dbPTM

NPHP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NPHP1_HUMAN
UniProt AC	O15259
Protein Name	Nephrocystin-1
Gene Name	NPHP1
Organism	Homo sapiens (Human).
Sequence Length	732
Subcellular Localization	Cell junction, adherens junction. Cell projection, cilium. Cytoplasm, cytoskeleton, cilium axoneme. Cell junction, tight junction. Colocalizes with E-cadherin and BCAR1 at or near the cell-cell adherens junctions (By similarity). Localized to respira
Protein Description	Together with BCAR1 it may play a role in the control of epithelial cell polarity. Involved in the organization of apical junctions in kidney cells together with NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). Seems to help to recruit PTK2B/PYK2 to cell matrix adhesions, thereby initiating phosphorylation of PTK2B/PYK2 and PTK2B/PYK2-dependent signaling. May play a role in the regulation of intraflagellar transport (IFT) during cilia assembly. Required for normal retina development. In connecting photoreceptor cilia influences the movement of some IFT proteins such as IFT88 and WDR19. Involved in spermatogenesis (By similarity)..
Protein Sequence	MLARRQRDPLQALRRRNQELKQQVDSLLSESQLKEALEPNKRQHIYQRCIQLKQAIDENKNALQKLSKADESAPVANYNQRKEEEHTLLDKLTQQLQGLAVTISRENITEVGAPTEEEEESESEDSEDSGGEEEDAEEEEEEKEENESHKWSTGEEYIAVGDFTAQQVGDLTFKKGEILLVIEKKPDGWWIAKDAKGNEGLVPRTYLEPYSEEEEGQESSEEGSEEDVEAVDETADGAEVKQRTDPHWSAVQKAISEAGIFCLVNHVSFCYLIVLMRNRMETVEDTNGSETGFRAWNVQSRGRIFLVSKPVLQINTVDVLTTMGAIPAGFRPSTLSQLLEEGNQFRANYFLQPELMPSQLAFRDLMWDATEGTIRSRPSRISLILTLWSCKMIPLPGMSIQVLSRHVRLCLFDGNKVLSNIHTVRATWQPKKPKTWTFSPQVTRILPCLLDGDCFIRSNSASPDLGILFELGISYIRNSTGERGELSCGWVFLKLFDASGVPIPAKTYELFLNGGTPYEKGIEVDPSISRRAHGSVFYQIMTMRRQPQLLVKLRSLNRRSRNVLSLLPETLIGNMCSIHLLIFYRQILGDVLLKDRMSLQSTDLISHPMLATFPMLLEQPDVMDALRSSWAGKESTLKRSEKRDKEFLKSTFLLVYHDCVLPLLHSTRLPPFRWAEEETETARWKVITDFLKQNQENQGALQALLSPDGVHEPFDLSEQTYDFLGEMRKNAV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
46	Phosphorylation	PNKRQHIYQRCIQLK CHHHHHHHHHHHHHH	6.43	21357692
60	Ubiquitination	KQAIDENKNALQKLS HHHHHHCHHHHHHHH	41.36	-
68	Ubiquitination	NALQKLSKADESAPV HHHHHHHHHCCCCCC	71.00	-
102	Phosphorylation	QLQGLAVTISRENIT HHHHHEEEEECCCCC	13.97	-
104	Phosphorylation	QGLAVTISRENITEV HHHEEEEECCCCCCC	24.95	-
121	Phosphorylation	PTEEEEESESEDSED CCHHHHHHCCCCCCC	50.10	16308564
123	Phosphorylation	EEEEESESEDSEDSG HHHHHHCCCCCCCCC	56.85	16308564
126	Phosphorylation	EESESEDSEDSGGEE HHHCCCCCCCCCCCC	38.97	16308564
193	Acetylation	PDGWWIAKDAKGNEG CCCEEEEECCCCCCC	49.43	18530233
196	Acetylation	WWIAKDAKGNEGLVP EEEEECCCCCCCCCC	72.85	18530241
300	Phosphorylation	FRAWNVQSRGRIFLV EEEEEEECCCEEEEE	32.21	28509920
349	Phosphorylation	GNQFRANYFLQPELM CCCCCCEECCCCCCC	12.51	28270605
376	Phosphorylation	ATEGTIRSRPSRISL CCCCCCCCCHHHHHH	44.70	-
379	Phosphorylation	GTIRSRPSRISLILT CCCCCCHHHHHHHHH	40.93	-
