Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 204 (29 Sep 2021)
Sequence version 3 (05 Oct 2010)
Previous versions | rss
Add a publicationFeedback
Protein

Acetyl-CoA carboxylase 2

Gene

ACACB

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

Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism (PubMed:16854592, PubMed:19236960, PubMed:20457939, PubMed:20952656, PubMed:19900410, PubMed:26976583).

Catalyzes a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (PubMed:19236960, PubMed:20457939, PubMed:20952656, PubMed:26976583).

Through the production of malonyl-CoA that allosterically inhibits carnitine palmitoyltransferase 1 at the mitochondria, negatively regulates fatty acid oxidation (By similarity).

Together with its cytosolic isozyme ACACA, which is involved in de novo fatty acid biosynthesis, promotes lipid storage (By similarity).

By similarity6 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

Protein has several cofactor binding sites:

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

Activity is increased by oligomerization of the protein into filaments (PubMed:19900410). The oligomerization and the activity of the enzyme are inhibited by phosphorylation at Ser-222 (PubMed:12488245). Inhibited by its product, malonyl-CoA (PubMed:16854592). Activated by citrate (PubMed:16854592). Activation by MID1IP1 is citrate-dependent (PubMed:20457939). Soraphen A, inhibits the enzyme by preventing the formation of active filamentous oligomers (Probable).1 Publication4 Publications

<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=120 µM for ATP1 Publication
  2. KM=110 µM for ATP (isoform 2)1 Publication
  3. KM=58 µM for acetyl-CoA1 Publication
  4. KM=94 µM for acetyl-CoA (isoform 3)1 Publication
  5. KM=6.5 mM for NaHCO3 (isoform 3)1 Publication
  6. KM=3.0 mM for NaHCO31 Publication

pH dependencei

Optimum pH is 7.5.1 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: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.2 Publications This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi567Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi580Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi580Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi582Magnesium or manganese 2PROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei584By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1934Coenzyme ABy similarity1
Binding sitei2238Coenzyme ABy similarity1
Binding sitei2240Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi458 – 463ATPPROSITE-ProRule annotation6

<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 functionAllosteric enzyme, Ligase, Multifunctional enzyme
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS01211-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.4.14, 2681
6.4.1.2, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
O00763

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-163765, ChREBP activates metabolic gene expression
R-HSA-196780, Biotin transport and metabolism
R-HSA-200425, Carnitine metabolism
R-HSA-2426168, Activation of gene expression by SREBF (SREBP)

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O00763

SIGNOR Signaling Network Open Resource

More...
SIGNORi
O00763

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

More...
UniPathwayi
UPA00655;UER00711

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000730

<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:
Acetyl-CoA carboxylase 2Curated (EC:6.4.1.26 Publications)
Alternative name(s):
ACC-beta
<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:ACACBImported
Synonyms:ACC2, ACCB
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 12

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:85, ACACB

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
601557, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O00763

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000076555

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

Keywords - Cellular componenti

Mitochondrion

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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Inhibition of ACACB may prevent lipid-induced insulin resistance and type 2 diabetes, making the enzyme a potential pharmaceutical target for treatment of obesity and type 2 diabetes.Curated

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>Mutagenesisi277R → A: Loss of regulation of oligomerization by phosphorylation at S-222. 1 Publication1
Mutagenesisi671E → A: Altered regulation of oligomerization by phosphorylation at S-222. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
32

Open Targets

More...
OpenTargetsi
ENSG00000076555

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24422

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O00763, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4829

Drug and drug target database

More...
DrugBanki
DB03781, 2-[4-(2,4-Dichlorophenoxy)Phenoxy]Propanoic Acid
DB00173, Adenine
DB00121, Biotin
DB07870, Haloxyfop-P
DB02859, Soraphen A

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1264

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ACACB

<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 – ?MitochondrionBy similarity
<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_0000146767? – 2458Acetyl-CoA carboxylase 2Curated

