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UniProtKB - O95396 (MOCS3_HUMAN)

Entry version 166 (13 Feb 2019)
Sequence version 1 (01 May 1999)
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Protein

Adenylyltransferase and sulfurtransferase MOCS3

Gene

MOCS3

Organism
Homo sapiens (Human)
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

Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions.UniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

<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

  1. KM=0.25 mM for thiosulfate1 Publication
  2. KM=0.28 mM for cyanide1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis

    This protein is involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis, which is part of tRNA modification.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis and in tRNA modification.

    Pathwayi: molybdopterin biosynthesis

    This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei92ATP; via amide nitrogenUniRule annotation1
    Binding sitei113ATPUniRule annotation1
    Binding sitei137ATPUniRule annotation1
    <p>This subsection of the ‘Function’ 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 bindingi222ZincUniRule annotation1
    Metal bindingi225ZincUniRule annotation1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei239Glycyl thioester intermediate; for adenylyltransferase activityUniRule annotation1
    Metal bindingi297ZincUniRule annotation1
    Metal bindingi300ZincUniRule annotation1
    Active sitei412Cysteine persulfide intermediate; for sulfurtransferase activityUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi120 – 124ATPUniRule annotation5
    Nucleotide bindingi181 – 182ATPUniRule annotation2

    <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

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <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 functionMultifunctional enzyme, Transferase
    Biological processMolybdenum cofactor biosynthesis, tRNA processing
    LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:HS04742-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.7.80 2681
    2.8.1.11 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-947581 Molybdenum cofactor biosynthesis

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi
    UPA00344

    UPA00988

    <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_and_taxonomy_section">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:
    Adenylyltransferase and sulfurtransferase MOCS3UniRule annotation
    Alternative name(s):
    Molybdenum cofactor synthesis protein 3UniRule annotation
    Molybdopterin synthase sulfurylase
    Short name:
    MPT synthase sulfurylase
    Including the following 2 domains:
    Molybdopterin-synthase adenylyltransferaseUniRule annotation (EC:2.7.7.80UniRule annotation3 Publications)
    Alternative name(s):
    Adenylyltransferase MOCS3UniRule annotation
    Sulfur carrier protein MOCS2A adenylyltransferaseUniRule annotation
    Molybdopterin-synthase sulfurtransferaseUniRule annotation (EC:2.8.1.11UniRule annotation3 Publications)
    Alternative name(s):
    Sulfur carrier protein MOCS2A sulfurtransferaseUniRule annotation
    Sulfurtransferase MOCS3UniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:MOCS3UniRule annotation
    Synonyms:UBA4UniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 20

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000124217.4

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:15765 MOCS3

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		609277 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_O95396

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    <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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi239C → A: Impairs sulfurtransferase activity. 1 Publication1
    Mutagenesisi316C → A: Does not affect sulfurtransferase activity. 1 Publication1
    Mutagenesisi324C → A: Does not affect sulfurtransferase activity. 1 Publication1
    Mutagenesisi365C → A: Does not affect sulfurtransferase activity. 1 Publication1
    Mutagenesisi412C → A: Abolishes sulfurtransferase activity. 1 Publication1
    Mutagenesisi413K → R: Does not affect sulfurtransferase specificity and activity. 1 Publication1
    Mutagenesisi414L → K: Does not affect sulfurtransferase specificity and activity. 1 Publication1
    Mutagenesisi415G → A: Does not affect sulfurtransferase specificity and activity. 1 Publication1
    Mutagenesisi416N → V: Does not affect sulfurtransferase specificity and activity. 1 Publication1
    Mutagenesisi417D → R: Results in 470-fold increased activity. 1 Publication1
    Mutagenesisi417D → T: Results in 90-fold increased activity. 1 Publication1
    Mutagenesisi458P → G: Does not affect sulfurtransferase specificity and activity. 1 Publication1
    Mutagenesisi460Y → A: Does not affect sulfurtransferase specificity and activity. 1 Publication1

    Organism-specific databases

    Open Targets

    More...    OpenTargetsi    		ENSG00000124217

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA30904

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		MOCS3

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001205831 – 460Adenylyltransferase and sulfurtransferase MOCS3Add BLAST460

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi316 ↔ 3241 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		O95396

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		O95396

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		O95396

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

    More...    PaxDbi    		O95396

    PeptideAtlas

    More...    PeptideAtlasi    		O95396

    PRoteomics IDEntifications database

    More...    PRIDEi    		O95396

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		50847

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		O95396

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...    PhosphoSitePlusi    		O95396

    <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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000124217 Expressed in 135 organ(s), highest expression level in sperm

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		O95396 HS

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with NFS1.UniRule annotation1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    URM1Q9BTM94EBI-373206,EBI-714589

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		118127, 22 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-31168N

    Protein interaction database and analysis system

    More...    IntActi    		O95396, 2 interactors

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000244051

    <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

    1460
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    3I2VX-ray1.25A335-460[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		O95396

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

    More...    SMRi    		O95396

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		O95396

    <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_and_domains_section">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>Domaini347 – 458RhodaneseUniRule annotationAdd BLAST112

    <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

    In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG2017 Eukaryota
    COG0476 LUCA
    COG0607 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000160847

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000281219

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG052491

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		O95396

    KEGG Orthology (KO)

    More...    KOi    		K11996

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		MIYDALE

    Database of Orthologous Groups

    More...    OrthoDBi    		1445129at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		O95396

    TreeFam database of animal gene trees

    More...    TreeFami    		TF106103

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.250.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_03049 MOCS3_Uba4, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR028885 MOCS3/Uba4
    IPR001763 Rhodanese-like_dom
    IPR036873 Rhodanese-like_dom_sf
    IPR000594 ThiF_NAD_FAD-bd
    IPR035985 Ubiquitin-activating_enz

