MEIS2_MOUSE - dbPTM
MEIS2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MEIS2_MOUSE
UniProt AC P97367
Protein Name Homeobox protein Meis2
Gene Name Meis2
Organism Mus musculus (Mouse).
Sequence Length 477
Subcellular Localization Nucleus . Cytoplasm, perinuclear region .
Protein Description Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform Meis2B is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoforms Meis2B and Meis2D can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription..
Protein Sequence MAQRYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAIYGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPSSWRDHDDATSTHSAGTPGPSSGGHASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAGFLLDPSVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGLQSMPGDYVSQGGPMGMGMAQPSYTPPQMTPHPTQLRHGPPMHSYLPSHPHHPAMVMHGGPPTHPGMTMSAQSPTMLNSVDPNVGGQVMDIHAQ
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
195PhosphorylationVIDERDGSSKSDHEE
EEECCCCCCCCCCCH
38.5927681418
196PhosphorylationIDERDGSSKSDHEEL
EECCCCCCCCCCCHH
41.5320415495
198PhosphorylationERDGSSKSDHEELSG
CCCCCCCCCCCHHCC
46.2628418008
204PhosphorylationKSDHEELSGSSTNLA
CCCCCHHCCCCCCCC
39.6520415495
206PhosphorylationDHEELSGSSTNLADH
CCCHHCCCCCCCCCC
30.5225338131
248PhosphorylationASQSGDNSSEQGDGL
CCCCCCCCCCCCCCC
39.7425338131
249PhosphorylationSQSGDNSSEQGDGLD
CCCCCCCCCCCCCCC
39.9525338131
261PhosphorylationGLDNSVASPGTGDDD
CCCCCCCCCCCCCCC
23.0025338131
264PhosphorylationNSVASPGTGDDDDPD
CCCCCCCCCCCCCCC
40.6025338131

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 MEIS2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MEIS2_MOUSE !!

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 MEIS2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAX6_MOUSEPax6physical
20211142
PBX1_MOUSEPbx1physical
20211142
PBX2_MOUSEPbx2physical
20211142
PBX3_MOUSEPbx3physical
20211142
TFE2_MOUSETcf3physical
20211142
PBX4_MOUSEPbx4physical
20211142

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MEIS2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND MASSSPECTROMETRY.

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