TSN_HUMAN - dbPTM
TSN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TSN_HUMAN
UniProt AC Q15631
Protein Name Translin
Gene Name TSN
Organism Homo sapiens (Human).
Sequence Length 228
Subcellular Localization Cytoplasm . Nucleus .
Protein Description DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. Seems to recognize single-stranded DNA ends generated by staggered breaks occurring at recombination hot spots.; Exhibits both single-stranded and double-stranded endoribonuclease activity. May act as an activator of RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand..
Protein Sequence MSVSEIFVELQGFLAAEQDIREEIRKVVQSLEQTAREILTLLQGVHQGAGFQDIPKRCLKAREHFGTVKTHLTSLKTKFPAEQYYRFHEHWRFVLQRLVFLAAFVVYLETETLVTREAVTEILGIEPDREKGFHLDVEDYLSGVLILASELSRLSVNSVTAGDYSRPLHISTFINELDSGFRLLNLKNDSLRKRYDGLKYDVKKVEEVVYDLSIRGFNKETAAACVEK
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
30PhosphorylationEIRKVVQSLEQTARE
HHHHHHHHHHHHHHH		23.4326699800
34PhosphorylationVVQSLEQTAREILTL
HHHHHHHHHHHHHHH		20.5026699800
56AcetylationAGFQDIPKRCLKARE
CCCCCHHHHHHHHHH		56.9526051181
56UbiquitinationAGFQDIPKRCLKARE
CCCCCHHHHHHHHHH		56.9521890473
562-HydroxyisobutyrylationAGFQDIPKRCLKARE
CCCCCHHHHHHHHHH		56.95-
56UbiquitinationAGFQDIPKRCLKARE
CCCCCHHHHHHHHHH		56.9521890473
69UbiquitinationREHFGTVKTHLTSLK
HHHHCCHHHHHHHHC		30.02-
70PhosphorylationEHFGTVKTHLTSLKT
HHHCCHHHHHHHHCC		20.13-
76UbiquitinationKTHLTSLKTKFPAEQ
HHHHHHHCCCCCHHH		49.81-
78AcetylationHLTSLKTKFPAEQYY
HHHHHCCCCCHHHHH		48.0025953088
84PhosphorylationTKFPAEQYYRFHEHW
CCCCHHHHHHHHHHH		6.5228152594
85PhosphorylationKFPAEQYYRFHEHWR
CCCHHHHHHHHHHHH		13.3928152594
152O-linked_GlycosylationLILASELSRLSVNSV
HHHHHHHHCCCCCCC		27.4223301498
160PhosphorylationRLSVNSVTAGDYSRP
CCCCCCCCCCCCCCC		25.4128152594
164PhosphorylationNSVTAGDYSRPLHIS
CCCCCCCCCCCCCHH		12.9828152594
165PhosphorylationSVTAGDYSRPLHIST
CCCCCCCCCCCCHHH		31.9628152594
187SuccinylationGFRLLNLKNDSLRKR
CCCHHCCCCHHHHHH		58.6023954790
187AcetylationGFRLLNLKNDSLRKR
CCCHHCCCCHHHHHH		58.6019608861
187UbiquitinationGFRLLNLKNDSLRKR
CCCHHCCCCHHHHHH		58.6021890473
1872-HydroxyisobutyrylationGFRLLNLKNDSLRKR
CCCHHCCCCHHHHHH		58.60-
190PhosphorylationLLNLKNDSLRKRYDG
HHCCCCHHHHHHCCC		39.1923403867
199UbiquitinationRKRYDGLKYDVKKVE
HHHCCCCCCCHHHHH		44.9619608861
199MalonylationRKRYDGLKYDVKKVE
HHHCCCCCCCHHHHH		44.9626320211
199AcetylationRKRYDGLKYDVKKVE
HHHCCCCCCCHHHHH		44.9619608861
210PhosphorylationKKVEEVVYDLSIRGF
HHHHHHHHHHHCCCC		19.1528152594
213PhosphorylationEEVVYDLSIRGFNKE
HHHHHHHHCCCCCHH		13.8224719451
215MethylationVVYDLSIRGFNKETA
HHHHHHCCCCCHHHH		40.03115919065
2192-HydroxyisobutyrylationLSIRGFNKETAAACV
HHCCCCCHHHHHHHH		54.93-
219MalonylationLSIRGFNKETAAACV
HHCCCCCHHHHHHHH		54.9326320211
219UbiquitinationLSIRGFNKETAAACV
HHCCCCCHHHHHHHH		54.93-
219AcetylationLSIRGFNKETAAACV
HHCCCCCHHHHHHHH		54.9326051181
225GlutathionylationNKETAAACVEK----
CHHHHHHHHCC----		3.3122555962
225S-nitrosylationNKETAAACVEK----
CHHHHHHHHCC----		3.3122178444
225S-nitrosocysteineNKETAAACVEK----
CHHHHHHHHCC----		3.31-
228AcetylationTAAACVEK-------
HHHHHHCC-------		45.297705913
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 TSN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TSN_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 TSN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TSNAX_HUMANTSNAXphysical
11278549
TSNAX_HUMANTSNAXphysical
9013868
ZBT18_HUMANZBTB18physical
9756912
UCHL3_HUMANUCHL3physical
22939629
UBA6_HUMANUBA6physical
22939629
TTC4_HUMANTTC4physical
22939629
VPS29_HUMANVPS29physical
22939629
TSN_HUMANTSNphysical
21988832
NSUN2_HUMANNSUN2physical
22863883
GLYC_HUMANSHMT1physical
22863883
TSNAX_HUMANTSNAXphysical
22863883
TSNAX_HUMANTSNAXphysical
26344197
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 TSN_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187 AND LYS-199, AND MASSSPECTROMETRY.

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