dbPTM

KLF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KLF1_HUMAN
UniProt AC	Q13351
Protein Name	Krueppel-like factor 1
Gene Name	KLF1
Organism	Homo sapiens (Human).
Sequence Length	362
Subcellular Localization	Nucleus . Colocalizes with SUMO1 in nuclear speckles..
Protein Description	Transcription regulator of erythrocyte development that probably serves as a general switch factor during erythropoiesis. Is a dual regulator of fetal-to-adult globin switching. Binds to the CACCC box in the beta-globin gene promoter and acts as a preferential activator of this gene. Furthermore, it binds to the BCL11A promoter and activates expression of BCL11A, which in turn represses the HBG1 and HBG2 genes. This dual activity ensures that, in most adults, fetal hemoglobin levels are low. Able to activate CD44 and AQP1 promoters. When sumoylated, acts as a transcriptional repressor by promoting interaction with CDH2/MI2beta and also represses megakaryocytic differentiation..
Protein Sequence	MATAETALPSISTLTALGPFPDTQDDFLKWWRSEEAQDMGPGPPDPTEPPLHVKSEDQPGEEEDDERGADATWDLDLLLTNFSGPEPGGAPQTCALAPSEASGAQYPPPPETLGAYAGGPGLVAGLLGSEDHSGWVRPALRARAPDAFVGPALAPAPAPEPKALALQPVYPGPGAGSSGGYFPRTGLSVPAASGAPYGLLSGYPAMYPAPQYQGHFQLFRGLQGPAPGPATSPSFLSCLGPGTVGTGLGGTAEDPGVIAETAPSKRGRRSWARKRQAAHTCAHPGCGKSYTKSSHLKAHLRTHTGEKPYACTWEGCGWRFARSDELTRHYRKHTGQRPFRCQLCPRAFSRSDHLALHMKRHL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MATAETALPS -----CCCHHHHCCC	24.59	19690332
6	Phosphorylation	--MATAETALPSIST --CCCHHHHCCCCHH	30.91	19690332
15	Phosphorylation	LPSISTLTALGPFPD CCCCHHHHCCCCCCC	21.67	22817900
23	Phosphorylation	ALGPFPDTQDDFLKW CCCCCCCCHHHHHHH	33.85	9722526
184	Methylation	SSGGYFPRTGLSVPA CCCCCCCCCCCCCCC	31.37	-
265	Acetylation	IAETAPSKRGRRSWA CCCCCCCCCCCHHHH	58.79	9707565
274	Acetylation	GRRSWARKRQAAHTC CCHHHHHHHHHHHHC	40.91	9707565
288	Acetylation	CAHPGCGKSYTKSSH CCCCCCCCCCCCCHH	44.35	11259590
297	Sumoylation	YTKSSHLKAHLRTHT CCCCHHHHHHHHHCC	28.47	-
297	Sumoylation	YTKSSHLKAHLRTHT CCCCHHHHHHHHHCC	28.47	-
297	Ubiquitination	YTKSSHLKAHLRTHT CCCCHHHHHHHHHCC	28.47	-
302	Phosphorylation	HLKAHLRTHTGEKPY HHHHHHHHCCCCCCE	30.10	-
304	Phosphorylation	KAHLRTHTGEKPYAC HHHHHHCCCCCCEEE	46.56	-

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
23	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
23	T	Phosphorylation	Kinase	CK2	-	Uniprot
23	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
23	T	Phosphorylation	-
Phosphorylation on Thr-23 is critical for the transactivation activity (By similarity).
274	K	Acetylation	-
Acetylated; can be acetylated on both Lys-274 and Lys-288.
274	K	Acetylation	-
Acetylation on Lys-274 (by CBP) appears to be the major site affecting EKLF transactivation activity (By similarity).
288	K	Acetylation	-
Acetylated; can be acetylated on both Lys-274 and Lys-288.

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 KLF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARI1A_HUMAN	ARID1A	physical	11018012
SMCA4_HUMAN	SMARCA4	physical	11018012
SMRC2_HUMAN	SMARCC2	physical	11018012
SMRC1_HUMAN	SMARCC1	physical	11018012
SMRD1_HUMAN	SMARCD1	physical	11018012
SMCE1_HUMAN	SMARCE1	physical	11018012
SNF5_HUMAN	SMARCB1	physical	11018012
CSK22_HUMAN	CSNK2A2	physical	9722526
CSK21_HUMAN	CSNK2A1	physical	9722526
FLI1_HUMAN	FLI1	physical	12556498
HDAC1_HUMAN	HDAC1	physical	15542849
SIN3A_HUMAN	SIN3A	physical	15542849
SIN3A_MOUSE	Sin3a	physical	11287616
TF2H1_HUMAN	GTF2H1	physical	21670263
CBP_HUMAN	CREBBP	physical	21670263
EP300_HUMAN	EP300	physical	21670263
UBC_HUMAN	UBC	physical	24139988

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613673	Anemia, congenital dyserythropoietic, 4 (CDAN4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KLF1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15, AND MASSSPECTROMETRY.	19690332 [Abstract]