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Entry version 148 (22 Apr 2020)
Sequence version 2 (20 Dec 2005)
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Protein

BRISC complex subunit Abraxas 2

Gene

ABRAXAS2

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

Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates (PubMed:19214193, PubMed:20032457, PubMed:20656690, PubMed:24075985). May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (PubMed:20656690). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression (PubMed:24075985, PubMed:26344097). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). Required for normal induction of p53/TP53 in response to DNA damage (PubMed:25283148). Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage (PubMed:25283148).By similarity5 Publications

Caution

Although strongly related to the ABRAXAS1 protein, lacks the C-terminal pSXXF that constitutes a specific recognition motif for the BRCT domain of BRCA1.Curated

<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 processCell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5689901 Metalloprotease DUBs

<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:
BRISC complex subunit Abraxas 2Imported
Alternative name(s):
Abraxas brother protein 11 Publication
Protein FAM175B
<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:ABRAXAS2Imported
Synonyms:ABRO11 Publication, FAM175BImported, KIAA01571 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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 10

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:28975 ABRAXAS2

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q15018

<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, Cytoskeleton, Microtubule, 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%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>Mutagenesisi11 – 12SA → RR: Slighly reduces interaction with BBRC36. Abolishes interaction with SHMT2. Strongly reduces interactions with BABAM2 and BABAM1. 1 Publication2
Mutagenesisi215 – 222Missing : Reduces interaction with SHMT2, but has no effect on interaction with BRCC3. 1 Publication8
Mutagenesisi220V → R: Strongly reduces interaction with BBRC3; SHMT2; BABAM2 and BABAM1; when associated with Y-231. Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BABAM2 and BABAM1; when associated with Y-231 and Y-241. 1 Publication1
Mutagenesisi231E → Y: Strongly reduces interaction with BBRC3; SHMT2; BABAM2 and BABAM1; when associated with R-220. Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BABAM2 and BABAM1; when associated with R-220 and Y-241. 1 Publication1
Mutagenesisi241V → R: Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BABAM2 and BABAM1; when associated with R-220 and Y-231. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
23172

Open Targets

More...
OpenTargetsi
ENSG00000165660

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA162387331

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q15018 Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ABRAXAS2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
84029317

<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_00000507251 – 415BRISC complex subunit Abraxas 2Add BLAST415

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 residuei274PhosphoserineCombined sources1
Modified residuei280PhosphoserineCombined sources1
Modified residuei368PhosphoserineCombined sources1
Modified residuei372PhosphoserineCombined sources1
Modified residuei375PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q15018

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q15018

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q15018

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q15018

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

More...
PaxDbi
Q15018

PeptideAtlas

More...
PeptideAtlasi
Q15018

PRoteomics IDEntifications database

More...
PRIDEi
Q15018

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
60367

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q15018

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

More...
PhosphoSitePlusi
Q15018

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in heart muscle (at protein level). Detected in heart and muscle, and at much lower levels in brain (PubMed:21195082).1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in response to DNA damage (PubMed:25283148). Up-regulated in myocardial infarction area (at protein level) (PubMed:21195082).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000165660 Expressed in secondary oocyte and 216 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q15018 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000165660 Low tissue specificity

<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

Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (PubMed:19214193, PubMed:20032457, PubMed:21282113, PubMed:24075985, PubMed:25283148, PubMed:26344097, PubMed:26195665).

Interacts with BRCC3/BRCC36; the interaction is direct (PubMed:20032457, PubMed:20656690, PubMed:26344097).

Interacts with BABAM1 (PubMed:21282113). Does not interact with BRCA1 (PubMed:17525340, PubMed:21282113).

Interacts with SHMT1 and SHMT2; the interaction is direct.

Identified in a complex with SHMT2 and the other subunits of the BRISC complex (PubMed:24075985). The BRISC complex binds monoubiquitin and both 'Lys-48'- and 'Lys-63'-linked polyubiquitin (PubMed:20032457). Identified in complexes with IFNAR1, IFNAR2 and SHMT2 (PubMed:24075985).

Interacts with THAP5 (PubMed:21195082).

Interacts with ATF4 (PubMed:22974638).

Identified in a complex with p53/TP53 and USP7; interacts directly with both proteins (PubMed:25283148).

Interacts with NUMA1 (PubMed:26195665).

Interacts with microtubule minus ends (PubMed:26195665). Binds polyubiquitin (PubMed:19261749).

12 Publications

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

More...
BioGridi
116784, 51 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q15018

Protein interaction database and analysis system

More...
IntActi
Q15018, 61 interactors

Molecular INTeraction database

More...
MINTi
Q15018

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000298492

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q15018

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q15018 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

3D structure databases

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

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SMRi
Q15018

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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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>Domaini3 – 149MPNPROSITE-ProRule annotationAdd BLAST147

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>Regioni215 – 222Important for interaction with SHMT21 Publication8
Regioni220 – 241Important for interaction with BBRC36 and other subunits of the BRISC complex1 PublicationAdd BLAST22

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 coili215 – 266Sequence analysisAdd BLAST52

<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 FAM175 family. Abro1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IPEG Eukaryota
ENOG410ZUYJ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00530000063424

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_040659_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q15018

KEGG Orthology (KO)

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KOi
K20799

Identification of Orthologs from Complete Genome Data

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OMAi
SRYNQRI

Database of Orthologous Groups

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OrthoDBi
954711at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q15018

TreeFam database of animal gene trees

More...
TreeFami
TF331751

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR023238 FAM175
IPR023240 FAM175_BRISC_cplx_Abro1_su
IPR037518 MPN

The PANTHER Classification System

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PANTHERi
PTHR31728 PTHR31728, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR02053 BRISCABRO1
PR02051 PROTEINF175

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50249 MPN, 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%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>Sequencei

<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.

