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UniProtKB - P05166 (PCCB_HUMAN)

Entry version 201 (02 Dec 2020)
Sequence version 3 (23 Jan 2007)
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Protein

Propionyl-CoA carboxylase beta chain, mitochondrial

Gene

PCCB

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

This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites (PubMed:6765947, PubMed:15890657). Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (PubMed:6765947, PubMed:15890657). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate (PubMed:6765947). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).By similarity2 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 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=0.29 mM for propanoyl-CoA1 Publication
  2. KM=0.41 mM for propanoyl-CoA (at 37 degrees Celsius and pH 8.0)1 Publication

    pH dependencei

    Optimum pH is 7.2-8.8 for the propionyl-CoA carboxylase activity as measured for the holoenzyme.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: propanoyl-CoA degradation

    This protein is involved in step 1 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.2 Publications
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Propanoyl-CoA:carbon dioxide ligase subunit alpha (PCCA), Propanoyl-CoA:carbon dioxide ligase subunit alpha (PCCA), Propionyl-CoA carboxylase alpha chain, mitochondrial (PCCA), Propanoyl-CoA:carbon dioxide ligase subunit alpha, Propionyl-CoA carboxylase beta chain, mitochondrial (PCCB), Propanoyl-CoA:carbon dioxide ligase subunit alpha (PCCA)
    2. no protein annotated in this organism
    3. no protein annotated in this organism
    This subpathway is part of the pathway propanoyl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from propanoyl-CoA, the pathway propanoyl-CoA degradation and in Metabolic intermediate metabolism.

    <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

    • ATP binding Source: UniProtKB-KW
    • propionyl-CoA carboxylase activity Source: UniProtKB
    Complete GO annotation on QuickGO ...

    GO - Biological processi

    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 functionLigase
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:ENSG00000114054-MONOMER

    Pathway Commons web resource for biological pathway data

    More...    PathwayCommonsi    		P05166

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-196780, Biotin transport and metabolism
    R-HSA-3371599, Defective HLCS causes multiple carboxylase deficiency
    R-HSA-71032, Propionyl-CoA catabolism

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P05166

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

    More...    UniPathwayi    		UPA00945;UER00908

    <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:
    Propionyl-CoA carboxylase beta chain, mitochondrial1 Publication (EC:6.4.1.32 Publications)
    Short name:
    PCCase subunit beta
    Alternative name(s):
    Propanoyl-CoA:carbon dioxide ligase subunit beta
    <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:PCCBImported
    <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>OrganismiHomo sapiens (Human)
    <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 identifieri9606 [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 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%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
    • UP000005640 <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 3

    Organism-specific databases

    Eukaryotic Pathogen and Host Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000114054.13

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:8654, PCCB

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		232050, gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_P05166

    <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 & Seán O’Donoghue; Source: COMPARTMENTS