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 residuei35PhosphoserineCombined sources1
Modified residuei70PhosphothreonineCombined sources1
Modified residuei91PhosphoserineCombined sources1
Modified residuei95PhosphoserineCombined sources1
Modified residuei169PhosphoserineBy similarity1
Modified residuei175PhosphoserineBy similarity1
Modified residuei192PhosphoserineBy similarity1
Modified residuei195PhosphoserineBy similarity1
Modified residuei200PhosphoserineCombined sources1
Modified residuei207PhosphothreonineBy similarity1
Modified residuei220PhosphoserineBy similarity1
Modified residuei222Phosphoserine; by AMPK2 Publications1
Modified residuei469PhosphoserineCombined sources1
Modified residuei753PhosphothreonineBy similarity1
Modified residuei929N6-biotinyllysinePROSITE-ProRule annotation1 Publication1
Modified residuei1340PhosphoserineBy similarity1
Modified residuei1342PhosphothreonineCombined sources1
Modified residuei1360PhosphoserineBy similarity1
Modified residuei1405PhosphoserineBy similarity1

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

The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity.1 Publication
Phosphorylation at Ser-222 by AMPK inactivates the enzyme (PubMed:12488245). Required for the maintenance of skeletal muscle lipid and glucose homeostasis (By similarity).By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O00763

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O00763

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
O00763

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O00763

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

More...
PaxDbi
O00763

PeptideAtlas

More...
PeptideAtlasi
O00763

PRoteomics IDEntifications database

More...
PRIDEi
O00763

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
48022 [O00763-1]
48023 [O00763-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O00763

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

More...
PhosphoSitePlusi
O00763

<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 a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed with highest levels in heart, skeletal muscle, liver, adipose tissue, mammary gland, adrenal gland and colon (PubMed:9099716). Isoform 3 is expressed in skeletal muscle, adipose tissue and liver (at protein level) (PubMed:19190759). Isoform 3 is detected at high levels in adipose tissue with lower levels in heart, liver, skeletal muscle and testis (PubMed:19190759).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000076555, Expressed in parietal pleura and 238 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O00763, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O00763, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000076555, Group enriched (adipose tissue, breast, liver, skeletal muscle)

<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

Monomer, homodimer, and homotetramer (PubMed:20952656, PubMed:18772397). Forms filamentous polymers (PubMed:20457939, PubMed:20952656, PubMed:19900410).

Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity in a citrate-dependent manner (PubMed:20952656, PubMed:20457939).

4 Publications

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

More...
BioGRIDi
106550, 28 interactors

Database of interacting proteins

More...
DIPi
DIP-51617N

Protein interaction database and analysis system

More...
IntActi
O00763, 14 interactors

Molecular INTeraction database

More...
MINTi
O00763

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000341044

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O00763

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
O00763, 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

Secondary structure

12458
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
O00763

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O00763

<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>Domaini259 – 761Biotin carboxylationPROSITE-ProRule annotationAdd BLAST503
Domaini414 – 609ATP-graspPROSITE-ProRule annotationAdd BLAST196
Domaini888 – 962Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
Domaini1695 – 2025CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST331
Domaini2029 – 2345CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST317

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>Regioni35 – 155DisorderedSequence analysisAdd BLAST121
Regioni174 – 193DisorderedSequence analysisAdd BLAST20
Regioni1695 – 2345CarboxyltransferasePROSITE-ProRule annotationAdd BLAST651

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 biasi35 – 73Polar residuesSequence analysisAdd BLAST39
Compositional biasi101 – 150Polar residuesSequence analysisAdd BLAST50

<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

Consists of an N-terminal biotin carboxylation/carboxylase (BC) domain that catalyzes the ATP-dependent transient carboxylation of the biotin covalently attached to the central biotinyl-binding/biotin carboxyl carrier (BCC) domain (Probable). The C-terminal carboxyl transferase (CT) domain catalyzes the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA to produce malonyl-CoA (Probable).2 Publications

