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Protein

BRISC complex subunit Abro1

Gene

Fam175b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (By similarity). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (PubMed:21195082). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. 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. 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 (By similarity).By similarity1 Publication2 Publications

GO - Molecular functioni

GO - Biological processi

  • attachment of spindle microtubules to kinetochore Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • cellular response to freezing Source: MGI
  • chromosome segregation Source: UniProtKB
  • mitotic cell cycle Source: UniProtKB
  • mitotic spindle assembly Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • protein K63-linked deubiquitination Source: UniProtKB
  • response to ischemia Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
BRISC complex subunit Abro1
Alternative name(s):
Abraxas brother protein 1
Protein FAM175B
Gene namesi
Name:Fam175b
Synonyms:Abro11 Publication, Kiaa0157
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1926116. Fam175b.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cytoplasmcytoskeletonspindle pole By similarity
  • Cytoplasmcytoskeleton By similarity

  • Note: A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K-fibers. Co-localizes with NUMA1 at mitotic spindle poles.By similarity

GO - Cellular componenti

  • BRISC complex Source: UniProtKB
  • cytoplasm Source: MGI
  • microtubule Source: UniProtKB-KW
  • nucleus Source: MGI
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile, and are protected against toxic shock caused by bacterial lipopolysaccharide (LPS). IFNAR1 'Lys-63'-linked ubiquitination and IFNAR1 internalization are increased.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415BRISC complex subunit Abro1PRO_0000050726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei280 – 2801PhosphoserineBy similarity
Modified residuei368 – 3681PhosphoserineBy similarity
Modified residuei372 – 3721PhosphoserineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3TCJ1.
MaxQBiQ3TCJ1.
PaxDbiQ3TCJ1.
PRIDEiQ3TCJ1.

PTM databases

iPTMnetiQ3TCJ1.
PhosphoSiteiQ3TCJ1.

Expressioni

Tissue specificityi

Detected in heart (at protein level).1 Publication

Inductioni

Up-regulated in heart in response to ischemia and reperfusion (at protein level).1 Publication

Gene expression databases

BgeeiQ3TCJ1.

Interactioni

Subunit structurei

Component of the BRISC complex, at least composed of FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. Interacts with BRCC3/BRCC36; the interaction is direct. Interacts with BABAM1. Does not interact with BRCA1. Interacts with SHMT1 and SHMT2; the interaction is direct. Identified in a complex with SHMT2 and the other subunits of the BRISC complex. Identified in complexes with INAR1, INAR2 and SHMT2. Interacts with ATF4 (PubMed:22974638). Interacts with p53/TP53; the interaction is direct. Interacts with USP7; the interaction is direct. Identified in a complex with p53/TP53 and USP7. Interacts with NUMA1. Interacts with microtubule minus ends. Binds polyubiquitin. The BRISC complex binds monoubiquitin and both 'Lys-48'- and 'Lys-63'-linked polyubiquitin.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi224665. 5 interactions.
STRINGi10090.ENSMUSP00000081541.

Structurei

3D structure databases

ProteinModelPortaliQ3TCJ1.
SMRiQ3TCJ1. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 116111MPN-likeBy similarityAdd
BLAST
Regioni215 – 2228Important for interaction with SHMT2By similarity
Regioni220 – 24122Important for interaction with BBRC36 and other subunits of the BRISC complexBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili215 – 26652Sequence analysisAdd
BLAST

Domaini

The MPN-like region is similar to the MPN (JAB/Mov34) domain.By similarity

Sequence similaritiesi

Belongs to the FAM175 family. Abro1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IPEG. Eukaryota.
ENOG410ZUYJ. LUCA.
HOGENOMiHOG000112450.
HOVERGENiHBG081817.
InParanoidiQ3TCJ1.
OrthoDBiEOG7J9VPJ.
PhylomeDBiQ3TCJ1.
TreeFamiTF331751.

Family and domain databases

InterProiIPR023238. FAM175.
IPR023240. FAM175_BRISC_cplx_Abro1_su.
[Graphical view]
PANTHERiPTHR31728:SF3. PTHR31728:SF3. 1 hit.
PRINTSiPR02053. BRISCABRO1.
PR02051. PROTEINF175.

Sequencei

Sequence statusi: Complete.

