dbPTM

PKD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PKD2_HUMAN
UniProt AC	Q13563
Protein Name	Polycystin-2
Gene Name	PKD2 {ECO:0000312\|HGNC:HGNC:9009}
Organism	Homo sapiens (Human).
Sequence Length	968
Subcellular Localization	Cell projection, cilium membrane Multi-pass membrane protein . Endoplasmic reticulum membrane Multi-pass membrane protein . Cell membrane Multi-pass membrane protein . Basolateral cell membrane . Cytoplasmic vesicle membrane . Retained in the e
Protein Description	Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. [PubMed: 18695040 Functions as outward-rectifying K(+) channel, but is also permeable to Ca(2+), and to a much lesser degree also to Na(+)]
Protein Sequence	MVNSSRVQPQQPGDAKRPPAPRAPDPGRLMAGCAAVGASLAAPGGLCEQRGLEIEMQRIRQAAARDPPAGAAASPSPPLSSCSRQAWSRDNPGFEAEEEEEEVEGEEGGMVVEMDVEWRPGSRRSAASSAVSSVGARSRGLGGYHGAGHPSGRRRRREDQGPPCPSPVGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESSTNREKYLKSVLRELVTYLLFLIVLCILTYGMMSSNVYYYTRMMSQLFLDTPVSKTEKTNFKTLSSMEDFWKFTEGSLLDGLYWKMQPSNQTEADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGTRATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLIRYVTTFDFFLAACEIIFCFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLEDQNTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEVKSDLAQQKAEMELSDLIRKGYHKALVKLKLKKNTVDDISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQMRDDLEKEREDLDLDHSSLPRPMSSRSFPRSLDDSEEDDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDERLGRDSEIHREQMERLVREELERWESDDAASQISHGLGTPVGLNGQPRPRSSRPSSSQSTEGMEGAGGNGSSNVHV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
74	Phosphorylation	PPAGAAASPSPPLSS CCCCCCCCCCCCCHH	22.60	29255136
76	Phosphorylation	AGAAASPSPPLSSCS CCCCCCCCCCCHHHC	36.33	29255136
80	Phosphorylation	ASPSPPLSSCSRQAW CCCCCCCHHHCCHHH	34.76	29255136
81	Phosphorylation	SPSPPLSSCSRQAWS CCCCCCHHHCCHHHH	24.64	29255136
83	Phosphorylation	SPPLSSCSRQAWSRD CCCCHHHCCHHHHCC	29.40	29255136
88	Phosphorylation	SCSRQAWSRDNPGFE HHCCHHHHCCCCCCC	32.54	22210691
122	Phosphorylation	DVEWRPGSRRSAASS EEEECCCCCCHHHHH	27.48	22210691
125	Phosphorylation	WRPGSRRSAASSAVS ECCCCCCHHHHHHHH	27.38	21406692
128	Phosphorylation	GSRRSAASSAVSSVG CCCCHHHHHHHHHHH	20.67	22210691
129	Phosphorylation	SRRSAASSAVSSVGA CCCHHHHHHHHHHHH	28.15	21406692
132	Phosphorylation	SAASSAVSSVGARSR HHHHHHHHHHHHHHC	21.01	30576142
133	Phosphorylation	AASSAVSSVGARSRG HHHHHHHHHHHHHCC	20.26	21406692
137	Methylation	AVSSVGARSRGLGGY HHHHHHHHHCCCCCC	22.43	-
138	Phosphorylation	VSSVGARSRGLGGYH HHHHHHHHCCCCCCC	30.11	-
139	Methylation	SSVGARSRGLGGYHG HHHHHHHCCCCCCCC	38.51	115487663
144	Phosphorylation	RSRGLGGYHGAGHPS HHCCCCCCCCCCCCC	8.69	22210691
151	Phosphorylation	YHGAGHPSGRRRRRE CCCCCCCCCCCCCCC	38.98	28857561
166	Phosphorylation	DQGPPCPSPVGGGDP CCCCCCCCCCCCCCC	38.65	29255136
216	Phosphorylation	SSTNREKYLKSVLRE CCCCHHHHHHHHHHH	18.01	27642862
219	Phosphorylation	NREKYLKSVLRELVT CHHHHHHHHHHHHHH	24.64	27642862
254	Phosphorylation	YYYTRMMSQLFLDTP HHHHHHHHHHHCCCC	17.87	22817900
260	Phosphorylation	MSQLFLDTPVSKTEK HHHHHCCCCCCCCCC	27.95	22817900
263	Phosphorylation	LFLDTPVSKTEKTNF HHCCCCCCCCCCCCC	34.75	22817900
299	N-linked_Glycosylation	YWKMQPSNQTEADNR EEEECCCCCCCCCCC	60.52	28092368
305	N-linked_Glycosylation	SNQTEADNRSFIFYE CCCCCCCCCCEEEEC	48.85	28092368
307	Phosphorylation	QTEADNRSFIFYENL CCCCCCCCEEEECCH	29.02	21406692
311	Phosphorylation	DNRSFIFYENLLLGV CCCCEEEECCHHHCC	10.09	21406692
328	N-linked_Glycosylation	IRQLRVRNGSCSIPQ CEEEEECCCCCCCCH	43.82	28092368
362	N-linked_Glycosylation	RAPFGPRNGTAWIYT CCCCCCCCCEEEEEE	56.13	28092368
375	N-linked_Glycosylation	YTSEKDLNGSSHWGI EECCCCCCCCCCEEE	59.44	28092368
408	Phosphorylation	ETAAQVASLKKNVWL HHHHHHHHHHHCEEE	41.69	-
588	Phosphorylation	RTMSQLSTTMSRCAK CHHHHHHHHHHHHHH	34.80	-
591	Phosphorylation	SQLSTTMSRCAKDLF HHHHHHHHHHHHHHH	23.32	-
695	Ubiquitination	KSDLAQQKAEMELSD HHHHHHHHHHHHHHH	33.94	2190698
719	Ubiquitination	LVKLKLKKNTVDDIS HHHHHCCCCCHHHHH	69.18	-
721	Phosphorylation	KLKLKKNTVDDISES HHHCCCCCHHHHHHH	33.90	28857561
726	Phosphorylation	KNTVDDISESLRQGG CCCHHHHHHHHHCCC	28.29	29514088
728	Phosphorylation	TVDDISESLRQGGGK CHHHHHHHHHCCCCC	23.28	29514088
735	Ubiquitination	SLRQGGGKLNFDELR HHHCCCCCCCHHHHH	43.46	-
751	Phosphorylation	DLKGKGHTDAEIEAI HHCCCCCCHHHHHHH	45.64	-
794	Phosphorylation	EDLDLDHSSLPRPMS HHCCCCCCCCCCCCC	32.98	29255136
795	Phosphorylation	DLDLDHSSLPRPMSS HCCCCCCCCCCCCCC	38.69	29255136
801	Phosphorylation	SSLPRPMSSRSFPRS CCCCCCCCCCCCCCC	25.86	21406692
802	Phosphorylation	SLPRPMSSRSFPRSL CCCCCCCCCCCCCCC	26.20	27251275
804	Phosphorylation	PRPMSSRSFPRSLDD CCCCCCCCCCCCCCC	41.36	24719451
808	Phosphorylation	SSRSFPRSLDDSEED CCCCCCCCCCCCCCC	36.07	23927012
812	Phosphorylation	FPRSLDDSEEDDDED CCCCCCCCCCCCCCC	42.42	23927012
820	Phosphorylation	EEDDDEDSGHSSRRR CCCCCCCCCCCCCCC	36.04	23927012
823	Phosphorylation	DDEDSGHSSRRRGSI CCCCCCCCCCCCCCC	29.12	23927012
824	Phosphorylation	DEDSGHSSRRRGSIS CCCCCCCCCCCCCCC	24.92	23927012
829	Phosphorylation	HSSRRRGSISSGVSY CCCCCCCCCCCCCCH	19.93	30266825
831	Phosphorylation	SRRRGSISSGVSYEE CCCCCCCCCCCCHHH	23.80	30266825
832	Phosphorylation	RRRGSISSGVSYEEF CCCCCCCCCCCHHHH	41.36	29255136
835	Phosphorylation	GSISSGVSYEEFQVL CCCCCCCCHHHHHHH	30.28	30108239
836	Phosphorylation	SISSGVSYEEFQVLV CCCCCCCHHHHHHHH	19.64	25850435
852	Phosphorylation	RVDRMEHSIGSIVSK HHHHCHHCHHHHHHH	18.48	29514088
855	Phosphorylation	RMEHSIGSIVSKIDA HCHHCHHHHHHHHHH	20.39	29514088
858	Phosphorylation	HSIGSIVSKIDAVIV HCHHHHHHHHHHHHH	23.40	29514088
898	Phosphorylation	DERLGRDSEIHREQM CHHCCCCCHHHHHHH	36.77	28555341
947	Phosphorylation	RPRSSRPSSSQSTEG CCCCCCCCCCCCCCC	41.32	28555341
948	Phosphorylation	PRSSRPSSSQSTEGM CCCCCCCCCCCCCCC	34.77	28555341
949	Phosphorylation	RSSRPSSSQSTEGME CCCCCCCCCCCCCCC	32.27	18077418
952	Phosphorylation	RPSSSQSTEGMEGAG CCCCCCCCCCCCCCC	28.99	-

