TRI16_HUMAN - dbPTM
TRI16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI16_HUMAN
UniProt AC O95361
Protein Name Tripartite motif-containing protein 16
Gene Name TRIM16
Organism Homo sapiens (Human).
Sequence Length 564
Subcellular Localization Cytoplasm.
Protein Description May play a role in the regulation of keratinocyte differentiation..
Protein Sequence MAELDLMAPGPLPRATAQPPAPLSPDSGSPSPDSGSASPVEEEDVGSSEKLGRETEEQDSDSAEQGDPAGEGKEVLCDFCLDDTRRVKAVKSCLTCMVNYCEEHLQPHQVNIKLQSHLLTEPVKDHNWRYCPAHHSPLSAFCCPDQQCICQDCCQEHSGHTIVSLDAARRDKEAELQCTQLDLERKLKLNENAISRLQANQKSVLVSVSEVKAVAEMQFGELLAAVRKAQANVMLFLEEKEQAALSQANGIKAHLEYRSAEMEKSKQELERMAAISNTVQFLEEYCKFKNTEDITFPSVYVGLKDKLSGIRKVITESTVHLIQLLENYKKKLQEFSKEEEYDIRTQVSAVVQRKYWTSKPEPSTREQFLQYAYDITFDPDTAHKYLRLQEENRKVTNTTPWEHPYPDLPSRFLHWRQVLSQQSLYLHRYYFEVEIFGAGTYVGLTCKGIDRKGEERNSCISGNNFSWSLQWNGKEFTAWYSDMETPLKAGPFRRLGVYIDFPGGILSFYGVEYDTMTLVHKFACKFSEPVYAAFWLSKKENAIRIVDLGEEPEKPAPSLVGTAP
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
16PhosphorylationPGPLPRATAQPPAPL
CCCCCCCCCCCCCCC		27.4029496963
24PhosphorylationAQPPAPLSPDSGSPS
CCCCCCCCCCCCCCC		26.1228355574
27PhosphorylationPAPLSPDSGSPSPDS
CCCCCCCCCCCCCCC		44.5525159151
29PhosphorylationPLSPDSGSPSPDSGS
CCCCCCCCCCCCCCC		26.5925159151
31PhosphorylationSPDSGSPSPDSGSAS
CCCCCCCCCCCCCCC		42.9325159151
34PhosphorylationSGSPSPDSGSASPVE
CCCCCCCCCCCCCCC		37.7225159151
36PhosphorylationSPSPDSGSASPVEEE
CCCCCCCCCCCCCHH		29.5323927012
38PhosphorylationSPDSGSASPVEEEDV
CCCCCCCCCCCHHHC		31.0423927012
47PhosphorylationVEEEDVGSSEKLGRE
CCHHHCCCCHHHCCC		34.8620873877
48PhosphorylationEEEDVGSSEKLGRET
CHHHCCCCHHHCCCC		32.5920873877
50UbiquitinationEDVGSSEKLGRETEE
HHCCCCHHHCCCCCC		59.18-
55PhosphorylationSEKLGRETEEQDSDS
CHHHCCCCCCCCCCC		43.3822167270
60PhosphorylationRETEEQDSDSAEQGD
CCCCCCCCCCHHHCC		32.9129255136
62PhosphorylationTEEQDSDSAEQGDPA
CCCCCCCCHHHCCCC		37.3429255136
116PhosphorylationQVNIKLQSHLLTEPV
HEEEEEECCCCCCCC		26.9227693506
172UbiquitinationLDAARRDKEAELQCT
HHHHHCCHHHHHHHC		57.94-
188MethylationLDLERKLKLNENAIS
HHHHHHHCCCHHHHH		52.91116251963
188UbiquitinationLDLERKLKLNENAIS
HHHHHHHCCCHHHHH		52.91-
202UbiquitinationSRLQANQKSVLVSVS
HHHHHCCCEEEEEHH		42.19-
203PhosphorylationRLQANQKSVLVSVSE
HHHHCCCEEEEEHHH		15.7727693506
240UbiquitinationVMLFLEEKEQAALSQ
EEEEEHHHHHHHHHH		45.83-
252UbiquitinationLSQANGIKAHLEYRS
HHHHHCHHHHHHHHH		31.02-
264AcetylationYRSAEMEKSKQELER
HHHHHHHHHHHHHHH		62.7419822899
266AcetylationSAEMEKSKQELERMA
HHHHHHHHHHHHHHH		59.8819822907
289UbiquitinationLEEYCKFKNTEDITF
HHHHHCCCCCCCCCC		48.75-
