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Q96RL1 (UIMC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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
Retinoid X receptor-interacting protein 110
Ubiquitin interaction motif-containing protein 1
Gene names
Name:UIMC1
Synonyms:RAP80, RXRIP110
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length719 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. Ref.1 Ref.10 Ref.11 Ref.16 Ref.17 Ref.18 Ref.23 Ref.25 Ref.26

Subunit structure

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. Ref.1 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.21 Ref.22 Ref.23

Subcellular location

Nucleus. Note: Localizes at sites of DNA damage at double-strand breaks (DSBs). Ref.1 Ref.10 Ref.11 Ref.16 Ref.17 Ref.18

Tissue specificity

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

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. Ref.24

The Abraxas-interacting region (AIR) mediates the interaction with FAM175A/Abraxas. Ref.24

Post-translational modification

Sumoylated. Ref.9

Phosphorylated upon DNA damage by ATM or ATR. Ref.10 Ref.16 Ref.17 Ref.18 Ref.19

Sequence similarities

Belongs to the RAP80 family.

Contains 2 UIM (ubiquitin-interacting motif) repeats.

Sequence caution

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

Ontologies

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

Inferred from mutant phenotype Ref.16Ref.17Ref.18Ref.11Ref.23. Source: UniProtKB

double-strand break repair

Inferred from mutant phenotype Ref.16Ref.17Ref.18Ref.11Ref.23. Source: UniProtKB

histone H2A K63-linked deubiquitination

Inferred from mutant phenotype Ref.26. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: HGNC

positive regulation of DNA repair

Inferred from mutant phenotype Ref.16Ref.17Ref.18Ref.11Ref.23. Source: UniProtKB

response to ionizing radiation

Inferred from mutant phenotype Ref.16Ref.17Ref.18Ref.11Ref.23. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentBRCA1-A complex

Inferred from direct assay Ref.16Ref.17Ref.18Ref.21Ref.23Ref.22. Source: UniProtKB

nucleus

Inferred from direct assay Ref.16Ref.17Ref.18Ref.11. Source: UniProtKB

   Molecular_functionK63-linked polyubiquitin binding

Inferred from direct assay Ref.17Ref.18Ref.22Ref.30. Source: UniProtKB

histone binding

Inferred from direct assay Ref.17Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12954732Ref.16Ref.11Ref.23Ref.22. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96RL1-1)

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: Q96RL1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     234-399: Missing.
Isoform 3 (identifier: Q96RL1-3)

Also known as: XHRIP110;

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.
Isoform 4 (identifier: Q96RL1-4)

Also known as: X2HRIP110;

The sequence of this isoform differs from the canonical sequence as follows:
     1-370: Missing.
     371-400: SKTKDFQESSIKSLKEKLLLEEEPTTSHGQ → MLPLPDLDLWPLDRLPSPIKRKPQTLGSLK
Isoform 5 (identifier: Q96RL1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     120-152: SCRPSDASATRSRPLATGPSSQSHQEKTTDSGL → VNMPCCKSLWRLISYIFDFCGVVVALGTSCSHL
     153-719: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 719719BRCA1-A complex subunit RAP80
PRO_0000097547

Regions

Repeat79 – 9618UIM 1
Repeat104 – 12421UIM 2
Region1 – 101101Necessary for transcriptional repression
Region97 – 1037UIM-linker
Region100 – 200101Necessary for interaction with NR6A1 N-terminus
Region270 – 400131AIR
Region400 – 500101Necessary for interaction with NR6A1 C-terminus
Region505 – 58278Zinc-finger-like region
Motif60 – 7819LR motif
Compositional bias81 – 10828Glu-rich

