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Entry version 63 (02 Jun 2021)
Sequence version 1 (01 Mar 2002)
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Protein

Terminal uridylyltransferase 1

Gene

KRET1

Organism
Trypanosoma brucei brucei
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Terminal uridylyltransferase which is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-RNA (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351).

Specifically, catalyzes the addition of Us to the 3'-hydroxyl group of guided RNA (gRNA), ribosomal RNA (rRNA) and some mRNAs (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351).

As part of the mitochondrial 3' processome (MPsome), catalyzes the primary 3' uridylation of gRNA precursors to facilitate their recognition and to induce their processive 3'-5' degradation by DSS1, and the secondary 3' uridylation of mature gRNAs (PubMed:26833087).

Involved in the 3' uridylylation of the long A/U tail of some edited and never-edited mRNAs (PubMed:20086102).

Promotes 3' uridylylation-mediated decay of some never-edited mRNAs (PubMed:20086102).

Does not mediate RNA-independent UTP polymerization (PubMed:27744351).

4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication1 Publication, Mn2+By similarityNote: Binds 1 Mg2+ or Mn2+ per subunit (PubMed:27744351). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg2+ induces predominantly uridine (U) incorporation while Mn2+ induces also substantial incorporation of both adenine (A) and cytosine (C) (By similarity).By similarity1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

KM is 18-28 mM for UTP (at 27 degrees Celsius and 12 (U) single-stranded RNA as substrate) (PubMed:15304317). kcat is 100 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.0012 min(-1) with UTP and double-stranded RNA as substrates (PubMed:19465686). kcat is 15.5 min(-1) with UTP as substrate (PubMed:27744351). kcat is 23.5 min(-1) with RNA as substrate (PubMed:27744351).3 Publications
  1. KM=17 µM for UTP (with 6(U) single-stranded RNA as substrate)1 Publication
  2. KM=1.5 µM for UTP (with double-stranded RNA as substrate)1 Publication
  3. KM=8.5 µM for UTP (at 27 degrees Celsius)1 Publication
  4. KM=0.53 µM for RNA (at 27 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi195ZincCombined sources1 Publication1
    Metal bindingi198ZincCombined sources1 Publication1
    Metal bindingi212Zinc; via tele nitrogenCombined sources1 Publication1
    Metal bindingi217Zinc; via tele nitrogenCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei298UTP; via amide nitrogenBy similarity1
    Metal bindingi310Magnesium or manganese; catalyticBy similarity1
    Metal bindingi312Magnesium or manganese; catalyticBy similarity1
    Binding sitei358RNABy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei473Important for catalytic activityBy similarity1
    Binding sitei505UTPCombined sources1 Publication1
    Binding sitei509UTPCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri190 – 221C2H2-type; atypical1 PublicationAdd BLAST32
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi309 – 312UTPBy similarity4
    Nucleotide bindingi480 – 484UTPCombined sources1 Publication5
    Nucleotide bindingi523 – 524UTPCombined sources1 Publication2

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionNucleotidyltransferase, RNA-binding, Transferase
    Biological processmRNA processing
    LigandMagnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Terminal uridylyltransferase 1Curated (EC:2.7.7.521 Publication5 Publications)
    Short name:
    TUTase 11 Publication
    Alternative name(s):
    3' terminal uridylyl transferase1 Publication
    Short name:
    3' TUTase1 Publication
    RNA editing 3' terminal uridylyltransferase 1Curated
    Short name:
    RET1Curated
    Short name:
    RNA editing TUTase 1Curated
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:KRET1Curated
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiTrypanosoma brucei brucei
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri5702 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaDiscobaEuglenozoaKinetoplasteaMetakinetoplastinaTrypanosomatidaTrypanosomatidaeTrypanosoma

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Mitochondrion

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    RNAi-mediated knockdown at the procyclic stage causes severe growth defect and a severe reduction in mRNA editing (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). Reduced production of guided RNAs (gRNA) and rRNAs due to a block in the processing of gRNA and rRNA precursors (PubMed:20086102, PubMed:26833087). Accumulation of unprocessed precursors for some pre-edited and never-edited mRNAs (PubMed:20086102).4 Publications

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – ?MitochondrionCurated
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000450678? – 976Terminal uridylyltransferase 1

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Expressed at the procyclic stage (at protein level).2 Publications

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Oligomer (PubMed:27744351).

    Component of the mitochondrial 3' processome (MPsome) complex composed at least of terminal uridylyltransferase KRET1/TUT1, 3'-5' exonuclease DSS1, MPSS1, MPSS2 and MPSS3 (PubMed:26833087, PubMed:27744351). Within the complex, interacts with DSS1, MPSS1 and MPSS3 (PubMed:26833087).

