dbPTM

CHSP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CHSP1_HUMAN
UniProt AC	Q9Y2V2
Protein Name	Calcium-regulated heat-stable protein 1
Gene Name	CARHSP1
Organism	Homo sapiens (Human).
Sequence Length	147
Subcellular Localization	Cytoplasm . Cytoplasm, P-body . Cytoplasmic granule . Detected at cytoplasmic stress granules and P-bodies. Detected at exosome granules where mRNA is degraded (By similarity)..
Protein Description	Binds mRNA and regulates the stability of target mRNA. Binds single-stranded DNA (in vitro)..
Protein Sequence	MSSEPPPPPQPPTHQASVGLLDTPRSRERSPSPLRGNVVPSPLPTRRTRTFSATVRASQGPVYKGVCKCFCRSKGHGFITPADGGPDIFLHISDVEGEYVPVEGDEVTYKMCSIPPKNEKLQAVEVVITHLAPGTKHETWSGHVISS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSEPPPPP ------CCCCCCCCC	43.33	28464451
2	Acetylation	------MSSEPPPPP ------CCCCCCCCC	43.33	21406692
3	Phosphorylation	-----MSSEPPPPPQ -----CCCCCCCCCC	53.47	28464451
13	Phosphorylation	PPPPQPPTHQASVGL CCCCCCCCCCCCEEC	33.05	22167270
17	Phosphorylation	QPPTHQASVGLLDTP CCCCCCCCEECCCCC	15.33	29255136
23	Phosphorylation	ASVGLLDTPRSRERS CCEECCCCCCCCCCC	22.14	29255136
26	Phosphorylation	GLLDTPRSRERSPSP ECCCCCCCCCCCCCC	39.43	23401153
30	Phosphorylation	TPRSRERSPSPLRGN CCCCCCCCCCCCCCC	25.61	29255136
32	Phosphorylation	RSRERSPSPLRGNVV CCCCCCCCCCCCCCC	37.50	29255136
41	Phosphorylation	LRGNVVPSPLPTRRT CCCCCCCCCCCCCCE	27.71	19664994
45	Phosphorylation	VVPSPLPTRRTRTFS CCCCCCCCCCEEEEE	40.23	22167270
45	O-linked_Glycosylation	VVPSPLPTRRTRTFS CCCCCCCCCCEEEEE	40.23	OGP
48	Phosphorylation	SPLPTRRTRTFSATV CCCCCCCEEEEEEEE	30.67	26503892
49	Methylation	PLPTRRTRTFSATVR CCCCCCEEEEEEEEE	31.78	-
50	Phosphorylation	LPTRRTRTFSATVRA CCCCCEEEEEEEEEH	22.71	29255136
52	Phosphorylation	TRRTRTFSATVRASQ CCCEEEEEEEEEHHC	23.55	29255136
54	Phosphorylation	RTRTFSATVRASQGP CEEEEEEEEEHHCCC	14.88	29255136
58	Phosphorylation	FSATVRASQGPVYKG EEEEEEHHCCCEEEE	25.71	25159151
63	Phosphorylation	RASQGPVYKGVCKCF EHHCCCEEEEEEEEE	12.73	20068231
64	Ubiquitination	ASQGPVYKGVCKCFC HHCCCEEEEEEEEEE	45.13	22817900
64	Acetylation	ASQGPVYKGVCKCFC HHCCCEEEEEEEEEE	45.13	25953088
64	2-Hydroxyisobutyrylation	ASQGPVYKGVCKCFC HHCCCEEEEEEEEEE	45.13	-
68	Acetylation	PVYKGVCKCFCRSKG CEEEEEEEEEECCCC	28.12	25953088
68	2-Hydroxyisobutyrylation	PVYKGVCKCFCRSKG CEEEEEEEEEECCCC	28.12	-
68	Ubiquitination	PVYKGVCKCFCRSKG CEEEEEEEEEECCCC	28.12	22817900
74	Malonylation	CKCFCRSKGHGFITP EEEEECCCCCEEEEC	35.26	26320211
74	Ubiquitination	CKCFCRSKGHGFITP EEEEECCCCCEEEEC	35.26	29967540
74	Acetylation	CKCFCRSKGHGFITP EEEEECCCCCEEEEC	35.26	26051181
80	Phosphorylation	SKGHGFITPADGGPD CCCCEEEECCCCCCC	15.34	27251275
85	Ubiquitination	FITPADGGPDIFLHI EEECCCCCCCEEEEE	19.77	21890473
89	Ubiquitination	ADGGPDIFLHISDVE CCCCCCEEEEEECCC	5.46	22817900
