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Protein

CCA tRNA nucleotidyltransferase 1, mitochondrial

Gene

TRNT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate.

Cofactori

Mg2+Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei77 – 771By similarity
Active sitei79 – 791By similarity
Active sitei121 – 1211By similarity

GO - Molecular functioni

  • ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity Source: UniProtKB-EC
  • ATP binding Source: UniProtKB
  • CTP:3'-cytidine-tRNA cytidylyltransferase activity Source: UniProtKB-EC
  • CTP:tRNA cytidylyltransferase activity Source: UniProtKB-EC
  • tRNA adenylyltransferase activity Source: UniProtKB
  • tRNA binding Source: UniProtKB

GO - Biological processi

  • protein targeting to mitochondrion Source: UniProtKB
  • tRNA 3'-end processing Source: UniProtKB
  • tRNA 3'-terminal CCA addition Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BRENDAi2.7.7.72. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
CCA tRNA nucleotidyltransferase 1, mitochondrial (EC:2.7.7.72)
Alternative name(s):
Mitochondrial tRNA nucleotidyl transferase, CCA-adding
mt CCA-adding enzyme
mt tRNA CCA-diphosphorylase
mt tRNA CCA-pyrophosphorylase
mt tRNA adenylyltransferase
Gene namesi
Name:TRNT1
ORF Names:CGI-47
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:17341. TRNT1.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: LIFEdb
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Sideroblastic anemia with B-cell immunodeficiency, periodic fevers, and developmental delay (SIFD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive disease characterized by severe sideroblastic anemia with onset in the neonatal period or infancy, recurrent periodic fevers without an infectious etiology, B-cell lymphopenia and hypogammaglobulinemia. Affected individuals show delayed psychomotor development with variable neurodegeneration. Additional variable features include sensorineural hearing loss, retinitis pigmentosa, nephrocalcinosis, and cardiomyopathy.

See also OMIM:616084
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541T → I in SIFD; reduced activity. 1 Publication
VAR_072421
Natural varianti158 – 1581M → V in SIFD; loss of activity. 1 Publication
VAR_072422
Natural varianti166 – 1661L → S in SIFD; loss of activity. 1 Publication
VAR_072423
Natural varianti190 – 1901R → I in SIFD; loss of activity. 1 Publication
VAR_072424
Natural varianti223 – 2231I → T in SIFD; loss of activity. 1 Publication
VAR_072425
Natural varianti326 – 3261I → T in SIFD; loss of activity. 1 Publication
VAR_072426
Natural varianti416 – 4161K → E in SIFD. 1 Publication
VAR_072427

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi616084. phenotype.
Orphaneti369861. Congenital sideroblastic anemia-B-cell immunodeficiency-periodic fever-developmental delay syndrome.
PharmGKBiPA38446.

Polymorphism and mutation databases

BioMutaiTRNT1.
DMDMi296452848.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionSequence AnalysisAdd
BLAST
Chaini42 – 434393CCA tRNA nucleotidyltransferase 1, mitochondrialPRO_0000004782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi373 – 373Interchain
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei402 – 4021N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ96Q11.
PaxDbiQ96Q11.
PRIDEiQ96Q11.

PTM databases

PhosphoSiteiQ96Q11.

Expressioni

Gene expression databases

BgeeiQ96Q11.
CleanExiHS_TRNT1.
ExpressionAtlasiQ96Q11. baseline and differential.
GenevisibleiQ96Q11. HS.

Organism-specific databases

HPAiHPA036938.

Interactioni

Subunit structurei

Monomer, and homodimer; disulfide-linked.

