SPRED2
entrez
200734
canonical
uniprot
Q7Z698
canonical
ensembl
ENSG00000198369
resolver
ensp
ENSP00000348753
resolver
ensp
ENSP00000393697
resolver
ensp
ENSP00000783499
resolver
genesymbol
SPRED2
resolver
hgnc
HGNC:17722
resolver
uniprot
A1L3V4
resolver
uniprot
B3KPL5
resolver
uniprot
B7Z5K7
resolver
uniprot
D6W5F7
resolver
uniprot
E9PEP0
resolver
uniprot
Q2NKX6
resolver
uniprot_entry
B3KPL5_HUMAN
resolver
uniprot_entry
SPRE2_HUMAN
resolver
uniprot_sec
A1L3V4
resolver
uniprot_sec
B7Z5K7
resolver
uniprot_sec
D6W5F7
resolver
uniprot_sec
E9PEP0
resolver
uniprot_sec
Q2NKX6
resolver
amino_acid_sequence
MTEETHPDDDSYIVRVKAVVMTRDDSSGGWFPQEGGGISRVGVCKVMHPEGNGRSGFLIHGERQKDKLVVLECYVRKDLVYTKANPTFHHWKVDNRKFGLTFQSPADARAFDRGVRKAIEDLIEGSTTSSSTIHNEAELGDDDVFTTATDSSSNSSQKREQPTRTISSPTSCEHRRIYTLGHLHDSYPTDHYHLDQPMPRPYRQVSFPDDDEEIVRINPREKIWMTGYEDYRHAPVRGKYPDPSEDADSSYVRFAKGEVPKHDYNYPYVDSSDFGLGEDPKGRGGSVIKTQPSRGKSRRRKEDGERSRCVYCRDMFNHEENRRGHCQDAPDSVRTCIRRVSCMWCADSMLYHCMSDPEGDYTDPCSCDTSDEKFCLRWMALIALSFLAPCMCCYLPLRACYHCGVMCRCCGGKHKAAA
uniprot
proteins
disease_involvement
DISEASE: Noonan syndrome 14 (NS14) [MIM:619745]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. NS14 inheritance is autosomal recessive. {ECO:0000269|PubMed:34626534}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Negatively regulates Ras signaling pathways and downstream activation of MAP kinases (PubMed:15683364, PubMed:34626534). Recruits and translocates NF1 to the cell membrane, thereby enabling NF1-dependent hydrolysis of active GTP-bound Ras to inactive GDP-bound Ras (PubMed:34626534). Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2 (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q924S7, ECO:0000269|PubMed:15683364, ECO:0000269|PubMed:34626534}.
uniprot
proteins
mass_dalton
47558
uniprot
proteins
mutagenesis
MUTAGEN 228; /note="Y->F: Reduces ubiquitination and CBL-induced phosphorylation; when associated with F-231."; /evidence="ECO:0000269|PubMed:17094949"; MUTAGEN 231; /note="Y->F: Reduces ubiquitination and CBL-induced phosphorylation; when associated with F-228."; /evidence="ECO:0000269|PubMed:17094949"; MUTAGEN 240; /note="Y->F: No effect on phosphorylation or ubiquitination."; /evidence="ECO:0000269|PubMed:17094949"; MUTAGEN 251; /note="Y->F: No effect on phosphorylation or ubiquitination."; /evidence="ECO:0000269|PubMed:17094949"; MUTAGEN 264; /note="Y->F: No effect on phosphorylation or ubiquitination; when associated with F-266."; /evidence="ECO:0000269|PubMed:17094949"; MUTAGEN 266; /note="Y->F: No effect on phosphorylation or ubiquitination; when associated with F-264."; /evidence="ECO:0000269|PubMed:17094949"; MUTAGEN 268; /note="Y->F: No effect on phosphorylation or ubiquitination."; /evidence="ECO:0000269|PubMed:17094949"; MUTAGEN 311; /note="Y->F: No effect on phosphorylation or ubiquitination."; /evidence="ECO:0000269|PubMed:17094949"; MUTAGEN 351; /note="Y->F: No effect on phosphorylation or ubiquitination."; /evidence="ECO:0000269|PubMed:17094949"; MUTAGEN 394; /note="Y->F: No effect on phosphorylation or ubiquitination."; /evidence="ECO:0000269|PubMed:17094949
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and threonine residues (PubMed:15683364). Phosphorylated on tyrosine. Phosphorylation of Tyr-228 and Tyr-231 are required for ubiquitination (PubMed:17094949). {ECO:0000269|PubMed:15683364, ECO:0000269|PubMed:17094949}.; PTM: Ubiquitinated; leading to degradation by the proteasome. {ECO:0000269|PubMed:17094949}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15213456
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15580519
uniprot
proteins
pubmed
15683364
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17094949
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
34626534
uniprot
proteins
sequence_length
418
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34626534}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q924S7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q924S7}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:15580519}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:15580519}. Note=Detected in the cytoplasm of the stratum spinosum cells, where it is associated with cytoplasmic vesicles that are supposed to be secretory granules. {ECO:0000269|PubMed:15580519}.
uniprot
proteins