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Protein

BRCA1-A complex subunit RAP80

Gene

Uimc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Plays a central role in the BRCA1-A complex by specifically binding '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). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1 (By similarity).By similarity

GO - Molecular functioni

  1. histone binding Source: UniProtKB
  2. K63-linked polyubiquitin binding Source: UniProtKB
  3. retinoid X receptor binding Source: MGI

GO - Biological processi

  1. double-strand break repair Source: UniProtKB
  2. G2 DNA damage checkpoint Source: UniProtKB
  3. histone H2A K63-linked deubiquitination Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: HGNC
  5. positive regulation of DNA repair Source: UniProtKB
  6. response to ionizing radiation Source: UniProtKB
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
BRCA1-A complex subunit RAP80
Alternative name(s):
Receptor-associated protein 80
Ubiquitin interaction motif-containing protein 1
Gene namesi
Name:Uimc1
Synonyms:Rap80, Rip110, Rxrip110
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:103185. Uimc1.

Subcellular locationi

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

GO - Cellular componenti

  1. BRCA1-A complex Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 727727BRCA1-A complex subunit RAP80PRO_0000097548Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphoserineBy similarity
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei205 – 2051PhosphoserineBy similarity
Modified residuei402 – 4021PhosphoserineBy similarity
Modified residuei637 – 6371PhosphoserineBy similarity
Modified residuei665 – 6651PhosphoserineBy similarity
Modified residuei689 – 6891PhosphoserineBy similarity

Post-translational modificationi

Sumoylated.By similarity
Phosphorylated upon DNA damage by ATM or ATR.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ5U5Q9.
PaxDbiQ5U5Q9.
PRIDEiQ5U5Q9.

PTM databases

PhosphoSiteiQ5U5Q9.

Expressioni

Gene expression databases

BgeeiQ5U5Q9.
CleanExiMM_UIMC1.
ExpressionAtlasiQ5U5Q9. baseline and differential.
GenevestigatoriQ5U5Q9.

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. Interacts with ESR1 and UBE2I (By similarity). Interacts with NR6A1 and TSP57.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UbcP629912EBI-7068640,EBI-413074

Protein-protein interaction databases

BioGridi203041. 4 interactions.
IntActiQ5U5Q9. 2 interactions.
MINTiMINT-4117130.

Structurei

Secondary structure

1
727
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi81 – 11939Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A1QX-ray2.20C/F80-120[»]
ProteinModelPortaliQ5U5Q9.
SMRiQ5U5Q9. Positions 80-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5U5Q9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 9920UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini104 – 12421UIM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 101101Necessary for transcriptional repressionBy similarityAdd
BLAST
Regioni97 – 1037UIM-linker
Regioni100 – 200101Necessary for interaction with NR6A1 N-terminusBy similarityAdd
BLAST
Regioni270 – 400131AIRAdd
BLAST
Regioni400 – 508109Necessary for interaction with NR6A1 C-terminusBy similarityAdd
BLAST
Regioni513 – 59078Zinc-finger-like regionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi60 – 7819LR motifAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi81 – 10828Glu-richAdd
BLAST

Domaini

The tandem UIM domains form a continuous 60 Angstrom-long alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and UIM2 bind to the proximal and distal ubiquitin moieties and recognize an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM domains determines the selectivity for 'Lys-63'-linkage, and its length is very important for specificity.1 Publication
The Abraxas-interacting region (AIR) mediates the interaction with FAM175A/Abraxas.By similarity

Sequence similaritiesi

Belongs to the RAP80 family.Curated
Contains 2 UIM (ubiquitin-interacting motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG72551.
GeneTreeiENSGT00390000007635.
HOGENOMiHOG000154772.
HOVERGENiHBG056783.
InParanoidiQ5U5Q9.
PhylomeDBiQ5U5Q9.