Protein-protein interaction databases

BioGridi119284. 16 interactions.
IntActiQ96Q11. 1 interaction.
MINTiMINT-4725447.
STRINGi9606.ENSP00000251607.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 384Combined sources
Helixi43 – 5412Combined sources
Beta strandi59 – 624Combined sources
Helixi64 – 707Combined sources
Beta strandi79 – 846Combined sources
Helixi86 – 9611Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi118 – 1247Combined sources
Beta strandi126 – 1294Combined sources
Beta strandi137 – 1404Combined sources
Helixi144 – 1507Combined sources
Beta strandi151 – 1533Combined sources
Helixi154 – 1563Combined sources
Beta strandi169 – 1713Combined sources
Helixi172 – 1776Combined sources
Beta strandi183 – 1853Combined sources
Helixi187 – 1937Combined sources
Helixi197 – 20812Combined sources
Beta strandi210 – 2134Combined sources
Helixi217 – 22610Combined sources
Helixi227 – 2326Combined sources
Helixi235 – 24713Combined sources
Helixi251 – 26010Combined sources
Helixi264 – 2674Combined sources
Helixi275 – 28511Combined sources
Helixi292 – 2965Combined sources
Helixi297 – 2993Combined sources
Helixi304 – 31310Combined sources
Helixi317 – 32913Combined sources
Turni330 – 3323Combined sources
Beta strandi337 – 3404Combined sources
Helixi344 – 3518Combined sources
Helixi358 – 36811Combined sources
Helixi372 – 3798Combined sources
Helixi390 – 3956Combined sources
Helixi401 – 41717Combined sources
Helixi424 – 43411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OU5X-ray3.40A/B30-434[»]
4X4WX-ray1.90A/B28-434[»]
ProteinModelPortaliQ96Q11.
SMRiQ96Q11. Positions 30-383.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96Q11.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0617.
GeneTreeiENSGT00390000009678.
HOGENOMiHOG000253345.
HOVERGENiHBG061403.
InParanoidiQ96Q11.
KOiK00974.
OMAiFPVSGHD.
OrthoDBiEOG7CCBR5.
PhylomeDBiQ96Q11.
TreeFamiTF313253.

Family and domain databases

InterProiIPR002646. PolA_pol_head_dom.
[Graphical view]
PfamiPF01743. PolyA_pol. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96Q11-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLRCLYHWHR PVLNRRWSRL CLPKQYLFTM KLQSPEFQSL FTEGLKSLTE
60 70 80 90 100
LFVKENHELR IAGGAVRDLL NGVKPQDIDF ATTATPTQMK EMFQSAGIRM
110 120 130 140 150
INNRGEKHGT ITARLHEENF EITTLRIDVT TDGRHAEVEF TTDWQKDAER
160 170 180 190 200
RDLTINSMFL GFDGTLFDYF NGYEDLKNKK VRFVGHAKQR IQEDYLRILR
210 220 230 240 250
YFRFYGRIVD KPGDHDPETL EAIAENAKGL AGISGERIWV ELKKILVGNH
260 270 280 290 300
VNHLIHLIYD LDVAPYIGLP ANASLEEFDK VSKNVDGFSP KPVTLLASLF
310 320 330 340 350
KVQDDVTKLD LRLKIAKEEK NLGLFIVKNR KDLIKATDSS DPLKPYQDFI
360 370 380 390 400
IDSREPDATT RVCELLKYQG EHCLLKEMQQ WSIPPFPVSG HDIRKVGISS
410 420 430
GKEIGALLQQ LREQWKKSGY QMEKDELLSY IKKT
Length:434
Mass (Da):50,128
Last modified:May 18, 2010 - v2
Checksum:i60B7387E203A53D0
GO
Isoform 2 (identifier: Q96Q11-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     248-267: Missing.

Show »
Length:414
Mass (Da):47,829
Checksum:i8E95DCE9B13C3743
GO
Isoform 3 (identifier: Q96Q11-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     50-57: ELFVKENH → GINAFHEN
     58-434: Missing.

