RSRC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RSRC2_HUMAN
• UniProt AC: Q7L4I2
• Protein Name: Arginine/serine-rich coiled-coil protein 2
• Gene Name: RSRC2
• Organism: Homo sapiens (Human).
• Sequence Length: 434
• Protein Sequence: MAASDTERDGLAPEKTSPDRDKKKEQSEVSVSPRASKHHYSRSRSRSRERKRKSDNEGRKHRSRSRSKEGRRHESKDKSSKKHKSEEHNDKEHSSDKGRERLNSSENGEDRHKRKERKSSRGRSHSRSRSRERRHRSRSRERKKSRSRSRERKKSRSRSRERKKSRSRSRERKRRIRSRSRSRSRHRHRTRSRSRTRSRSRDRKKRIEKPRRFSRSLSRTPSPPPFRGRNTAMDAQEALARRLERAKKLQEQREKEMVEKQKQQEIAAAAATGGSVLNVAALLASGTQVTPQIAMAAQMAALQAKALAETGIAVPSYYNPAAVNPMKFAEQEKKRKMLWQGKKEGDKSQSAEIWEKLNFGNKDQNVKFRKLMGIKSEDEAGCSSVDEESYKTLKQQEEVFRNLDAQYEMARSQTHTQRGMGLGFTSSMRGMDAV

