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P46736

- BRCC3_HUMAN

UniProt

P46736 - BRCC3_HUMAN

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Protein
Lys-63-specific deubiquitinase BRCC36
Gene
BRCC3, BRCC36, C6.1A, CXorf53
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi122 – 1221Zinc; catalytic Inferred
Metal bindingi124 – 1241Zinc; catalytic Inferred
Metal bindingi135 – 1351Zinc; catalytic By similarity

GO - Molecular functioni

  1. enzyme regulator activity Source: MGI
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: UniProtKB
  4. polyubiquitin binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. ubiquitin thiolesterase activity Source: UniProtKB
  7. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. G2 DNA damage checkpoint Source: UniProtKB
  2. double-strand break repair Source: UniProtKB
  3. histone H2A K63-linked deubiquitination Source: UniProtKB
  4. positive regulation of DNA repair Source: UniProtKB
  5. protein K63-linked deubiquitination Source: UniProtKB
  6. regulation of catalytic activity Source: GOC
  7. response to X-ray Source: MGI
  8. response to ionizing radiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM67.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Lys-63-specific deubiquitinase BRCC36 (EC:3.4.19.-)
Alternative name(s):
BRCA1-A complex subunit BRCC36
BRCA1/BRCA2-containing complex subunit 3
BRCA1/BRCA2-containing complex subunit 36
BRISC complex subunit BRCC36
Gene namesi
Name:BRCC3
Synonyms:BRCC36, C6.1A, CXorf53
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:24185. BRCC3.

Subcellular locationi

Nucleus
Note: Localizes at sites of DNA damage at double-strand breaks (DSBs).4 Publications

GO - Cellular componenti

  1. BRCA1-A complex Source: UniProtKB
  2. BRISC complex Source: UniProtKB
  3. nuclear ubiquitin ligase complex Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. ubiquitin ligase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving BRCC3 is a cause of pro-lymphocytic T-cell leukemia (T-PLL). Translocation t(X;14)(q28;q11) with TCRA.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1243HSH → QSQ: Abolishes metalloprotease activity and function in DNA repair. 4 Publications
Mutagenesisi122 – 1221H → Q: Loss of deubiquitinase activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti280679. Moyamoya disease - short stature - facial dysmorphism - hypergonadotropic hypogonadism.
PharmGKBiPA134922847.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 316315Lys-63-specific deubiquitinase BRCC36
PRO_0000213967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP46736.
PaxDbiP46736.
PRIDEiP46736.

PTM databases

PhosphoSiteiP46736.

Expressioni

Tissue specificityi

Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Aberrantly expressed in the vast majority of breast tumors.1 Publication

Gene expression databases

ArrayExpressiP46736.
BgeeiP46736.
CleanExiHS_BRCC3.
GenevestigatoriP46736.

Organism-specific databases

HPAiHPA048737.

Interactioni

Subunit structurei

Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. In the BRCA1-A complex, interacts directly with FAM175A/Abraxas and BRE/BRCC45. Component of the BRISC complex, at least composed of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. The BRISC complex interacts with the CSN complex. Component of the BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1, BRCA2, BARD1, BRE and RAD51. BRCC is a ubiquitin E3 ligase complex that enhances cellular survival following DNA damage. Interacts with BRCA1. Binds polyubiquitin.7 Publications

Protein-protein interaction databases

BioGridi122599. 46 interactions.
DIPiDIP-48719N.
IntActiP46736. 21 interactions.
MINTiMINT-1475401.

