dbPTM

KLF3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KLF3_HUMAN
UniProt AC	P57682
Protein Name	Krueppel-like factor 3
Gene Name	KLF3
Organism	Homo sapiens (Human).
Sequence Length	345
Subcellular Localization	Nucleus .
Protein Description	Binds to the CACCC box of erythroid cell-expressed genes. May play a role in hematopoiesis (By similarity)..
Protein Sequence	MLMFDPVPVKQEAMDPVSVSYPSNYMESMKPNKYGVIYSTPLPEKFFQTPEGLSHGIQMEPVDLTVNKRSSPPSAGNSPSSLKFPSSHRRASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPVMAAALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMENSSSSMQVPVIESYEKPISQKKIKIEPGIEPQRTDYYPEEMSPPLMNSVSPPQALLQENHPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MLMFDPVP -------CCCCCCCC	5.74	-
10	Sumoylation	MFDPVPVKQEAMDPV CCCCCCCCCCCCCCC	36.03	-
10	Sumoylation	MFDPVPVKQEAMDPV CCCCCCCCCCCCCCC	36.03	-
18	Phosphorylation	QEAMDPVSVSYPSNY CCCCCCCCCCCCHHH	15.67	19413330
21	Phosphorylation	MDPVSVSYPSNYMES CCCCCCCCCHHHHHH	14.44	-
34	Phosphorylation	ESMKPNKYGVIYSTP HHCCCCCEEEEEECC	24.22	21945579
38	Phosphorylation	PNKYGVIYSTPLPEK CCCEEEEEECCCCHH	12.23	21945579
39	Phosphorylation	NKYGVIYSTPLPEKF CCEEEEEECCCCHHH	16.66	21945579
40	Phosphorylation	KYGVIYSTPLPEKFF CEEEEEECCCCHHHC	16.33	21945579
49	Phosphorylation	LPEKFFQTPEGLSHG CCHHHCCCCCCCCCC	20.39	25159151
68	Sumoylation	PVDLTVNKRSSPPSA EECCEECCCCCCCCC	49.69	28112733
70	Phosphorylation	DLTVNKRSSPPSAGN CCEECCCCCCCCCCC	49.13	23401153
71	Phosphorylation	LTVNKRSSPPSAGNS CEECCCCCCCCCCCC	44.88	30266825
74	Phosphorylation	NKRSSPPSAGNSPSS CCCCCCCCCCCCCCC	52.79	23927012
78	Phosphorylation	SPPSAGNSPSSLKFP CCCCCCCCCCCCCCC	25.82	23927012
80	Phosphorylation	PSAGNSPSSLKFPSS CCCCCCCCCCCCCCC	48.39	25159151
81	Phosphorylation	SAGNSPSSLKFPSSH CCCCCCCCCCCCCCC	38.67	23663014
86	Phosphorylation	PSSLKFPSSHRRASP CCCCCCCCCCCCCCC	41.74	26074081
87	Phosphorylation	SSLKFPSSHRRASPG CCCCCCCCCCCCCCC	22.66	26074081
92	Phosphorylation	PSSHRRASPGLSMPS CCCCCCCCCCCCCCC	20.07	23927012
96	Phosphorylation	RRASPGLSMPSSSPP CCCCCCCCCCCCCCC	34.26	30266825
99	Phosphorylation	SPGLSMPSSSPPIKK CCCCCCCCCCCCCCC	34.50	30266825
100	Phosphorylation	PGLSMPSSSPPIKKY CCCCCCCCCCCCCCC	40.78	23401153
101	Phosphorylation	GLSMPSSSPPIKKYS CCCCCCCCCCCCCCC	38.75	23927012
107	Phosphorylation	SSPPIKKYSPPSPGV CCCCCCCCCCCCCCC	22.77	22617229
108	Phosphorylation	SPPIKKYSPPSPGVQ CCCCCCCCCCCCCCC	38.93	26055452
111	Phosphorylation	IKKYSPPSPGVQPFG CCCCCCCCCCCCCCC	37.36	21955146
122	Phosphorylation	QPFGVPLSMPPVMAA CCCCCCCCCCHHHHH	24.15	23403867
132	Phosphorylation	PVMAAALSRHGIRSP HHHHHHHHHCCCCCC	19.94	23403867
196	Sumoylation	EKPISQKKIKIEPGI CCCCCCCCCEECCCC	41.41	28112733
198	Sumoylation	PISQKKIKIEPGIEP CCCCCCCEECCCCCC	50.31	28112733
198	Sumoylation	PISQKKIKIEPGIEP CCCCCCCEECCCCCC	50.31	-
208	Phosphorylation	PGIEPQRTDYYPEEM CCCCCCCCCCCCHHH	24.09	27251275
210	Phosphorylation	IEPQRTDYYPEEMSP CCCCCCCCCCHHHCC	21.95	27251275
211	Phosphorylation	EPQRTDYYPEEMSPP CCCCCCCCCHHHCCC	13.64	27251275
216	Phosphorylation	DYYPEEMSPPLMNSV CCCCHHHCCCCCCCC	27.01	29116813
222	Phosphorylation	MSPPLMNSVSPPQAL HCCCCCCCCCCCHHH	15.26	26657352
224	Phosphorylation	PPLMNSVSPPQALLQ CCCCCCCCCCHHHHH	30.59	29116813
236	Phosphorylation	LLQENHPSVIVQPGK HHHCCCCCEEECCCC	19.54	27251275
250	Phosphorylation	KRPLPVESPDTQRKR CCCCCCCCCCHHHCC	28.45	29255136
253	Phosphorylation	LPVESPDTQRKRRIH CCCCCCCHHHCCCCC	33.39	23401153
283	Phosphorylation	HLKAHRRTHTGEKPY HHHHCCCCCCCCCCC	24.60	28348404
285	Phosphorylation	KAHRRTHTGEKPYKC HHCCCCCCCCCCCEE	46.56	26270265
288	Ubiquitination	RRTHTGEKPYKCTWE CCCCCCCCCCEECCC	55.80	-
315	Phosphorylation	TRHFRKHTGIKPFQC HHHHHHHHCCCCCCC	43.57	29214152
330	Phosphorylation	PDCDRSFSRSDHLAL CCCCCCCCHHHHHHH	31.92	17081983

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
71	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
78	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
92	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
101	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
108	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
111	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
216	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
224	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
250	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
198	K	Sumoylation		25218447
Sumoylation on Lys-198 is the major site (By similarity).

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FHL3_HUMAN	FHL3	physical	12556451
CTBP2_HUMAN	CTBP2	physical	12556451
KDM1A_HUMAN	KDM1A	physical	23455924
SUV92_HUMAN	SUV39H2	physical	23455924
LHX8_HUMAN	LHX8	physical	25416956

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.

Regulatory Network of KLF3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-101, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.	17081983 [Abstract]

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