SBP2_MOUSE - dbPTM
SBP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SBP2_MOUSE
UniProt AC Q63836
Protein Name Selenium-binding protein 2
Gene Name Selenbp2
Organism Mus musculus (Mouse).
Sequence Length 472
Subcellular Localization Nucleus. Cytoplasm, cytosol. Membrane
Peripheral membrane protein. May associate with Golgi membrane. May associate with the membrane of autophagosomes (By similarity)..
Protein Description Selenium- and acetaminophen-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity)..
Protein Sequence MATKCTKCGPGYPTPLEAMKGPREEIVYLPCIYRNTGTEAPDYLATVDVDPKSPQYSQVIHRLPMPYLKDELHHSGWNTCSSCFGDSTKSRNKLILPGLISSRIYVVDVGSEPRAPKLHKVIEASEIQAKCNVSNTHTSHCLASGEVMVNTLGDLQGNGKGSFVLLDGETFEVKGTWEKPGGASPMGYDFWYQPRHNVMVSTEWAAPNVFKDGFNPAHVEAGLYGSRIFVWDWQRHEIIQTLQMTDGLIPLEIRFLHDPSATQGFVGCALSSNIQRFYKNEEGTWSVEKVIQVPSKKVKGWMLPEMPGLITDILLSLDDRFLYFSNWLHGDIRQYDISNPQKPRLTGQIFLGGSIVRGGSVQVLEDQELTCQPEPLVVKGKRIPGGPQMIQLSLDGKRLYATTSLYSDWDKQFYPDLIREGSVMLQVDVDTVNGGLKLNPNFLVDFGKEPLGPALAHELRYPGGDCSSDIWI
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
7Malonylation-MATKCTKCGPGYPT
-CCCCCCCCCCCCCC
46.8226320211
7Ubiquitination-MATKCTKCGPGYPT
-CCCCCCCCCCCCCC
46.82-
20UbiquitinationPTPLEAMKGPREEIV
CCCHHHCCCCHHHEE
73.1922790023
52AcetylationATVDVDPKSPQYSQV
EEEECCCCCCCHHHH
71.01-
52MalonylationATVDVDPKSPQYSQV
EEEECCCCCCCHHHH
71.0126073543
52UbiquitinationATVDVDPKSPQYSQV
EEEECCCCCCCHHHH
71.01-
53PhosphorylationTVDVDPKSPQYSQVI
EEECCCCCCCHHHHH
23.7125521595
56PhosphorylationVDPKSPQYSQVIHRL
CCCCCCCHHHHHHCC
12.4023984901
57PhosphorylationDPKSPQYSQVIHRLP
CCCCCCHHHHHHCCC
16.8423984901
69UbiquitinationRLPMPYLKDELHHSG
CCCCCHHCCCCCCCC
43.2322790023
69MalonylationRLPMPYLKDELHHSG
CCCCCHHCCCCCCCC
43.2326320211
89UbiquitinationSCFGDSTKSRNKLIL
HHHCCCCCCCCEECC
51.9022790023
89MalonylationSCFGDSTKSRNKLIL
HHHCCCCCCCCEECC
51.9026320211
93UbiquitinationDSTKSRNKLILPGLI
CCCCCCCEECCCCCC
35.4822790023
111PhosphorylationIYVVDVGSEPRAPKL
EEEEECCCCCCCCCC
44.2525521595
120MalonylationPRAPKLHKVIEASEI
CCCCCCHHEEEHHHH
56.1726320211
120UbiquitinationPRAPKLHKVIEASEI
CCCCCCHHEEEHHHH
56.1722790023
125PhosphorylationLHKVIEASEIQAKCN
CHHEEEHHHHHCCCC
23.5725521595
162PhosphorylationLQGNGKGSFVLLDGE
CCCCCCCEEEEECCC
18.7023567750
179AcetylationEVKGTWEKPGGASPM
EEEEEEECCCCCCCC
40.2923954790
179MalonylationEVKGTWEKPGGASPM
EEEEEEECCCCCCCC
40.2926320211
179UbiquitinationEVKGTWEKPGGASPM
EEEEEEECCCCCCCC
40.29-
201PhosphorylationPRHNVMVSTEWAAPN
CCCCEEEECCCCCCC
