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Entry version 163 (11 Dec 2019)
Sequence version 2 (01 Feb 1996)
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Protein

Choline-phosphate cytidylyltransferase A

Gene

Pcyt1a

Organism
Rattus norvegicus (Rat)
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

Controls phosphatidylcholine synthesis.

Miscellaneous

The cytidylyltransferase may interact with membranes through its amphipathic helix.

<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 <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

By phosphorylation.

<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: phosphatidylcholine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phosphatidylcholine from phosphocholine.2 Publications
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Choline-phosphate cytidylyltransferase A (Pcyt1a), Choline-phosphate cytidylyltransferase B (Pcyt1b)
  2. Choline/ethanolaminephosphotransferase 1 (Cept1), Cholinephosphotransferase 1 (Chpt1)
This subpathway is part of the pathway phosphatidylcholine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylcholine from phosphocholine, the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei122CTPCombined sources1 Publication1
Binding sitei122SubstrateCombined sources1 Publication1
Binding sitei151SubstrateCombined sources1 Publication1
Binding sitei173CTPCombined sources1 Publication1

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 bindingi84 – 92CTPCombined sources1 Publication9
Nucleotide bindingi168 – 169CTPCombined sources1 Publication2
Nucleotide bindingi196 – 200CTPCombined sources1 Publication5

<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 functionNucleotidyltransferase, Transferase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.15 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1483191 Synthesis of PC

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

More...
UniPathwayi
UPA00753;UER00739

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001188

<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:
Choline-phosphate cytidylyltransferase A (EC:2.7.7.152 Publications)
Alternative name(s):
CCT-alpha
CTP:phosphocholine cytidylyltransferase A
Short name:
CCT A
Short name:
CT A
Phosphorylcholine transferase A
<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:Pcyt1a
Synonyms:Ctpct, Pcyt1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 11

Organism-specific databases

Rat genome database

More...
RGDi
70515 Pcyt1a

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

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

Keywords - Cellular componenti

Cytoplasm, Membrane

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi122K → A: Nearly abolishes enzyme activity. Decreases affinity for phosphocholine about 500-fold. 1 Publication1
Mutagenesisi122K → R: Nearly abolishes enzyme activity. Decreases affinity for phosphocholine about 80-fold. 1 Publication1
Mutagenesisi168H → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi173Y → A: Reduced catalytic activity. Reduces affinity for phosphocholine. 1 Publication1

<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_00002084551 – 367Choline-phosphate cytidylyltransferase AAdd BLAST367

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-acetylmethionineBy similarity1
Modified residuei8N6-acetyllysineBy similarity1
Modified residuei233PhosphoserineBy similarity1
Modified residuei315Phosphoserine; by PKC1 Publication1
Modified residuei319PhosphoserineCombined sources1 Publication1
Modified residuei321Phosphoserine1 Publication1
Modified residuei322Phosphoserine1 Publication1
Modified residuei323Phosphoserine1 Publication1
Modified residuei325PhosphothreonineBy similarity1
Modified residuei329Phosphoserine1 Publication1
Modified residuei331PhosphoserineCombined sources1 Publication1
Modified residuei333Phosphoserine; by PKC1 Publication1
Modified residuei342PhosphothreonineCombined sources1
Modified residuei343Phosphoserine1 Publication1
Modified residuei345Phosphoserine1 Publication1
Modified residuei346Phosphoserine1 Publication1
Modified residuei347PhosphoserineCombined sources1 Publication1
Modified residuei350Phosphoserine1 Publication1
Modified residuei352Phosphoserine1 Publication1
Modified residuei358PhosphothreonineBy similarity1
Modified residuei362Phosphoserine; by CK2Combined sources1 Publication1

<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 serine residues of the C-terminus are phosphorylated. The inactive soluble form is stabilized by phosphorylation, the active membrane bound form is promoted by anionic lipids or diacylglycerol, and is stabilized by dephosphorylation.1 Publication
The N-terminus is blocked.
Monoubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P19836

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

More...
PaxDbi
P19836

PRoteomics IDEntifications database

More...
PRIDEi
P19836

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P19836

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

More...
PhosphoSitePlusi
P19836

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000001762 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P19836 RN

<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

Homodimer.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000002403

<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

1367
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
P19836

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
P19836

<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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati319 – 32416
Repeati329 – 3332; approximate5
Repeati343 – 34836

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>Regioni228 – 287AmphipathicSequence analysisAdd BLAST60
Regioni256 – 2883 X 11 AA approximate tandem repeatsAdd BLAST33
Regioni298 – 315AmphipathicSequence analysisAdd BLAST18
Regioni319 – 3483 X repeatsAdd BLAST30

<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 cytidylyltransferase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2804 Eukaryota
COG0615 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157384

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230945

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P19836

KEGG Orthology (KO)

More...
KOi
K00968

Identification of Orthologs from Complete Genome Data

More...
OMAi
FWNESKG

Database of Orthologous Groups

More...
OrthoDBi
1172502at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P19836

TreeFam database of animal gene trees

More...
TreeFami
TF106336

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02174 CCT, 1 hit

Database of protein disorder

More...
DisProti
DP02118

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.620, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR041723 CCT
IPR004821 Cyt_trans-like
IPR014729 Rossmann-like_a/b/a_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01467 CTP_transf_like, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00125 cyt_tran_rel, 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.

