RTNLH_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RTNLH_ARATH
• UniProt AC: Q9SS37
• Protein Name: Reticulon-like protein B8
• Gene Name: RTNLB8
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 247
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Sequence: MPDKNIVEDVIGDLVDNFTETVQKNKHGSSFFEQEDSVSSRFNRLFDRQKPIHHVLGGGKSADVLLWRNKKISASVLMGATAIWVLFEWINFHFLSLVCYALLLGMIAQFVWSNASGFLNRSQSRVPRLVLPKDFFAEVGVAVGKEVNRGLLFLQDLACKGNLKQFLMAVIGLWVAAMVGSCCNFLTVLYIGFVGAHTMPVLYERYEDEVDGFMDSMIMKFHSHYKKLDTGFLSRIPSGKFGLKKRE

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
29	Phosphorylation	VQKNKHGSSFFEQED HHHCCCCCCCCCCHH	24.56	25561503
30	Phosphorylation	QKNKHGSSFFEQEDS HHCCCCCCCCCCHHH	38.25	25561503
37	Phosphorylation	SFFEQEDSVSSRFNR CCCCCHHHHHHHHHH	24.13	29654922
39	Phosphorylation	FEQEDSVSSRFNRLF CCCHHHHHHHHHHHH	21.54	30407730
40	Phosphorylation	EQEDSVSSRFNRLFD CCHHHHHHHHHHHHC	38.44	25561503
230	Phosphorylation	SHYKKLDTGFLSRIP HHHHHCCCCHHHCCC	40.02	19376835
234	Phosphorylation	KLDTGFLSRIPSGKF HCCCCHHHCCCCCCC	26.38	19376835
238	Phosphorylation	GFLSRIPSGKFGLKK CHHHCCCCCCCCCCC	52.85	19376835

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RTNLH_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 RTNLH_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LCB1_ARATH	LCB1	physical	21798944
PR1B5_ARATH	PRA1.B5	physical	21798944
PR1F4_ARATH	PRA1.F4	physical	21798944
RTNLL_ARATH	AT3G54120	physical	21798944
RTNLH_ARATH	AT3G10260	physical	21798944
RAD2B_ARATH	RAB1A	physical	21798944
CUT1A_ARATH	AT4G01150	physical	21798944
RBL15_ARATH	RBL15	physical	21798944
VAP11_ARATH	VAP	physical	21798944
BET12_ARATH	ATBET12	physical	21798944

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASSSPECTROMETRY.
PubMed: 19376835