304UbiquitinationPSVYVGLKDKLSGIR
CCHHHHHHHHHCCHH		47.06-
306UbiquitinationVYVGLKDKLSGIRKV
HHHHHHHHHCCHHHH		42.86-
308PhosphorylationVGLKDKLSGIRKVIT
HHHHHHHCCHHHHHC		37.6024719451
329UbiquitinationIQLLENYKKKLQEFS
HHHHHHHHHHHHHCC		55.82-
331UbiquitinationLLENYKKKLQEFSKE
HHHHHHHHHHHCCHH		51.77-
337UbiquitinationKKLQEFSKEEEYDIR
HHHHHCCHHHHCCHH		74.58-
341PhosphorylationEFSKEEEYDIRTQVS
HCCHHHHCCHHHHHH		21.6825106551
345PhosphorylationEEEYDIRTQVSAVVQ
HHHCCHHHHHHHHHH		33.3926074081
348PhosphorylationYDIRTQVSAVVQRKY
CCHHHHHHHHHHHHH		12.9126074081
354UbiquitinationVSAVVQRKYWTSKPE
HHHHHHHHHCCCCCC		28.22-
355PhosphorylationSAVVQRKYWTSKPEP
HHHHHHHHCCCCCCC		18.9926074081
357PhosphorylationVVQRKYWTSKPEPST
HHHHHHCCCCCCCCH		24.6326074081
358PhosphorylationVQRKYWTSKPEPSTR
HHHHHCCCCCCCCHH		31.8726074081
359UbiquitinationQRKYWTSKPEPSTRE
HHHHCCCCCCCCHHH		46.13-
363PhosphorylationWTSKPEPSTREQFLQ
CCCCCCCCHHHHHHH		38.1326074081
364PhosphorylationTSKPEPSTREQFLQY
CCCCCCCHHHHHHHH		49.2826074081
384UbiquitinationFDPDTAHKYLRLQEE
CCCHHHHHHHHHHHH		43.44-
429PhosphorylationQSLYLHRYYFEVEIF
HCHHEEEEEEEEEEE		11.1927811184
430PhosphorylationSLYLHRYYFEVEIFG
CHHEEEEEEEEEEEC		8.01-
441PhosphorylationEIFGAGTYVGLTCKG
EEECCCCEEEEEEEC		7.51-
445PhosphorylationAGTYVGLTCKGIDRK
CCCEEEEEEECCCCC		13.2727811184
531PhosphorylationCKFSEPVYAAFWLSK
HCCCCCCHHHHEEEC		11.7019664994
537PhosphorylationVYAAFWLSKKENAIR
CHHHHEEECCCCEEE		32.0719664994
554UbiquitinationDLGEEPEKPAPSLVG
ECCCCCCCCCCCCCC		58.14-
558PhosphorylationEPEKPAPSLVGTAP-
CCCCCCCCCCCCCC-		37.4828555341
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 TRI16_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI16_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 TRI16_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
E2F1_HUMANE2F1physical
20729920
A4_HUMANAPPphysical
21832049
CLU_HUMANCLUHphysical
22863883
MCM7_HUMANMCM7physical
22863883
TOM34_HUMANTOMM34physical
22863883
TR16L_HUMANTRIM16Lphysical
26186194
TR16L_HUMANTRIM16Lphysical
28514442
OPTN_HUMANOPTNphysical
28514442
LEG3_HUMANLGALS3physical
27693506
ULK1_HUMANULK1physical
27693506
CUL4A_HUMANCUL4Aphysical
27693506
BECN1_HUMANBECN1physical
27693506
A16L1_HUMANATG16L1physical
27693506
CUL5_HUMANCUL5physical
27693506
DPTOR_HUMANDEPTORphysical
27693506
RRAGB_HUMANRRAGBphysical
27693506
RRAGD_HUMANRRAGDphysical
27693506
TFEB_HUMANTFEBphysical
27693506
PP2BB_HUMANPPP3CBphysical
27693506
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 TRI16_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory