XBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: XBP1_HUMAN
• UniProt AC: P17861
• Protein Name: X-box-binding protein 1 {ECO:0000303|PubMed:2321018, ECO:0000312|HGNC:HGNC:12801}
• Gene Name: XBP1 {ECO:0000312|HGNC:HGNC:12801}
• Organism: Homo sapiens (Human).
• Sequence Length: 261
• Subcellular Localization: Endoplasmic reticulum . Colocalizes with ERN1 and KDR in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (PubMed:23529610).; Isoform 1: Nucleus . Cytoplasm . Endoplasmic reticulum membran
• Protein Description: Functions as a transcription factor during endoplasmic reticulum (ER) stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development, and the development of secretory tissues such as exocrine pancreas and salivary gland (By similarity). Involved in terminal differentiation of B lymphocytes to plasma cells and production of immunoglobulins. [PubMed: 11460154 Modulates the cellular response to ER stress in a PIK3R-dependent manner]
• Protein Sequence: MVVVAAAPNPADGTPKVLLLSGQPASAAGAPAGQALPLMVPAQRGASPEAASGGLPQARKRQRLTHLSPEEKALRRKLKNRVAAQTARDRKKARMSELEQQVVDLEEENQKLLLENQLLREKTHGLVVENQELRQRLGMDALVAEEEAEAKGNEVRPVAGSAESAALRLRAPLQQVQAQLSPLQNISPWILAVLTLQIQSLISCWAFWTTWTQSCSSNALPQSLPAWRSSQRSTQKDPVPYQPPFLCQWGRHQPSWKPLMN

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	APNPADGTPKVLLLS CCCCCCCCCEEEEEC	22.08	23403867
47	Phosphorylation	VPAQRGASPEAASGG EECCCCCCHHHHCCC	26.54	23401153
52	Phosphorylation	GASPEAASGGLPQAR CCCHHHHCCCCCHHH	40.20	24732914
68	Phosphorylation	RQRLTHLSPEEKALR HHHHHCCCHHHHHHH	23.74	25849741
72	Ubiquitination	THLSPEEKALRRKLK HCCCHHHHHHHHHHH	51.57	-
96	Phosphorylation	DRKKARMSELEQQVV HHHHHHHHHHHHHHH	33.21	25159151
111	Ubiquitination	DLEEENQKLLLENQL CHHHHHHHHHHHHHH	53.32	-
122	Ubiquitination	ENQLLREKTHGLVVE HHHHHHHHHCCCEEC	39.11	-
151	Ubiquitination	AEEEAEAKGNEVRPV HHHHHHHCCCCCCCC	54.49	2190698
151 (in isoform 1)	Ubiquitination	-	54.49	21906983
181	Phosphorylation	QQVQAQLSPLQNISP HHHHHHHCCCCCCCH	16.10	-
212 (in isoform 2)	Phosphorylation	-	14.44	28348404
236	Ubiquitination	SSQRSTQKDPVPYQP HCCCCCCCCCCCCCC	65.18	-
255	Phosphorylation	QWGRHQPSWKPLMN- CCCCCCCCCCCCCC-	40.96	-
262 (in isoform 2)	Ubiquitination	-		21906983
281 (in isoform 2)	Sumoylation	-		-
288 (in isoform 2)	Phosphorylation	-		26657352
290 (in isoform 2)	Phosphorylation	-		30266825
300 (in isoform 2)	Phosphorylation	-		30266825
302 (in isoform 2)	Sumoylation	-		-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
68	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
68	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
181	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
181	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:30783083

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of XBP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of XBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESR1_HUMAN	ESR1	physical	12954762
FOS_HUMAN	FOS	physical	1903538
NR0B2_HUMAN	NR0B2	physical	20211142
FUBP3_HUMAN	FUBP3	physical	20211142
H1X_HUMAN	H1FX	physical	20211142
TRIP4_HUMAN	TRIP4	physical	20211142
ZN580_HUMAN	ZNF580	physical	20211142
PHS2_HUMAN	PCBD2	physical	20211142
ZN440_HUMAN	ZNF440	physical	20211142
PSA5_HUMAN	PSMA5	physical	19941857
PSA6_HUMAN	PSMA6	physical	19941857
PSA7L_HUMAN	PSMA8	physical	19941857
ATF6B_HUMAN	ATF6B	physical	23661758
ATF6A_HUMAN	ATF6	physical	23661758
XBP1_HUMAN	XBP1	physical	23661758
ZHANG_HUMAN	CREBZF	physical	23661758
HM13_HUMAN	HM13	physical	25239945
UBC9_HUMAN	UBE2I	physical	23470653
KAT2B_HUMAN	KAT2B	physical	25426559
KAT2A_HUMAN	KAT2A	physical	25426559

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612371: Major affective disorder 7 (MAFD7)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
PubMed: 19413330