##gff-version 3
P17861	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000076543;Note=X-box-binding protein 1	
P17861	UniProtKB	Chain	1	193	.	.	.	ID=PRO_0000431891;Note=X-box-binding protein 1%2C cytoplasmic form;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Chain	196	261	.	.	.	ID=PRO_0000431892;Note=X-box-binding protein 1%2C luminal form;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Topological domain	1	185	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Transmembrane	186	203	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000303;evidence=ECO:0000255,ECO:0000269|PubMed:25239945,ECO:0000303|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Topological domain	204	261	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Domain	70	133	.	.	.	Note=BZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
P17861	UniProtKB	Region	44	93	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P17861	UniProtKB	Region	72	94	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
P17861	UniProtKB	Region	75	92	.	.	.	Note=Nuclear localization signal (NLS)%3B in isoforms 1 and isoform 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16461360;Dbxref=PMID:16461360	
P17861	UniProtKB	Region	98	133	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
P17861	UniProtKB	Region	235	261	.	.	.	Note=Necessary for the translational pausing of its own mRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233347;Dbxref=PMID:21233347	
P17861	UniProtKB	Compositional bias	63	93	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P17861	UniProtKB	Site	194	195	.	.	.	Note=Cleavage%3B by HM13/SPP;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
P17861	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
P17861	UniProtKB	Alternative sequence	167	261	.	.	.	ID=VSP_012936;Note=In isoform 2. LRLRAPLQQVQAQLSPLQNISPWILAVLTLQIQSLISCWAFWTTWTQSCSSNALPQSLPAWRSSQRSTQKDPVPYQPPFLCQWGRHQPSWKPLMN->GAGPVVTPPEHLPMDSGGIDSSDSESDILLGILDNLDPVMFFKCPSPEPASLEELPEVYPEGPSSLPASLSLSVGTSSAKLEAINELIRFDHIYTKPLVLEIPSETESQANVVVKIEEAPLSPSENDHPEFIVSVKEEPVEDDLVPELGISNLLSSSHCPKPSSCLLDAYSDCGYGGSLSPFSDMSSLLGVNHSWEDTFANELFPQLISV;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11779464;Dbxref=PMID:11779464	
P17861	UniProtKB	Natural variant	12	12	.	.	.	ID=VAR_035998;Note=In a breast cancer sample%3B somatic mutation. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974	
P17861	UniProtKB	Natural variant	232	232	.	.	.	ID=VAR_033023;Note=In a breast cancer sample%3B somatic mutation. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17224074;Dbxref=dbSNP:rs1379560430,PMID:17224074	
P17861	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Reduces endoplasmic reticulum localization of its own mRNA%3B when associated with E-193 and D-196. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19394296;Dbxref=PMID:19394296	
P17861	UniProtKB	Mutagenesis	193	193	.	.	.	Note=Reduces endoplasmic reticulum localization of its own mRNA%3B when associated with E-189 and D-196. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19394296;Dbxref=PMID:19394296	
P17861	UniProtKB	Mutagenesis	194	194	.	.	.	Note=Reduces endoplasmic reticulum localization of its own mRNA%3B when associated with D-198 and E-205. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19394296;Dbxref=PMID:19394296	
P17861	UniProtKB	Mutagenesis	196	196	.	.	.	Note=Reduces endoplasmic reticulum localization of its own mRNA%3B when associated with E-189 and E-193. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19394296;Dbxref=PMID:19394296	
P17861	UniProtKB	Mutagenesis	197	197	.	.	.	Note=Inhibits HM13/SPP-mediated degradation of XBP1%3B when associated with L-199%3B L-200 and L-203. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Reduces endoplasmic reticulum localization of its own mRNA%3B when associated with E-194 and E-205. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19394296;Dbxref=PMID:19394296	
P17861	UniProtKB	Mutagenesis	199	199	.	.	.	Note=Inhibits HM13/SPP-mediated degradation of XBP1%3B when associated with L-197%3B L-200 and L-203. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Inhibits HM13/SPP-mediated degradation of XBP1%3B when associated with L-197%3B L-199 and L-203. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Mutagenesis	203	203	.	.	.	Note=Inhibits HM13/SPP-mediated degradation of XBP1%3B when associated with L-197%3B L-199 and L-200. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Reduces endoplasmic reticulum localization of its own mRNA%3B when associated with E-194 and D-198. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19394296;Dbxref=PMID:19394296	
P17861	UniProtKB	Mutagenesis	212	212	.	.	.	Note=Does not induce glycosylation. T->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Induces glycosylation. C->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Mutagenesis	232	232	.	.	.	Note=Induces glycosylation. R->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25239945;Dbxref=PMID:25239945	
P17861	UniProtKB	Mutagenesis	246	246	.	.	.	Note=Reduces translational pausing%2C membrane targeting and cytoplasmic splicing of its own mRNA. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233347;Dbxref=PMID:21233347	
P17861	UniProtKB	Mutagenesis	255	255	.	.	.	Note=Increases translational pausing of its own mRNA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233347;Dbxref=PMID:21233347	
P17861	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Reduces translational pausing%2C membrane targeting and cytoplasmic splicing of its own mRNA. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233347;Dbxref=PMID:21233347	
P17861	UniProtKB	Sequence conflict	33	35	.	.	.	Note=GQA->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P17861	UniProtKB	Sequence conflict	130	130	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P17861	UniProtKB	Sequence conflict	196	196	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305