Structurei

3D structure databases

ProteinModelPortaliP46736.
SMRiP46736. Positions 10-176.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 148142MPN
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi122 – 13514JAMM motif
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG322509.
HOVERGENiHBG002142.
KOiK11864.
PhylomeDBiP46736.
TreeFamiTF328524.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: P46736-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAVQVVQAVQ AVHLESDAFL VCLNHALSTE KEEVMGLCIG ELNDDTRSDS    50
KFAYTGTEMR TVAEKVDAVR IVHIHSVIIL RRSDKRKDRV EISPEQLSAA 100
STEAERLAEL TGRPMRVVGW YHSHPHITVW PSHVDVRTQA MYQMMDQGFV 150
GLIFSCFIED KNTKTGRVLY TCFQSIQAQK SSESLHGPRD FWSSSQHISI 200
EGQKEEERYE RIEIPIHIVP HVTIGKVCLE SAVELPKILC QEEQDAYRRI 250
HSLTHLDSVT KIHNGSVFTK NLCSQMSAVS GPLLQWLEDR LEQNQQHLQE 300
LQQEKEELMQ ELSSLE 316
Length:316
Mass (Da):36,072
Last modified:May 10, 2002 - v2
Checksum:i5720358C1A2F7421
GO
Isoform 1 (identifier: P46736-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     184-208: Missing.

Show »
Length:291
Mass (Da):33,150
Checksum:i56F03D91E313E1D9
GO
Isoform 3 (identifier: P46736-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-46: T → TS
     184-208: Missing.

Show »
Length:292
Mass (Da):33,237
Checksum:i70302DC19999753C
GO
Isoform 4 (identifier: P46736-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-114: Missing.

Note: No experimental confirmation available.

Show »
Length:202
Mass (Da):23,458
Checksum:iD6F04C7365A7336D
GO
Isoform 5 (identifier: P46736-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     183-252: ESLHGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHS → D

Note: No experimental confirmation available.

Show »
Length:247
Mass (Da):28,027
Checksum:i817A177F34ED1ED8
GO

Sequence cautioni

The sequence AAB29005.2 differs from that shown. Reason: Erroneous initiation.
The sequence CAO03573.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741I → V.
Corresponds to variant rs28997578 [ dbSNP | Ensembl ].
VAR_050097

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 114114Missing in isoform 4.
VSP_037257Add
BLAST
Alternative sequencei46 – 461T → TS in isoform 3.
VSP_037258
Alternative sequencei183 – 25270ESLHG…RRIHS → D in isoform 5.
VSP_037259Add
BLAST
Alternative sequencei184 – 20825Missing in isoform 1 and isoform 3.
VSP_003261Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251G → W in AAB29005. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64643 mRNA. Translation: CAA45917.1.
S68015 mRNA. Translation: AAB29005.2. Different initiation.
AY438030 mRNA. Translation: AAR30498.1.
AK298886 mRNA. Translation: BAG60999.1.
AK299194 mRNA. Translation: BAG61237.1.
AK313544 mRNA. Translation: BAG36320.1.
BX293995, BX470111 Genomic DNA. Translation: CAH70537.1.
BX293995, BX470111 Genomic DNA. Translation: CAH70538.1.
BX470111, BX293995 Genomic DNA. Translation: CAI41654.1.
BX470111, BX293995 Genomic DNA. Translation: CAI41655.1.
BX470111 Genomic DNA. Translation: CAO03573.1. Sequence problems.
BX470111 Genomic DNA. Translation: CAO03574.1.
BX470111, BX293995 Genomic DNA. Translation: CAO03575.1.
BX470111, BX293995 Genomic DNA. Translation: CAO03576.1.
BX293995, BX470111 Genomic DNA. Translation: CAO03601.1.
BX293995, BX470111 Genomic DNA. Translation: CAO03602.1.
BC002999 mRNA. Translation: AAH02999.1.
BC006540 mRNA. Translation: AAH06540.1.
CCDSiCCDS56610.1. [P46736-3]
CCDS56611.1. [P46736-1]
CCDS56612.1. [P46736-2]
PIRiI38167.
RefSeqiNP_001018065.1. NM_001018055.2. [P46736-2]
NP_001229569.1. NM_001242640.1. [P46736-3]
NP_077308.1. NM_024332.3. [P46736-1]
XP_005274806.1. XM_005274749.1. [P46736-5]
XP_005274807.1. XM_005274750.1. [P46736-4]
UniGeneiHs.558537.

