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Entry version 132 (02 Dec 2020)
Sequence version 1 (01 Dec 2001)
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Protein

AN1-type zinc finger protein 2B

Gene

Zfand2b

Organism
Mus musculus (Mouse)
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 role in protein homeostasis by regulating both the translocation and the ubiquitin-mediated proteasomal degradation of nascent proteins at the endoplasmic reticulum (PubMed:24160817, PubMed:26337389, PubMed:26692333). It is involved in the regulation of signal-mediated translocation of proteins into the endoplasmic reticulum (PubMed:24160817). It also plays a role in the ubiquitin-mediated proteasomal degradation of proteins for which signal-mediated translocation to the endoplasmic reticulum has failed (PubMed:18467495, PubMed:26337389). May therefore function in the endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:24160817, PubMed:26337389). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333).4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri7 – 52AN1-type 1PROSITE-ProRule annotationAdd BLAST46
Zinc fingeri97 – 145AN1-type 2PROSITE-ProRule annotationAdd BLAST49

<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

LigandMetal-binding, Zinc

<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%5Fand%5Ftaxonomy%5Fsection">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:
AN1-type zinc finger protein 2BCurated
Alternative name(s):
Arsenite-inducible RNA-associated protein-like protein1 Publication
Short name:
AIRAP-like protein1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Zfand2bImported
Synonyms:Airapl1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 1

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1916068, Zfand2b

<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

Endoplasmic reticulum, 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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Knockout mice undergo premature death due to the occurrence of myelo-proliferative neoplasms. The absence of Zfand2b plays a driver role in the development of these neoplasms by hyperactivating the insulin-like growth factor receptor signaling pathway. This is due to increased expression, in particular at the cell surface, of the IGF1R receptor.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi163S → A: No effect on association with the proteasome complex; when associated with A-173 and A-187. 1 Publication1
Mutagenesisi163S → D: No effect on association with the proteasome complex; when associated with D-173 and D-187. 1 Publication1
Mutagenesisi173S → A: No effect on association with the proteasome complex; when associated with A-163 and A-187. 1 Publication1
Mutagenesisi173S → D: No effect on association with the proteasome complex; when associated with D-163 and D-187. 1 Publication1
Mutagenesisi187S → A: No effect on association with the proteasome complex; when associated with A-163 and A-173. 1 Publication1
Mutagenesisi187S → D: No effect on association with the proteasome complex; when associated with D-163 and D-173. 1 Publication1
Mutagenesisi201A → Q: Loss of interaction with ubiquitin polymers and ubiquitinated proteins, loss of interaction with BAG6 and no effect on association with the proteasome complex; when associated with Q-229 and Q-231. 2 Publications1
Mutagenesisi202L → A: Decreased 'Lys-48'-linked polyubiquitin binding. 1 Publication1
Mutagenesisi205A → Q: Decreased 'Lys-48'-linked polyubiquitin binding. Loss of 'Lys-48'-linked polyubiquitin binding, loss of interaction with BAG6 and loss of association with the proteasome complex; when associated with Q-229 and Q-231. 1 Publication1
Mutagenesisi206L → A: Decreased 'Lys-48'-linked polyubiquitin binding. 1 Publication1
Mutagenesisi213 – 220AKPQVLSS → QQQQQQQQ: No effect on 'Lys-48'-linked polyubiquitin binding. 1 Publication8
Mutagenesisi214K → A or G: No effect on 'Lys-48'-linked polyubiquitin binding. 1 Publication1
Mutagenesisi215P → A or G: No effect on 'Lys-48'-linked polyubiquitin binding. 1 Publication1
Mutagenesisi215Missing : No effect on 'Lys-48'-linked polyubiquitin binding. 1 Publication1
Mutagenesisi218L → A: No effect on 'Lys-48'-linked polyubiquitin binding. 1 Publication1
Mutagenesisi226L → A: No effect on 'Lys-48'-linked polyubiquitin binding. 1 Publication1
Mutagenesisi227A → Q: Decreased 'Lys-48'-linked polyubiquitin binding; when associated with A-230. 1 Publication1
Mutagenesisi228L → A: Decreased 'Lys-48'-linked polyubiquitin binding. Loss of interaction with BAG6. Decreased association with the proteasome complex. 1 Publication1
Mutagenesisi229A → Q: Decreased 'Lys-48'-linked polyubiquitin binding. Loss of interaction with ubiquitin polymers and ubiquitinated proteins, loss of interaction with BAG6 and no effect on association with the proteasome complex; when associated with Q-201 and Q-231. Loss of 'Lys-48'-linked polyubiquitin binding, loss of interaction with BAG6 and loss of association with the proteasome complex; when associated with Q-205 and Q-231. 3 Publications1
Mutagenesisi230Q → A: Decreased 'Lys-48'-linked polyubiquitin binding; when associated with Q-227. 1 Publication1
Mutagenesisi231A → Q: Decreased 'Lys-48'-linked polyubiquitin binding. Loss of interaction with ubiquitin polymers and ubiquitinated proteins, loss of interaction with BAG6 and no effect on association with the proteasome complex; when associated with Q-201 and Q-229. Loss of 'Lys-48'-linked polyubiquitin binding, loss of interaction with BAG6 and loss of association with the proteasome complex; when associated with Q-205 and Q-229. 3 Publications1
Mutagenesisi233S → G: Decreased 'Lys-48'-linked polyubiquitin binding. 1 Publication1
Mutagenesisi254C → S: Loss of localization to the endoplasmic reticulum membrane. Loss of interaction with BAG6. No effect on association with the proteasome complex. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002328771 – 254AN1-type zinc finger protein 2BAdd BLAST254
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000444336255 – 257Removed in mature form1 Publication3

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 residuei163Phosphoserine; by MAPK141 Publication1
Modified residuei173Phosphoserine; by MAPK141 Publication1
Modified residuei187Phosphoserine; by MAPK141 Publication1
Modified residuei254Cysteine methyl ester1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi254S-geranylgeranyl cysteine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylated by MAPK14 (Probable). Phosphorylation has no effect on association with the proteasome complex (Probable).1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q91X58

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q91X58

MaxQB - The MaxQuant DataBase

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MaxQBi
Q91X58

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

More...
PaxDbi
Q91X58

PRoteomics IDEntifications database

More...
PRIDEi
Q91X58

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q91X58

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

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PhosphoSitePlusi
Q91X58

<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

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Bgeei
ENSMUSG00000026197, Expressed in granulocyte and 267 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q91X58, MM

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds 'Lys-48'-linked polyubiquitin chains of ubiquitinated proteins (PubMed:18467495, PubMed:24160817, PubMed:26876100). Associates with the proteasome complex; upon exposure to arsenite (PubMed:18467495, PubMed:26876100).

Interacts (via VIM motif) with VCP; the interaction is direct (PubMed:24160817, PubMed:26337389).

Interacts with BAG6 (PubMed:24160817, PubMed:26337389, PubMed:26876100).

Interacts with IGF1R (nascent precursor form) (PubMed:26692333).

Interacts with DERL1, FAF2, NPLOC4 and UFD1; probably through VCP (PubMed:24160817).

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
213068, 26 interactors

Database of interacting proteins

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DIPi
DIP-46091N

Protein interaction database and analysis system

More...
IntActi
Q91X58, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000027394

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q91X58, protein

<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

1257
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

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SMRi
Q91X58

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini197 – 216UIM 1PROSITE-ProRule annotationAdd BLAST20
Domaini221 – 240UIM 2PROSITE-ProRule annotationAdd BLAST20

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>Regioni141 – 151VCP/p97-interacting motif (VIM)1 PublicationAdd BLAST11

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>Motifi254 – 257CAAX motif1 Publication4

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 biasi170 – 175Poly-Ser6

<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 UIM domains specifically bind 'Lys-48'-linked ubiquitin polymers (PubMed:18467495, PubMed:26876100). The UIM domains mediate interaction with polyubiquitinated proteins (PubMed:18467495, PubMed:26337389).3 Publications

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri7 – 52AN1-type 1PROSITE-ProRule annotationAdd BLAST46
Zinc fingeri97 – 145AN1-type 2PROSITE-ProRule annotationAdd BLAST49

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3183, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000159648

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q91X58

Database of Orthologous Groups

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OrthoDBi
1422113at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q91X58

TreeFam database of animal gene trees

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TreeFami
TF314219

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.1110.10, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR035896, AN1-like_Znf
IPR003903, UIM_dom
IPR000058, Znf_AN1

