dbPTM

TRNT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRNT1_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
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

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	LFTMKLQSPEFQSLF EEEEECCCHHHHHHH	36.51	27050516
54	Ubiquitination	SLTELFVKENHELRI HHHHHHHHCCCEEEE	45.52	-
107	Acetylation	MINNRGEKHGTITAR EECCCCCCCCEEEEE	50.59	25953088
131	Phosphorylation	TLRIDVTTDGRHAEV EEEEEEECCCCEEEE	35.98	23836654
142	Phosphorylation	HAEVEFTTDWQKDAE EEEEEEECCHHHHHH	40.33	24719451
188	Acetylation	VRFVGHAKQRIQEDY EEECHHHHHHHHHHH	34.14	25953088
211	Acetylation	FYGRIVDKPGDHDPE HHCEECCCCCCCCHH	39.75	25953088
271	Ubiquitination	APYIGLPANASLEEF HHHCCCCCCCCHHHH	29.30	21890473
271 (in isoform 2)	Ubiquitination	-	29.30	21890473
289	Phosphorylation	SKNVDGFSPKPVTLL HCCCCCCCCCHHHHH	37.23	25159151
291	Ubiquitination	NVDGFSPKPVTLLAS CCCCCCCCHHHHHHH	51.42	21890473
291 (in isoform 1)	Ubiquitination	-	51.42	21890473
291	Ubiquitination	NVDGFSPKPVTLLAS CCCCCCCCHHHHHHH	51.42	21890473
298	O-linked_Glycosylation	KPVTLLASLFKVQDD CHHHHHHHHHCCCCC	34.02	28510447
298	Phosphorylation	KPVTLLASLFKVQDD CHHHHHHHHHCCCCC	34.02	24719451
308	Ubiquitination	KVQDDVTKLDLRLKI CCCCCCHHHHHHHHH	39.59	-
317	Acetylation	DLRLKIAKEEKNLGL HHHHHHHHHHCCCEE	70.63	25953088
320	Acetylation	LKIAKEEKNLGLFIV HHHHHHHCCCEEEEE	59.57	25953088
328	Malonylation	NLGLFIVKNRKDLIK CCEEEEECCHHHHHH	46.34	26320211
335	Ubiquitination	KNRKDLIKATDSSDP CCHHHHHHCCCCCCC	53.16	-
340	Phosphorylation	LIKATDSSDPLKPYQ HHHCCCCCCCCCCCC	46.16	28555341
344	Ubiquitination	TDSSDPLKPYQDFII CCCCCCCCCCCCEEE	47.25	-
367	Ubiquitination	TRVCELLKYQGEHCL HHHHHHHHHCCCCEE	48.42	-
367	Acetylation	TRVCELLKYQGEHCL HHHHHHHHHCCCCEE	48.42	25038526
376	Acetylation	QGEHCLLKEMQQWSI CCCCEEHHHHHHCCC	37.89	26051181
382	Acetylation	LKEMQQWSIPPFPVS HHHHHHCCCCCCCCC	22.37	19608861
395	Acetylation	VSGHDIRKVGISSGK CCCCCCHHHCCCCHH	45.18	134049
399	Phosphorylation	DIRKVGISSGKEIGA CCHHHCCCCHHHHHH	27.40	20068231
400	Phosphorylation	IRKVGISSGKEIGAL CHHHCCCCHHHHHHH	52.54	26055452
402	Acetylation	KVGISSGKEIGALLQ HHCCCCHHHHHHHHH	48.37	19608861
418	Phosphorylation	LREQWKKSGYQMEKD HHHHHHHHCCCCCHH	38.72	23401153
420	Phosphorylation	EQWKKSGYQMEKDEL HHHHHHCCCCCHHHH	16.27	29083192
429	Phosphorylation	MEKDELLSYIKKT-- CCHHHHHHHHHCC--	37.12	29083192
430	Phosphorylation	EKDELLSYIKKT--- CHHHHHHHHHCC---	19.41	29083192
432	Ubiquitination	DELLSYIKKT----- 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
TXD17_HUMAN	TXNDC17	physical	22939629
BASP1_HUMAN	BASP1	physical	22863883
ICLN_HUMAN	CLNS1A	physical	22863883
GNPI1_HUMAN	GNPDA1	physical	22863883
MSHR_HUMAN	MC1R	physical	22863883
OGFD1_HUMAN	OGFOD1	physical	22863883
PYGL_HUMAN	PYGL	physical	22863883
RD23A_HUMAN	RAD23A	physical	22863883
TBCE_HUMAN	TBCE	physical	22863883
UBA6_HUMAN	UBA6	physical	22863883
UBXN1_HUMAN	UBXN1	physical	22863883
UBP5_HUMAN	USP5	physical	22863883
DPYD_HUMAN	DPYD	physical	26344197
3BP1_HUMAN	SH3BP1	physical	26344197
SYNM_HUMAN	NARS2	physical	28514442
MRRP1_HUMAN	TRMT10C	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616084	Sideroblastic 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

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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.	19608861 [Abstract]