    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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Propionic acidemia type II (PA-2)9 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionLife-threatening disease characterized by episodic vomiting, lethargy and ketosis, neutropenia, periodic thrombocytopenia, hypogammaglobulinemia, developmental retardation, and intolerance to protein.
    Related information in OMIM
    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_00908017L → M in PA-2; likely benign variant. 1 PublicationCorresponds to variant dbSNP:rs200185747EnsemblClinVar.1
    Natural variantiVAR_00027144R → P in PA-2. 1
    Natural variantiVAR_02384767R → S in PA-2. 1 PublicationCorresponds to variant dbSNP:rs747053913Ensembl.1
    Natural variantiVAR_000272106S → R in PA-2. 1
    Natural variantiVAR_023848107V → M in PA-2. 1 PublicationCorresponds to variant dbSNP:rs1553774114EnsemblClinVar.1
    Natural variantiVAR_023849112G → D in PA-2. 1 PublicationCorresponds to variant dbSNP:rs202247818EnsemblClinVar.1
    Natural variantiVAR_000273131G → R in PA-2. 1
    Natural variantiVAR_009081140K → KICK in PA-2. 1
    Natural variantiVAR_023850153A → P in PA-2. 1 PublicationCorresponds to variant dbSNP:rs202247819EnsemblClinVar.1
    Natural variantiVAR_023851165R → Q in PA-2; does not affect either heteromeric or homomeric assembly. 2 PublicationsCorresponds to variant dbSNP:rs1304714042EnsemblClinVar.1
    Natural variantiVAR_000274165R → W in PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization. 2 PublicationsCorresponds to variant dbSNP:rs879253815EnsemblClinVar.1
    Natural variantiVAR_000275168E → K in PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization. 3 PublicationsCorresponds to variant dbSNP:rs121964960EnsemblClinVar.1
    Natural variantiVAR_023852188G → R in PA-2. 1 PublicationCorresponds to variant dbSNP:rs746102997EnsemblClinVar.1
    Natural variantiVAR_000276198G → D in PA-2. Corresponds to variant dbSNP:rs762354873Ensembl.1
    Natural variantiVAR_009082205V → D in PA-2. 1 Publication1
    Natural variantiVAR_009083228P → L in PA-2. Corresponds to variant dbSNP:rs374722096EnsemblClinVar.1
    Natural variantiVAR_023853246G → V in PA-2. 1 Publication1
    Natural variantiVAR_023854341Missing in PA-2. 1 Publication1
    Natural variantiVAR_000277408Missing in PA-2. 2 Publications1
    Natural variantiVAR_000278410R → W in PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization. 4 PublicationsCorresponds to variant dbSNP:rs121964959EnsemblClinVar.1
    Natural variantiVAR_009084428T → I in PA-2. 2 PublicationsCorresponds to variant dbSNP:rs111033542EnsemblClinVar.1
    Natural variantiVAR_023855430I → L in PA-2. 1 Publication1
    Natural variantiVAR_023856435Y → C in PA-2. 1 PublicationCorresponds to variant dbSNP:rs121964961EnsemblClinVar.1
    Natural variantiVAR_023857439Y → C in PA-2. 1 PublicationCorresponds to variant dbSNP:rs769521436EnsemblClinVar.1
    Natural variantiVAR_009085442M → T in PA-2. 1 Publication1
    Natural variantiVAR_023858468A → T in PA-2. 1 PublicationCorresponds to variant dbSNP:rs775563122EnsemblClinVar.1
    Natural variantiVAR_000280512R → C in PA-2; affects heteromeric and homomeric assembly. 2 PublicationsCorresponds to variant dbSNP:rs186710233EnsemblClinVar.1
    Natural variantiVAR_000281519L → P in PA-2; affects heteromeric and homomeric assembly. 1 PublicationCorresponds to variant dbSNP:rs202247822EnsemblClinVar.1
    Natural variantiVAR_009086536N → D in PA-2; affects heteromeric and homomeric assembly. 1 PublicationCorresponds to variant dbSNP:rs202247823EnsemblClinVar.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		5096

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...    GeneReviewsi    		PCCB

    MalaCards human disease database

    More...    MalaCardsi    		PCCB
    MIMi606054, phenotype

    Open Targets

    More...    OpenTargetsi    		ENSG00000114054

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...    Orphaneti    		35, Propionic acidemia

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA32993

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...    Pharosi    		P05166, Tbio

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB00121, Biotin
    DB00161, Valine

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		PCCB

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		124106304

    <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 – 28Mitochondrion1 PublicationAdd BLAST28
    <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_000000029329 – 539Propionyl-CoA carboxylase beta chain, mitochondrialAdd BLAST511

    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 residuei71PhosphoserineCombined sources1
    Modified residuei99N6-acetyllysine; alternateBy similarity1
    Modified residuei99N6-succinyllysine; alternateBy similarity1
    Modified residuei248N6-succinyllysineBy similarity1
    Modified residuei474N6-acetyllysine; alternateBy similarity1
    Modified residuei474N6-succinyllysine; alternateBy similarity1
    Modified residuei489N6-acetyllysine; alternateBy similarity1
    Modified residuei489N6-succinyllysine; alternateBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P05166

