RMXL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RMXL2_HUMAN
• UniProt AC: O75526
• Protein Name: RNA-binding motif protein, X-linked-like-2
• Gene Name: RBMXL2
• Organism: Homo sapiens (Human).
• Sequence Length: 392
• Subcellular Localization: Nucleus .
• Protein Sequence: MVEADRPGKLFIGGLNLETDEKALEAEFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKAAARDMNGKSLDGKAIKVAQATKPAFESSRRGPPPPRSRGRPRFLRGTRGGGGGPRRSPSRGGPDDDGGYTADFDLRPSRAPMPMKRGPPPRRVGPPPKRAAPSGPARSSGGGMRGRALAVRGRDGYSGPPRREPLPPRRDPYLGPRDEGYSSRDGYSSRDYREPRGFAPSPGEYTHRDYGHSSVRDDCPLRGYSDRDGYGGRDRDYGDHLSRGSHREPFESYGELRGAAPGRGTPPSYGGGGRYEEYRGYSPDAYSGGRDSYSSSYGRSDRYSRGRHRVGRPDRGLSLSMERGCPPQRDSYSRSGCRVPRGGGRLGGRLERGGGRSRY

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
1	Acetylation	-------MVEADRPG -------CCCCCCCC	5.77	-
9	Acetylation	VEADRPGKLFIGGLN CCCCCCCCEEECCCC	42.79	23749302
9	Ubiquitination	VEADRPGKLFIGGLN CCCCCCCCEEECCCC	42.79	23000965
31	Phosphorylation	LEAEFGKYGRIVEVL HHHHHHHHHHEEEEE	16.41	-
40	Sulfoxidation	RIVEVLLMKDRETNK HEEEEEEEECCCCCC	3.57	21406390
41	Ubiquitination	IVEVLLMKDRETNKS EEEEEEEECCCCCCC	54.31	23000965
47	Ubiquitination	MKDRETNKSRGFAFV EECCCCCCCCCEEEE	49.28	23000965
48	Phosphorylation	KDRETNKSRGFAFVT ECCCCCCCCCEEEEE	39.44	23882029
49	Methylation	DRETNKSRGFAFVTF CCCCCCCCCEEEEEE	45.95	-
55	Phosphorylation	SRGFAFVTFESPADA CCCEEEEEECCHHHH	18.41	30266825
58	Phosphorylation	FAFVTFESPADAKAA EEEEEECCHHHHHHH	22.61	29255136
63	Ubiquitination	FESPADAKAAARDMN ECCHHHHHHHHHHCC	38.82	16196087
72	Acetylation	AARDMNGKSLDGKAI HHHHCCCCCCCCCHH	42.72	23749302
73	Phosphorylation	ARDMNGKSLDGKAIK HHHCCCCCCCCCHHH	32.84	28857561
77	Acetylation	NGKSLDGKAIKVAQA CCCCCCCCHHHEEEC	46.75	25953088
77	Ubiquitination	NGKSLDGKAIKVAQA CCCCCCCCHHHEEEC	46.75	32015554
80	Acetylation	SLDGKAIKVAQATKP CCCCCHHHEEECCHH	36.06	25953088
85	Phosphorylation	AIKVAQATKPAFESS HHHEEECCHHHHHHH	26.02	-
111	Phosphorylation	RPRFLRGTRGGGGGP CCCCCCCCCCCCCCC	21.51	-
142	Phosphorylation	ADFDLRPSRAPMPMK CCCCCCCCCCCCCCC	34.34	24719451
150	Methylation	RAPMPMKRGPPPRRV CCCCCCCCCCCCCCC	57.51	-
167	Phosphorylation	PPKRAAPSGPARSSG CCCCCCCCCCCCCCC	53.32	23898821
172	Phosphorylation	APSGPARSSGGGMRG CCCCCCCCCCCCCCC	35.13	22210691
173	Phosphorylation	PSGPARSSGGGMRGR CCCCCCCCCCCCCCC	35.58	22210691
190	Phosphorylation	AVRGRDGYSGPPRRE EECCCCCCCCCCCCC	18.10	21712546
191	Phosphorylation	VRGRDGYSGPPRREP ECCCCCCCCCCCCCC	50.80	20860994
215	Phosphorylation	GPRDEGYSSRDGYSS CCCCCCCCCCCCCCC	29.74	25367160
220	Phosphorylation	GYSSRDGYSSRDYRE CCCCCCCCCCCCCCC	14.04	22468782
221	Phosphorylation	YSSRDGYSSRDYREP CCCCCCCCCCCCCCC	25.15	-
222	Phosphorylation	SSRDGYSSRDYREPR CCCCCCCCCCCCCCC	22.23	20363803
263	Phosphorylation	GYSDRDGYGGRDRDY CCCCCCCCCCCCCCC	22.24	28060719
276	Methylation	DYGDHLSRGSHREPF CCCCCCCCCCCCCCC	57.92	115383769
298	Phosphorylation	GAAPGRGTPPSYGGG CCCCCCCCCCCCCCC	30.57	20860994
301	Phosphorylation	PGRGTPPSYGGGGRY CCCCCCCCCCCCCCC	37.30	20860994

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

Oops, there are no upstream regulatory protein records of RMXL2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RMXL2_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 RMXL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PGTA_HUMAN	RABGGTA	physical	22939629

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

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

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-58, 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-58, AND MASSSPECTROMETRY.
PubMed: 17081983