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Q96RL1

- UIMC1_HUMAN

UniProt

Q96RL1 - UIMC1_HUMAN

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Protein

BRCA1-A complex subunit RAP80

Gene
UIMC1, RAP80, RXRIP110
Organism
Homo sapiens (Human)
Status
Reviewed - 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 NCOR1.9 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
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
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
Note: Localizes at sites of DNA damage at double-strand breaks (DSBs).6 Publications

GO - Cellular componenti

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

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. 1 Publication
Mutagenesisi97 – 1037REVNSQE → AAAAAAA: Increases the selectivity for 'K-63'-linked ubiquitin. 1 Publication
Mutagenesisi97 – 1037REVNSQE → AAAAAAAAA: Impairs the selectivity for 'K-63'-linked ubiquitin. 1 Publication
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.5 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.11 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. 46 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.

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.

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.

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. VSP_012933Add
BLAST
Alternative sequencei1 – 7878Missing in isoform 3. VSP_012932Add
BLAST
Alternative sequencei120 – 15233SCRPS…TDSGL → VNMPCCKSLWRLISYIFDFC GVVVALGTSCSHL in isoform 5. VSP_037264Add
BLAST
Alternative sequencei153 – 719567Missing in isoform 5. VSP_037265Add
BLAST
Alternative sequencei234 – 399166Missing in isoform 2. VSP_012935Add
BLAST
Alternative sequencei371 – 40030SKTKD…TSHGQ → MLPLPDLDLWPLDRLPSPIK RKPQTLGSLK in isoform 4. VSP_012934Add
BLAST

Sequence conflict

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

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. 46 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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 106 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

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