dbPTM

CRCM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CRCM1_HUMAN
UniProt AC	Q96D31
Protein Name	Calcium release-activated calcium channel protein 1
Gene Name	ORAI1
Organism	Homo sapiens (Human).
Sequence Length	301
Subcellular Localization	Cell membrane Multi-pass membrane protein . Isoform beta is more mobile in the plasma membrane (PubMed:23307288). Colocalizes with STIM1 at the cell membrane (PubMed:27185316).
Protein Description	Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which mediates Ca(2+) influx following depletion of intracellular Ca(2+) stores and channel activation by the Ca(2+) sensor, STIM1. [PubMed: 16582901]
Protein Sequence	MHPEPAPPPSRSSPELPPSGGSTTSGSRRSRRRSGDGEPPGAPPPPPSAVTYPDWIGQSYSEVMSLNEHSMQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLDADHDYPPGLLIAFSACTTVLVAVHLFALMISTCILPNIEAVSNVHNLNSVKESPHERMHRHIELAWAFSTVIGTLLFLAEVVLLCWVKFLPLKKQPGQPRPTSKPPASGAAANVSTSGITPGQAAAIASTTIMVPFGLIFIVFAVHFYRSLVSHKTDRQFQELNELAEFARLQDQLDHRGDHPLTPGSHYA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	PEPAPPPSRSSPELP CCCCCCCCCCCCCCC	51.04	23401153
12	Phosphorylation	PAPPPSRSSPELPPS CCCCCCCCCCCCCCC	55.36	28450419
13	Phosphorylation	APPPSRSSPELPPSG CCCCCCCCCCCCCCC	22.68	28450419
19	Phosphorylation	SSPELPPSGGSTTSG CCCCCCCCCCCCCCC	54.57	28270605
22	Phosphorylation	ELPPSGGSTTSGSRR CCCCCCCCCCCCCCC	31.85	28270605
23	Phosphorylation	LPPSGGSTTSGSRRS CCCCCCCCCCCCCCC	28.40	28270605
24	Phosphorylation	PPSGGSTTSGSRRSR CCCCCCCCCCCCCCC	32.56	28270605
25	Phosphorylation	PSGGSTTSGSRRSRR CCCCCCCCCCCCCCC	34.55	28270605
27	Phosphorylation	GGSTTSGSRRSRRRS CCCCCCCCCCCCCCC	25.04	22817900
30	Phosphorylation	TTSGSRRSRRRSGDG CCCCCCCCCCCCCCC	29.09	22817900
34	Phosphorylation	SRRSRRRSGDGEPPG CCCCCCCCCCCCCCC	39.15	-
65	Phosphorylation	QSYSEVMSLNEHSMQ CCHHHHHHCCHHHHH	32.97	28270605
67	Phosphorylation	YSEVMSLNEHSMQAL HHHHHHCCHHHHHHH	37.31	18578522
70	Phosphorylation	VMSLNEHSMQALSWR HHHCCHHHHHHHHHH	13.35	29083192
75	Phosphorylation	EHSMQALSWRKLYLS HHHHHHHHHHHHHHH	28.05	24719451
80	Ubiquitination	ALSWRKLYLSRAKLK HHHHHHHHHHHHHHH	12.98	-
159	Phosphorylation	SNVHNLNSVKESPHE HCCCCCCCCCCCHHH	37.42	24719451
223	N-linked_Glycosylation	PASGAAANVSTSGIT CCCCCCCCCCCCCCC	24.44	26956484
225	N-linked_Glycosylation	SGAAANVSTSGITPG CCCCCCCCCCCCCHH	19.36	17293345
225	N-linked_Glycosylation	SGAAANVSTSGITPG CCCCCCCCCCCCCHH	19.36	17293345
295	Phosphorylation	HRGDHPLTPGSHYA- HCCCCCCCCCCCCC-	30.01	23401153
297	Phosphorylation	GDHPLTPGSHYA--- CCCCCCCCCCCC---	23.09	20068231
298	Phosphorylation	DHPLTPGSHYA---- CCCCCCCCCCC----	17.96	30266825
300	Phosphorylation	PLTPGSHYA------ CCCCCCCCC------	18.72	30266825
302	Phosphorylation	TPGSHYA-------- CCCCCCC--------		-

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
27	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
30	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
34	S	Phosphorylation	Kinase	PKACA	P17612	PSP
34	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4L	Q96PU5	PMID:22682960

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
195	C	Oxidation		20354224
Cys-195 is oxidated, leading to inactivation of channel activity.

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 CRCM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CRCM1_HUMAN !!

Drug and Disease Associations

Kegg Disease
H00093	Combined immunodeficiencies (CIDs), including the following nine diseases: X-linked hyper IgM syndro
OMIM Disease
612782	Immunodeficiency 9 (IMD9)
615883	Myopathy, tubular aggregate, 2 (TAM2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CRCM1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-295 AND SER-298, ANDMASS SPECTROMETRY.	18669648 [Abstract]

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