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Protein

Calpain small subunit 1

Gene

CAPNS1

Organism
Sus scrofa (Pig)
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>
-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

Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi107Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi110Calcium 1By similarity1
Metal bindingi112Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi117Calcium 1By similarity1
Metal bindingi135Calcium 4By similarity1
Metal bindingi150Calcium 2By similarity1
Metal bindingi152Calcium 2By similarity1
Metal bindingi154Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi156Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi161Calcium 2By similarity1
Metal bindingi180Calcium 3By similarity1
Metal bindingi182Calcium 3By similarity1
Metal bindingi184Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi186Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi191Calcium 3By similarity1
Metal bindingi223Calcium 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi106 – 1171By similarityAdd BLAST12
Calcium bindingi150 – 1612By similarityAdd BLAST12
Calcium bindingi180 – 1913By similarityAdd BLAST12

<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

LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.22.B24 6170

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SSC-1474228 Degradation of the extracellular matrix

<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:
Calpain small subunit 1
Short name:
CSS1
Alternative name(s):
Calcium-activated neutral proteinase small subunit
Short name:
CANP small subunit
Calcium-dependent protease small subunit
Short name:
CDPS
Calcium-dependent protease small subunit 1
Calpain regulatory subunit
<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:CAPNS1
Synonyms:CAPN4
<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>OrganismiSus scrofa (Pig)
<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 identifieri9823 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
<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
  • UP000008227 <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 6

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, 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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2205

<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_00000737151 – 266Calpain small subunit 1Add BLAST266

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 residuei6PhosphoserineBy similarity1
Modified residuei177N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P04574

PeptideAtlas

More...
PeptideAtlasi
P04574

PRoteomics IDEntifications database

More...
PRIDEi
P04574

<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
ENSSSCG00000030149 Expressed in 6 organ(s), highest expression level in lung

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P04574 SS

<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 or heterodimer of a large (catalytic) and a small (regulatory) subunit. In presence of calcium, the heterodimer dissociates.1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P04574, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9823.ENSSSCP00000025968

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P04574

<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

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1ALVX-ray1.90A/B94-266[»]
1ALWX-ray2.03A/B94-266[»]
1NX0X-ray2.30A/B94-266[»]
1NX1X-ray2.00A/B94-266[»]
1NX2X-ray2.20A94-266[»]
1NX3X-ray2.45A94-266[»]
4PHNX-ray1.79A/B94-266[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P04574

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

More...
SMRi
P04574

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P04574

<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>Domaini94 – 128EF-hand 1; atypicalPROSITE-ProRule annotationAdd BLAST35
Domaini137 – 170EF-hand 2PROSITE-ProRule annotationAdd BLAST34
Domaini167 – 202EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini203 – 231EF-hand 4PROSITE-ProRule annotationAdd BLAST29
Domaini232 – 266EF-hand 5PROSITE-ProRule annotationAdd BLAST35

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 67Gly-rich (hydrophobic)Add BLAST67
Compositional biasi10 – 26Poly-GlyAdd BLAST17
Compositional biasi35 – 54Poly-GlyAdd BLAST20
Compositional biasi76 – 81Poly-Pro6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The contact of the 5th EF-hand domain from each monomer allows the formation of the homodimer and also appears to mediate the contact between the large catalytic subunit and small regulatory subunit for the formation of the heterodimer.
EF-hand domains are paired. EF-hand 1 is paired with EF-hand 2 and EF-hand 3 is paired with EF-hand 4. The fifth EF-hand domain, left unpaired, does not bind the calcium but is responsible of the dimerization by EF-embrace. The first four EF-hand domains bind calcium, however it is not sure if the binding of EF-hand 4 to calcium is physiologically relevant.

