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Entry version 150 (12 Aug 2020)
Sequence version 1 (01 Jul 1989)
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Protein

Acetyl-CoA carboxylase

Gene

ACAC

Organism
Gallus gallus (Chicken)
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

Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.By similarity

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

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

Protein has several cofactor binding sites:

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

By phosphorylation.

<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: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-CoA carboxylase (ACACA), Acetyl-CoA carboxylase (ACACA), Acetyl-CoA carboxylase (ACAC), Acetyl-CoA carboxylase (ACACA)
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%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi424Manganese 1By similarity1
Metal bindingi437Manganese 1By similarity1
Metal bindingi437Manganese 2By similarity1
Metal bindingi439Manganese 2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei441By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1800Coenzyme ABy similarity1
Binding sitei2104Coenzyme ABy similarity1
Binding sitei2106Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi315 – 320ATPPROSITE-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 functionLigase, Multifunctional enzyme
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P11029

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

More...
UniPathwayi
UPA00655;UER00711

<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:
Acetyl-CoA carboxylase (EC:6.4.1.2)
Short name:
ACC
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
<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:ACAC
<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>OrganismiGallus gallus (Chicken)
<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 identifieri9031 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<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
  • UP000000539 <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: Unplaced

<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

Cytoplasm

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001467681 – 2324Acetyl-CoA carboxylaseAdd BLAST2324

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 residuei1N-acetylmethionine1 Publication1
Modified residuei78PhosphoserineBy similarity1
Modified residuei80PhosphoserineBy similarity1
Modified residuei786N6-biotinyllysinePROSITE-ProRule annotation1 Publication1
Modified residuei1193PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P11029

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
676751, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000034072

<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
P11029

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>Domaini117 – 618Biotin carboxylationAdd BLAST502
Domaini275 – 466ATP-graspPROSITE-ProRule annotationAdd BLAST192
Domaini745 – 819Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
Domaini1553 – 1891CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST339
Domaini1895 – 2211CoA 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>Regioni1553 – 2211CarboxyltransferasePROSITE-ProRule annotationAdd BLAST659

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0368, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P11029

KEGG Orthology (KO)

More...
KOi
K11262

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P11029

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
IPR001882, Biotin_BS
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
PS00188, BIOTIN, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

