TUSC3_HUMAN - dbPTM
TUSC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TUSC3_HUMAN
UniProt AC Q13454
Protein Name Tumor suppressor candidate 3
Gene Name TUSC3
Organism Homo sapiens (Human).
Sequence Length 348
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with MAGT1. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition.; Magnesium transporter..
Protein Sequence MGARGAPSRRRQAGRRLRYLPTGSFPFLLLLLLLCIQLGGGQKKKENLLAEKVEQLMEWSSRRSIFRMNGDKFRKFIKAPPRNYSMIVMFTALQPQRQCSVCRQANEEYQILANSWRYSSAFCNKLFFSMVDYDEGTDVFQQLNMNSAPTFMHFPPKGRPKRADTFDLQRIGFAAEQLAKWIADRTDVHIRVFRPPNYSGTIALALLVSLVGGLLYLRRNNLEFIYNKTGWAMVSLCIVFAMTSGQMWNHIRGPPYAHKNPHNGQVSYIHGSSQAQFVAESHIILVLNAAITMGMVLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPYSDLDFE
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
63DimethylationLMEWSSRRSIFRMNG
HHHHHHHHHHHHHCH
35.73-
63MethylationLMEWSSRRSIFRMNG
HHHHHHHHHHHHHCH
35.7358855423
67DimethylationSSRRSIFRMNGDKFR
HHHHHHHHHCHHHHH
18.91-
67MethylationSSRRSIFRMNGDKFR
HHHHHHHHHCHHHHH
18.9158855429
72AcetylationIFRMNGDKFRKFIKA
HHHHCHHHHHHHHCC
48.7627452117
109PhosphorylationCRQANEEYQILANSW
HHHHCHHHHHHHHHH
8.4824043423
115PhosphorylationEYQILANSWRYSSAF
HHHHHHHHHHHCHHH
13.8124043423
124UbiquitinationRYSSAFCNKLFFSMV
HHCHHHHHHHHHHCC
37.3021987572
180UbiquitinationFAAEQLAKWIADRTD
HHHHHHHHHHHHCCC
47.9621987572
180 (in isoform 2)Ubiquitination-47.9620972266
216PhosphorylationSLVGGLLYLRRNNLE
HHHHHHHHHHHCCCC
11.82-
281PhosphorylationQAQFVAESHIILVLN
HHHHHHHHHHHHHHH
15.39-
292PhosphorylationLVLNAAITMGMVLLN
HHHHHHHHHHHHHHH
11.71-
327PhosphorylationGLVVFFFSFLLSIFR
HHHHHHHHHHHHHHH
15.1619276368
331PhosphorylationFFFSFLLSIFRSKYH
HHHHHHHHHHHHHHC
23.1019276368

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 TUSC3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TUSC3_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 TUSC3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPN2_HUMANRPN2physical
28514442
F122B_HUMANFAM122Bphysical
28514442
STXB2_HUMANSTXBP2physical
28514442
LIN54_HUMANLIN54physical
28514442
STXB1_HUMANSTXBP1physical
28514442
NDRG3_HUMANNDRG3physical
28514442
GGT7_HUMANGGT7physical
28514442
NHRF2_HUMANSLC9A3R2physical
28514442

Drug and Disease Associations
Kegg Disease
H00768 Nonsyndromic autosomal recessive mental retardation (NS-ARMR)
OMIM Disease
611093Mental retardation, autosomal recessive 7 (MRT7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TUSC3_HUMAN

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Related Literatures of Post-Translational Modification

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