UBD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBD_HUMAN
• UniProt AC: O15205
• Protein Name: Ubiquitin D
• Gene Name: UBD
• Organism: Homo sapiens (Human).
• Sequence Length: 165
• Subcellular Localization: Nucleus . Cytoplasm. Accumulates in aggresomes under proteasome inhibition conditions.
• Protein Description: Ubiquitin-like protein modifier which can be covalently attached to target protein and subsequently leads to their degradation by the 26S proteasome, in a NUB1-dependent manner. Probably functions as a survival factor. Conjugation ability activated by UBA6. Promotes the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and LPS-mediated activation of the central mediator of innate immunity NF-kappa-B by promoting TNF-alpha-mediated proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required for TNF-alpha-induced p65 nuclear translocation in renal tubular epithelial cells (RTECs). May be involved in dendritic cell (DC) maturation, the process by which immature dendritic cells differentiate into fully competent antigen-presenting cells that initiate T-cell responses. Mediates mitotic non-disjunction and chromosome instability, in long-term in vitro culture and cancers, by abbreviating mitotic phase and impairing the kinetochore localization of MAD2L1 during the prometaphase stage of the cell cycle. May be involved in the formation of aggresomes when proteasome is saturated or impaired. Mediates apoptosis in a caspase-dependent manner, especially in renal epithelium and tubular cells during renal diseases such as polycystic kidney disease and Human immunodeficiency virus (HIV)-associated nephropathy (HIVAN)..
• Protein Sequence: MAPNASCLCVHVRSEEWDLMTFDANPYDSVKKIKEHVRSKTKVPVQDQVLLLGSKILKPRRSLSSYGIDKEKTIHLTLKVVKPSDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIPETQIVTCNGKRLEDGKMMADYGIRKGNLLFLACYCIGG

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
62	Phosphorylation	KILKPRRSLSSYGID EECCCCCCHHHCCCC	33.60	26074081
64	Phosphorylation	LKPRRSLSSYGIDKE CCCCCCHHHCCCCCC	23.82	29978859
65	Phosphorylation	KPRRSLSSYGIDKEK CCCCCHHHCCCCCCC	32.45	26074081
66	Phosphorylation	PRRSLSSYGIDKEKT CCCCHHHCCCCCCCE	18.09	26074081
73	Phosphorylation	YGIDKEKTIHLTLKV CCCCCCCEEEEEEEE	18.08	26074081
77	Phosphorylation	KEKTIHLTLKVVKPS CCCEEEEEEEEECCC	15.46	26074081
109	Phosphorylation	HLLQVRRSSSVAQVK HHHHHHCCCCHHHHH	19.19	22817900
110	Phosphorylation	LLQVRRSSSVAQVKA HHHHHCCCCHHHHHH	27.33	22817900
111	Phosphorylation	LQVRRSSSVAQVKAM HHHHCCCCHHHHHHH	23.79	22817900
148	Phosphorylation	DGKMMADYGIRKGNL CCCEECCCCCCCCCE	12.62	-
161	Phosphorylation	NLLFLACYCIGG--- CEEEEEEEEECC---	4.98	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBD_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 UBD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MD2L1_HUMAN	MAD2L1	physical	10200259
HDAC6_HUMAN	HDAC6	physical	19033385
PRS6A_HUMAN	PSMC3	physical	22072791
PSA6_HUMAN	PSMA6	physical	22072791
NUB1_HUMAN	NUB1	physical	22434192
PSMD4_HUMAN	PSMD4	physical	22434192
RPN10_YEAST	RPN10	physical	22434192
MD2L1_HUMAN	MAD2L1	physical	16495226
NUB1_HUMAN	NUB1	physical	16707496
PSA6_HUMAN	PSMA6	physical	16707496
UBE2Z_HUMAN	UBE2Z	physical	20975683
UBA6_HUMAN	UBA6	physical	20975683
LRRF2_HUMAN	LRRFIP2	physical	23036196
EF1A1_HUMAN	EEF1A1	physical	22569823
TOIP2_HUMAN	TOR1AIP2	physical	23036196
IFG15_HUMAN	TOR1AIP2	physical	23036196
DDX58_HUMAN	DDX58	physical	26996158

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-109; SER-110 ANDSER-111, AND MASS SPECTROMETRY.
PubMed: 18187866