P11029-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEESSQPAKP LEMNPHSRFI IGSVSEDNSE DETSSLVKLD LLEEKERSLS
60 70 80 90 100
PVSVCSDSLS DLGLPSAQDG LANHMRPSMS GLHLVKQGRD RKKVDVQRDF
110 120 130 140 150
TVASPAEFVT RFGGNRVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA
160 170 180 190 200
IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI
210 220 230 240 250
PVQAVWAGWG HASENPKLPE LLHKNGIAFM GPPSQAMWAL GDKIASSIVA
260 270 280 290 300
QTAGIPTLPW NGSGLRVDWQ ENDLQKRILN VPQELYEKGY VKDADDGLRA
310 320 330 340 350
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR
360 370 380 390 400
LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APASIATSVV
410 420 430 440 450
FEHMEQCAVK LAKMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE
460 470 480 490 500
MVADVNLPAA QLQIAMGIPL HRIKDIRVMY GVSPWGDGSI DFENSAHVPC
510 520 530 540 550
PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH
560 570 580 590 600
EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
610 620 630 640 650
ESFQQNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSFRNSVSN
660 670 680 690 700
FLHSLERGQV LPAHTLLNTV DVELIYEGRK YVLKVTRQSP NSYVVIMNSS
710 720 730 740 750
CVEVDVHRLS DGGLLLSYDG SSYTTYMKEE VDRYRITIGN KTCVFEKEND
760 770 780 790 800
PSILRSPSAG KLIQYVVEDG GHVFAGQCFA EIEVMKMVMT LTAGESGCIH
810 820 830 840 850
YVKRPGAVLD PGCVIAKLQL DDPSRVQQAE LHTGTLPQIQ STALRGEKLH
860 870 880 890 900
RIFHYVLDNL VNVMNGYCLP EPYFSSKVKG WVERLMKTLR DPSLPLLELQ
910 920 930 940 950
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA
960 970 980 990 1000
TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLKVETQ
1010 1020 1030 1040 1050
FQHGHYDKCV FALREENKSD MNAVLNYIFS HAQVTKKNLL VTMLIDQLCG
1060 1070 1080 1090 1100
RDPTLTDELI NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRHNQV
1110 1120 1130 1140 1150
ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL
1160 1170 1180 1190 1200
EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RMSFSSNLNH
1210 1220 1230 1240 1250
YGMVHVASVS DVLLDNSFTP PCQRMGGMVS FRTFEDFVRI FDEVMSCFCD
1260 1270 1280 1290 1300
SPPQSPTFPE AGHASLYDED KAAREEPIHI LNVAIKTDGD VDDDGLAAMF
1310 1320 1330 1340 1350
REFTQSKKSV LIEHGIRRLT FLVAQKREFP KFFTFRARDK FEEDRIYRHL
1360 1370 1380 1390 1400
EPALAFQLEL NRMRNFDLTA IPCANHKMHL YLGAAKVEVG TEVTDYRFFV
1410 1420 1430 1440 1450
RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN TNVRTDCNHI
1460 1470 1480 1490 1500
FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTPTG
1510 1520 1530 1540 1550
KAIPIRLFLT NESGYYLDIS LYKEVTDSRT GQIMFQAYGD KQGPLHGMLI
1560 1570 1580 1590 1600
NTPYVTKDLL QSKRFQAQSL GTSYVYDIPE MFRQSLIKLW DSMNEHAFLP
1610 1620 1630 1640 1650
TPPLPSDILT YTELVLDDQG QLVHMNRLPG GNEIGMVAWK MTLKTPEYPE
1660 1670 1680 1690 1700
GRDIIVIGND ITYRIGSFGP QEDVLFLRAS ELARTHGIPR IYVAANSGAR
1710 1720 1730 1740 1750
IGLAEEIRHM FHVAWEDPDD PYKGYKYLYL TPQDYKKVSA LNSVHCEHVE
1760 1770 1780 1790 1800
DNGESRYKIT DIIGKEDGLG IENLRGSGMI AGESSLAYES IITINLVTCR
1810 1820 1830 1840 1850
AIGIGAYLVR LGQRTIQVEN SHIILTGCGA LNKVLGREVY TSNNQLGGIQ
1860 1870 1880 1890 1900
IMHNNGVTHG TVCDDFEGVY TILLWLSYMP KSVYSPVPIL KVKDPIDRTI
1910 1920 1930 1940 1950
DFVPTKTPYD PRWMLAGRPN PSQKGQWQSG FFDNGSFLEI MQPWAQTVVV
1960 1970 1980 1990 2000
GRARLGGIPV GVVAVETRTV ELSIPADPAN LDSEAKIIQQ AGQVWFPDSA
2010 2020 2030 2040 2050
FKTAQAINDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF GAYIVDGLRE
2060 2070 2080 2090 2100
YRQPVLIYIP PQAELRGGSW AVIDPTINPR HMEMYADRES RGGILEPEGT
2110 2120 2130 2140 2150
VEIKFRRKDL VKTMRRVDPV YMRLAERLGT PELSAADRKD LESKLKEREE
2160 2170 2180 2190 2200
FLIPIYHQVA MQFADLHDTP GRMQEKGAIT DILDWKTSRT FFYWRLRRLL
2210 2220 2230 2240 2250
LEDVVKKKIH DANPELTDGQ IQAMLRRWFV EVEGTVKAYL WDSNKDLVEW
2260 2270 2280 2290 2300
LEKQLMEEEG VRSVVDENIK YISRDYILKQ IRSLVQANPE VAMDSIVHMT
2310 2320
QHISPTQRAE IVRILSTMDS PSST
Length:2,324
Mass (Da):262,720
Last modified:July 1, 1989 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3F1C541F01BBBEF6
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J03541 mRNA Translation: AAA48701.1
X05019 mRNA Translation: CAA28675.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A29924

NCBI Reference Sequences

More...
RefSeqi
NP_990836.1, NM_205505.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
396504

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gga:396504

<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
J03541 mRNA Translation: AAA48701.1
X05019 mRNA Translation: CAA28675.1
PIRiA29924
RefSeqiNP_990836.1, NM_205505.1

3D structure databases

SMRiP11029
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi676751, 1 interactor
STRINGi9031.ENSGALP00000034072

Proteomic databases

PRIDEiP11029

Genome annotation databases

GeneIDi396504
KEGGigga:396504

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
31

Phylogenomic databases

eggNOGiKOG0368, Eukaryota
InParanoidiP11029
KOiK11262
PhylomeDBiP11029

Enzyme and pathway databases

UniPathwayiUPA00655;UER00711
SABIO-RKiP11029

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P11029

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
IPR001882, Biotin_BS
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
PS00188, BIOTIN, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiACAC_CHICK
<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: P11029
<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: July 1, 1989
Last sequence update: July 1, 1989
Last modified: August 12, 2020
This is version 150 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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