TMTC3_HUMAN - dbPTM
TMTC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMTC3_HUMAN
UniProt AC Q6ZXV5
Protein Name Transmembrane and TPR repeat-containing protein 3
Gene Name TMTC3
Organism Homo sapiens (Human).
Sequence Length 915
Subcellular Localization Membrane
Multi-pass membrane protein . Endoplasmic reticulum . In odontoblast cultures, it colocalizes with PDIA3 in the endoplasmic reticulum.
Protein Description Involved in the positive regulation of proteasomal protein degradation in the endoplasmic reticulum (ER), and the control of ER stress response..
Protein Sequence MANINLKEITLIVGVVTACYWNSLFCGFVFDDVSAILDNKDLHPSTPLKTLFQNDFWGTPMSEERSHKSYRPLTVLTFRLNYLLSELKPMSYHLLNMIFHAVVSVIFLKVCKLFLDNKSSVIASLLFAVHPIHTEAVTGVVGRAELLSSIFFLAAFLSYTRSKGPDNSIIWTPIALTVFLVAVATLCKEQGITVVGICCVYEVFIAQGYTLPLLCTTAGQFLRGKGSIPFSMLQTLVKLIVLMFSTLLLVVIRVQVIQSQLPVFTRFDNPAAVSPTPTRQLTFNYLLPVNAWLLLNPSELCCDWTMGTIPLIESLLDIRNLATFTFFCFLGMLGVFSIRYSGDSSKTVLMALCLMALPFIPASNLFFPVGFVVAERVLYVPSMGFCILVAHGWQKISTKSVFKKLSWICLSMVILTHSLKTFHRNWDWESEYTLFMSALKVNKNNAKLWNNVGHALENEKNFERALKYFLQATHVQPDDIGAHMNVGRTYKNLNRTKEAEESYMMAKSLMPQIIPGKKYAARIAPNHLNVYINLANLIRANESRLEEADQLYRQAISMRPDFKQAYISRGELLLKMNKPLKAKEAYLKALELDRNNADLWYNLAIVHIELKEPNEALKKNFNRALELNPKHKLALFNSAIVMQESGEVKLRPEARKRLLSYINEEPLDANGYFNLGMLAMDDKKDNEAEIWMKKAIKLQADFRSALFNLALLYSQTAKELKALPILEELLRYYPDHIKGLILKGDILMNQKKDILGAKKCFERILEMDPSNVQGKHNLCVVYFEEKDLLKAERCLLETLALAPHEEYIQRHLNIVRDKISSSSFIEPIFPTSKISSVEGKKIPTESVKEIRGESRQTQIVKTSDNKSQSKSNKQLGKNGDEETPHKTTKDIKEIEKKRVAALKRLEEIERILNGE
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
50PhosphorylationHPSTPLKTLFQNDFW
CCCCCHHHHHCCCCC
40.2524719451
50 (in isoform 2)Phosphorylation-40.2524719451
66 (in isoform 2)Phosphorylation-38.2524719451
66PhosphorylationTPMSEERSHKSYRPL
CCCCCCCCCCCCCCC
38.2524719451
117N-linked_GlycosylationVCKLFLDNKSSVIAS
HHHHHHCCHHHHHHH
48.53UniProtKB CARBOHYD
227PhosphorylationQFLRGKGSIPFSMLQ
HHHCCCCCCCHHHHH
30.4921406692
231PhosphorylationGKGSIPFSMLQTLVK
CCCCCCHHHHHHHHH
17.1521406692
235PhosphorylationIPFSMLQTLVKLIVL
CCHHHHHHHHHHHHH
29.5621406692
274PhosphorylationFDNPAAVSPTPTRQL
CCCCCCCCCCCCCCE
20.52-
337O-linked_GlycosylationLGMLGVFSIRYSGDS
HHHHHHHHCCCCCCC
12.0729351928
460UbiquitinationGHALENEKNFERALK
HHHHHCHHHHHHHHH
77.7621890473
460 (in isoform 2)Ubiquitination-77.7621890473
460 (in isoform 1)Ubiquitination-77.7621890473
468PhosphorylationNFERALKYFLQATHV
HHHHHHHHHHHHCCC
15.4624719451
473PhosphorylationLKYFLQATHVQPDDI
HHHHHHHCCCCCCHH
15.0424719451
490PhosphorylationHMNVGRTYKNLNRTK
HCCCCCHHHCCCCCH
9.12-
494N-linked_GlycosylationGRTYKNLNRTKEAEE
CCHHHCCCCCHHHHH
59.99UniProtKB CARBOHYD
503 (in isoform 2)Phosphorylation-8.32-
503PhosphorylationTKEAEESYMMAKSLM
CHHHHHHHHHHHHHC
8.3218669648
5172-HydroxyisobutyrylationMPQIIPGKKYAARIA
CCCCCCCCCHHHHHC
36.94-
541N-linked_GlycosylationLANLIRANESRLEEA
HHHHHHHCHHHHHHH
37.62UniProtKB CARBOHYD
552PhosphorylationLEEADQLYRQAISMR
HHHHHHHHHHHHHCC
8.6121406692
563AcetylationISMRPDFKQAYISRG
HHCCCCHHHHHHHHH
41.2026051181
737 (in isoform 2)Ubiquitination-5.0221890473
7382-HydroxyisobutyrylationRYYPDHIKGLILKGD
HHCCHHHCEEEECCC
44.22-
738 (in isoform 1)Ubiquitination-44.2221890473
738UbiquitinationRYYPDHIKGLILKGD
HHCCHHHCEEEECCC
44.2221890473
743AcetylationHIKGLILKGDILMNQ
HHCEEEECCCHHHCC
47.767711367
782PhosphorylationKHNLCVVYFEEKDLL
CCEEEEEEECHHHHH
5.72-
821PhosphorylationIVRDKISSSSFIEPI
HHHHHHCCCCCCCCC
33.2124114839
823PhosphorylationRDKISSSSFIEPIFP
HHHHCCCCCCCCCCC
31.99-
831O-linked_GlycosylationFIEPIFPTSKISSVE
CCCCCCCCCCCEECC
31.72OGP
832PhosphorylationIEPIFPTSKISSVEG
CCCCCCCCCCEECCC
28.3824114839
844O-linked_GlycosylationVEGKKIPTESVKEIR
CCCCCCCCHHHHHHC
44.35OGP
857PhosphorylationIRGESRQTQIVKTSD
HCCCCCCEEEEECCC
21.1029083192
887PhosphorylationDEETPHKTTKDIKEI
CCCCCCCCHHHHHHH
35.7226074081
888PhosphorylationEETPHKTTKDIKEIE
CCCCCCCHHHHHHHH
31.3626074081
896AcetylationKDIKEIEKKRVAALK
HHHHHHHHHHHHHHH
52.0912433699
897AcetylationDIKEIEKKRVAALKR
HHHHHHHHHHHHHHH
39.0412433707

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 TMTC3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMTC3_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 TMTC3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COTL1_HUMANCOTL1physical
26344197

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 TMTC3_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 TYR-503, AND MASSSPECTROMETRY.

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