UBXN7_MOUSE - dbPTM
UBXN7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBXN7_MOUSE
UniProt AC Q6P5G6
Protein Name UBX domain-containing protein 7
Gene Name Ubxn7
Organism Mus musculus (Mouse).
Sequence Length 467
Subcellular Localization Nucleus .
Protein Description Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates (By similarity)..
Protein Sequence MAAHGGSAASSALKGLIQQFTAITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGVRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSAQAKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPARTEPGTATNHQGLPSMDSEVLEMSPEKSDGIVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN
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------MAAHGGSAA
------CCCCCHHHH		14.25-
7Phosphorylation-MAAHGGSAASSALK
-CCCCCHHHHHHHHH		25.8429514104
11PhosphorylationHGGSAASSALKGLIQ
CCHHHHHHHHHHHHH		32.6620531401
84UbiquitinationVRAPIPQKQEILVEP
HCCCCCCCCEEEECC		44.54-
114PhosphorylationGAIDKKLTTLADLFR
CCCCHHHHHHHHHHC		28.7427600695
226PhosphorylationEWHQLDVSSFLDQVT
EEHHCCHHHHHHHHH		18.2925777480
227PhosphorylationWHQLDVSSFLDQVTG
EHHCCHHHHHHHHHH		29.6725777480
233PhosphorylationSSFLDQVTGFLGEHG
HHHHHHHHHHHCCCC		19.3123984901
246PhosphorylationHGQLDGLSSSPPKKC
CCCCCCCCCCCCCHH		34.0123984901
247PhosphorylationGQLDGLSSSPPKKCA
CCCCCCCCCCCCHHC		52.4826239621
248PhosphorylationQLDGLSSSPPKKCAR
CCCCCCCCCCCHHCC		41.6726239621
256PhosphorylationPPKKCARSESLIDAS
CCCHHCCCCCCCCCC		17.0125521595
258PhosphorylationKKCARSESLIDASED
CHHCCCCCCCCCCCH		31.6925521595
263PhosphorylationSESLIDASEDSQLEA
CCCCCCCCCHHHHHH		37.8823527152
266PhosphorylationLIDASEDSQLEAAIR
CCCCCCHHHHHHHHH		32.3925521595
275PhosphorylationLEAAIRASLQETHFD
HHHHHHHHHHHHCCC		22.2728066266
279PhosphorylationIRASLQETHFDSAQA
HHHHHHHHCCCHHHH		18.1928066266
283PhosphorylationLQETHFDSAQAKQDS
HHHHCCCHHHHHCCC		22.7225338131
328PhosphorylationNLAKSRKSPHKDLGH
HHHHHCCCCCCCCCC		31.0025266776
351PhosphorylationLTEPPARTEPGTATN
CCCCCCCCCCCCCCC		48.9525619855
355PhosphorylationPARTEPGTATNHQGL
CCCCCCCCCCCCCCC		40.8125619855
357PhosphorylationRTEPGTATNHQGLPS
CCCCCCCCCCCCCCC		32.8325619855
364PhosphorylationTNHQGLPSMDSEVLE
CCCCCCCCCCHHHHH		40.0225619855
367PhosphorylationQGLPSMDSEVLEMSP
CCCCCCCHHHHHCCC		22.4425619855
373PhosphorylationDSEVLEMSPEKSDGI
CHHHHHCCCCCCCCE		22.1124925903
377PhosphorylationLEMSPEKSDGIVEGI
HHCCCCCCCCEEEEE		39.1325619855
412AcetylationITLPEQAKLLALVKH
CCCHHHHHHHHHHHH		43.6722902405
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 UBXN7_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBXN7_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 UBXN7_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UBXN7_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBXN7_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND MASSSPECTROMETRY.
"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 SER-256 AND SER-258, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-266, ANDMASS SPECTROMETRY.
"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-256, AND MASSSPECTROMETRY.

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