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Q96RL1

- UIMC1_HUMAN

UniProt

Q96RL1 - UIMC1_HUMAN

Protein

BRCA1-A complex subunit RAP80

Gene

UIMC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (01 Mar 2005)
      Previous versions | rss
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    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 NCOR1.9 Publications

    GO - Molecular functioni

    1. histone binding Source: UniProtKB
    2. K63-linked polyubiquitin binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    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

    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
    Retinoid X receptor-interacting protein 110
    Ubiquitin interaction motif-containing protein 1
    Gene namesi
    Name:UIMC1
    Synonyms:RAP80, RXRIP110
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:30298. UIMC1.

    Subcellular locationi

    Nucleus 6 Publications
    Note: Localizes at sites of DNA damage at double-strand breaks (DSBs).

    GO - Cellular componenti

    1. BRCA1-A complex Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91K → A: Does not affect symoylation; when associated with A-19; A-31; A-52 and A-61. 1 Publication
    Mutagenesisi19 – 191K → A: Does not affect symoylation; when associated with A-9; A-31; A-52 and A-61. 1 Publication
    Mutagenesisi31 – 311K → A: Does not affect symoylation; when associated with A-9; A-19; A-52 and A-61. 1 Publication
    Mutagenesisi52 – 521K → A: Does not affect symoylation; when associated with A-9; A-19; A-31 and A-61. 1 Publication
    Mutagenesisi61 – 611K → A: Does not affect symoylation; when associated with A-9; A-19; A-31 and A-52. 1 Publication
    Mutagenesisi88 – 881A → G or S: Impairs localization to DNA damages sites; when associated with A-92; S-113 and A-117. 3 Publications
    Mutagenesisi92 – 921S → A: Impairs localization to DNA damages sites; when associated with S-88; S-113 and A-117. 2 Publications
    Mutagenesisi97 – 1037REVNSQE → AA: Impairs the selectivity for 'K-63'-linked ubiquitin.
    Mutagenesisi97 – 1037REVNSQE → AAAAAAA: Increases the selectivity for 'K-63'-linked ubiquitin.
    Mutagenesisi97 – 1037REVNSQE → AAAAAAAAA: Impairs the selectivity for 'K-63'-linked ubiquitin.
    Mutagenesisi101 – 1011S → A or E: Slightly impairs the selectivity for 'K-63'-linked ubiquitin. 1 Publication
    Mutagenesisi113 – 1131A → G or S: Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88; A-92 and A-117. 3 Publications
    Mutagenesisi117 – 1171S → A: Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88; A-92 and S-113. 2 Publications
    Mutagenesisi205 – 2051S → G: Abolishes phosphorylation at this position. 1 Publication
    Mutagenesisi508 – 5081C → A: Abolishes interaction with histone monoubiquitinated H2B without affecting the interaction with H2A. 1 Publication

    Organism-specific databases

    PharmGKBiPA162408624.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 719719BRCA1-A complex subunit RAP80PRO_0000097547Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441Phosphoserine3 Publications
    Modified residuei46 – 461Phosphoserine3 Publications
    Modified residuei101 – 1011Phosphoserine2 Publications
    Modified residuei140 – 1401Phosphoserine1 Publication
    Modified residuei205 – 2051Phosphoserine2 Publications
    Modified residuei402 – 4021Phosphoserine2 Publications
    Modified residuei419 – 4191Phosphoserine1 Publication
    Modified residuei627 – 6271Phosphoserine1 Publication
    Modified residuei653 – 6531Phosphoserine1 Publication
    Modified residuei677 – 6771Phosphoserine3 Publications

    Post-translational modificationi

    Sumoylated.1 Publication
    Phosphorylated upon DNA damage by ATM or ATR.10 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96RL1.
    PaxDbiQ96RL1.
    PRIDEiQ96RL1.

    PTM databases

    PhosphoSiteiQ96RL1.

    Expressioni

    Tissue specificityi

    Expressed in testis, ovary, thymus and heart. Expressed in germ cells of the testis.1 Publication

    Gene expression databases

    ArrayExpressiQ96RL1.
    BgeeiQ96RL1.
    CleanExiHS_UIMC1.
    GenevestigatoriQ96RL1.

    Organism-specific databases

    HPAiHPA037503.
    HPA037504.

    Interactioni

    Subunit structurei

    Interacts with TSP57 By similarity. 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, NR6A1 and UBE2I.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BLMP541322EBI-725300,EBI-621372
    BRCA1P383989EBI-725300,EBI-349905
    FAM175AQ6UWZ79EBI-725300,EBI-1263451

    Protein-protein interaction databases

    BioGridi119697. 57 interactions.
    DIPiDIP-29936N.
    IntActiQ96RL1. 47 interactions.
    MINTiMINT-1197441.