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0368, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155049

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000395_5_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O00763

Identification of Orthologs from Complete Genome Data

More...
OMAi
ENIKCLK

Database of Orthologous Groups

More...
OrthoDBi
861989at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O00763

TreeFam database of animal gene trees

More...
TreeFami
TF300061

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1490.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034733, AcCoA_carboxyl
IPR013537, AcCoA_COase_cen
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR005481, BC-like_N
IPR011764, Biotin_carboxylation_dom
IPR005482, Biotin_COase_C
IPR000089, Biotin_lipoyl
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR029045, ClpP/crotonase-like_dom_sf
IPR011763, COA_CT_C
IPR011762, COA_CT_N
IPR016185, PreATP-grasp_dom_sf
IPR011054, Rudment_hybrid_motif
IPR011053, Single_hybrid_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08326, ACC_central, 1 hit
PF02785, Biotin_carb_C, 1 hit
PF00289, Biotin_carb_N, 1 hit
PF00364, Biotin_lipoyl, 1 hit
PF01039, Carboxyl_trans, 1 hit
PF02786, CPSase_L_D2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00878, Biotin_carb_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51230, SSF51230, 1 hit
SSF51246, SSF51246, 1 hit
SSF52096, SSF52096, 2 hits
SSF52440, SSF52440, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975, ATP_GRASP, 1 hit
PS50979, BC, 1 hit
PS50968, BIOTINYL_LIPOYL, 1 hit
PS50989, COA_CT_CTER, 1 hit
PS50980, COA_CT_NTER, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">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 (3+)i

<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.

<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 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 3 <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

This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O00763-1) [UniParc]FASTAAdd to basket
Also known as: Long

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
MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA
60 70 80 90 100
SDNSGETPQR NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP
110 120 130 140 150
RNPLSSSDAA PSPELQANGT GTQGLEATDT NGLSSSARPQ GQQAGSPSKE
160 170 180 190 200
DKKQANIKRQ LMTNFILGSF DDYSSDEDSV AGSSRESTRK GSRASLGALS
210 220 230 240 250
LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR DFTVASPAEF
260 270 280 290 300
VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT
310 320 330 340 350
PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG
360 370 380 390 400
WGHASENPKL PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL
410 420 430 440 450
PWSGSGLTVE WTEDDLQQGK RISVPEDVYD KGCVKDVDEG LEAAERIGFP
460 470 480 490 500
LMIKASEGGG GKGIRKAESA EDFPILFRQV QSEIPGSPIF LMKLAQHARH
510 520 530 540 550
LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP LAIFEFMEQC
560 570 580 590 600
AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL
610 620 630 640 650
PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA
660 670 680 690 700
ARITSENPDE GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF
710 720 730 740 750
GHCFSWGENR EEAISNMVVA LKELSIRGDF RTTVEYLINL LETESFQNND
760 770 780 790 800
IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL NVADAMFRTC MTDFLHSLER
810 820 830 840 850
GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM NGCHIEIDAH
860 870 880 890 900
RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP
910 920 930 940 950
SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA
960 970 980 990 1000
VLEAGCVVAR LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL
1010 1020 1030 1040 1050
ENLTNVMSGF CLPEPVFSIK LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA
1060 1070 1080 1090 1100
GRIPAPVEKS VRRVMAQYAS NITSVLCQFP SQQIATILDC HAATLQRKAD
1110 1120 1130 1140 1150
REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV EHHFQQAHYD
1160 1170 1180 1190 1200
KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD
1210 1220 1230 1240 1250
ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA
1260 1270 1280 1290 1300
IDMYGHQFCP ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG
1310 1320 1330 1340 1350
YIAYELNSLQ HRQLPDGTCV VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS
1360 1370 1380 1390 1400
TELFMDSGFS PLCQRMGAMV AFRRFEDFTR NFDEVISCFA NVPKDTPLFS
1410 1420 1430 1440 1450
EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP ILRTFVQSKK
1460 1470 1480 1490 1500
NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL
1510 1520 1530 1540 1550
ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD
1560 1570 1580 1590 1600
LITKEASFEY LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV
1610 1620 1630 1640 1650
IMDPFKIEES VRYMVMRYGS RLWKLRVLQA EVKINIRQTT TGSAVPIRLF
1660 1670 1680 1690 1700
ITNESGYYLD ISLYKEVTDS RSGNIMFHSF GNKQGPQHGM LINTPYVTKD
1710 1720 1730 1740 1750
LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK DILTYTELVL
1760 1770 1780 1790 1800
DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG
1810 1820 1830 1840 1850
SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV
1860 1870 1880 1890 1900
DPEDPHKGFK YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD
1910 1920 1930 1940 1950
DGLGVENLRG SGMIAGESSL AYEEIVTISL VTCRAIGIGA YLVRLGQRVI
1960 1970 1980 1990 2000
QVENSHIILT GASALNKVLG REVYTSNNQL GGVQIMHYNG VSHITVPDDF
2010 2020 2030 2040 2050
EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR APYDPRWMLA
2060 2070 2080 2090 2100
GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE
2110 2120 2130 2140 2150
TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP
2160 2170 2180 2190 2200
LMIFANWRGF SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR
2210 2220 2230 2240 2250
GGSWVVIDAT INPLCIEMYA DKESRGGVLE PEGTVEIKFR KKDLIKSMRR
2260 2270 2280 2290 2300
IDPAYKKLME QLGEPDLSDK DRKDLEGRLK AREDLLLPIY HQVAVQFADF
2310 2320 2330 2340 2350
HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK QEILQASGEL
2360 2370 2380 2390 2400
SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR
2410 2420 2430 2440 2450
ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS

TMDSPAST
Length:2,458
Mass (Da):276,541
Last modified:October 5, 2010 - 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:iED12674A1A8A0706
GO
Isoform 2 (identifier: O00763-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1118-1187: Missing.

Show »
Length:2,388
Mass (Da):268,166
Checksum:i10A218FFD1408B68
GO
Isoform 3Curated (identifier: O00763-3) [UniParc]FASTAAdd to basket
Also known as: ACC2.v21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-202: Missing.
     203-218: AYLTTGEAETRVPTMR → MSPAKCKICFPDREVK

Show »
Length:2,256
Mass (Da):255,093
Checksum:iA0736151D792EC18
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8W8T8F8W8T8_HUMAN
Acetyl-CoA carboxylase 2
ACACB
858Annotation 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>
H0YGH5H0YGH5_HUMAN
Acetyl-CoA carboxylase 2
ACACB
859Annotation 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>
F5H5C3F5H5C3_HUMAN
Acetyl-CoA carboxylase 2
ACACB
143Annotation 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>
S4R3S7S4R3S7_HUMAN
Acetyl-CoA carboxylase 2
ACACB
155Annotation 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>
A0A087WUA1A0A087WUA1_HUMAN
Acetyl-CoA carboxylase 2
ACACB
112Annotation 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB58382 differs from that shown. Many Frameshifts and conflicts.Curated
The sequence CAE01470 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

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 conflicti9C → R in ABF48723 (PubMed:16854592).Curated1
Sequence conflicti120T → I in AAR37018 (Ref. 4) Curated1
Sequence conflicti422I → T in AAR37018 (Ref. 4) Curated1
Sequence conflicti1340S → N in AAC50571 (PubMed:8670171).Curated1
Sequence conflicti1383D → G in AAC50571 (PubMed:8670171).Curated1
Sequence conflicti1425V → M in AAC50571 (PubMed:8670171).Curated1
Sequence conflicti1819 – 1821AEG → PEA in AAC50571 (PubMed:8670171).Curated3
Sequence conflicti1892 – 1893MI → IM in AAC50571 (PubMed:8670171).Curated2