Note: No experimental confirmation available.
Show »
Length:57
Mass (Da):6,937
Checksum:iB76351899690B303
GO

Sequence cautioni

The sequence AAD34042.1 differs from that shown. Reason: Frameshift at position 16. Curated
The sequence AAH12537.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231P → L.6 Publications
Corresponds to variant rs334773 [ dbSNP | Ensembl ].
VAR_048698
Natural varianti154 – 1541T → I in SIFD; reduced activity. 1 Publication
VAR_072421
Natural varianti158 – 1581M → V in SIFD; loss of activity. 1 Publication
VAR_072422
Natural varianti166 – 1661L → S in SIFD; loss of activity. 1 Publication
VAR_072423
Natural varianti190 – 1901R → I in SIFD; loss of activity. 1 Publication
VAR_072424
Natural varianti223 – 2231I → T in SIFD; loss of activity. 1 Publication
VAR_072425
Natural varianti326 – 3261I → T in SIFD; loss of activity. 1 Publication
VAR_072426
Natural varianti416 – 4161K → E in SIFD. 1 Publication
VAR_072427

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei50 – 578ELFVKENH → GINAFHEN in isoform 3. 1 PublicationVSP_008440
Alternative sequencei58 – 434377Missing in isoform 3. 1 PublicationVSP_008441Add
BLAST
Alternative sequencei248 – 26720Missing in isoform 2. 1 PublicationVSP_008442Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB063105 mRNA. Translation: BAB70662.1.
AF151805 mRNA. Translation: AAD34042.1. Frameshift.
AK290411 mRNA. Translation: BAF83100.1.
AL834397 mRNA. Translation: CAD39059.1.
AC024060 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW63886.1.
BC005184 mRNA. Translation: AAH05184.1.
BC012537 mRNA. Translation: AAH12537.1. Different initiation.
CCDSiCCDS2561.2. [Q96Q11-1]
CCDS77691.1. [Q96Q11-2]
RefSeqiNP_001289875.1. NM_001302946.1.
NP_886552.2. NM_182916.2.
XP_005265253.1. XM_005265196.1. [Q96Q11-1]
XP_011532078.1. XM_011533776.1. [Q96Q11-1]
XP_011532079.1. XM_011533777.1. [Q96Q11-1]
XP_011532080.1. XM_011533778.1. [Q96Q11-1]
UniGeneiHs.732725.

Genome annotation databases

EnsembliENST00000251607; ENSP00000251607; ENSG00000072756.
ENST00000280591; ENSP00000280591; ENSG00000072756. [Q96Q11-2]
ENST00000339437; ENSP00000342985; ENSG00000072756. [Q96Q11-3]
ENST00000402675; ENSP00000385745; ENSG00000072756. [Q96Q11-3]
ENST00000420393; ENSP00000400394; ENSG00000072756. [Q96Q11-3]
ENST00000434583; ENSP00000415100; ENSG00000072756.
GeneIDi51095.
KEGGihsa:51095.
UCSCiuc003bpp.4. human. [Q96Q11-1]
uc010hbv.3. human. [Q96Q11-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB063105 mRNA. Translation: BAB70662.1.
AF151805 mRNA. Translation: AAD34042.1. Frameshift.
AK290411 mRNA. Translation: BAF83100.1.
AL834397 mRNA. Translation: CAD39059.1.
AC024060 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW63886.1.
BC005184 mRNA. Translation: AAH05184.1.
BC012537 mRNA. Translation: AAH12537.1. Different initiation.
CCDSiCCDS2561.2. [Q96Q11-1]
CCDS77691.1. [Q96Q11-2]
RefSeqiNP_001289875.1. NM_001302946.1.
NP_886552.2. NM_182916.2.
XP_005265253.1. XM_005265196.1. [Q96Q11-1]
XP_011532078.1. XM_011533776.1. [Q96Q11-1]
XP_011532079.1. XM_011533777.1. [Q96Q11-1]
XP_011532080.1. XM_011533778.1. [Q96Q11-1]
UniGeneiHs.732725.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OU5X-ray3.40A/B30-434[»]
4X4WX-ray1.90A/B28-434[»]
ProteinModelPortaliQ96Q11.
SMRiQ96Q11. Positions 30-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119284. 16 interactions.
IntActiQ96Q11. 1 interaction.
MINTiMINT-4725447.
STRINGi9606.ENSP00000251607.

