KLF8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KLF8_HUMAN
• UniProt AC: O95600
• Protein Name: Krueppel-like factor 8
• Gene Name: KLF8
• Organism: Homo sapiens (Human).
• Sequence Length: 359
• Subcellular Localization: Nucleus .
• Protein Description: Transcriptional repressor and activator. Binds to CACCC-boxes promoter elements. Also binds the GT-box of cyclin D1 promoter and mediates cell cycle progression at G(1) phase as a downstream target of focal adhesion kinase (FAK)..
• Protein Sequence: MVDMDKLINNLEVQLNSEGGSMQVFKQVTASVRNRDPPEIEYRSNMTSPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAPIRPPKPQSSPQTLVVSTSTSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLIGGDGKNAGSVKVDPTSMSPLEIPSDSEESTIESGSSALQSLQGLQQEPAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	Phosphorylation	PPEIEYRSNMTSPTL CCCCCCCCCCCCCCC	30.01	28102081
47	Phosphorylation	IEYRSNMTSPTLLDA CCCCCCCCCCCCCCC	35.49	28348404
48	Phosphorylation	EYRSNMTSPTLLDAN CCCCCCCCCCCCCCC	12.72	28348404
50	Phosphorylation	RSNMTSPTLLDANPM CCCCCCCCCCCCCCC	39.46	28348404
67	Acetylation	PALFNDIKIEPPEEL CCCCCCCCCCCCHHH	43.83	21416054
67	Sumoylation	PALFNDIKIEPPEEL CCCCCCCCCCCCHHH	43.83	-
67	Sumoylation	PALFNDIKIEPPEEL CCCCCCCCCCCCHHH	43.83	-
93	Acetylation	PVDLSFHKPKAPLQP CCCCCCCCCCCCCCC	46.32	21416054
95	Acetylation	DLSFHKPKAPLQPAS CCCCCCCCCCCCCCH	68.39	21416054
299	Phosphorylation	KAHRRIHTGEKPYKC HHCCCCCCCCCCCEE	44.67	29496963
342	Phosphorylation	RCTDCNRSFSRSDHL ECCCCCCCCCCCCCC	17.37	29496963
344	Phosphorylation	TDCNRSFSRSDHLSL CCCCCCCCCCCCCHH	31.92	23909892

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
48	S	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
67	K	Sumoylation	Sumoylation at Lys-67 represses transcriptional activity and reduces cell cycle progression into the G(1) phase.	16617055

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KLF8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PARP1_HUMAN	PARP1	physical	21518760
XPO1_HUMAN	XPO1	physical	21518760
A4_HUMAN	APP	physical	21832049
BIN1_HUMAN	BIN1	physical	26496610
SGSM3_HUMAN	SGSM3	physical	26496610
DGCR8_HUMAN	DGCR8	physical	26496610
ANTR1_HUMAN	ANTXR1	physical	26496610
MILK1_HUMAN	MICALL1	physical	26496610
CTBP1_HUMAN	CTBP1	physical	21416054

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Sumoylation

"Sumoylation delimits KLF8 transcriptional activity associated withthe cell cycle regulation.";
Wei H., Wang X., Gan B., Urvalek A.M., Melkoumian Z.K., Guan J.-L.,Zhao J.;
J. Biol. Chem. 281:16664-16671(2006).
Cited for: SUMOYLATION AT LYS-67, INTERACTION WITH PIAS1; PIAS2 AND PIAS4,FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-67 AND LYS-217.
PubMed: 16617055