dbPTM

CSRP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CSRP1_HUMAN
UniProt AC	P21291
Protein Name	Cysteine and glycine-rich protein 1
Gene Name	CSRP1
Organism	Homo sapiens (Human).
Sequence Length	193
Subcellular Localization	Nucleus .
Protein Description	Could play a role in neuronal development..
Protein Sequence	MPNWGGGKKCGVCQKTVYFAEEVQCEGNSFHKSCFLCMVCKKNLDSTTVAVHGEEIYCKSCYGKKYGPKGYGYGQGAGTLSTDKGESLGIKHEEAPGHRPTTNPNASKFAQKIGGSERCPRCSQAVYAAEKVIGAGKSWHKACFRCAKCGKGLESTTLADKDGEIYCKGCYAKNFGPKGFGFGQGAGALVHSE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Ubiquitination	MPNWGGGKKCGVCQK CCCCCCCCCCCCCCC	48.44	-
8	Succinylation	MPNWGGGKKCGVCQK CCCCCCCCCCCCCCC	48.44	23954790
8	Acetylation	MPNWGGGKKCGVCQK CCCCCCCCCCCCCCC	48.44	7618947
15	Acetylation	KKCGVCQKTVYFAEE CCCCCCCCEEEEEEE	34.53	26051181
15	Ubiquitination	KKCGVCQKTVYFAEE CCCCCCCCEEEEEEE	34.53	-
16	Phosphorylation	KCGVCQKTVYFAEEV CCCCCCCEEEEEEEE	8.44	27251275
18	Phosphorylation	GVCQKTVYFAEEVQC CCCCCEEEEEEEEEE	11.42	28152594
33	Phosphorylation	EGNSFHKSCFLCMVC CCCCCCCCEEEEHHC	11.09	21712546
38	Sulfoxidation	HKSCFLCMVCKKNLD CCCEEEEHHCCCCCC	4.28	21406390
40	S-nitrosylation	SCFLCMVCKKNLDST CEEEEHHCCCCCCCC	1.75	25040305
41	Acetylation	CFLCMVCKKNLDSTT EEEEHHCCCCCCCCE	33.03	26051181
41	2-Hydroxyisobutyrylation	CFLCMVCKKNLDSTT EEEEHHCCCCCCCCE	33.03	-
42	Acetylation	FLCMVCKKNLDSTTV EEEHHCCCCCCCCEE	58.58	26051181
42	Malonylation	FLCMVCKKNLDSTTV EEEHHCCCCCCCCEE	58.58	26320211
46	Phosphorylation	VCKKNLDSTTVAVHG HCCCCCCCCEEEECC	29.19	29759185
47	Phosphorylation	CKKNLDSTTVAVHGE CCCCCCCCEEEECCE	25.59	26657352
57	Phosphorylation	AVHGEEIYCKSCYGK EECCEEEEEEECCCC	9.34	25159151
58	S-nitrosylation	VHGEEIYCKSCYGKK ECCEEEEEEECCCCC	3.00	2212679
59	2-Hydroxyisobutyrylation	HGEEIYCKSCYGKKY CCEEEEEEECCCCCC	26.96	-
59	Ubiquitination	HGEEIYCKSCYGKKY CCEEEEEEECCCCCC	26.96	-
59	Acetylation	HGEEIYCKSCYGKKY CCEEEEEEECCCCCC	26.96	26051181
60	Phosphorylation	GEEIYCKSCYGKKYG CEEEEEEECCCCCCC	14.71	27080861
62	Phosphorylation	EIYCKSCYGKKYGPK EEEEEECCCCCCCCC	38.79	22817900
66	Phosphorylation	KSCYGKKYGPKGYGY EECCCCCCCCCCCCC	41.99	22817900
69	2-Hydroxyisobutyrylation	YGKKYGPKGYGYGQG CCCCCCCCCCCCCCC	61.47	-
69	Ubiquitination	YGKKYGPKGYGYGQG CCCCCCCCCCCCCCC	61.47	2190698
69	Acetylation	YGKKYGPKGYGYGQG CCCCCCCCCCCCCCC	61.47	26051181
71	Phosphorylation	KKYGPKGYGYGQGAG CCCCCCCCCCCCCCC	17.19	24927040
