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Entry version 108 (08 May 2019)
Sequence version 1 (01 Oct 2003)
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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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

<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

Mg2+By similarity, Mn2+By similarityNote: Binds 4 Mg2+ or Mn2+ ions per subunit.By similarity

<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: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes carbamoyl phosphate from bicarbonate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes carbamoyl phosphate from bicarbonate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
  2. Aspartate carbamoyltransferase (pyrB)
  3. Putative dihydroorotase (pyrC)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine 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 bindingi285Magnesium or manganese 1UniRule annotation1
Metal bindingi299Magnesium or manganese 1UniRule annotation1
Metal bindingi299Magnesium or manganese 2UniRule annotation1
Metal bindingi301Magnesium or manganese 2UniRule annotation1
Metal bindingi833Magnesium or manganese 3UniRule annotation1
Metal bindingi849Magnesium or manganese 3UniRule annotation1
Metal bindingi849Magnesium or manganese 4UniRule annotation1
Metal bindingi851Magnesium or manganese 4UniRule annotation1

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 bindingi159 – 216ATPUniRule annotationAdd BLAST58
Nucleotide bindingi710 – 766ATPUniRule annotationAdd BLAST57

<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
Biological processAmino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
RBAL243090:RB12113-MONOMER

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

More...
UniPathwayi
UPA00068;UER00171
UPA00070;UER00115

<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:
Carbamoyl-phosphate synthase large chainUniRule annotation (EC:6.3.5.5UniRule annotation)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chainUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:carBUniRule annotation
Ordered Locus Names:RB12113
<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>OrganismiRhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
<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 identifieri243090 [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 lineageiBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula
<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
  • UP000001025 <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

<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

GO - Cellular componenti

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002270221 – 1083Carbamoyl-phosphate synthase large chainAdd BLAST1083

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q7UJ58

<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

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.

UniRule annotation

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
243090.RB12113

<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
Q7UJ58

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_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>Domaini133 – 328ATP-grasp 1UniRule annotationAdd BLAST196
Domaini683 – 878ATP-grasp 2UniRule annotationAdd BLAST196
Domaini945 – 1083MGS-likePROSITE-ProRule annotationAdd BLAST139

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>Regioni1 – 402Carboxyphosphate synthetic domainAdd BLAST402
Regioni403 – 557Oligomerization domainAdd BLAST155
Regioni558 – 944Carbamoyl phosphate synthetic domainAdd BLAST387
Regioni945 – 1083Allosteric domainAdd BLAST139

<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 CarB family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CU6 Bacteria
COG0458 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234582

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q7UJ58

KEGG Orthology (KO)

More...
KOi
K01955

Identification of Orthologs from Complete Genome Data

More...
OMAi
AVFPFNK

Database of Orthologous Groups

More...
OrthoDBi
48855at2

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01424 MGS_CPS_II, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1030.10, 1 hit
3.40.50.1380, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01210_A CPSase_L_chain_A, 1 hit
MF_01210_B CPSase_L_chain_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011761 ATP-grasp
IPR006275 CarbamoylP_synth_lsu
IPR005480 CarbamoylP_synth_lsu_oligo
IPR036897 CarbamoylP_synth_lsu_oligo_sf
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR005483 CbamoylP_synth_lsu_CPSase_dom
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR033937 MGS_CPS_CarB
IPR016185 PreATP-grasp_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02786 CPSase_L_D2, 2 hits
PF02787 CPSase_L_D3, 1 hit
PF02142 MGS, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00098 CPSASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01096 CPSase_L_D3, 1 hit
SM00851 MGS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48108 SSF48108, 1 hit
SSF52335 SSF52335, 1 hit
SSF52440 SSF52440, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01369 CPSaseII_lrg, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975 ATP_GRASP, 2 hits
PS00867 CPSASE_2, 2 hits
PS51855 MGS, 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>Sequencei