    Structurei

    Secondary structure

    1
    719
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi82 – 9413
    Helixi101 – 11919

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MKFNMR-A74-131[»]
    2MKGNMR-A74-131[»]
    2RR9NMR-C79-124[»]
    ProteinModelPortaliQ96RL1.
    SMRiQ96RL1. Positions 79-124.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96RL1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati79 – 9618UIM 1Add
    BLAST
    Repeati104 – 12421UIM 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 101101Necessary for transcriptional repressionAdd
    BLAST
    Regioni97 – 1037UIM-linker
    Regioni100 – 200101Necessary for interaction with NR6A1 N-terminusAdd
    BLAST
    Regioni270 – 400131AIRAdd
    BLAST
    Regioni400 – 500101Necessary for interaction with NR6A1 C-terminusAdd
    BLAST
    Regioni505 – 58278Zinc-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 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.1 Publication
    The Abraxas-interacting region (AIR) mediates the interaction with FAM175A/Abraxas.1 Publication

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG72551.
    HOVERGENiHBG056783.
    OrthoDBiEOG74XS6K.
    PhylomeDBiQ96RL1.
    TreeFamiTF336575.

    Family and domain databases

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

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96RL1-1) [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

    MPRRKKKVKE VSESRNLEKK DVETTSSVSV KRKRRLEDAF IVISDSDGEE    50
    PKEENGLQKT KTKQSNRAKC LAKRKIAQMT EEEQFALALK MSEQEAREVN 100
    SQEEEEEELL RKAIAESLNS CRPSDASATR SRPLATGPSS QSHQEKTTDS 150
    GLTEGIWQLV PPSLFKGSHI SQGNEAEERE EPWDHTEKTE EEPVSGSSGS 200
    WDQSSQPVFE NVNVKSFDRC TGHSAEHTQC GKPQESTGRG SAFLKAVQGS 250
    GDTSRHCLPT LADAKGLQDT GGTVNYFWGI PFCPDGVDPN QYTKVILCQL 300
    EVYQKSLKMA QRQLLNKKGF GEPVLPRPPS LIQNECGQGE QASEKNECIS 350
    EDMGDEDKEE RQESRASDWH SKTKDFQESS IKSLKEKLLL EEEPTTSHGQ 400
    SSQGIVEETS EEGNSVPASQ SVAALTSKRS LVLMPESSAE EITVCPETQL 450
    SSSETFDLER EVSPGSRDIL DGVRIIMADK EVGNKEDAEK EVAISTFSSS 500
    NQVSCPLCDQ CFPPTKIERH AMYCNGLMEE DTVLTRRQKE AKTKSDSGTA 550
    AQTSLDIDKN EKCYLCKSLV PFREYQCHVD SCLQLAKADQ GDGPEGSGRA 600
    CSTVEGKWQQ RLKNPKEKGH SEGRLLSFLE QSEHKTSDAD IKSSETGAFR 650
    VPSPGMEEAG CSREMQSSFT RRDLNESPVK SFVSISEATD CLVDFKKQVT 700
    VQPGSRTRTK AGRGRRRKF 719
    Length:719
    Mass (Da):79,727
    Last modified:March 1, 2005 - v2
    Checksum:i56B7699E42395861
    GO
    Isoform 2 (identifier: Q96RL1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         234-399: Missing.

    Show »
    Length:553
    Mass (Da):61,325
    Checksum:i61E2037D20BB900B
    GO
    Isoform 3 (identifier: Q96RL1-3) [UniParc]FASTAAdd to Basket

    Also known as: XHRIP110

    The sequence of this isoform differs from the canonical sequence as follows:
         1-78: Missing.

    Show »
    Length:641
    Mass (Da):70,744
    Checksum:i62A782DFDA0E30AD
    GO
    Isoform 4 (identifier: Q96RL1-4) [UniParc]FASTAAdd to Basket

    Also known as: X2HRIP110

    The sequence of this isoform differs from the canonical sequence as follows:
         1-370: Missing.
         371-400: SKTKDFQESSIKSLKEKLLLEEEPTTSHGQ → MLPLPDLDLWPLDRLPSPIKRKPQTLGSLK

    Show »
    Length:349
    Mass (Da):38,477
    Checksum:iF6A39455A3642247
    GO
    Isoform 5 (identifier: Q96RL1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         120-152: SCRPSDASATRSRPLATGPSSQSHQEKTTDSGL → VNMPCCKSLWRLISYIFDFCGVVVALGTSCSHL
         153-719: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:152
    Mass (Da):17,412
    Checksum:iC0CB4F0EBE4ADA49
    GO

