DLX2_HUMAN - dbPTM
DLX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DLX2_HUMAN
UniProt AC Q07687
Protein Name Homeobox protein DLX-2
Gene Name DLX2
Organism Homo sapiens (Human).
Sequence Length 328
Subcellular Localization Nucleus .
Protein Description Acts as a transcriptional activator. Plays a role in terminal differentiation of interneurons, such as amacrine and bipolar cells in the developing retina. Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis..
Protein Sequence MTGVFDSLVADMHSTQIAASSTYHQHQQPPSGGGAGPGGNSSSSSSLHKPQESPTLPVSTATDSSYYTNQQHPAGGGGGGGSPYAHMGSYQYQASGLNNVPYSAKSSYDLGYTAAYTSYAPYGTSSSPANNEPEKEDLEPEIRIVNGKPKKVRKPRTIYSSFQLAALQRRFQKTQYLALPERAELAASLGLTQTQVKIWFQNRRSKFKKMWKSGEIPSEQHPGASASPPCASPPVSAPASWDFGVPQRMAGGGGPGSGGSGAGSSGSSPSSAASAFLGNYPWYHQTSGSASHLQATAPLLHPTQTPQPHHHHHHHGGGGAPVSAGTIF
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
122PhosphorylationAYTSYAPYGTSSSPA
EEEECCCCCCCCCCC
25.5118669648
127PhosphorylationAPYGTSSSPANNEPE
CCCCCCCCCCCCCCC
28.00-
157PhosphorylationKKVRKPRTIYSSFQL
CCCCCCCCHHHHHHH
32.5624114839
159PhosphorylationVRKPRTIYSSFQLAA
CCCCCCHHHHHHHHH
9.5424114839
160PhosphorylationRKPRTIYSSFQLAAL
CCCCCHHHHHHHHHH
22.3324114839
161PhosphorylationKPRTIYSSFQLAALQ
CCCCHHHHHHHHHHH
10.4724114839
173UbiquitinationALQRRFQKTQYLALP
HHHHHHHHHHHHCCH
34.5821890473
173UbiquitinationALQRRFQKTQYLALP
HHHHHHHHHHHHCCH
34.5821890473
173UbiquitinationALQRRFQKTQYLALP
HHHHHHHHHHHHCCH
34.5821890473
213PhosphorylationKFKKMWKSGEIPSEQ
HHHHHHHCCCCCCCC
26.5826074081
218PhosphorylationWKSGEIPSEQHPGAS
HHCCCCCCCCCCCCC
56.3928387310
225PhosphorylationSEQHPGASASPPCAS
CCCCCCCCCCCCCCC
34.8830576142
227PhosphorylationQHPGASASPPCASPP
CCCCCCCCCCCCCCC
27.2122617229
232PhosphorylationSASPPCASPPVSAPA
CCCCCCCCCCCCCCC
36.1322617229
236PhosphorylationPCASPPVSAPASWDF
CCCCCCCCCCCCCCC
34.0226074081
240PhosphorylationPPVSAPASWDFGVPQ
CCCCCCCCCCCCCCC
26.5626074081
257PhosphorylationAGGGGPGSGGSGAGS
CCCCCCCCCCCCCCC
43.01-

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 DLX2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DLX2_HUMAN !!

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 DLX2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MSX1_HUMANMSX1physical
9111364
MSX2_HUMANMSX2physical
9111364
DLX2_HUMANDLX2physical
9111364
DLX5_HUMANDLX5physical
9111364
HXC8_HUMANHOXC8physical
9111364
P85A_HUMANPIK3R1physical
21988832
GRN_HUMANGRNphysical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DLX2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-232, ANDMASS SPECTROMETRY.

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