SCIMP
entrez
388325
canonical
uniprot
Q6UWF3
canonical
ensembl
ENSG00000161929
resolver
ensp
ENSP00000382509
resolver
ensp
ENSP00000459153
resolver
ensp
ENSP00000459605
resolver
ensp
ENSP00000461269
resolver
enst
ENST00000574297
resolver
genesymbol
SCIMP
resolver
genesymbol_syn
C17orf87
resolver
hgnc
HGNC:33504
resolver
uniprot
A6XGL4
resolver
uniprot
B4DLK1
resolver
uniprot
I3L1W2
resolver
uniprot
Q96MD0
resolver
uniprot_entry
I3L1W2_HUMAN
resolver
uniprot_entry
SCIMP_HUMAN
resolver
uniprot_sec
A6XGL4
resolver
uniprot_sec
B4DLK1
resolver
uniprot_sec
Q96MD0
resolver
amino_acid_sequence
MDTFTVQDSTAMSWWRNNFWIILAVAIIVVSVGLGLILYCVCKWQLRRGKKWEIAKPLKHKQVDEEKMYENVLNESPVQLPPLPPRNWPSLEDSSPQEAPSQPPATYSLVNKVKNKKTVSIPSYIEPEDDYDDVEIPANTEKASF
uniprot
proteins
function
FUNCTION: Lipid tetraspanin-associated transmembrane adapter/mediator that acts as a scaffold for Src-family kinases and other signaling proteins in immune cells (PubMed:21930792). It is involved in major histocompatibility complex class II (MHC-II) signaling transduction in B cells, where it is required in generating the calcium response and enhancing ERK activity upon MHC-II stimulation (PubMed:21930792). In dendritic cells, it is involved in sustaining CLEC7A/DECTIN1 signaling after CLEC7A activation by fungal beta-glucans (By similarity). It also acts as an agonist-inducible signaling adapter for TLR1, TLR2, TLR3, TLR4, and TLR7 by selectively enabling the expression of pro-inflammatory cytokines IL6 and IL12B in macrophages and acting as a scaffold for phosphorylation of Toll-like receptors by Src-family kinases (By similarity). {ECO:0000250|UniProtKB:Q3UU41, ECO:0000269|PubMed:21930792}.
uniprot
proteins
mass_dalton
16618
uniprot
proteins
mutagenesis
MUTAGEN 69; /note="Y->F: Inhibits interaction with GRB2."; /evidence="ECO:0000269|PubMed:21930792"; MUTAGEN 81..86; /note="Missing: Inhibits interaction with LYN."; /evidence="ECO:0000269|PubMed:21930792"; MUTAGEN 107; /note="Y->F: Inhibits interaction with CSK. Stimulates activation of several downstream signaling pathways."; /evidence="ECO:0000269|PubMed:21930792"; MUTAGEN 131; /note="Y->F: Inhibits interaction with BLNK. Inhibits activation of several downstream signaling pathways."; /evidence="ECO:0000269|PubMed:21930792
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by the Src-family protein tyrosine kinases LYN and SRC (PubMed:21930792). Phosphorylation occurs on tyrosine residues upon MHC-II stimulation (PubMed:21930792). Phosphorylation also occurs on tyrosine residues after activation of CLEC7A/DECTIN1 by particulate beta-glucan (By similarity). Lipopolysaccharide (LPS) induces phosphorylation of Tyr-69, Tyr-107 and Tyr-131 differentially to allow temporal recruitment of effector proteins GRB2, CSK and BLNK (By similarity). Phosphorylation of Tyr-69 is immediately induced by LPS stimulation and allows GRB2 to bind (By similarity). Tyr-107 is phosphorylated 5 minutes after LPS stimulation, which then allows CSK to bind, followed by phosphorylation of Tyr-131 10 minutes after LPS induction, which allows BLNK to bind (By similarity). Phosphorylation at Tyr-107 by LYN occurs after activation of TLR4 by lipopolysaccharide; phosphorylation enhances binding to TLR4 (By similarity). {ECO:0000250|UniProtKB:Q3UU41, ECO:0000269|PubMed:21930792}.; PTM: Palmitoylated. {ECO:0000269|PubMed:21930792}.
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
21930792
uniprot
proteins
sequence_length
145
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21930792}; Lipid-anchor {ECO:0000269|PubMed:21930792}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q3UU41}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q3UU41}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q3UU41}. Note=Together with MHC-II, associates with lipid-enriched microdomains called tetraspanin-enriched microdomains (TEMs) (PubMed:21930792). Rapidly translocates into immunological synapse (IS) at cell-cell contacts between antigen-presenting cells (APCs) and T-cells (PubMed:21930792). Colocalized with tetraspanins CD37, CD53, and CD81 at the uropod (PubMed:21930792). Present at regions of cell-cell contacts but also at the leading edge of migrating cells (PubMed:21930792). Localizes to phagosomes in dendritic cells after exposure to particulate beta-glucan (By similarity). {ECO:0000250|UniProtKB:Q3UU41, ECO:0000269|PubMed:21930792}.
uniprot
proteins
transmembrane_region
TRANSMEM 19..39; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins