| UniProt ID | CTU2_HUMAN | |
|---|---|---|
| UniProt AC | Q2VPK5 | |
| Protein Name | Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054} | |
| Gene Name | CTU2 {ECO:0000255|HAMAP-Rule:MF_03054} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 515 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.. | |
| Protein Sequence | MCQVGEDYGEPAPEEPPPAPRPSREQKCVKCKEAQPVVVIRAGDAFCRDCFKAFYVHKFRAMLGKNRLIFPGEKVLLAWSGGPSSSSMVWQVLEGLSQDSAKRLRFVAGVIFVDEGAACGQSLEERSKTLAEVKPILQATGFPWHVVALEEVFSLPPSVLWCSAQELVGSEGAYKAAVDSFLQQQHVLGAGGGPGPTQGEEQPPQPPLDPQNLARPPAPAQTEALSQLFCSVRTLTAKEELLQTLRTHLILHMARAHGYSKVMTGDSCTRLAIKLMTNLALGRGAFLAWDTGFSDERHGDVVVVRPMRDHTLKEVAFYNRLFSVPSVFTPAVDTKAPEKASIHRLMEAFILRLQTQFPSTVSTVYRTSEKLVKGPRDGPAAGDSGPRCLLCMCALDVDAADSATAFGAQTSSRLSQMQSPIPLTETRTPPGPCCSPGVGWAQRCGQGACRREDPQACIEEQLCYSCRVNMKDLPSLDPLPPYILAEAQLRTQRAWGLQEIRDCLIEDSDDEAGQS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MCQVGEDYG ------CCCCCCCCC | 4.51 | 19413330 | |
| 8 | Phosphorylation | MCQVGEDYGEPAPEE CCCCCCCCCCCCCCC | 21.06 | 26552605 | |
| 23 | Phosphorylation | PPPAPRPSREQKCVK CCCCCCCCCCCCCCC | 50.13 | 26552605 | |
| 151 (in isoform 3) | Ubiquitination | - | 50.11 | 21906983 | |
| 226 (in isoform 3) | Ubiquitination | - | 31.70 | 21906983 | |
| 238 | Ubiquitination | SVRTLTAKEELLQTL HHHHHCCHHHHHHHH | 46.62 | 21906983 | |
| 238 (in isoform 1) | Ubiquitination | - | 46.62 | 21906983 | |
| 248 (in isoform 3) | Ubiquitination | - | 12.39 | 21906983 | |
| 261 | Ubiquitination | ARAHGYSKVMTGDSC HHHCCCCCCCCCCHH | 27.78 | - | |
| 264 | Phosphorylation | HGYSKVMTGDSCTRL CCCCCCCCCCHHHHH | 40.60 | 30576142 | |
| 269 | Phosphorylation | VMTGDSCTRLAIKLM CCCCCHHHHHHHHHH | 32.44 | 30576142 | |
| 313 (in isoform 1) | Ubiquitination | - | 51.83 | 21906983 | |
| 313 | Ubiquitination | PMRDHTLKEVAFYNR ECCCCCHHHHHHHHH | 51.83 | 21906983 | |
| 323 | Phosphorylation | AFYNRLFSVPSVFTP HHHHHHHCCCCCCCC | 37.40 | 27050516 | |
| 335 | Ubiquitination | FTPAVDTKAPEKASI CCCCCCCCCCCHHHH | 58.44 | 21906983 | |
| 335 (in isoform 1) | Ubiquitination | - | 58.44 | 21906983 | |
| 368 | Phosphorylation | VSTVYRTSEKLVKGP HHHEEECCCHHCCCC | 24.60 | 28555341 | |
| 373 | Ubiquitination | RTSEKLVKGPRDGPA ECCCHHCCCCCCCCC | 73.89 | - | |
| 384 (in isoform 3) | Ubiquitination | - | 50.18 | 21906983 | |
| 415 | Phosphorylation | AQTSSRLSQMQSPIP CHHHHHHHHCCCCCC | 23.61 | 21712546 | |
| 419 | Phosphorylation | SRLSQMQSPIPLTET HHHHHCCCCCCCCCC | 21.32 | 29255136 | |
| 424 | Phosphorylation | MQSPIPLTETRTPPG CCCCCCCCCCCCCCC | 29.92 | 23403867 | |
| 426 | Phosphorylation | SPIPLTETRTPPGPC CCCCCCCCCCCCCCC | 34.31 | 23403867 | |
| 428 | Phosphorylation | IPLTETRTPPGPCCS CCCCCCCCCCCCCCC | 41.05 | 25159151 | |
| 435 | Phosphorylation | TPPGPCCSPGVGWAQ CCCCCCCCCCCCHHH | 31.26 | 23401153 | |
| 471 | Ubiquitination | YSCRVNMKDLPSLDP HHCCCCCCCCCCCCC | 51.41 | 2190698 | |
| 471 (in isoform 1) | Ubiquitination | - | 51.41 | 21906983 | |
| 508 | Phosphorylation | RDCLIEDSDDEAGQS HHHHCCCCCCCCCCC | 33.88 | 26503892 | |
| 515 | Phosphorylation | SDDEAGQS------- CCCCCCCC------- | 41.07 | 21712546 |
| 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 CTU2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CTU2_HUMAN !! | ||||||
* 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 CTU2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CTU2_HUMAN !! | ||||
| 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. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419 AND SER-508, ANDMASS SPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND MASSSPECTROMETRY. | |