Family and domain databases

InterProiIPR003903. Ubiquitin-int_motif.
[Graphical view]
SMARTiSM00726. UIM. 2 hits.
[Graphical view]
PROSITEiPS50330. UIM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5U5Q9-1) [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

        10         20         30         40         50
MPRRKKKIKE ASESQNLEKK DLETSSCVSI KKKRRLEDLL IVISDSDGEE
60 70 80 90 100
TKEENGLQKT KTKQSNRSKC LAKRKVAHMS EEEQFALALK MSEQEAREVN
110 120 130 140 150
NQEEKEEELL RKAIAESLNS CWSSAASATR SRPLAAELSS HSHQENTKDS
160 170 180 190 200
GTTEGVWQLV PPSLCKGSHV SQGNEAEQRK EPWDHNENTE EEPVSGSSGS
210 220 230 240 250
WDQSSQPVFE NENVKCFDRC TGHLAEHTQC GKPQESTGSG YAFSKAVQGR
260 270 280 290 300
GDTSRQCLPI PADTKGLQDT GGTVHYYWGI PFCPAGVDPN QYTNVILCQL
310 320 330 340 350
EVYQKSLKMA QRQLVKKRGF GEPVLPRPPF LIQNECGQED QTSDKNEGIS
360 370 380 390 400
EDMGDEAKEE RQESRASVWH SETKDFQKSP IKSLKQKLLL EEEPTTSRGQ
410 420 430 440 450
SSQGLFVEET SEEGLKSSEG DNSVPTTQSI AALTSKRSLV LMPESSAEEI
460 470 480 490 500
TVCPETQLSF LEPLDLNRED SPDSRELPIE VRMAVGDKQV ANREDCMKEN
510 520 530 540 550
PPPAVSSSTR VSCPLCNQDF PPTKIEQHAM YCNGLMEQET VLTRRRREAK
560 570 580 590 600
NKSDGRTAAQ PALDANRKEK CYLCKSLVPL GEYQCHVEAC LQLAKVDRED
610 620 630 640 650
GIEGTRRPRV CAPVEGKQQQ RLKKSKDKGH SQGRLLSLLE QSEHRTTGVE
660 670 680 690 700
KKPKYSEVRT FRMPSPEVEE ASCSREMQST LSQLNLNESP IKSFVPVSEA
710 720
TNCLVDFKEQ FAFRSRTKSG RGRRRKS
Length:727
Mass (Da):81,478
Last modified:May 5, 2009 - v2
Checksum:iB753BF61180D63ED
GO
Isoform 2 (identifier: Q5U5Q9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     401-406: SSQGLF → HCSFDQ
     407-727: Missing.

Note: No experimental confirmation available.

Show »
Length:406
Mass (Da):45,575
Checksum:i904F4FDD0F27ECB0
GO
Isoform 3 (identifier: Q5U5Q9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     120-400: Missing.

Note: No experimental confirmation available.

Show »
Length:446
Mass (Da):50,382
Checksum:i4E76F9B20CF84D80
GO

Sequence cautioni

The sequence AAH37092.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti377 – 3771Q → R in BAC38875. (PubMed:16141072)Curated
Sequence conflicti450 – 4501I → T in BAC35106. (PubMed:16141072)Curated
Sequence conflicti450 – 4501I → T in BAC38875. (PubMed:16141072)Curated
Sequence conflicti450 – 4501I → T in BAE36094. (PubMed:16141072)Curated
Sequence conflicti554 – 5541D → G in AAH40808. (PubMed:15489334)Curated
Sequence conflicti722 – 7221G → E in AAC52167. (PubMed:7760852)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei120 – 400281Missing in isoform 3. 1 PublicationVSP_037266Add
BLAST
Alternative sequencei401 – 4066SSQGLF → HCSFDQ in isoform 2. 1 PublicationVSP_037267
Alternative sequencei407 – 727321Missing in isoform 2. 1 PublicationVSP_037268Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052704 mRNA. Translation: BAC35106.1.
AK083342 mRNA. Translation: BAC38875.1.
AK160926 mRNA. Translation: BAE36094.1.
BC037092 mRNA. Translation: AAH37092.1. Different initiation.
BC040808 mRNA. Translation: AAH40808.1.
U22015 mRNA. Translation: AAC52167.1.
CCDSiCCDS36671.1. [Q5U5Q9-1]
RefSeqiNP_001280589.1. NM_001293660.1.
NP_035437.1. NM_011307.2.
XP_006517229.1. XM_006517166.1.
UniGeneiMm.259301.