    2 Publications

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1976
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q8WQX5

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini366 – 425PAP-associatedSequence analysisAdd BLAST60

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 188Required for oligomerization and may contribute to the incorporation into the MPsome complex1 PublicationAdd BLAST188
    Regioni1 – 47DisorderedSequence analysisAdd BLAST47
    Regioni129 – 185DisorderedSequence analysisAdd BLAST57
    Regioni700 – 976Important for catalytic activity and RNA binding1 PublicationAdd BLAST277
    Regioni732 – 755DisorderedSequence analysisAdd BLAST24

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi652 – 661Nucleotide recognition motif (NRM)1 Publication10

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi9 – 47Basic and acidic residuesSequence analysisAdd BLAST39
    Compositional biasi151 – 179Acidic residuesSequence analysisAdd BLAST29
    Compositional biasi732 – 752Polar residuesSequence analysisAdd BLAST21

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The C2H2-type zinc finger domain is required for the proper folding of the catalytic domain, but is dispensable for uridylation of single strand RNA substrate.1 Publication

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the DNA polymerase type-B-like family.Curated

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri190 – 221C2H2-type; atypical1 PublicationAdd BLAST32

    Keywords - Domaini

    Transit peptide, Zinc-finger

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR043519, NT_sf
    IPR002058, PAP_assoc

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03828, PAP_assoc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF81301, SSF81301, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50157, ZINC_FINGER_C2H2_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8WQX5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVSKYHRLLQ QGLREEEEGV TERNMVAGGE QRHGHVDDDN AEGDADFYDQ
    60 70 80 90 100
    KDERRAKMWN PKHESANVSA GGKQNRSVRD CLPGSLPPVA NTSTDAAVRF
    110 120 130 140 150
    DRERKNAGHG VDISCVEGDG AQMGTYVSTG RSDAKAGGGS SAIGVTADDE
    160 170 180 190 200
    SDGNLDTDGS DASEGDEVES TTDADVYGED DTTEGPRGGV RLYSCDACPH
    210 220 230 240 250
    AVFTTHAALL AHAEEHHADL LPDHARLRRI AQKLNPVWNR ALNARRNTIT
    260 270 280 290 300
    SWGKKIFHVA AQRDAGESKM QEAHRARAQL ECVVRRWHDK ARVFIFGSSV
    310 320 330 340 350
    AMGVWDGTAD IDFAVVDVDA MERGSWPPLE KNAVRSITEL LRRVGFSFVN
    360 370 380 390 400
    LEPISHARVP IIKHHASSPI LTVARRDAED VVARSIRFIL NGPATREDRL
    410 420 430 440 450
    LLEGSVRDAV GPTGVQQVWW NRTSDMMSAT LESTTAAVRA AMCSPALASA
    460 470 480 490 500
    SLRTKVQPAH DECRPELYNI DFDLSFRAFG IRNSTLLRKY LLSHPCARPG
    510 520 530 540 550
    AIVLKDWSKT SGVNNSVNGY FTSYAINIMW IYYLVQKGYV PYVDPLEIPE
    560 570 580 590 600
    SLVNYTDFDP RYTPMIDPEI TNTEREELYK AAGDMLVGFF YFYSFEFDWG
    610 620 630 640 650
    HNVISLNRPG ITTKRMLGWH VEDVVPVAST SVSSGGGGSN VKRHPTRYEL
    660 670 680 690 700
    CIEDPYEENL NLGRHIGVTK SLRVRTELYR GLLSLLKEGE TRSCVFAAAD
    710 720 730 740 750
    SSGTPAAGGK QSAALPARAL FKLMALTTQA ISESRRLPQS NSDNSGRIAN
    760 770 780 790 800
    GDNESLTEVG GGHRVEGAGV DPASCAGASL SSFGEPPIGV HEKTLESIFV
    810 820 830 840 850
    EKAPMEFQLV RKVWNWHQLI HRLGYKIHRG HVMPRREVGV RCTARRDAEE
    860 870 880 890 900
    TTTELASGVD TTKSLRPGRG LTDTMLRDLS RGYMTLTPEW VAWSAPWVSQ
    910 920 930 940 950
    HLRGYSRLTT VRSAVADETP PALATVPSVV KPPTGEAVMG AMRTTRRNAA
    960 970
    PARRVELLKL WLWRGISKVT PFKSPR
    Length:976
    Mass (Da):107,524
    Last modified:March 1, 2002 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5B497C08732D393E
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AY029070 Genomic DNA Translation: AAK38334.1

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY029070 Genomic DNA Translation: AAK38334.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5HZDX-ray1.60A189-699[»]
    5I49X-ray1.80A189-699[»]
    5IDOX-ray2.20A189-699[»]
    SMRiQ8WQX5
    ModBaseiSearch...
    PDBe-KBiSearch...

    Family and domain databases

    InterProiView protein in InterPro
    IPR043519, NT_sf
    IPR002058, PAP_assoc
    PfamiView protein in Pfam
    PF03828, PAP_assoc, 1 hit
    SUPFAMiSSF81301, SSF81301, 1 hit
    PROSITEiView protein in PROSITE
    PS50157, ZINC_FINGER_C2H2_2, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTUT1_TRYBB
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8WQX5
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 12, 2020
    Last sequence update: March 1, 2002
    Last modified: June 2, 2021
    This is version 63 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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