UBQL2_MOUSE - dbPTM
UBQL2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBQL2_MOUSE
UniProt AC Q9QZM0
Protein Name Ubiquilin-2
Gene Name Ubqln2
Organism Mus musculus (Mouse).
Sequence Length 638
Subcellular Localization Cytoplasm . Nucleus . Membrane . Cytoplasmic vesicle, autophagosome . Colocalizes with a subset of proteasomes, namely those that are cytoskeleton associated or free in the cytosol. Associated with fibers in mitotic cells.
Protein Description Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and the 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 FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. 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 endocytosis of GPCR receptors: AVPR2 and ADRB2, by specifically reducing the rate at which receptor-arrestin complexes concentrate in clathrin-coated pits (CCPs) (By similarity). Links CD47 to vimentin-containing intermediate filaments of the cytoskeleton. [PubMed: 10549293]
Protein Sequence MAENGESSGPPRPSRGPAAAPGAASPPAEPKIIKVTVKTPKEKEEFAVPENSTVQQFKEAISKRFKSQTDQLVLIFAGKILKDQDTLMQHGIHDGLTVHLVIKSQNRPQGQATTQPSTTAGTSTTTTTTTTAAAPAATTSSAPRSSSTPTTTNSSSFGLGSLSSLSNLGLNSPNFTELQNQMQQQLLASPEMMIQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHLLNNPDIMRQTLEIARNPAMMQEMMRNQDLALSNLESIPGGYNALRRMYTDIQEPMLNAAQEQFGGNPFATVGSSSTSGEGTQPSRTENRDPLPNPWAPPPTTQTAATTTTTTTTSSGSGSGSSSSSTTAGNTMAAANYVASIFSTPGMQSLLQQITENPQLIQNMLSAPYMRSMMQSLSQNPDMAAQMMLSSPLFTSNPQLQEQMRPQLPNFLQQMQNPETIAAMSNPRAMQALMQIQQGLQTLATEAPGLIPSFAPGVGMGVLGTAITPVGPVTPIGPIGPIVPFTPIGPIGPIGPTGPASSPGSTGTGIPPATTVSSSAPTETISPTSESGPNQQFIQQMVQALTGGSPPQPPNPEVRFQQQLEQLNAMGFLNREANLQALIATGGDINAAIERLLGSQPS
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 Orthologous
Protein Cluster
2Acetylation------MAENGESSG
------CCCCCCCCC		20.97-
8PhosphorylationMAENGESSGPPRPSR
CCCCCCCCCCCCCCC		51.5224719451
14PhosphorylationSSGPPRPSRGPAAAP
CCCCCCCCCCCCCCC		51.6629514104
25PhosphorylationAAAPGAASPPAEPKI
CCCCCCCCCCCCCCE		30.7725521595
31UbiquitinationASPPAEPKIIKVTVK
CCCCCCCCEEEEEEC		48.8722790023
41UbiquitinationKVTVKTPKEKEEFAV
EEEECCCCHHHCCCC		83.2522790023
43AcetylationTVKTPKEKEEFAVPE
EECCCCHHHCCCCCC		69.53-
43UbiquitinationTVKTPKEKEEFAVPE
EECCCCHHHCCCCCC		69.5322790023
58UbiquitinationNSTVQQFKEAISKRF
CHHHHHHHHHHHHHH		41.7322790023
63UbiquitinationQFKEAISKRFKSQTD
HHHHHHHHHHHHHHH		56.6027667366
66UbiquitinationEAISKRFKSQTDQLV
HHHHHHHHHHHHHEE		45.7622790023
79UbiquitinationLVLIFAGKILKDQDT
EEEEEECHHHCCHHH		41.2422790023
245PhosphorylationNPDIMRQTLEIARNP
CHHHHHHHHHHHHCH		18.9229899451
267PhosphorylationRNQDLALSNLESIPG
HCCCHHHHCCCCCCC		33.4927600695
271PhosphorylationLALSNLESIPGGYNA
HHHHCCCCCCCHHHH		36.9328066266
276PhosphorylationLESIPGGYNALRRMY
CCCCCCHHHHHHHHH		11.8129514104
283PhosphorylationYNALRRMYTDIQEPM
HHHHHHHHHHCHHHH		10.2325777480
284PhosphorylationNALRRMYTDIQEPML
HHHHHHHHHCHHHHH		19.7925777480
305PhosphorylationFGGNPFATVGSSSTS
HCCCCCCCCCCCCCC		26.2725777480
308PhosphorylationNPFATVGSSSTSGEG
CCCCCCCCCCCCCCC		19.4425777480
309PhosphorylationPFATVGSSSTSGEGT
CCCCCCCCCCCCCCC		31.5426239621
310PhosphorylationFATVGSSSTSGEGTQ
CCCCCCCCCCCCCCC		28.4325777480
311PhosphorylationATVGSSSTSGEGTQP
CCCCCCCCCCCCCCC		42.5725777480
312PhosphorylationTVGSSSTSGEGTQPS
CCCCCCCCCCCCCCC		36.4725777480
316PhosphorylationSSTSGEGTQPSRTEN
CCCCCCCCCCCCCCC		32.7625777480
319PhosphorylationSGEGTQPSRTENRDP
CCCCCCCCCCCCCCC		41.8525777480
635PhosphorylationAIERLLGSQPS----
HHHHHHCCCCC----		38.6028066266
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 UBQL2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBQL2_MOUSE !!
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 UBQL2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITB3_MOUSEItgb3physical
10549293
CD47_MOUSECd47physical
10549293
HSP7C_MOUSEHspa8physical
27477512
HSP72_MOUSEHspa2physical
27477512
HS71L_MOUSEHspa1lphysical
27477512
HS71B_MOUSEHspa1bphysical
27477512
PRS6B_MOUSEPsmc4physical
27477512
PSMD3_MOUSEPsmd3physical
27477512
PRS8_MOUSEPsmc5physical
27477512
UBC_MOUSEUbcphysical
27477512
UBQL1_MOUSEUbqln1physical
27477512
UBQL4_MOUSEUbqln4physical
27477512
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBQL2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.

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