93	Phosphorylation	PDIFLHISDVEGEYV CCEEEEEECCCCCEE	25.51	27642862
99	Phosphorylation	ISDVEGEYVPVEGDE EECCCCCEECCCCCE	22.40	28796482
108	Phosphorylation	PVEGDEVTYKMCSIP CCCCCEEEEEEECCC	18.51	27642862
109	Phosphorylation	VEGDEVTYKMCSIPP CCCCEEEEEEECCCC	11.25	27642862
110	Ubiquitination	EGDEVTYKMCSIPPK CCCEEEEEEECCCCC	24.86	29967540
117	Ubiquitination	KMCSIPPKNEKLQAV EEECCCCCCCCCCEE	72.83	29967540
120	2-Hydroxyisobutyrylation	SIPPKNEKLQAVEVV CCCCCCCCCCEEEEE	56.12	-
120	Acetylation	SIPPKNEKLQAVEVV CCCCCCCCCCEEEEE	56.12	25953088
120	Ubiquitination	SIPPKNEKLQAVEVV CCCCCCCCCCEEEEE	56.12	33845483
129	O-linked_Glycosylation	QAVEVVITHLAPGTK CEEEEEEEECCCCCC	10.14	OGP
135	O-linked_Glycosylation	ITHLAPGTKHETWSG EEECCCCCCCCCEEC	28.33	OGP
139	Phosphorylation	APGTKHETWSGHVIS CCCCCCCCEECCCCC	25.34	29396449
141	O-linked_Glycosylation	GTKHETWSGHVISS- CCCCCCEECCCCCC-	26.83	OGP
141	Phosphorylation	GTKHETWSGHVISS- CCCCCCEECCCCCC-	26.83	25159151
146	Phosphorylation	TWSGHVISS------ CEECCCCCC------	28.98	25159151
147	Phosphorylation	WSGHVISS------- EECCCCCC-------	32.87	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
23	T	Phosphorylation	Kinase	CDK1	P06493	PSP
30	S	Phosphorylation	Kinase	DYRK2	Q92630	PSP
32	S	Phosphorylation	Kinase	DYRK2	Q92630	PSP
41	S	Phosphorylation	Kinase	DYRK2	Q92630	PSP
52	S	Phosphorylation	Kinase	AKT1	P31749	PSP
52	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
52	S	Phosphorylation	Kinase	SGK1	O00141	PSP
52	S	Phosphorylation	Kinase	SGK-FAMILY	-	GPS
52	S	Phosphorylation	Kinase	SGK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CHSP1_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 CHSP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STC2_HUMAN	STC2	physical	16169070
DOCK8_HUMAN	DOCK8	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
FKBP2_HUMAN	FKBP2	physical	26344197
IMPA2_HUMAN	IMPA2	physical	26344197
PCBP1_HUMAN	PCBP1	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 CHSP1_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-41, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-52, AND MASSSPECTROMETRY.	19413330 [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-30; SER-32; SER-41;SER-52; SER-146 AND SER-147, AND MASS SPECTROMETRY.	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-41; SER-146 AND SER-147,AND MASS SPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-52, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32; SER-41 ANDSER-52, AND MASS SPECTROMETRY.	18187866 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32 AND SER-41,AND MASS SPECTROMETRY.	17287340 [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-41 AND SER-52, 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-30; SER-32 AND SER-41,AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASSSPECTROMETRY.	15302935 [Abstract]