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01428, zf-AN1, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00726, UIM, 2 hits
SM00154, ZnF_AN1, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF118310, SSF118310, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50330, UIM, 1 hit
PS51039, ZF_AN1, 2 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%5Flength">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q91X58-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEFPDLGAHC SEPSCQRLDF LPLKCDACSG IFCADHVAYA QHHCGSAYQK
60 70 80 90 100
DIQVPVCPLC NVPVPVARGE PPDRAVGEHI DRDCRSDPAQ QKRKIFTNKC
110 120 130 140 150
ERSGCRQREM MKLTCDRCGR NFCIKHRHPL DHECSGEGHQ TSRAGLAAIS
160 170 180 190 200
RAQGLASTST APSPSRTLPS SSSPSRATPQ LPTRTASPVI ALQNGLSEDE
210 220 230 240 250
ALQRALELSL AEAKPQVLSS QEEDDLALAQ ALSASEAEYQ QQQAQSRSLK

PSNCSLC
Length:257
Mass (Da):27,895
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:iD9B35C96BB3876E2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WPF5A0A087WPF5_MOUSE
AN1-type zinc finger protein 2B
Zfand2b
255Annotation score:

Annotation score:1 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>
E0CY18E0CY18_MOUSE
AN1-type zinc finger protein 2B
Zfand2b
218Annotation score:

Annotation score:1 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 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 conflicti174P → S in BAB23266 (PubMed:16141072).Curated1

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
AK004332 mRNA Translation: BAB23266.1
AK151430 mRNA Translation: BAE30394.1
BC011495 mRNA Translation: AAH11495.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS15064.1

NCBI Reference Sequences

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RefSeqi
NP_001153377.1, NM_001159905.1
NP_001153378.1, NM_001159906.1
NP_081122.2, NM_026846.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000027394; ENSMUSP00000027394; ENSMUSG00000026197
ENSMUST00000160439; ENSMUSP00000125086; ENSMUSG00000026197

Database of genes from NCBI RefSeq genomes

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GeneIDi
68818

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:68818

UCSC genome browser

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UCSCi
uc007bnw.2, mouse

<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
AK004332 mRNA Translation: BAB23266.1
AK151430 mRNA Translation: BAE30394.1
BC011495 mRNA Translation: AAH11495.1
CCDSiCCDS15064.1
RefSeqiNP_001153377.1, NM_001159905.1
NP_001153378.1, NM_001159906.1
NP_081122.2, NM_026846.3

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
4XKHX-ray3.00C/E/H187-240[»]
SMRiQ91X58
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi213068, 26 interactors
DIPiDIP-46091N
IntActiQ91X58, 2 interactors
STRINGi10090.ENSMUSP00000027394

PTM databases

iPTMnetiQ91X58
PhosphoSitePlusiQ91X58

Proteomic databases

EPDiQ91X58
jPOSTiQ91X58
MaxQBiQ91X58
PaxDbiQ91X58
PRIDEiQ91X58

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
51845, 180 antibodies

Genome annotation databases

EnsembliENSMUST00000027394; ENSMUSP00000027394; ENSMUSG00000026197
ENSMUST00000160439; ENSMUSP00000125086; ENSMUSG00000026197
GeneIDi68818
KEGGimmu:68818
UCSCiuc007bnw.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
130617
MGIiMGI:1916068, Zfand2b

Phylogenomic databases

eggNOGiKOG3183, Eukaryota
GeneTreeiENSGT00940000159648
InParanoidiQ91X58
OrthoDBi1422113at2759
PhylomeDBiQ91X58
TreeFamiTF314219

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
68818, 0 hits in 17 CRISPR screens

Protein Ontology

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PROi
PR:Q91X58
RNActiQ91X58, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000026197, Expressed in granulocyte and 267 other tissues
GenevisibleiQ91X58, MM

Family and domain databases

Gene3Di4.10.1110.10, 2 hits
InterProiView protein in InterPro
IPR035896, AN1-like_Znf
IPR003903, UIM_dom
IPR000058, Znf_AN1
PfamiView protein in Pfam
PF01428, zf-AN1, 2 hits
SMARTiView protein in SMART
SM00726, UIM, 2 hits
SM00154, ZnF_AN1, 2 hits
SUPFAMiSSF118310, SSF118310, 2 hits
PROSITEiView protein in PROSITE
PS50330, UIM, 1 hit
PS51039, ZF_AN1, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiZFN2B_MOUSE
<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: Q91X58
Secondary accession number(s): Q9D0W4
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: December 1, 2001
Last modified: December 2, 2020
This is version 132 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
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