    Sequence cautioni

    The sequence AAH06078.1 differs from that shown. Reason: Erroneous termination at position 386. Translated as Glu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti187 – 1871E → K in AAH06078. (PubMed:15489334)Curated
    Sequence conflicti192 – 1921E → G in BAG51153. (PubMed:14702039)Curated
    Sequence conflicti247 – 2471V → C in AAG59851. 1 PublicationCurated
    Sequence conflicti347 – 3471E → G in AAK61871. (PubMed:12080054)Curated
    Sequence conflicti518 – 5181E → G in AAK61871. (PubMed:12080054)Curated
    Sequence conflicti634 – 6341H → R in AAG59855. 1 PublicationCurated
    Sequence conflicti638 – 6381D → N in BAG51153. (PubMed:14702039)Curated
    Sequence conflicti694 – 6941D → V in AAG59855. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151R → W Common polymorphism not associated with susceptibility to breast cancer. 1 Publication
    Corresponds to variant rs13167812 [ dbSNP | Ensembl ].
    VAR_051469
    Natural varianti353 – 3531M → T Common polymorphism not associated with susceptibility to breast cancer. 1 Publication
    Corresponds to variant rs143282828 [ dbSNP | Ensembl ].
    VAR_055328
    Natural varianti435 – 4351P → L Common polymorphism not associated with susceptibility to breast cancer. 1 Publication
    Corresponds to variant rs3733876 [ dbSNP | Ensembl ].
    VAR_051470
    Natural varianti511 – 5111C → R Common polymorphism not associated with susceptibility to breast cancer. 1 Publication
    Corresponds to variant rs13360277 [ dbSNP | Ensembl ].
    VAR_051471
    Natural varianti596 – 5961G → E.
    Corresponds to variant rs10475633 [ dbSNP | Ensembl ].
    VAR_051472

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 370370Missing in isoform 4. 2 PublicationsVSP_012933Add
    BLAST
    Alternative sequencei1 – 7878Missing in isoform 3. 1 PublicationVSP_012932Add
    BLAST
    Alternative sequencei120 – 15233SCRPS…TDSGL → VNMPCCKSLWRLISYIFDFC GVVVALGTSCSHL in isoform 5. 1 PublicationVSP_037264Add
    BLAST
    Alternative sequencei153 – 719567Missing in isoform 5. 1 PublicationVSP_037265Add
    BLAST
    Alternative sequencei234 – 399166Missing in isoform 2. 1 PublicationVSP_012935Add
    BLAST
    Alternative sequencei371 – 40030SKTKD…TSHGQ → MLPLPDLDLWPLDRLPSPIK RKPQTLGSLK in isoform 4. 2 PublicationsVSP_012934Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF349313 mRNA. Translation: AAK61871.1.
    AF113538 mRNA. Translation: AAF14875.1.
    AF284749 mRNA. Translation: AAG59851.1.
    AF284753 mRNA. Translation: AAG59855.1.
    AK023044 mRNA. Translation: BAG51153.1.
    AK304794 mRNA. Translation: BAG65544.1.
    BX537376 mRNA. Translation: CAD97618.1.
    AC027318 Genomic DNA. No translation available.
    BC006078 mRNA. Translation: AAH06078.1. Different termination.
    BC032561 mRNA. Translation: AAH32561.1.
    CCDSiCCDS4408.1. [Q96RL1-1]
    RefSeqiNP_001186226.1. NM_001199297.1. [Q96RL1-1]
    NP_001186227.1. NM_001199298.1. [Q96RL1-1]
    NP_057374.3. NM_016290.4. [Q96RL1-1]
    XP_005265987.1. XM_005265930.1. [Q96RL1-1]
    XP_005265993.1. XM_005265936.1. [Q96RL1-4]
    XP_006714934.1. XM_006714871.1. [Q96RL1-1]
    XP_006714935.1. XM_006714872.1. [Q96RL1-2]
    XP_006714936.1. XM_006714873.1. [Q96RL1-2]
    UniGeneiHs.232721.

