RTNLA_ARATH - dbPTM
RTNLA_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTNLA_ARATH
UniProt AC Q9SUR3
Protein Name Reticulon-like protein B1
Gene Name RTNLB1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 275
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Cell membrane
Multi-pass membrane protein .
Protein Description Plays a role in the Agrobacterium-mediated plant transformation via its interaction with VirB2, the major component of the T-pilus..
Protein Sequence MAEEHKHDESVIAPEPAVEVVERESLMDKISEKIHHGGDSSSSSSSSDDEDEKKKTKKPSSPSSSMKSKVYRLFGREQPVHKVLGGGKPADIFMWKNKKMSGGVLGGATAAWVVFELMEYHLLTLLCHVMIVVLAVLFLWSNATMFINKSPPKIPEVHIPEEPILQLASGLRIEINRGFSSLREIASGRDLKKFLIAIAGLWVLSILGGCFNFLTLAYIALVLLFTVPLAYDKYEDKVDPLGEKAMIELKKQYAVLDEKVLSKIPLGPLKNKKKD
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 Orthologous
Protein Cluster
2Acetylation------MAEEHKHDE
------CCCCCCCCC
30.77-
6Acetylation--MAEEHKHDESVIA
--CCCCCCCCCCCCC
56.9121311031
10PhosphorylationEEHKHDESVIAPEPA
CCCCCCCCCCCCCCC
25.5325368622
31PhosphorylationESLMDKISEKIHHGG
HHHHHHHHHHHCCCC
38.2830291188
40PhosphorylationKIHHGGDSSSSSSSS
HHCCCCCCCCCCCCC
35.0819376835
41PhosphorylationIHHGGDSSSSSSSSD
HCCCCCCCCCCCCCC
38.6919376835
42PhosphorylationHHGGDSSSSSSSSDD
CCCCCCCCCCCCCCC
37.8919376835
43PhosphorylationHGGDSSSSSSSSDDE
CCCCCCCCCCCCCCH
35.8719376835
44PhosphorylationGGDSSSSSSSSDDED
CCCCCCCCCCCCCHH
35.8727531888
45PhosphorylationGDSSSSSSSSDDEDE
CCCCCCCCCCCCHHH
35.4919376835
46PhosphorylationDSSSSSSSSDDEDEK
CCCCCCCCCCCHHHH
39.4727531888
47PhosphorylationSSSSSSSSDDEDEKK
CCCCCCCCCCHHHHH
51.5319376835
56PhosphorylationDEDEKKKTKKPSSPS
CHHHHHHCCCCCCCC
53.8619376835
60PhosphorylationKKKTKKPSSPSSSMK
HHHCCCCCCCCHHHH
64.8523776212
61PhosphorylationKKTKKPSSPSSSMKS
HHCCCCCCCCHHHHH
37.0119880383
63PhosphorylationTKKPSSPSSSMKSKV
CCCCCCCCHHHHHHH
36.6723776212
64PhosphorylationKKPSSPSSSMKSKVY
CCCCCCCHHHHHHHH
37.5223776212
65PhosphorylationKPSSPSSSMKSKVYR
CCCCCCHHHHHHHHH
34.2723776212

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

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

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

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

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RTNLB_ARATHBTI2physical
15494553
RTNLD_ARATHBTI3physical
15494553
RAE1A_ARATHRAB8physical
15494553
RTNLA_ARATHBTI1physical
15494553
RTNLA_ARATHBTI1physical
20424177
RTNLC_ARATHRTNLB3physical
20424177
RTNLD_ARATHBTI3physical
20424177
FLS2_ARATHFLS2physical
21949153

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RTNLA_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-61, AND MASSSPECTROMETRY.

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