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

Q7UJ58-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPRRDDIKKI LLIGSGPIVI GQACEFDYSG TQACKALREE GYEVVLVNSN
60 70 80 90 100
PATIMTDPAT ADATYIEPLT WQIVEKVIAK ERPDALLPTL GGQTGLNVAM
110 120 130 140 150
DLDANGVLEK YGVEMIAANA KVIAKAEERE QFKQAMDKIG LDVCKGFTVR
160 170 180 190 200
TLADARKALA EVGLPAVVRP SFTMGGSGSA IAYNKDDFDS LVQNGLDQSP
210 220 230 240 250
VTEVLIEESI IGWKEYEMEV MRDCDDNVVI ICAIENFDPM GVHTGDSITV
260 270 280 290 300
APAQTLSDKE YQRMRDASLA VIREIGVETG GSNIQFAIEP DTGRMIVIEM
310 320 330 340 350
NPRVSRSSAL ASKATGFPIA KIAAKLAVGY RLWELPNDIT QKTKACFEPT
360 370 380 390 400
IDYVVTKMPR FAFEKFPEAD ATLTTQMKSV GETMSIGRTF QESFQKALRG
410 420 430 440 450
LEVGAFGFGS DPKDLWGTED QPSRDEIRAK LSTPGSERVF YIRYAFKDGM
460 470 480 490 500
TAAEIHSLTN IDPWFLDHLQ QLIETEDNLR AIGKLDAIDV DTMRDAKRRG
510 520 530 540 550
FSDRQIATIT SKTESQVRAK RLEMGIRPVY KSVDTCAAEF EAFTPYYYST
560 570 580 590 600
YESETEVPAK GDKKRVVILG GGPNRIGQGI EFDYCCCHAS FALQEMGIES
610 620 630 640 650
IMVNSNPETV STDYDTSDIL FFEPLTIEDV LNICDAMQPD GVIVQFGGQT
660 670 680 690 700
PLNLARGLEQ AGVPIIGTSV DTIDTAEDRE LFSSLIDELG LRQPPSGIAR
710 720 730 740 750
NMDEARVEAK RIGYPALVRP SFVLGGRAME ICYDHSQFAR YVAEAFIVAD
760 770 780 790 800
GQPVLIDRFL EDATEVDVDA ISDGNDCVIM GIMEHIEEAG VHSGDSACCI
810 820 830 840 850
PPFSLTQPVL AEIRDATRKL AARLNVVGLM NIQFAVKMEG TQPTLYILEV
860 870 880 890 900
NPRASRTVPF VAKATGVPVA NLATKVMAGK TLKELNVTEE PIPRHVSIKE
910 920 930 940 950
SVLPFRKFAG VDIVLGPEMR STGEVMGVSE LFSIAFAKSQ LAAGTVLPES
960 970 980 990 1000
GKIFLSLSAN HKEAAESLGK SLIELGFELL ATEGTAVRLE ANGIAVTRVK
1010 1020 1030 1040 1050
KLSEGHPNLI DYLKNDDVQL ILNTPSGKGA RTDEGKIRAA GVQHGVPCIT
1060 1070 1080
TLAAAEAAVR AMVAMRDTPM EVESLQRRYA QNV
Length:1,083
Mass (Da):118,068
Last modified:October 1, 2003 - 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:i8DBC1CEE1298456A
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
BX294154 Genomic DNA Translation: CAD77400.1

NCBI Reference Sequences

More...
RefSeqi
NP_870325.1, NC_005027.1
WP_011123580.1, NC_005027.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAD77400; CAD77400; RB12113

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1796855

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rba:RB12113

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|243090.15.peg.5853

<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
BX294154 Genomic DNA Translation: CAD77400.1
RefSeqiNP_870325.1, NC_005027.1
WP_011123580.1, NC_005027.1

3D structure databases

SMRiQ7UJ58
ModBaseiSearch...

Protein-protein interaction databases

STRINGi243090.RB12113

Proteomic databases

PRIDEiQ7UJ58

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD77400; CAD77400; RB12113
GeneIDi1796855
KEGGirba:RB12113
PATRICifig|243090.15.peg.5853

Phylogenomic databases

eggNOGiENOG4105CU6 Bacteria
COG0458 LUCA
HOGENOMiHOG000234582
InParanoidiQ7UJ58
KOiK01955
OMAiAVFPFNK
OrthoDBi48855at2

Enzyme and pathway databases

UniPathwayiUPA00068;UER00171
UPA00070;UER00115
BioCyciRBAL243090:RB12113-MONOMER

Family and domain databases

CDDicd01424 MGS_CPS_II, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.40.50.1380, 1 hit
HAMAPiMF_01210_A CPSase_L_chain_A, 1 hit
MF_01210_B CPSase_L_chain_B, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
IPR006275 CarbamoylP_synth_lsu
IPR005480 CarbamoylP_synth_lsu_oligo
IPR036897 CarbamoylP_synth_lsu_oligo_sf
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR005483 CbamoylP_synth_lsu_CPSase_dom
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR033937 MGS_CPS_CarB
IPR016185 PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF02786 CPSase_L_D2, 2 hits
PF02787 CPSase_L_D3, 1 hit
PF02142 MGS, 1 hit
PRINTSiPR00098 CPSASE
SMARTiView protein in SMART
SM01096 CPSase_L_D3, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF48108 SSF48108, 1 hit
SSF52335 SSF52335, 1 hit
SSF52440 SSF52440, 2 hits
TIGRFAMsiTIGR01369 CPSaseII_lrg, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 2 hits
PS00867 CPSASE_2, 2 hits
PS51855 MGS, 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 nameiCARB_RHOBA
<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: Q7UJ58
<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: March 7, 2006
Last sequence update: October 1, 2003
Last modified: May 8, 2019
This is version 108 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 programProkaryotic 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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