SUMO3_MOUSE - dbPTM
SUMO3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUMO3_MOUSE
UniProt AC Q9Z172
Protein Name Small ubiquitin-related modifier 3 {ECO:0000305}
Gene Name Sumo3 {ECO:0000312|MGI:MGI:1336201}
Organism Mus musculus (Mouse).
Sequence Length 110
Subcellular Localization Cytoplasm. Nucleus. Nucleus, PML body .
Protein Description Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. Plays a role in the regulation of sumoylation status of SETX (By similarity)..
Protein Sequence MSEEKPKEGVKTENDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGSASRGSVPTPNRCPDLCY
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
2Phosphorylation------MSEEKPKEG
------CCCCCCCCC
55.2325266776
11UbiquitinationEKPKEGVKTENDHIN
CCCCCCCCCCCCCEE
62.06-
11AcetylationEKPKEGVKTENDHIN
CCCCCCCCCCCCCEE
62.0623806337
12PhosphorylationKPKEGVKTENDHINL
CCCCCCCCCCCCEEE
37.3024719451
27PhosphorylationKVAGQDGSVVQFKIK
EEECCCCCEEEEEEE
27.6626824392
32UbiquitinationDGSVVQFKIKRHTPL
CCCEEEEEEECCCHH
30.17-
34UbiquitinationSVVQFKIKRHTPLSK
CEEEEEEECCCHHHH
38.42-
37PhosphorylationQFKIKRHTPLSKLMK
EEEEECCCHHHHHHH
29.9222817900
41UbiquitinationKRHTPLSKLMKAYCE
ECCCHHHHHHHHHHH
61.35-
44UbiquitinationTPLSKLMKAYCERQG
CHHHHHHHHHHHHCC
46.79-
53PhosphorylationYCERQGLSMRQIRFR
HHHHCCCCCEEEEEE
20.8124719451
95PhosphorylationQQTGGSASRGSVPTP
HHHCCCCCCCCCCCC
38.5821082442

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 SUMO3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUMO3_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 SUMO3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SENP6_MOUSESenp6physical
23825957
XIAP_HUMANXIAPphysical
26496610
GABP1_HUMANGABPB1physical
26496610
ITPR2_HUMANITPR2physical
26496610
RPAB2_HUMANPOLR2Fphysical
26496610
RENT1_HUMANUPF1physical
26496610
SMC1A_HUMANSMC1Aphysical
26496610
GT2D1_HUMANGTF2IRD1physical
26496610
SAE1_HUMANSAE1physical
26496610
EXOC3_HUMANEXOC3physical
26496610
INT7_HUMANINTS7physical
26496610
RM18_HUMANMRPL18physical
26496610
RCC2_HUMANRCC2physical
26496610
TBC14_HUMANTBC1D14physical
26496610
RT35_HUMANMRPS35physical
26496610
UTP15_HUMANUTP15physical
26496610
SFXN1_HUMANSFXN1physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SUMO3_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP