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Protein

BRISC complex subunit Abro1

Gene

FAM175B

Organism
Homo sapiens (Human)
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 (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

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • polyubiquitin binding Source: UniProtKB

GO - Biological processi

  • attachment of spindle microtubules to kinetochore Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB
  • mitotic cell cycle Source: UniProtKB
  • mitotic spindle assembly 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 11 Publication
Protein FAM175B
Gene namesi
Name:FAM175B
Synonyms:ABRO11 Publication, KIAA01571 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:28975. FAM175B.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 122SA → RR: Slighly reduces interaction with BBRC36. Abolishes interaction with SHMT2. Strongly reduces interactions with BRE and BABAM1. 1 Publication
Mutagenesisi215 – 2228Missing : Reduces interaction with SHMT2, but has no effect on interaction with BRCC3. 1 Publication
Mutagenesisi220 – 2201V → R: Strongly reduces interaction with BBRC3; SHMT2; BRE and BABAM1; when associated with Y-231. Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BRE and BABAM1; when associated with Y-231 and Y-241. 1 Publication
Mutagenesisi231 – 2311E → Y: Strongly reduces interaction with BBRC3; SHMT2; BRE and BABAM1; when associated with R-220. Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BRE and BABAM1; when associated with R-220 and Y-241. 1 Publication
Mutagenesisi241 – 2411V → R: Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BRE and BABAM1; when associated with R-220 and Y-231. 1 Publication

Organism-specific databases

PharmGKBiPA162387331.

Polymorphism and mutation databases

BioMutaiFAM175B.
DMDMi84029317.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415BRISC complex subunit Abro1PRO_0000050725Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15018.
MaxQBiQ15018.
PaxDbiQ15018.
PRIDEiQ15018.

PTM databases

iPTMnetiQ15018.
PhosphoSiteiQ15018.

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

BgeeiQ15018.
CleanExiHS_FAM175B.
GenevisibleiQ15018. HS.

Organism-specific databases

HPAiHPA037591.
HPA037592.

Interactioni

Subunit structurei

Component of the BRISC complex, at least composed of FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 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). Identified in complexes with INAR1, INAR2 and SHMT2 (PubMed:24075985). Interacts with THAP5 (PubMed:21195082). 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 (PubMed:25283148). Interacts with NUMA1 (PubMed:26195665). Interacts with microtubule minus ends (PubMed:26195665). Binds polyubiquitin (PubMed:19261749). The BRISC complex binds monoubiquitin and both 'Lys-48'- and 'Lys-63'-linked polyubiquitin (PubMed:20032457).12 Publications

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116784. 38 interactions.
IntActiQ15018. 12 interactions.
MINTiMINT-1181536.
STRINGi9606.ENSP00000298492.

Structurei

3D structure databases

ProteinModelPortaliQ15018.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 116111MPN-likeCuratedAdd
BLAST
Regioni215 – 2228Important for interaction with SHMT21 Publication
Regioni220 – 24122Important for interaction with BBRC36 and other subunits of the BRISC complex1 PublicationAdd
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.1 Publication

Sequence similaritiesi

Belongs to the FAM175 family. Abro1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IPEG. Eukaryota.
ENOG410ZUYJ. LUCA.
GeneTreeiENSGT00530000063424.
HOGENOMiHOG000112450.
HOVERGENiHBG081817.
InParanoidiQ15018.
OMAiREQVLHK.
OrthoDBiEOG7J9VPJ.
PhylomeDBiQ15018.
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.

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 BAA09927.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 573EIH → QIY in BAA09927 (PubMed:8590280).Curated
Sequence conflicti230 – 2301S → G in BAG59274 (PubMed:14702039).Curated

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.

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116784. 38 interactions.
IntActiQ15018. 12 interactions.
MINTiMINT-1181536.
STRINGi9606.ENSP00000298492.

PTM databases

iPTMnetiQ15018.
PhosphoSiteiQ15018.

Polymorphism and mutation databases

BioMutaiFAM175B.
DMDMi84029317.

