SLIRP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SLIRP_HUMAN
• UniProt AC: Q9GZT3
• Protein Name: SRA stem-loop-interacting RNA-binding protein, mitochondrial
• Gene Name: SLIRP
• Organism: Homo sapiens (Human).
• Sequence Length: 109
• Subcellular Localization: Mitochondrion . Nucleus . Predominantly mitochondrial. Some fraction is nuclear. In the nucleus, it is recruited to nuclear receptor target promoters.
• Protein Description: RNA-binding protein that acts as a nuclear receptor corepressor. Probably acts by binding the SRA RNA, and repressing the SRA-mediated nuclear receptor coactivation. Binds the STR7 loop of SRA RNA. Also able to repress glucocorticoid (GR), androgen (AR), thyroid (TR) and VDR-mediated transactivation..
• Protein Sequence: MAASAARGAAALRRSINQPVAFVRRIPWTAASSQLKEHFAQFGHVRRCILPFDKETGFHRGLGWVQFSSEEGLRNALQQENHIIDGVKVQVHTRRPKLPQTSDDEKKDF

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
4	Phosphorylation	----MAASAARGAAA ----CHHHHHHHHHH	16.96	-
7	Methylation	-MAASAARGAAALRR -CHHHHHHHHHHHHH	34.69	115368649
15	Phosphorylation	GAAALRRSINQPVAF HHHHHHHHCCCCEEE	21.32	30266825
36	Ubiquitination	TAASSQLKEHFAQFG HHCHHHHHHHHHHHC	41.32	21890473
36	Acetylation	TAASSQLKEHFAQFG HHCHHHHHHHHHHHC	41.32	25953088
48	S-nitrosocysteine	QFGHVRRCILPFDKE HHCCEEEEEEECCCC	2.34	-
48	Glutathionylation	QFGHVRRCILPFDKE HHCCEEEEEEECCCC	2.34	22555962
48	S-nitrosylation	QFGHVRRCILPFDKE HHCCEEEEEEECCCC	2.34	19483679
54	Acetylation	RCILPFDKETGFHRG EEEEECCCCCCCCCC	58.52	26822725
68	Phosphorylation	GLGWVQFSSEEGLRN CCCCEEECCHHHHHH	21.54	30108239
69	Phosphorylation	LGWVQFSSEEGLRNA CCCEEECCHHHHHHH	40.74	30108239
88	Ubiquitination	NHIIDGVKVQVHTRR CCCCCCEEEEEEECC	32.26	21890473
88	2-Hydroxyisobutyrylation	NHIIDGVKVQVHTRR CCCCCCEEEEEEECC	32.26	-
88	Acetylation	NHIIDGVKVQVHTRR CCCCCCEEEEEEECC	32.26	25953088
99 (in isoform 2)	Phosphorylation	-	41.34	29743597
100 (in isoform 2)	Phosphorylation	-	65.16	25849741
101	Phosphorylation	RRPKLPQTSDDEKKD CCCCCCCCCCCCCCC	31.98	29255136
102	Phosphorylation	RPKLPQTSDDEKKDF CCCCCCCCCCCCCCC	37.50	29255136
106	Acetylation	PQTSDDEKKDF---- CCCCCCCCCCC----	65.71	25953088

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SLIRP_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SLIRP_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 SLIRP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
U2AF2_HUMAN	U2AF2	physical	22939629
K1C40_HUMAN	KRT40	physical	25416956

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

"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-15 AND SER-102, AND MASSSPECTROMETRY.
PubMed: 18669648

"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-102, AND MASSSPECTROMETRY.
PubMed: 17081983