HAT22_ARATH - dbPTM
HAT22_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAT22_ARATH
UniProt AC P46604
Protein Name Homeobox-leucine zipper protein HAT22
Gene Name HAT22
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 278
Subcellular Localization Nucleus .
Protein Description Probable transcription factor..
Protein Sequence MGLDDSCNTGLVLGLGLSPTPNNYNHAIKKSSSTVDHRFIRLDPSLTLSLSGESYKIKTGAGAGDQICRQTSSHSGISSFSSGRVKREREISGGDGEEEAEETTERVVCSRVSDDHDDEEGVSARKKLRLTKQQSALLEDNFKLHSTLNPKQKQALARQLNLRPRQVEVWFQNRRARTKLKQTEVDCEFLKKCCETLTDENRRLQKELQDLKALKLSQPFYMHMPAATLTMCPSCERLGGGGVGGDTTAVDEETAKGAFSIVTKPRFYNPFTNPSAAC
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
92PhosphorylationVKREREISGGDGEEE
EEEEEECCCCCCHHH
31.7819880383
103PhosphorylationGEEEAEETTERVVCS
CHHHHHHHCEEEEEE
26.0125561503
110PhosphorylationTTERVVCSRVSDDHD
HCEEEEEECCCCCCC
24.9025561503
113PhosphorylationRVVCSRVSDDHDDEE
EEEEECCCCCCCCCC
35.8930407730

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 HAT22_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HAT22_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 HAT22_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAT2_ARATHHAT2physical
21798944
HAT14_ARATHHAT14physical
21798944

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HAT22_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.

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