73	Phosphorylation	YGPKGYGYGQGAGTL CCCCCCCCCCCCCEE	9.59	24702127
79	Phosphorylation	GYGQGAGTLSTDKGE CCCCCCCEECCCCCC	19.59	25159151
81	Phosphorylation	GQGAGTLSTDKGESL CCCCCEECCCCCCCC	34.10	25159151
82	Phosphorylation	QGAGTLSTDKGESLG CCCCEECCCCCCCCC	44.86	21815630
84	Acetylation	AGTLSTDKGESLGIK CCEECCCCCCCCCCC	65.74	23954790
84	Malonylation	AGTLSTDKGESLGIK CCEECCCCCCCCCCC	65.74	26320211
84	Ubiquitination	AGTLSTDKGESLGIK CCEECCCCCCCCCCC	65.74	-
84	2-Hydroxyisobutyrylation	AGTLSTDKGESLGIK CCEECCCCCCCCCCC	65.74	-
87	Phosphorylation	LSTDKGESLGIKHEE ECCCCCCCCCCCCCC	40.33	28857561
91	Sumoylation	KGESLGIKHEEAPGH CCCCCCCCCCCCCCC	43.07	28112733
91	Sumoylation	KGESLGIKHEEAPGH CCCCCCCCCCCCCCC	43.07	-
91	Ubiquitination	KGESLGIKHEEAPGH CCCCCCCCCCCCCCC	43.07	-
101	O-linked_Glycosylation	EAPGHRPTTNPNASK CCCCCCCCCCCCHHH	38.88	OGP
101	Phosphorylation	EAPGHRPTTNPNASK CCCCCCCCCCCCHHH	38.88	29449344
102	Phosphorylation	APGHRPTTNPNASKF CCCCCCCCCCCHHHH	51.89	27251275
107	Phosphorylation	PTTNPNASKFAQKIG CCCCCCHHHHHHHHC	34.64	28555341
107	O-linked_Glycosylation	PTTNPNASKFAQKIG CCCCCCHHHHHHHHC	34.64	OGP
108	Ubiquitination	TTNPNASKFAQKIGG CCCCCHHHHHHHHCC	42.16	19608861
108	Acetylation	TTNPNASKFAQKIGG CCCCCHHHHHHHHCC	42.16	23954790
112	Ubiquitination	NASKFAQKIGGSERC CHHHHHHHHCCCCCC	39.63	19608861
112	2-Hydroxyisobutyrylation	NASKFAQKIGGSERC CHHHHHHHHCCCCCC	39.63	-
112	Succinylation	NASKFAQKIGGSERC CHHHHHHHHCCCCCC	39.63	23954790
112	Acetylation	NASKFAQKIGGSERC CHHHHHHHHCCCCCC	39.63	19608861
116	Phosphorylation	FAQKIGGSERCPRCS HHHHHCCCCCCCCHH	19.36	24670416
122	S-nitrosylation	GSERCPRCSQAVYAA CCCCCCCHHHHHHHH	1.82	25040305
123	Phosphorylation	SERCPRCSQAVYAAE CCCCCCHHHHHHHHH	23.58	25159151
127	Phosphorylation	PRCSQAVYAAEKVIG CCHHHHHHHHHHHHC	11.78	28152594
131	Ubiquitination	QAVYAAEKVIGAGKS HHHHHHHHHHCCCCH	34.13	19608861
131	Acetylation	QAVYAAEKVIGAGKS HHHHHHHHHHCCCCH	34.13	19608861
137	2-Hydroxyisobutyrylation	EKVIGAGKSWHKACF HHHHCCCCHHHHHHH	50.25	-
137	Ubiquitination	EKVIGAGKSWHKACF HHHHCCCCHHHHHHH	50.25	-
137	Acetylation	EKVIGAGKSWHKACF HHHHCCCCHHHHHHH	50.25	25953088
138	Phosphorylation	KVIGAGKSWHKACFR HHHCCCCHHHHHHHH	33.23	28857561
141	Acetylation	GAGKSWHKACFRCAK CCCCHHHHHHHHHHC	40.36	26051181
141	2-Hydroxyisobutyrylation	GAGKSWHKACFRCAK CCCCHHHHHHHHHHC	40.36	-
151	Acetylation	FRCAKCGKGLESTTL HHHHCCCCCCCCCCE	70.55	26051181