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P05166

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...    MassIVEi    		P05166

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P05166

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

    More...    PaxDbi    		P05166

    PeptideAtlas

    More...    PeptideAtlasi    		P05166

    PRoteomics IDEntifications database

    More...    PRIDEi    		P05166

    ProteomicsDB: a multi-organism proteome resource

    More...    ProteomicsDBi    		51816 [P05166-1]
    51817 [P05166-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P05166

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

    More...    PhosphoSitePlusi    		P05166

    <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    		ENSG00000114054, Expressed in right adrenal gland and 238 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P05166, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P05166, HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		ENSG00000114054, Tissue enhanced (liver)

    <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

    The holoenzyme is a dodecamer composed of 6 PCCA/alpha subunits and 6 PCCB/beta subunits.

    2 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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		111129, 70 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...    CORUMi    		P05166

    Database of interacting proteins

    More...    DIPi    		DIP-38244N

    Protein interaction database and analysis system

    More...    IntActi    		P05166, 14 interactors

    Molecular INTeraction database

    More...    MINTi    		P05166

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000419027

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...    RNActi    		P05166, protein

    <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

    3D structure databases

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

    More...    SMRi    		P05166

    Database of comparative protein structure models

    More...    ModBasei    		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>Domaini32 – 290CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST259
    Domaini294 – 533CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST240

    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>Regioni32 – 533CarboxyltransferasePROSITE-ProRule annotationAdd BLAST502
    Regioni325 – 358Acyl-CoA bindingSequence analysisAdd BLAST34

    <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 beta subunit contains the carboxyl transferase (CT) domain.By similarity

    <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 AccD/PCCB family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG0540, Eukaryota

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000157741

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P05166

    Database of Orthologous Groups

    More...    OrthoDBi    		402617at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P05166

    TreeFam database of animal gene trees

    More...    TreeFami    		TF314350

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR034733, AcCoA_carboxyl
    IPR029045, ClpP/crotonase-like_dom_sf
    IPR011763, COA_CT_C
    IPR011762, COA_CT_N

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01039, Carboxyl_trans, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF52096, SSF52096, 2 hits

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS50989, COA_CT_CTER, 1 hit
    PS50980, COA_CT_NTER, 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.

    <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.

    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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P05166-1) [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
    MAAALRVAAV GARLSVLASG LRAAVRSLCS QATSVNERIE NKRRTALLGG 
            60         70         80         90        100
    GQRRIDAQHK RGKLTARERI SLLLDPGSFV ESDMFVEHRC ADFGMAADKN 
           110        120        130        140        150
    KFPGDSVVTG RGRINGRLVY VFSQDFTVFG GSLSGAHAQK ICKIMDQAIT 
           160        170        180        190        200
    VGAPVIGLND SGGARIQEGV ESLAGYADIF LRNVTASGVI PQISLIMGPC 
           210        220        230        240        250
    AGGAVYSPAL TDFTFMVKDT SYLFITGPDV VKSVTNEDVT QEELGGAKTH 
           260        270        280        290        300
    TTMSGVAHRA FENDVDALCN LRDFFNYLPL SSQDPAPVRE CHDPSDRLVP 
           310        320        330        340        350
    ELDTIVPLES TKAYNMVDII HSVVDEREFF EIMPNYAKNI IVGFARMNGR 
           360        370        380        390        400
    TVGIVGNQPK VASGCLDINS SVKGARFVRF CDAFNIPLIT FVDVPGFLPG 
           410        420        430        440        450
    TAQEYGGIIR HGAKLLYAFA EATVPKVTVI TRKAYGGAYD VMSSKHLCGD 
           460        470        480        490        500
    TNYAWPTAEI AVMGAKGAVE IIFKGHENVE AAQAEYIEKF ANPFPAAVRG 
           510        520        530 
    FVDDIIQPSS TRARICCDLD VLASKKVQRP WRKHANIPL
    Length:539
    Mass (Da):58,216
    Last modified:January 23, 2007 - v3
    <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:iA2DAAC00312D3C0F
    GO
    Isoform 2 (identifier: P05166-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         124-124: Q → QQIIGWAQWLPLVISALWEAE