    Genome annotation databases

    EnsembliENST00000377227; ENSP00000366434; ENSG00000087206. [Q96RL1-1]
    ENST00000506128; ENSP00000427480; ENSG00000087206. [Q96RL1-2]
    ENST00000511320; ENSP00000421926; ENSG00000087206. [Q96RL1-1]
    GeneIDi51720.
    KEGGihsa:51720.
    UCSCiuc003mfd.2. human. [Q96RL1-4]
    uc011dfq.2. human. [Q96RL1-5]
    uc021yil.1. human. [Q96RL1-1]

    Polymorphism databases

    DMDMi60390957.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF349313 mRNA. Translation: AAK61871.1 .
    AF113538 mRNA. Translation: AAF14875.1 .
    AF284749 mRNA. Translation: AAG59851.1 .
    AF284753 mRNA. Translation: AAG59855.1 .
    AK023044 mRNA. Translation: BAG51153.1 .
    AK304794 mRNA. Translation: BAG65544.1 .
    BX537376 mRNA. Translation: CAD97618.1 .
    AC027318 Genomic DNA. No translation available.
    BC006078 mRNA. Translation: AAH06078.1 . Different termination.
    BC032561 mRNA. Translation: AAH32561.1 .
    CCDSi CCDS4408.1. [Q96RL1-1 ]
    RefSeqi NP_001186226.1. NM_001199297.1. [Q96RL1-1 ]
    NP_001186227.1. NM_001199298.1. [Q96RL1-1 ]
    NP_057374.3. NM_016290.4. [Q96RL1-1 ]
    XP_005265987.1. XM_005265930.1. [Q96RL1-1 ]
    XP_005265993.1. XM_005265936.1. [Q96RL1-4 ]
    XP_006714934.1. XM_006714871.1. [Q96RL1-1 ]
    XP_006714935.1. XM_006714872.1. [Q96RL1-2 ]
    XP_006714936.1. XM_006714873.1. [Q96RL1-2 ]
    UniGenei Hs.232721.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MKF NMR - A 74-131 [» ]
    2MKG NMR - A 74-131 [» ]
    2RR9 NMR - C 79-124 [» ]
    ProteinModelPortali Q96RL1.
    SMRi Q96RL1. Positions 79-124.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119697. 57 interactions.
    DIPi DIP-29936N.
    IntActi Q96RL1. 47 interactions.
    MINTi MINT-1197441.

    PTM databases

    PhosphoSitei Q96RL1.

    Polymorphism databases

    DMDMi 60390957.

    Proteomic databases

    MaxQBi Q96RL1.
    PaxDbi Q96RL1.
    PRIDEi Q96RL1.

    Protocols and materials databases

    DNASUi 51720.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377227 ; ENSP00000366434 ; ENSG00000087206 . [Q96RL1-1 ]
    ENST00000506128 ; ENSP00000427480 ; ENSG00000087206 . [Q96RL1-2 ]
    ENST00000511320 ; ENSP00000421926 ; ENSG00000087206 . [Q96RL1-1 ]
    GeneIDi 51720.
    KEGGi hsa:51720.
    UCSCi uc003mfd.2. human. [Q96RL1-4 ]
    uc011dfq.2. human. [Q96RL1-5 ]
    uc021yil.1. human. [Q96RL1-1 ]

    Organism-specific databases

    CTDi 51720.
    GeneCardsi GC05M176265.
    H-InvDB HIX0005450.
    HGNCi HGNC:30298. UIMC1.
    HPAi HPA037503.
    HPA037504.
    MIMi 609433. gene.
    neXtProti NX_Q96RL1.
    PharmGKBi PA162408624.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72551.
    HOVERGENi HBG056783.
    OrthoDBi EOG74XS6K.
    PhylomeDBi Q96RL1.
    TreeFami TF336575.

    Miscellaneous databases

    ChiTaRSi UIMC1. human.
    EvolutionaryTracei Q96RL1.
    GeneWikii UIMC1.
    GenomeRNAii 51720.
    NextBioi 55772.
    PROi Q96RL1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96RL1.
    Bgeei Q96RL1.
    CleanExi HS_UIMC1.
    Genevestigatori Q96RL1.

