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P46736 (BRCC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:BRCC3
Synonyms:BRCC36, C6.1A, CXorf53
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Subunit structure

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. Ref.3 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Nucleus. Note: Localizes at sites of DNA damage at double-strand breaks (DSBs). Ref.9 Ref.11 Ref.13 Ref.15

Tissue specificity

Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Aberrantly expressed in the vast majority of breast tumors. Ref.8

Involvement in disease

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

Sequence similarities

Belongs to the peptidase M67A family. BRCC36 subfamily.

Contains 1 MPN (JAB/Mov34) domain.

Sequence caution

The sequence AAB29005.2 differs from that shown. Reason: Erroneous initiation.

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Hydrolase
Metalloprotease
Protease
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2 DNA damage checkpoint

Inferred from mutant phenotype Ref.10Ref.12Ref.13. Source: UniProtKB

double-strand break repair

Inferred from mutant phenotype Ref.10Ref.12Ref.13. Source: UniProtKB

histone H2A K63-linked deubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of DNA repair

Inferred from mutant phenotype Ref.10Ref.12Ref.13. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from direct assay Ref.10Ref.14. Source: UniProtKB

regulation of catalytic activity

Inferred from direct assay Ref.3. Source: GOC

response to X-ray

Inferred from direct assay Ref.3. Source: MGI

response to ionizing radiation

Inferred from mutant phenotype Ref.10Ref.12Ref.13. Source: UniProtKB

   Cellular_componentBRCA1-A complex

Inferred from direct assay Ref.10Ref.15Ref.12Ref.13Ref.11. Source: UniProtKB

BRISC complex

Inferred from direct assay Ref.14. Source: UniProtKB

nuclear ubiquitin ligase complex

Inferred from direct assay Ref.3. Source: UniProtKB

nucleus

Inferred from direct assay Ref.15. Source: UniProtKB

ubiquitin ligase complex

Inferred from direct assay Ref.3. Source: MGI

   Molecular_functionenzyme regulator activity

Inferred from direct assay Ref.3. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from mutant phenotype Ref.10Ref.15Ref.14Ref.12. Source: UniProtKB

polyubiquitin binding

Inferred from direct assay Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.3Ref.13Ref.11. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from mutant phenotype Ref.15Ref.14Ref.12. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P46736-1)

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.
Isoform 1 (identifier: P46736-2)

The sequence of this isoform differs from the canonical sequence as follows:
     184-208: Missing.
Isoform 3 (identifier: P46736-3)

The sequence of this isoform differs from the canonical sequence as follows:
     46-46: T → TS
     184-208: Missing.
Isoform 4 (identifier: P46736-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-114: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P46736-5)

The sequence of this isoform differs from the canonical sequence as follows:
     183-252: ESLHGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHS → D
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 316315Lys-63-specific deubiquitinase BRCC36
PRO_0000213967

Regions

Domain7 – 148142MPN
Motif122 – 13514JAMM motif

Sites

Metal binding1221Zinc; catalytic Probable
Metal binding1241Zinc; catalytic Probable
Metal binding1351Zinc; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7

Natural variations

Alternative sequence1 – 114114Missing in isoform 4.
VSP_037257
Alternative sequence461T → TS in isoform 3.
VSP_037258
Alternative sequence183 – 25270ESLHG…RRIHS → D in isoform 5.
VSP_037259
Alternative sequence184 – 20825Missing in isoform 1 and isoform 3.
VSP_003261
Natural variant741I → V.
Corresponds to variant rs28997578 [ dbSNP | Ensembl ].
VAR_050097

Experimental info

Mutagenesis122 – 1243HSH → QSQ: Abolishes metalloprotease activity and function in DNA repair. Ref.10 Ref.12 Ref.14 Ref.15
Mutagenesis1221H → Q: Loss of deubiquitinase activity. Ref.14
Sequence conflict2251G → W in AAB29005. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified May 10, 2002. Version 2.
Checksum: 5720358C1A2F7421

FASTA31636,072
        10         20         30         40         50         60 
MAVQVVQAVQ AVHLESDAFL VCLNHALSTE KEEVMGLCIG ELNDDTRSDS KFAYTGTEMR 

        70         80         90        100        110        120 
TVAEKVDAVR IVHIHSVIIL RRSDKRKDRV EISPEQLSAA STEAERLAEL TGRPMRVVGW 

       130        140        150        160        170        180 
YHSHPHITVW PSHVDVRTQA MYQMMDQGFV GLIFSCFIED KNTKTGRVLY TCFQSIQAQK 

       190        200        210        220        230        240 
SSESLHGPRD FWSSSQHISI EGQKEEERYE RIEIPIHIVP HVTIGKVCLE SAVELPKILC 

       250        260        270        280        290        300 
QEEQDAYRRI HSLTHLDSVT KIHNGSVFTK NLCSQMSAVS GPLLQWLEDR LEQNQQHLQE 

       310 
LQQEKEELMQ ELSSLE 

« Hide

Isoform 1 [UniParc].

Checksum: 56F03D91E313E1D9
Show »

FASTA29133,150
Isoform 3 [UniParc].

Checksum: 70302DC19999753C
Show »

FASTA29233,237
Isoform 4 [UniParc].

Checksum: D6F04C7365A7336D
Show »

FASTA20223,458
Isoform 5 [UniParc].

Checksum: 817A177F34ED1ED8
Show »

FASTA24728,027

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS56610.1. [P46736-3]
CCDS56611.1. [P46736-1]
CCDS56612.1. [P46736-2]
PIRI38167.
RefSeqNP_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]
UniGeneHs.558537.

3D structure databases

ProteinModelPortalP46736.
SMRP46736. Positions 10-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122599. 45 interactions.
DIPDIP-48719N.
IntActP46736. 21 interactions.
MINTMINT-1475401.

Protein family/group databases

MEROPSM67.004.

PTM databases

PhosphoSiteP46736.

Polymorphism databases

DMDM20532383.

Proteomic databases

MaxQBP46736.
PaxDbP46736.
PRIDEP46736.

Protocols and materials databases

DNASU79184.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330045; 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]
GeneID79184.
KEGGhsa:79184.
UCSCuc004fna.3. human. [P46736-1]
uc004fnb.3. human. [P46736-2]
uc011mzy.2. human. [P46736-3]

Organism-specific databases

CTD79184.
GeneCardsGC0XP154299.
HGNCHGNC:24185. BRCC3.
HPAHPA048737.
MIM300617. gene.
neXtProtNX_P46736.
Orphanet280679. Moyamoya disease - short stature - facial dysmorphism - hypergonadotropic hypogonadism.
PharmGKBPA134922847.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322509.
HOVERGENHBG002142.
KOK11864.
PhylomeDBP46736.
TreeFamTF328524.

Gene expression databases

ArrayExpressP46736.
BgeeP46736.
CleanExHS_BRCC3.
GenevestigatorP46736.

Family and domain databases

InterProIPR000555. JAMM/MPN+_dom.
[Graphical view]
PfamPF01398. JAB. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBRCC3.
GenomeRNAi79184.
NextBio68176.
PROP46736.
SOURCESearch...

Entry information

Entry nameBRCC3_HUMAN
AccessionPrimary (citable) accession number: P46736
Secondary accession number(s): A6QRF8 expand/collapse secondary AC list , A6QRF9, A8MUX5, A8MWH0, A9Z1Y0, A9Z1Y5, B1B062, B4DQN7, Q16107, Q53YX5, Q9BTZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 10, 2002
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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