Nphs1
entrez
64563
canonical
uniprot
Q9R044
canonical
ensembl
ENSRNOG00000020873
resolver
ensp
ENSRNOP00000104408
resolver
genesymbol
Nphs1
resolver
genesymbol_syn
Nphn
resolver
uniprot
Q9JIX2
resolver
uniprot
Q9QXX7
resolver
uniprot_entry
NPHN_RAT
resolver
uniprot_sec
Q9JIX2
resolver
uniprot_sec
Q9QXX7
resolver
amino_acid_sequence
MGAKRVTVRGARTSPIHRMSSLTPLLLMGMLTSGLAESPVPTSAPRGFWALSENLTAVEGTTVKLWCGVRAPGSVVQWAKDGLLLGPNPKMPGFPRYSLEGDRAKGEFHLLIEACDLSDDAEYECQVGRSELGPELVSPKVILSILVSPKVLLLTPEAGSTVTWVAGQEYVVTCVSGDAKPAPDITFIQSGRTILDVSSNVNEGSEEKLCITEAEARVIPQSSDNGQLLVCEGSNPALDTPIKASFTMNILFPPGPPVIDWPGLNEGHVRAGENLELPCTARGGNPPATLQWLKNGKPVSTAWGTEHAQAVAHSVLVMTVRPEDHGARLSCQSYNSVSAGTQERSITLQVTFPPSAITILGSVSQSENKNVTLCCLTKSSRPRVLLRWWLGGRQLLPTDETVMDGLHGGHISMSNLTFLVRREDNGLPLTCEAFSDAFSKETFKKSLTLNVKYPAQKLWIEGPPEGQYIRTGTRVRLVCLAIGGNPDPSLIWFKDSRPVSEPRQPQEPRRVQLGSVEKSGSTFSRELVLIIGPPDNRAKFSCKAGQLSASTQLVVQFPPTNLTILANSSALRPGDALNLTCVSISSNPPVNLSWDKEGERLEDVAAKPQSAPFKGSAASRSVFLRVSSRDHGQRVTCRAHSEALRETVSSFYRFNVLYPPEFLGEQVRAVTVVEQGQVLLPVSVSANPAPEAFNWTFRGYRLSPAGGPRHRILSGGALQLWNVTRADDGFYQLHCQNSEGTAEALLKLDVHYAPTIRALRDPTEVNVGGSVDIVCTVDANPILPEMFSWERLGEEEEDLNLDDMEKVSKGSTGRLRIRQAKLSQAGAYQCIVDNGVAPAARGLVRLVVRFAPQVDQPTPLTKVAAAGDSTSSATLHCRARGVPNIDFTWTKNGVPLDLQDPRYTEHRYHQGVVHSSLLTIANVSAAQDYALFKCTATNALGSDHTNIQLVSISRPDPPLGLKVVSISPHSVGLEWKPGFDGGLPQRFQIRYEALETPGFLHVDVLPTQATTFTLTGLKPSTRYRIWLLASNALGDSGLTDKGIQVSVTTPGPDQAPEDTDHQLPTELPPGPPRLPLLPVLFAVGGLLLLSNASCVGGLLWRRRLRRLAEEISEKTEAGSEDRIRNEYEESQWTGDRDTRSSTVSTAEVDPNYYSMRDFSPQLPPTLEEVLYHQGAEGEDMAFPGHLHDEVERAYGPPGAWGPLYDEVRMDPYDLRWPEVQCEDPRGIYDQVAADMDAVEASSLPFELRGHLV
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:10487848, ECO:0000269|PubMed:11880318}.
uniprot
proteins
mass_dalton
136281
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Tyr-1204 by FYN, leading to the recruitment and activation of phospholipase C-gamma-1/PLCG1 (PubMed:19179337). Tyrosine phosphorylation is reduced by high glucose levels (By similarity). Dephosphorylated by tensin TNS2 which leads to reduced binding of NPHN1 to PIK3R1 (By similarity). {ECO:0000250|UniProtKB:O60500, ECO:0000269|PubMed:19179337}.
uniprot
proteins
protein_family
Immunoglobulin superfamily
uniprot
proteins
pubmed
10487848
uniprot
proteins
pubmed
10792613
uniprot
proteins
pubmed
10820162
uniprot
proteins
pubmed
11012881
uniprot
proteins
pubmed
11880318
uniprot
proteins
pubmed
15994232
uniprot
proteins
pubmed
16155592
uniprot
proteins
pubmed
17537921
uniprot
proteins
pubmed
19179337
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
29959197
uniprot
proteins
sequence_length
1252
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Located at podocyte slit diaphragm between podocyte foot processes (PubMed:10792613). Partially colocalizes with GAPVD1 in membranes of podocytes (PubMed:29959197). {ECO:0000269|PubMed:10792613, ECO:0000269|PubMed:29959197}.
uniprot
proteins
transmembrane_region
TRANSMEM 1079..1099; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins