S35C2_HUMAN - dbPTM
S35C2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S35C2_HUMAN
UniProt AC Q9NQQ7
Protein Name Solute carrier family 35 member C2
Gene Name SLC35C2
Organism Homo sapiens (Human).
Sequence Length 365
Subcellular Localization Membrane
Multi-pass membrane protein . Golgi apparatus, cis-Golgi network membrane . Endoplasmic reticulum-Golgi intermediate compartment membrane .
Protein Description May play an important role in the cellular response to tissue hypoxia. May be either a GDP-fucose transporter that competes with SLC35C1 for GDP-fucose, or a factor that otherwise enhances the fucosylation of Notch and is required for optimal Notch signaling in mammalian cells..
Protein Sequence MGRWALDVAFLWKAVLTLGLVLLYYCFSIGITFYNKWLTKSFHFPLFMTMLHLAVIFLFSALSRALVQCSSHRARVVLSWADYLRRVAPTALATALDVGLSNWSFLYVTVSLYTMTKSSAVLFILIFSLIFKLEELRAALVLVVLLIAGGLFMFTYKSTQFNVEGFALVLGASFIGGIRWTLTQMLLQKAELGLQNPIDTMFHLQPLMFLGLFPLFAVFEGLHLSTSEKIFRFQDTGLLLRVLGSLFLGGILAFGLGFSEFLLVSRTSSLTLSIAGIFKEVCTLLLAAHLLGDQISLLNWLGFALCLSGISLHVALKALHSRGDGGPKALKGLGSSPDLELLLRSSQREEGDNEEEEYFVAQGQQ
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
101PhosphorylationTALDVGLSNWSFLYV
HHHHHCCCCCCCEEE
30.2624719451
102N-linked_GlycosylationALDVGLSNWSFLYVT
HHHHCCCCCCCEEEE
43.37UniProtKB CARBOHYD
104PhosphorylationDVGLSNWSFLYVTVS
HHCCCCCCCEEEEHH
15.0424719451
107PhosphorylationLSNWSFLYVTVSLYT
CCCCCCEEEEHHHHH
7.6524719451
118PhosphorylationSLYTMTKSSAVLFIL
HHHHCCHHHHHHHHH
17.86-
119PhosphorylationLYTMTKSSAVLFILI
HHHCCHHHHHHHHHH
24.77-
155PhosphorylationAGGLFMFTYKSTQFN
HCCHHHHEECCCCCC
20.4620068231
156PhosphorylationGGLFMFTYKSTQFNV
CCHHHHEECCCCCCC
7.5320068231
265PhosphorylationFSEFLLVSRTSSLTL
CCHHHHHHCCCCCHH
29.7924719451
310 (in isoform 2)Ubiquitination-3.3921890473
314 (in isoform 2)Phosphorylation-8.94-
315 (in isoform 2)Phosphorylation-7.81-
331UbiquitinationDGGPKALKGLGSSPD
CCCCHHHCCCCCCCC
57.8821890473
331UbiquitinationDGGPKALKGLGSSPD
CCCCHHHCCCCCCCC
57.8821890473
335PhosphorylationKALKGLGSSPDLELL
HHHCCCCCCCCHHHH
43.6829255136
336PhosphorylationALKGLGSSPDLELLL
HHCCCCCCCCHHHHH
22.1929255136
345PhosphorylationDLELLLRSSQREEGD
CHHHHHHHHCCCCCC
30.6923186163
346PhosphorylationLELLLRSSQREEGDN
HHHHHHHHCCCCCCC
27.1623186163
358PhosphorylationGDNEEEEYFVAQGQQ
CCCHHHHCHHHCCCC
13.46-
360UbiquitinationNEEEEYFVAQGQQ--
CHHHHCHHHCCCC--
3.6821890473
360 (in isoform 1)Ubiquitination-3.6821890473

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 S35C2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S35C2_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 S35C2_HUMAN !!

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

Oops, there are no PPI records of S35C2_HUMAN !!

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 S35C2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASSSPECTROMETRY.
"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 SER-335, AND MASSSPECTROMETRY.
"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-335, AND MASSSPECTROMETRY.

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