reference
 [1] Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process.
 Wang YT, Chuang JY, Shen MR, Yang WB, Chang WC, Hung JJ.
 J Mol Biol. 2008 Jul 25;380(5):869-85. [PMID: 18572193]
 [2] Interplay of posttranslational modifications in Sp1 mediates Sp1 stability during cell cycle progression.
 Wang YT, Yang WB, Chang WC, Hung JJ.
 J Mol Biol. 2011 Nov 18;414(1):1-14. [PMID: 21983342]
 [3] 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]
 [4] Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription.
 Hung JJ, Wang YT, Chang WC.
 Mol Cell Biol. 2006 Mar;26(5):1770-85. [PMID: 16478997] 
Functional Description
 Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR- alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. 
Sequence Annotation
 ZN_FING 626 650 C2H2-type 1.
 ZN_FING 656 680 C2H2-type 2.
 ZN_FING 686 708 C2H2-type 3.
 REGION 2 82 Repressor domain.
 REGION 146 251 Transactivation domain A (Gln-rich).
 REGION 261 495 Transactivation domain B (Gln-rich).
 REGION 496 610 Transactivation domain C (highly
 REGION 619 785 VZV IE62-binding.
 REGION 708 785 Domain D.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 7 7 Phosphoserine.
 MOD_RES 59 59 Phosphoserine.
 MOD_RES 101 101 Phosphoserine; by ATM.
 MOD_RES 278 278 Phosphothreonine; by MAPK8.
 MOD_RES 453 453 Phosphothreonine; by MAPK1 AND MAPK3.
 MOD_RES 612 612 Phosphoserine; alternate.
 MOD_RES 640 640 Phosphothreonine; alternate.
 MOD_RES 641 641 Phosphoserine; by PKC/PRKCZ; alternate.
 MOD_RES 651 651 Phosphothreonine; by PKC/PRKCZ.
 MOD_RES 668 668 Phosphothreonine.
 MOD_RES 670 670 Phosphoserine; by PKC/PRKCZ.
 MOD_RES 681 681 Phosphothreonine; by PKC/PRKCZ.
 MOD_RES 702 702 Phosphoserine; alternate.
 MOD_RES 703 703 N6-acetyllysine.
 MOD_RES 739 739 Phosphothreonine; by MAPK1, MAPK3 AND
 CARBOHYD 491 491 O-linked (GlcNAc).
 CARBOHYD 612 612 O-linked (GlcNAc); alternate.
 CARBOHYD 640 640 O-linked (GlcNAc); alternate.
 CARBOHYD 641 641 O-linked (GlcNAc); alternate.
 CARBOHYD 698 698 O-linked (GlcNAc).
 CARBOHYD 702 702 O-linked (GlcNAc); alternate.
 CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Activator; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Glycoprotein; Host-virus interaction; 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
 785 AA 
Protein Sequence
MSDQDHSMDE MTAVVKIEKG VGGNNGGNGN GGGAFSQARS SSTGSSSSTG GGGQESQPSP 60
LALLAATCSR IESPNENSNN SQGPSQSGGT GELDLTATQL SQGANGWQII SSSSGATPTS 120
KEQSGSSTNG SNGSESSKNR TVSGGQYVVA AAPNLQNQQV LTGLPGVMPN IQYQVIPQFQ 180
TVDGQQLQFA ATGAQVQQDG SGQIQIIPGA NQQIITNRGS GGNIIAAMPN LLQQAVPLQG 240
LANNVLSGQT QYVTNVPVAL NGNITLLPVN SVSAATLTPS SQAVTISSSG SQESGSQPVT 300
SGTTISSASL VSSQASSSSF FTNANSYSTT TTTSNMGIMN FTTSGSSGTN SQGQTPQRVS 360
GLQGSDALNI QQNQTSGGSL QAGQQKEGEQ NQQTQQQQIL IQPQLVQGGQ ALQALQAAPL 420
SGQTFTTQAI SQETLQNLQL QAVPNSGPII IRTPTVGPNG QVSWQTLQLQ NLQVQNPQAQ 480
TITLAPMQGV SLGQTSSSNT TLTPIASAAS IPAGTVTVNA AQLSSMPGLQ TINLSALGTS 540
GIQVHPIQGL PLAIANAPGD HGAQLGLHGA GGDGIHDDTA GGEEGENSPD AQPQAGRRTR 600
REACTCPYCK DSEGRGSGDP GKKKQHICHI QGCGKVYGKT SHLRAHLRWH TGERPFMCTW 660
SYCGKRFTRS DELQRHKRTH TGEKKFACPE CPKRFMRSDH LSKHIKTHQN KKGGPGVALS 720
VGTLPLDSGA GSEGSGTATP SALITTNMVA MEAICPEGIA RLANSGINVM QVADLQSINI 780
SGNGF 785 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0032993; C:protein-DNA complex; IEA:Compara.
 GO:0043425; F:bHLH transcription factor binding; ISS:BHF-UCL.
 GO:0003690; F:double-stranded DNA binding; IDA:BHF-UCL.
 GO:0035326; F:enhancer binding; IEA:Compara.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISS:BHF-UCL.
 GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IEA:Compara.
 GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Compara.
 GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISS:BHF-UCL.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 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:0001889; P:liver development; IEA:Compara.
 GO:0030324; P:lung development; IEA:Compara.
 GO:0030219; P:megakaryocyte differentiation; IEA:Compara.
 GO:0001503; P:ossification; IEA:Compara.
 GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0001829; P:trophectodermal cell differentiation; IEA:Compara.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
 PF00096; zf-C2H2 
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS