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Entry version 136 (11 Dec 2019)
Sequence version 1 (01 Dec 2001)
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Protein

Beclin-1

Gene

Becn1

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

Plays a central role in autophagy. Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. May play a role in antiviral host defense (By similarity).By similarity
Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors.By similarity

Miscellaneous

Expanded poly-Gln tracts inhibit ATXN3-BECN1 interaction, decrease BECN1 levels and impair starvation-induced autophagy (By similarity).By similarity

<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

Biological processAntiviral defense, Apoptosis, Autophagy, Cell cycle, Cell division

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1632852 Macroautophagy
R-RNO-5689880 Ub-specific processing proteases

<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:
Beclin-1
Alternative name(s):
Coiled-coil myosin-like BCL2-interacting protein
Protein GT197
Cleaved into the following 2 chains:
<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:Becn1
<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 10

Organism-specific databases

Rat genome database

More...
RGDi
620190 Becn1

<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, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Mitochondrion, 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>Mutagenesisi178L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-192. 1 Publication1
Mutagenesisi178L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-196. 1 Publication1
Mutagenesisi178L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-259. 1 Publication1
Mutagenesisi189E → L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-217, L-224 and L-255. 1 Publication1
Mutagenesisi192L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-178. 1 Publication1
Mutagenesisi196L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-178. 1 Publication1
Mutagenesisi217A → L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-189, L-224 and L-255. 1 Publication1
Mutagenesisi224E → L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-189, L-217 and L-255. 1 Publication1
Mutagenesisi255A → L: Decreases interaction with ATG14, no effect on interaction with UVRAG; when associated with L-189, L-217 and L-224. 1 Publication1
Mutagenesisi259L → A: Disrupts homodimerization, no effect on interaction with ATG14 and UVRAG; when associated with A-178. 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_00003162901 – 448Beclin-1Add BLAST448
ChainiPRO_0000435044132 – 448Beclin-1-C 37 kDaBy similarityAdd BLAST317
ChainiPRO_0000435045148 – 448Beclin-1-C 35 kDaBy similarityAdd BLAST301

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 residuei29PhosphoserineBy similarity1
Modified residuei88Phosphoserine; by AMPKBy similarity1
Modified residuei91Phosphoserine; by AMPKBy similarity1
Modified residuei94Phosphoserine; by AMPKBy similarity1
Modified residuei117Phosphothreonine; by DAPK1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

<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

Phosphorylation at Thr-117 by DAPK1 reduces its interaction with BCL2 and BCL2L1 and promotes induction of autophagy. In response to autophagic stimuli, phosphorylated at serine residues by AMPK in an ATG14-dependent manner, and this phosphorylation is critical for maximally efficient autophagy.By similarity
Polyubiquitinated by NEDD4, both with 'Lys-11'- and 'Lys-63'-linkages (By similarity). 'Lys-11'-linked polyubiquitination leads to degradation and is enhanced when the stabilizing interaction partner VPS34 is depleted (By similarity). Deubiquitinated by USP10 and USP13, leading to stabilize the PIK3C3/VPS34-containing complexes (By similarity). Polyubiquitinated at Lys-400 with 'Lys-48'-linkages (By similarity). 'Lys-48'-linked polyubiquitination of Lys-400 leads to degradation (By similarity). Deubiquitinated by ATXN3, leading to stabilization (By similarity).By similarity
Proteolytically processed by caspases including CASP8 and CASP3; the C-terminal fragments lack autophagy-inducing capacity and are proposed to induce apoptosis. Thus the cleavage is proposed to be an determinant to switch from autophagy to apoptosis pathways affecting cellular homeostasis including viral infections and survival of tumor cells.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q91XJ1

PRoteomics IDEntifications database

More...
PRIDEi
Q91XJ1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q91XJ1

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

More...
PhosphoSitePlusi
Q91XJ1

<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
ENSRNOG00000020513 Expressed in 10 organ(s), highest expression level in colon

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q91XJ1 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

A homodimeric form is proposed to exist; this metastable form readily transits to ATG14- or UVRAG-containing complexes with BECN1:UVRAG being more stable than BECN1:ATG14 (PubMed:22314358).

Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex the core of which is composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 associating with additional regulatory/auxilliary subunits to form alternative complex forms. Alternative complex forms containing a forth regulatory subunit in a mutually exclusive manner are PI3K complex I (PI3KC3-C1) containing ATG14, and PI3K complex II (PI3KC3-C2) containing UVRAG. PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex. Both, PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory subunits, such as RUBCN, SH3GLB1/Bif-1 and AMBRA1. PI3KC3-C1 probably associates with PIK3CB.

Interacts with AMBRA1, GOPC, GRID2.

Interacts with BCL2 and BCL2L1; the interaction inhibits BECN1 function in promoting autophagy by interfering with the formation of the PI3K complex.

Interacts with cytosolic HMGB1; inhibits the interaction of BECN1 and BCL2 leading to promotion of autophagy.

Interacts with USP10, USP13, DAPK1, RAB39A.

Interacts with SLAMF1 (By similarity).

Interacts with VMP1 (PubMed:17724469).

Interacts with TRIM5; the interaction causes activation of BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (By similarity).

Interacts with active ULK1 (phosphorylated on 'Ser-317') and MEFV simultaneously (By similarity).

Interacts with WDR81 and WDR91; negatively regulates the PI3 kinase/PI3K activity associated with endosomal membranes (By similarity).

Interacts with LAPTM4B; competes with EGFR for LAPTM4B binding; regulates EGFR activity (By similarity).

Interacts with TRIM50 (By similarity).

Interacts with TRIM16 (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
250376, 1 interactor

Database of interacting proteins

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DIPi
DIP-61888N

Protein interaction database and analysis system

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IntActi
Q91XJ1, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000027868

<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

1448
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
Q91XJ1

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>Regioni110 – 157Interaction with BCL2 and BCL2L1 isoform Bcl-X(L)By similarityAdd BLAST48
Regioni243 – 448Evolutionary conserved domain (ECD)By similarityAdd BLAST206
Regioni423 – 448Required for membrane-associationBy similarityAdd BLAST26

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 coili140 – 267Sequence analysisAdd BLAST128

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi106 – 125BH3By similarityAdd BLAST20

<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 C-terminal evolutionary conserved domain (ECD) contains poly-Gln-binding domains such as the ATXN3 poly-Gln motif, consistent with structural docking models revealing two highly scored poly-Gln-binding pockets in the ECD (By similarity). As some binding is observed with BECN1 lacking the ECD, other domains of BECN1 may also interact with ATXN3 (By similarity).By similarity
The coiled coil domain can form antiparallel homodimers and mediates dimerization with the coiled coil domains of ATG14 or UVRAG involved in the formation of PI3K complexes.1 Publication

<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 beclin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2751 Eukaryota
ENOG410XQ85 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000008164

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000158093

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q91XJ1

KEGG Orthology (KO)

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KOi
K08334

Identification of Orthologs from Complete Genome Data

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OMAi
CTEMLVD

Database of Orthologous Groups

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OrthoDBi
1085752at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q91XJ1

TreeFam database of animal gene trees

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TreeFami
TF314282

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.418.40, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007243 Atg6/Beclin
IPR038274 Atg6/Beclin_C_sf
IPR041691 Atg6/beclin_CC
IPR040455 Atg6_BARA
IPR032913 BECN1
IPR029318 BH3_dom

The PANTHER Classification System

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PANTHERi
PTHR12768 PTHR12768, 1 hit
PTHR12768:SF6 PTHR12768:SF6, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF04111 APG6, 1 hit
PF17675 APG6_N, 1 hit
PF15285 BH3, 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.