Q3TCJ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASISGYTF SAVCFHSANS NADHEGFLLG EVRQEETFSI SDSQISNTEF
60 70 80 90 100
LQVIEIHNHQ PCSQLFSFYD YASKVNEESL DRILKDRRKK VIGWYRFRRN
110 120 130 140 150
TQQQMSYREQ VIHKQLTRIL 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
KKNEKEQERR LQQALLSRQM PSESLEPAFS PRMSYSGFSA EGRSTLAETE
310 320 330 340 350
PSDPPPPYSD FHPNNQESTL SHSRMERSVF MPRPQAVGSS SYASTSGGLK
360 370 380 390 400
FTGSGADLLP SQSAAGDSGE ESDDSDYENL IDPAESPHSE YSHSKNSRPS
410
THPDEDPRNT QTSQI
Length:415
Mass (Da):46,943
Last modified:October 11, 2005 - v1
Checksum:iC9CB374DA089AFA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK170704 mRNA. Translation: BAE41965.1.
AK171524 mRNA. Translation: BAE42506.1.
BC030838 mRNA. Translation: AAH30838.2.
RefSeqiNP_932134.3. NM_198017.3.
UniGeneiMm.274824.
Mm.465624.

Genome annotation databases

GeneIDi109359.
KEGGimmu:109359.
UCSCiuc009kcr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK170704 mRNA. Translation: BAE41965.1.
AK171524 mRNA. Translation: BAE42506.1.
BC030838 mRNA. Translation: AAH30838.2.
RefSeqiNP_932134.3. NM_198017.3.
UniGeneiMm.274824.
Mm.465624.

3D structure databases

ProteinModelPortaliQ3TCJ1.
SMRiQ3TCJ1. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224665. 5 interactions.
STRINGi10090.ENSMUSP00000081541.

PTM databases

iPTMnetiQ3TCJ1.
PhosphoSiteiQ3TCJ1.

Proteomic databases

EPDiQ3TCJ1.
MaxQBiQ3TCJ1.
PaxDbiQ3TCJ1.
PRIDEiQ3TCJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi109359.
KEGGimmu:109359.
UCSCiuc009kcr.2. mouse.

Organism-specific databases

CTDi23172.
MGIiMGI:1926116. Fam175b.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IPEG. Eukaryota.
ENOG410ZUYJ. LUCA.
HOGENOMiHOG000112450.
HOVERGENiHBG081817.
InParanoidiQ3TCJ1.
OrthoDBiEOG7J9VPJ.
PhylomeDBiQ3TCJ1.
TreeFamiTF331751.

Miscellaneous databases

ChiTaRSiFam175b. mouse.
NextBioi361963.
PROiQ3TCJ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TCJ1.

Family and domain databases

InterProiIPR023238. FAM175.
IPR023240. FAM175_BRISC_cplx_Abro1_su.
[Graphical view]
PANTHERiPTHR31728:SF3. PTHR31728:SF3. 1 hit.
PRINTSiPR02053. BRISCABRO1.
PR02051. PROTEINF175.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-415.
    Strain: FVB/N.
    Tissue: Kidney.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "Regulation of Abro1/KIAA0157 during myocardial infarction and cell death reveals a novel cardioprotective mechanism for Lys63-specific deubiquitination."
    Cilenti L., Balakrishnan M.P., Wang X.L., Ambivero C., Sterlicchi M., del Monte F., Ma X.L., Zervos A.S.
    J. Mol. Cell. Cardiol. 50:652-661(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY HEART ISCHEMIA.
  5. "ATF4 interacts with Abro1/KIAA0157 scaffold protein and participates in a cytoprotective pathway."
    Ambivero C.T., Cilenti L., Zervos A.S.
    Biochim. Biophys. Acta 1823:2149-2156(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATF4.
  6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. Cited for: FUNCTION.

Entry informationi

Entry nameiF175B_MOUSE
AccessioniPrimary (citable) accession number: Q3TCJ1
Secondary accession number(s): Q3TB08, Q8K0R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 11, 2005
Last modified: May 11, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Interaction with THAP5 has been shown in human, but rodents lack a THAP5 homolog.Curated

Caution

Although strongly related to the FAM175A/CCDC98 protein, lacks the C-terminal pSXXF that constitutes a specific recognition motif for the BRCT domain of BRCA1.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.