TRI59_HUMAN - dbPTM
TRI59_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI59_HUMAN
UniProt AC Q8IWR1
Protein Name Tripartite motif-containing protein 59
Gene Name TRIM59
Organism Homo sapiens (Human).
Sequence Length 403
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein .
Protein Description May serve as a multifunctional regulator for innate immune signaling pathways..
Protein Sequence MHNFEEELTCPICYSIFEDPRVLPCSHTFCRNCLENILQASGNFYIWRPLRIPLKCPNCRSITEIAPTGIESLPVNFALRAIIEKYQQEDHPDIVTCPEHYRQPLNVYCLLDKKLVCGHCLTIGQHHGHPIDDLQSAYLKEKDTPQKLLEQLTDTHWTDLTHLIEKLKEQKSHSEKMIQGDKEAVLQYFKELNDTLEQKKKSFLTALCDVGNLINQEYTPQIERMKEIREQQLELMALTISLQEESPLKFLEKVDDVRQHVQILKQRPLPEVQPVEIYPRVSKILKEEWSRTEIGQIKNVLIPKMKISPKRMSCSWPGKDEKEVEFLKILNIVVVTLISVILMSILFFNQHIITFLSEITLIWFSEASLSVYQSLSNSLHKVKNILCHIFYLLKEFVWKIVSH
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
61PhosphorylationLKCPNCRSITEIAPT
CCCCCCCCEEEECCC
35.7427080861
63PhosphorylationCPNCRSITEIAPTGI
CCCCCCEEEECCCCH
23.6827080861
85UbiquitinationALRAIIEKYQQEDHP
HHHHHHHHHHCCCCC
37.6433845483
171UbiquitinationIEKLKEQKSHSEKMI
HHHHHHCCCCCHHHH
51.7522817900
176UbiquitinationEQKSHSEKMIQGDKE
HCCCCCHHHHHCCHH
44.3022817900
182AcetylationEKMIQGDKEAVLQYF
HHHHHCCHHHHHHHH
55.1623236377
1992-HydroxyisobutyrylationLNDTLEQKKKSFLTA
HHHHHHHHHHHHHHH
53.44-
246PhosphorylationTISLQEESPLKFLEK
HHHCCCCCCHHHHHH
34.4824719451
249UbiquitinationLQEESPLKFLEKVDD
CCCCCCHHHHHHHHH
51.8122817900
253UbiquitinationSPLKFLEKVDDVRQH
CCHHHHHHHHHHHHH
53.7821906983
278PhosphorylationEVQPVEIYPRVSKIL
CCCCCEEHHHHHHHH
3.2821552520
298UbiquitinationRTEIGQIKNVLIPKM
CCCHHHHCCEEECCC
32.8722817900
298AcetylationRTEIGQIKNVLIPKM
CCCHHHHCCEEECCC
32.8721339330
304AcetylationIKNVLIPKMKISPKR
HCCEEECCCCCCCCC
45.9221339330
306AcetylationNVLIPKMKISPKRMS
CEEECCCCCCCCCCC
46.2721339330
308PhosphorylationLIPKMKISPKRMSCS
EECCCCCCCCCCCCC
20.8924719451
310AcetylationPKMKISPKRMSCSWP
CCCCCCCCCCCCCCC
54.687681813

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
308SPhosphorylationKinaseCDK5Q00535
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI59_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 TRI59_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECSIT_HUMANECSITphysical
22588174
P53_HUMANTP53physical
25046164

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 TRI59_HUMAN

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Related Literatures of Post-Translational Modification

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