SENP2_MOUSE - dbPTM
SENP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP2_MOUSE
UniProt AC Q91ZX6
Protein Name Sentrin-specific protease 2
Gene Name Senp2
Organism Mus musculus (Mouse).
Sequence Length 588
Subcellular Localization Isoform 1: Nucleus, nuclear pore complex . Nucleus membrane
Peripheral membrane protein
Nucleoplasmic side . Shuttles between cytoplasm and nucleus.
Isoform 2: Cytoplasm. Cytoplasmic vesicle. Found in the cytoplasm and in cytoplasmic vesicl
Protein Description Protease that catalyzes two essential functions in the SUMO pathway. The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway. Deconjugates SUMO2 from MTA1 (By similarity). Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB. [PubMed: 20194620 Isoform 3 activates transcription.]
Protein Sequence MYRWLAKVLGTILRLCERPAPGARALLKRRRSSSTLFSTAVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKPMVSSACNGTRNVAPSGEVFSNSSSCELMSSGSCSSMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLKSEGYNRRPSGRRHSKSNPESSLTWKPQEQGVTEMISEEGGKGVRRPHCTVEEGVQKDEREKYRKLLERLKEGAHGSTFPPTVSHHSSQRIQMDTLKTKGWVEEQNHGVRTTHFVPKQYRVVETRGPLCSMRSEKRYSKGKADTEKVVGLRFEKEGTRGHQMEPDLSEEVSARLRLGSGSNGLLRRKISVLEIKEKNFPSKEKDRRTEDLFEFTEDMEKEISNALGHGPPDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLLVERSKKQGYPALHAFSTFFYPKLKSGGYQAVKRWTKGVNLFEQELVLVPIHRKVHWSLVVMDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNTDLNLLEWTHYSMKPHEIPQQLNGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL
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
32PhosphorylationALLKRRRSSSTLFST
HHHHHHHCCCCCEEC
27.1625159016
33PhosphorylationLLKRRRSSSTLFSTA
HHHHHHCCCCCEECC
26.0725159016
34PhosphorylationLKRRRSSSTLFSTAV
HHHHHCCCCCEECCC
30.3125159016
35PhosphorylationKRRRSSSTLFSTAVD
HHHHCCCCCEECCCC
33.5025159016
38PhosphorylationRSSSTLFSTAVDTDE
HCCCCCEECCCCCCC
20.6925293948
43PhosphorylationLFSTAVDTDEIPAKR
CEECCCCCCCCCCCC
29.0029899451
124PhosphorylationMLKLGNKSPNGISDY
HHHCCCCCCCCCCCC
27.8322817900
131PhosphorylationSPNGISDYPKIRVTV
CCCCCCCCCCEEEEE
10.3028059163
178PhosphorylationSNPESSLTWKPQEQG
CCCCCCCCCCCHHCC
33.13-
273PhosphorylationTHFVPKQYRVVETRG
EEECCCEEEEEEECC
16.1129514104
332PhosphorylationSARLRLGSGSNGLLR
HHHHHCCCCCCHHHH
43.5726643407
334PhosphorylationRLRLGSGSNGLLRRK
HHHCCCCCCHHHHCC
29.4428066266
343PhosphorylationGLLRRKISVLEIKEK
HHHHCCEEEEEHHHH
24.5526824392
368PhosphorylationTEDLFEFTEDMEKEI
HHHHHHHCHHHHHHH
24.71-
376PhosphorylationEDMEKEISNALGHGP
HHHHHHHHHHHCCCC
19.69-

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
35TPhosphorylationKinaseRPS6KA1Q15418
GPS
38SPhosphorylationKinaseRPS6KA1Q15418
GPS
368TPhosphorylationKinaseRPS6KA1Q15418
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SENP2_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 SENP2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDM2_MOUSEMdm2physical
21183956
RAGP1_HUMANRANGAP1physical
12419228
PML_HUMANPMLphysical
12419228

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SENP2_MOUSE

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Related Literatures of Post-Translational Modification

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