SENP6_MOUSE - dbPTM
SENP6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP6_MOUSE
UniProt AC Q6P7W0
Protein Name Sentrin-specific protease 6
Gene Name Senp6
Organism Mus musculus (Mouse).
Sequence Length 1132
Subcellular Localization Nucleus.
Protein Description Protease that deconjugates SUMO1, SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional activation. Involved in chromosome alignment and spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI, protecting them from degradation by the ubiquitin ligase RNF4, which targets polysumoylated proteins for proteasomal degradation. Desumoylates also RPA1, thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination..
Protein Sequence MAAGKSGGSAGALFLKALDRSESKRDGGFKNNWSFDHEEESEGDADKDGANLLSVEDEDSEISKGKKLNRRSEIVATSSGDFILKTYVRRSKTDGFKTLKGNPIGLNMLSNNKKLSESTAGTALCSGTVVHGRRFHHAHSQTPGIRTAAQRKEYPPYVHKAENSPVMLSHGQGGDHIMKKTEESESYVESEIKRKVQQKRHCSTYQLSPLSPASKKCLTHLEVSEQREYCPKCGKEKENQTKCQSCGIVFHNDLQRNCRQAVTLNEPTGPLLRTSIHQNSGGQKSQNTGLTAKKFYGNSVDKIPIDILVTCDDSRHNYIQTNGKVILPGGKIPKLTNPKERKISVSDLNDPIILSSDDDDDDDDRTKRRESTSPKPADSACSSPVPSTGKVEAALNADACRAEQEPRSSPAEPELNTIVIPRKARMKDQLGNSISTPLKRRKVNSHAAFIHPMSLSCQNFESVILNCRSIRVGTLFRLLVEPVIFSLESITIHLDGPESDPVDIILNTSDLTKCEWCNVRKLPVVFLQAIPAVYQKLSMQLQMSKEDKVWNDCKGINRITSLEEQYIILIFQTGLDHQAEVVFESIITDIGIRNNVPNFFAKILFDEANSRLVACTRSYEESIKGNCAQKENKVKTVSFESKIQLRSKQELQFFDDDEEAGESHTIFIGPVEKLIVYPPPPAKGGISVTNEDLHCLSEGEFLNDVIIDFYLKYLVLEKLKKEDADRIHIFSSFFYKRLNQRERRNPETTNLSIQQKRHGRVKTWTRHVDIFEKDFIFVPLNEAAHWFLAVVCFPGLEKPKYEPNPHYHENAVMQKTPSAEDSCVSSASEMGACSQNSAAKPVIKKMLNRKHCLAVTDSSAAQEESEPCYRRNAYSVKCSMKKKNHAINENEEPSNGESTCQDICDRTQSENGLRDECFSSVHHPDALSKIRLNYGDQSADGGKLLEDELIDFSEDQDDPDDSSDDGLLADENYSSEIGQWHLKPTVCKQPCILLMDSLRGPSRSNVVKILREYLEVEWEVKKGSKRSFSKDVMKGSNPKVPQQNNFSDCGVYVLQYVESFFENPVLNFELPMNLMNWFPPPRMKTKREEIRNIILKLQESQSKDKKLLKDSLAETSLGDGAEQYASASGGSE
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
6Phosphorylation--MAAGKSGGSAGAL
--CCCCCCCCHHHHH		47.6817203969
9PhosphorylationAAGKSGGSAGALFLK
CCCCCCCHHHHHHHH		27.3617203969
34PhosphorylationGGFKNNWSFDHEEES
CCCCCCCCCCCCCCC		23.9523375375
41PhosphorylationSFDHEEESEGDADKD
CCCCCCCCCCCCCCC		50.5922817900
116PhosphorylationLSNNKKLSESTAGTA
HCCCCCCCCCCCCCC		38.0825777480
118PhosphorylationNNKKLSESTAGTALC
CCCCCCCCCCCCCCC		21.8525777480
119PhosphorylationNKKLSESTAGTALCS
CCCCCCCCCCCCCCC		25.6725777480
122PhosphorylationLSESTAGTALCSGTV
CCCCCCCCCCCCCEE		17.6225777480
126PhosphorylationTAGTALCSGTVVHGR
CCCCCCCCCEEEECC		38.0525777480
128PhosphorylationGTALCSGTVVHGRRF
CCCCCCCEEEECCCC		11.7625777480
164PhosphorylationYVHKAENSPVMLSHG
CCCCCCCCCCEECCC		15.4626643407
187PhosphorylationKTEESESYVESEIKR
