SIX2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SIX2_HUMAN
• UniProt AC: Q9NPC8
• Protein Name: Homeobox protein SIX2
• Gene Name: SIX2
• Organism: Homo sapiens (Human).
• Sequence Length: 291
• Subcellular Localization: Nucleus .
• Protein Description: Transcription factor that plays an important role in the development of several organs, including kidney, skull and stomach. During kidney development, maintains cap mesenchyme multipotent nephron progenitor cells in an undifferentiated state by opposing the inductive signals emanating from the ureteric bud and cooperates with WNT9B to promote renewing progenitor cells proliferation. Acts through its interaction with TCF7L2 and OSR1 in a canonical Wnt signaling independent manner preventing transcription of differentiation genes in cap mesenchyme such as WNT4. Also acts independently of OSR1 to activate expression of many cap mesenchyme genes, including itself, GDNF and OSR1. During craniofacial development plays a role in growth and elongation of the cranial base through regulation of chondrocyte differentiation. During stomach organogenesis, controls pyloric sphincter formation and mucosal growth through regulation of a gene network including NKX2-5, BMPR1B, BMP4, SOX9 and GREM1. During branchial arch development, acts to mediate HOXA2 control over the insulin-like growth factor pathway. Also may be involved in limb tendon and ligament development (By similarity). Plays a role in cell proliferation and migration..
• Protein Sequence: MSMLPTFGFTQEQVACVCEVLQQGGNIERLGRFLWSLPACEHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHAKLQQLWLKAHYIEAEKLRGRPLGAVGKYRVRRKFPLPRSIWDGEETSYCFKEKSRSVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENNENSNSNSHNPLNGSGKSVLGSSEDEKTPSGTPDHSSSSPALLLSPPPPGLPSLHSLGHPPGPSAVPVPVPGGGGADPLQHHHGLQDSILNPMSANLVDLGS

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
53	Ubiquitination	NESVLKAKAVVAFHR CCHHHHHHHHEEECC	39.88	-
72	Phosphorylation	ELYKILESHQFSPHN HHHHHHHHCCCCCCC	21.10	28555341
76	Phosphorylation	ILESHQFSPHNHAKL HHHHCCCCCCCHHHH	20.76	25627689
148	Phosphorylation	EWYAHNPYPSPREKR HHHHHCCCCCHHHHH	22.97	27080861
150	Phosphorylation	YAHNPYPSPREKREL HHHCCCCCHHHHHHH	30.64	25159151
164	Phosphorylation	LAEATGLTTTQVSNW HHHHHCCCHHHHHHH	29.19	-
211	Phosphorylation	SGKSVLGSSEDEKTP CCCCCCCCCCCCCCC	26.79	23663014
212	Phosphorylation	GKSVLGSSEDEKTPS CCCCCCCCCCCCCCC	47.47	23663014

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SIX2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SIX2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SIX2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
EYA1_HUMAN	EYA1	physical	28514442
EYA4_HUMAN	EYA4	physical	28514442
EYA3_HUMAN	EYA3	physical	28514442
ERC6L_HUMAN	ERCC6L	physical	28514442
KPCD1_HUMAN	PRKD1	physical	28514442
BN3D2_HUMAN	BCDIN3D	physical	28514442
EYA2_HUMAN	EYA2	physical	28514442
CHMP3_HUMAN	CHMP3	physical	28514442
CHM1A_HUMAN	CHMP1A	physical	28514442
ANKH1_HUMAN	ANKHD1	physical	28514442
PSMG3_HUMAN	PSMG3	physical	28514442
THNS1_HUMAN	THNSL1	physical	28514442
MARK2_HUMAN	MARK2	physical	28514442
CHM2A_HUMAN	CHMP2A	physical	28514442
TLE1_HUMAN	TLE1	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
IMB1_HUMAN	KPNB1	physical	28514442
ANR17_HUMAN	ANKRD17	physical	28514442
TLE3_HUMAN	TLE3	physical	28514442

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.