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Entry version 162 (02 Jun 2021)
Sequence version 1 (01 Feb 1994)
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Protein

Meiotic spindle formation protein mei-1

Gene

mei-1

Organism
Caenorhabditis elegans
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

Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner (PubMed:28783150).

Microtubule severing may promote rapid reorganization of cellular microtubule arrays. Required specifically for meiotic spindle formation in the female germline; the presence of this protein is inimical to the formation of mitotic spindles (PubMed:8027178, PubMed:10809666, PubMed:12885567, PubMed:19087961, PubMed:23918937).

In body wall muscles, regulates organization of myosin thick filaments (PubMed:22621901).

UniRule annotation6 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

ATPase activity is stimulated by microtubules, which promote homooligomerization. ATP-dependent microtubule severing is stimulated by interaction with mei-2.UniRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi233 – 240ATPUniRule annotationCombined sources1 Publication8
Nucleotide bindingi351 – 352ATPCombined 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 functionIsomerase
Biological processCell cycle, Cell division, Meiosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.6.1.1, 1045

<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:
Meiotic spindle formation protein mei-1UniRule annotation (EC:5.6.1.1UniRule annotation1 Publication)
Alternative name(s):
Katanin p60 ATPase-containing subunit A1UniRule annotation
Short name:
Katanin p60 subunit A1UniRule annotation
p60 kataninUniRule annotation
<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:mei-1UniRule annotation
ORF Names:T01G9.5
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome I

Organism-specific databases

WormBase

More...
WormBasei
T01G9.5a ; CE06342 ; WBGene00003183 ; mei-1
T01G9.5b ; CE32479 ; WBGene00003183 ; mei-1

<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

Chromosome, Cytoplasm, Cytoskeleton, Microtubule

<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 L1 larval stage results in the disorganization of myosin thick filaments in adult body wall muscles characterized by the formation of abnormal myosin heavy chain myo-3 aggregates and V-shaped crossing of A-bands. In addition, body wall muscle cells appear shorter and broader.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi36R → C in ct46ct99; loss of function. Does not affect mei-1 degradation. Prevents mei-1 degradation during the transition from meiosis to mitosis; when associated with A-92. 2 Publications1
Mutagenesisi66E → K in ct46sb18; gain of function. 1 Publication1
Mutagenesisi92S → A: Abolishes phosphorylation by mbk-2. Abolishes interaction with mel-26. Prevents mei-1 degradation during the transition from meiosis to mitosis; when associated with C-36. 2 Publications1
Mutagenesisi92S → D: Phosphomimetic mutant. No effect on the interaction with mel-26. 1 Publication1
Mutagenesisi99P → L in ct46; gain of function. Embryonic lethal. Abolishes interaction with mel-26 and probably mel-26-mediated degradation. Simultaneous RNAi-mediated knockdown of ppfr-1, pph-4.1 or ppfr-4, partially rescues embryonic lethality. Myosin thick filaments are disorganized in body wall muscles in an unc-29 (e1072) mutant background. 3 Publications1
Mutagenesisi126G → S in ct46sb9 and ct46sb17; gain of function. 1 Publication1
Mutagenesisi128R → C in ct46sb22; gain of function. 1 Publication1
Mutagenesisi195I → K in ct46sb3; dominant negative. 1 Publication1
Mutagenesisi225P → L in b284; dominant negative. 1 Publication1
Mutagenesisi231L → P in ct81; dominant negative. 1 Publication1
Mutagenesisi235P → L in ct93; dominant negative. 1 Publication1
Mutagenesisi235P → S in ct46ct103; dominant negative. Formation of an abnormally large polar body during oocyte meiosis II. Increased in metaphase and anaphase meiotic spindle length, failure of chromosomes to align on the metaphase plate persistence of spindle poles during anaphase resulting in their mis-positioning and delay in anaphase meiotic spindle disassembly. 2 Publications1
Mutagenesisi308E → D in ct46ct101; null. Formation of an abnormally large polar body during oocyte meiosis II. Myosin thick filaments are disorganized in body wall muscles in an unc-29 (e1072) mutant background. 3 Publications1
Mutagenesisi322D → R: Severe loss of ATPase activity and complete loss of microtubule severing activity. 1 Publication1
Mutagenesisi351R → A: Severe loss of ATPase activity and complete loss of microtubule severing activity. 1 Publication1
Mutagenesisi352R → A: Severe loss of ATPase activity and complete loss of microtubule severing activity. 1 Publication1
Mutagenesisi360P → S in ct46sb23; gain of function. 1 Publication1
Mutagenesisi414R → K in ct46ct89; dominant negative. 1 Publication1
Mutagenesisi469F → A: Severe loss of ATPase activity and complete loss of microtubule severing activity. 1 Publication1
Mutagenesisi470G → D in ct46ct82; dominant negative. 1 Publication1

