SIX1_HUMAN - dbPTM
SIX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIX1_HUMAN
UniProt AC Q15475
Protein Name Homeobox protein SIX1
Gene Name SIX1
Organism Homo sapiens (Human).
Sequence Length 284
Subcellular Localization Nucleus . Cytoplasm.
Protein Description Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development. Plays an important role in the development of several organs, including kidney, muscle and inner ear. Depending on context, functions as transcriptional repressor or activator. Lacks an activation domain, and requires interaction with EYA family members for transcription activation. Mediates nuclear translocation of EYA1 and EYA2. Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the MYOG promoter. Regulates the expression of numerous genes, including MYC, CCND1 and EZR. Acts as activator of the IGFBP5 promoter, probably coactivated by EYA2. Repression of precursor cell proliferation in myoblasts is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex. During myogenesis, seems to act together with EYA2 and DACH2 (By similarity). Regulates the expression of CCNA1..
Protein Sequence MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQGNMGHARSSNYSLPGLTASQPSHGLQTHQHQLQDSLLGPLTSSLVDLGS
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
6Phosphorylation--MSMLPSFGFTQEQ
--CCCCCCCCCCHHH
33.7629759185
10PhosphorylationMLPSFGFTQEQVACV
CCCCCCCCHHHHHHH
31.4129759185
53UbiquitinationNESVLKAKAVVAFHR
CCHHHHHHHHEEECC
39.88-
76PhosphorylationILESHQFSPHNHPKL
HHHHCCCCCCCCHHH
20.7628555341
97UbiquitinationAHYVEAEKLRGRPLG
HHHHHHHHHCCCCCC
51.0029967540
143PhosphorylationRGVLREWYAHNPYPS
CCHHHHHHHHCCCCC
8.01-
148PhosphorylationEWYAHNPYPSPREKR
HHHHHCCCCCHHHHH
22.9727080861
150PhosphorylationYAHNPYPSPREKREL
HHHCCCCCHHHHHHH
30.6425159151
164PhosphorylationLAEATGLTTTQVSNW
HHHHHCCCHHHHHHH
29.19-
204PhosphorylationSNKQNQLSPLEGGKP
CCCCCCCCCCCCCCC
20.0625159151
215PhosphorylationGGKPLMSSSEEEFSP
CCCCCCCCCCCCCCC
28.0127251275
216PhosphorylationGKPLMSSSEEEFSPP
CCCCCCCCCCCCCCC
41.5427251275
276O-linked_GlycosylationDSLLGPLTSSLVDLG
HHHHHHHHHHHHHCC
21.2832863962

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 SIX1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIX1_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 SIX1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
EYA2_HUMANEYA2physical
10906137
FZR1_HUMANFZR1physical
17130831
VTNC_HUMANVTNphysical
21988832
EYA4_HUMANEYA4physical
26186194
EYA1_HUMANEYA1physical
26186194
MYH3_HUMANMYH3physical
26186194
MYH7_HUMANMYH7physical
26186194
MYH4_HUMANMYH4physical
26186194
EYA1_HUMANEYA1physical
28514442
EYA4_HUMANEYA4physical
28514442
MYH3_HUMANMYH3physical
28514442
MYH4_HUMANMYH4physical
28514442
MYH7_HUMANMYH7physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SIX1_HUMAN

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Related Literatures of Post-Translational Modification

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