    Show »
    Length:559
    Mass (Da):60,521
    Checksum:i07788B2E955626AA
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    H7C5C9H7C5C9_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		163Annotation score:

    Annotation score:1 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>
    C9JVW9C9JVW9_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		133Annotation score:

    Annotation score:1 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>
    E7EX59E7EX59_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		570Annotation score:

    Annotation score:1 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>
    E7ENC1E7ENC1_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		303Annotation score:

    Annotation score:1 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>
    C9JQS9C9JQS9_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		559Annotation score:

    Annotation score:1 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>
    E7EUY3E7EUY3_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		516Annotation score:

    Annotation score:1 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>
    E9PEC3E9PEC3_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		423Annotation score:

    Annotation score:1 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>
    C9JVY9C9JVY9_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		191Annotation score:

    Annotation score:1 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>
    E7ETT1E7ETT1_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		520Annotation score:

    Annotation score:1 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>
    E7ETT4E7ETT4_HUMAN
    Propionyl-CoA carboxylase beta chai...
    PCCB
    		482Annotation score:

    Annotation score:1 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>
    There are more potential isoformsShow all

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti58 – 59QH → HD in AAB28900 (PubMed:8225321).Curated2

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00908017L → M in PA-2; likely benign variant. 1 PublicationCorresponds to variant dbSNP:rs200185747EnsemblClinVar.1
    Natural variantiVAR_00027144R → P in PA-2. 1
    Natural variantiVAR_02384767R → S in PA-2. 1 PublicationCorresponds to variant dbSNP:rs747053913Ensembl.1
    Natural variantiVAR_000272106S → R in PA-2. 1
    Natural variantiVAR_023848107V → M in PA-2. 1 PublicationCorresponds to variant dbSNP:rs1553774114EnsemblClinVar.1
    Natural variantiVAR_023849112G → D in PA-2. 1 PublicationCorresponds to variant dbSNP:rs202247818EnsemblClinVar.1
    Natural variantiVAR_000273131G → R in PA-2. 1
    Natural variantiVAR_009081140K → KICK in PA-2. 1
    Natural variantiVAR_023850153A → P in PA-2. 1 PublicationCorresponds to variant dbSNP:rs202247819EnsemblClinVar.1
    Natural variantiVAR_023851165R → Q in PA-2; does not affect either heteromeric or homomeric assembly. 2 PublicationsCorresponds to variant dbSNP:rs1304714042EnsemblClinVar.1
    Natural variantiVAR_000274165R → W in PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization. 2 PublicationsCorresponds to variant dbSNP:rs879253815EnsemblClinVar.1
    Natural variantiVAR_000275168E → K in PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization. 3 PublicationsCorresponds to variant dbSNP:rs121964960EnsemblClinVar.1
    Natural variantiVAR_023852188G → R in PA-2. 1 PublicationCorresponds to variant dbSNP:rs746102997EnsemblClinVar.1
    Natural variantiVAR_000276198G → D in PA-2. Corresponds to variant dbSNP:rs762354873Ensembl.1
    Natural variantiVAR_009082205V → D in PA-2. 1 Publication1
    Natural variantiVAR_009083228P → L in PA-2. Corresponds to variant dbSNP:rs374722096EnsemblClinVar.1
    Natural variantiVAR_023853246G → V in PA-2. 1 Publication1
    Natural variantiVAR_048163287P → S1 PublicationCorresponds to variant dbSNP:rs2228310Ensembl.1
    Natural variantiVAR_023854341Missing in PA-2. 1 Publication1
    Natural variantiVAR_000277408Missing in PA-2. 2 Publications1
    Natural variantiVAR_000278410R → W in PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization. 4 PublicationsCorresponds to variant dbSNP:rs121964959EnsemblClinVar.1
    Natural variantiVAR_009084428T → I in PA-2. 2 PublicationsCorresponds to variant dbSNP:rs111033542EnsemblClinVar.1
    Natural variantiVAR_023855430I → L in PA-2. 1 Publication1
    Natural variantiVAR_023856435Y → C in PA-2. 1 PublicationCorresponds to variant dbSNP:rs121964961EnsemblClinVar.1
    Natural variantiVAR_023857439Y → C in PA-2. 1 PublicationCorresponds to variant dbSNP:rs769521436EnsemblClinVar.1
    Natural variantiVAR_009085442M → T in PA-2. 1 Publication1
    Natural variantiVAR_023858468A → T in PA-2. 1 PublicationCorresponds to variant dbSNP:rs775563122EnsemblClinVar.1
    Natural variantiVAR_000279497A → V Found in patients with propionic acidemia; does not affect either heteromeric or homomeric assembly; decreased thermostability affecting holoenzyme oligomerization; no effect on propionyl-CoA carboxylase activity. 1 PublicationCorresponds to variant dbSNP:rs142403318EnsemblClinVar.1
    Natural variantiVAR_000280512R → C in PA-2; affects heteromeric and homomeric assembly. 2 PublicationsCorresponds to variant dbSNP:rs186710233EnsemblClinVar.1
    Natural variantiVAR_000281519L → P in PA-2; affects heteromeric and homomeric assembly. 1 PublicationCorresponds to variant dbSNP:rs202247822EnsemblClinVar.1
    Natural variantiVAR_009086536N → D in PA-2; affects heteromeric and homomeric assembly. 1 PublicationCorresponds to variant dbSNP:rs202247823EnsemblClinVar.1