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0037 Eukaryota
ENOG410YKQK LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155478

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004492

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P04574

KEGG Orthology (KO)

More...
KOi
K08583

Identification of Orthologs from Complete Genome Data

More...
OMAi
SDEGGNM

Database of Orthologous Groups

More...
OrthoDBi
1330600at2759

TreeFam database of animal gene trees

More...
TreeFami
TF314682

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029642 CAPN4
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom

The PANTHER Classification System

More...
PANTHERi
PTHR44408:SF3 PTHR44408:SF3, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13833 EF-hand_8, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47473 SSF47473, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 3 hits

<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>.<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.

P04574-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFLVNSFLKG GGGGGGGGGG LGGGLGNVLG GLISGAGGGG GGGGGGGGGG
60 70 80 90 100
GGGGTAMRIL GGVISAISEA AAQYNPEPPP PRTHYSNIEA NESEEVRQFR
110 120 130 140 150
RLFAQLAGDD MEVSATELMN ILNKVVTRHP DLKTDGFGID TCRSMVAVMD
160 170 180 190 200
SDTTGKLGFE EFKYLWNNIK KWQAIYKQFD VDRSGTIGSS ELPGAFEAAG
210 220 230 240 250
FHLNEHLYSM IIRRYSDEGG NMDFDNFISC LVRLDAMFRA FKSLDKDGTG
260
QIQVNIQEWL QLTMYS
Length:266
Mass (Da):28,068
Last modified:August 13, 1987 - 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:i3FA81023EDC4141A
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
M11778 mRNA Translation: AAA31010.1
M11779 mRNA Translation: AAA31011.1
AJ410870 Genomic DNA Translation: CAC85483.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A25166 CIPGL
S39392

NCBI Reference Sequences

More...
RefSeqi
NP_999483.1, NM_214318.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Ssc.54048

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSSSCT00000031590; ENSSSCP00000025968; ENSSSCG00000030149

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
397587

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:397587

<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
M11778 mRNA Translation: AAA31010.1
M11779 mRNA Translation: AAA31011.1
AJ410870 Genomic DNA Translation: CAC85483.2
PIRiA25166 CIPGL
S39392
RefSeqiNP_999483.1, NM_214318.2
UniGeneiSsc.54048

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ALVX-ray1.90A/B94-266[»]
1ALWX-ray2.03A/B94-266[»]
1NX0X-ray2.30A/B94-266[»]
1NX1X-ray2.00A/B94-266[»]
1NX2X-ray2.20A94-266[»]
1NX3X-ray2.45A94-266[»]
4PHNX-ray1.79A/B94-266[»]
ProteinModelPortaliP04574
SMRiP04574
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04574, 1 interactor
STRINGi9823.ENSSSCP00000025968

Chemistry databases

BindingDBiP04574
ChEMBLiCHEMBL2205

Proteomic databases

PaxDbiP04574
PeptideAtlasiP04574
PRIDEiP04574

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000031590; ENSSSCP00000025968; ENSSSCG00000030149
GeneIDi397587
KEGGissc:397587

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
826

Phylogenomic databases

eggNOGiKOG0037 Eukaryota
ENOG410YKQK LUCA
GeneTreeiENSGT00940000155478
HOVERGENiHBG004492
InParanoidiP04574
KOiK08583
OMAiSDEGGNM
OrthoDBi1330600at2759
TreeFamiTF314682

Enzyme and pathway databases

BRENDAi3.4.22.B24 6170
ReactomeiR-SSC-1474228 Degradation of the extracellular matrix

Miscellaneous databases

EvolutionaryTraceiP04574

Gene expression databases

BgeeiENSSSCG00000030149 Expressed in 6 organ(s), highest expression level in lung
GenevisibleiP04574 SS

Family and domain databases

InterProiView protein in InterPro
IPR029642 CAPN4
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
PANTHERiPTHR44408:SF3 PTHR44408:SF3, 1 hit
PfamiView protein in Pfam
PF13833 EF-hand_8, 1 hit
SUPFAMiSSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiCPNS1_PIG
<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: P04574
Secondary accession number(s): Q8SPJ8
<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: August 13, 1987
Last sequence update: August 13, 1987
Last modified: January 16, 2019
This is version 145 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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