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Q5U5Q9 (UIMC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BRCA1-A complex subunit RAP80
Alternative name(s):
Receptor-associated protein 80
Ubiquitin interaction motif-containing protein 1
Gene names
Name:Uimc1
Synonyms:Rap80, Rip110, Rxrip110
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length727 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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. Interacts with ESR1 and UBE2I By similarity. Interacts with NR6A1 and TSP57. Ref.3 Ref.4

Subcellular location

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

Domain

The UIM-linker region between the 2 UIM repeats determines the selectivity for 'Lys-63'-linked ubiquitin. The length of the linker is important. The linker reduces the flexibility between the UIM repeats and promotes high-affinity and linkage-selective interactions By similarity.

The Abraxas-interacting region (AIR) mediates the interaction with FAM175A/Abraxas By similarity.

Post-translational modification

Sumoylated By similarity.

Phosphorylated upon DNA damage by ATM or ATR By similarity.

Sequence similarities

Belongs to the RAP80 family.

Contains 2 UIM (ubiquitin-interacting motif) repeats.

Sequence caution

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionChromatin regulator
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2 DNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

histone H2A K63-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity PubMed 12080054. Source: HGNC

positive regulation of DNA repair

Inferred from sequence or structural similarity. Source: UniProtKB

response to ionizing radiation

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentBRCA1-A complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionK63-linked polyubiquitin binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

retinoid X receptor binding

Inferred from direct assay Ref.3. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UbcP629912EBI-7068640,EBI-413074

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5U5Q9-1)

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 2 (identifier: Q5U5Q9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     401-406: SSQGLF → HCSFDQ
     407-727: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5U5Q9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     120-400: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 727727BRCA1-A complex subunit RAP80
PRO_0000097548

Regions

Repeat79 – 9618UIM 1
Repeat104 – 12421UIM 2
Region1 – 101101Necessary for transcriptional repression By similarity
Region97 – 1037UIM-linker
Region100 – 200101Necessary for interaction with NR6A1 N-terminus By similarity
Region270 – 400131AIR
Region400 – 508109Necessary for interaction with NR6A1 C-terminus By similarity
Region513 – 59078Zinc-finger-like region
Motif60 – 7819LR motif
Compositional bias81 – 10828Glu-rich

Amino acid modifications

Modified residue441Phosphoserine By similarity
Modified residue461Phosphoserine By similarity
Modified residue1401Phosphoserine By similarity
Modified residue2051Phosphoserine By similarity
Modified residue4021Phosphoserine By similarity
Modified residue6371Phosphoserine By similarity
Modified residue6651Phosphoserine By similarity
Modified residue6891Phosphoserine By similarity

Natural variations

Alternative sequence120 – 400281Missing in isoform 3.
VSP_037266
Alternative sequence401 – 4066SSQGLF → HCSFDQ in isoform 2.
VSP_037267
Alternative sequence407 – 727321Missing in isoform 2.
VSP_037268

Experimental info

Sequence conflict3771Q → R in BAC38875. Ref.1
Sequence conflict4501I → T in BAC35106. Ref.1
Sequence conflict4501I → T in BAC38875. Ref.1
Sequence conflict4501I → T in BAE36094. Ref.1
Sequence conflict5541D → G in AAH40808. Ref.2
Sequence conflict7221G → E in AAC52167. Ref.3

Secondary structure

... 727
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: B753BF61180D63ED

FASTA72781,478
        10         20         30         40         50         60 
MPRRKKKIKE ASESQNLEKK DLETSSCVSI KKKRRLEDLL IVISDSDGEE TKEENGLQKT 

        70         80         90        100        110        120 
KTKQSNRSKC LAKRKVAHMS EEEQFALALK MSEQEAREVN NQEEKEEELL RKAIAESLNS 

       130        140        150        160        170        180 
CWSSAASATR SRPLAAELSS HSHQENTKDS GTTEGVWQLV PPSLCKGSHV SQGNEAEQRK 

