dbPTM

KLF3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KLF3_MOUSE
UniProt AC	Q60980
Protein Name	Krueppel-like factor 3
Gene Name	Klf3
Organism	Mus musculus (Mouse).
Sequence Length	344
Subcellular Localization	Nucleus .
Protein Description	Binds to the CACCC box of erythroid cell-expressed genes. May play a role in hematopoiesis..
Protein Sequence	MLMFDPVPVKQEAMDPVSVSFPSNYIESMKPNKYGVIYSTPLPDKFFQTPEGLTHGIQVEPVDLTVNKRGSPPAAGGSPSSLKFPSHRRASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPVMAAALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMDNSNSGMPVPVIESYEKPLLQKKIKIEPGIEPQRTDYYPEEMSPPLMNPVSPPQALLQENHPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Sumoylation	MFDPVPVKQEAMDPV CCCCCCCCCCCCCCC	36.03	-
10	Sumoylation	MFDPVPVKQEAMDPV CCCCCCCCCCCCCCC	36.03	15684403
71	Phosphorylation	LTVNKRGSPPAAGGS EEEECCCCCCCCCCC	31.57	25521595
78	Phosphorylation	SPPAAGGSPSSLKFP CCCCCCCCCHHCCCC	22.23	25521595
80	Phosphorylation	PAAGGSPSSLKFPSH CCCCCCCHHCCCCCC	50.42	25168779
81	Phosphorylation	AAGGSPSSLKFPSHR CCCCCCHHCCCCCCC	38.67	21082442
86	Phosphorylation	PSSLKFPSHRRASPG CHHCCCCCCCCCCCC	32.53	25168779
91	Phosphorylation	FPSHRRASPGLSMPS CCCCCCCCCCCCCCC	20.07	25521595
95	Phosphorylation	RRASPGLSMPSSSPP CCCCCCCCCCCCCCC	34.26	25168779
98	Phosphorylation	SPGLSMPSSSPPIKK CCCCCCCCCCCCCCC	34.50	25521595
99	Phosphorylation	PGLSMPSSSPPIKKY CCCCCCCCCCCCCCC	40.78	27087446
100	Phosphorylation	GLSMPSSSPPIKKYS CCCCCCCCCCCCCCC	38.75	27087446
106	Phosphorylation	SSPPIKKYSPPSPGV CCCCCCCCCCCCCCC	22.77	26239621
107	Phosphorylation	SPPIKKYSPPSPGVQ CCCCCCCCCCCCCCC	38.93	26239621
110	Phosphorylation	IKKYSPPSPGVQPFG CCCCCCCCCCCCCCC	37.36	26824392
121	Phosphorylation	QPFGVPLSMPPVMAA CCCCCCCCCCHHHHH	24.15	26643407
197	Sumoylation	PLLQKKIKIEPGIEP CHHHCCCCCCCCCCC	50.31	-
207	Phosphorylation	PGIEPQRTDYYPEEM CCCCCCCCCCCCHHC	24.09	26643407
209	Phosphorylation	IEPQRTDYYPEEMSP CCCCCCCCCCHHCCC	21.95	26643407
210	Phosphorylation	EPQRTDYYPEEMSPP CCCCCCCCCHHCCCC	13.64	26643407
215	Phosphorylation	DYYPEEMSPPLMNPV CCCCHHCCCCCCCCC	27.01	21149613
223	Phosphorylation	PPLMNPVSPPQALLQ CCCCCCCCCCHHHHH	31.92	21149613
235	Phosphorylation	LLQENHPSVIVQPGK HHHCCCCCEEECCCC	19.54	21149613
249	Phosphorylation	KRPLPVESPDTQRKR CCCCCCCCCCHHHCC	28.45	27087446
252	Phosphorylation	LPVESPDTQRKRRIH CCCCCCCHHHCCCCC	33.39	25619855
284	Phosphorylation	KAHRRTHTGEKPYKC HHCCCCCCCCCCCEE	46.56	-
327	Phosphorylation	QCPDCDRSFSRSDHL CCCCCCCCCCHHHHH	17.83	23140645
329	Phosphorylation	PDCDRSFSRSDHLAL CCCCCCCCHHHHHHH	31.92	23140645

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
Oops, there are no upstream regulatory protein records of KLF3_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
197	K	Sumoylation		15684403
Sumoylation on Lys-197 is the major site.

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 KLF3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SQSTM_MOUSE	Sqstm1	physical	23754749

Drug and Disease Associations

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

Regulatory Network of KLF3_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-71 AND SER-91, AND MASSSPECTROMETRY.	19367708 [Abstract]
Sumoylation
Reference	PubMed
"Role for SUMO modification in facilitating transcriptional repressionby BKLF."; Perdomo J., Verger A., Turner J., Crossley M.; Mol. Cell. Biol. 25:1549-1559(2005). Cited for: SUMOYLATION AT LYS-10 AND LYS-197, FUNCTION, AND MUTAGENESIS OFLYS-10; GLU-12; LYS-197 AND GLU-199.	15684403 [Abstract]

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