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_062667193R → L in a pancreatic ductal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_031255552I → V. Corresponds to variant dbSNP:rs16940029Ensembl.1
Natural variantiVAR_031256651A → T. Corresponds to variant dbSNP:rs2300455Ensembl.1
Natural variantiVAR_0312572141V → I2 PublicationsCorresponds to variant dbSNP:rs2075260Ensembl.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_0570811 – 202Missing in isoform 3. 1 PublicationAdd BLAST202
Alternative sequenceiVSP_057082203 – 218AYLTT…VPTMR → MSPAKCKICFPDREVK in isoform 3. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_0005471118 – 1187Missing in isoform 2. 1 PublicationAdd BLAST70

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
U89344 mRNA Translation: AAB58382.1 Sequence problems.
DQ493870 mRNA Translation: ABF48723.1
AJ575431 mRNA Translation: CAE01470.2 Sequence problems.
AJ575592 mRNA Translation: CAE01471.3
AY382667 mRNA Translation: AAR37018.1
AC007637 Genomic DNA No translation available.
U34591 mRNA Translation: AAC50571.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31898.1 [O00763-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S71091

NCBI Reference Sequences

More...
RefSeqi
NP_001084.3, NM_001093.3 [O00763-1]
XP_005253933.1, XM_005253876.4
XP_006719430.1, XM_006719367.3 [O00763-3]
XP_011536561.1, XM_011538259.2 [O00763-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000338432; ENSP00000341044; ENSG00000076555 [O00763-1]
ENST00000377848; ENSP00000367079; ENSG00000076555 [O00763-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
32

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:32

UCSC genome browser

More...
UCSCi
uc001tob.4, human [O00763-1]

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
U89344 mRNA Translation: AAB58382.1 Sequence problems.
DQ493870 mRNA Translation: ABF48723.1
AJ575431 mRNA Translation: CAE01470.2 Sequence problems.
AJ575592 mRNA Translation: CAE01471.3
AY382667 mRNA Translation: AAR37018.1
AC007637 Genomic DNA No translation available.
U34591 mRNA Translation: AAC50571.1
CCDSiCCDS31898.1 [O00763-1]
PIRiS71091
RefSeqiNP_001084.3, NM_001093.3 [O00763-1]
XP_005253933.1, XM_005253876.4
XP_006719430.1, XM_006719367.3 [O00763-3]
XP_011536561.1, XM_011538259.2 [O00763-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DN8NMR-A885-971[»]
2HJWX-ray2.50A217-775[»]
2KCCNMR-A891-965[»]
3FF6X-ray3.19A/B/C/D1693-2450[»]
3GIDX-ray2.30A/B238-760[»]
3GLKX-ray2.10A238-760[»]
3JRWX-ray2.60A217-775[»]
3JRXX-ray2.50A217-775[»]
3TDCX-ray2.41A1690-2445[»]
4HQ6X-ray2.70A217-776[»]
5KKNX-ray2.60B/C238-760[»]
SMRiO00763
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi106550, 28 interactors
DIPiDIP-51617N
IntActiO00763, 14 interactors
MINTiO00763
STRINGi9606.ENSP00000341044

Chemistry databases

BindingDBiO00763
ChEMBLiCHEMBL4829
DrugBankiDB03781, 2-[4-(2,4-Dichlorophenoxy)Phenoxy]Propanoic Acid
DB00173, Adenine
DB00121, Biotin
DB07870, Haloxyfop-P
DB02859, Soraphen A
GuidetoPHARMACOLOGYi1264
SwissLipidsiSLP:000000730

PTM databases

iPTMnetiO00763
PhosphoSitePlusiO00763

Genetic variation databases

BioMutaiACACB

Proteomic databases

EPDiO00763
jPOSTiO00763
MassIVEiO00763
MaxQBiO00763
PaxDbiO00763
PeptideAtlasiO00763
PRIDEiO00763
ProteomicsDBi48022 [O00763-1]
48023 [O00763-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
1321, 186 antibodies