Q15018-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAASISGYTF SAVCFHSANS NADHEGFLLG EVRQEETFSI SDSQISNTEF
60 70 80 90 100
LQVIEIHNHQ PCSKLFSFYD YASKVNEESL DRILKDRRKK VIGWYRFRRN
110 120 130 140 150
TQQQMSYREQ VLHKQLTRIL GVPDLVFLLF SFISTANNST HALEYVLFRP
160 170 180 190 200
NRRYNQRISL AIPNLGNTSQ QEYKVSSVPN TSQSYAKVIK EHGTDFFDKD
210 220 230 240 250
GVMKDIRAIY QVYNALQEKV QAVCADVEKS ERVVESCQAE VNKLRRQITQ
260 270 280 290 300
RKNEKEQERR LQQAVLSRQM PSESLDPAFS PRMPSSGFAA EGRSTLGDAE
310 320 330 340 350
ASDPPPPYSD FHPNNQESTL SHSRMERSVF MPRPQAVGSS NYASTSAGLK
360 370 380 390 400
YPGSGADLPP PQRAAGDSGE DSDDSDYENL IDPTEPSNSE YSHSKDSRPM
410
AHPDEDPRNT QTSQI
Length:415
Mass (Da):46,901
Last modified:December 20, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEDA67ACB10C66C51
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA09927 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 conflicti55 – 57EIH → QIY in BAA09927 (PubMed:8590280).Curated3
Sequence conflicti230S → G in BAG59274 (PubMed:14702039).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

More...
DDBJi
Links Updated
D63877 mRNA Translation: BAA09927.1 Different initiation.
AK296677 mRNA Translation: BAG59274.1
BC008999 mRNA Translation: AAH08999.2

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31308.2

NCBI Reference Sequences

More...
RefSeqi
NP_115558.3, NM_032182.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000298492; ENSP00000298492; ENSG00000165660

Database of genes from NCBI RefSeq genomes

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GeneIDi
23172

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:23172

UCSC genome browser

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UCSCi
uc001lib.4 human

<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
D63877 mRNA Translation: BAA09927.1 Different initiation.
AK296677 mRNA Translation: BAG59274.1
BC008999 mRNA Translation: AAH08999.2
CCDSiCCDS31308.2
RefSeqiNP_115558.3, NM_032182.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6H3Celectron microscopy3.90A/F1-415[»]
6R8Felectron microscopy3.80B/D1-267[»]
SMRiQ15018
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi116784, 51 interactors
CORUMiQ15018
IntActiQ15018, 61 interactors
MINTiQ15018
STRINGi9606.ENSP00000298492

Chemistry databases

BindingDBiQ15018

PTM databases

iPTMnetiQ15018
PhosphoSitePlusiQ15018

Polymorphism and mutation databases

BioMutaiABRAXAS2
DMDMi84029317

Proteomic databases

EPDiQ15018
jPOSTiQ15018
MassIVEiQ15018
MaxQBiQ15018
PaxDbiQ15018
PeptideAtlasiQ15018
PRIDEiQ15018
ProteomicsDBi60367

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
32387 83 antibodies

Genome annotation databases

EnsembliENST00000298492; ENSP00000298492; ENSG00000165660
GeneIDi23172
KEGGihsa:23172
UCSCiuc001lib.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
23172
DisGeNETi23172

GeneCards: human genes, protein and diseases

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GeneCardsi
ABRAXAS2
HGNCiHGNC:28975 ABRAXAS2
HPAiENSG00000165660 Low tissue specificity
neXtProtiNX_Q15018
OpenTargetsiENSG00000165660
PharmGKBiPA162387331

Human Unidentified Gene-Encoded large proteins database

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HUGEi
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GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiENOG410IPEG Eukaryota
ENOG410ZUYJ LUCA
GeneTreeiENSGT00530000063424
HOGENOMiCLU_040659_0_0_1
InParanoidiQ15018
KOiK20799
OMAiSRYNQRI
OrthoDBi954711at2759
PhylomeDBiQ15018
TreeFamiTF331751

Enzyme and pathway databases

ReactomeiR-HSA-5689901 Metalloprotease DUBs

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
ABRAXAS2 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
KIAA0157

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
23172
PharosiQ15018 Tbio

Protein Ontology

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PROi
PR:Q15018
RNActiQ15018 protein

Gene expression databases

BgeeiENSG00000165660 Expressed in secondary oocyte and 216 other tissues
GenevisibleiQ15018 HS

Family and domain databases

InterProiView protein in InterPro
IPR023238 FAM175
IPR023240 FAM175_BRISC_cplx_Abro1_su
IPR037518 MPN
PANTHERiPTHR31728 PTHR31728, 1 hit
PRINTSiPR02053 BRISCABRO1
PR02051 PROTEINF175
PROSITEiView protein in PROSITE
PS50249 MPN, 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 nameiABRX2_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: Q15018
Secondary accession number(s): B4DKR2, Q96H11
<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: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 22, 2020
This is version 148 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  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

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