TRNT1_HUMAN - dbPTM
TRNT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRNT1_HUMAN
UniProt AC Q96Q11
Protein Name CCA tRNA nucleotidyltransferase 1, mitochondrial
Gene Name TRNT1
Organism Homo sapiens (Human).
Sequence Length 434
Subcellular Localization Mitochondrion .
Protein Description Isoform 1: Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates.; Isoform 2: Adds 2 C residues (CC-) to the 3' terminus of tRNA molecules instead of a complete CCA end as isoform 1 does (in vitro)..
Protein Sequence MLRCLYHWHRPVLNRRWSRLCLPKQYLFTMKLQSPEFQSLFTEGLKSLTELFVKENHELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAGIRMINNRGEKHGTITARLHEENFEITTLRIDVTTDGRHAEVEFTTDWQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRFVGHAKQRIQEDYLRILRYFRFYGRIVDKPGDHDPETLEAIAENAKGLAGISGERIWVELKKILVGNHVNHLIHLIYDLDVAPYIGLPANASLEEFDKVSKNVDGFSPKPVTLLASLFKVQDDVTKLDLRLKIAKEEKNLGLFIVKNRKDLIKATDSSDPLKPYQDFIIDSREPDATTRVCELLKYQGEHCLLKEMQQWSIPPFPVSGHDIRKVGISSGKEIGALLQQLREQWKKSGYQMEKDELLSYIKKT
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
34PhosphorylationLFTMKLQSPEFQSLF
EEEEECCCHHHHHHH		36.5127050516
54UbiquitinationSLTELFVKENHELRI
HHHHHHHHCCCEEEE		45.52-
107AcetylationMINNRGEKHGTITAR
EECCCCCCCCEEEEE		50.5925953088
131PhosphorylationTLRIDVTTDGRHAEV
EEEEEEECCCCEEEE		35.9823836654
142PhosphorylationHAEVEFTTDWQKDAE
EEEEEEECCHHHHHH		40.3324719451
188AcetylationVRFVGHAKQRIQEDY
EEECHHHHHHHHHHH		34.1425953088
211AcetylationFYGRIVDKPGDHDPE
HHCEECCCCCCCCHH		39.7525953088
271UbiquitinationAPYIGLPANASLEEF
HHHCCCCCCCCHHHH		29.3021890473
271 (in isoform 2)Ubiquitination-29.3021890473
289PhosphorylationSKNVDGFSPKPVTLL
HCCCCCCCCCHHHHH		37.2325159151
291UbiquitinationNVDGFSPKPVTLLAS
CCCCCCCCHHHHHHH		51.4221890473
291 (in isoform 1)Ubiquitination-51.4221890473
291UbiquitinationNVDGFSPKPVTLLAS
CCCCCCCCHHHHHHH		51.4221890473
298O-linked_GlycosylationKPVTLLASLFKVQDD
CHHHHHHHHHCCCCC		34.0228510447
298PhosphorylationKPVTLLASLFKVQDD
CHHHHHHHHHCCCCC		34.0224719451
308UbiquitinationKVQDDVTKLDLRLKI
CCCCCCHHHHHHHHH		39.59-
317AcetylationDLRLKIAKEEKNLGL
HHHHHHHHHHCCCEE		70.6325953088
320AcetylationLKIAKEEKNLGLFIV
HHHHHHHCCCEEEEE		59.5725953088
328MalonylationNLGLFIVKNRKDLIK
CCEEEEECCHHHHHH		46.3426320211
335UbiquitinationKNRKDLIKATDSSDP
CCHHHHHHCCCCCCC		53.16-
340PhosphorylationLIKATDSSDPLKPYQ
HHHCCCCCCCCCCCC		46.1628555341
344UbiquitinationTDSSDPLKPYQDFII
CCCCCCCCCCCCEEE		47.25-
367UbiquitinationTRVCELLKYQGEHCL
HHHHHHHHHCCCCEE		48.42-
367AcetylationTRVCELLKYQGEHCL
HHHHHHHHHCCCCEE		48.4225038526
376AcetylationQGEHCLLKEMQQWSI
CCCCEEHHHHHHCCC		37.8926051181
382AcetylationLKEMQQWSIPPFPVS
HHHHHHCCCCCCCCC		22.3719608861
395AcetylationVSGHDIRKVGISSGK
CCCCCCHHHCCCCHH		45.18134049
399PhosphorylationDIRKVGISSGKEIGA
CCHHHCCCCHHHHHH		27.4020068231
400PhosphorylationIRKVGISSGKEIGAL
CHHHCCCCHHHHHHH		52.5426055452
402AcetylationKVGISSGKEIGALLQ
HHCCCCHHHHHHHHH		48.3719608861
418PhosphorylationLREQWKKSGYQMEKD
HHHHHHHHCCCCCHH		38.7223401153
420PhosphorylationEQWKKSGYQMEKDEL
HHHHHHCCCCCHHHH		16.2729083192
429PhosphorylationMEKDELLSYIKKT--
CCHHHHHHHHHCC--		37.1229083192
430PhosphorylationEKDELLSYIKKT---
CHHHHHHHHHCC---		19.4129083192
432UbiquitinationDELLSYIKKT-----
HHHHHHHHCC-----		41.97-
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 TRNT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRNT1_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 TRNT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TXD17_HUMANTXNDC17physical
22939629
BASP1_HUMANBASP1physical
22863883
ICLN_HUMANCLNS1Aphysical
22863883
GNPI1_HUMANGNPDA1physical
22863883
MSHR_HUMANMC1Rphysical
22863883
OGFD1_HUMANOGFOD1physical
22863883
PYGL_HUMANPYGLphysical
22863883
RD23A_HUMANRAD23Aphysical
22863883
TBCE_HUMANTBCEphysical
22863883
UBA6_HUMANUBA6physical
22863883
UBXN1_HUMANUBXN1physical
22863883
UBP5_HUMANUSP5physical
22863883
DPYD_HUMANDPYDphysical
26344197
3BP1_HUMANSH3BP1physical
26344197
SYNM_HUMANNARS2physical
28514442
MRRP1_HUMANTRMT10Cphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616084Sideroblastic anemia with B-cell immunodeficiency, periodic fevers, and developmental delay (SIFD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRNT1_HUMAN

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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-402, AND MASS SPECTROMETRY.

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