dbPTM

UBXN8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBXN8_HUMAN
UniProt AC	O00124
Protein Name	UBX domain-containing protein 8
Gene Name	UBXN8
Organism	Homo sapiens (Human).
Sequence Length	270
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein .
Protein Description	Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction..
Protein Sequence	MASRGVVGIFFLSAVPLVCLELRRGIPDIGIKDFLLLCGRILLLLALLTLIISVTTSWLNSFKSPQVYLKEEEEKNEKRQKLVRKKQQEAQGEKASRYIENVLKPHQEMKLRKLEERFYQMTGEAWKLSSGHKLGGDEGTSQTSFETSNREAAKSQNLPKPLTEFPSPAEQPTCKEIPDLPEEPSQTAEEVVTVALRCPSGNVLRRRFLKSYSSQVLFDWMTRIGYHISLYSLSTSFPRRPLAVEGGQSLEDIGITVDTVLILEEKEQTN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
55	Phosphorylation	LTLIISVTTSWLNSF HHHHHHHHHHHHHCC	14.34	-
64	Phosphorylation	SWLNSFKSPQVYLKE HHHHCCCCCCEECCH	20.67	29449344
67 (in isoform 3)	Ubiquitination	-	7.39	21890473
68	Phosphorylation	SFKSPQVYLKEEEEK CCCCCCEECCHHHHH	13.55	29449344
86	Ubiquitination	RQKLVRKKQQEAQGE HHHHHHHHHHHHHHH	46.80	-
94	Ubiquitination	QQEAQGEKASRYIEN HHHHHHHHHHHHHHH	59.49	-
96 (in isoform 3)	Ubiquitination	-	36.36	21890473
96	Phosphorylation	EAQGEKASRYIENVL HHHHHHHHHHHHHCC	36.36	18187866
98	Phosphorylation	QGEKASRYIENVLKP HHHHHHHHHHHCCCH	15.30	18187866
104	Ubiquitination	RYIENVLKPHQEMKL HHHHHCCCHHHHHHH	35.85	21890473
104 (in isoform 1)	Ubiquitination	-	35.85	21890473
119	Phosphorylation	RKLEERFYQMTGEAW HHHHHHHHHHHHCEE	12.00	22210691
127	Ubiquitination	QMTGEAWKLSSGHKL HHHHCEEECCCCCCC	45.60	-
133	Ubiquitination	WKLSSGHKLGGDEGT EECCCCCCCCCCCCC	52.96	2190698
133 (in isoform 1)	Ubiquitination	-	52.96	21890473
141	Phosphorylation	LGGDEGTSQTSFETS CCCCCCCCCCCCCCC	42.17	29507054
144	Phosphorylation	DEGTSQTSFETSNRE CCCCCCCCCCCCCHH	17.28	25627689
163	Phosphorylation	QNLPKPLTEFPSPAE CCCCCCCCCCCCCCC	44.07	20068231
167	Phosphorylation	KPLTEFPSPAEQPTC CCCCCCCCCCCCCCC	41.90	25159151
173	Phosphorylation	PSPAEQPTCKEIPDL CCCCCCCCCCCCCCC	35.58	20068231
222	Phosphorylation	QVLFDWMTRIGYHIS HHHHHHHHHHCHHEE	18.19	22210691
234	Phosphorylation	HISLYSLSTSFPRRP HEEEEECCCCCCCCC	18.96	22210691

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
Oops, there are no upstream regulatory protein records of UBXN8_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBXN8_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of UBXN8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TERA_HUMAN	VCP	physical	18775313
NPL4_HUMAN	NPLOC4	physical	18775313
UFD1_HUMAN	UFD1L	physical	18775313
VCIP1_HUMAN	VCPIP1	physical	18775313
TERA_HUMAN	VCP	physical	21949850
TBC15_HUMAN	TBC1D15	physical	26389662
TERA_HUMAN	VCP	physical	26389662
ATP4A_HUMAN	ATP4A	physical	26389662
ELAV2_HUMAN	ELAVL2	physical	26389662
AT2B2_HUMAN	ATP2B2	physical	26389662
RHBD2_HUMAN	RHBDD2	physical	26389662
S38A1_HUMAN	SLC38A1	physical	26389662
TM165_HUMAN	TMEM165	physical	26389662
VDAC3_HUMAN	VDAC3	physical	26389662
SURF4_HUMAN	SURF4	physical	26389662
MTCH2_HUMAN	MTCH2	physical	26389662
CTR1_HUMAN	SLC7A1	physical	26389662
MSH2_HUMAN	MSH2	physical	26389662
ADT1_HUMAN	SLC25A4	physical	26389662
SUCB1_HUMAN	SUCLA2	physical	26389662

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of UBXN8_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND TYR-98, AND MASSSPECTROMETRY.	18187866 [Abstract]