The DNASU plasmid repository

More...
DNASUi
32

Genome annotation databases

EnsembliENST00000338432; ENSP00000341044; ENSG00000076555 [O00763-1]
ENST00000377848; ENSP00000367079; ENSG00000076555 [O00763-1]
GeneIDi32
KEGGihsa:32
UCSCiuc001tob.4, human [O00763-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
32
DisGeNETi32

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ACACB
HGNCiHGNC:85, ACACB
HPAiENSG00000076555, Group enriched (adipose tissue, breast, liver, skeletal muscle)
MIMi601557, gene
neXtProtiNX_O00763
OpenTargetsiENSG00000076555
PharmGKBiPA24422
VEuPathDBiHostDB:ENSG00000076555

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0368, Eukaryota
GeneTreeiENSGT00940000155049
HOGENOMiCLU_000395_5_0_1
InParanoidiO00763
OMAiENIKCLK
OrthoDBi861989at2759
PhylomeDBiO00763
TreeFamiTF300061

Enzyme and pathway databases

UniPathwayiUPA00655;UER00711
BioCyciMetaCyc:HS01211-MONOMER
BRENDAi6.3.4.14, 2681
6.4.1.2, 2681
PathwayCommonsiO00763
ReactomeiR-HSA-163765, ChREBP activates metabolic gene expression
R-HSA-196780, Biotin transport and metabolism
R-HSA-200425, Carnitine metabolism
R-HSA-2426168, Activation of gene expression by SREBF (SREBP)
SABIO-RKiO00763
SIGNORiO00763

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
32, 3 hits in 1011 CRISPR screens

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

More...
ChiTaRSi
ACACB, human
EvolutionaryTraceiO00763

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ACACB

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

More...
GenomeRNAii
32
PharosiO00763, Tchem

Protein Ontology

More...
PROi
PR:O00763
RNActiO00763, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000076555, Expressed in parietal pleura and 238 other tissues
ExpressionAtlasiO00763, baseline and differential
GenevisibleiO00763, HS

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR034733, AcCoA_carboxyl
IPR013537, AcCoA_COase_cen
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR005481, BC-like_N
IPR011764, Biotin_carboxylation_dom
IPR005482, Biotin_COase_C
IPR000089, Biotin_lipoyl
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR029045, ClpP/crotonase-like_dom_sf
IPR011763, COA_CT_C
IPR011762, COA_CT_N
IPR016185, PreATP-grasp_dom_sf
IPR011054, Rudment_hybrid_motif
IPR011053, Single_hybrid_motif
PfamiView protein in Pfam
PF08326, ACC_central, 1 hit
PF02785, Biotin_carb_C, 1 hit
PF00289, Biotin_carb_N, 1 hit
PF00364, Biotin_lipoyl, 1 hit
PF01039, Carboxyl_trans, 1 hit
PF02786, CPSase_L_D2, 1 hit
SMARTiView protein in SMART
SM00878, Biotin_carb_C, 1 hit
SUPFAMiSSF51230, SSF51230, 1 hit
SSF51246, SSF51246, 1 hit
SSF52096, SSF52096, 2 hits
SSF52440, SSF52440, 1 hit
PROSITEiView protein in PROSITE
PS50975, ATP_GRASP, 1 hit
PS50979, BC, 1 hit
PS50968, BIOTINYL_LIPOYL, 1 hit
PS50989, COA_CT_CTER, 1 hit
PS50980, COA_CT_NTER, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACACB_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: O00763
Secondary accession number(s): A6NK36
, Q16852, Q1HEC1, Q6KE87, Q6KE89, Q6TY48
<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: November 1, 1997
Last sequence update: October 5, 2010
Last modified: September 29, 2021
This is version 204 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

3D-structure, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again