       190        200        210        220        230        240 
EPWDHNENTE EEPVSGSSGS WDQSSQPVFE NENVKCFDRC TGHLAEHTQC GKPQESTGSG 

       250        260        270        280        290        300 
YAFSKAVQGR GDTSRQCLPI PADTKGLQDT GGTVHYYWGI PFCPAGVDPN QYTNVILCQL 

       310        320        330        340        350        360 
EVYQKSLKMA QRQLVKKRGF GEPVLPRPPF LIQNECGQED QTSDKNEGIS EDMGDEAKEE 

       370        380        390        400        410        420 
RQESRASVWH SETKDFQKSP IKSLKQKLLL EEEPTTSRGQ SSQGLFVEET SEEGLKSSEG 

       430        440        450        460        470        480 
DNSVPTTQSI AALTSKRSLV LMPESSAEEI TVCPETQLSF LEPLDLNRED SPDSRELPIE 

       490        500        510        520        530        540 
VRMAVGDKQV ANREDCMKEN PPPAVSSSTR VSCPLCNQDF PPTKIEQHAM YCNGLMEQET 

       550        560        570        580        590        600 
VLTRRRREAK NKSDGRTAAQ PALDANRKEK CYLCKSLVPL GEYQCHVEAC LQLAKVDRED 

       610        620        630        640        650        660 
GIEGTRRPRV CAPVEGKQQQ RLKKSKDKGH SQGRLLSLLE QSEHRTTGVE KKPKYSEVRT 

       670        680        690        700        710        720 
FRMPSPEVEE ASCSREMQST LSQLNLNESP IKSFVPVSEA TNCLVDFKEQ FAFRSRTKSG 


RGRRRKS 

« Hide

Isoform 2 [UniParc].

Checksum: 904F4FDD0F27ECB0
Show »

FASTA40645,575
Isoform 3 [UniParc].

Checksum: 4E76F9B20CF84D80
Show »

FASTA44650,382

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS36671.1. [Q5U5Q9-1]
RefSeqNP_035437.1. NM_011307.2.
XP_006517229.1. XM_006517166.1.
XP_006517231.1. XM_006517168.1.
UniGeneMm.259301.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3A1QX-ray2.20C/F80-120[»]
ProteinModelPortalQ5U5Q9.
SMRQ5U5Q9. Positions 80-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203041. 4 interactions.
IntActQ5U5Q9. 2 interactions.
MINTMINT-4117130.

PTM databases

PhosphoSiteQ5U5Q9.

Proteomic databases

PaxDbQ5U5Q9.
PRIDEQ5U5Q9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026997; ENSMUSP00000026997; ENSMUSG00000025878.
ENSMUST00000099496; ENSMUSP00000097095; ENSMUSG00000025878.
GeneID20184.
KEGGmmu:20184.
UCSCuc007qpv.1. mouse. [Q5U5Q9-1]
uc007qpw.1. mouse. [Q5U5Q9-3]

Organism-specific databases

CTD51720.
MGIMGI:103185. Uimc1.

Phylogenomic databases

eggNOGNOG72551.
GeneTreeENSGT00390000007635.
HOGENOMHOG000154772.
HOVERGENHBG056783.
InParanoidQ8C3Z8.
PhylomeDBQ5U5Q9.

Gene expression databases

ArrayExpressQ5U5Q9.
BgeeQ5U5Q9.
CleanExMM_UIMC1.
GenevestigatorQ5U5Q9.

Family and domain databases

InterProIPR003903. Ubiquitin-int_motif.
[Graphical view]
SMARTSM00726. UIM. 2 hits.
[Graphical view]
PROSITEPS50330. UIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5U5Q9.
NextBio297717.
PROQ5U5Q9.
SOURCESearch...

Entry information

Entry nameUIMC1_MOUSE
AccessionPrimary (citable) accession number: Q5U5Q9
Secondary accession number(s): Q3TU77 expand/collapse secondary AC list , Q60811, Q8C3Z8, Q8C719, Q8K1X7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot