P46736 (BRCC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	BRCC3
Synonyms:	BRCC36, C6.1A, CXorf53

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Hydrolase Metalloprotease Protease
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G2 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 proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to X-ray Inferred from direct assay Ref.3. Source: MGI
Cellular_component	BRCA1-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
Molecular_function	enzyme 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 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 316	315	Lys-63-specific deubiquitinase BRCC36		PRO_0000213967
Regions
	Domain	7 – 148	142	MPN
	Motif	122 – 135	14	JAMM motif
Sites
	Metal binding	122	1	Zinc; catalytic Probable
	Metal binding	124	1	Zinc; catalytic Probable
	Metal binding	135	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
Natural variations
	Alternative sequence	1 – 114	114	Missing in isoform 4.		VSP_037257
	Alternative sequence	46	1	T → TS in isoform 3.		VSP_037258
	Alternative sequence	183 – 252	70	ESLHG…RRIHS → D in isoform 5.		VSP_037259
	Alternative sequence	184 – 208	25	Missing in isoform 1 and isoform 3.		VSP_003261
	Natural variant	74	1	I → V. Corresponds to variant rs28997578 [ dbSNP | Ensembl ].		VAR_050097
Experimental info
	Mutagenesis	122 – 124	3	HSH → QSQ: Abolishes metalloprotease activity and function in DNA repair. Ref.10 Ref.12 Ref.14 Ref.15
	Mutagenesis	122	1	H → Q: Loss of deubiquitinase activity. Ref.14
	Sequence conflict	225	1	G → W in AAB29005. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified May 10, 2002. Version 2. Checksum: 5720358C1A2F7421	FASTA	316	36,072
	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
	Isoform 1 [UniParc]. Checksum: 56F03D91E313E1D9	FASTA	291	33,150
	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 SSEYERIEIP IHIVPHVTIG KVCLESAVEL PKILCQEEQD AYRRIHSLTH LDSVTKIHNG 250 260 270 280 290 SVFTKNLCSQ MSAVSGPLLQ WLEDRLEQNQ QHLQELQQEK EELMQELSSL E
	Isoform 3 [UniParc]. Checksum: 70302DC19999753C	FASTA	292	33,237
	10 20 30 40 50 60 MAVQVVQAVQ AVHLESDAFL VCLNHALSTE KEEVMGLCIG ELNDDTSRSD SKFAYTGTEM 70 80 90 100 110 120 RTVAEKVDAV RIVHIHSVII LRRSDKRKDR VEISPEQLSA ASTEAERLAE LTGRPMRVVG 130 140 150 160 170 180 WYHSHPHITV WPSHVDVRTQ AMYQMMDQGF VGLIFSCFIE DKNTKTGRVL YTCFQSIQAQ 190 200 210 220 230 240 KSSEYERIEI PIHIVPHVTI GKVCLESAVE LPKILCQEEQ DAYRRIHSLT HLDSVTKIHN 250 260 270 280 290 GSVFTKNLCS QMSAVSGPLL QWLEDRLEQN QQHLQELQQE KEELMQELSS LE
	Isoform 4 [UniParc]. Checksum: D6F04C7365A7336D	FASTA	202	23,458
	10 20 30 40 50 60 MRVVGWYHSH PHITVWPSHV DVRTQAMYQM MDQGFVGLIF SCFIEDKNTK TGRVLYTCFQ 70 80 90 100 110 120 SIQAQKSSES LHGPRDFWSS SQHISIEGQK EEERYERIEI PIHIVPHVTI GKVCLESAVE 130 140 150 160 170 180 LPKILCQEEQ DAYRRIHSLT HLDSVTKIHN GSVFTKNLCS QMSAVSGPLL QWLEDRLEQN 190 200 QQHLQELQQE KEELMQELSS LE
	Isoform 5 [UniParc]. Checksum: 817A177F34ED1ED8	FASTA	247	28,027
	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 SSDLTHLDSV TKIHNGSVFT KNLCSQMSAV SGPLLQWLED RLEQNQQHLQ ELQQEKEELM QELSSLE

References

	« Hide 'large scale' referencesShow '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. , 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, 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.
IPI	IPI00853631. IPI00871617. IPI00936224. IPI00939471. IPI01010909.
PIR	I38167.
RefSeq	NP_001018065.1. NM_001018055.2. NP_001229569.1. NM_001242640.1. NP_077308.1. NM_024332.3.
UniGene	Hs.558537.
3D structure databases
ProteinModelPortal	P46736.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48719N.
IntAct	P46736. 20 interactions.
MINT	MINT-1475401.
Protein family/group databases
MEROPS	M67.004.
PTM databases
PhosphoSite	P46736.
Polymorphism databases
DMDM	20532383.
Proteomic databases
PaxDb	P46736.
PRIDE	P46736.
Protocols and materials databases
DNASU	79184.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000330045; ENSP00000328641; ENSG00000185515. ENST00000340647; ENSP00000344103; ENSG00000185515. ENST00000369459; ENSP00000358471; ENSG00000185515. ENST00000369462; ENSP00000358474; ENSG00000185515. ENST00000399026; ENSP00000381988; ENSG00000185515. ENST00000411985; ENSP00000413170; ENSG00000185515. ENST00000594541; ENSP00000470674; ENSG00000269884. ENST00000596060; ENSP00000471044; ENSG00000269884. ENST00000597217; ENSP00000469831; ENSG00000269884. ENST00000597826; ENSP00000473083; ENSG00000269884. ENST00000600398; ENSP00000472343; ENSG00000269884. ENST00000601378; ENSP00000469902; ENSG00000269884.
GeneID	79184.
KEGG	hsa:79184.
UCSC	uc004fna.3. human. uc004fnb.3. human. uc011mzy.2. human.
Organism-specific databases
CTD	79184.
GeneCards	GC0XP154299.
HGNC	HGNC:24185. BRCC3.
MIM	300617. gene.
neXtProt	NX_P46736.
Orphanet	280679. Moyamoya disease - short stature - facial dysmorphism - hypergonadotropic hypogonadism.
PharmGKB	PA134922847.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG322509.
HOVERGEN	HBG002142.
KO	K11864.
Gene expression databases
ArrayExpress	P46736.
Bgee	P46736.
CleanEx	HS_BRCC3.
Genevestigator	P46736.
GermOnline	ENSG00000185515. Homo sapiens.
Family and domain databases
InterPro	IPR000555. JAB1_Mov34_MPN_PAD1. [Graphical view]
Pfam	PF01398. JAB. 1 hit. [Graphical view]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	79184.
NextBio	68176.
SOURCE	Search...

Entry information

Entry name

BRCC3_HUMAN

Accession

Primary (citable) accession number: P46736
Secondary accession number(s): A6QRF8 , 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:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.