Proteomic databases

EPDiQ15018.
MaxQBiQ15018.
PaxDbiQ15018.
PRIDEiQ15018.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23172.
GeneCardsiFAM175B.
H-InvDBHIX0009288.
HGNCiHGNC:28975. FAM175B.
HPAiHPA037591.
HPA037592.
neXtProtiNX_Q15018.
PharmGKBiPA162387331.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPEG. Eukaryota.
ENOG410ZUYJ. LUCA.
GeneTreeiENSGT00530000063424.
HOGENOMiHOG000112450.
HOVERGENiHBG081817.
InParanoidiQ15018.
OMAiREQVLHK.
OrthoDBiEOG7J9VPJ.
PhylomeDBiQ15018.
TreeFamiTF331751.

Miscellaneous databases

GeneWikiiKIAA0157.
GenomeRNAii23172.
NextBioi44583.
PROiQ15018.

Gene expression databases

BgeeiQ15018.
CleanExiHS_FAM175B.
GenevisibleiQ15018. HS.

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. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Tongue.
  3. "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].
    Tissue: Placenta.
  4. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response."
    Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S., Elledge S.J.
    Science 316:1194-1198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF INTERACTION WITH BRCA1, SUBUNIT.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-368; SER-372 AND SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1."
    Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E.
    EMBO J. 28:621-631(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BRISC COMPLEX, FUNCTION, SUBUNIT.
  9. "NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control."
    Wang B., Hurov K., Hofmann K., Elledge S.J.
    Genes Dev. 23:729-739(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN MPN-LIKE, UBIQUITIN-BINDING, SUBUNIT.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368; SER-372 AND SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Specificity of the BRISC deubiquitinating enzyme is not due to selective binding to Lys63-linked polyubiquitin."
    Cooper E.M., Boeke J.D., Cohen R.E.
    J. Biol. Chem. 285:10344-10352(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION OF THE BRISC COMPLEX WITH UBIQUITIN.
  12. "The Lys63-specific deubiquitinating enzyme BRCC36 is regulated by two scaffold proteins localizing in different subcellular compartments."
    Feng L., Wang J., Chen J.
    J. Biol. Chem. 285:30982-30988(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BRCC3, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "NBA1/MERIT40 and BRE interaction is required for the integrity of two distinct deubiquitinating enzyme BRCC36-containing complexes."
    Hu X., Kim J.A., Castillo A., Huang M., Liu J., Wang B.
    J. Biol. Chem. 286:11734-11745(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BABAM1, IDENTIFICATION IN THE BRISC COMPLEX, LACK OF INTERACTION WITH BRCA1, SUBCELLULAR LOCATION.
  16. "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: INTERACTION WITH THAP5, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION.
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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, SUBCELLULAR LOCATION.
  19. Cited for: FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION WITH SHMT1 AND SHMT2, IDENTIFICATION IN A COMPLEX WITH SHMT2 AND INAR1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, MUTAGENESIS OF 215-ALA--ALA-222.
  20. "ABRO1 suppresses tumourigenesis and regulates the DNA damage response by stabilizing p53."
    Zhang J., Cao M., Dong J., Li C., Xu W., Zhan Y., Wang X., Yu M., Ge C., Ge Z., Yang X.
    Nat. Commun. 5:5059-5059(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY DNA DAMAGE, INTERACTION WITH USP7 AND TP53, IDENTIFICATION IN THE BRISC COMPLEX.
  21. "The deubiquitinating enzyme complex BRISC is required for proper mitotic spindle assembly in mammalian cells."
    Yan K., Li L., Wang X., Hong R., Zhang Y., Yang H., Lin M., Zhang S., He Q., Zheng D., Tang J., Yin Y., Shao G.
    J. Cell Biol. 210:209-224(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUMA1, SUBUNIT, SUBCELLULAR LOCATION.
  22. Cited for: FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION WITH BRCC3; BRE; BABAM1 AND SHMT2, SUBUNIT, MUTAGENESIS OF 11-SER-ALA-12; VAL-220; GLU-231 AND VAL-241.

Entry informationi

Entry nameiF175B_HUMAN
AccessioniPrimary (citable) accession number: Q15018
Secondary accession number(s): B4DKR2, Q96H11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 11, 2016
This is version 117 of the entry and version 2 of the sequence. [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

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. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  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.