Q91XJ1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEGSKASSST MQVSFVCQRC SQPLKLDTSF KILDRVTIQE LTAPLLTTAQ
60 70 80 90 100
AKPGESQEEE ANSGEEPFIE TRQDGVSRRF IPPARMMSTE SANSFTLIGE
110 120 130 140 150
ASDGGTMENL SRRLKVTGDL FDIMSGQTDV DHPLCEECTD TLLDQLDTQL
160 170 180 190 200
NVTENECQNY KRCLEMLEQM NEGDSEQLQR ELKELALEEE RLIQELEDVE
210 220 230 240 250
KNRKVVAENL EKVQAEAERL DQEEAQYQRE YSEFKRQQLE LDDELKSVEN
260 270 280 290 300
QMRYAQMQLD KLKKTNVFNA TFHIWHSGQF GTINNFRLGR LPSAPVEWNE
310 320 330 340 350
INAAWGQTVL LLHALANKMG LKFQRYRLVP YGNHSYLESL TDKSKELPLY
360 370 380 390 400
CSGGLRFFWD NKFDHAMVAF LDCVQQFKEE VEKGETRFCL PYRMDVEKGK
410 420 430 440
IEDTGGSGGS YSIKTQFNSE EQWTKALKFM LTNLKWGLAW VSSQFYNK
Length:448
Mass (Da):51,557
Last modified:December 1, 2001 - 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:i34981BE560F3354B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AY033824 mRNA Translation: AAK56548.1
BC074011 mRNA Translation: AAH74011.1

NCBI Reference Sequences

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RefSeqi
NP_001029289.1, NM_001034117.1
NP_446191.1, NM_053739.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000027868; ENSRNOP00000027868; ENSRNOG00000020513
ENSRNOT00000082010; ENSRNOP00000071966; ENSRNOG00000020513

Database of genes from NCBI RefSeq genomes

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GeneIDi
114558

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:114558

UCSC genome browser

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UCSCi
RGD:620190 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
AY033824 mRNA Translation: AAK56548.1
BC074011 mRNA Translation: AAH74011.1
RefSeqiNP_001029289.1, NM_001034117.1
NP_446191.1, NM_053739.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3Q8TX-ray1.90A/B174-264[»]
SMRiQ91XJ1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi250376, 1 interactor
DIPiDIP-61888N
IntActiQ91XJ1, 1 interactor
STRINGi10116.ENSRNOP00000027868

PTM databases

iPTMnetiQ91XJ1
PhosphoSitePlusiQ91XJ1

Proteomic databases

PaxDbiQ91XJ1
PRIDEiQ91XJ1

Genome annotation databases

EnsembliENSRNOT00000027868; ENSRNOP00000027868; ENSRNOG00000020513
ENSRNOT00000082010; ENSRNOP00000071966; ENSRNOG00000020513
GeneIDi114558
KEGGirno:114558
UCSCiRGD:620190 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8678
RGDi620190 Becn1

Phylogenomic databases

eggNOGiKOG2751 Eukaryota
ENOG410XQ85 LUCA
GeneTreeiENSGT00390000008164
HOGENOMiHOG000158093
InParanoidiQ91XJ1
KOiK08334
OMAiCTEMLVD
OrthoDBi1085752at2759
PhylomeDBiQ91XJ1
TreeFamiTF314282

Enzyme and pathway databases

ReactomeiR-RNO-1632852 Macroautophagy
R-RNO-5689880 Ub-specific processing proteases

Miscellaneous databases

Protein Ontology

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PROi
PR:Q91XJ1

Gene expression databases

BgeeiENSRNOG00000020513 Expressed in 10 organ(s), highest expression level in colon
GenevisibleiQ91XJ1 RN

Family and domain databases

Gene3Di1.10.418.40, 1 hit
InterProiView protein in InterPro
IPR007243 Atg6/Beclin
IPR038274 Atg6/Beclin_C_sf
IPR041691 Atg6/beclin_CC
IPR040455 Atg6_BARA
IPR032913 BECN1
IPR029318 BH3_dom
PANTHERiPTHR12768 PTHR12768, 1 hit
PTHR12768:SF6 PTHR12768:SF6, 1 hit
PfamiView protein in Pfam
PF04111 APG6, 1 hit
PF17675 APG6_N, 1 hit
PF15285 BH3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiBECN1_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: Q91XJ1
<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 5, 2008
Last sequence update: December 1, 2001
Last modified: December 11, 2019
This is version 136 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, 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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