UBQL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBQL1_MOUSE
• UniProt AC: Q8R317
• Protein Name: Ubiquilin-1
• Gene Name: Ubqln1
• Organism: Mus musculus (Mouse).
• Sequence Length: 582
• Subcellular Localization: Nucleus . Cytoplasm . Endoplasmic reticulum . Cytoplasmic vesicle, autophagosome . Cell membrane . Detected in neuronal processes and at synapses. Recruited to the ER during ER-associated protein degradation (ERAD). Colocalizes with PSEN1 in the cell
• Protein Description: Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. Plays a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress. Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway. Plays a key role in the regulation of the levels of PSEN1 by targeting its accumulation to aggresomes which may then be removed from cells by autophagocytosis. Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently downregulating the ORAI1-mediated Ca2+ mobilization. Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing (By similarity). Links CD47 to the cytoskeleton. [PubMed: 10549293]
• Protein Sequence: MAESAESGGPPGAQDSAADGGPAEPKIMKVTVKTPKEKEEFAVPENSSVQQFKEEISKRFKSHIDQLVLIFAGKILKDQDTLSQHGIHDGLTVHLVIKTQNRPQDNSAQQTNAPGSTVTSSPAPDSNPTSGSAANSSFGVGGLGGLAGLSSLGLNTTNFSELQSQMQRQLLSNPEMMVQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHMLNNPDIMRQTLELARNPAMMQEMMRNQDRALSNLESIPGGYNALRRMYTDIQEPMLNAAQEQFGGNPFASLVSSSSSAEGTQPSRTENRDPLPNPWAPQTSQSSPASGTTGSTTNTMSTSGGTATSTPAGQSTSGPSLVPGAGASMFNTPGMQSLLQQITENPQLMQNMLSAPYMRSMLQSLSQNPDLAAQMMLNNPLFAGNPQLQEQMRQQLPTFLQQMQNPDTLSAMSNPRAMQALLQIQQGLQTLATEAPGLIPGFTPGLAAGNSGGSSGTNAPSTAPSEDTNPQGGTAEPGHQQFIQQMLQALAGVNPQLQSPEVRFQQQLEQLSAMGFLNREANLQALIATGGDINAAIERLLGSQPS

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
2	Acetylation	------MAESAESGG ------CCCCHHCCC	21.32	-
4	Phosphorylation	----MAESAESGGPP ----CCCCHHCCCCC	28.00	25293948
7	Phosphorylation	-MAESAESGGPPGAQ -CCCCHHCCCCCCCC	49.09	25293948
16	Phosphorylation	GPPGAQDSAADGGPA CCCCCCCCCCCCCCC	17.18	25293948
36	Ubiquitination	KVTVKTPKEKEEFAV EEEECCCHHHHCCCC	83.25	-
38	Acetylation	TVKTPKEKEEFAVPE EECCCHHHHCCCCCC	69.53	23236377
38	Ubiquitination	TVKTPKEKEEFAVPE EECCCHHHHCCCCCC	69.53	-
53	Ubiquitination	NSSVQQFKEEISKRF CCHHHHHHHHHHHHH	50.53	-
58	Ubiquitination	QFKEEISKRFKSHID HHHHHHHHHHHHHHH	68.46	-
61	Ubiquitination	EEISKRFKSHIDQLV HHHHHHHHHHHHHHH	45.19	-
74	Ubiquitination	LVLIFAGKILKDQDT HHHHHHCCHHCCCCH	41.24	-
77	Ubiquitination	IFAGKILKDQDTLSQ HHHCCHHCCCCHHHH	57.74	-
251	Phosphorylation	RNQDRALSNLESIPG HCHHHHHHCHHHCCC	38.08	27600695
255	Phosphorylation	RALSNLESIPGGYNA HHHHCHHHCCCHHHH	36.93	28066266
579	Phosphorylation	AIERLLGSQPS---- HHHHHHCCCCC----	38.60	28066266

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

Oops, there are no upstream regulatory protein records of UBQL1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBQL1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of UBQL1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BCR_MOUSE	Bcr	physical	22451666

Drug and Disease Associations

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