P19836-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDAQSSAKVN SRKRRKEVPG PNGATEEDGI PSKVQRCAVG LRQPAPFSDE
60 70 80 90 100
IEVDFSKPYV RVTMEEACRG TPCERPVRVY ADGIFDLFHS GHARALMQAK
110 120 130 140 150
NLFPNTYLIV GVCSDELTHN FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP
160 170 180 190 200
WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD VYKHIKEAGM FAPTQRTEGI
210 220 230 240 250
STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY HLQERVDKVK
260 270 280 290 300
KKVKDVEEKS KEFVQKVEEK SIDLIQKWEE KSREFIGSFL EMFGPEGALK
310 320 330 340 350
HMLKEGKGRM LQAISPKQSP SSSPTHERSP SPSFRWPFSG KTSPSSSPAS
360
LSRCKAVTCD ISEDEED
Length:367
Mass (Da):41,681
Last modified:February 1, 1996 - v2
<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:i44DFFFC0F1608969
GO

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 conflicti91G → S in AAA40995 (PubMed:2166941).Curated1
Sequence conflicti114S → C in AAA40995 (PubMed:2166941).Curated1
Sequence conflicti116 – 117EL → DV in AAB60489 (Ref. 2) Curated2

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
M36071 mRNA Translation: AAA40995.1
U03490 mRNA Translation: AAB60489.1
L13245 mRNA Translation: AAB59683.1
BC085713 mRNA Translation: AAH85713.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A36001

NCBI Reference Sequences

More...
RefSeqi
NP_511177.2, NM_078622.2
XP_006248506.1, XM_006248444.3
XP_008766916.1, XM_008768694.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000002403; ENSRNOP00000002403; ENSRNOG00000001762

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
140544

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:140544

UCSC genome browser

More...
UCSCi
RGD:70515 rat

<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
M36071 mRNA Translation: AAA40995.1
U03490 mRNA Translation: AAB60489.1
L13245 mRNA Translation: AAB59683.1
BC085713 mRNA Translation: AAH85713.1
PIRiA36001
RefSeqiNP_511177.2, NM_078622.2
XP_006248506.1, XM_006248444.3
XP_008766916.1, XM_008768694.2

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
1PEHNMR-A236-268[»]
1PEINMR-A267-288[»]
3HL4X-ray2.20A/B1-236[»]
4MVCX-ray3.00A/B1-312[»]
4MVDX-ray8.00A/B/C/D/E/F/G/H1-312[»]
SMRiP19836
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002403

Chemistry databases

SwissLipidsiSLP:000001188

PTM databases

iPTMnetiP19836
PhosphoSitePlusiP19836

Proteomic databases

jPOSTiP19836
PaxDbiP19836
PRIDEiP19836

Genome annotation databases

EnsembliENSRNOT00000002403; ENSRNOP00000002403; ENSRNOG00000001762
GeneIDi140544
KEGGirno:140544
UCSCiRGD:70515 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5130
RGDi70515 Pcyt1a

Phylogenomic databases

eggNOGiKOG2804 Eukaryota
COG0615 LUCA
GeneTreeiENSGT00940000157384
HOGENOMiHOG000230945
InParanoidiP19836
KOiK00968
OMAiFWNESKG
OrthoDBi1172502at2759
PhylomeDBiP19836
TreeFamiTF106336

Enzyme and pathway databases

UniPathwayiUPA00753;UER00739
BRENDAi2.7.7.15 5301
ReactomeiR-RNO-1483191 Synthesis of PC

Miscellaneous databases

EvolutionaryTraceiP19836

Protein Ontology

More...
PROi
PR:P19836

Gene expression databases

BgeeiENSRNOG00000001762 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
GenevisibleiP19836 RN

Family and domain databases

CDDicd02174 CCT, 1 hit
DisProtiDP02118
Gene3Di3.40.50.620, 1 hit
InterProiView protein in InterPro
IPR041723 CCT
IPR004821 Cyt_trans-like
IPR014729 Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF01467 CTP_transf_like, 1 hit
TIGRFAMsiTIGR00125 cyt_tran_rel, 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 nameiPCY1A_RAT
<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: P19836
<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: February 1, 1991
Last sequence update: February 1, 1996
Last modified: December 11, 2019
This is version 163 of the entry and version 2 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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