PIN4_ARATH - dbPTM
PIN4_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIN4_ARATH
UniProt AC Q8RWZ6
Protein Name Auxin efflux carrier component 4 {ECO:0000303|PubMed:11893337}
Gene Name PIN4 {ECO:0000303|PubMed:11893337}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 616
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Acts as a component of the auxin efflux carrier. Plays a role in generating a sink for auxin into columella cells. Maintains the endogenous auxin gradient, which is essential for correct root patterning..
Protein Sequence MITWHDLYTVLTAVVPLYVAMILAYGSVQWWKIFSPDQCSGINRFVAIFAVPLLSFHFISTNDPYAMNFRFVAADTLQKIIMLVLLALWANLTKNGSLEWMITIFSLSTLPNTLVMGIPLLIAMYGTYAGSLMVQVVVLQCIIWYTLLLFLFEYRGAKLLIMEQFPETGASIVSFKVESDVVSLDGHDFLETDAEIGNDGKLHVTVRKSNASRRSLMMTPRPSNLTGAEIYSLSSTPRGSNFNHSDFYSVMGFPGGRLSNFGPADLYSVQSSRGPTPRPSNFEENNAVKYGFYNNTNSSVPAAGSYPAPNPEFSTGTGVSTKPNKIPKENQQQLQEKDSKASHDAKELHMFVWSSSASPVSDVFGGGAGDNVATEQSEQGAKEIRMVVSDQPRKSNARGGGDDIGGLDSGEGEREIEKATAGLNKMGSNSTAELEAAGGDGGGNNGTHMPPTSVMTRLILIMVWRKLIRNPNTYSSLIGLIWALVAYRWHVAMPKILQQSISILSDAGLGMAMFSLGLFMALQPKIIACGNSVATFAMAVRFITGPAIMAVAGIAIGLHGDLLRIAIVQAALPQGIVPFVFAKEYNVHPTILSTGVIFGMLIALPITLVYYILLGL
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
174PhosphorylationETGASIVSFKVESDV
CCCCEEEEEEEECCE		20.0619880383
179PhosphorylationIVSFKVESDVVSLDG
EEEEEEECCEEEECC		38.4023110452
183PhosphorylationKVESDVVSLDGHDFL
EEECCEEEECCCCEE		22.1617317660
215PhosphorylationKSNASRRSLMMTPRP
CCCCCCCEEECCCCC		21.3624243849
219PhosphorylationSRRSLMMTPRPSNLT
CCCEEECCCCCCCCC		11.3724243849
223PhosphorylationLMMTPRPSNLTGAEI
EECCCCCCCCCCCEE		45.8324243849
224N-linked_GlycosylationMMTPRPSNLTGAEIY
ECCCCCCCCCCCEEE		44.28-
226PhosphorylationTPRPSNLTGAEIYSL
CCCCCCCCCCEEEEC		38.3019376835
231PhosphorylationNLTGAEIYSLSSTPR
CCCCCEEEECCCCCC		8.6119376835
232PhosphorylationLTGAEIYSLSSTPRG
CCCCEEEECCCCCCC		27.6919376835
234PhosphorylationGAEIYSLSSTPRGSN
CCEEEECCCCCCCCC		26.6519376835
235PhosphorylationAEIYSLSSTPRGSNF
CEEEECCCCCCCCCC		47.9619376835
236PhosphorylationEIYSLSSTPRGSNFN
EEEECCCCCCCCCCC		17.4019376835
240PhosphorylationLSSTPRGSNFNHSDF
CCCCCCCCCCCHHHH		39.26-
243N-linked_GlycosylationTPRGSNFNHSDFYSV
CCCCCCCCHHHHHHC		37.69-
259PhosphorylationGFPGGRLSNFGPADL
CCCCCCCCCCCCHHH		28.8425561503
267PhosphorylationNFGPADLYSVQSSRG
CCCCHHHCCCCCCCC		13.8225561503
268PhosphorylationFGPADLYSVQSSRGP
CCCHHHCCCCCCCCC		22.4525561503
271PhosphorylationADLYSVQSSRGPTPR
HHHCCCCCCCCCCCC		21.6125561503
272PhosphorylationDLYSVQSSRGPTPRP
HHCCCCCCCCCCCCC		24.9425561503
276PhosphorylationVQSSRGPTPRPSNFE
CCCCCCCCCCCCCCC		34.4530291188
280PhosphorylationRGPTPRPSNFEENNA
CCCCCCCCCCCCCCC		56.2730291188
358PhosphorylationFVWSSSASPVSDVFG
HHHCCCCCCHHHCCC		27.99-
389 (in isoform 2)Phosphorylation-21.0819880383
395PhosphorylationVSDQPRKSNARGGGD
ECCCCCCCCCCCCCC		36.6819376835
395 (in isoform 2)Phosphorylation-36.6830291188
409PhosphorylationDDIGGLDSGEGEREI
CCCCCCCCCCCHHHH		43.7330291188
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 PIN4_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIN4_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 PIN4_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FYPP1_ARATHAT1G50370physical
22715043
FYPP3_ARATHFYPP3physical
22715043
UTR2_ARATHUTR2physical
24833385
HHP4_ARATHHHP4physical
24833385
HHP2_ARATHHHP2physical
24833385
IRX10_ARATHGUT2physical
24833385
ATL4_ARATHATL4physical
24833385
UBC34_ARATHUBC34physical
24833385
NPC3_ARATHNPC3physical
24833385
KSG4_ARATHSK42physical
24833385
PIP13_ARATHPIP1Cphysical
24833385
CCX5_ARATHCAX11physical
24833385
FACE2_ARATHFACE2physical
24833385
CDPK3_ARATHCDPK6physical
24833385
ELIP2_ARATHELIP2physical
24833385
PRS4A_ARATHRPT2aphysical
24833385
WAXS1_ARATHAT5G55380physical
24833385
AGP27_ARATHAGP27physical
24833385
BOR5_ARATHBOR5physical
24833385
CALX2_ARATHAT5G07340physical
24833385
AB12I_ARATHAT3G21580physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
CDPKR_ARATHCPK27physical
24833385
TMN2_ARATHAT1G14670physical
24833385
DTX44_ARATHAT2G38330physical
24833385
CP21D_ARATHAT3G66654physical
24833385
PAM74_ARATHAT5G59650physical
24833385
RAC8_ARATHROP10physical
24833385
BETL2_ARATHAT1G29060physical
24833385
BET12_ARATHATBET12physical
24833385
GAE5_ARATHGAE5physical
24833385
MMGT_ARATHAT5G03345physical
24833385
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIN4_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-395, AND MASSSPECTROMETRY.

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