11.5223984901
202PhosphorylationRHNVMVSTEWAAPNV
CCCEEEECCCCCCCC
24.9223984901
211UbiquitinationWAAPNVFKDGFNPAH
CCCCCCCCCCCCHHH
53.3022790023
211AcetylationWAAPNVFKDGFNPAH
CCCCCCCCCCCCHHH
53.30-
260PhosphorylationIRFLHDPSATQGFVG
EEECCCCCCCCCCHH
50.4323984901
262PhosphorylationFLHDPSATQGFVGCA
ECCCCCCCCCCHHHH
33.3023984901
279UbiquitinationSNIQRFYKNEEGTWS
CCHHHHHCCCCCCEE
55.99-
279AcetylationSNIQRFYKNEEGTWS
CCHHHHHCCCCCCEE
55.9922733758
279MalonylationSNIQRFYKNEEGTWS
CCHHHHHCCCCCCEE
55.9926320211
284PhosphorylationFYKNEEGTWSVEKVI
HHCCCCCCEEEEEEE
20.1822871156
286PhosphorylationKNEEGTWSVEKVIQV
CCCCCCEEEEEEEEC
21.8922871156
289UbiquitinationEGTWSVEKVIQVPSK
CCCEEEEEEEECCCC
42.35-
289MalonylationEGTWSVEKVIQVPSK
CCCEEEEEEEECCCC
42.3526320211
289AcetylationEGTWSVEKVIQVPSK
CCCEEEEEEEECCCC
42.3566692673
295PhosphorylationEKVIQVPSKKVKGWM
EEEEECCCCCCCCCC
46.3722871156
296UbiquitinationKVIQVPSKKVKGWML
EEEECCCCCCCCCCC
56.3622790023
316PhosphorylationLITDILLSLDDRFLY
CHHHHHHHCCCHHHH
26.72-
338PhosphorylationDIRQYDISNPQKPRL
CHHHCCCCCCCCCCC
39.2929472430
342AcetylationYDISNPQKPRLTGQI
CCCCCCCCCCCEEEE
33.1023954790
342UbiquitinationYDISNPQKPRLTGQI
CCCCCCCCCCCEEEE
33.10-
342MalonylationYDISNPQKPRLTGQI
CCCCCCCCCCCEEEE
33.1026073543
360PhosphorylationGSIVRGGSVQVLEDQ
CEEECCCCEEEECCC
16.5222324799
379UbiquitinationQPEPLVVKGKRIPGG
CCCCEEECCEECCCC
51.7622790023
397AcetylationIQLSLDGKRLYATTS
EEEEECCCEEEEEEC
38.6115605279
397MalonylationIQLSLDGKRLYATTS
EEEEECCCEEEEEEC
38.6126073543
397UbiquitinationIQLSLDGKRLYATTS
EEEEECCCEEEEEEC
38.61-
411SuccinylationSLYSDWDKQFYPDLI
CCCCCCHHHHHHHHH
37.7423954790
411UbiquitinationSLYSDWDKQFYPDLI
CCCCCCHHHHHHHHH
37.74-
448AcetylationNFLVDFGKEPLGPAL
CEEEECCCCCCCHHH
57.03-
448MalonylationNFLVDFGKEPLGPAL
CEEEECCCCCCCHHH
57.0326073543
448UbiquitinationNFLVDFGKEPLGPAL
CEEEECCCCCCCHHH
57.03-
467PhosphorylationRYPGGDCSSDIWI--
CCCCCCCCCCCCC--
35.4715378723

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 SBP2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SBP2_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 SBP2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SBP2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SBP2_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of mouse liver using immobilized metalaffinity purification and linear ion trap mass spectrometry.";
Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
Cited for: PHOSPHORYLATION AT SER-467.

TOP