155	Phosphorylation	KCGKGLESTTLADKD CCCCCCCCCCEECCC	31.56	26657352
156	Phosphorylation	CGKGLESTTLADKDG CCCCCCCCCEECCCC	19.22	21815630
157	Phosphorylation	GKGLESTTLADKDGE CCCCCCCCEECCCCC	29.27	28348404
161	Acetylation	ESTTLADKDGEIYCK CCCCEECCCCCEEEC	63.12	23954790
161	2-Hydroxyisobutyrylation	ESTTLADKDGEIYCK CCCCEECCCCCEEEC	63.12	-
161	Malonylation	ESTTLADKDGEIYCK CCCCEECCCCCEEEC	63.12	26320211
166	Phosphorylation	ADKDGEIYCKGCYAK ECCCCCEEECCCEEC	5.47	22817900
167	S-nitrosylation	DKDGEIYCKGCYAKN CCCCCEEECCCEECC	3.62	2212679
168	Ubiquitination	KDGEIYCKGCYAKNF CCCCEEECCCEECCC	34.74	-
168	Acetylation	KDGEIYCKGCYAKNF CCCCEEECCCEECCC	34.74	25953088
168	2-Hydroxyisobutyrylation	KDGEIYCKGCYAKNF CCCCEEECCCEECCC	34.74	-
168	Malonylation	KDGEIYCKGCYAKNF CCCCEEECCCEECCC	34.74	26320211
171	Phosphorylation	EIYCKGCYAKNFGPK CEEECCCEECCCCCC	29.31	-
173	Ubiquitination	YCKGCYAKNFGPKGF EECCCEECCCCCCCC	26.74	-
173	2-Hydroxyisobutyrylation	YCKGCYAKNFGPKGF EECCCEECCCCCCCC	26.74	-
173	Acetylation	YCKGCYAKNFGPKGF EECCCEECCCCCCCC	26.74	26051181
178	2-Hydroxyisobutyrylation	YAKNFGPKGFGFGQG EECCCCCCCCCCCCC	68.22	-
178	Ubiquitination	YAKNFGPKGFGFGQG EECCCCCCCCCCCCC	68.22	-
178	Acetylation	YAKNFGPKGFGFGQG EECCCCCCCCCCCCC	68.22	23236377
192	O-linked_Glycosylation	GAGALVHSE------ CCCCCCCCC------	37.21	31373491
192	Phosphorylation	GAGALVHSE------ CCCCCCCCC------	37.21	19664994

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 CSRP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CSRP1_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 CSRP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSRP1_HUMAN	CSRP1	physical	7938009
A4_HUMAN	APP	physical	21832049
YBOX3_HUMAN	YBX3	physical	22863883
MACF1_HUMAN	MACF1	physical	22863883
KAP2_HUMAN	PRKAR2A	physical	22863883
FUBP3_HUMAN	FUBP3	physical	26344197
TALDO_HUMAN	TALDO1	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 CSRP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-131, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-192, 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-192, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASSSPECTROMETRY.	18220336 [Abstract]
"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-192, AND MASSSPECTROMETRY.	16964243 [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-192, AND MASSSPECTROMETRY.	17081983 [Abstract]