dbPTM

TRPC6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRPC6_HUMAN
UniProt AC	Q9Y210
Protein Name	Short transient receptor potential channel 6
Gene Name	TRPC6 {ECO:0000303\|PubMed:9930701, ECO:0000312\|HGNC:HGNC:12338}
Organism	Homo sapiens (Human).
Sequence Length	931
Subcellular Localization	Cell membrane Multi-pass membrane protein .
Protein Description	Thought to form a receptor-activated non-selective calcium permeant cation channel. [PubMed: 19936226]
Protein Sequence	MSQSPAFGPRRGSSPRGAAGAAARRNESQDYLLMDSELGEDGCPQAPLPCYGYYPCFRGSDNRLAHRRQTVLREKGRRLANRGPAYMFSDRSTSLSIEEERFLDAAEYGNIPVVRKMLEECHSLNVNCVDYMGQNALQLAVANEHLEITELLLKKENLSRVGDALLLAISKGYVRIVEAILSHPAFAEGKRLATSPSQSELQQDDFYAYDEDGTRFSHDVTPIILAAHCQEYEIVHTLLRKGARIERPHDYFCKCNDCNQKQKHDSFSHSRSRINAYKGLASPAYLSLSSEDPVMTALELSNELAVLANIEKEFKNDYKKLSMQCKDFVVGLLDLCRNTEEVEAILNGDVETLQSGDHGRPNLSRLKLAIKYEVKKFVAHPNCQQQLLSIWYENLSGLRQQTMAVKFLVVLAVAIGLPFLALIYWFAPCSKMGKIMRGPFMKFVAHAASFTIFLGLLVMNAADRFEGTKLLPNETSTDNAKQLFRMKTSCFSWMEMLIISWVIGMIWAECKEIWTQGPKEYLFELWNMLDFGMLAIFAASFIARFMAFWHASKAQSIIDANDTLKDLTKVTLGDNVKYYNLARIKWDPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYIGAKQNEAFTTVEESFKTLFWAIFGLSEVKSVVINYNHKFIENIGYVLYGVYNVTMVIVLLNMLIAMINSSFQEIEDDADVEWKFARAKLWFSYFEEGRTLPVPFNLVPSPKSLFYLLLKLKKWISELFQGHKKGFQEDAEMNKINEEKKLGILGSHEDLSKLSLDKKQVGHNKQPSIRSSEDFHLNSFNNPPRQYQKIMKRLIKRYVLQAQIDKESDEVNEGELKEIKQDISSLRYELLEEKSQNTEDLAELIRELGEKLSMEPNQEETNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSQSPAFGP ------CCCCCCCCC	39.09	28270605
4	Phosphorylation	----MSQSPAFGPRR ----CCCCCCCCCCC	15.76	28270605
13	Phosphorylation	AFGPRRGSSPRGAAG CCCCCCCCCCCCHHH	35.04	22817900
14	Phosphorylation	FGPRRGSSPRGAAGA CCCCCCCCCCCHHHH	22.80	22817900
28	Phosphorylation	AAARRNESQDYLLMD HHHHCCCCCCEEEEC	31.72	22210691
31	Phosphorylation	RRNESQDYLLMDSEL HCCCCCCEEEECCCC	8.29	22817900
70	Phosphorylation	RLAHRRQTVLREKGR HHHHHHHHHHHHHHH	21.50	17081983
92	Phosphorylation	AYMFSDRSTSLSIEE CCCCCCCCCCCCCCH	27.60	26699800
93	Phosphorylation	YMFSDRSTSLSIEEE CCCCCCCCCCCCCHH	34.28	26699800
94	Phosphorylation	MFSDRSTSLSIEEER CCCCCCCCCCCCHHH	22.74	26699800
96	Phosphorylation	SDRSTSLSIEEERFL CCCCCCCCCCHHHHH	27.93	26699800
108	Phosphorylation	RFLDAAEYGNIPVVR HHHHHHHHCCHHHHH	15.67	-
194	Phosphorylation	AEGKRLATSPSQSEL HCCCCCCCCCCHHHH	45.84	28270605
195	Phosphorylation	EGKRLATSPSQSELQ CCCCCCCCCCHHHHH	19.56	28270605
197	Phosphorylation	KRLATSPSQSELQQD CCCCCCCCHHHHHCC	46.21	26657352
199	Phosphorylation	LATSPSQSELQQDDF CCCCCCHHHHHCCCC	44.61	26657352
207	Phosphorylation	ELQQDDFYAYDEDGT HHHCCCCEEECCCCC	15.96	28270605
237	Phosphorylation	QEYEIVHTLLRKGAR CHHHHHHHHHHCCCC	19.32	24260401
270	Phosphorylation	KHDSFSHSRSRINAY CCCCCCCHHHHHHHH	30.65	-
