dbPTM

PINI_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PINI_ARATH
UniProt AC	Q9C6B8
Protein Name	Auxin efflux carrier component 1 {ECO:0000303\|PubMed:9856939}
Gene Name	PIN1 {ECO:0000303\|PubMed:9856939}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	622
Subcellular Localization	Cell membrane Multi-pass membrane protein .
Protein Description	Acts as a component of the auxin efflux carrier. Seems to be involved in the basipetal auxin transport. Mediates the formation of auxin gradient which is required to ensure correct organogenesis. Coordinated polar localization of PIN1 is directly regulated by the vesicle trafficking process and apical-basal PIN1 polarity also depends on the phosphorylation of conserved serine residues by PID kinase. The ARF-GEF protein GNOM is required for the correct recycling of PIN1 between the plasma membrane and endosomal compartments..
Protein Sequence	MITAADFYHVMTAMVPLYVAMILAYGSVKWWKIFTPDQCSGINRFVALFAVPLLSFHFIAANNPYAMNLRFLAADSLQKVIVLSLLFLWCKLSRNGSLDWTITLFSLSTLPNTLVMGIPLLKGMYGNFSGDLMVQIVVLQCIIWYTLMLFLFEYRGAKLLISEQFPDTAGSIVSIHVDSDIMSLDGRQPLETEAEIKEDGKLHVTVRRSNASRSDIYSRRSQGLSATPRPSNLTNAEIYSLQSSRNPTPRGSSFNHTDFYSMMASGGGRNSNFGPGEAVFGSKGPTPRPSNYEEDGGPAKPTAAGTAAGAGRFHYQSGGSGGGGGAHYPAPNPGMFSPNTGGGGGTAAKGNAPVVGGKRQDGNGRDLHMFVWSSSASPVSDVFGGGGGNHHADYSTATNDHQKDVKISVPQGNSNDNQYVEREEFSFGNKDDDSKVLATDGGNNISNKTTQAKVMPPTSVMTRLILIMVWRKLIRNPNSYSSLFGITWSLISFKWNIEMPALIAKSISILSDAGLGMAMFSLGLFMALNPRIIACGNRRAAFAAAMRFVVGPAVMLVASYAVGLRGVLLHVAIIQAALPQGIVPFVFAKEYNVHPDILSTAVIFGMLIALPITLLYYILLGL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
212	Phosphorylation	TVRRSNASRSDIYSR EEECCCCCHHHHHCC	36.25	29654922
214	Phosphorylation	RRSNASRSDIYSRRS ECCCCCHHHHHCCHH	26.35	29654922
218	Phosphorylation	ASRSDIYSRRSQGLS CCHHHHHCCHHCCCC	22.88	29654922
221	Phosphorylation	SDIYSRRSQGLSATP HHHHCCHHCCCCCCC	27.73	29654922
227	Phosphorylation	RSQGLSATPRPSNLT HHCCCCCCCCCCCCC	19.22	17317660
231	Phosphorylation	LSATPRPSNLTNAEI CCCCCCCCCCCCCEE	45.83	20407025
232	N-linked_Glycosylation	SATPRPSNLTNAEIY CCCCCCCCCCCCEEE	54.27	-
252	Phosphorylation	RNPTPRGSSFNHTDF CCCCCCCCCCCHHHH	32.79	19880383
253	Phosphorylation	NPTPRGSSFNHTDFY CCCCCCCCCCHHHHH	32.65	27531888
255	N-linked_Glycosylation	TPRGSSFNHTDFYSM CCCCCCCCHHHHHHH	38.81	-
257	Phosphorylation	RGSSFNHTDFYSMMA CCCCCCHHHHHHHHC	28.98	19880383
271	Phosphorylation	ASGGGRNSNFGPGEA CCCCCCCCCCCCCCC	31.98	17317660
282	Phosphorylation	PGEAVFGSKGPTPRP CCCCCCCCCCCCCCC	23.99	20374526
286	Phosphorylation	VFGSKGPTPRPSNYE CCCCCCCCCCCCCCC	40.37	25561503
290	Phosphorylation	KGPTPRPSNYEEDGG CCCCCCCCCCCCCCC	54.01	17317660
337	Phosphorylation	APNPGMFSPNTGGGG CCCCCCCCCCCCCCC	14.35	17317660
340	Phosphorylation	PGMFSPNTGGGGGTA CCCCCCCCCCCCCCC	40.36	20080776
377	Phosphorylation	FVWSSSASPVSDVFG EEEECCCCCHHHHCC	27.99	-
414	Phosphorylation	ISVPQGNSNDNQYVE EECCCCCCCCCCCEE	53.00	30291188
426	Phosphorylation	YVEREEFSFGNKDDD CEEEEEECCCCCCCC	35.21	25561503

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 PINI_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PINI_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 PINI_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DRP1A_ARATH	DL1	physical	21658946
FYPP1_ARATH	AT1G50370	physical	22715043
FYPP3_ARATH	FYPP3	physical	22715043
2AAA_ARATH	RCN1	physical	22715043
DPNP1_ARATH	SAL1	physical	22715043
PP14_ARATH	TOPP4	physical	25560878
SRF8_ARATH	SRF8	physical	24833385
AB19B_ARATH	ABCB19	physical	17237354

Drug and Disease Associations

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

Regulatory Network of PINI_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"PIN phosphorylation is sufficient to mediate PIN polarity and directauxin transport."; Zhang J., Nodzynski T., Pencik A., Rolcik J., Friml J.; Proc. Natl. Acad. Sci. U.S.A. 107:918-922(2010). Cited for: PHOSPHORYLATION AT SER-337 AND THR-340.	20080776 [Abstract]
"Phosphorylation of conserved PIN motifs directs Arabidopsis PIN1polarity and auxin transport."; Huang F., Zago M.K., Abas L., van Marion A., Galvan-Ampudia C.S.,Offringa R.; Plant Cell 22:1129-1142(2010). Cited for: FUNCTION, PHOSPHORYLATION AT SER-231; SER-252 AND SER-290, ANDMUTAGENESIS OF SER-231; SER-252 AND SER-290.	20407025 [Abstract]
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis."; Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.; Mol. Cell. Proteomics 6:1198-1214(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-337, ANDMASS SPECTROMETRY.	17317660 [Abstract]