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00581 Rhodanese, 1 hit
    PF00899 ThiF, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00450 RHOD, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF69572 SSF69572, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS50206 RHODANESE_3, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    O95396-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MASREEVLAL QAEVAQREEE LNSLKQKLAS ALLAEQEPQP ERLVPVSPLP 
            60         70         80         90        100
    PKAALSRDEI LRYSRQLVLP ELGVHGQLRL GTACVLIVGC GGLGCPLAQY 
           110        120        130        140        150
    LAAAGVGRLG LVDYDVVEMS NLARQVLHGE ALAGQAKAFS AAASLRRLNS 
           160        170        180        190        200
    AVECVPYTQA LTPATALDLV RRYDVVADCS DNVPTRYLVN DACVLAGRPL 
           210        220        230        240        250
    VSASALRFEG QITVYHYDGG PCYRCIFPQP PPAETVTNCA DGGVLGVVTG 
           260        270        280        290        300
    VLGCLQALEV LKIAAGLGPS YSGSLLLFDA LRGHFRSIRL RSRRLDCAAC 
           310        320        330        340        350
    GERPTVTDLL DYEAFCGSSA TDKCRSLQLL SPEERVSVTD YKRLLDSGAF 
           360        370        380        390        400
    HLLLDVRPQV EVDICRLPHA LHIPLKHLER RDAESLKLLK EAIWEEKQGT 
           410        420        430        440        450
    QEGAAVPIYV ICKLGNDSQK AVKILQSLSA AQELDPLTVR DVVGGLMAWA 
           460
    AKIDGTFPQY
    Length:460
    Mass (Da):49,669
    Last modified:May 1, 1999 - 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:i299A4E755173E324
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_049349429S → A. Corresponds to variant dbSNP:rs7269297Ensembl.1

    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
    		AF102544 mRNA Translation: AAC72412.1
    AL034553 Genomic DNA No translation available.
    BC015939 mRNA Translation: AAH15939.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS13435.1

    NCBI Reference Sequences

    More...    RefSeqi    		NP_055299.1, NM_014484.4

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Hs.159410
    Hs.736268

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000244051; ENSP00000244051; ENSG00000124217

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		27304

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:27304

    UCSC genome browser

    More...    UCSCi    		uc002xvy.3 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <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
    		AF102544 mRNA Translation: AAC72412.1
    AL034553 Genomic DNA No translation available.
    BC015939 mRNA Translation: AAH15939.1
    CCDSiCCDS13435.1
    RefSeqiNP_055299.1, NM_014484.4
    UniGeneiHs.159410
    Hs.736268

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3I2VX-ray1.25A335-460[»]
    ProteinModelPortaliO95396
    SMRiO95396
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi118127, 22 interactors
    DIPiDIP-31168N
    IntActiO95396, 2 interactors
    STRINGi9606.ENSP00000244051

    PTM databases

    iPTMnetiO95396
    PhosphoSitePlusiO95396

    Polymorphism and mutation databases

    BioMutaiMOCS3

    Proteomic databases

    EPDiO95396
    jPOSTiO95396
    MaxQBiO95396
    PaxDbiO95396
    PeptideAtlasiO95396
    PRIDEiO95396
    ProteomicsDBi50847

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		27304
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000244051; ENSP00000244051; ENSG00000124217
    GeneIDi27304
    KEGGihsa:27304
    UCSCiuc002xvy.3 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		27304
    EuPathDBiHostDB:ENSG00000124217.4

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		MOCS3
    HGNCiHGNC:15765 MOCS3
    MIMi609277 gene
    neXtProtiNX_O95396
    OpenTargetsiENSG00000124217
    PharmGKBiPA30904

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG2017 Eukaryota
    COG0476 LUCA
    COG0607 LUCA
    GeneTreeiENSGT00940000160847
    HOGENOMiHOG000281219
    HOVERGENiHBG052491
    InParanoidiO95396
    KOiK11996
    OMAiMIYDALE
    OrthoDBi1445129at2759
    PhylomeDBiO95396
    TreeFamiTF106103

    Enzyme and pathway databases

    UniPathwayi
    UPA00344

    UPA00988

    BioCyciMetaCyc:HS04742-MONOMER
    BRENDAi2.7.7.80 2681
    2.8.1.11 2681
    ReactomeiR-HSA-947581 Molybdenum cofactor biosynthesis

    Miscellaneous databases

    EvolutionaryTraceiO95396

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		MOCS3

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...    GenomeRNAii    		27304

    Protein Ontology

    More...    PROi    		PR:O95396

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000124217 Expressed in 135 organ(s), highest expression level in sperm
    GenevisibleiO95396 HS

    Family and domain databases

    Gene3Di3.40.250.10, 1 hit
    HAMAPiMF_03049 MOCS3_Uba4, 1 hit
    InterProiView protein in InterPro
    IPR028885 MOCS3/Uba4
    IPR001763 Rhodanese-like_dom
    IPR036873 Rhodanese-like_dom_sf
    IPR000594 ThiF_NAD_FAD-bd
    IPR035985 Ubiquitin-activating_enz
    PfamiView protein in Pfam
    PF00581 Rhodanese, 1 hit
    PF00899 ThiF, 1 hit
    SMARTiView protein in SMART
    SM00450 RHOD, 1 hit
    SUPFAMiSSF69572 SSF69572, 1 hit
    PROSITEiView protein in PROSITE
    PS50206 RHODANESE_3, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		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 nameiMOCS3_HUMAN
    <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: O95396
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 26, 2002
    Last sequence update: May 1, 1999
    Last modified: February 13, 2019
    This is version 166 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 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.

    <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, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    6. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    7. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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