dbPTM

HES1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HES1_HUMAN
UniProt AC	Q14469
Protein Name	Transcription factor HES-1
Gene Name	HES1
Organism	Homo sapiens (Human).
Sequence Length	280
Subcellular Localization	Nucleus.
Protein Description	Transcriptional repressor of genes that require a bHLH protein for their transcription. May act as a negative regulator of myogenesis by inhibiting the functions of MYOD1 and ASH1. Binds DNA on N-box motifs: 5'-CACNAG-3' with high affinity and on E-box motifs: 5'-CANNTG-3' with low affinity (By similarity). May play a role in a functional FA core complex response to DNA cross-link damage, being required for the stability and nuclear localization of FA core complex proteins, as well as for FANCD2 monoubiquitination in response to DNA damage..
Protein Sequence	MPADIMEKNSSSPVAATPASVNTTPDKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQMTAALSTDPSVLGKYRAGFSECMNEVTRFLSTCEGVNTEVRTRLLGHLANCMTQINAMTYPGQPHPALQAPPPPPPGPGGPQHAPFAPPPPLVPIPGGAAPPPGGAPCKLGSQAGEAAKVFGGFQVVPAPDGQFAFLIPNGAFAHSGPVIPVYTSNSGTSVGPNAVSPSSGPSLTADSMWRPWRN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	ADIMEKNSSSPVAAT HHHHCCCCCCCCCCC	43.17	30266825
11	Phosphorylation	DIMEKNSSSPVAATP HHHCCCCCCCCCCCC	48.32	30266825
12	Phosphorylation	IMEKNSSSPVAATPA HHCCCCCCCCCCCCC	24.18	30266825
17	Phosphorylation	SSSPVAATPASVNTT CCCCCCCCCCCCCCC	15.06	30266825
20	Phosphorylation	PVAATPASVNTTPDK CCCCCCCCCCCCCCC	19.66	23403867
23	Phosphorylation	ATPASVNTTPDKPKT CCCCCCCCCCCCCCC	37.23	23403867
24	Phosphorylation	TPASVNTTPDKPKTA CCCCCCCCCCCCCCH	25.04	19413330
32	Phosphorylation	PDKPKTASEHRKSSK CCCCCCHHHHHHCCC	38.88	-
37	Phosphorylation	TASEHRKSSKPIMEK CHHHHHHCCCHHHHH	43.48	22817900
38	Phosphorylation	ASEHRKSSKPIMEKR HHHHHHCCCHHHHHH	45.55	22817900
55	Phosphorylation	ARINESLSQLKTLIL HHHHHHHHHHHHHHH	42.62	24719451
59	Phosphorylation	ESLSQLKTLILDALK HHHHHHHHHHHHHHH	27.85	-
77	Ubiquitination	SRHSKLEKADILEMT CCCHHHHHHHHHHHH	62.89	29967540
84	Phosphorylation	KADILEMTVKHLRNL HHHHHHHHHHHHHHH	19.61	26546556
86	Ubiquitination	DILEMTVKHLRNLQR HHHHHHHHHHHHHHH	27.96	22817900
97	Phosphorylation	NLQRAQMTAALSTDP HHHHHHHHHHHCCCH	9.19	-
109	Ubiquitination	TDPSVLGKYRAGFSE CCHHHHHHHHHCHHH	27.66	22817900
115	O-linked_Glycosylation	GKYRAGFSECMNEVT HHHHHCHHHHHHHHH	29.03	OGP
122	O-linked_Glycosylation	SECMNEVTRFLSTCE HHHHHHHHHHHHHCC	14.99	OGP
126	O-linked_Glycosylation	NEVTRFLSTCEGVNT HHHHHHHHHCCCCCH	28.44	OGP
127	O-linked_Glycosylation	EVTRFLSTCEGVNTE HHHHHHHHCCCCCHH	19.41	OGP

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
37	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
37	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
37	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
38	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
38	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
38	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HES1_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 HES1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIR1_HUMAN	SIRT1	physical	12535671
TLE2_HUMAN	TLE2	physical	9874198
RUNX2_HUMAN	RUNX2	physical	16195230
FANCF_HUMAN	FANCF	physical	18550849
FANCG_HUMAN	FANCG	physical	18550849
FANCL_HUMAN	FANCL	physical	18550849
FANCA_HUMAN	FANCA	physical	18550849
FANCE_HUMAN	FANCE	physical	18550849
HSP74_HUMAN	HSPA4	physical	18550849
HS90A_HUMAN	HSP90AA1	physical	18550849
SPTN1_HUMAN	SPTAN1	physical	18550849
PARP1_HUMAN	PARP1	physical	21224467
TLE1_HUMAN	TLE1	physical	18611861
STAT3_HUMAN	STAT3	physical	15156153
JAK2_HUMAN	JAK2	physical	15156153
TNR3_HUMAN	LTBR	physical	21988832
FANCE_HUMAN	FANCE	physical	26277624
TLE1_HUMAN	TLE1	physical	19321451
FANCG_HUMAN	FANCG	physical	19321451
FANCF_HUMAN	FANCF	physical	19321451
FANCA_HUMAN	FANCA	physical	19321451
FANCE_HUMAN	FANCE	physical	19321451
HES1_HUMAN	HES1	physical	19321451
VIE1_HCMVM	UL123	physical	28750047

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.

Regulatory Network of HES1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-10 AND THR-24, AND MASSSPECTROMETRY.	19413330 [Abstract]