Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9UN81 (LORF1_HUMAN)

Entry version 89 (18 Sep 2019)
Sequence version 1 (01 May 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

LINE-1 retrotransposable element ORF1 protein

Gene

L1RE1

Organism
Homo sapiens (Human)
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

Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.5 Publications

Miscellaneous

Long interspersed element-1/LINE-1/L1 retrotransposons are present in more than 500'000 full (6 kb) or truncated copies in the human genome. Most of them are inactive but 80 to 100 of those elements could be transcribed, translated and active in any individual. An active LINE-1 encodes for 2 proteins translated from a single RNA containing 2 non-overlapping ORFs, ORF1 and ORF2. ORF1p is described in this entry as a representative of all ORF1p potentially expressed by active elements. ORF2p is described in the related entry AC O00370.

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

LigandNucleotide-binding

<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:
LINE-1 retrotransposable element ORF1 protein
Short name:
L1ORF1p
Alternative name(s):
LINE retrotransposable element 1
LINE1 retrotransposable element 1
<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:L1RE1
Synonyms:LRE1
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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: Unplaced

Organism-specific databases

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		151626 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9UN81

<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, Nucleus

<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>Mutagenesisi93L → A: Small decrease in localization to stress granules; when associated with A-100 and A-114. 1 Publication1
Mutagenesisi100L → A: Small decrease in localization to stress granules; when associated with A-93 and A-114. 1 Publication1
Mutagenesisi114L → A: Small decrease in localization to stress granules; when associated with A-93 and A-100. 1 Publication1
Mutagenesisi116E → A: Loss of LINE-1 retrotransposition without affecting RNA-binding; when associated with A-123. 1 Publication1
Mutagenesisi123D → A: Loss of LINE-1 retrotransposition without affecting RNA-binding; when associated with A-116. 1 Publication1
Mutagenesisi132G → I: Loss of LINE-1 retrotransposition without affecting RNA-binding; when associated with I-135 and I-142. 1 Publication1
Mutagenesisi133K → S: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with A-137, A-140 and S-141. 1 Publication1
Mutagenesisi135R → I: Loss of LINE-1 retrotransposition without effect on RNA-binding; when associated with I-132 and I-142. 1 Publication1
Mutagenesisi137K → A: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with S-133, A-140 and S-141. 1 Publication1
Mutagenesisi140K → A: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with S-133, A-137 and S-141. 1 Publication1
Mutagenesisi141R → S: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with S-133, A-137 and A-140. 1 Publication1
Mutagenesisi142N → I: Loss of LINE-1 retrotransposition without effect on RNA-binding; when associated with I-132 and I-135. 1 Publication1
Mutagenesisi155R → A: No effect on subcellular localization; when associated with A-157. 1 Publication1
Mutagenesisi157N → A: No effect on subcellular localization; when associated with A-155. Complete loss of localization to stress granules, slightly increased localization to the nucleus; when associated with G-159. 1 Publication1
Mutagenesisi159R → A: Moderately alters RNA-binding activity. 1 Publication1
Mutagenesisi159R → G: Decreased localization to stress granules. Complete loss of localization to stress granules, slightly increased localization to the nucleus; when associated with A-157. 1 Publication1
Mutagenesisi165E → G: No effect on cytoplasmic localization, may increase nucleolar localization. 1 Publication1
Mutagenesisi206R → A: Loss of RNA-binding activity; when associated with A-210 and A-211. 2 Publications1
Mutagenesisi210R → A: Loss of RNA-binding activity; when associated with A-206 and A-211. 2 Publications1
Mutagenesisi211R → A: Loss of RNA-binding activity; when associated with A-206 and A-210. 2 Publications1
Mutagenesisi218I → Y: Moderately alters RNA-binding activity. 2 Publications1
Mutagenesisi220R → A: Loss of LINE-1 retrotransposition without affecting RNA-binding. 2 Publications1
Mutagenesisi235R → A: Loss of LINE-1 retrotransposition with decreased RNA-binding. 2 Publications1
Mutagenesisi261 – 262RR → AA: Small decrease in localization to stress granules. 1 Publication2
Mutagenesisi261R → A: Loss of LINE-1 retrotransposition with decreased RNA-binding. 2 Publications1
Mutagenesisi261R → K: Loss of LINE-1 retrotransposition without affecting RNA-binding. 2 Publications1
Mutagenesisi282Y → A: Loss of LINE-1 retrotransposition without affecting RNA-binding. 1 Publication1

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9UN81

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HGNC:6686

<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_00004250811 – 338LINE-1 retrotransposable element ORF1 proteinAdd BLAST338

<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

Polyubiquitinated, probably by UBR2, which induces its degradation.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9UN81

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9UN81

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9UN81

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9UN81

PeptideAtlas

More...PeptideAtlasi		Q9UN81

PRoteomics IDEntifications database

More...PRIDEi		Q9UN81

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9UN81

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

More...PhosphoSitePlusi		Q9UN81

<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

Homotrimer (via coiled coil domain). May also form larger homooligomers. May interact with DDX39A, HNRNPA1, SERBP1 and YBX1.

