PIN7_ARATH - dbPTM
PIN7_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIN7_ARATH
UniProt AC Q940Y5
Protein Name Auxin efflux carrier component 7 {ECO:0000303|PubMed:14614497}
Gene Name PIN7 {ECO:0000303|PubMed:14614497}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 619
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Acts as a component of the auxin efflux carrier. [PubMed: 14614497]
Protein Sequence MITWHDLYTVLTAVIPLYVAMILAYGSVRWWKIFSPDQCSGINRFVAIFAVPLLSFHFISSNNPYAMNLRFIAADTLQKLIMLTLLIIWANFTRSGSLEWSITIFSLSTLPNTLVMGIPLLIAMYGEYSGSLMVQIVVLQCIIWYTLLLFLFEYRGAKILIMEQFPETGASIVSFKVESDVVSLDGHDFLETDAQIGDDGKLHVTVRKSNASRRSFYGGGGTNMTPRPSNLTGAEIYSLNTTPRGSNFNHSDFYSMMGFPGGRLSNFGPADMYSVQSSRGPTPRPSNFEESCAMASSPRFGYYPGGAPGSYPAPNPEFSTGNKTGSKAPKENHHHVGKSNSNDAKELHMFVWGSNGSPVSDRAGLQVDNGANEQVGKSDQGGAKEIRMLISDHTQNGENKAGPMNGDYGGEEESERVKEVPNGLHKLRCNSTAELNPKEAIETGETVPVKHMPPASVMTRLILIMVWRKLIRNPNTYSSLIGLIWALVAFRWDVAMPKIIQQSISILSDAGLGMAMFSLGLFMALQPKLIACGNSTATFAMAVRFFTGPAVMAVAAMAIGLRGDLLRVAIVQAALPQGIVPFVFAKEYNVHPAILSTGVIFGMLIALPITLVYYILLGL
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
215PhosphorylationKSNASRRSFYGGGGT
CCCCCCCCCCCCCCC		23.0125561503
217PhosphorylationNASRRSFYGGGGTNM
CCCCCCCCCCCCCCC		18.9925561503
225PhosphorylationGGGGTNMTPRPSNLT
CCCCCCCCCCCCCCC		20.4429654922
229PhosphorylationTNMTPRPSNLTGAEI
CCCCCCCCCCCCCEE		45.8325561503
230N-linked_GlycosylationNMTPRPSNLTGAEIY
CCCCCCCCCCCCEEE		44.28-
232PhosphorylationTPRPSNLTGAEIYSL
CCCCCCCCCCEEEEC		38.3019376835
237PhosphorylationNLTGAEIYSLNTTPR
CCCCCEEEECCCCCC		9.9025561503
238PhosphorylationLTGAEIYSLNTTPRG
CCCCEEEECCCCCCC		22.3230407730
241PhosphorylationAEIYSLNTTPRGSNF
CEEEECCCCCCCCCC		43.3929654922
242PhosphorylationEIYSLNTTPRGSNFN
EEEECCCCCCCCCCC		15.2030407730
246PhosphorylationLNTTPRGSNFNHSDF
CCCCCCCCCCCHHHH		39.26-
249N-linked_GlycosylationTPRGSNFNHSDFYSM
CCCCCCCCHHHHHHC		37.69-
265PhosphorylationGFPGGRLSNFGPADM
CCCCCCCCCCCCCHH		28.8425561503
277PhosphorylationADMYSVQSSRGPTPR
CHHCCCCCCCCCCCC		21.6117317660
278PhosphorylationDMYSVQSSRGPTPRP
HHCCCCCCCCCCCCC		24.9425561503
282PhosphorylationVQSSRGPTPRPSNFE
CCCCCCCCCCCCCHH		34.4519376835
286PhosphorylationRGPTPRPSNFEESCA
CCCCCCCCCHHHHHH		56.2719376835
291PhosphorylationRPSNFEESCAMASSP
CCCCHHHHHHCCCCC		10.4419376835
296PhosphorylationEESCAMASSPRFGYY
HHHHHCCCCCCCCCC		27.9923111157
297PhosphorylationESCAMASSPRFGYYP
HHHHCCCCCCCCCCC		15.5727532006
320PhosphorylationAPNPEFSTGNKTGSK
CCCCCCCCCCCCCCC		50.52-
354PhosphorylationLHMFVWGSNGSPVSD
EEEEEECCCCCCCHH		23.4726811356
357PhosphorylationFVWGSNGSPVSDRAG
EEECCCCCCCHHHCC		26.7826811356
360PhosphorylationGSNGSPVSDRAGLQV
CCCCCCCHHHCCCEE		25.4327643528
431PhosphorylationLHKLRCNSTAELNPK
CEEECCCCCCCCCHH		32.4019880383
432PhosphorylationHKLRCNSTAELNPKE
EEECCCCCCCCCHHH		15.3419880383
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 PIN7_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIN7_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 PIN7_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HHP2_ARATHHHP2physical
24833385
HHP4_ARATHHHP4physical
24833385
UBC34_ARATHUBC34physical
24833385
CP21D_ARATHAT3G66654physical
24833385
BET12_ARATHATBET12physical
24833385
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIN7_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-297, AND MASSSPECTROMETRY.

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