    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_042568124Q → QQIIGWAQWLPLVISALWEA E in isoform 2. 1 Publication1

    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
    		X73424 mRNA Translation: CAA51825.1
    S67325 mRNA Translation: AAB28900.1
    AJ006487 AJ006499 Genomic DNA Translation: CAA07066.1
    AK295312 mRNA Translation: BAH12030.1
    AC069524 Genomic DNA No translation available.
    CH471052 Genomic DNA Translation: EAW79118.1
    BC013768 mRNA Translation: AAH13768.1
    BC053661 mRNA Translation: AAH53661.1
    M13573 mRNA Translation: AAA60036.1
    M31167 Genomic DNA Translation: AAA60037.1
    M31169 Genomic DNA Translation: AAA60038.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS3089.1 [P05166-1]
    CCDS54643.1 [P05166-2]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		T45009

    NCBI Reference Sequences

    More...    RefSeqi    		NP_000523.2, NM_000532.4 [P05166-1]
    NP_001171485.1, NM_001178014.1 [P05166-2]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000251654; ENSP00000251654; ENSG00000114054 [P05166-1]
    ENST00000469217; ENSP00000419027; ENSG00000114054 [P05166-2]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		5096

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:5096

    UCSC genome browser

    More...    UCSCi    		uc003eqy.3, human [P05166-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, 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
    		X73424 mRNA Translation: CAA51825.1
    S67325 mRNA Translation: AAB28900.1
    AJ006487 AJ006499 Genomic DNA Translation: CAA07066.1
    AK295312 mRNA Translation: BAH12030.1
    AC069524 Genomic DNA No translation available.
    CH471052 Genomic DNA Translation: EAW79118.1
    BC013768 mRNA Translation: AAH13768.1
    BC053661 mRNA Translation: AAH53661.1
    M13573 mRNA Translation: AAA60036.1
    M31167 Genomic DNA Translation: AAA60037.1
    M31169 Genomic DNA Translation: AAA60038.1
    CCDSiCCDS3089.1 [P05166-1]
    CCDS54643.1 [P05166-2]
    PIRiT45009
    RefSeqiNP_000523.2, NM_000532.4 [P05166-1]
    NP_001171485.1, NM_001178014.1 [P05166-2]

