STX17
entrez
55014
canonical
uniprot
P56962
canonical
ensembl
ENSG00000136874
resolver
ensp
ENSP00000259400
resolver
ensp
ENSP00000433484
resolver
ensp
ENSP00000435981
resolver
ensp
ENSP00000436666
resolver
ensp
ENSP00000531188
resolver
ensp
ENSP00000531189
resolver
ensp
ENSP00000531190
resolver
ensp
ENSP00000531191
resolver
ensp
ENSP00000598387
resolver
ensp
ENSP00000598388
resolver
ensp
ENSP00000628360
resolver
ensp
ENSP00000628361
resolver
enst
ENST00000259400
resolver
enst
ENST00000525640
resolver
enst
ENST00000534052
resolver
enst
ENST00000861129
resolver
enst
ENST00000861130
resolver
enst
ENST00000861131
resolver
enst
ENST00000861132
resolver
enst
ENST00000928328
resolver
enst
ENST00000928329
resolver
enst
ENST00000958301
resolver
enst
ENST00000958302
resolver
genesymbol
STX17
resolver
hgnc
HGNC:11432
resolver
uniprot
Q4VXC2
resolver
uniprot_entry
STX17_HUMAN
resolver
uniprot_sec
Q4VXC2
resolver
amino_acid_sequence
MSEDEEKVKLRRLEPAIQKFIKIVIPTDLERLRKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREIEKLCLKVRKDDLVLLKRMIDPVKEEASAATAEFLQLHLESVEELKKQFNDEETLLQPPLTRSMTVGGAFHTTEAEASSQSLTQIYALPEIPQDQNAAESWETLEADLIELSQLVTDFSLLVNSQQEKIDSIADHVNSAAVNVEEGTKNLGKAAKYKLAALPVAGALIGGMVGGPIGLLAGFKVAGIAAALGGGVLGFTGGKLIQRKKQKMMEKLTSSCPDLPSQTDKKCS
uniprot
proteins
function
FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion (PubMed:23217709, PubMed:25686604, PubMed:28306502). STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane (PubMed:23217709, PubMed:25686604, PubMed:28306502, PubMed:28504273). May also play a role in the early secretory pathway where it may maintain the architecture of the endoplasmic reticulum-Golgi intermediate compartment/ERGIC and Golgi and/or regulate transport between the endoplasmic reticulum, the ERGIC and the Golgi (PubMed:21545355). {ECO:0000269|PubMed:21545355, ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604, ECO:0000269|PubMed:28306502, ECO:0000269|PubMed:28504273}.
uniprot
proteins
mass_dalton
33403
uniprot
proteins
mutagenesis
MUTAGEN 244; /note="G->L: Alters localization to the autophagosome; when associated with Leu-248."; /evidence="ECO:0000269|PubMed:23217709"; MUTAGEN 248; /note="G->L: Alters localization to the autophagosome; when associated with Leu-244."; /evidence="ECO:0000269|PubMed:23217709"; MUTAGEN 264; /note="G->L: Alters localization to the autophagosome; when associated with Leu-268."; /evidence="ECO:0000269|PubMed:23217709"; MUTAGEN 268; /note="G->L: Alters localization to the autophagosome; when associated with Leu-264."; /evidence="ECO:0000269|PubMed:23217709"; MUTAGEN 299..300; /note="KK->AA: Localizes to the Golgi instead of the endoplasmic reticulum."; /evidence="ECO:0000269|PubMed:23217709
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Tyr-157 probably by ABL1. Dephosphorylation by PTPN2; regulates exit from the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q9Z158}.; PTM: (Microbial infection) Cleaved by the L.pneumophila serine protease Lpg1137, impairing endoplasmic reticulum-mitochondria communication, leading to inhibit autophagy. {ECO:0000269|PubMed:28504273}.
uniprot
proteins
protein_family
Syntaxin family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21545355
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23006999
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23217709
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25686604
uniprot
proteins
pubmed
26416964
uniprot
proteins
pubmed
28306502
uniprot
proteins
pubmed
28504273
uniprot
proteins
pubmed
29420192
uniprot
proteins
pubmed
30704899
uniprot
proteins
pubmed
31806350
uniprot
proteins
pubmed
32980859
uniprot
proteins
pubmed
33422265
uniprot
proteins
pubmed
37632749
uniprot
proteins
pubmed
37821429
uniprot
proteins
sequence_length
302
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23006999}; Multi-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:23006999}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604, ECO:0000269|PubMed:26416964, ECO:0000269|PubMed:28306502, ECO:0000269|PubMed:29420192}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z158}. Mitochondrion membrane {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:28504273}; Multi-pass membrane protein {ECO:0000255}. Autolysosome membrane {ECO:0000269|PubMed:37821429}; Multi-pass membrane protein {ECO:0000255}. Note=Has a hairpin-like insertion into membranes. Localizes to the completed autophagosome membrane upon cell starvation (PubMed:23217709). Colocalized with RAB39A and RAB39B in autolysosomes in autophagy-induced conditions (PubMed:37821429). {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:37821429}.
uniprot
proteins
transmembrane_region
TRANSMEM 229..249; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 255..275; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins