P08047

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession SP1_HUMAN; P08047;
Entrez ID 6667
GenBank Protein ID NM_001251825.1; NM_003109.1; NM_138473.2; XM_011538696.2;
GenBank Nucleotide ID NP_001238754.1; NP_003100.1; NP_612482.2; XP_011536998.1;
Protein Name Transcription factor Sp1
Gene Name SP1; TSFP1
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionTranscription 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. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component ARNTL/BMAL1.
Sequence
(Fasta)
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 786

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1GlycosylationPancreatic cancer/carcinoma/adenocarcinomaA3837133; 24129563
[Reference]: Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1
2Serine PhosphorylationSystemic lupus erythematosusDS5921097497
[Reference]: Our results show that nuclei from SLE T cells contain lower levels of Ser(59)-phosphorylated SP-1 protein and a stronger SP-1 binding to the CREM promoter. We conclude that protein phosphatase 2A accounts for enhanced SP-1 dephosphorylation at Ser(59) in SLE T cells. More importantly, CREM promoter activity mirrors reliably disease activity in SLE patients
3Threonine PhosphorylationLung cancer/carcinomaUT73922266860
[Reference]: Moreover, we showed that Sp1 is a novel mitotic substrate of CDK1/cyclin B1 and is phosphorylated by it at Thr 739 before the onset of mitosis. Phospho-Sp1 reduced its DNA-binding ability and facilitated the chromatin condensation process during mitosis.

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 5)
MESH:D002471 ; Cell Transformation, Neoplastic
MESH:D006943 ; Hyperglycemia
MESH:D009361 ; Neoplasm Invasiveness
MESH:D009362 ; Neoplasm Metastasis
MESH:D012878 ; Skin Neoplasms
GWASdb
(count: 1)
rs34656641; Bone mineral density; bone resorption disease

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 47)
(view all)
101       DLTATQLSQGANGWQ     dbPAF
12        DHSMDEMTAVVKIEK     dbPAF
2         ******MSDQDHSMD     dbPAF
278       SVSAATLTPSSQAVT     dbPAF
36        GNGGGAFSQARSSST     dbPAF
375       LNIQQNQTSGGSLQA     dbPAF
Acetylation
(count: 2)
19        TAVVKIEKGVGGNNG     PLMD
703       MRSDHLSKHIKTHQN     PLMD
Ubiquitination
(count: 4)
19        TAVVKIEKGVGGNNG     PLMD
610       ACTCPYCKDSEGRGS     PLMD
685       RTHTGEKKFACPECP     PLMD
712       IKTHQNKKGGPGVAL     PLMD
Sumoylation
(count: 1)
16        DEMTAVVKIEKGVGG     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource
E9PFC7P08047HPRD
F5GX74P08047HPRD; IntAct
H0YBT0P08047IntAct
O00268P08047HPRD
O00716P08047HPRD
O15294P08047HPRD
O43474P08047HPRD
O60476P08047IntAct
O75376P08047HPRD
O95365P08047HPRD
P00519P08047IntAct
P00846P08047IntAct
P01106P08047HPRD
P03087P08047MINT
P03372P08047HPRD; IntAct
P03905P08047IntAct
P03915P08047IntAct
P04198P08047IntAct
P04637P08047HPRD; MINT
P05412P08047HPRD
P06241P08047IntAct
P06400P08047HPRD
P06729P08047HPRD
P08047P08047HPRD; IntAct
P08047P10275HPRD
P08047P10276HPRD
P08047P10589HPRD
P08047P11142HPRD
P08047P12931IntAct
P08047P14859IntAct;HPRD; MINT
P08047P14921HPRD
P08047P15172HPRD
P08047P15173HPRD
P08047P16333IntAct
P08047P17096HPRD; MINT
P08047P17542HPRD
P08047P17676HPRD
P08047P17844IntAct
P08047P18146HPRD; MINT
P08047P19793HPRD
P08047P20226HPRD
P08047P21453IntAct
P08047P22059IntAct
P08047P23511HPRD
P08047P24385HPRD
P08047P25208HPRD
P08047P25490HPRD; DIP
P08047P27361HPRD
P08047P28360HPRD
P08047P28482HPRD
P08047P28749HPRD
P08047P29353HPRD
P08047P29474HPRD
P08047P29590HPRD
P08047P32519HPRD; IntAct
P08047P36956HPRD
P08047P40337HPRD
P08047P41182HPRD
P08047P41235HPRD
P08047P42285HPRD
P08047P42574HPRD
P08047P42858HPRD; MINT
P08047P46108IntAct
P08047P51532IntAct
P08047P51610HPRD; IntAct
P08047P55209IntAct
P08047P56645HPRD
P08047P56693HPRD
P08047P57073HPRD
P08047P60174IntAct
P08047P62195HPRD
P08047P62993IntAct
P08047P68400HPRD
P08047P78527HPRD
P08047P84022HPRD
P08047Q00403DIP
P08047Q00577HPRD
P08047Q01094HPRD; IntAct
P08047Q01196MINT
P08047Q01780IntAct
P08047Q02446HPRD
P08047Q02447HPRD
P08047Q04206HPRD; IntAct
P08047Q04864HPRD
P08047Q05516HPRD
P08047Q06413HPRD
P08047Q06546HPRD; MINT
P08047Q09028HPRD
P08047Q09472HPRD
P08047Q12756IntAct
P08047Q12772HPRD; IntAct
P08047Q12873IntAct
P08047Q13118HPRD; IntAct
P08047Q13285HPRD
P08047Q13427IntAct
P08047Q13485HPRD; IntAct
P08047Q13547HPRD; MINT
P08047Q13952IntAct
P08047Q14209HPRD
P08047Q14814HPRD
P08047Q15306MINT
P08047Q15459HPRD; IntAct
P08047Q15545DIP
P08047Q15759IntAct
P08047Q15796HPRD
P08047Q16665HPRD; MINT
P08047Q53GS9IntAct
P08047Q5T5U3IntAct
P08047Q5U623HPRD
P08047Q6NW34IntAct
P08047Q6P0N0HPRD
P08047Q6W2J9HPRD
P08047Q7Z3K3HPRD; IntAct
P08047Q8IXK0IntAct
P08047Q8N108HPRD
P08047Q8WUF5HPRD
P08047Q92731HPRD
P08047Q92769HPRD; IntAct
P08047Q92988IntAct
P08047Q99612HPRD
P08047Q99814MINT
P08047Q9GZR1IntAct
P08047Q9NRR4HPRD; IntAct
P08047Q9NV58IntAct
P08047Q9NY61HPRD; MINT
P08047Q9NZU7IntAct
P08047Q9UBL3IntAct
P08047Q9Y276MINT
P08047Q9Y618HPRD