LCBK1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LCBK1_ARATH
• UniProt AC: Q9LRB0
• Protein Name: Sphingoid long-chain bases kinase 1
• Gene Name: LCBK1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 763
• Protein Description: Involved in the production of sphingolipid metabolites. Active on sphingosine, phytosphingosine (PHS, 4-hydroxysphinganine), D-erythro-dihydrosphingosine, D-erythro-sphingosine and trans-4, trans-8-sphingadienine, an LCB found exclusively in plants, but not on N-acetyl-dihydrosphingosine (C2-dihydroceramide) and D-threo-dihydrosphingosine..
• Protein Sequence: MQKSGVNRNPSLKVAIPQAQQSLRRLGFCSQIATGGSQQSSPIVFPEKRNKKVKASSRRGEVTNDPQVKPKPDEHRIDIGGGDEKSDLLGSLVYAGKLVLDKRKSASGKDATEIQQPAATDISIKKAVDAKLTSSALVWGSDMLQLNDVVSVTYNVGLRHFTVHAYPIGKGSCGLSCFTKPKRSRKDFRFVAPTVEEAVQWVASFGDQQCFINCLPHPLVAKKQASSELFSVPIDTPPELVFRCKSAPKMLVILNPRSGHGRSIKVFHNVVEPIFKLAGIKMEVVKTTKAGHARELASTVDINLCSDGIICVGGDGIINEVLNGLLTRSNPKEGVSIPIGIVPAGSDNSLVWTVLGVRDPISAALSIVKGGLTATDVFAVEWIHTGIIHFGMTVSYYGFVSDVLELSEKYQKRFGPLRYFVAGFLKFMCLPKYSYEVEYLPAQKEDAEGKIRLEKEAVDMQDLYTDVMRRSSREGFPRASSLSSIDSIMTPSVGELDTCSSTHASTEPSEYVRGIDPKMKRLSSGRRDVTAEPEVIHPQAQSTTPNWPRTRSKSRMDKGWMGLTSVQDPPTRCSWGNTGGQDREDISSTVSDPGPIWDAGPKWDTEPSAWDVENSIELPGPPEDIETGLRKQSITPIFEDKWVSRKGHFLGIMVCNHACRTVQSSQVVAPNSEHDDGTMDMLLVHGCGRLRLLRFFILLQTGRHLSLPYVECVKVKSVKIKAGKNTHDSCGIDGELFALHGEVISTMLPEQCRLIGNAPGRHS

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
22	Phosphorylation	AIPQAQQSLRRLGFC HHHHHHHHHHHCCCC	16.26	23111157
34	Phosphorylation	GFCSQIATGGSQQSS CCCCCCCCCCCCCCC	43.64	17317660
41	Phosphorylation	TGGSQQSSPIVFPEK CCCCCCCCCCCCCHH	17.82	17317660
86	Phosphorylation	IGGGDEKSDLLGSLV CCCCCCHHHHHHHHH	31.29	17317660
226	Phosphorylation	LVAKKQASSELFSVP HHCCCCCCCCCCCCC	23.11	17317660
227	Phosphorylation	VAKKQASSELFSVPI HCCCCCCCCCCCCCC	41.14	17317660
231	Phosphorylation	QASSELFSVPIDTPP CCCCCCCCCCCCCCH	39.34	26811356
471	Phosphorylation	YTDVMRRSSREGFPR HHHHHHHHHCCCCCC	24.31	25561503
472	Phosphorylation	TDVMRRSSREGFPRA HHHHHHHHCCCCCCC	32.32	25561503
543	Phosphorylation	IHPQAQSTTPNWPRT ECCCCCCCCCCCCCC	33.90	30589143
591	Phosphorylation	EDISSTVSDPGPIWD HHHHHCCCCCCCCCC	37.87	17317660
633	Phosphorylation	ETGLRKQSITPIFED HCCCHHCCCCHHHCC	31.31	19880383
635	Phosphorylation	GLRKQSITPIFEDKW CCHHCCCCHHHCCCC	18.64	19880383
726	Phosphorylation	KIKAGKNTHDSCGID EEECCCCCCCCCCCC	30.46	23776212
729	Phosphorylation	AGKNTHDSCGIDGEL CCCCCCCCCCCCHHH	13.46	23776212
745	Phosphorylation	ALHGEVISTMLPEQC HCCCHHHHHHCHHHH	16.97	23776212
746	Phosphorylation	LHGEVISTMLPEQCR CCCHHHHHHCHHHHH	16.17	23776212

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

Oops, there are no upstream regulatory protein records of LCBK1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LCBK1_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 LCBK1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis.";
Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.;
Mol. Cell. Proteomics 6:1198-1214(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.
PubMed: 17317660