dbPTM

CASQ2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CASQ2_HUMAN
UniProt AC	O14958
Protein Name	Calsequestrin-2
Gene Name	CASQ2
Organism	Homo sapiens (Human).
Sequence Length	399
Subcellular Localization	Sarcoplasmic reticulum lumen . This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells.
Protein Description	Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats..
Protein Sequence	MKRTHLFIVGIYFLSSCRAEEGLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAKLAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDEDDDDDDNSDEEDNDDSDDDDDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	HLFIVGIYFLSSCRA EEEEEEEHHHHHCCC	7.79	25072903
15	Phosphorylation	IVGIYFLSSCRAEEG EEEEHHHHHCCCCCC	19.93	25072903
16	Phosphorylation	VGIYFLSSCRAEEGL EEEHHHHHCCCCCCC	15.12	25072903
36	Phosphorylation	DGKDRVVSLSEKNFK CCCCCEEECCHHHHH	24.26	26437602
38	Phosphorylation	KDRVVSLSEKNFKQV CCCEEECCHHHHHHH	38.73	26437602
97	Acetylation	GFVMVDAKKEAKLAK EEEEEEHHHHHHHHH	46.84	30587425
98	Acetylation	FVMVDAKKEAKLAKK EEEEEHHHHHHHHHH	65.70	30587431
150	Phosphorylation	EDPVEIISSKLEVQA CCCHHHHHCHHHHHH	27.38	28060719
151	Phosphorylation	DPVEIISSKLEVQAF CCHHHHHCHHHHHHH	30.74	28060719
173	Phosphorylation	KLIGFFKSEDSEYYK HHHHCCCCCCHHHHH	41.29	26437602
176	Phosphorylation	GFFKSEDSEYYKAFE HCCCCCCHHHHHHHH	24.36	26437602
178	Phosphorylation	FKSEDSEYYKAFEEA CCCCCHHHHHHHHHH	17.76	26437602
179	Phosphorylation	KSEDSEYYKAFEEAA CCCCHHHHHHHHHHH	7.56	22673903
277	Phosphorylation	IVAFAEKSDPDGYEF EEEEEECCCCCHHHH	45.97	22673903
282	Phosphorylation	EKSDPDGYEFLEILK ECCCCCHHHHHHHHH	15.76	22673903
302	Phosphorylation	NTDNPDLSILWIDPD CCCCCCCEEEEECCC	24.02	18669648
335	N-linked_Glycosylation	RPQIGVVNVTDADSV CCCCCEEEECCCCCE	28.68	UniProtKB CARBOHYD
385	Phosphorylation	DDDDDDNSDEEDNDD CCCCCCCCCCCCCCC	54.09	1985907
393	Phosphorylation	DEEDNDDSDDDDDE- CCCCCCCCCCCCCC-	45.89	15485681

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
385	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
393	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CASQ2_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 CASQ2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRDN_HUMAN	TRDN	physical	11113462
ACTA_HUMAN	ACTA2	physical	26186194
ZFP91_HUMAN	ZFP91	physical	26186194
TF3C2_HUMAN	GTF3C2	physical	26186194
CBX6_HUMAN	CBX6	physical	26186194
CUL7_HUMAN	CUL7	physical	26186194
GTPB6_HUMAN	GTPBP6	physical	26186194
NEB1_HUMAN	PPP1R9A	physical	26186194
NEB2_HUMAN	PPP1R9B	physical	26186194
TF3C3_HUMAN	GTF3C3	physical	26186194
ZBT21_HUMAN	ZBTB21	physical	26186194
TF3C1_HUMAN	GTF3C1	physical	26186194
WDR12_HUMAN	WDR12	physical	26186194
PRD10_HUMAN	PRDM10	physical	26186194
