dbPTM

SRA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRA1_HUMAN
UniProt AC	Q9HD15
Protein Name	Steroid receptor RNA activator 1
Gene Name	SRA1 {ECO:0000312\|HGNC:HGNC:11281}
Organism	Homo sapiens (Human).
Sequence Length	236
Subcellular Localization	Nucleus . Cytoplasm .
Protein Description	Functional RNA which acts as a transcriptional coactivator that selectively enhances steroid receptor-mediated transactivation ligand-independently through a mechanism involving the modulating N-terminal domain (AF-1) of steroid receptors. Also mediates transcriptional coactivation of steroid receptors ligand-dependently through the steroid-binding domain (AF-2). Enhances cellular proliferation and differentiation and promotes apoptosis in vivo. May play a role in tumorigenesis..
Protein Sequence	MTRCPAGQAEVEMAELYVKPGNKERGWNDPPQFSYGLQTQAGGPRRSLLTKRVAAPQDGSPRVPASETSPGPPPMGPPPPSSKAPRSPPVGSGPASGVEPTSFPVESEAVMEDVLRPLEQALEDCRGHTRKQVCDDISRRLALLQEQWAGGKLSIPVKKRMALLVQELSSHRWDAADDIHRSLMVDHVTEVSQWMVGVKRLIAEKRSLFSEEAANEEKSAATAEKNHTIPGFQQAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
35	Phosphorylation	NDPPQFSYGLQTQAG CCCCCCCCCCCCCCC	24.12	27642862
39	Phosphorylation	QFSYGLQTQAGGPRR CCCCCCCCCCCCCCC	25.98	28348404
45	Methylation	QTQAGGPRRSLLTKR CCCCCCCCCCHHHCC	44.06	80702657
47	Phosphorylation	QAGGPRRSLLTKRVA CCCCCCCCHHHCCCC	29.07	26434776
50	Phosphorylation	GPRRSLLTKRVAAPQ CCCCCHHHCCCCCCC	23.30	28348404
60	Phosphorylation	VAAPQDGSPRVPASE CCCCCCCCCCCCCCC	20.16	29255136
66	Phosphorylation	GSPRVPASETSPGPP CCCCCCCCCCCCCCC	35.02	23401153
68	Phosphorylation	PRVPASETSPGPPPM CCCCCCCCCCCCCCC	37.41	25159151
69	Phosphorylation	RVPASETSPGPPPMG CCCCCCCCCCCCCCC	24.65	30278072
69	O-linked_Glycosylation	RVPASETSPGPPPMG CCCCCCCCCCCCCCC	24.65	31373491
81	Phosphorylation	PMGPPPPSSKAPRSP CCCCCCCCCCCCCCC	50.69	30576142
82	Phosphorylation	MGPPPPSSKAPRSPP CCCCCCCCCCCCCCC	38.31	30576142
83 (in isoform 1)	Ubiquitination	-	67.74	21906983
83	Acetylation	GPPPPSSKAPRSPPV CCCCCCCCCCCCCCC	67.74	25953088
83	Ubiquitination	GPPPPSSKAPRSPPV CCCCCCCCCCCCCCC	67.74	22817900
87	Phosphorylation	PSSKAPRSPPVGSGP CCCCCCCCCCCCCCC	32.28	19664994
92	Phosphorylation	PRSPPVGSGPASGVE CCCCCCCCCCCCCCC	41.66	25850435
96	Phosphorylation	PVGSGPASGVEPTSF CCCCCCCCCCCCCCC	46.64	25850435
101	Phosphorylation	PASGVEPTSFPVESE CCCCCCCCCCCCCCH	29.51	26074081
102	Phosphorylation	ASGVEPTSFPVESEA CCCCCCCCCCCCCHH	37.96	26074081
107	Phosphorylation	PTSFPVESEAVMEDV CCCCCCCCHHHHHHH	30.96	26074081
138	Phosphorylation	KQVCDDISRRLALLQ HHHHHHHHHHHHHHH	20.52	-
158	2-Hydroxyisobutyrylation	GKLSIPVKKRMALLV CCCCCCHHHHHHHHH	29.34	-
218	Methylation	EEAANEEKSAATAEK HHHHHHHHHHHHHHH	38.94	-
225	Acetylation	KSAATAEKNHTIPGF HHHHHHHHHCCCCCC	52.11	25953088
236	Phosphorylation	IPGFQQAS------- CCCCCCCC-------	36.09	25159151

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 SRA1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRA1_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 SRA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
UBE2T_HUMAN	UBE2T	physical	22939629
HDAC2_HUMAN	HDAC2	physical	20398657

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 SRA1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-60 AND THR-68, AND MASSSPECTROMETRY.	18669648 [Abstract]