    3D structure databases

    SMRiP05166
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi111129, 70 interactors
    CORUMiP05166
    DIPiDIP-38244N
    IntActiP05166, 14 interactors
    MINTiP05166
    STRINGi9606.ENSP00000419027

    Chemistry databases

    DrugBankiDB00121, Biotin
    DB00161, Valine

    PTM databases

    iPTMnetiP05166
    PhosphoSitePlusiP05166

    Polymorphism and mutation databases

    BioMutaiPCCB
    DMDMi124106304

    Proteomic databases

    EPDiP05166
    jPOSTiP05166
    MassIVEiP05166
    MaxQBiP05166
    PaxDbiP05166
    PeptideAtlasiP05166
    PRIDEiP05166
    ProteomicsDBi51816 [P05166-1]
    51817 [P05166-2]

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...    Antibodypediai    		33408, 198 antibodies

    The DNASU plasmid repository

    More...    DNASUi    		5096

    Genome annotation databases

    EnsembliENST00000251654; ENSP00000251654; ENSG00000114054 [P05166-1]
    ENST00000469217; ENSP00000419027; ENSG00000114054 [P05166-2]
    GeneIDi5096
    KEGGihsa:5096
    UCSCiuc003eqy.3, human [P05166-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		5096
    DisGeNETi5096
    EuPathDBiHostDB:ENSG00000114054.13

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		PCCB
    GeneReviewsiPCCB
    HGNCiHGNC:8654, PCCB
    HPAiENSG00000114054, Tissue enhanced (liver)
    MalaCardsiPCCB
    MIMi232050, gene
    606054, phenotype
    neXtProtiNX_P05166
    OpenTargetsiENSG00000114054
    Orphaneti35, Propionic acidemia
    PharmGKBiPA32993

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG0540, Eukaryota
    GeneTreeiENSGT00940000157741
    InParanoidiP05166
    OrthoDBi402617at2759
    PhylomeDBiP05166
    TreeFamiTF314350

    Enzyme and pathway databases

    UniPathwayiUPA00945;UER00908
    BioCyciMetaCyc:ENSG00000114054-MONOMER
    PathwayCommonsiP05166
    ReactomeiR-HSA-196780, Biotin transport and metabolism
    R-HSA-3371599, Defective HLCS causes multiple carboxylase deficiency
    R-HSA-71032, Propionyl-CoA catabolism
    SABIO-RKiP05166

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...    BioGRID-ORCSi    		5096, 4 hits in 843 CRISPR screens

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...    ChiTaRSi    		PCCB, human

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

    More...    GenomeRNAii    		5096
    PharosiP05166, Tbio

    Protein Ontology

    More...    PROi    		PR:P05166
    RNActiP05166, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000114054, Expressed in right adrenal gland and 238 other tissues
    ExpressionAtlasiP05166, baseline and differential
    GenevisibleiP05166, HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR034733, AcCoA_carboxyl
    IPR029045, ClpP/crotonase-like_dom_sf
    IPR011763, COA_CT_C
    IPR011762, COA_CT_N
    PfamiView protein in Pfam
    PF01039, Carboxyl_trans, 1 hit
    SUPFAMiSSF52096, SSF52096, 2 hits
    PROSITEiView protein in PROSITE
    PS50989, COA_CT_CTER, 1 hit
    PS50980, COA_CT_NTER, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    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 nameiPCCB_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: P05166
    Secondary accession number(s): B7Z2Z4, Q16813, Q96CX0
    <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 13, 1987
    Last sequence update: January 23, 2007
    Last modified: December 2, 2020
    This is version 201 of the entry and version 3 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

    Direct protein sequencing, Reference proteome

    Documents

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