Genome annotation databases

EnsembliENSMUST00000026997; ENSMUSP00000026997; ENSMUSG00000025878.
ENSMUST00000099496; ENSMUSP00000097095; ENSMUSG00000025878.
GeneIDi20184.
KEGGimmu:20184.
UCSCiuc007qpv.1. mouse. [Q5U5Q9-1]
uc007qpw.1. mouse. [Q5U5Q9-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052704 mRNA. Translation: BAC35106.1.
AK083342 mRNA. Translation: BAC38875.1.
AK160926 mRNA. Translation: BAE36094.1.
BC037092 mRNA. Translation: AAH37092.1. Different initiation.
BC040808 mRNA. Translation: AAH40808.1.
U22015 mRNA. Translation: AAC52167.1.
CCDSiCCDS36671.1. [Q5U5Q9-1]
RefSeqiNP_001280589.1. NM_001293660.1.
NP_035437.1. NM_011307.2.
XP_006517229.1. XM_006517166.1.
UniGeneiMm.259301.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A1QX-ray2.20C/F80-120[»]
ProteinModelPortaliQ5U5Q9.
SMRiQ5U5Q9. Positions 80-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203041. 4 interactions.
IntActiQ5U5Q9. 2 interactions.
MINTiMINT-4117130.

PTM databases

PhosphoSiteiQ5U5Q9.

Proteomic databases

MaxQBiQ5U5Q9.
PaxDbiQ5U5Q9.
PRIDEiQ5U5Q9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026997; ENSMUSP00000026997; ENSMUSG00000025878.
ENSMUST00000099496; ENSMUSP00000097095; ENSMUSG00000025878.
GeneIDi20184.
KEGGimmu:20184.
UCSCiuc007qpv.1. mouse. [Q5U5Q9-1]
uc007qpw.1. mouse. [Q5U5Q9-3]

Organism-specific databases

CTDi51720.
MGIiMGI:103185. Uimc1.

Phylogenomic databases

eggNOGiNOG72551.
GeneTreeiENSGT00390000007635.
HOGENOMiHOG000154772.
HOVERGENiHBG056783.
InParanoidiQ5U5Q9.
PhylomeDBiQ5U5Q9.

Miscellaneous databases

EvolutionaryTraceiQ5U5Q9.
NextBioi297717.
PROiQ5U5Q9.
SOURCEiSearch...

Gene expression databases

BgeeiQ5U5Q9.
CleanExiMM_UIMC1.
ExpressionAtlasiQ5U5Q9. baseline and differential.
GenevestigatoriQ5U5Q9.

Family and domain databases

InterProiIPR003903. Ubiquitin-int_motif.
[Graphical view]
SMARTiSM00726. UIM. 2 hits.
[Graphical view]
PROSITEiPS50330. UIM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Extraembryonic tissue, Kidney, Placenta and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and FVB/N.
    Tissue: Mammary cancer and Mammary tumor.
  3. "Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors."
    Seol W., Choi H.S., Moore D.D.
    Mol. Endocrinol. 9:72-85(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 148-727 (ISOFORM 1), INTERACTION WITH NR6A1.
    Tissue: Liver.
  4. "Tsp57: a novel gene induced during a specific stage of spermatogenesis."
    Kim Y.-S., Nakanishi G., Oudes A.J., Kim K.H., Wang H., Kilpatrick D.L., Jetten A.M.
    Biol. Reprod. 70:106-113(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSP57.
  5. "Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by tandem UIMs of RAP80."
    Sato Y., Yoshikawa A., Mimura H., Yamashita M., Yamagata A., Fukai S.
    EMBO J. 28:2461-2468(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 80-120 IN COMPLEX WITH DI-UBIQUITIN, UIM DOMAINS.

Entry informationi

Entry nameiUIMC1_MOUSE
AccessioniPrimary (citable) accession number: Q5U5Q9
Secondary accession number(s): Q3TU77
, Q60811, Q8C3Z8, Q8C719, Q8K1X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 5, 2009
Last modified: February 4, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.