399	Phosphorylation	MIPLPGMSIQVLSRH CCCCCCCCHHHHHCC	18.78	26503892
402 (in isoform 3)	Ubiquitination	-	5.09	21906983
404	Phosphorylation	GMSIQVLSRHVRLCL CCCHHHHHCCEEEEE	22.83	26503892
439	Phosphorylation	KPKTWTFSPQVTRIL CCCCCEECCCHHHHH	13.67	23828894
460	Phosphorylation	DCFIRSNSASPDLGI CEEEECCCCCCCHHH	31.22	-
464 (in isoform 2)	Ubiquitination	-	55.84	21906983
474	Phosphorylation	ILFELGISYIRNSTG HHHHHHCCCHHCCCC	16.83	-
487	Phosphorylation	TGERGELSCGWVFLK CCCCCEECCEEEEEE	13.28	28842319
508	Phosphorylation	VPIPAKTYELFLNGG CCCCCEEEEEHHCCC	15.21	29759185
515 (in isoform 3)	Ubiquitination	-	23.57	21906983
520 (in isoform 1)	Ubiquitination	-	60.38	21906983
520	Ubiquitination	NGGTPYEKGIEVDPS CCCCCCCCCCCCCCC	60.38	21906983
521 (in isoform 4)	Ubiquitination	-	14.89	21906983
542	Phosphorylation	SVFYQIMTMRRQPQL CHHHHHHHCCCCCHH	14.78	-
577 (in isoform 2)	Ubiquitination	-	11.41	21906983
601	Phosphorylation	KDRMSLQSTDLISHP HCCCCCCCCCCCCCH	29.22	-
633	Ubiquitination	LRSSWAGKESTLKRS HHHCCCCCHHHCCHH	40.52	2190698
633 (in isoform 1)	Ubiquitination	-	40.52	21906983
634 (in isoform 4)	Ubiquitination	-	48.30	21906983
635	Phosphorylation	SSWAGKESTLKRSEK HCCCCCHHHCCHHHH	42.39	29449344
636	Phosphorylation	SWAGKESTLKRSEKR CCCCCHHHCCHHHHH	37.07	29449344
640	Phosphorylation	KESTLKRSEKRDKEF CHHHCCHHHHHHHHH	45.97	29449344
721	Phosphorylation	FDLSEQTYDFLGEMR CCCCHHHHHHHHHHH	12.37	15723349

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
46	Y	Phosphorylation	Kinase	PTK2B	Q14289	GPS
121	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
121	S	Phosphorylation	Kinase	CK2	-	Uniprot
123	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
123	S	Phosphorylation	Kinase	CK2	-	Uniprot
126	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
126	S	Phosphorylation	Kinase	CK2	-	Uniprot
349	Y	Phosphorylation	Kinase	PTK2B	Q14289	GPS
721	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NPHP1_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 NPHP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
INVS_HUMAN	INVS	physical	12872123
TBB5_HUMAN	TUBB	physical	12872123
NPHP1_HUMAN	NPHP1	physical	12006559
FLNA_HUMAN	FLNA	physical	12006559
FLNB_HUMAN	FLNB	physical	12006559
BCAR1_HUMAN	BCAR1	physical	10739664
NPHP4_HUMAN	NPHP4	physical	12244321
FAK2_HUMAN	PTK2B	physical	11493697
TENS1_HUMAN	TNS1	physical	11493697
BCAR1_HUMAN	BCAR1	physical	11493697
ACK1_HUMAN	TNK2	physical	18477472
BCAR1_HUMAN	BCAR1	physical	18477472
RHG32_HUMAN	ARHGAP32	physical	18477472
CE164_HUMAN	CEP164	physical	22863007
AGK_HUMAN	AGK	physical	26638075
AT2B1_HUMAN	ATP2B1	physical	26638075
BI2L1_HUMAN	BAIAP2L1	physical	26638075
BCAS3_HUMAN	BCAS3	physical	26638075
TM256_HUMAN	TMEM256	physical	26638075
CYBP_HUMAN	CACYBP	physical	26638075
CBL_HUMAN	CBL	physical	26638075
CE170_HUMAN	CEP170	physical	26638075
CHTOP_HUMAN	CHTOP	physical	26638075
