TRI65_HUMAN - dbPTM
TRI65_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI65_HUMAN
UniProt AC Q6PJ69
Protein Name Tripartite motif-containing protein 65
Gene Name TRIM65
Organism Homo sapiens (Human).
Sequence Length 517
Subcellular Localization
Protein Description
Protein Sequence MAAQLLEEKLTCAICLGLYQDPVTLPCGHNFCGACIRDWWDRCGKACPECREPFPDGAELRRNVALSGVLEVVRAGPARDPGPDPGPGPDPAARCPRHGRPLELFCRTEGRCVCSVCTVRECRLHERALLDAERLKREAQLRASLEVTQQQATQAEGQLLELRKQSSQIQNSACILASWVSGKFSSLLQALEIQHTTALRSIEVAKTQALAQARDEEQRLRVHLEAVARHGCRIRELLEQVDEQTFLQESQLLQPPGPLGPLTPLQWDEDQQLGDLKQLLSRLCGLLLEEGSHPGAPAKPVDLAPVEAPGPLAPVPSTVCPLRRKLWQNYRNLTFDPVSANRHFYLSRQDQQVKHCRQSRGPGGPGSFELWQVQCAQSFQAGHHYWEVRASDHSVTLGVSYPQLPRCRLGPHTDNIGRGPCSWGLCVQEDSLQAWHNGEAQRLPGVSGRLLGMDLDLASGCLTFYSLEPQTQPLYTFHALFNQPLTPVFWLLEGRTLTLCHQPGAVFPLGPQEEVLS
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------MAAQLLEEK
------CHHHHHHHH
12.1522223895
144PhosphorylationREAQLRASLEVTQQQ
HHHHHHHHHHHHHHH
20.7322210691
148PhosphorylationLRASLEVTQQQATQA
HHHHHHHHHHHHHHH
15.9822210691
153PhosphorylationEVTQQQATQAEGQLL
HHHHHHHHHHHHHHH
24.7922210691
167PhosphorylationLELRKQSSQIQNSAC
HHHHHHCHHHHHHHH
28.89-
185PhosphorylationSWVSGKFSSLLQALE
HHHHCHHHHHHHHHH
24.46-
206UbiquitinationLRSIEVAKTQALAQA
HHHHHHHHHHHHHHC
46.4727667366
219UbiquitinationQARDEEQRLRVHLEA
HCCCHHHHHHHHHHH
27.9527667366
277UbiquitinationDQQLGDLKQLLSRLC
CCCHHHHHHHHHHHH
43.57-
299UbiquitinationSHPGAPAKPVDLAPV
CCCCCCCCCCCCCCC
44.5129967540
317PhosphorylationGPLAPVPSTVCPLRR
CCCCCCCCCCCHHHH
33.4332142685
325UbiquitinationTVCPLRRKLWQNYRN
CCCHHHHHHHHHHHC
47.8721906983
334PhosphorylationWQNYRNLTFDPVSAN
HHHHHCCCCCCCCCC
29.5528857561
338UbiquitinationRNLTFDPVSANRHFY
HCCCCCCCCCCCCEE
10.1921890473
339PhosphorylationNLTFDPVSANRHFYL
CCCCCCCCCCCCEEE
25.8032142685
342MethylationFDPVSANRHFYLSRQ
CCCCCCCCCEEECHH
22.47115918961
367PhosphorylationRGPGGPGSFELWQVQ
CCCCCCCCEEEEEEE
20.77-
413PhosphorylationRCRLGPHTDNIGRGP
CCCCCCCCCCCCCCC
33.60-

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 TRI65_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI65_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 TRI65_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MKRN3_HUMANMKRN3physical
22493164
TNR6A_HUMANTNRC6Aphysical
24778252

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 TRI65_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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