dbPTM

NPHN_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NPHN_RAT
UniProt AC	Q9R044
Protein Name	Nephrin
Gene Name	Nphs1
Organism	Rattus norvegicus (Rat).
Sequence Length	1252
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Located at podocyte slit diaphragm between podocyte foot processes.
Protein Description	Seems to play a role in the development or function of the kidney glomerular filtration barrier. Regulates glomerular vascular permeability. May anchor the podocyte slit diaphragm to the actin cytoskeleton. Plays a role in skeletal muscle formation through regulation of myoblast fusion..
Protein Sequence	MGAKRVTVRGARTSPIHRMSSLTPLLLMGMLTSGLAESPVPTSAPRGFWALSENLTAVEGTTVKLWCGVRAPGSVVQWAKDGLLLGPNPKMPGFPRYSLEGDRAKGEFHLLIEACDLSDDAEYECQVGRSELGPELVSPKVILSILVSPKVLLLTPEAGSTVTWVAGQEYVVTCVSGDAKPAPDITFIQSGRTILDVSSNVNEGSEEKLCITEAEARVIPQSSDNGQLLVCEGSNPALDTPIKASFTMNILFPPGPPVIDWPGLNEGHVRAGENLELPCTARGGNPPATLQWLKNGKPVSTAWGTEHAQAVAHSVLVMTVRPEDHGARLSCQSYNSVSAGTQERSITLQVTFPPSAITILGSVSQSENKNVTLCCLTKSSRPRVLLRWWLGGRQLLPTDETVMDGLHGGHISMSNLTFLVRREDNGLPLTCEAFSDAFSKETFKKSLTLNVKYPAQKLWIEGPPEGQYIRTGTRVRLVCLAIGGNPDPSLIWFKDSRPVSEPRQPQEPRRVQLGSVEKSGSTFSRELVLIIGPPDNRAKFSCKAGQLSASTQLVVQFPPTNLTILANSSALRPGDALNLTCVSISSNPPVNLSWDKEGERLEDVAAKPQSAPFKGSAASRSVFLRVSSRDHGQRVTCRAHSEALRETVSSFYRFNVLYPPEFLGEQVRAVTVVEQGQVLLPVSVSANPAPEAFNWTFRGYRLSPAGGPRHRILSGGALQLWNVTRADDGFYQLHCQNSEGTAEALLKLDVHYAPTIRALRDPTEVNVGGSVDIVCTVDANPILPEMFSWERLGEEEEDLNLDDMEKVSKGSTGRLRIRQAKLSQAGAYQCIVDNGVAPAARGLVRLVVRFAPQVDQPTPLTKVAAAGDSTSSATLHCRARGVPNIDFTWTKNGVPLDLQDPRYTEHRYHQGVVHSSLLTIANVSAAQDYALFKCTATNALGSDHTNIQLVSISRPDPPLGLKVVSISPHSVGLEWKPGFDGGLPQRFQIRYEALETPGFLHVDVLPTQATTFTLTGLKPSTRYRIWLLASNALGDSGLTDKGIQVSVTTPGPDQAPEDTDHQLPTELPPGPPRLPLLPVLFAVGGLLLLSNASCVGGLLWRRRLRRLAEEISEKTEAGSEDRIRNEYEESQWTGDRDTRSSTVSTAEVDPNYYSMRDFSPQLPPTLEEVLYHQGAEGEDMAFPGHLHDEVERAYGPPGAWGPLYDEVRMDPYDLRWPEVQCEDPRGIYDQVAADMDAVEASSLPFELRGHLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
54	N-linked_Glycosylation	GFWALSENLTAVEGT CEEEECCCEEEEECC	39.04	-
370	N-linked_Glycosylation	VSQSENKNVTLCCLT EECCCCCCEEEEEEE	43.52	-
379	Phosphorylation	TLCCLTKSSRPRVLL EEEEEECCCCCCEEE	26.75	30322021
446	Phosphorylation	SKETFKKSLTLNVKY CHHHHHHHEEEEEEC	27.46	-
500	Phosphorylation	FKDSRPVSEPRQPQE EECCCCCCCCCCCCC	44.56	22673903
561	N-linked_Glycosylation	VVQFPPTNLTILANS EEECCCCCEEEEECC	40.75	-
578	N-linked_Glycosylation	LRPGDALNLTCVSIS CCCCCCEEEEEEECC	34.72	-
591	N-linked_Glycosylation	ISSNPPVNLSWDKEG CCCCCCCCCCCCCCC	33.85	-
722	N-linked_Glycosylation	GGALQLWNVTRADDG CCCEEEEEEEECCCC	33.60	-
1112	Phosphorylation	RRLAEEISEKTEAGS HHHHHHHHHHHCCCC	36.00	22673903
1115	Phosphorylation	AEEISEKTEAGSEDR HHHHHHHHCCCCCHH	27.32	22673903
1119	Phosphorylation	SEKTEAGSEDRIRNE HHHHCCCCCHHHHHH	43.29	22673903
1127	Phosphorylation	EDRIRNEYEESQWTG CHHHHHHHHHHCCCC	28.66	19179337
1152	Phosphorylation	TAEVDPNYYSMRDFS EEEECCCCCCCCCCC	11.42	22013520
1153	Phosphorylation	AEVDPNYYSMRDFSP EEECCCCCCCCCCCC	11.57	19179337
1171	Phosphorylation	PTLEEVLYHQGAEGE CCHHHHHHCCCCCCC	9.40	19179337
1194	Phosphorylation	HDEVERAYGPPGAWG HHHHHHHHCCCCCCC	36.06	19179337
1204	Phosphorylation	PGAWGPLYDEVRMDP CCCCCCCCCCCCCCC	17.12	22013520
1212	Phosphorylation	DEVRMDPYDLRWPEV CCCCCCCCCCCCCCC	24.28	19179337
1228	Phosphorylation	CEDPRGIYDQVAADM CCCCCCHHHHHCCCC	11.80	22013520

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
1127	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1152	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1153	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1153	Y	Phosphorylation	Kinase	FYN	Q62844	PSP
1171	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1194	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1204	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1204	Y	Phosphorylation	Kinase	FYN	Q62844	Uniprot
1212	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1228	Y	Phosphorylation	Kinase	FYN	P06241	PSP

Functions of PTM Sites

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

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 NPHN_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CSKP_RAT	Cask	physical	15331416
ZO1_CANLF	TJP1	physical	15331416

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NPHN_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation of nephrin triggers Ca2+ signaling by recruitment andactivation of phospholipase C-{gamma}1."; Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T.,Ohsawa I., Ohta S., Hattori S.; J. Biol. Chem. 284:8951-8962(2009). Cited for: PHOSPHORYLATION AT TYR-1204 BY FYN.	19179337 [Abstract]