TRI55_HUMAN - dbPTM
TRI55_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI55_HUMAN
UniProt AC Q9BYV6
Protein Name Tripartite motif-containing protein 55
Gene Name TRIM55
Organism Homo sapiens (Human).
Sequence Length 548
Subcellular Localization Cytoplasm. Nucleus. Nuclear under atrophic conditions and upon mechanical signals. Localizes to the sarcomeric M-band in cardiomyocytes. Colocalizes in part with microtubules (By similarity)..
Protein Description May regulate gene expression and protein turnover in muscle cells..
Protein Sequence MSASLNYKSFSKEQQTMDNLEKQLICPICLEMFTKPVVILPCQHNLCRKCASDIFQASNPYLPTRGGTTMASGGRFRCPSCRHEVVLDRHGVYGLQRNLLVENIIDIYKQESTRPEKKSDQPMCEEHEEERINIYCLNCEVPTCSLCKVFGAHKDCQVAPLTHVFQRQKSELSDGIAILVGSNDRVQGVISQLEDTCKTIEECCRKQKQELCEKFDYLYGILEERKNEMTQVITRTQEEKLEHVRALIKKYSDHLENVSKLVESGIQFMDEPEMAVFLQNAKTLLKKISEASKAFQMEKIEHGYENMNHFTVNLNREEKIIREIDFYREDEDEEEEEGGEGEKEGEGEVGGEAVEVEEVENVQTEFPGEDENPEKASELSQVELQAAPGALPVSSPEPPPALPPAADAPVTQGEVVPTGSEQTTESETPVPAAAETADPLFYPSWYKGQTRKATTNPPCTPGSEGLGQIGPPGSEDSNVRKAEVAAAAASERAAVSGKETSAPAATSQIGFEAPPLQGQAAAPASGSGADSEPARHIFSFSWLNSLNE
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
4Phosphorylation----MSASLNYKSFS
----CCCCCCHHHCC		15.1624719451
9PhosphorylationSASLNYKSFSKEQQT
CCCCCHHHCCHHHHH		25.1324719451
61PhosphorylationIFQASNPYLPTRGGT
HHHHCCCCCCCCCCC		29.57-
93PhosphorylationVLDRHGVYGLQRNLL
EECCCCHHHHHHHHH		19.4023879269
112PhosphorylationIDIYKQESTRPEKKS
HHHHHHCCCCCCCCC		27.5029083192
113PhosphorylationDIYKQESTRPEKKSD
HHHHHCCCCCCCCCC		49.8729083192
170PhosphorylationHVFQRQKSELSDGIA
HHHHHCHHCCCCCEE		35.1228857561
173PhosphorylationQRQKSELSDGIAILV
HHCHHCCCCCEEEEE		29.7328857561
218 (in isoform 4)Phosphorylation-3.21-
220 (in isoform 4)Phosphorylation-18.53-
224 (in isoform 4)Phosphorylation-66.56-
226MethylationYGILEERKNEMTQVI
HHHHHHHHCHHCHHH		61.61-
226"N6,N6-dimethyllysine"YGILEERKNEMTQVI
HHHHHHHHCHHCHHH		61.61-
230PhosphorylationEERKNEMTQVITRTQ
HHHHCHHCHHHHHCH		17.3230377224
234PhosphorylationNEMTQVITRTQEEKL
CHHCHHHHHCHHHHH		28.8930377224
236PhosphorylationMTQVITRTQEEKLEH
HCHHHHHCHHHHHHH		31.5130377224
292PhosphorylationLKKISEASKAFQMEK
HHHHHHHHHHHHHHH		22.0620363803
304PhosphorylationMEKIEHGYENMNHFT
HHHHHHHCCCCCCEE		13.1622468782
311PhosphorylationYENMNHFTVNLNREE
CCCCCCEEECCCHHH		10.84-
525PhosphorylationGQAAAPASGSGADSE
CCCCCCCCCCCCCCC		32.22-
527PhosphorylationAAAPASGSGADSEPA
CCCCCCCCCCCCCCH		28.45-
531PhosphorylationASGSGADSEPARHIF
CCCCCCCCCCHHHHC		44.97-
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 TRI55_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI55_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 TRI55_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_HUMANUBE2Iphysical
15802564
SQSTM_HUMANSQSTM1physical
15802564
UBP5_HUMANUSP5physical
22626734
ATX3_HUMANATXN3physical
22626734
UBP7_HUMANUSP7physical
22626734
OTUB1_HUMANOTUB1physical
22626734
UCHL3_HUMANUCHL3physical
22626734
UBP8_HUMANUSP8physical
22626734
UCHL5_HUMANUCHL5physical
22626734
OTUB2_HUMANOTUB2physical
22626734
ATX3L_HUMANATXN3Lphysical
22626734
UBP28_HUMANUSP28physical
22626734
ESPL1_HUMANESPL1physical
22626734
STAM1_HUMANSTAMphysical
22626734
OTU1_HUMANYOD1physical
22626734
UBP4_HUMANUSP4physical
22626734
UB2D3_HUMANUBE2D3physical
22626734
TRI55_HUMANTRIM55physical
22493164
MDM4_HUMANMDM4physical
22493164
TRI27_HUMANTRIM27physical
22493164
DESM_HUMANDESphysical
18157088
TRI63_HUMANTRIM63physical
18157088
ACTS_HUMANACTA1physical
18157088
MYOTI_HUMANMYOTphysical
18157088
TNNI3_HUMANTNNI3physical
18157088
TNNI2_HUMANTNNI2physical
18157088
TNNI1_HUMANTNNI1physical
18157088
MYPC3_HUMANMYBPC3physical
18157088
MYPC1_HUMANMYBPC1physical
18157088
TITIN_HUMANTTNphysical
18157088
TELT_HUMANTCAPphysical
18157088
NEBU_HUMANNEBphysical
18157088
NEBL_HUMANNEBLphysical
18157088
FLNA_HUMANFLNAphysical
18157088
FLNB_HUMANFLNBphysical
18157088
FLNC_HUMANFLNCphysical
18157088
ANKR1_HUMANANKRD1physical
18157088
FHL2_HUMANFHL2physical
18157088
SQSTM_HUMANSQSTM1physical
18157088
MYOZ1_HUMANMYOZ1physical
18157088
PIAS1_HUMANPIAS1physical
18157088
PIAS3_HUMANPIAS3physical
18157088
PIAS2_HUMANPIAS2physical
18157088
DCAF6_HUMANDCAF6physical
18157088
UXT_HUMANUXTphysical
18157088
GMEB1_HUMANGMEB1physical
18157088
LMCD1_HUMANLMCD1physical
18157088
NOMO1_HUMANNOMO1physical
18157088
EF1G_HUMANEEF1Gphysical
18157088
EFGM_HUMANGFM1physical
18157088
EIF3E_HUMANEIF3Ephysical
18157088
RM41_HUMANMRPL41physical
18157088
RM19_HUMANMRPL19physical
18157088
ECHP_HUMANEHHADHphysical
18157088
TBA8_HUMANEHHADHphysical
18157088
ATPB_HUMANATP5Bphysical
18157088
NDUA1_HUMANNDUFA1physical
18157088
KCRM_HUMANCKMphysical
18157088
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 TRI55_HUMAN

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Related Literatures of Post-Translational Modification

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