dbPTM

ARGL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARGL1_HUMAN
UniProt AC	Q9NWB6
Protein Name	Arginine and glutamate-rich protein 1
Gene Name	ARGLU1
Organism	Homo sapiens (Human).
Sequence Length	273
Subcellular Localization	Nucleus . Recruited, in an estrogen-dependent manner, to ESR1 target gene promoters. Colocalizes with MED1.
Protein Description	Required for the estrogen-dependent expression of ESR1 target genes. Can act in cooperation with MED1..
Protein Sequence	MGRSRSRSSSRSKHTKSSKHNKKRSRSRSRSRDKERVRKRSKSRESKRNRRRESRSRSRSTNTAVSRRERDRERASSPPDRIDIFGRTVSKRSSLDEKQKREEEEKKAEFERQRKIRQQEIEEKLIEEETARRVEELVAKRVEEELEKRKDEIEREVLRRVEEAKRIMEKQLLEELERQRQAELAAQKAREEEERAKREELERILEENNRKIAEAQAKLAEEQLRIVEEQRKIHEERMKLEQERQRQQKEEQKIILGKGKSRPKLSFSLKTQD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	GRSRSRSSSRSKHTK CCCCCCCCCCCCCCC	28.76	22210691
10	Phosphorylation	RSRSRSSSRSKHTKS CCCCCCCCCCCCCCC	41.65	22210691
12	Phosphorylation	RSRSSSRSKHTKSSK CCCCCCCCCCCCCHH	30.64	23911959
25	Phosphorylation	SKHNKKRSRSRSRSR HHHHHHHHHHHHHHH	43.41	27135362
27	Phosphorylation	HNKKRSRSRSRSRDK HHHHHHHHHHHHHHH	35.54	27135362
29	Phosphorylation	KKRSRSRSRSRDKER HHHHHHHHHHHHHHH	35.54	27135362
31	Phosphorylation	RSRSRSRSRDKERVR HHHHHHHHHHHHHHH	46.18	27135362
46	Phosphorylation	KRSKSRESKRNRRRE HHHHHHHHHHHHHHH	35.49	27135362
54	Phosphorylation	KRNRRRESRSRSRST HHHHHHHHHHHHHHH	33.47	20068231
56	Phosphorylation	NRRRESRSRSRSTNT HHHHHHHHHHHHHHH	43.84	26055452
58	Phosphorylation	RRESRSRSRSTNTAV HHHHHHHHHHHHHHH	31.65	28355574
60	Phosphorylation	ESRSRSRSTNTAVSR HHHHHHHHHHHHHHH	27.53	30266825
61	Phosphorylation	SRSRSRSTNTAVSRR HHHHHHHHHHHHHHH	35.16	30266825
63	Phosphorylation	SRSRSTNTAVSRRER HHHHHHHHHHHHHHH	28.64	23663014
66	Phosphorylation	RSTNTAVSRRERDRE HHHHHHHHHHHHHHH	24.13	23663014
76	Phosphorylation	ERDRERASSPPDRID HHHHHHHCCCCCHHH	49.99	22167270
77	Phosphorylation	RDRERASSPPDRIDI HHHHHHCCCCCHHHH	39.19	22167270
88	Phosphorylation	RIDIFGRTVSKRSSL HHHHCCCCHHCCCCC	29.52	26074081
90	Phosphorylation	DIFGRTVSKRSSLDE HHCCCCHHCCCCCCH	23.03	26074081
93	Phosphorylation	GRTVSKRSSLDEKQK CCCHHCCCCCCHHHH	38.70	20068231
94	Phosphorylation	RTVSKRSSLDEKQKR CCHHCCCCCCHHHHH	43.82	20068231
124	Ubiquitination	RQQEIEEKLIEEETA HHHHHHHHHHHHHHH	41.81	-
140	Ubiquitination	RVEELVAKRVEEELE HHHHHHHHHHHHHHH	49.88	-
165	2-Hydroxyisobutyrylation	LRRVEEAKRIMEKQL HHHHHHHHHHHHHHH	45.82	-
188	Ubiquitination	QAELAAQKAREEEER HHHHHHHHHHHHHHH	44.69	-
188	2-Hydroxyisobutyrylation	QAELAAQKAREEEER HHHHHHHHHHHHHHH	44.69	-
225	Methylation	KLAEEQLRIVEEQRK HHHHHHHHHHHHHHH	30.51	-
261	Phosphorylation	IILGKGKSRPKLSFS HHCCCCCCCCCCCCE	63.58	28152594
266	Phosphorylation	GKSRPKLSFSLKTQD CCCCCCCCCEECCCC	20.93	22167270
268	Phosphorylation	SRPKLSFSLKTQD-- CCCCCCCEECCCC--	26.11	22167270
271	Phosphorylation	KLSFSLKTQD----- CCCCEECCCC-----	43.17	29214152
271	O-linked_Glycosylation	KLSFSLKTQD----- CCCCEECCCC-----	43.17	29237092

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 ARGL1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARGL1_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 ARGL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
CHERP_HUMAN	CHERP	physical	22365833
ARGL1_HUMAN	ARGLU1	physical	22365833
ANM5_HUMAN	PRMT5	physical	22365833
ZCH10_HUMAN	ZCCHC10	physical	22365833
SRPK2_HUMAN	SRPK2	physical	22365833
PUF60_HUMAN	PUF60	physical	26344197
TCP4_HUMAN	SUB1	physical	26344197

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 ARGL1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASSSPECTROMETRY.	17081983 [Abstract]