PIP27_ARATH - dbPTM
PIP27_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIP27_ARATH
UniProt AC P93004
Protein Name Aquaporin PIP2-7
Gene Name PIP2-7
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 280
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Water channel required to facilitate the transport of water across cell membrane. May be involved in the osmoregulation in plants under high osmotic stress such as under a high salt condition..
Protein Sequence MSKEVSEEGKTHHGKDYVDPPPAPLLDMGELKSWSFYRALIAEFIATLLFLYVTVATVIGHKKQTGPCDGVGLLGIAWAFGGMIFVLVYCTAGISGGHINPAVTFGLFLARKVSLVRALGYMIAQCLGAICGVGFVKAFMKTPYNTLGGGANTVADGYSKGTALGAEIIGTFVLVYTVFSATDPKRSARDSHIPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNNEKAWDDQWIFWVGPFLGALAAAAYHQYILRASAIKALGSFRSNATN
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
1Acetylation-------MSKEVSEE
-------CCHHCCCC
13.41-
2Phosphorylation------MSKEVSEEG
------CCHHCCCCC
37.2125561503
3"N6,N6-dimethyllysine"-----MSKEVSEEGK
-----CCHHCCCCCC
61.92-
3Methylation-----MSKEVSEEGK
-----CCHHCCCCCC
61.92-
6Phosphorylation--MSKEVSEEGKTHH
--CCHHCCCCCCCCC
30.9019880383
11PhosphorylationEVSEEGKTHHGKDYV
HCCCCCCCCCCCCCC
29.9325561503
266PhosphorylationHQYILRASAIKALGS
HHHHHHHHHHHHHHH
24.8819376835
273PhosphorylationSAIKALGSFRSNATN
HHHHHHHHHHHCCCC
20.5230291188
276PhosphorylationKALGSFRSNATN---
HHHHHHHHCCCC---
28.8919880383
279PhosphorylationGSFRSNATN------
HHHHHCCCC------
45.7919880383

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 PIP27_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIP27_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 PIP27_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NAC89_ARATHNAC089physical
21798944
SY121_ARATHSYP121physical
25082856
SYP61_ARATHSYP61physical
25082856
PIP27_ARATHPIP3physical
25082856
TSPO_ARATHTSPOphysical
25538184
PIP15_ARATHPIP1;5physical
24833385
UTR2_ARATHUTR2physical
24833385
HHP2_ARATHHHP2physical
24833385
HHP4_ARATHHHP4physical
24833385
PIP14_ARATHPIP1;4physical
24833385
UBC34_ARATHUBC34physical
24833385
ACBP6_ARATHACBP6physical
24833385
PIP22_ARATHPIP2Bphysical
24833385
ELIP2_ARATHELIP2physical
24833385
HSDD3_ARATHAT2G43420physical
24833385
CP21D_ARATHAT3G66654physical
24833385
BETL2_ARATHAT1G29060physical
24833385
VAP21_ARATHAT5G47180physical
24833385

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIP27_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-273; SER-276 ANDTHR-279, AND MASS SPECTROMETRY.
"Novel subsets of the Arabidopsis plasmalemma phosphoproteome identifyphosphorylation sites in secondary active transporters.";
Hem S., Rofidal V., Sommerer N., Rossignol M.;
Biochem. Biophys. Res. Commun. 363:375-380(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-276 ANDTHR-279, AND MASS SPECTROMETRY.
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Plant Cell 16:2394-2405(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND MASSSPECTROMETRY.

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