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Protein

BRISC complex subunit Abraxas 2

Gene

ABRAXAS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • polyubiquitin modification-dependent protein binding Source: UniProtKB

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-HSA-5689901 Metalloprotease DUBs

Names & Taxonomyi

Protein namesi
Recommended name:
BRISC complex subunit Abraxas 2Imported
Alternative name(s):
Abraxas brother protein 11 Publication
Protein FAM175B
Gene namesi
Name:ABRAXAS2Imported
Synonyms:ABRO11 Publication, FAM175BImported, KIAA01571 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000165660.7
HGNCiHGNC:28975 ABRAXAS2
neXtProtiNX_Q15018

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi23172
OpenTargetsiENSG00000165660
PharmGKBiPA162387331

Polymorphism and mutation databases

BioMutaiFAM175B
DMDMi84029317

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000507251 – 415BRISC complex subunit Abraxas 2Add BLAST415

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei274PhosphoserineCombined sources1
Modified residuei280PhosphoserineCombined sources1
Modified residuei368PhosphoserineCombined sources1
Modified residuei372PhosphoserineCombined sources1
Modified residuei375PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15018
MaxQBiQ15018
PaxDbiQ15018
PeptideAtlasiQ15018
PRIDEiQ15018
ProteomicsDBi60367

PTM databases

iPTMnetiQ15018
PhosphoSitePlusiQ15018

Expressioni

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

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

BgeeiENSG00000165660 Expressed in 217 organ(s), highest expression level in secondary oocyte
CleanExiHS_FAM175B
GenevisibleiQ15018 HS

Organism-specific databases

HPAiHPA037591
HPA037592
HPA074089

Interactioni

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi116784, 51 interactors
IntActiQ15018, 40 interactors
MINTiQ15018
STRINGi9606.ENSP00000298492

Chemistry databases

BindingDBiQ15018

Structurei

3D structure databases

ProteinModelPortaliQ15018
SMRiQ15018
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 149MPNPROSITE-ProRule annotationAdd BLAST147

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Coiled coili215 – 266Sequence analysisAdd BLAST52

Sequence similaritiesi

Belongs to the FAM175 family. Abro1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IPEG Eukaryota
ENOG410ZUYJ LUCA
GeneTreeiENSGT00530000063424
HOGENOMiHOG000112450
HOVERGENiHBG081817
InParanoidiQ15018
KOiK20799
OMAiREQVLHK
OrthoDBiEOG091G07ID
PhylomeDBiQ15018
TreeFamiTF331751

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

Sequencei

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
Checksum:iEDA67ACB10C66C51
GO

Sequence cautioni

The sequence BAA09927 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55 – 57EIH → QIY in BAA09927 (PubMed:8590280).Curated3
Sequence conflicti230S → G in BAG59274 (PubMed:14702039).Curated1

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
UniGeneiHs.280695

Genome annotation databases

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

Similar proteinsi

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
UniGeneiHs.280695

3D structure databases

ProteinModelPortaliQ15018
SMRiQ15018
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116784, 51 interactors
IntActiQ15018, 40 interactors
MINTiQ15018
STRINGi9606.ENSP00000298492

Chemistry databases

BindingDBiQ15018

PTM databases

iPTMnetiQ15018
PhosphoSitePlusiQ15018

Polymorphism and mutation databases

BioMutaiFAM175B
DMDMi84029317

Proteomic databases

EPDiQ15018
MaxQBiQ15018
PaxDbiQ15018
PeptideAtlasiQ15018
PRIDEiQ15018
ProteomicsDBi60367

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23172
DisGeNETi23172
EuPathDBiHostDB:ENSG00000165660.7
GeneCardsiABRAXAS2
H-InvDBiHIX0009288
HGNCiHGNC:28975 ABRAXAS2
HPAiHPA037591
HPA037592
HPA074089
neXtProtiNX_Q15018
OpenTargetsiENSG00000165660
PharmGKBiPA162387331
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPEG Eukaryota
ENOG410ZUYJ LUCA
GeneTreeiENSGT00530000063424
HOGENOMiHOG000112450
HOVERGENiHBG081817
InParanoidiQ15018
KOiK20799
OMAiREQVLHK
OrthoDBiEOG091G07ID
PhylomeDBiQ15018
TreeFamiTF331751

Enzyme and pathway databases

ReactomeiR-HSA-5689901 Metalloprotease DUBs

Miscellaneous databases

ChiTaRSiFAM175B human
GeneWikiiKIAA0157
GenomeRNAii23172
PROiPR:Q15018

Gene expression databases

BgeeiENSG00000165660 Expressed in 217 organ(s), highest expression level in secondary oocyte
CleanExiHS_FAM175B
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
ProtoNetiSearch...

Entry informationi

Entry nameiABRX2_HUMAN
AccessioniPrimary (citable) accession number: Q15018
Secondary accession number(s): B4DKR2, Q96H11
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 12, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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
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Main funding by: National Institutes of Health

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