CCCCCHHHHHHHHHH		12.2728576409
208PhosphorylationHCSTYQLSPLSPASK
CCCCCCCCCCCHHHH		14.3126745281
211PhosphorylationTYQLSPLSPASKKCL
CCCCCCCCHHHHHHH		23.0825266776
214PhosphorylationLSPLSPASKKCLTHL
CCCCCHHHHHHHHCC		35.7126745281
299PhosphorylationAKKFYGNSVDKIPID
CHHHCCCCCCCCCEE		27.5929899451
344PhosphorylationNPKERKISVSDLNDP
CCCCCCCCHHHCCCC		20.7122802335
346PhosphorylationKERKISVSDLNDPII
CCCCCCHHHCCCCEE		29.5925293948
355PhosphorylationLNDPIILSSDDDDDD
CCCCEEECCCCCCCC		22.7027087446
356PhosphorylationNDPIILSSDDDDDDD
CCCEEECCCCCCCCC		41.4327087446
366PhosphorylationDDDDDDRTKRRESTS
CCCCCHHHHHHHCCC		35.5822324799
371PhosphorylationDRTKRRESTSPKPAD
HHHHHHHCCCCCCCC		32.1625266776
372PhosphorylationRTKRRESTSPKPADS
HHHHHHCCCCCCCCC		44.2719060867
373PhosphorylationTKRRESTSPKPADSA
HHHHHCCCCCCCCCC		39.9625521595
379PhosphorylationTSPKPADSACSSPVP
CCCCCCCCCCCCCCC		33.0325266776
382PhosphorylationKPADSACSSPVPSTG
CCCCCCCCCCCCCCC		37.0823375375
383PhosphorylationPADSACSSPVPSTGK
CCCCCCCCCCCCCCC		29.7825521595
387PhosphorylationACSSPVPSTGKVEAA
CCCCCCCCCCCHHHH		50.4530635358
388PhosphorylationCSSPVPSTGKVEAAL
CCCCCCCCCCHHHHH		34.6530635358
408PhosphorylationRAEQEPRSSPAEPEL
HHHCCCCCCCCCCCC		51.9225266776
409PhosphorylationAEQEPRSSPAEPELN
HHCCCCCCCCCCCCC		29.4325266776
417PhosphorylationPAEPELNTIVIPRKA
CCCCCCCEEEEECCH		29.2825777480
433PhosphorylationMKDQLGNSISTPLKR
CHHHCCCCCCHHHHH		19.0023984901
435PhosphorylationDQLGNSISTPLKRRK
HHCCCCCCHHHHHCC		24.6425266776
436PhosphorylationQLGNSISTPLKRRKV
HCCCCCCHHHHHCCC		30.8525266776
521AcetylationCEWCNVRKLPVVFLQ
CCCCCCCCCCEEHHH		53.5122826441
638PhosphorylationENKVKTVSFESKIQL
CCCCCEEEEHHCEEC		28.6427600695
641PhosphorylationVKTVSFESKIQLRSK
CCEEEEHHCEECCCC		32.8029109428
894PhosphorylationINENEEPSNGESTCQ
CCCCCCCCCCCCHHH		61.8330635358
898PhosphorylationEEPSNGESTCQDICD
CCCCCCCCHHHHHHH		35.5630635358
899PhosphorylationEPSNGESTCQDICDR
CCCCCCCHHHHHHHH		15.1930635358
938PhosphorylationRLNYGDQSADGGKLL
CCCCCCCCCCCCCCC		32.8228066266
962PhosphorylationDQDDPDDSSDDGLLA
CCCCCCCCCCCCCCC		42.9421082442
963PhosphorylationQDDPDDSSDDGLLAD
CCCCCCCCCCCCCCC		46.8721082442
1131PhosphorylationYASASGGSE------
HHHCCCCCC------		43.5925293948
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 SENP6_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SENP6_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 SENP6_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEMO_MOUSEIkbkgphysical
23825957
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SENP6_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-6 AND SER-9, AND MASSSPECTROMETRY.

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