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Q96Q11

- TRNT1_HUMAN

UniProt

Q96Q11 - TRNT1_HUMAN

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Protein

CCA tRNA nucleotidyltransferase 1, mitochondrial

Gene

TRNT1

Organism
Homo sapiens (Human)
Status
Reviewed - 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).

Catalytic activityi

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

Cofactori

Magnesium.Curated

Sites

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

GO - Molecular functioni

  1. ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB
  3. CTP:3'-cytidine-tRNA cytidylyltransferase activity Source: UniProtKB-EC
  4. CTP:tRNA cytidylyltransferase activity Source: UniProtKB-EC
  5. tRNA adenylyltransferase activity Source: UniProtKB
  6. tRNA binding Source: UniProtKB

GO - Biological processi

  1. protein targeting to mitochondrion Source: UniProtKB
  2. tRNA 3'-end processing Source: UniProtKB
  3. tRNA 3'-terminal CCA addition Source: UniProtKB-EC
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

BRENDAi2.7.7.21. 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: Chromosome 3

Organism-specific databases

HGNCiHGNC:17341. TRNT1.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. intracellular Source: LIFEdb
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38446.

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.
GenevestigatoriQ96Q11.

Organism-specific databases

HPAiHPA036938.

Interactioni

Subunit structurei

Monomer, and homodimer; disulfide-linked.

Protein-protein interaction databases

BioGridi119284. 17 interactions.
IntActiQ96Q11. 1 interaction.
MINTiMINT-4725447.
STRINGi9606.ENSP00000251607.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 406
Helixi45 – 5410
Beta strandi59 – 635
Turni64 – 663
Helixi67 – 715
Beta strandi79 – 846
Helixi86 – 938
Turni94 – 974
Beta strandi111 – 1133
Turni115 – 1184
Beta strandi120 – 1245
Helixi148 – 1503
Beta strandi151 – 1533
Helixi154 – 1563
Beta strandi169 – 1713
Helixi172 – 1754
Turni176 – 1794
Beta strandi183 – 1853
Turni186 – 1905
Beta strandi191 – 1933
Helixi197 – 20711
Beta strandi210 – 2134
Helixi217 – 2259
Helixi230 – 2323
Helixi236 – 24611
Helixi251 – 26010
Helixi264 – 2674
Helixi276 – 28510
Helixi292 – 2965
Helixi297 – 2993
Turni303 – 3064
Helixi307 – 3137
Helixi319 – 3268
Turni327 – 3337
Beta strandi338 – 3414
Helixi344 – 3529
Helixi358 – 36912
Helixi372 – 3787

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OU5X-ray3.40A/B30-434[»]
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.
OMAiEPDATTR.
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. Align

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.
The sequence AAH12537.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231P → L.6 Publications
Corresponds to variant rs334773 [ dbSNP | Ensembl ].
VAR_048698

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:
EMBL
GenBank
DDBJ
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]
RefSeqiNP_886552.2. NM_182916.2.
XP_005265253.1. XM_005265196.1. [Q96Q11-1]
UniGeneiHs.732725.

Genome annotation databases

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

Polymorphism databases

DMDMi296452848.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS2561.2. [Q96Q11-1 ]
RefSeqi NP_886552.2. NM_182916.2.
XP_005265253.1. XM_005265196.1. [Q96Q11-1 ]
UniGenei Hs.732725.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OU5 X-ray 3.40 A/B 30-434 [» ]
ProteinModelPortali Q96Q11.
SMRi Q96Q11. Positions 30-383.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119284. 17 interactions.
IntActi Q96Q11. 1 interaction.
MINTi MINT-4725447.
STRINGi 9606.ENSP00000251607.

PTM databases

PhosphoSitei Q96Q11.

Polymorphism databases

DMDMi 296452848.

Proteomic databases

MaxQBi Q96Q11.
PaxDbi Q96Q11.
PRIDEi Q96Q11.

Protocols and materials databases

DNASUi 51095.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251607 ; ENSP00000251607 ; ENSG00000072756 . [Q96Q11-1 ]
ENST00000280591 ; ENSP00000280591 ; ENSG00000072756 . [Q96Q11-2 ]
ENST00000339437 ; ENSP00000342985 ; ENSG00000072756 . [Q96Q11-3 ]
ENST00000402675 ; ENSP00000385745 ; ENSG00000072756 . [Q96Q11-3 ]
ENST00000420393 ; ENSP00000400394 ; ENSG00000072756 . [Q96Q11-3 ]
ENST00000434583 ; ENSP00000415100 ; ENSG00000072756 . [Q96Q11-1 ]
GeneIDi 51095.
KEGGi hsa:51095.
UCSCi uc003bpp.4. human. [Q96Q11-1 ]
uc010hbv.3. human. [Q96Q11-2 ]

Organism-specific databases

CTDi 51095.
GeneCardsi GC03P003168.
HGNCi HGNC:17341. TRNT1.
HPAi HPA036938.
MIMi 612907. gene.
neXtProti NX_Q96Q11.
PharmGKBi PA38446.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0617.
GeneTreei ENSGT00390000009678.
HOGENOMi HOG000253345.
HOVERGENi HBG061403.
InParanoidi Q96Q11.
KOi K00974.
OMAi EPDATTR.
OrthoDBi EOG7CCBR5.
PhylomeDBi Q96Q11.
TreeFami TF313253.

Enzyme and pathway databases

BRENDAi 2.7.7.21. 2681.

Miscellaneous databases

EvolutionaryTracei Q96Q11.
GeneWikii TRNT1.
GenomeRNAii 51095.
NextBioi 53789.
PROi Q96Q11.
SOURCEi Search...

Gene expression databases

Bgeei Q96Q11.
CleanExi HS_TRNT1.
ExpressionAtlasi Q96Q11. baseline and differential.
Genevestigatori Q96Q11.

Family and domain databases

InterProi IPR002646. PolA_pol_head_dom.
[Graphical view ]
Pfami PF01743. PolyA_pol. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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: October 29, 2014
This is version 133 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