PLAG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PLAG1_HUMAN
• UniProt AC: Q6DJT9
• Protein Name: Zinc finger protein PLAG1
• Gene Name: PLAG1
• Organism: Homo sapiens (Human).
• Sequence Length: 500
• Subcellular Localization: Nucleus . Strong nucleolar localization when sumoylation is inhibited.
• Protein Description: Transcription factor whose activation results in up-regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation: when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Overexpression is associated with up-regulation of IGFII, is frequently observed in hepatoblastoma, common primary liver tumor in childhood. Cooperates with CBFB-MYH11, a fusion gene important for myeloid leukemia..
• Protein Sequence: MATVIPGDLSEVRDTQKVPSGKRKRGETKPRKNFPCQLCDKAFNSVEKLKVHSYSHTGERPYKCIQQDCTKAFVSKYKLQRHMATHSPEKTHKCNYCEKMFHRKDHLKNHLHTHDPNKETFKCEECGKNYNTKLGFKRHLALHAATSGDLTCKVCLQTFESTGVLLEHLKSHAGKSSGGVKEKKHQCEHCDRRFYTRKDVRRHMVVHTGRKDFLCQYCAQRFGRKDHLTRHMKKSHNQELLKVKTEPVDFLDPFTCNVSVPIKDELLPVMSLPSSELLSKPFTNTLQLNLYNTPFQSMQSSGSAHQMITTLPLGMTCPIDMDTVHPSHHLSFKYPFSSTSYAISIPEKEQPLKGEIESYLMELQGGVPSSSQDSQASSSSKLGLDPQIGSLDDGAGDLSLSKSSISISDPLNTPALDFSQLFNFIPLNGPPYNPLSVGSLGMSYSQEEAHSSVSQLPPQTQDLQDPANTIGLGSLHSLSAAFTSSLSTSTTLPRFHQAFQ

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
28	Phosphorylation	GKRKRGETKPRKNFP CCCCCCCCCCCCCCC	49.53	-
55	Phosphorylation	KLKVHSYSHTGERPY EECEEECCCCCCCCC	20.00	24719451
57	Phosphorylation	KVHSYSHTGERPYKC CEEECCCCCCCCCHH	34.49	27251275
85	Phosphorylation	KLQRHMATHSPEKTH HHHHHHCCCCCCCCC	18.47	-
87	Phosphorylation	QRHMATHSPEKTHKC HHHHCCCCCCCCCCC	30.33	-
91	Phosphorylation	ATHSPEKTHKCNYCE CCCCCCCCCCCCHHH	25.55	-
208	Phosphorylation	RRHMVVHTGRKDFLC HHHEEEECCCHHHHH	27.37	-
235	Phosphorylation	LTRHMKKSHNQELLK HHHHHHHHHCHHHHE	23.35	29457462
244	Sumoylation	NQELLKVKTEPVDFL CHHHHEECCCCCCCC	45.65	-
244	Sumoylation	NQELLKVKTEPVDFL CHHHHEECCCCCCCC	45.65	-
263	Sumoylation	CNVSVPIKDELLPVM CEEECCCCCCCCCCC	38.80	-
263	Sumoylation	CNVSVPIKDELLPVM CEEECCCCCCCCCCC	38.80	-
331	Phosphorylation	VHPSHHLSFKYPFSS CCCCCCEEEECCCCC	18.48	24719451
334	Phosphorylation	SHHLSFKYPFSSTSY CCCEEEECCCCCCEE	13.90	23663014
337	Phosphorylation	LSFKYPFSSTSYAIS EEEECCCCCCEEEEE	28.36	23663014
338	Phosphorylation	SFKYPFSSTSYAISI EEECCCCCCEEEEEC	23.04	23663014
339	Phosphorylation	FKYPFSSTSYAISIP EECCCCCCEEEEECC	25.26	23663014
340	Phosphorylation	KYPFSSTSYAISIPE ECCCCCCEEEEECCC	17.95	23663014
341	Phosphorylation	YPFSSTSYAISIPEK CCCCCCEEEEECCCC	14.19	23663014
344	Phosphorylation	SSTSYAISIPEKEQP CCCEEEEECCCCCCC	24.74	23663014
353	Sumoylation	PEKEQPLKGEIESYL CCCCCCCCHHHHHHH	62.27	-
353	Sumoylation	PEKEQPLKGEIESYL CCCCCCCCHHHHHHH	62.27	-
399	Phosphorylation	DDGAGDLSLSKSSIS CCCCCCCCCCCCCEE	35.02	24719451
401	Phosphorylation	GAGDLSLSKSSISIS CCCCCCCCCCCEECC	27.41	25627689

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PLAG1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PLAG1_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 PLAG1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PLAG1_HUMAN !!

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.