SELS_HUMAN - dbPTM
SELS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SELS_HUMAN
UniProt AC Q9BQE4
Protein Name Selenoprotein S {ECO:0000303|PubMed:27645994}
Gene Name SELENOS {ECO:0000303|PubMed:27645994, ECO:0000312|HGNC:HGNC:30396}
Organism Homo sapiens (Human).
Sequence Length 189
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein. Cytoplasm.
Protein Description Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination..
Protein Sequence MERQEESLSARPALETEGLRFLHTTVGSLLATYGWYIVFSCILLYVVFQKLSARLRALRQRQLDRAAAAVEPDVVVKRQEALAAARLKMQEELNAQVEKHKEKLKQLEEEKRRQKIEMWDSMQEGKSYKGNAKKPQEEDSPGPSTSSVLKRKSDRKPLRGGGYNPLSGEGGGACSWRPGRRGPSSGGUG
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
77UbiquitinationVEPDVVVKRQEALAA
CCCCHHHHHHHHHHH
36.4321890473
88UbiquitinationALAAARLKMQEELNA
HHHHHHHHHHHHHHH
32.74-
115UbiquitinationEEEKRRQKIEMWDSM
HHHHHHHHHHHHHHH
38.53-
121PhosphorylationQKIEMWDSMQEGKSY
HHHHHHHHHHCCCCC
13.5728348404
126AcetylationWDSMQEGKSYKGNAK
HHHHHCCCCCCCCCC
50.2719816919
126UbiquitinationWDSMQEGKSYKGNAK
HHHHHCCCCCCCCCC
50.27-
133UbiquitinationKSYKGNAKKPQEEDS
CCCCCCCCCCCCCCC
69.82-
133AcetylationKSYKGNAKKPQEEDS
CCCCCCCCCCCCCCC
69.8219816925
133MethylationKSYKGNAKKPQEEDS
CCCCCCCCCCCCCCC
69.8219816925
134UbiquitinationSYKGNAKKPQEEDSP
CCCCCCCCCCCCCCC
49.9121906983
140PhosphorylationKKPQEEDSPGPSTSS
CCCCCCCCCCCCHHH
34.7330266825
144PhosphorylationEEDSPGPSTSSVLKR
CCCCCCCCHHHHHHC
47.0027050516
145PhosphorylationEDSPGPSTSSVLKRK
CCCCCCCHHHHHHCC
28.3129396449
146PhosphorylationDSPGPSTSSVLKRKS
CCCCCCHHHHHHCCC
23.8429396449
147PhosphorylationSPGPSTSSVLKRKSD
CCCCCHHHHHHCCCC
31.4025159151
150MethylationPSTSSVLKRKSDRKP
CCHHHHHHCCCCCCC
56.47115982003
150UbiquitinationPSTSSVLKRKSDRKP
CCHHHHHHCCCCCCC
56.472190698
167PhosphorylationGGGYNPLSGEGGGAC
CCCCCCCCCCCCCCC
35.7328348404

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 SELS_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SELS_HUMAN !!

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 SELS_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
15215856
UFD1_HUMANUFD1Lphysical
15215856
HSP74_HUMANHSPA4physical
15215856
DERL1_HUMANDERL1physical
15215856
SAA1_HUMANSAA1physical
12031974
SVIP_HUMANSVIPphysical
17872946
SYVN1_HUMANSYVN1physical
17872946
AMFR_HUMANAMFRphysical
17872946
DERL1_HUMANDERL1physical
17872946
TERA_HUMANVCPphysical
17872946
NPL4_HUMANNPLOC4physical
17872946
HERP1_HUMANHERPUD1physical
16289116
SYVN1_HUMANSYVN1physical
16289116
DERL1_HUMANDERL1physical
16289116
TERA_HUMANVCPphysical
16289116
DERL1_HUMANDERL1physical
16186510
DERL1_HUMANDERL1physical
16186509
DERL2_HUMANDERL2physical
16186509
TERA_HUMANVCPphysical
21832065
IMB1_HUMANKPNB1physical
21832065
AMFR_HUMANAMFRphysical
21832065
DERL1_HUMANDERL1physical
21832065
SELK_HUMANSELKphysical
22119785
KLDC2_HUMANKLHDC2physical
22119785
UBXN8_HUMANUBXN8physical
22119785
DERL1_HUMANDERL1physical
22119785
DERL2_HUMANDERL2physical
22119785
TERA_HUMANVCPphysical
22119785
UBE4A_HUMANUBE4Aphysical
22119785
FAF2_HUMANFAF2physical
22119785
TERA_HUMANVCPphysical
24424410
CKAP4_HUMANCKAP4physical
25008318
TERA_HUMANVCPphysical
25008318
SNTG2_HUMANSNTG2physical
25008318
TERA_HUMANVCPphysical
24700463

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASSSPECTROMETRY.

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