SC61B_HUMAN - dbPTM
SC61B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC61B_HUMAN
UniProt AC P60468
Protein Name Protein transport protein Sec61 subunit beta
Gene Name SEC61B
Organism Homo sapiens (Human).
Sequence Length 96
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein.
Protein Description Necessary for protein translocation in the endoplasmic reticulum..
Protein Sequence MPGPTPSGTNVGSSGRSPSKAVAARAAGSTVRQRKNASCGTRSAGRTTSAGTGGMWRFYTEDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS
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
2Acetylation------MPGPTPSGT
------CCCCCCCCC
58.4321406692
5Phosphorylation---MPGPTPSGTNVG
---CCCCCCCCCCCC
35.6829255136
7Phosphorylation-MPGPTPSGTNVGSS
-CCCCCCCCCCCCCC
61.8129255136
9PhosphorylationPGPTPSGTNVGSSGR
CCCCCCCCCCCCCCC
30.9429255136
13PhosphorylationPSGTNVGSSGRSPSK
CCCCCCCCCCCCHHH
25.9029255136
13O-linked_GlycosylationPSGTNVGSSGRSPSK
CCCCCCCCCCCCHHH
25.9028510447
14PhosphorylationSGTNVGSSGRSPSKA
CCCCCCCCCCCHHHH
32.0929255136
14O-linked_GlycosylationSGTNVGSSGRSPSKA
CCCCCCCCCCCHHHH
32.0928510447
17PhosphorylationNVGSSGRSPSKAVAA
CCCCCCCCHHHHHHH
36.7329255136
19PhosphorylationGSSGRSPSKAVAARA
CCCCCCHHHHHHHHH
34.2022167270
20UbiquitinationSSGRSPSKAVAARAA
CCCCCHHHHHHHHHC
50.7124816145
29PhosphorylationVAARAAGSTVRQRKN
HHHHHCCCCHHHHCC
21.0029900121
30PhosphorylationAARAAGSTVRQRKNA
HHHHCCCCHHHHCCC
20.8423403867
38PhosphorylationVRQRKNASCGTRSAG
HHHHCCCCCCCCCCC
23.6024719451
39S-palmitoylationRQRKNASCGTRSAGR
HHHCCCCCCCCCCCC
6.3221044946
43PhosphorylationNASCGTRSAGRTTSA
CCCCCCCCCCCCCCC
34.6122199227
47PhosphorylationGTRSAGRTTSAGTGG
CCCCCCCCCCCCCCC
24.9623403867
48PhosphorylationTRSAGRTTSAGTGGM
CCCCCCCCCCCCCCC
18.4123403867
49PhosphorylationRSAGRTTSAGTGGMW
CCCCCCCCCCCCCCE
24.8826846344
52PhosphorylationGRTTSAGTGGMWRFY
CCCCCCCCCCCEEEE
30.2223403867
59PhosphorylationTGGMWRFYTEDSPGL
CCCCEEEEECCCCCC
10.7228152594
59NitrationTGGMWRFYTEDSPGL
CCCCEEEEECCCCCC
10.72-
60PhosphorylationGGMWRFYTEDSPGLK
CCCEEEEECCCCCCC
30.5128152594
63PhosphorylationWRFYTEDSPGLKVGP
EEEEECCCCCCCCCC
18.0321815630

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 SC61B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SC61B_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 SC61B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APOB_HUMANAPOBphysical
9565615
BAG6_HUMANBAG6physical
20676083
GET4_HUMANGET4physical
20676083
UBL4A_HUMANUBL4Aphysical
20676083
ASNA_HUMANASNA1physical
20676083
BAP31_HUMANBCAP31physical
18555783
EGFR_HUMANEGFRphysical
19602593
S61A1_HUMANSEC61A1physical
9585408
SPC25_HUMANSPC25physical
9585408
SC61B_HUMANSEC61Bphysical
9585408
RAGE_HUMANAGERphysical
10601334
SGTA_HUMANSGTAphysical
23533635
SGTA_HUMANSGTAphysical
20516149
CALX_HUMANCANXphysical
26344197
LTN1_HUMANLTN1physical
25877867
SSRA_HUMANSSR1physical
25877867
RL6_HUMANRPL6physical
25877867
RS9_HUMANRPS9physical
25877867
S61A1_HUMANSEC61A1physical
26085089

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 SC61B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; SER-7; SER-14 ANDSER-17, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; SER-14; SER-17 ANDSER-19, AND MASS SPECTROMETRY.
"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-13; SER-14 AND SER-17,AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-19; SER-29 ANDTHR-30, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASSSPECTROMETRY.

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