dbPTM

KLF4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KLF4_MOUSE
UniProt AC	Q60793
Protein Name	Krueppel-like factor 4
Gene Name	Klf4
Organism	Mus musculus (Mouse).
Sequence Length	483
Subcellular Localization	Nucleus .
Protein Description	Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription (By similarity)..
Protein Sequence	MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRPAGAPTNRWREELSHMKRLPPLPGRPYDLAATVATDLESGGAGAACSSNNPALLARRETEEFNDLLDLDFILSNSLTHQESVAATVTTSASASSSSSPASSGPASAPSTCSFSYPIRAGGDPGVAASNTGGGLLYSRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLTTPGSEYSSPSVISVSKGSPDGSHPVVVAPYSGGPPRMCPKIKQEAVPSCTVSRSLEAHLSAGPQLSNGHRPNTHDFPLGRQLPTRTTPTLSPEELLNSRDCHPGLPLPPGFHPHPGPNYPPFLPDQMQSQVPSLHYQELMPPGSCLPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	GPAGREKTLRPAGAP CCCCCCCCCCCCCCC	24.20	-
132	Phosphorylation	ASASSSSSPASSGPA CCCCCCCCCCCCCCC	26.83	23384938
162	Phosphorylation	GDPGVAASNTGGGLL CCCCCCCCCCCCCCE	25.78	-
225	Acetylation	PGGGLMGKFVLKASL CCCCCCCEEEEEEEE	20.52	17908689
229	Acetylation	LMGKFVLKASLTTPG CCCEEEEEEEECCCC	30.54	17908689
241	Phosphorylation	TPGSEYSSPSVISVS CCCCCCCCCCEEEEE	21.94	23608596
251	Phosphorylation	VISVSKGSPDGSHPV EEEEECCCCCCCCCE	24.45	26824392
255	Phosphorylation	SKGSPDGSHPVVVAP ECCCCCCCCCEEEEE	31.81	21149613
263	Phosphorylation	HPVVVAPYSGGPPRM CCEEEEECCCCCCCC	15.37	21149613
264	Phosphorylation	PVVVAPYSGGPPRMC CEEEEECCCCCCCCC	35.89	21149613
275	Sumoylation	PRMCPKIKQEAVPSC CCCCHHHCHHHCCCC	48.49	-
275	Sumoylation	PRMCPKIKQEAVPSC CCCCHHHCHHHCCCC	48.49	-
319	Phosphorylation	GRQLPTRTTPTLSPE CCCCCCCCCCCCCHH	39.34	25293948
320	Phosphorylation	RQLPTRTTPTLSPEE CCCCCCCCCCCCHHH	15.81	22817900
322	Phosphorylation	LPTRTTPTLSPEELL CCCCCCCCCCHHHHH	37.46	25293948
324	Phosphorylation	TRTTPTLSPEELLNS CCCCCCCCHHHHHCC	32.51	29895711
418	Ubiquitination	YTKSSHLKAHLRTHT EECCHHHHHHHHHCC	28.47	-

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
132	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
132	S	Phosphorylation	Kinase	ERK2	P63085	PSP
132	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
132	S	Phosphorylation	Kinase	ERK1	Q63844	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KLF4_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of KLF4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SMCA4_MOUSE	Smarca4	physical	20305087

Drug and Disease Associations

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

Regulatory Network of KLF4_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASSSPECTROMETRY.	19367708 [Abstract]