SPRED1
entrez
161742
canonical
uniprot
Q7Z699
canonical
ensembl
ENSG00000166068
resolver
ensp
ENSP00000299084
resolver
ensp
ENSP00000551439
resolver
ensp
ENSP00000595429
resolver
enst
ENST00000299084
resolver
enst
ENST00000925370
resolver
genesymbol
SPRED1
resolver
hgnc
HGNC:20249
resolver
uniprot
B2RPJ8
resolver
uniprot
Q05D53
resolver
uniprot
Q8N256
resolver
uniprot_entry
SPRE1_HUMAN
resolver
uniprot_sec
B2RPJ8
resolver
uniprot_sec
Q05D53
resolver
uniprot_sec
Q8N256
resolver
amino_acid_sequence
MSEETATSDNDNSYARVRAVVMTRDDSSGGWLPLGGSGLSSVTVFKVPHQEENGCADFFIRGERLRDKMVVLECMLKKDLIYNKVTPTFHHWKIDDKKFGLTFQSPADARAFDRGIRRAIEDISQGCPESKNEAEGADDLQANEEDSSSSLVKDHLFQQETVVTSEPYRSSNIRPSPFEDLNARRVYMQSQANQITFGQPGLDIQSRSMEYVQRQISKECGSLKSQNRVPLKSIRHVSFQDEDEIVRINPRDILIRRYADYRHPDMWKNDLERDDADSSIQFSKPDSKKSDYLYSCGDETKLSSPKDSVVFKTQPSSLKIKKSKRRKEDGERSRCVYCQERFNHEENVRGKCQDAPDPIKRCIYQVSCMLCAESMLYHCMSDSEGDFSDPCSCDTSDDKFCLRWLALVALSFIVPCMCCYVPLRMCHRCGEACGCCGGKHKAAG
uniprot
proteins
disease_involvement
DISEASE: Legius syndrome (LGSS) [MIM:611431]: An autosomal dominant syndrome characterized mainly by cafe-au-lait macules without neurofibromas or other tumor manifestations of neurofibromatosis type 1, axillary freckling, and macrocephaly. Additional clinical manifestations include Noonan-like facial dysmorphism, lipomas, learning disabilities, and features of attention deficit-hyperactivity disorder. {ECO:0000269|PubMed:17704776, ECO:0000269|PubMed:19443465, ECO:0000269|PubMed:20108422, ECO:0000269|PubMed:21089071}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Tyrosine kinase substrate that inhibits growth-factor-mediated activation of MAP kinase (By similarity). Negatively regulates hematopoiesis of bone marrow (By similarity). Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2 (By similarity). Attenuates actin stress fiber formation via inhibition of TESK1-mediated phosphorylation of cofilin (PubMed:18216281). Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q924S8, ECO:0000269|PubMed:18216281}.
uniprot
proteins
mass_dalton
50477
uniprot
proteins
post_translational_modification
PTM: Palmitoylated by ZDHHC17/HIP14. {ECO:0000250|UniProtKB:Q924S8}.; PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:17094949}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:17094949}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15580519
uniprot
proteins
pubmed
15683364
uniprot
proteins
pubmed
16115197
uniprot
proteins
pubmed
17094949
uniprot
proteins
pubmed
17704776
uniprot
proteins
pubmed
18216281
uniprot
proteins
pubmed
19443465
uniprot
proteins
pubmed
20108422
uniprot
proteins
pubmed
21089071
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24705354
uniprot
proteins
sequence_length
444
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16115197}; Peripheral membrane protein {ECO:0000269|PubMed:16115197}. Membrane, caveola {ECO:0000269|PubMed:16115197}; Peripheral membrane protein {ECO:0000269|PubMed:16115197}. Nucleus {ECO:0000269|PubMed:16115197}. Note=Localized in cholesterol-rich membrane raft/caveola fractions.
uniprot
proteins