SOX2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SOX2_MOUSE
• UniProt AC: P48432
• Protein Name: Transcription factor SOX-2
• Gene Name: Sox2
• Organism: Mus musculus (Mouse).
• Sequence Length: 319
• Subcellular Localization: Nucleus .
• Protein Description: Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency. May function as a switch in neuronal development. Downstream SRRT target that mediates the promotion of neural stem cell self-renewal. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity)..
• Protein Sequence: MYNMMETELKPPGPQQASGGGGGGGNATAAATGGNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGGNSMASGVGVGAGLGGGLNQRMDSYAHMNGWSNGSYSMMQEQLGYPQHPGLNAHGAAQMQPMHRYVVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVKSEASSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMAQHYQSGPVPGTAKYGTLPLSHM

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
2	Phosphorylation	------MYNMMETEL ------CCCCCCCCC	16.27	-
18	Phosphorylation	PPGPQQASGGGGGGG CCCCCCCCCCCCCCC	33.36	-
37	Acetylation	AATGGNQKNSPDRVK CCCCCCCCCCHHHCC	64.49	19591226
39	Phosphorylation	TGGNQKNSPDRVKRP CCCCCCCCHHHCCCH	34.90	22006019
60	Acetylation	WSRGQRRKMAQENPK CCHHHHHHHHHHCCC	40.55	19591226
67	Acetylation	KMAQENPKMHNSEIS HHHHHCCCCCHHHHH	65.46	19591226
75	Acetylation	MHNSEISKRLGAEWK CCHHHHHHHHCHHHH	58.25	19591226
89	Acetylation	KLLSETEKRPFIDEA HCCCCCCCCCCCCHH	73.18	19591226
97	Acetylation	RPFIDEAKRLRALHM CCCCCHHHHHHHHHH	50.33	19591226
105	Acetylation	RLRALHMKEHPDYKY HHHHHHHCCCCCCCC	41.97	19591226
111	Acetylation	MKEHPDYKYRPRRKT HCCCCCCCCCCCCCC	42.01	19591226
117	Acetylation	YKYRPRRKTKTLMKK CCCCCCCCCCCCCCC	56.50	19591226
118	Phosphorylation	KYRPRRKTKTLMKKD CCCCCCCCCCCCCCC	27.70	22817900
119	Acetylation	YRPRRKTKTLMKKDK CCCCCCCCCCCCCCC	42.57	19591226
123	Acetylation	RKTKTLMKKDKYTLP CCCCCCCCCCCCCCC	62.02	19591226
123	Ubiquitination	RKTKTLMKKDKYTLP CCCCCCCCCCCCCCC	62.02	-
127	Phosphorylation	TLMKKDKYTLPGGLL CCCCCCCCCCCCCEE	24.52	-
128	Phosphorylation	LMKKDKYTLPGGLLA CCCCCCCCCCCCEEC	32.02	-
140	Phosphorylation	LLAPGGNSMASGVGV EECCCCCCCCCCCCC	20.99	-
143	Phosphorylation	PGGNSMASGVGVGAG CCCCCCCCCCCCCCC	25.93	-
247	Sumoylation	GSMGSVVKSEASSSP CCHHHEEHHHHCCCC	40.18	-
247	Sumoylation	GSMGSVVKSEASSSP CCHHHEEHHHHCCCC	40.18	-
248	O-linked_Glycosylation	SMGSVVKSEASSSPP CHHHEEHHHHCCCCC	27.13	22645316
248	Phosphorylation	SMGSVVKSEASSSPP CHHHEEHHHHCCCCC	27.13	27149854
251	Phosphorylation	SVVKSEASSSPPVVT HEEHHHHCCCCCEEC	27.57	22006019
252	Phosphorylation	VVKSEASSSPPVVTS EEHHHHCCCCCEECC	54.64	29899451
253	Phosphorylation	VKSEASSSPPVVTSS EHHHHCCCCCEECCC	30.63	29895711
258	O-linked_Glycosylation	SSSPPVVTSSSHSRA CCCCCEECCCCCCCC	24.11	22645316
258	Phosphorylation	SSSPPVVTSSSHSRA CCCCCEECCCCCCCC	24.11	-
259	O-linked_Glycosylation	SSPPVVTSSSHSRAP CCCCEECCCCCCCCC	20.45	22645316
277	Phosphorylation	GDLRDMISMYLPGAE CCHHHHHHHCCCCCC	8.50	-
279	Phosphorylation	LRDMISMYLPGAEVP HHHHHHHCCCCCCCC	11.71	-

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
39	S	Phosphorylation	Kinase	CDK1	P06493	PSP
39	S	Phosphorylation	Kinase	CDK1	P11440	PSP
39	S	Phosphorylation	Kinase	CDK2	P24941	PSP
39	S	Phosphorylation	Kinase	CDK2	P97377	PSP
118	T	Phosphorylation	Kinase	AKT1	P31749	PSP
253	S	Phosphorylation	Kinase	CDK2	P24941	PSP
253	S	Phosphorylation	Kinase	CDK2	P97377	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Wwp2	Q9DBH0	PMID:25042802

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SOX2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SOX2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XPO4_MOUSE	Xpo4	physical	19349578
PO5F1_MOUSE	Pou5f1	physical	15863505
HDAC1_MOUSE	Hdac1	physical	21321941
HDAC1_MOUSE	Hdac1	physical	21103394
LN28A_MOUSE	Lin28a	physical	21103394
SALL4_MOUSE	Sall4	physical	21103394
HDAC2_MOUSE	Hdac2	physical	21103394
SOX2_MOUSE	Sox2	physical	21103394
SIX1_MOUSE	Six1	physical	22340499
EYA1_MOUSE	Eya1	physical	22340499
PO5F1_MOUSE	Pou5f1	physical	17507372
SOX2_MOUSE	Sox2	physical	17507372
NANOG_MOUSE	Nanog	physical	23892456
PO5F1_MOUSE	Pou5f1	physical	22344693
SALL4_MOUSE	Sall4	physical	23269686
OGT1_MOUSE	Ogt	physical	22608532

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Sumoylation

"Inhibition of DNA binding of Sox2 by the SUMO conjugation.";
Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y.,Aoto T., Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M.;
Biochem. Biophys. Res. Commun. 351:920-926(2006).
Cited for: SUMOYLATION AT LYS-247, MUTAGENESIS OF LYS-247, SUBCELLULAR LOCATION,AND FUNCTION.
PubMed: 17097055