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
2	Acetylation	------MAASDTERD ------CCCCCCCCC	18.70	21406692
4	Phosphorylation	----MAASDTERDGL ----CCCCCCCCCCC	35.21	29255136
6	Phosphorylation	--MAASDTERDGLAP --CCCCCCCCCCCCC	30.35	29255136
16	Phosphorylation	DGLAPEKTSPDRDKK CCCCCCCCCCCCHHH	43.78	29255136
17	Phosphorylation	GLAPEKTSPDRDKKK CCCCCCCCCCCHHHH	35.55	29255136
27	Phosphorylation	RDKKKEQSEVSVSPR CHHHHHHCCCCCCHH	40.85	29255136
30	Phosphorylation	KKEQSEVSVSPRASK HHHHCCCCCCHHHHH	16.90	29255136
32	Phosphorylation	EQSEVSVSPRASKHH HHCCCCCCHHHHHHH	10.93	19664994
36	Phosphorylation	VSVSPRASKHHYSRS CCCCHHHHHHHHCHH	33.53	30576142
40	Phosphorylation	PRASKHHYSRSRSRS HHHHHHHHCHHHHHH	12.90	29083192
41	Phosphorylation	RASKHHYSRSRSRSR HHHHHHHCHHHHHHH	21.30	29083192
43	Phosphorylation	SKHHYSRSRSRSRER HHHHHCHHHHHHHHH	28.77	29083192
45	Phosphorylation	HHYSRSRSRSRERKR HHHCHHHHHHHHHHH	35.54	20068231
47	Phosphorylation	YSRSRSRSRERKRKS HCHHHHHHHHHHHHC	39.48	20068231
63	Phosphorylation	NEGRKHRSRSRSKEG CCHHHHHHHHHCHHH	34.04	17081983
65	Phosphorylation	GRKHRSRSRSKEGRR HHHHHHHHHCHHHHC	42.00	17081983
67	Phosphorylation	KHRSRSRSKEGRRHE HHHHHHHCHHHHCCC	35.98	26657352
94	Phosphorylation	EHNDKEHSSDKGRER HCCCCCCCCHHHHHH	41.13	30576142
95	Phosphorylation	HNDKEHSSDKGRERL CCCCCCCCHHHHHHH	45.29	23312004
104	Phosphorylation	KGRERLNSSENGEDR HHHHHHHCCCCCHHH	43.55	29255136
105	Phosphorylation	GRERLNSSENGEDRH HHHHHHCCCCCHHHH	33.73	30266825
126	Phosphorylation	SSRGRSHSRSRSRER HHHCCCHHHHHHHHH	32.95	17081983
128	Phosphorylation	RGRSHSRSRSRERRH HCCCHHHHHHHHHHH	37.31	20068231
130	Phosphorylation	RSHSRSRSRERRHRS CCHHHHHHHHHHHHH	39.48	20068231
137	Phosphorylation	SRERRHRSRSRERKK HHHHHHHHHHHHHHH	28.60	17081983
139	Phosphorylation	ERRHRSRSRERKKSR HHHHHHHHHHHHHHH	39.48	17081983
145	Phosphorylation	RSRERKKSRSRSRER HHHHHHHHHHHHHHH	38.22	26074081
147	Phosphorylation	RERKKSRSRSRERKK HHHHHHHHHHHHHHH	41.52	20068231
149	Phosphorylation	RKKSRSRSRERKKSR HHHHHHHHHHHHHHH	39.48	20068231
155	Phosphorylation	RSRERKKSRSRSRER HHHHHHHHHHHHHHH	38.22	-
157	Phosphorylation	RERKKSRSRSRERKK HHHHHHHHHHHHHHH	41.52	20068231
159	Phosphorylation	RKKSRSRSRERKKSR HHHHHHHHHHHHHHH	39.48	20068231
165	Phosphorylation	RSRERKKSRSRSRER HHHHHHHHHHHHHHH	38.22	26074081
167	Phosphorylation	RERKKSRSRSRERKR HHHHHHHHHHHHHHH	41.52	20068231
169	Phosphorylation	RKKSRSRSRERKRRI HHHHHHHHHHHHHHH	39.48	20068231
198	Phosphorylation	RSRSRTRSRSRDRKK HHHHHHHCHHHHHHH	33.71	20068231
200	Phosphorylation	RSRTRSRSRDRKKRI HHHHHCHHHHHHHHH	39.52	20068231
214	Phosphorylation	IEKPRRFSRSLSRTP HCHHHHHHHHHCCCC	21.10	29116813
216	Phosphorylation	KPRRFSRSLSRTPSP HHHHHHHHHCCCCCC	29.51	23927012
218	Phosphorylation	RRFSRSLSRTPSPPP HHHHHHHCCCCCCCC	35.04	23927012
220	Phosphorylation	FSRSLSRTPSPPPFR HHHHHCCCCCCCCCC	25.41	22167270
222	Phosphorylation	RSLSRTPSPPPFRGR HHHCCCCCCCCCCCC	49.80	22167270
231	Phosphorylation	PPFRGRNTAMDAQEA CCCCCCCCCHHHHHH	23.23	28555341
233	Sulfoxidation	FRGRNTAMDAQEALA CCCCCCCHHHHHHHH	4.06	21406390
317	Phosphorylation	TGIAVPSYYNPAAVN HCCCCCCCCCHHHCC	10.95	22817900
327	Ubiquitination	PAAVNPMKFAEQEKK HHHCCHHHHHHHHHH	42.55	-
333	2-Hydroxyisobutyrylation	MKFAEQEKKRKMLWQ HHHHHHHHHHHHHHC	58.53	-
342	Acetylation	RKMLWQGKKEGDKSQ HHHHHCCCCCCCHHH	32.33	25953088
348	Phosphorylation	GKKEGDKSQSAEIWE CCCCCCHHHHHHHHH	33.82	25627689
350	Phosphorylation	KEGDKSQSAEIWEKL CCCCHHHHHHHHHHH	34.65	25159151
356	Ubiquitination	QSAEIWEKLNFGNKD HHHHHHHHHCCCCCC	33.46	-
362	Ubiquitination	EKLNFGNKDQNVKFR HHHCCCCCCCCCHHH	62.16	-
375	Sumoylation	FRKLMGIKSEDEAGC HHHHHCCCCCCCCCC	41.90	-
375	Sumoylation	FRKLMGIKSEDEAGC HHHHHCCCCCCCCCC	41.90	25114211
376	Phosphorylation	RKLMGIKSEDEAGCS HHHHCCCCCCCCCCC	48.65	23401153
383	Phosphorylation	SEDEAGCSSVDEESY CCCCCCCCCCCHHHH	32.26	25262027
384	Phosphorylation	EDEAGCSSVDEESYK CCCCCCCCCCHHHHH	37.35	25159151
389	Phosphorylation	CSSVDEESYKTLKQQ CCCCCHHHHHHHHHH	29.86	30108239
390	Phosphorylation	SSVDEESYKTLKQQE CCCCHHHHHHHHHHH	15.98	-
391	Ubiquitination	SVDEESYKTLKQQEE CCCHHHHHHHHHHHH	57.57	-
394	Ubiquitination	EESYKTLKQQEEVFR HHHHHHHHHHHHHHH	55.99	-
394	Sumoylation	EESYKTLKQQEEVFR HHHHHHHHHHHHHHH	55.99	-
394	Sumoylation	EESYKTLKQQEEVFR HHHHHHHHHHHHHHH	55.99	-
407	Phosphorylation	FRNLDAQYEMARSQT HHHHHHHHHHHHHCC	14.91	21945579
409	Sulfoxidation	NLDAQYEMARSQTHT HHHHHHHHHHHCCCC	2.98	21406390
418	Methylation	RSQTHTQRGMGLGFT HHCCCCCCCCCCCCC	37.92	54558911
425	Phosphorylation	RGMGLGFTSSMRGMD CCCCCCCCHHHCCCC	20.35	26074081
426	Phosphorylation	GMGLGFTSSMRGMDA CCCCCCCHHHCCCCC	21.63	26074081
427	Phosphorylation	MGLGFTSSMRGMDAV CCCCCCHHHCCCCCC	14.94	26074081
429	Methylation	LGFTSSMRGMDAV-- CCCCHHHCCCCCC--	38.95	115492959

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

Oops, there are no upstream regulatory protein records of RSRC2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RSRC2_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 RSRC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
CKLF5_HUMAN	CMTM5	physical	25416956
KASH5_HUMAN	CCDC155	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

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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-6; THR-16; SER-17; SER-30 AND SER-32, AND MASSSPECTROMETRY.
PubMed: 19413330

Phosphorylation

"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-32, AND MASSSPECTROMETRY.
PubMed: 19690332

"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-6; THR-16; SER-17; SER-30 AND SER-32, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-30 AND SER-32, AND MASSSPECTROMETRY.
PubMed: 18669648

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY.
PubMed: 16964243

"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-4; SER-17; SER-32;SER-104; SER-126; SER-216; SER-218; THR-220 AND SER-222, AND MASSSPECTROMETRY.
PubMed: 17081983