MKL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MKL1_HUMAN
• UniProt AC: Q969V6
• Protein Name: MKL/myocardin-like protein 1
• Gene Name: MKL1
• Organism: Homo sapiens (Human).
• Sequence Length: 931
• Subcellular Localization: Nucleus . Cytoplasm. Binding to globular actin is required to maintain cytoplasmic localization. Nuclear localization is regulated by MICAL2, which mediates depolymerization of nuclear globular actin, promoting retention of MKL1 in the nucleus and su
• Protein Description: Transcriptional coactivator of serum response factor (SRF) with the potential to modulate SRF target genes. Suppresses TNF-induced cell death by inhibiting activation of caspases; its transcriptional activity is indispensable for the antiapoptotic function. It may up-regulate antiapoptotic molecules, which in turn inhibit caspase activation (By similarity)..
• Protein Sequence: MPPLKSPAAFHEQRRSLERARTEDYLKRKIRSRPERSELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILPVESSLKEAIIVGQVNYPKVADSSSFDEDSSDALSPEQPASHESQGSVPSPLEARVSEPLLSATSASPTQVVSQLPMGRDSREMLFLAEQPPLPPPPLLPPSLTNGTTIPTAKSTPTLIKQSQPKSASEKSQRSKKAKELKPKVKKLKYHQYIPPDQKQDRGAPPMDSSYAKILQQQQLFLQLQILNQQQQQHHNYQAILPAPPKSAGEALGSSGTPPVRSLSTTNSSSSSGAPGPCGLARQNSTSLTGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQISPVPGAPKAPAATSILHKAGEVVVAFPAARLSTGPALVAAGLAPAEVVVATVASSGVVKFGSTGSTPPVSPTPSERSLLSTGDENSTPGDTFGEMVTSPLTQLTLQASPLQILVKEEGPRAGSCCLSPGGRAELEGRDKDQMLQEKDKQIEALTRMLRQKQQLVERLKLQLEQEKRAQQPAPAPAPLGTPVKQENSFSSCQLSQQPLGPAHPFNPSLAAPATNHIDPCAVAPGPPSVVVKQEALQPEPEPVPAPQLLLGPQGPSLIKGVAPPTLITDSTGTHLVLTVTNKNADSPGLSSGSPQQPSSQPGSPAPAPSAQMDLEHPLQPLFGTPTSLLKKEPPGYEEAMSQQPKQQENGSSSQQMDDLFDILIQSGEISADFKEPPSLPGKEKPSPKTVCGSPLAAQPSPSAELPQAAPPPPGSPSLPGRLEDFLESSTGLPLLTSGHDGPEPLSLIDDLHSQMLSSTAILDHPPSPMDTSELHFVPEPSSTMGLDLADGHLDSMDWLELSSGGPVLSLAPLSTTAPSLFSTDFLDGHDLQLHWDSCL

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
57	Acetylation	AEPSLQAKQLKLKRA CCCCHHHHHHHHHHH	43.11	23236377
351	Methylation	PANLDDMKVAELKQE CCCHHHCCHHHHHHH	45.33	-

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
312	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
312	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
333	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
333	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
454	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
454	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
573	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MKL1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MKL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRF_HUMAN	SRF	physical	14565952
MKL2_HUMAN	MKL2	physical	14565952
SP16H_HUMAN	SUPT16H	physical	18036521
SSRP1_HUMAN	SSRP1	physical	18036521
KDM3A_HUMAN	KDM3A	physical	17991879
SRF_HUMAN	SRF	physical	17599918
SMCA4_HUMAN	SMARCA4	physical	17599918
SRF_HUMAN	SRF	physical	21965288
GSK3B_HUMAN	GSK3B	physical	21965288
SMAD3_HUMAN	SMAD3	physical	21965288
ACTB_HUMAN	ACTB	physical	21670154
EP300_HUMAN	EP300	physical	26476216

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

Phosphorylation

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450 AND SER-454, ANDMASS SPECTROMETRY.
PubMed: 19413330

"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 THR-305; THR-450 ANDSER-454, AND MASS SPECTROMETRY.
PubMed: 18669648

"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-6, AND MASSSPECTROMETRY.
PubMed: 17081983