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
76	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
801	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
801	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP
801	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
812	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
829	S	Phosphorylation	Kinase	AURA	O14965	PSP
829	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:17636028

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
305	N	Glycosylation	28092368
Thus, glycosylation at Asn-305 is not compatible with glycosylation at Asn-328; only one of these two residues is glycosylated at a given time.
328	N	Glycosylation	19139490
Thus, glycosylation at Asn-305 is not compatible with glycosylation at Asn-328; only one of these two residues is glycosylated at a given time.

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 PKD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PKD2_HUMAN	PKD2	physical	9192675
TRPC1_HUMAN	TRPC1	physical	10097141
TNNI3_HUMAN	TNNI3	physical	12525172
PKD1_HUMAN	PKD1	physical	10097141
PKD1_HUMAN	PKD1	physical	11901144
CALX_HUMAN	CANX	physical	11901144
GOGA2_HUMAN	GOLGA2	physical	11901144
AT1A1_HUMAN	ATP1A1	physical	11901144
PLS1_HUMAN	PLSCR1	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
GCC2_HUMAN	GCC2	physical	27173435

Drug and Disease Associations

Kegg Disease
H00542	Polycystic kidney disease
OMIM Disease
613095	Polycystic kidney disease 2 (PKD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PKD2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; THR-260; SER-263;SER-852 AND SER-858, AND MASS SPECTROMETRY.	17287340 [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-166, AND MASSSPECTROMETRY.	17081983 [Abstract]

show

show