dbPTM

TMCO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TMCO1_HUMAN
UniProt AC	Q9UM00
Protein Name	Calcium load-activated calcium channel {ECO:0000305\|PubMed:27212239}
Gene Name	TMCO1 {ECO:0000312\|HGNC:HGNC:18188}
Organism	Homo sapiens (Human).
Sequence Length	188
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein . Golgi apparatus membrane Multi-pass membrane protein . The first transmembrane region is required for localization to the endoplasmic reticulum (PubMed:27212239). A publication reported
Protein Description	Calcium-selective channel required to prevent calcium stores from overfilling, thereby playing a key role in calcium homeostasis. [PubMed: 27212239 In response to endoplasmic reticulum overloading, assembles into a homotetramer, forming a functional calcium-selective channel, regulating the calcium content in endoplasmic reticulum store]
Protein Sequence	MSTMFADTLLIVFISVCTALLAEGITWVLVYRTDKYKRLKAEVEKQSKKLEKKKETITESAGRQQKKKIERQEEKLKNNNRDLSMVRMKSMFAIGFCFTALMGMFNSIFDGRVVAKLPFTPLSYIQGLSHRNLLGDDTTDCSFIFLYILCTMSIRQNIQKILGLAPSRAATKQAGGFLGPPPPSGKFS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSTMFADTL ------CCCCHHHHH	28.69	24043423
3	Phosphorylation	-----MSTMFADTLL -----CCCCHHHHHH	18.27	24043423
8	Phosphorylation	MSTMFADTLLIVFIS CCCCHHHHHHHHHHH	21.75	24043423
15	Phosphorylation	TLLIVFISVCTALLA HHHHHHHHHHHHHHH	10.32	24043423
18	Phosphorylation	IVFISVCTALLAEGI HHHHHHHHHHHHCCC	20.41	24043423
26	Phosphorylation	ALLAEGITWVLVYRT HHHHCCCCEEEEEEC	22.00	24043423
31	Phosphorylation	GITWVLVYRTDKYKR CCCEEEEEECHHHHH	12.02	24043423
40 (in isoform 1)	Ubiquitination	-	46.67	21890473
40 (in isoform 2)	Ubiquitination	-	46.67	21890473
40	Ubiquitination	TDKYKRLKAEVEKQS CHHHHHHHHHHHHHH	46.67	21906983
45	Ubiquitination	RLKAEVEKQSKKLEK HHHHHHHHHHHHHHH	66.11	-
53	Ubiquitination	QSKKLEKKKETITES HHHHHHHHHHHHHHH	46.60	-
54	Ubiquitination	SKKLEKKKETITESA HHHHHHHHHHHHHHH	71.77	-
56	Phosphorylation	KLEKKKETITESAGR HHHHHHHHHHHHHHH	41.92	25262027
58	Phosphorylation	EKKKETITESAGRQQ HHHHHHHHHHHHHHH	31.16	29255136
60	Phosphorylation	KKETITESAGRQQKK HHHHHHHHHHHHHHH	27.63	23401153
60 (in isoform 2)	Phosphorylation	-	27.63	25849741
91	2-Hydroxyisobutyrylation	SMVRMKSMFAIGFCF HHHHHHHHHHHHHHH	1.88	-
97 (in isoform 2)	Ubiquitination	-	2.21	21890473
105	2-Hydroxyisobutyrylation	FTALMGMFNSIFDGR HHHHHHHHHHHHCCC	5.55	-
109	Phosphorylation	MGMFNSIFDGRVVAK HHHHHHHHCCCEEEE	9.04	18691976
111	Phosphorylation	MFNSIFDGRVVAKLP HHHHHHCCCEEEECC	17.34	19007248
116	Ubiquitination	FDGRVVAKLPFTPLS HCCCEEEECCCCCHH	45.12	21890473
116 (in isoform 1)	Ubiquitination	-	45.12	21890473
120	Phosphorylation	VVAKLPFTPLSYIQG EEEECCCCCHHHHCC	22.75	-
141 (in isoform 2)	Ubiquitination	-	3.17	21890473
153 (in isoform 2)	Ubiquitination	-	9.10	21890473
160	Ubiquitination	SIRQNIQKILGLAPS HHHHHHHHHHCCCCC	35.78	21906983
160 (in isoform 1)	Ubiquitination	-	35.78	21890473
167 (in isoform 2)	Ubiquitination	-	29.01	21890473
171	Phosphorylation	LAPSRAATKQAGGFL CCCCCHHHHHCCCCC	23.78	-
172 (in isoform 1)	Ubiquitination	-	33.16	21890473
172	Ubiquitination	APSRAATKQAGGFLG CCCCHHHHHCCCCCC	33.16	2190698
184	Phosphorylation	FLGPPPPSGKFS--- CCCCCCCCCCCC---	61.46	30266825
186 (in isoform 1)	Ubiquitination	-	46.93	21890473
186	Ubiquitination	GPPPPSGKFS----- CCCCCCCCCC-----	46.93	21890473
188	Phosphorylation	PPPSGKFS------- CCCCCCCC-------	42.68	25463755
235	Phosphorylation	------------------------------------------------------ ------------------------------------------------------		18691976
239	Phosphorylation	---------------------------------------------------------- ----------------------------------------------------------		18691976

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 TMCO1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TMCO1_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 TMCO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AT5F1_HUMAN	ATP5F1	physical	26344197
CY1_HUMAN	CYC1	physical	26344197
DHB12_HUMAN	HSD17B12	physical	26344197
ODPB_HUMAN	PDHB	physical	26344197
RAB1B_HUMAN	RAB1B	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
QCR8_HUMAN	UQCRQ	physical	26344197

Drug and Disease Associations

Kegg Disease
OMIM Disease
213980	Craniofacial dysmorphism, skeletal anomalies and mental retardation syndrome (CFSMR)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TMCO1_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 SER-60 AND SER-188, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-184 AND SER-188,AND MASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.	16565220 [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-60, AND MASSSPECTROMETRY.	17081983 [Abstract]