PTM databases

PhosphoSiteiQ96Q11.

Polymorphism and mutation databases

BioMutaiTRNT1.
DMDMi296452848.

Proteomic databases

MaxQBiQ96Q11.
PaxDbiQ96Q11.
PRIDEiQ96Q11.

Protocols and materials databases

DNASUi51095.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251607; ENSP00000251607; ENSG00000072756.
ENST00000280591; ENSP00000280591; ENSG00000072756. [Q96Q11-2]
ENST00000339437; ENSP00000342985; ENSG00000072756. [Q96Q11-3]
ENST00000402675; ENSP00000385745; ENSG00000072756. [Q96Q11-3]
ENST00000420393; ENSP00000400394; ENSG00000072756. [Q96Q11-3]
ENST00000434583; ENSP00000415100; ENSG00000072756.
GeneIDi51095.
KEGGihsa:51095.
UCSCiuc003bpp.4. human. [Q96Q11-1]
uc010hbv.3. human. [Q96Q11-2]

Organism-specific databases

CTDi51095.
GeneCardsiGC03P003168.
HGNCiHGNC:17341. TRNT1.
HPAiHPA036938.
MIMi612907. gene.
616084. phenotype.
neXtProtiNX_Q96Q11.
Orphaneti369861. Congenital sideroblastic anemia-B-cell immunodeficiency-periodic fever-developmental delay syndrome.
PharmGKBiPA38446.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0617.
GeneTreeiENSGT00390000009678.
HOGENOMiHOG000253345.
HOVERGENiHBG061403.
InParanoidiQ96Q11.
KOiK00974.
OMAiFPVSGHD.
OrthoDBiEOG7CCBR5.
PhylomeDBiQ96Q11.
TreeFamiTF313253.

Enzyme and pathway databases

BRENDAi2.7.7.72. 2681.

Miscellaneous databases

ChiTaRSiTRNT1. human.
EvolutionaryTraceiQ96Q11.
GeneWikiiTRNT1.
GenomeRNAii51095.
NextBioi53789.
PROiQ96Q11.
SOURCEiSearch...

Gene expression databases

BgeeiQ96Q11.
CleanExiHS_TRNT1.
ExpressionAtlasiQ96Q11. baseline and differential.
GenevisibleiQ96Q11. HS.

Family and domain databases

InterProiIPR002646. PolA_pol_head_dom.
[Graphical view]
PfamiPF01743. PolyA_pol. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of mammalian mitochondrial tRNA nucleotidyltransferases."
    Nagaike T., Suzuki T., Tomari Y., Takemoto-Hori C., Negayama F., Watanabe K., Ueda T.
    J. Biol. Chem. 276:40041-40049(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-23.
  2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-23.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-23.
    Tissue: Umbilical cord blood.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LEU-23.
    Tissue: Brain.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-23.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT LEU-23.
    Tissue: Bone marrow.
  8. "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing."
    Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.
    EMBO Rep. 1:287-292(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "A splice variant of the human CCA-adding enzyme with modified activity."
    Lizano E., Schuster J., Muller M., Kelso J., Morl M.
    J. Mol. Biol. 366:1258-1265(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2).
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: INVOLVEMENT IN SIFD, VARIANTS SIFD ILE-154; VAL-158; SER-166; ILE-190; THR-223; THR-326 AND GLU-416, CHARACTERIZATION OF VARIANTS SIFD ILE-154; VAL-158; SER-166; ILE-190; THR-223 AND THR-326.
  15. "Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization."
    Augustin M.A., Reichert A.S., Betat H., Huber R., Moerl M., Steegborn C.
    J. Mol. Biol. 328:985-994(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 30-434, DIMERIZATION.

Entry informationi

Entry nameiTRNT1_HUMAN
AccessioniPrimary (citable) accession number: Q96Q11
Secondary accession number(s): A8K2Z6
, B7WP13, C9JKA2, Q8ND57, Q9BS97, Q9Y362
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 18, 2010
Last modified: July 22, 2015
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.