Y1501_ARATH - dbPTM
Y1501_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID Y1501_ARATH
UniProt AC F4I8B9
Protein Name Putative WEB family protein At1g65010, chloroplastic
Gene Name At1g65010
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1345
Subcellular Localization Plastid, chloroplast .
Protein Description
Protein Sequence MASRTKTGLMETPRSKPSPPPPRLSKLSASKSDSNSASPVPNTRLSLDRSPPTVNSKPTPDRRPSRIPTPEKVHSRLVKGTELQTQLNQIQEDLKKADEQIELLKKDKAKAIDDLKESEKLVEEANEKLKEALAAQKRAEESFEVEKFRAVELEQAGLEAVQKKDVTSKNELESIRSQHALDISALLSTTEELQRVKHELSMTADAKNKALSHAEEATKIAEIHAEKAEILASELGRLKALLGSKEEKEAIEGNEIVSKLKSEIELLRGELEKVSILESSLKEQEGLVEQLKVDLEAAKMAESCTNSSVEEWKNKVHELEKEVEESNRSKSSASESMESVMKQLAELNHVLHETKSDNAAQKEKIELLEKTIEAQRTDLEEYGRQVCIAKEEASKLENLVESIKSELEISQEEKTRALDNEKAATSNIQNLLDQRTELSIELERCKVEEEKSKKDMESLTLALQEASTESSEAKATLLVCQEELKNCESQVDSLKLASKETNEKYEKMLEDARNEIDSLKSTVDSIQNEFENSKAGWEQKELHLMGCVKKSEEENSSSQEEVSRLVNLLKESEEDACARKEEEASLKNNLKVAEGEVKYLQETLGEAKAESMKLKESLLDKEEDLKNVTAEISSLREWEGSVLEKIEELSKVKESLVDKETKLQSITQEAEELKGREAAHMKQIEELSTANASLVDEATKLQSIVQESEDLKEKEAGYLKKIEELSVANESLADNVTDLQSIVQESKDLKEREVAYLKKIEELSVANESLVDKETKLQHIDQEAEELRGREASHLKKIEELSKENENLVDNVANMQNIAEESKDLREREVAYLKKIDELSTANGTLADNVTNLQNISEENKELRERETTLLKKAEELSELNESLVDKASKLQTVVQENEELRERETAYLKKIEELSKLHEILSDQETKLQISNHEKEELKERETAYLKKIEELSKVQEDLLNKENELHGMVVEIEDLRSKDSLAQKKIEELSNFNASLLIKENELQAVVCENEELKSKQVSTLKTIDELSDLKQSLIHKEKELQAAIVENEKLKAEAALSLQRIEELTNLKQTLIDKQNELQGVFHENEELKAKEASSLKKIDELLHLEQSWLEKESEFQRVTQENLELKTQDALAAKKIEELSKLKESLLEKETELKCREAAALEKMEEPSKHGNSELNSIGKDYDLVQFSEVNGASNGDEKTKTDHYQQRSREHMIQESPMEAIDKHLMGERAAIHKVAHRVEGERNVEKESEFKMWDSYKIEKSEVSPERETELDSVEEEVDSKAESSENMDQYSNGFSLTDHTEDSGNLLLKEQHMKKKKPLLRKFGNLLKKKSTSSSSQK
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
32PhosphorylationSKLSASKSDSNSASP
HHCCCCCCCCCCCCC
43.7225561503
34PhosphorylationLSASKSDSNSASPVP
CCCCCCCCCCCCCCC
39.5129654922
50PhosphorylationTRLSLDRSPPTVNSK
CCCCCCCCCCCCCCC
34.5929654922
69PhosphorylationRRPSRIPTPEKVHSR
CCCCCCCCCHHHHHH
41.5327545962
75PhosphorylationPTPEKVHSRLVKGTE
CCCHHHHHHHCCHHH
30.2327545962
1213PhosphorylationTDHYQQRSREHMIQE
CHHHHHHHHHHHCCC
37.3730291188
1221PhosphorylationREHMIQESPMEAIDK
HHHHCCCCHHHHHHH
17.1123776212
1261PhosphorylationSEFKMWDSYKIEKSE
HHHHEHHCCEECCCC
16.8930589143
1267PhosphorylationDSYKIEKSEVSPERE
HCCEECCCCCCCCCC
30.3623776212
1270PhosphorylationKIEKSEVSPERETEL
EECCCCCCCCCCHHH
19.5919880383
1275PhosphorylationEVSPERETELDSVEE
CCCCCCCHHHHHHHH
48.3323776212
1279PhosphorylationERETELDSVEEEVDS
CCCHHHHHHHHHHHH
44.0130291188
1286PhosphorylationSVEEEVDSKAESSEN
HHHHHHHHHHHCCCC
38.6523776212

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 Y1501_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of Y1501_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 Y1501_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of Y1501_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of Y1501_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-1279, AND MASSSPECTROMETRY.

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