UBP14_MOUSE - dbPTM
UBP14_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP14_MOUSE
UniProt AC Q9JMA1
Protein Name Ubiquitin carboxyl-terminal hydrolase 14
Gene Name Usp14
Organism Mus musculus (Mouse).
Sequence Length 493
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein.
Protein Description Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation..
Protein Sequence MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKMKNGMTVLMMGSADALPEEPSAKTVFVEDMTEEQLATAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSGRETDSSSAPAVTPSKKKSLIDQYFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDVYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNANDKNSPPKEIKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVRRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ
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
4Phosphorylation----MPLYSVTVKWG
----CCCEEEEEEEC		8.6725367039
5Phosphorylation---MPLYSVTVKWGK
---CCCEEEEEEECH		20.9925367039
7Phosphorylation-MPLYSVTVKWGKEK
-CCCEEEEEEECHHH		15.4925367039
14UbiquitinationTVKWGKEKFEGVELN
EEEECHHHCCCEECC		52.8022790023
49MalonylationARQKVMVKGGTLKDD
CCCEEEEECCCCCCC		33.2626320211
49UbiquitinationARQKVMVKGGTLKDD
CCCEEEEECCCCCCC		33.26-
52PhosphorylationKVMVKGGTLKDDDWG
EEEEECCCCCCCCCC		39.0219060867
54AcetylationMVKGGTLKDDDWGNI
EEECCCCCCCCCCCE		59.9723954790
62AcetylationDDDWGNIKMKNGMTV
CCCCCCEEEECCEEE		48.067970527
62UbiquitinationDDDWGNIKMKNGMTV
CCCCCCEEEECCEEE		48.0622790023
64UbiquitinationDWGNIKMKNGMTVLM
CCCCEEEECCEEEEE		45.4022790023
130UbiquitinationIRSVPELKDALKRYA
HHCCHHHHHHHHHHH		39.0122790023
136PhosphorylationLKDALKRYAGALRAS
HHHHHHHHHHHHHHC		14.0619060867
143PhosphorylationYAGALRASGEMASAQ
HHHHHHHCHHHHHHH		28.9325521595
146OxidationALRASGEMASAQYIT
HHHHCHHHHHHHHHH		3.9917242355
148PhosphorylationRASGEMASAQYITAA
HHCHHHHHHHHHHHH		18.0026824392
151PhosphorylationGEMASAQYITAALRD
HHHHHHHHHHHHHHH		10.4328833060
153PhosphorylationMASAQYITAALRDLF
HHHHHHHHHHHHHHH		10.8428833060
203GlutathionylationLQQDANECWIQMMRV
HHHHHHHHHHHHHHH		3.7824333276
203S-palmitoylationLQQDANECWIQMMRV
HHHHHHHHHHHHHHH		3.7828680068
214AcetylationMMRVLQQKLEAIEDD
HHHHHHHHHHHHHCC		35.0222826441
214UbiquitinationMMRVLQQKLEAIEDD
HHHHHHHHHHHHHCC		35.0222790023
222PhosphorylationLEAIEDDSGRETDSS
HHHHHCCCCCCCCCC		52.6625619855
226PhosphorylationEDDSGRETDSSSAPA
HCCCCCCCCCCCCCC		39.5625619855
228PhosphorylationDSGRETDSSSAPAVT
CCCCCCCCCCCCCCC		33.3425619855
229PhosphorylationSGRETDSSSAPAVTP
CCCCCCCCCCCCCCC		33.0725619855
230PhosphorylationGRETDSSSAPAVTPS
CCCCCCCCCCCCCCC		42.0725619855
235PhosphorylationSSSAPAVTPSKKKSL
CCCCCCCCCCCCHHH		24.7725619855
237PhosphorylationSAPAVTPSKKKSLID
CCCCCCCCCCHHHHH		47.9825619855
238UbiquitinationAPAVTPSKKKSLIDQ
CCCCCCCCCHHHHHH		66.4822790023
239UbiquitinationPAVTPSKKKSLIDQY
CCCCCCCCHHHHHHH		52.51-
257S-nitrosocysteineEFETTMKCTESEEEE
EEEEEEECCCCCHHH		3.38-
257S-nitrosylationEFETTMKCTESEEEE
EEEEEEECCCCCHHH		3.3821278135
260PhosphorylationTTMKCTESEEEEVTK
EEEECCCCCHHHHHC		31.9622668510
285PhosphorylationFINQEVKYLFTGLKL
CCCHHHHHHHHCHHH		16.5425367039
291UbiquitinationKYLFTGLKLRLQEEI
HHHHHCHHHHHHHHH		32.6722790023
291AcetylationKYLFTGLKLRLQEEI
HHHHHCHHHHHHHHH		32.6722826441
300UbiquitinationRLQEEITKQSPTLQR
HHHHHHHHCCCCHHC		55.2122790023
302PhosphorylationQEEITKQSPTLQRNA
HHHHHHCCCCHHCCE		22.77-
313UbiquitinationQRNALYIKSSKISRL
HCCEEEEECCCCCCC		34.8122790023
313AcetylationQRNALYIKSSKISRL
HCCEEEEECCCCCCC		34.8122826441
342UbiquitinationEKESVNAKVLKDVKF
CCCCCCCHHHCCCCC		42.7822790023
359GlutathionylationMLDVYELCTPELQEK
EEEHHHHCCHHHHHH		3.8924333276
369PhosphorylationELQEKMVSFRSKFKD
HHHHHHHHHHHHCCC		16.0821183079
393PhosphorylationPNANDKNSPPKEIKY
CCCCCCCCCCCCCCC		48.6025521595
414GlutathionylationDDIGSNNCGYYDLQA
CCCCCCCCCEEEEEE		4.3024333276
429PhosphorylationVLTHQGRSSSSGHYV
EEEECCCCCCCCCCE		41.2023984901
430PhosphorylationLTHQGRSSSSGHYVS
EEECCCCCCCCCCEE		27.4523984901
431PhosphorylationTHQGRSSSSGHYVSW
EECCCCCCCCCCEEE		41.4023984901
432PhosphorylationHQGRSSSSGHYVSWV
ECCCCCCCCCCEEEE		31.3823984901
435PhosphorylationRSSSSGHYVSWVRRK
CCCCCCCCEEEEEEC		10.3323984901
448AcetylationRKQDEWIKFDDDKVS
ECCCCCEECCCCCEE		43.7623954790
448UbiquitinationRKQDEWIKFDDDKVS
ECCCCCEECCCCCEE		43.7622790023
453UbiquitinationWIKFDDDKVSIVTPE
CEECCCCCEEEECHH		44.8922790023
491PhosphorylationVEIMEEESEQ-----
EEECHHHCCC-----		44.5726525534
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 UBP14_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP14_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 UBP14_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBRA1_MOUSEGabra1physical
19759851
UBX2B_MOUSEUbxn2bphysical
11566882
PSA4_MOUSEPsma4physical
11566882
ERN1_MOUSEErn1physical
24951540
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP14_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-136; SER-143 ANDSER-222, AND MASS SPECTROMETRY.

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