Interacts with TEX19 and UBR2 (PubMed:28806172).

Interacts with MOV10 (PubMed:23093941).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-48676N

Protein interaction database and analysis system

More...IntActi		Q9UN81, 20 interactors

<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

1338
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		Q9UN81

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

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>Regioni157 – 252RNA recognition motif (RRM) domainAdd BLAST96
Regioni253 – 317C-terminal domain (CTD)Add BLAST65

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 coili49 – 153Sequence analysisAdd BLAST105

<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 coiled coil domain mediates homotrimerization.
The RRM and the CTD domain are both required for proper RNA-binding activity.

<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 transposase 22 family.Curated

Keywords - Domaini

Coiled coil

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.250.20, 1 hit
3.30.70.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR042566 L1_C
IPR035300 L1_dsRBD
IPR035301 L1_trimer
IPR004244 Transposase_22
IPR042497 Transposase_L1_sf

The PANTHER Classification System

More...PANTHERi		PTHR11505 PTHR11505, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF17490 Tnp_22_dsRBD, 1 hit
PF17489 Tnp_22_trimer, 1 hit
PF02994 Transposase_22, 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.

Q9UN81-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGKKQNRKTG NSKTQSASPP PKERSSSPAT EQSWMENDFD ELREEGFRRS 
        60         70         80         90        100
NYSELREDIQ TKGKEVENFE KNLEECITRI TNTEKCLKEL MELKTKAREL 
       110        120        130        140        150
REECRSLRSR CDQLEERVSA MEDEMNEMKR EGKFREKRIK RNEQSLQEIW 
       160        170        180        190        200
DYVKRPNLRL IGVPESDVEN GTKLENTLQD IIQENFPNLA RQANVQIQEI 
       210        220        230        240        250
QRTPQRYSSR RATPRHIIVR FTKVEMKEKM LRAAREKGRV TLKGKPIRLT 
       260        270        280        290        300
ADLSAETLQA RREWGPIFNI LKEKNFQPRI SYPAKLSFIS EGEIKYFIDK 
       310        320        330 
QMLRDFVTTR PALKELLKEA LNMERNNRYQ PLQNHAKM
Length:338
Mass (Da):40,056
Last modified:May 1, 2000 - 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:iC9ED80C33ED37523
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 conflicti251A → V in AAB59367 (PubMed:10655552).Curated1

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
AF148856 Genomic DNA Translation: AAD39214.1
M80343 Genomic DNA Translation: AAB59367.1

<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
AF148856 Genomic DNA Translation: AAD39214.1
M80343 Genomic DNA Translation: AAB59367.1

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
2LDYNMR-A157-330[»]
2W7AX-ray1.40A/B157-250[»]
2YKOX-ray2.10A/B/C106-330[»]
2YKPX-ray3.10A/B/C106-326[»]
2YKQX-ray3.10A/B/C106-326[»]
6FIAX-ray2.65A/B/C/D/E/F53-152[»]
SMRiQ9UN81
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-48676N
IntActiQ9UN81, 20 interactors

PTM databases

iPTMnetiQ9UN81
PhosphoSitePlusiQ9UN81

Polymorphism and mutation databases

BioMutaiHGNC:6686

Proteomic databases

EPDiQ9UN81
jPOSTiQ9UN81
MassIVEiQ9UN81
MaxQBiQ9UN81
PeptideAtlasiQ9UN81
PRIDEiQ9UN81

Organism-specific databases

MIMi151626 gene
neXtProtiNX_Q9UN81

Miscellaneous databases

PharosiQ9UN81

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Family and domain databases

Gene3Di3.30.250.20, 1 hit
3.30.70.1820, 1 hit
InterProiView protein in InterPro
IPR042566 L1_C
IPR035300 L1_dsRBD
IPR035301 L1_trimer
IPR004244 Transposase_22
IPR042497 Transposase_L1_sf
PANTHERiPTHR11505 PTHR11505, 1 hit
PfamiView protein in Pfam
PF17490 Tnp_22_dsRBD, 1 hit
PF17489 Tnp_22_trimer, 1 hit
PF02994 Transposase_22, 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 nameiLORF1_HUMAN
<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: Q9UN81
Secondary accession number(s): Q15605
<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: January 22, 2014
Last sequence update: May 1, 2000
Last modified: September 18, 2019
This is version 89 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again