<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 polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000845991 – 472Meiotic spindle formation protein mei-1Add BLAST472

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei92Phosphoserine; by mbk-21 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated (PubMed:16338136, PubMed:23918937). Phosphorylation by mbk-2 is required for its rapid degradation following meiosis II (PubMed:16338136). Likely dephosphorylated by the PP4 complex composed of catalytic subunit pph-4.1 and regulatory subunit ppfr-1 (PubMed:23918937).2 Publications
Polyubiquitination targets the protein for rapid degradation via the ubiquitin system at the end of meiosis. The BTB domain protein mel-26 may serve to specifically target mei-1 for ubiquitination by cul-3 containing complexes. The cul-3 protein is in turn regulated by neddylation by ned-8.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P34808

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P34808

PeptideAtlas

More...
PeptideAtlasi
P34808

PRoteomics IDEntifications database

More...
PRIDEi
P34808

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P34808

<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

Highly expressed in the female germline. Degradation at the meiosis-mitosis transition reduces cytoplasmic microtubule severing activity, thereby allowing the formation of larger mitotic spindles.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00003183, Expressed in multi-cellular organism and 5 other tissues

<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

Homohexamer; ATP hydrolysis initiates a cycle between an open spiral and a closed ring conformation which is probably involved in pulling tubulin dimers out from microtubules (PubMed:28783150).

Interacts with mei-2, which may serve as a targeting subunit (PubMed:10809666).

Interacts with mel-26, which targets mei-1 for ubiquitin mediated proteolysis (PubMed:13679921, PubMed:14528312, PubMed:23918937).

Interacts with phosphatase pph-4.1 (PubMed:19087961).

UniRule annotation7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
38046, 14 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3889, Katanin complex

Database of interacting proteins

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DIPi
DIP-25343N

Protein interaction database and analysis system

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IntActi
P34808, 7 interactors

Molecular INTeraction database

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MINTi
P34808

STRING: functional protein association networks

More...
STRINGi
6239.T01G9.5b

<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

1472
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

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SMRi
P34808

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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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

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>Regioni83 – 161DisorderedSequence analysisAdd BLAST79

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 biasi131 – 161Polar residuesSequence analysisAdd BLAST31

<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 AAA ATPase family. Katanin p60 subunit A1 subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0738, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000169739

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000688_21_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P34808

Identification of Orthologs from Complete Genome Data

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OMAi
LKCKEWC

Database of Orthologous Groups

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OrthoDBi
714481at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P34808

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_03023, Katanin_p60_A1, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003593, AAA+_ATPase
IPR041569, AAA_lid_3
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR028596, KATNA1
IPR027417, P-loop_NTPase

Pfam protein domain database

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Pfami
View protein in Pfam
PF00004, AAA, 1 hit
PF17862, AAA_lid_3, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382, AAA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00674, AAA, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform a (identifier: P34808-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MNGDVQSVIR GYLERAQVAK TMSDAGRWNE AGDLLRQLMT DVKSCKISAS
60 70 80 90 100
NRDEHDARNT FLRALEANLK LVQQNVRDED DLHEAMTRQS GSPEPPADPD
110 120 130 140 150
VWSKPSPPLP SSSKFGATKK GVGAAGPRPR EISKSTSSMS TNPADVKPAN
160 170 180 190 200
PTQGILPQNS AGDSFDASAY DAYIVQAVRG TMATNTENTM SLDDIIGMHD
210 220 230 240 250
VKQVLHEAVT LPLLVPEFFQ GLRSPWKAMV LAGPPGTGKT LIARAIASES
260 270 280 290 300
SSTFFTVSST DLSSKWRGDS EKIVRLLFEL ARFYAPSIIF IDEIDTLGGQ
310 320 330 340 350
RGNSGEHEAS RRVKSEFLVQ MDGSQNKFDS RRVFVLAATN IPWELDEALR
360 370 380 390 400
RRFEKRIFIP LPDIDARKKL IEKSMEGTPK SDEINYDDLA ARTEGFSGAD
410 420 430 440 450
VVSLCRTAAI NVLRRYDTKS LRGGELTAAM ESLKAELVRN IDFEAALQAV
460 470
SPSAGPDTML KCKEWCDSFG AM
Length:472
Mass (Da):51,739
Last modified:February 1, 1994 - 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:i167A3929E573CD59
GO
Isoform b (identifier: P34808-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-416: Y → YFRY

