dbPTM

TRPV5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRPV5_HUMAN
UniProt AC	Q9NQA5
Protein Name	Transient receptor potential cation channel subfamily V member 5
Gene Name	TRPV5
Organism	Homo sapiens (Human).
Sequence Length	729
Subcellular Localization	Apical cell membrane Multi-pass membrane protein . Colocalized with S100A10 and ANAX2 along the apical domain of kidney distal tubular cells (By similarity). The expression of the glycosylated form in the cell membrane is increased in the presence
Protein Description	Constitutively active calcium selective cation channel thought to be involved in Ca(2+) reabsorption in kidney and intestine. [PubMed: 11549322]
Protein Sequence	MGGFLPKAEGPGSQLQKLLPSFLVREQDWDQHLDKLHMLQQKRILESPLLRASKENDLSVLRQLLLDCTCDVRQRGALGETALHIAALYDNLEAALVLMEAAPELVFEPTTCEAFAGQTALHIAVVNQNVNLVRALLTRRASVSARATGTAFRRSPRNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDGHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRRHIQWTYGPLTSILYDLTEIDSWGEELSFLELVVSSDKREARQILEQTPVKELVSFKWNKYGRPYFCILAALYLLYMICFTTCCVYRPLKFRGGNRTHSRDITILQQKLLQEAYETREDIIRLVGELVSIVGAVIILLLEIPDIFRVGASRYFGKTILGGPFHVIIITYASLVLVTMVMRLTNTNGEVVPMSFALVLGWCSVMYFTRGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPTSLGQFYDYPMALFTTFELFLTVIDAPANYDVDLPFMFSIVNFAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKLPRCLWPRSGICGCEFGLGDRWFLRVENHNDQNPLRVLRYVEVFKNSDKEDDQEHPSEKQPSGAESGTLARASLALPTSSLSRTASQSSSHRGWEILRQNTLGHLNLGLNLSEGDGEEVYHF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
42	Acetylation	KLHMLQQKRILESPL HHHHHHHHHHHHCHH	28.57	30593111
47	Phosphorylation	QQKRILESPLLRASK HHHHHHHCHHHHCCC	19.87	22817900
53	Phosphorylation	ESPLLRASKENDLSV HCHHHHCCCCCCHHH	33.78	23186163
59	Phosphorylation	ASKENDLSVLRQLLL CCCCCCHHHHHHHHH	23.20	24719451
142	Phosphorylation	ALLTRRASVSARATG HHHHCCHHHHHHHCC	18.13	-
144	Phosphorylation	LTRRASVSARATGTA HHCCHHHHHHHCCCC	15.00	-
148	Phosphorylation	ASVSARATGTAFRRS HHHHHHHCCCCCCCC	29.52	22210691
150	Phosphorylation	VSARATGTAFRRSPR HHHHHCCCCCCCCCC	20.47	22210691
155	Phosphorylation	TGTAFRRSPRNLIYF CCCCCCCCCCCEEEE	24.77	17081983
299	Phosphorylation	FLELVVSSDKREARQ HHHHHHCCCHHHHHH	35.23	22817900
358	N-linked_Glycosylation	PLKFRGGNRTHSRDI CCCCCCCCCCCCCCH	48.80	18768590
647	Phosphorylation	NPLRVLRYVEVFKNS CCCHHEEEEEHHCCC	9.22	-
654	Phosphorylation	YVEVFKNSDKEDDQE EEEHHCCCCCCCCCC	51.12	22817900
669	Phosphorylation	HPSEKQPSGAESGTL CCCCCCCCCCCCCHH	48.41	22210691
673	Phosphorylation	KQPSGAESGTLARAS CCCCCCCCCHHHHHH	36.22	22210691
675	Phosphorylation	PSGAESGTLARASLA CCCCCCCHHHHHHHC	26.90	22210691
680	Phosphorylation	SGTLARASLALPTSS CCHHHHHHHCCCCCC	14.50	29759185
685	Phosphorylation	RASLALPTSSLSRTA HHHHCCCCCCCCCCC	31.62	18669648
689	Phosphorylation	ALPTSSLSRTASQSS CCCCCCCCCCCCCCC	29.54	18669648
708	Phosphorylation	WEILRQNTLGHLNLG HHHHHHHCCCCEEEC	26.27	21576356

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
299	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
654	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
708	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	UBR4	Q5T4S7	PMID:23747339

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRPV5_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 TRPV5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S10AA_HUMAN	S100A10	physical	12660155
ANXA2_HUMAN	ANXA2	physical	12660155
UBP15_HUMAN	USP15	physical	26186194
TRUA_HUMAN	PUS1	physical	26186194
PSPC1_HUMAN	PSPC1	physical	26186194
STAT3_HUMAN	STAT3	physical	26186194
RPIA_HUMAN	RPIA	physical	26186194
KAISO_HUMAN	ZBTB33	physical	26186194
ATF1_HUMAN	ATF1	physical	26186194
CREB1_HUMAN	CREB1	physical	26186194
TR61B_HUMAN	TRMT61B	physical	26186194
UHRF1_HUMAN	UHRF1	physical	26186194
GSH0_HUMAN	GCLM	physical	26186194
HMGN1_HUMAN	HMGN1	physical	26186194
TYY1_HUMAN	YY1	physical	26186194
NUP53_HUMAN	NUP35	physical	26186194
RN138_HUMAN	RNF138	physical	26186194
ALR_HUMAN	GFER	physical	26186194
UBE3A_HUMAN	UBE3A	physical	26186194
UHRF1_HUMAN	UHRF1	physical	28514442
STAT3_HUMAN	STAT3	physical	28514442
TRUA_HUMAN	PUS1	physical	28514442
RPIA_HUMAN	RPIA	physical	28514442
UBE3A_HUMAN	UBE3A	physical	28514442
GSH0_HUMAN	GCLM	physical	28514442
ATF1_HUMAN	ATF1	physical	28514442
TYY1_HUMAN	YY1	physical	28514442
NUP53_HUMAN	NUP35	physical	28514442
RN138_HUMAN	RNF138	physical	28514442
CREB1_HUMAN	CREB1	physical	28514442
TRPV5_HUMAN	TRPV5	physical	15489237

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 TRPV5_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"WNK3 positively regulates epithelial calcium channels TRPV5 and TRPV6via a kinase-dependent pathway."; Zhang W., Na T., Peng J.B.; Am. J. Physiol. 295:F1472-F1484(2008). Cited for: GLYCOSYLATION AT ASN-358, SUBCELLULAR LOCATION, ENZYME REGULATION, ANDMUTAGENESIS OF ASN-358.	18768590 [Abstract]