TRI54_HUMAN - dbPTM
TRI54_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI54_HUMAN
UniProt AC Q9BYV2
Protein Name Tripartite motif-containing protein 54
Gene Name TRIM54
Organism Homo sapiens (Human).
Sequence Length 358
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. Associates with microtubules. Localizes to the Z-lines in skeletal muscles (By similarity)..
Protein Description May bind and stabilize microtubules during myotubes formation..
Protein Sequence MNFTVGFKPLLGDAHSMDNLEKQLICPICLEMFSKPVVILPCQHNLCRKCANDVFQASNPLWQSRGSTTVSSGGRFRCPSCRHEVVLDRHGVYGLQRNLLVENIIDIYKQESSRPLHSKAEQHLMCEEHEEEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTIYKRQKSELSDGIAMLVAGNDRVQAVITQMEEVCQTIEDNSRRQKQLLNQRFESLCAVLEERKGELLQALAREQEEKLQRVRGLIRQYGDHLEASSKLVESAIQSMEEPQMALYLQQAKELINKVGAMSKVELAGRPEPGYESMEQFTVRVEHVAEMLRTIDFQPGASGEEEEVAPDGEEGSAGPEEERPDGP
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
34PhosphorylationPICLEMFSKPVVILP
HHHHHHCCCCEEEEE		34.4425219547
93PhosphorylationVLDRHGVYGLQRNLL
EECCCCHHHHHHHHH		19.4023879269
171AcetylationPTIYKRQKSELSDGI
CCHHHHCHHHCCCCE		50.3520167786
172PhosphorylationTIYKRQKSELSDGIA
CHHHHCHHHCCCCEE		35.1226437602
176 (in isoform 2)Phosphorylation-66.21-
190 (in isoform 2)Phosphorylation-7.5722210691
206 (in isoform 2)Phosphorylation-40.9622210691
209 (in isoform 2)Phosphorylation-36.4222210691
347PhosphorylationAPDGEEGSAGPEEER
CCCCCCCCCCCCCCC		33.0722673903
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 TRI54_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI54_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 TRI54_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI63_HUMANTRIM63physical
11243782
PERF_HUMANPRF1physical
17360532
FLNC_HUMANFLNCphysical
17360532
UBP5_HUMANUSP5physical
22626734
ATX3_HUMANATXN3physical
22626734
UBP7_HUMANUSP7physical
22626734
OTUB1_HUMANOTUB1physical
22626734
JOS1_HUMANJOSD1physical
22626734
UCHL3_HUMANUCHL3physical
22626734
UBP8_HUMANUSP8physical
22626734
UCHL5_HUMANUCHL5physical
22626734
OTUB2_HUMANOTUB2physical
22626734
ATX3L_HUMANATXN3Lphysical
22626734
UBP33_HUMANUSP33physical
22626734
UBP15_HUMANUSP15physical
22626734
UBP18_HUMANUSP18physical
22626734
STAM1_HUMANSTAMphysical
22626734
UBP2_HUMANUSP2physical
22626734
OTU1_HUMANYOD1physical
22626734
UCHL1_HUMANUCHL1physical
22626734
UBP21_HUMANUSP21physical
22626734
SENP3_HUMANSENP3physical
22626734
UBP4_HUMANUSP4physical
22626734
UB2D3_HUMANUBE2D3physical
22626734
TRI54_HUMANTRIM54physical
25416956
TSH3_HUMANTSHZ3physical
25416956
CC146_HUMANCCDC146physical
25416956
LSM2_HUMANLSM2physical
25416956
ZN250_HUMANZNF250physical
25416956
CARD9_HUMANCARD9physical
25416956
GMCL1_HUMANGMCL1physical
25416956
EAF6_HUMANMEAF6physical
25416956
TTC23_HUMANTTC23physical
25416956
RSRC2_HUMANRSRC2physical
25416956
OTUB2_HUMANOTUB2physical
25416956
SCNM1_HUMANSCNM1physical
25416956
LENG1_HUMANLENG1physical
25416956
CL049_HUMANC12orf49physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
F124B_HUMANFAM124Bphysical
25416956
F110A_HUMANFAM110Aphysical
25416956
USBP1_HUMANUSHBP1physical
25416956
ENKD1_HUMANENKD1physical
25416956
F161A_HUMANFAM161Aphysical
25416956
GTD2A_HUMANGTF2IRD2physical
25416956
ZGPAT_HUMANZGPATphysical
25416956
LNX1_HUMANLNX1physical
25416956
ZN587_HUMANZNF587physical
25416956
FBF1_HUMANFBF1physical
25416956
WDR34_HUMANWDR34physical
25416956
DTX2_HUMANDTX2physical
25416956
C1QT2_HUMANC1QTNF2physical
25416956
HAUS1_HUMANHAUS1physical
25416956
SH21B_HUMANSH2D1Bphysical
25416956
ADIP_HUMANSSX2IPphysical
25416956
CA216_HUMANC1orf216physical
25416956
ZN572_HUMANZNF572physical
25416956
C19L2_HUMANCWF19L2physical
25416956
ZN417_HUMANZNF417physical
25416956
C2CD6_HUMANALS2CR11physical
25416956
IQUB_HUMANIQUBphysical
25416956
DEUP1_HUMANCCDC67physical
25416956
PPR18_HUMANPPP1R18physical
25416956
ADCY4_HUMANADCY4physical
25416956
CENPX_HUMANSTRA13physical
25416956
F124A_HUMANFAM124Aphysical
25416956
CE57L_HUMANCEP57L1physical
25416956
K2C6C_HUMANKRT6Cphysical
25416956
KLH38_HUMANKLHL38physical
25416956
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 TRI54_HUMAN

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Related Literatures of Post-Translational Modification

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