dbPTM

BAME1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BAME1_ARATH
UniProt AC	O49545
Protein Name	Leucine-rich repeat receptor-like serine/threonine-protein kinase BAM1
Gene Name	BAM1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	1003
Subcellular Localization	Cell membrane Single-pass type I membrane protein .
Protein Description	Necessary for male gametophyte development, as well as ovule specification and function. Involved in cell-cell communication process required during early anther development, and regulating cell division and differentiation to organize cell layers. Required for the development of high-ordered vascular strands within the leaf and a correlated control of leaf shape, size and symmetry. May regulate the CLV1-dependent CLV3-mediated signaling in meristems maintenance..
Protein Sequence	MKLFLLLLFLLHISHTFTASRPISEFRALLSLKTSLTGAGDDKNSPLSSWKVSTSFCTWIGVTCDVSRRHVTSLDLSGLNLSGTLSPDVSHLRLLQNLSLAENLISGPIPPEISSLSGLRHLNLSNNVFNGSFPDEISSGLVNLRVLDVYNNNLTGDLPVSVTNLTQLRHLHLGGNYFAGKIPPSYGSWPVIEYLAVSGNELVGKIPPEIGNLTTLRELYIGYYNAFEDGLPPEIGNLSELVRFDGANCGLTGEIPPEIGKLQKLDTLFLQVNVFSGPLTWELGTLSSLKSMDLSNNMFTGEIPASFAELKNLTLLNLFRNKLHGEIPEFIGDLPELEVLQLWENNFTGSIPQKLGENGKLNLVDLSSNKLTGTLPPNMCSGNKLETLITLGNFLFGSIPDSLGKCESLTRIRMGENFLNGSIPKGLFGLPKLTQVELQDNYLSGELPVAGGVSVNLGQISLSNNQLSGPLPPAIGNFTGVQKLLLDGNKFQGPIPSEVGKLQQLSKIDFSHNLFSGRIAPEISRCKLLTFVDLSRNELSGEIPNEITAMKILNYLNLSRNHLVGSIPGSISSMQSLTSLDFSYNNLSGLVPGTGQFSYFNYTSFLGNPDLCGPYLGPCKDGVAKGGHQSHSKGPLSASMKLLLVLGLLVCSIAFAVVAIIKARSLKKASESRAWRLTAFQRLDFTCDDVLDSLKEDNIIGKGGAGIVYKGVMPNGDLVAVKRLAAMSRGSSHDHGFNAEIQTLGRIRHRHIVRLLGFCSNHETNLLVYEYMPNGSLGEVLHGKKGGHLHWDTRYKIALEAAKGLCYLHHDCSPLIVHRDVKSNNILLDSNFEAHVADFGLAKFLQDSGTSECMSAIAGSYGYIAPEYAYTLKVDEKSDVYSFGVVLLELVTGRKPVGEFGDGVDIVQWVRKMTDSNKDSVLKVLDPRLSSIPIHEVTHVFYVAMLCVEEQAVERPTMREVVQILTEIPKLPPSKDQPMTESAPESELSPKSGVQSPPDLLNL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	RALLSLKTSLTGAGD HHHHHHHHHCCCCCC	33.97	19880383
80	N-linked_Glycosylation	SLDLSGLNLSGTLSP EEECCCCCCCCCCCC	35.37	-
97	N-linked_Glycosylation	SHLRLLQNLSLAENL HHHHHHHHHHHHHHH	31.41	-
123	N-linked_Glycosylation	LSGLRHLNLSNNVFN CCCCCCEECCCCCCC	34.99	-
130	N-linked_Glycosylation	NLSNNVFNGSFPDEI ECCCCCCCCCCCHHH	40.70	-
153	N-linked_Glycosylation	VLDVYNNNLTGDLPV EEECCCCCCCCCCCC	35.03	-
164	N-linked_Glycosylation	DLPVSVTNLTQLRHL CCCCEEECHHHCEEE	38.65	-
212	N-linked_Glycosylation	KIPPEIGNLTTLREL CCCCCCCCCCCHHHH	39.62	-
237	N-linked_Glycosylation	GLPPEIGNLSELVRF CCCCCCCCHHHHEEE	46.16	-
312	N-linked_Glycosylation	ASFAELKNLTLLNLF CCHHHHHHHHHHHHH	51.38	-
346	N-linked_Glycosylation	VLQLWENNFTGSIPQ HHHHHHHCCCCCCCH	25.09	-
420	N-linked_Glycosylation	RMGENFLNGSIPKGL ECCCCCCCCCCCCCC	37.72	-
477	N-linked_Glycosylation	PLPPAIGNFTGVQKL CCCCCCCCCCCHHEE	25.78	-
516	Phosphorylation	DFSHNLFSGRIAPEI CCCCCCCCCCCCCCH	30.26	27531888
557	N-linked_Glycosylation	MKILNYLNLSRNHLV HHHHHHHCCCCCCCC	26.13	-
586	N-linked_Glycosylation	SLDFSYNNLSGLVPG EEECCCCCCCCCCCC	27.61	-
601	N-linked_Glycosylation	TGQFSYFNYTSFLGN CCCCCCCCCHHCCCC	30.82	-
686	Phosphorylation	AFQRLDFTCDDVLDS HHHHCCCCHHHHHHH	18.07	-
731	Phosphorylation	LAAMSRGSSHDHGFN HHHHHCCCCCCCCCC	24.32	29654922
732	Phosphorylation	AAMSRGSSHDHGFNA HHHHCCCCCCCCCCH	35.44	29654922
769	Phosphorylation	HETNLLVYEYMPNGS CCCCEEEEEECCCCC	11.00	-
807	Phosphorylation	EAAKGLCYLHHDCSP HHHCCCHHHCCCCCC	17.70	-
855	Phosphorylation	SGTSECMSAIAGSYG CCCHHHHHHHHHHCC	28.34	-
863	Phosphorylation	AIAGSYGYIAPEYAY HHHHHCCEECCCEEE	5.91	-
870	Phosphorylation	YIAPEYAYTLKVDEK EECCCEEEEEEECCC	16.23	-
871	Phosphorylation	IAPEYAYTLKVDEKS ECCCEEEEEEECCCC	16.36	-
931	Phosphorylation	VLDPRLSSIPIHEVT HHCCHHHCCCHHHHH	36.66	29654922
980	Phosphorylation	PSKDQPMTESAPESE CCCCCCCCCCCCHHH	33.21	19376835
982	Phosphorylation	KDQPMTESAPESELS CCCCCCCCCCHHHCC	39.70	19376835
986	Phosphorylation	MTESAPESELSPKSG CCCCCCHHHCCCCCC	42.66	20374526
989	Phosphorylation	SAPESELSPKSGVQS CCCHHHCCCCCCCCC	26.65	30291188
992	Phosphorylation	ESELSPKSGVQSPPD HHHCCCCCCCCCCHH	47.80	15308754
996	Phosphorylation	SPKSGVQSPPDLLNL CCCCCCCCCHHHHCC	35.67	30291188

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 BAME1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BAME1_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 BAME1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCI1_ARATH	CPI1	physical	23776660
CLV3_ARATH	CLV3	physical	25754504
RPK2_ARATH	RPK2	physical	26083273

Drug and Disease Associations

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

Regulatory Network of BAME1_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-992 AND SER-996, ANDMASS SPECTROMETRY.	19376835 [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 AT SER-989, IDENTIFICATION BY MASS SPECTROMETRY, ANDSUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].	17317660 [Abstract]
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-996, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.	14506206 [Abstract]