Show »
Length:475
Mass (Da):52,206
Checksum:iF5EAF7893FF8FF99
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012951416Y → YFRY in isoform b. Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L25423 Genomic DNA Translation: AAA28109.1
Z75713 Genomic DNA Translation: CAB00052.1
Z75713 Genomic DNA Translation: CAD56596.1

Protein sequence database of the Protein Information Resource

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PIRi
S47861
T24316

NCBI Reference Sequences

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RefSeqi
NP_492257.1, NM_059856.6 [P34808-1]
NP_871793.1, NM_181993.5

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
T01G9.5a.1; T01G9.5a.1; WBGene00003183 [P34808-1]
T01G9.5b.1; T01G9.5b.1; WBGene00003183 [P34808-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
172612

UCSC genome browser

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UCSCi
T01G9.5a.1, c. elegans [P34808-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
L25423 Genomic DNA Translation: AAA28109.1
Z75713 Genomic DNA Translation: CAB00052.1
Z75713 Genomic DNA Translation: CAD56596.1
PIRiS47861
T24316
RefSeqiNP_492257.1, NM_059856.6 [P34808-1]
NP_871793.1, NM_181993.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5WC0electron microscopy4.40A/B/C/D/E/F1-472[»]
5WC1X-ray3.30A1-472[»]
5WCBelectron microscopy6.00A/B/C/D/E/F1-472[»]
6B5DX-ray3.10A164-471[»]
6UGDelectron microscopy3.50A/B/C/D/E/F1-472[»]
6UGEelectron microscopy3.60A/B/C/D/E/F1-472[»]
6UGFelectron microscopy4.20A/B/C/D/E/F1-472[»]
SMRiP34808
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi38046, 14 interactors
ComplexPortaliCPX-3889, Katanin complex
DIPiDIP-25343N
IntActiP34808, 7 interactors
MINTiP34808
STRINGi6239.T01G9.5b

PTM databases

iPTMnetiP34808

Proteomic databases

EPDiP34808
PaxDbiP34808
PeptideAtlasiP34808
PRIDEiP34808

Genome annotation databases

EnsemblMetazoaiT01G9.5a.1; T01G9.5a.1; WBGene00003183 [P34808-1]
T01G9.5b.1; T01G9.5b.1; WBGene00003183 [P34808-2]
GeneIDi172612
UCSCiT01G9.5a.1, c. elegans [P34808-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
249838
WormBaseiT01G9.5a ; CE06342 ; WBGene00003183 ; mei-1
T01G9.5b ; CE32479 ; WBGene00003183 ; mei-1

Phylogenomic databases

eggNOGiKOG0738, Eukaryota
GeneTreeiENSGT00940000169739
HOGENOMiCLU_000688_21_1_1
InParanoidiP34808
OMAiLKCKEWC
OrthoDBi714481at2759
PhylomeDBiP34808

Enzyme and pathway databases

BRENDAi5.6.1.1, 1045

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P34808

Gene expression databases

BgeeiWBGene00003183, Expressed in multi-cellular organism and 5 other tissues

Family and domain databases

HAMAPiMF_03023, Katanin_p60_A1, 1 hit
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR041569, AAA_lid_3
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR028596, KATNA1
IPR027417, P-loop_NTPase
PfamiView protein in Pfam
PF00004, AAA, 1 hit
PF17862, AAA_lid_3, 1 hit
SMARTiView protein in SMART
SM00382, AAA, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00674, AAA, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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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 nameiKTNA1_CAEEL
<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: P34808
Secondary accession number(s): Q8I4G6
<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: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 2, 2021
This is version 162 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)
Annotation programCaenorhabditis annotation project

<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, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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