HEY2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HEY2_HUMAN
• UniProt AC: Q9UBP5
• Protein Name: Hairy/enhancer-of-split related with YRPW motif protein 2
• Gene Name: HEY2
• Organism: Homo sapiens (Human).
• Sequence Length: 337
• Subcellular Localization: Nucleus .
• Protein Description: Downstream effector of Notch signaling which may be required for cardiovascular development. Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3'. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6..
• Protein Sequence: MKRPCEETTSESDMDETIDVGSENNYSGQSTSSVIRLNSPTTTSQIMARKKRRGIIEKRRRDRINNSLSELRRLVPTAFEKQGSAKLEKAEILQMTVDHLKMLQATGGKGYFDAHALAMDFMSIGFRECLTEVARYLSSVEGLDSSDPLRVRLVSHLSTCATQREAAAMTSSMAHHHHPLHPHHWAAAFHHLPAALLQPNGLHASESTPCRLSTTSEVPPAHGSALLTATFAHADSALRMPSTGSVAPCVPPLSTSLLSLSATVHAAAAAATAAAHSFPLSFAGAFPMLPPNAAAAVAAATAISPPLSVSATSSPQQTSSGTNNKPYRPWGTEVGAF

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
39	Phosphorylation	SSVIRLNSPTTTSQI CCEEECCCCCCHHHH	28.37	28857561
41	Phosphorylation	VIRLNSPTTTSQIMA EEECCCCCCHHHHHH	42.39	23403867
42	Phosphorylation	IRLNSPTTTSQIMAR EECCCCCCHHHHHHH	28.03	29449344
43	Phosphorylation	RLNSPTTTSQIMARK ECCCCCCHHHHHHHH	22.55	27251275
44	Phosphorylation	LNSPTTTSQIMARKK CCCCCCHHHHHHHHH	18.67	27251275
58	Acetylation	KRRGIIEKRRRDRIN HHHCHHHHHHHHHHH	40.57	30589153
96	Phosphorylation	KAEILQMTVDHLKML HHHHHHHHHHHHHHH	15.15	-
131	Phosphorylation	IGFRECLTEVARYLS HCHHHHHHHHHHHHH	39.82	-
138	Phosphorylation	TEVARYLSSVEGLDS HHHHHHHHHCCCCCC	24.33	-
139	Phosphorylation	EVARYLSSVEGLDSS HHHHHHHHCCCCCCC	22.92	-
145	Phosphorylation	SSVEGLDSSDPLRVR HHCCCCCCCCHHHHH	41.50	-
205	Phosphorylation	QPNGLHASESTPCRL CCCCCCCCCCCCCCE	22.72	-
207	Phosphorylation	NGLHASESTPCRLST CCCCCCCCCCCCEEC	34.84	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	SH3RF1	Q7Z6J0	PMID:17420289

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HEY2_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 HEY2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIR1_HUMAN	SIRT1	physical	12535671
HDAC9_HUMAN	HDAC9	physical	11486045
NCOR1_HUMAN	NCOR1	physical	11486045
SIN3A_HUMAN	SIN3A	physical	11486045
HDAC1_HUMAN	HDAC1	physical	11486045
HES1_HUMAN	HES1	physical	11486045
FBW1A_HUMAN	BTRC	physical	17217622
NOTC1_HUMAN	NOTCH1	genetic	18239137
HD_HUMAN	HTT	physical	23275563
SE1L1_HUMAN	SEL1L	physical	24366871
SYVN1_HUMAN	SYVN1	physical	24366871
HEY1_HUMAN	HEY1	physical	24366871
DERL2_HUMAN	DERL2	physical	24366871
HEY1_HUMAN	HEY1	physical	26186194
CARM1_HUMAN	CARM1	physical	26186194
ARL10_HUMAN	ARL10	physical	26186194
IST1_HUMAN	IST1	physical	26186194
FBSP1_HUMAN	FBXO45	physical	26068074
HEY1_HUMAN	HEY1	physical	28514442
ARL10_HUMAN	ARL10	physical	28514442
CHM1A_HUMAN	CHMP1A	physical	28514442
IST1_HUMAN	IST1	physical	28514442
CARM1_HUMAN	CARM1	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.
PubMed: 19413330