Genome annotation databases

EnsembliENST00000330045; ENSP00000328641; ENSG00000185515. [P46736-2]
ENST00000340647; ENSP00000344103; ENSG00000185515. [P46736-3]
ENST00000369459; ENSP00000358471; ENSG00000185515. [P46736-5]
ENST00000369462; ENSP00000358474; ENSG00000185515. [P46736-1]
ENST00000594541; ENSP00000470674; ENSG00000269884. [P46736-1]
ENST00000597217; ENSP00000469831; ENSG00000269884. [P46736-3]
ENST00000597826; ENSP00000473083; ENSG00000269884. [P46736-5]
ENST00000601378; ENSP00000469902; ENSG00000269884. [P46736-2]
GeneIDi79184.
KEGGihsa:79184.
UCSCiuc004fna.3. human. [P46736-1]
uc004fnb.3. human. [P46736-2]
uc011mzy.2. human. [P46736-3]

Polymorphism databases

DMDMi20532383.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64643 mRNA. Translation: CAA45917.1 .
S68015 mRNA. Translation: AAB29005.2 . Different initiation.
AY438030 mRNA. Translation: AAR30498.1 .
AK298886 mRNA. Translation: BAG60999.1 .
AK299194 mRNA. Translation: BAG61237.1 .
AK313544 mRNA. Translation: BAG36320.1 .
BX293995 , BX470111 Genomic DNA. Translation: CAH70537.1 .
BX293995 , BX470111 Genomic DNA. Translation: CAH70538.1 .
BX470111 , BX293995 Genomic DNA. Translation: CAI41654.1 .
BX470111 , BX293995 Genomic DNA. Translation: CAI41655.1 .
BX470111 Genomic DNA. Translation: CAO03573.1 . Sequence problems.
BX470111 Genomic DNA. Translation: CAO03574.1 .
BX470111 , BX293995 Genomic DNA. Translation: CAO03575.1 .
BX470111 , BX293995 Genomic DNA. Translation: CAO03576.1 .
BX293995 , BX470111 Genomic DNA. Translation: CAO03601.1 .
BX293995 , BX470111 Genomic DNA. Translation: CAO03602.1 .
BC002999 mRNA. Translation: AAH02999.1 .
BC006540 mRNA. Translation: AAH06540.1 .
CCDSi CCDS56610.1. [P46736-3 ]
CCDS56611.1. [P46736-1 ]
CCDS56612.1. [P46736-2 ]
PIRi I38167.
RefSeqi NP_001018065.1. NM_001018055.2. [P46736-2 ]
NP_001229569.1. NM_001242640.1. [P46736-3 ]
NP_077308.1. NM_024332.3. [P46736-1 ]
XP_005274806.1. XM_005274749.1. [P46736-5 ]
XP_005274807.1. XM_005274750.1. [P46736-4 ]
UniGenei Hs.558537.

3D structure databases

ProteinModelPortali P46736.
SMRi P46736. Positions 10-176.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122599. 46 interactions.
DIPi DIP-48719N.
IntActi P46736. 21 interactions.
MINTi MINT-1475401.

Protein family/group databases

MEROPSi M67.004.

PTM databases

PhosphoSitei P46736.

Polymorphism databases

DMDMi 20532383.

Proteomic databases

MaxQBi P46736.
PaxDbi P46736.
PRIDEi P46736.

Protocols and materials databases

DNASUi 79184.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330045 ; ENSP00000328641 ; ENSG00000185515 . [P46736-2 ]
ENST00000340647 ; ENSP00000344103 ; ENSG00000185515 . [P46736-3 ]
ENST00000369459 ; ENSP00000358471 ; ENSG00000185515 . [P46736-5 ]
ENST00000369462 ; ENSP00000358474 ; ENSG00000185515 . [P46736-1 ]
ENST00000594541 ; ENSP00000470674 ; ENSG00000269884 . [P46736-1 ]
ENST00000597217 ; ENSP00000469831 ; ENSG00000269884 . [P46736-3 ]
ENST00000597826 ; ENSP00000473083 ; ENSG00000269884 . [P46736-5 ]
ENST00000601378 ; ENSP00000469902 ; ENSG00000269884 . [P46736-2 ]
GeneIDi 79184.
KEGGi hsa:79184.
UCSCi uc004fna.3. human. [P46736-1 ]
uc004fnb.3. human. [P46736-2 ]
uc011mzy.2. human. [P46736-3 ]

Organism-specific databases

CTDi 79184.
GeneCardsi GC0XP154299.
HGNCi HGNC:24185. BRCC3.
HPAi HPA048737.
MIMi 300617. gene.
neXtProti NX_P46736.
Orphaneti 280679. Moyamoya disease - short stature - facial dysmorphism - hypergonadotropic hypogonadism.
PharmGKBi PA134922847.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322509.
HOVERGENi HBG002142.
KOi K11864.
PhylomeDBi P46736.
TreeFami TF328524.

Miscellaneous databases

GeneWikii BRCC3.
GenomeRNAii 79184.
NextBioi 68176.
PROi P46736.
SOURCEi Search...

Gene expression databases

ArrayExpressi P46736.
Bgeei P46736.
CleanExi HS_BRCC3.
Genevestigatori P46736.

Family and domain databases

InterProi IPR000555. JAMM/MPN+_dom.
[Graphical view ]
Pfami PF01398. JAB. 1 hit.
[Graphical view ]
SMARTi SM00232. JAB_MPN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence of two genes associated with a CpG island 5' of the factor VIII gene."
    Kenwrick S., Levinson B., Taylor S., Shapiro A., Gitschier J.
    Hum. Mol. Genet. 1:179-186(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "The chromosomal translocation t(X;14)(q28;q11) in T-cell pro-lymphocytic leukaemia breaks within one gene and activates another."
    Fisch P., Forster A., Sherrington P.D., Dyer M.J.S., Rabbitts T.H.
    Oncogene 8:3271-3276(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHROMOSOMAL TRANSLOCATION.
  3. "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair."
    Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S., Godwin A.K., Shiekhattar R.
    Mol. Cell 12:1087-1099(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, IDENTIFICATION IN BRCC COMPLEX, INTERACTION WITH BRCA1.
  4. "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] (ISOFORMS 2; 3 AND 4).
    Tissue: Brain and Teratocarcinoma.
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 2).
    Tissue: Lung.
  7. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-31; 90-106 AND 227-237, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  8. "BRCC36 is essential for ionizing radiation-induced BRCA1 phosphorylation and nuclear foci formation."
    Chen X., Arciero C.A., Wang C., Broccoli D., Godwin A.K.
    Cancer Res. 66:5039-5046(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage."
    Wang B., Elledge S.J.
    Proc. Natl. Acad. Sci. U.S.A. 104:20759-20763(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH FAM175A.
  10. "RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites."
    Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B., Livingston D.M., Greenberg R.A.
    Science 316:1198-1202(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, MUTAGENESIS OF 122-HIS--HIS-124.
  11. "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: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, UBIQUITIN-BINDING, INTERACTION WITH FAM175A.
  12. "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks."
    Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y., Greenberg R.A.
    Genes Dev. 23:740-754(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, MUTAGENESIS OF 122-HIS--HIS-124.
  13. "MERIT40 facilitates BRCA1 localization and DNA damage repair."
    Feng L., Huang J., Chen J.
    Genes Dev. 23:719-728(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH BRE AND FAM175A.
  14. "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: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION WITH THE CSN COMPLEX, MUTAGENESIS OF HIS-122.
  15. "The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks."
    Shao G., Lilli D.R., Patterson-Fortin J., Coleman K.A., Morrissey D.E., Greenberg R.A.
    Proc. Natl. Acad. Sci. U.S.A. 106:3166-3171(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 122-HIS--HIS-124.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBRCC3_HUMAN
AccessioniPrimary (citable) accession number: P46736
Secondary accession number(s): A6QRF8
, A6QRF9, A8MUX5, A8MWH0, A9Z1Y0, A9Z1Y5, B1B062, B4DQN7, Q16107, Q53YX5, Q9BTZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 10, 2002
Last modified: September 3, 2014
This is version 136 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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