TMKL1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TMKL1_ARATH
• UniProt AC: P33543
• Protein Name: Putative kinase-like protein TMKL1
• Gene Name: TMKL1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 674
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Does not seem to have conserved a kinase activity..
• Protein Sequence: MGMEALRFLHVIFFFVLILHCHCGTSLSGSSDVKLLLGKIKSSLQGNSESLLLSSWNSSVPVCQWRGVKWVFSNGSPLQCSDLSSPQWTNTSLFNDSSLHLLSLQLPSANLTGSLPREIGEFSMLQSVFLNINSLSGSIPLELGYTSSLSDVDLSGNALAGVLPPSIWNLCDKLVSFKIHGNNLSGVLPEPALPNSTCGNLQVLDLGGNKFSGEFPEFITRFKGVKSLDLSSNVFEGLVPEGLGVLELESLNLSHNNFSGMLPDFGESKFGAESFEGNSPSLCGLPLKPCLGSSRLSPGAVAGLVIGLMSGAVVVASLLIGYLQNKKRKSSIESEDDLEEGDEEDEIGEKEGGEGKLVVFQGGENLTLDDVLNATGQVMEKTSYGTVYKAKLSDGGNIALRLLREGTCKDRSSCLPVIRQLGRIRHENLVPLRAFYQGKRGEKLLIYDYLPNISLHDLLHESKPRKPALNWARRHKIALGIARGLAYLHTGQEVPIIHGNIRSKNVLVDDFFFARLTEFGLDKIMVQAVADEIVSQAKSDGYKAPELHKMKKCNPRSDVYAFGILLLEILMGKKPGKSGRNGNEFVDLPSLVKAAVLEETTMEVFDLEAMKGIRSPMEEGLVHALKLAMGCCAPVTTVRPSMEEVVKQLEENRPRNRSALYSPTETRSDAETPF

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	N-linked_Glycosylation	SLLLSSWNSSVPVCQ HEEEHHCCCCCCCEE	26.76	-
90	N-linked_Glycosylation	LSSPQWTNTSLFNDS CCCCCCCCCCCCCCC	25.39	-
95	N-linked_Glycosylation	WTNTSLFNDSSLHLL CCCCCCCCCCHHEEE	54.25	-
110	N-linked_Glycosylation	SLQLPSANLTGSLPR EEECCCCCCCCCCCH	42.34	-
183	N-linked_Glycosylation	SFKIHGNNLSGVLPE EEEEECCCCCCCCCC	39.93	-
195	N-linked_Glycosylation	LPEPALPNSTCGNLQ CCCCCCCCCCCCCEE	51.29	-
252	N-linked_Glycosylation	VLELESLNLSHNNFS EEEEEECCCCCCCCC	49.10	-
257	N-linked_Glycosylation	SLNLSHNNFSGMLPD ECCCCCCCCCCCCCC	27.34	-
330	Phosphorylation	LQNKKRKSSIESEDD HHCCCCCCCCCCHHH	40.35	17317660
331	Phosphorylation	QNKKRKSSIESEDDL HCCCCCCCCCCHHHH	33.15	17317660
334	Phosphorylation	KRKSSIESEDDLEEG CCCCCCCCHHHHHCC	44.66	30291188
375	Phosphorylation	LDDVLNATGQVMEKT HHHHHHHHCCEEEEC	27.37	-
407	Phosphorylation	LRLLREGTCKDRSSC HHHHHHCCCCCHHHH	16.19	22074104
454	Phosphorylation	YDYLPNISLHDLLHE EEECCCCCHHHHHHC	26.71	-
658	Phosphorylation	ENRPRNRSALYSPTE HCCCCCCCCCCCCCC	26.61	30407730
661	Phosphorylation	PRNRSALYSPTETRS CCCCCCCCCCCCCCC	16.60	25561503
662	Phosphorylation	RNRSALYSPTETRSD CCCCCCCCCCCCCCC	26.62	30407730
664	Phosphorylation	RSALYSPTETRSDAE CCCCCCCCCCCCCCC	44.01	25561503
666	Phosphorylation	ALYSPTETRSDAETP CCCCCCCCCCCCCCC	37.64	30407730
668	Phosphorylation	YSPTETRSDAETPF- CCCCCCCCCCCCCC-	48.90	17317660
672	Phosphorylation	ETRSDAETPF----- CCCCCCCCCC-----	31.54	30407730

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

Oops, there are no upstream regulatory protein records of TMKL1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TMKL1_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TMKL1_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of TMKL1_ARATH !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASSSPECTROMETRY.
PubMed: 19245862