OBSL1_HUMAN	OBSL1	physical	26186194
E41L5_HUMAN	EPB41L5	physical	26186194
E41LB_HUMAN	EPB41L4B	physical	26186194
RIC8B_HUMAN	RIC8B	physical	26186194
SENP5_HUMAN	SENP5	physical	26186194
NOP53_HUMAN	GLTSCR2	physical	26186194
KLH11_HUMAN	KLHL11	physical	26186194
RS15_HUMAN	RPS15	physical	26186194
RM44_HUMAN	MRPL44	physical	26186194
DAXX_HUMAN	DAXX	physical	26186194
RM20_HUMAN	MRPL20	physical	26186194
CCDC8_HUMAN	CCDC8	physical	26186194
PRPF3_HUMAN	PRPF3	physical	26186194
SULF2_HUMAN	SULF2	physical	26186194
ASB1_HUMAN	ASB1	physical	26186194
MARK3_HUMAN	MARK3	physical	26186194
PESC_HUMAN	PES1	physical	26186194
MYCB2_HUMAN	MYCBP2	physical	26186194
TSNA1_HUMAN	TSNARE1	physical	26186194
FBXW8_HUMAN	FBXW8	physical	26186194
RM21_HUMAN	MRPL21	physical	26186194
RM43_HUMAN	MRPL43	physical	26186194
NIN_HUMAN	NIN	physical	26186194
BOP1_HUMAN	BOP1	physical	26186194
DDX51_HUMAN	DDX51	physical	26186194
PLCD3_HUMAN	PLCD3	physical	26186194
RPP38_HUMAN	RPP38	physical	26186194
SGO2_HUMAN	SGOL2	physical	26186194
RM42_HUMAN	MRPL42	physical	26186194
FBX30_HUMAN	FBXO30	physical	26186194
ZBT21_HUMAN	ZBTB21	physical	28514442
ASB1_HUMAN	ASB1	physical	28514442
KLH11_HUMAN	KLHL11	physical	28514442
FBXW8_HUMAN	FBXW8	physical	28514442
E41LB_HUMAN	EPB41L4B	physical	28514442
CUL7_HUMAN	CUL7	physical	28514442
DAXX_HUMAN	DAXX	physical	28514442
PRD10_HUMAN	PRDM10	physical	28514442
MARK3_HUMAN	MARK3	physical	28514442
ZFP91_HUMAN	ZFP91	physical	28514442
TSNA1_HUMAN	TSNARE1	physical	28514442
NEB1_HUMAN	PPP1R9A	physical	28514442
CCDC8_HUMAN	CCDC8	physical	28514442
E41L5_HUMAN	EPB41L5	physical	28514442
SULF2_HUMAN	SULF2	physical	28514442
SGO2_HUMAN	SGOL2	physical	28514442
NIN_HUMAN	NIN	physical	28514442
PLCD3_HUMAN	PLCD3	physical	28514442
BOP1_HUMAN	BOP1	physical	28514442
RS15_HUMAN	RPS15	physical	28514442
RM20_HUMAN	MRPL20	physical	28514442
TF3C2_HUMAN	GTF3C2	physical	28514442
SENP5_HUMAN	SENP5	physical	28514442
NOP53_HUMAN	GLTSCR2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
OBSL1_HUMAN	OBSL1	physical	28514442
NEB2_HUMAN	PPP1R9B	physical	28514442
DDX51_HUMAN	DDX51	physical	28514442
RM44_HUMAN	MRPL44	physical	28514442
WDR12_HUMAN	WDR12	physical	28514442
TF3C3_HUMAN	GTF3C3	physical	28514442
PESC_HUMAN	PES1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611938	Ventricular tachycardia, catecholaminergic polymorphic, 2 (CPVT2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CASQ2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation of human calsequestrin: implications for calciumregulation."; Sanchez E.J., Munske G.R., Criswell A., Milting H., Dunker A.K.,Kang C.; Mol. Cell. Biochem. 353:195-204(2011). Cited for: PHOSPHORYLATION AT SER-385 AND SER-393.	21416293 [Abstract]