    Family and domain databases

    InterProi IPR003903. Ubiquitin-int_motif.
    [Graphical view ]
    SMARTi SM00726. UIM. 2 hits.
    [Graphical view ]
    PROSITEi PS50330. UIM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RAP80: a novel nuclear protein that interacts with the retinoid-related testis-associated receptor."
      Yan Z., Kim Y.-S., Jetten A.M.
      J. Biol. Chem. 277:32379-32388(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSCRIPTIONAL REPRESSION, INTERACTION WITH NR6A1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Testis.
    2. "A novel gene expressed in the human hypothalamus."
      Peng Y., Gu Y., Gu J., Huang Q., Fu S., Wu T., Dong H., Jin W., Fu G., Han Z., Chen Z., Wang Y.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      Tissue: Hypothalamus.
    3. Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
      Tissue: Hypothalamus.
    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 1 AND 5).
      Tissue: Teratocarcinoma and Uterus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Esophageal carcinoma.
    6. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
      Tissue: Ovary and Skin.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation."
      Yan J., Yang X.-P., Kim Y.-S., Joo J.H., Jetten A.M.
      Biochem. Biophys. Res. Commun. 362:132-138(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, INTERACTION WITH UBE2I, MUTAGENESIS OF LYS-9; LYS-19; LYS-31; LYS-52 AND LYS-61.
    10. "The ubiquitin-interacting motif containing protein RAP80 interacts with BRCA1 and functions in DNA damage repair response."
      Yan J., Kim Y.S., Yang X.-P., Li L.-P., Liao G., Xia F., Jetten A.M.
      Cancer Res. 67:6647-6656(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ALA-88 AND ALA-113, PHOSPHORYLATION AT SER-205 AND SER-402.
    11. "CCDC98 targets BRCA1 to DNA damage sites."
      Liu Z., Wu J., Yu X.
      Nat. Struct. Mol. Biol. 14:716-720(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FAM175A.
    12. "CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response."
      Kim H., Huang J., Chen J.
      Nat. Struct. Mol. Biol. 14:710-715(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAM175A.
    13. "Ubiquitin-interaction motifs of RAP80 are critical in its regulation of estrogen receptor alpha."
      Yan J., Kim Y.S., Yang X.-P., Albers M., Koegl M., Jetten A.M.
      Nucleic Acids Res. 35:1673-1686(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ESR1.
    14. "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: INTERACTION WITH FAM175A.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    16. "Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response."
      Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S., Elledge S.J.
      Science 316:1194-1198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140; SER-402 AND SER-419, MUTAGENESIS OF ALA-88; SER-92; ALA-113 AND SER-117.
    17. "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, SUBCELLULAR LOCATION, UBIQUITIN-BINDING, PHOSPHORYLATION AT SER-101.
    18. "Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response."
      Kim H., Chen J., Yu X.
      Science 316:1202-1205(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, UBIQUITIN-BINDING, PHOSPHORYLATION AT SER-101, MUTAGENESIS OF ALA-88; SER-92; ALA-113 AND SER-117.
    19. "RAP80 responds to DNA damage induced by both ionizing radiation and UV irradiation and is phosphorylated at Ser 205."
      Yan J., Yang X.-P., Kim Y.-S., Jetten A.M.
      Cancer Res. 68:4269-4276(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-205, MUTAGENESIS OF SER-205.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627; SER-653 AND SER-677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "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: IDENTIFICATION IN THE BRCA1-A COMPLEX.
    22. "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: IDENTIFICATION IN THE BRCA1-A COMPLEX, UBIQUITIN-BINDING, INTERACTION WITH FAM175A.
    23. "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, INTERACTION WITH FAM175A.
    24. "Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80."
      Sims J.J., Cohen R.E.
      Mol. Cell 33:775-783(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITIN-BINDING, DOMAIN UIM-LINKER, MUTAGENESIS OF 97-ARG--GLU-103 AND SER-101.
    25. "Histone ubiquitination associates with BRCA1-dependent DNA damage response."
      Wu J., Huen M.S.Y., Lu L.-Y., Ye L., Dou Y., Ljungman M., Chen J., Yu X.
      Mol. Cell. Biol. 29:849-860(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-508.
    26. "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.
    27. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    28. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-46 AND SER-677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks."
      Panier S., Ichijima Y., Fradet-Turcotte A., Leung C.C., Kaustov L., Arrowsmith C.H., Durocher D.
      Mol. Cell 47:383-395(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITIN-BINDING, LR MOTIF.
    31. "Analysis of the genes coding for the BRCA1-interacting proteins, RAP80 and Abraxas (CCDC98), in high-risk, non-BRCA1/2, multiethnic breast cancer cases."
      Novak D.J., Sabbaghian N., Maillet P., Chappuis P.O., Foulkes W.D., Tischkowitz M.
      Breast Cancer Res. Treat. 117:453-459(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TRP-15; THR-353; LEU-435 AND ARG-511.

    Entry informationi

    Entry nameiUIMC1_HUMAN
    AccessioniPrimary (citable) accession number: Q96RL1
    Secondary accession number(s): A8MSA1
    , B3KMZ1, B4E3N2, Q5XKQ1, Q7Z3W7, Q8N5B9, Q9BZR1, Q9BZR5, Q9UHX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: March 1, 2005
    Last modified: October 1, 2014
    This is version 107 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3