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Q96Q11

- TRNT1_HUMAN

UniProt

Q96Q11 - TRNT1_HUMAN

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
    • BLAST
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ96Q11.
    BgeeiQ96Q11.
    CleanExiHS_TRNT1.
    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.
    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

    MLRCLYHWHR PVLNRRWSRL CLPKQYLFTM KLQSPEFQSL FTEGLKSLTE    50
    LFVKENHELR IAGGAVRDLL NGVKPQDIDF ATTATPTQMK EMFQSAGIRM 100
    INNRGEKHGT ITARLHEENF EITTLRIDVT TDGRHAEVEF TTDWQKDAER 150
    RDLTINSMFL GFDGTLFDYF NGYEDLKNKK VRFVGHAKQR IQEDYLRILR 200
    YFRFYGRIVD KPGDHDPETL EAIAENAKGL AGISGERIWV ELKKILVGNH 250
    VNHLIHLIYD LDVAPYIGLP ANASLEEFDK VSKNVDGFSP KPVTLLASLF 300
    KVQDDVTKLD LRLKIAKEEK NLGLFIVKNR KDLIKATDSS DPLKPYQDFI 350
    IDSREPDATT RVCELLKYQG EHCLLKEMQQ WSIPPFPVSG HDIRKVGISS 400
    GKEIGALLQQ LREQWKKSGY QMEKDELLSY IKKT 434
    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.
    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

    ArrayExpressi Q96Q11.
    Bgeei Q96Q11.
    CleanExi HS_TRNT1.
    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

    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 1, 2014
    This is version 132 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