CLH1_HUMAN	CLTC	physical	26638075
COPA_HUMAN	COPA	physical	26638075
ODB2_HUMAN	DBT	physical	26638075
DYN2_HUMAN	DNM2	physical	26638075
DNMBP_HUMAN	DNMBP	physical	26638075
DYHC1_HUMAN	DYNC1H1	physical	26638075
ECD_HUMAN	ECD	physical	26638075
FCHO2_HUMAN	FCHO2	physical	26638075
FKBP4_HUMAN	FKBP4	physical	26638075
GARS_HUMAN	GARS	physical	26638075
GPTC1_HUMAN	GPATCH1	physical	26638075
HXK1_HUMAN	HK1	physical	26638075
HSDL2_HUMAN	HSDL2	physical	26638075
HYOU1_HUMAN	HYOU1	physical	26638075
IDH3B_HUMAN	IDH3B	physical	26638075
IQGA1_HUMAN	IQGAP1	physical	26638075
ERD22_HUMAN	KDELR2	physical	26638075
PHOCN_HUMAN	MOB4	physical	26638075
SYNC_HUMAN	NARS	physical	26638075
NDUS3_HUMAN	NDUFS3	physical	26638075
NDUV1_HUMAN	NDUFV1	physical	26638075
NNTM_HUMAN	NNT	physical	26638075
NPHP4_HUMAN	NPHP4	physical	26638075
NUDC3_HUMAN	NUDCD3	physical	26638075
PDRG1_HUMAN	PDRG1	physical	26638075
PHAR4_HUMAN	PHACTR4	physical	26638075
PIHD1_HUMAN	PIH1D1	physical	26638075
RPAB1_HUMAN	POLR2E	physical	26638075
PRC2A_HUMAN	PRRC2A	physical	26638075
PSDE_HUMAN	PSMD14	physical	26638075
PSMD7_HUMAN	PSMD7	physical	26638075
RAB35_HUMAN	RAB35	physical	26638075
RB3GP_HUMAN	RAB3GAP1	physical	26638075
RAB6A_HUMAN	RAB6A	physical	26638075
RPAP3_HUMAN	RPAP3	physical	26638075
FTM_HUMAN	RPGRIP1L	physical	26638075
S23IP_HUMAN	SEC23IP	physical	26638075
SEC63_HUMAN	SEC63	physical	26638075
SH319_HUMAN	SH3D19	physical	26638075
SNX9_HUMAN	SNX9	physical	26638075
SRSF2_HUMAN	SRSF2	physical	26638075
TM9S3_HUMAN	TM9SF3	physical	26638075
TM237_HUMAN	TMEM237	physical	26638075
TNR6B_HUMAN	TNRC6B	physical	26638075
TTL12_HUMAN	TTLL12	physical	26638075
UN45A_HUMAN	UNC45A	physical	26638075
QCR1_HUMAN	UQCRC1	physical	26638075
RMP_HUMAN	URI1	physical	26638075
UBP22_HUMAN	USP22	physical	26638075
UXT_HUMAN	UXT	physical	26638075
WDR41_HUMAN	WDR41	physical	26638075
WDR92_HUMAN	WDR92	physical	26638075
XPO7_HUMAN	XPO7	physical	26638075
BAG2_HUMAN	BAG2	physical	26638075
FLII_HUMAN	FLII	physical	26638075
WDR83_HUMAN	WDR83	physical	26638075
NPHP4_HUMAN	NPHP4	physical	27173435
FTM_HUMAN	RPGRIP1L	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
256100	Nephronophthisis 1 (NPHP1)
266900	Senior-Loken syndrome 1 (SLSN1)
609583	Joubert syndrome 4 (JBTS4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NPHP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Nephrocystin-4 regulates Pyk2-induced tyrosine phosphorylation ofnephrocystin-1 to control targeting to monocilia."; Liebau M.C., Hopker K., Muller R.U., Schmedding I., Zank S.,Schairer B., Fabretti F., Hohne M., Bartram M.P., Dafinger C.,Hackl M., Burst V., Habbig S., Zentgraf H., Blaukat A., Walz G.,Benzing T., Schermer B.; J. Biol. Chem. 286:14237-14245(2011). Cited for: INTERACTION WITH PTK2B/PYK2, AND PHOSPHORYLATION AT TYR-46; TYR-349AND TYR-721.	21357692 [Abstract]