272	Phosphorylation	DSFSHSRSRINAYKG CCCCCHHHHHHHHCC	40.29	-
282	Phosphorylation	NAYKGLASPAYLSLS HHHCCCCCCHHHHCC	18.33	-
285	Phosphorylation	KGLASPAYLSLSSED CCCCCCHHHHCCCCC	10.54	-
318	Phosphorylation	EKEFKNDYKKLSMQC HHHHHHHHHHHHHHH	21.29	29759185
322	Phosphorylation	KNDYKKLSMQCKDFV HHHHHHHHHHHHHHH	18.71	22817900
396	Phosphorylation	SIWYENLSGLRQQTM HHHHHCCCCHHHHHH	47.57	24719451
473	N-linked_Glycosylation	EGTKLLPNETSTDNA CCCCCCCCCCCCCCH	66.21	17660510
561	N-linked_Glycosylation	AQSIIDANDTLKDLT HHHHHCCCCHHHHHC	38.77	17660510
606	Phosphorylation	YAIAVVLSFSRIAYI HHHHHHHHHHHEEEE	15.01	-
612	Phosphorylation	LSFSRIAYILPANES HHHHHEEEEEECCCC	10.71	-
630	Phosphorylation	LQISLGRTVKDIFKF CCCCCCCHHHHHHHH	30.06	-
759	Phosphorylation	SYFEEGRTLPVPFNL HHCCCCCCCCCCCCC	46.39	-
769	Phosphorylation	VPFNLVPSPKSLFYL CCCCCCCCHHHHHHH	37.16	21815630
775	Phosphorylation	PSPKSLFYLLLKLKK CCHHHHHHHHHHHHH	11.18	-
785	Phosphorylation	LKLKKWISELFQGHK HHHHHHHHHHHHHHH	27.42	-
815	Phosphorylation	KKLGILGSHEDLSKL HHHCCCCCHHHHHHC	21.91	23401153
820	Phosphorylation	LGSHEDLSKLSLDKK CCCHHHHHHCCCCHH	43.82	28060719
823	Phosphorylation	HEDLSKLSLDKKQVG HHHHHHCCCCHHHCC	37.95	28060719
836	Phosphorylation	VGHNKQPSIRSSEDF CCCCCCCCCCCCCCC	28.30	24719451
839	Phosphorylation	NKQPSIRSSEDFHLN CCCCCCCCCCCCCCC	36.09	28060719
840	Phosphorylation	KQPSIRSSEDFHLNS CCCCCCCCCCCCCCC	31.19	33259812
847	Phosphorylation	SEDFHLNSFNNPPRQ CCCCCCCCCCCCHHH	35.39	28060719
892	Phosphorylation	KEIKQDISSLRYELL HHHHHHHHHHHHHHH	31.45	24719451
893	Phosphorylation	EIKQDISSLRYELLE HHHHHHHHHHHHHHH	19.73	25954137
896	Phosphorylation	QDISSLRYELLEEKS HHHHHHHHHHHHHHC	19.07	-
903	Phosphorylation	YELLEEKSQNTEDLA HHHHHHHCCCHHHHH	31.76	28270605

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
14	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
70	T	Phosphorylation	Kinase	PKACA	P17612	PSP
70	T	Phosphorylation	Kinase	PRKG1	Q13976	GPS
322	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRPC6_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 TRPC6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FYN_HUMAN	FYN	physical	14761972
TRPC6_HUMAN	TRPC6	physical	12032305
TRPC7_HUMAN	TRPC7	physical	12032305
RNF24_HUMAN	RNF24	physical	17850865

Drug and Disease Associations

Kegg Disease
H00626	Nephrotic syndrome and focal segmental glomerulosclerosis
OMIM Disease
603965	Focal segmental glomerulosclerosis 2 (FSGS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TRPC6_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-815 AND SER-839, ANDMASS SPECTROMETRY.	18088087 [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 THR-70, AND MASSSPECTROMETRY.	17081983 [Abstract]