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Entry version 141 (16 Oct 2019)
Sequence version 2 (01 Jan 1990)
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Protein

ATPase inhibitor, mitochondrial

Gene

ATP5IF1

Organism
Bos taurus (Bovine)
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

Endogenous F1F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F1F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F1F(o)-ATP synthase enzyme acts as an ATP hydrolase.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei51Participates in pH sensing1
Sitei74Participates in pH sensing1

<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>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:
ATPase inhibitor, mitochondrialCurated
Alternative name(s):
ATP synthase F1 subunit epsilonBy similarity
Inhibitor of F(1)F(o)-ATPase
Short name:
IF(1)
Short name:
IF1
<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:ATP5IF1By similarity
Synonyms:ATPI, ATPIF1
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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 2

<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

<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>Keywords - Cellular componenti

Mitochondrion

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

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>Mutagenesisi46A → V: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi47F → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi49K → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi50R → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi51E → A: No effect on F(1)F(o)-ATP synthase-binding. 2 Publications1
Mutagenesisi51E → A: Retains its inhibitory activity at pH 8.2 although it still form a homotetramer at high pH. 2 Publications1
Mutagenesisi52Q → A: Impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi53A → V: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi54E → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi55E → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi56E → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi57R → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi58Y → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi59F → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi60R → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi62R → A: Impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi64K → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi65E → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi66Q → A: Impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi67L → A: Impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi68A → V: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi69A → V: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi70L → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication1
Mutagenesisi74H → K: Retains its inhibitory activity at pH 8.2 and does not form a homotetramer at high pH. 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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 25Mitochondrion1 PublicationAdd BLAST25
<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_000000254626 – 109ATPase inhibitor, mitochondrialAdd BLAST84

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 residuei103N6-succinyllysineBy similarity1

Proteomic databases

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

More...
PaxDbi
P01096

PRoteomics IDEntifications database

More...
PRIDEi
P01096

<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
ENSBTAG00000006342 Expressed in 9 organ(s), highest expression level in heart

<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; represents the active form and is present at a pH value below 6.5. Homotetramer; represents the inactive form and is present at a pH value above 7.0.

6 Publications

GO - Molecular functioni

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P01096

Database of interacting proteins

More...
DIPi
DIP-46311N

Protein interaction database and analysis system

More...
IntActi
P01096, 5 interactors

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000008319

<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

1109
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
P01096

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
P01096

<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

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>Regioni26 – 52N-terminal inhibitory regionAdd BLAST27
Regioni74 – 106Antiparallel alpha-helical coiled coil regionAdd BLAST33

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili69 – 109Add BLAST41

<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

Forms an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 74-106, leaving each N-terminal inhibitory region (residues 26-62) accessible for interaction with an F1 catalytic domain. The inhibitory N-terminal region (residues 26-62) binds the alpha(ADP-bound)-beta(ADP-bound) (ATP5F1A-ATP5F1B) interface of F1-ATPase, and also contact the central gamma subunit (ATP5F1C). This dimeric state is favored by pH values below 7.0, and at higher values the dimers associate to form inactive homotetramer, where the inhibitory region is occluded, masking its inhibitory activity (PubMed:11742976, PubMed:12923572 and PubMed:17895376).

<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 ATPase inhibitor family.Curated

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410J2TJ Eukaryota
ENOG41127Z5 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000006264

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000247022

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P01096

KEGG Orthology (KO)

More...
KOi
K22255

Identification of Orthologs from Complete Genome Data

More...
OMAi
SHHAKEI

Database of Orthologous Groups

More...
OrthoDBi
1566610at2759

TreeFam database of animal gene trees

More...
TreeFami
TF320659

Family and domain databases

Database of protein disorder

More...
DisProti
DP00844

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007648 ATPase_inhibitor_mt

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04568 IATP, 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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P01096-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAATALAART RQAVWSVWAM QGRGFGSESG DNVRSSAGAV RDAGGAFGKR
60 70 80 90 100
EQAEEERYFR ARAKEQLAAL KKHHENEISH HAKEIERLQK EIERHKQSIK

KLKQSEDDD
Length:109
Mass (Da):12,301
Last modified:January 1, 1990 - 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:i0F8816DECCAABA7E
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 conflicti55E → Q AA sequence (PubMed:6461003).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M22559 mRNA Translation: AAA30396.1
BC111645 mRNA Translation: AAI11646.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C27382 IWBO

NCBI Reference Sequences

More...
RefSeqi
NP_787010.1, NM_175816.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000008319; ENSBTAP00000008319; ENSBTAG00000006342

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
327699

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:327699

<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
M22559 mRNA Translation: AAA30396.1
BC111645 mRNA Translation: AAI11646.1
PIRiC27382 IWBO
RefSeqiNP_787010.1, NM_175816.3

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
1GMJX-ray2.20A/B/C/D26-109[»]
1HF9NMR-A/B69-109[»]
1OHHX-ray2.80H26-109[»]
2V7QX-ray2.10J26-85[»]
4TSFX-ray3.20H/I26-85[»]
4TT3X-ray3.21H/I/J26-85[»]
4Z1MX-ray3.30H/I/J26-85[»]
5LQXelectron microscopy7.90J26-85[»]
5LQYelectron microscopy7.80J26-85[»]
5LQZelectron microscopy7.00J26-85[»]
SMRiP01096
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

CORUMiP01096
DIPiDIP-46311N
IntActiP01096, 5 interactors
STRINGi9913.ENSBTAP00000008319

Proteomic databases

PaxDbiP01096
PRIDEiP01096

Genome annotation databases

EnsembliENSBTAT00000008319; ENSBTAP00000008319; ENSBTAG00000006342
GeneIDi327699
KEGGibta:327699

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
93974

Phylogenomic databases

eggNOGiENOG410J2TJ Eukaryota
ENOG41127Z5 LUCA
GeneTreeiENSGT00390000006264
HOGENOMiHOG000247022
InParanoidiP01096
KOiK22255
OMAiSHHAKEI
OrthoDBi1566610at2759
TreeFamiTF320659

Miscellaneous databases

EvolutionaryTraceiP01096

Gene expression databases

BgeeiENSBTAG00000006342 Expressed in 9 organ(s), highest expression level in heart

Family and domain databases

DisProtiDP00844
InterProiView protein in InterPro
IPR007648 ATPase_inhibitor_mt
PfamiView protein in Pfam
PF04568 IATP, 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 nameiATIF1_BOVIN
<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: P01096
Secondary accession number(s): Q2M2T4
<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: July 21, 1986
Last sequence update: January 1, 1990
Last modified: October 16, 2019
This is version 141 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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