Amino acid modifications

Modified residue441Phosphoserine Ref.8 Ref.27 Ref.28
Modified residue461Phosphoserine Ref.8 Ref.27 Ref.28
Modified residue1011Phosphoserine Ref.17 Ref.18
Modified residue1401Phosphoserine Ref.16
Modified residue2051Phosphoserine Ref.10 Ref.19
Modified residue4021Phosphoserine Ref.10 Ref.16
Modified residue4191Phosphoserine Ref.16
Modified residue6271Phosphoserine Ref.20
Modified residue6531Phosphoserine Ref.20
Modified residue6771Phosphoserine Ref.20 Ref.28 Ref.29

Natural variations

Alternative sequence1 – 370370Missing in isoform 4.
VSP_012933
Alternative sequence1 – 7878Missing in isoform 3.
VSP_012932
Alternative sequence120 – 15233SCRPS…TDSGL → VNMPCCKSLWRLISYIFDFC GVVVALGTSCSHL in isoform 5.
VSP_037264
Alternative sequence153 – 719567Missing in isoform 5.
VSP_037265
Alternative sequence234 – 399166Missing in isoform 2.
VSP_012935
Alternative sequence371 – 40030SKTKD…TSHGQ → MLPLPDLDLWPLDRLPSPIK RKPQTLGSLK in isoform 4.
VSP_012934
Natural variant151R → W Common polymorphism not associated with susceptibility to breast cancer. Ref.31
Corresponds to variant rs13167812 [ dbSNP | Ensembl ].
VAR_051469
Natural variant3531M → T Common polymorphism not associated with susceptibility to breast cancer. Ref.31
Corresponds to variant rs143282828 [ dbSNP | Ensembl ].
VAR_055328
Natural variant4351P → L Common polymorphism not associated with susceptibility to breast cancer. Ref.31
Corresponds to variant rs3733876 [ dbSNP | Ensembl ].
VAR_051470
Natural variant5111C → R Common polymorphism not associated with susceptibility to breast cancer. Ref.31
Corresponds to variant rs13360277 [ dbSNP | Ensembl ].
VAR_051471
Natural variant5961G → E.
Corresponds to variant rs10475633 [ dbSNP | Ensembl ].
VAR_051472

Experimental info

Mutagenesis91K → A: Does not affect symoylation; when associated with A-19; A-31; A-52 and A-61. Ref.9
Mutagenesis191K → A: Does not affect symoylation; when associated with A-9; A-31; A-52 and A-61. Ref.9
Mutagenesis311K → A: Does not affect symoylation; when associated with A-9; A-19; A-52 and A-61. Ref.9
Mutagenesis521K → A: Does not affect symoylation; when associated with A-9; A-19; A-31 and A-61. Ref.9
Mutagenesis611K → A: Does not affect symoylation; when associated with A-9; A-19; A-31 and A-52. Ref.9
Mutagenesis881A → G or S: Impairs localization to DNA damages sites; when associated with A-92; S-113 and A-117. Ref.10 Ref.16 Ref.18
Mutagenesis921S → A: Impairs localization to DNA damages sites; when associated with S-88; S-113 and A-117. Ref.16 Ref.18
Mutagenesis97 – 1037REVNSQE → AA: Impairs the selectivity for 'K-63'-linked ubiquitin. Ref.24
Mutagenesis97 – 1037REVNSQE → AAAAAAA: Increases the selectivity for 'K-63'-linked ubiquitin. Ref.24
Mutagenesis97 – 1037REVNSQE → AAAAAAAAA: Impairs the selectivity for 'K-63'-linked ubiquitin. Ref.24
Mutagenesis1011S → A or E: Slightly impairs the selectivity for 'K-63'-linked ubiquitin. Ref.24
Mutagenesis1131A → G or S: Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88; A-92 and A-117. Ref.10 Ref.16 Ref.18
Mutagenesis1171S → A: Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88; A-92 and S-113. Ref.16 Ref.18
Mutagenesis2051S → G: Abolishes phosphorylation at this position. Ref.19
Mutagenesis5081C → A: Abolishes interaction with histone monoubiquitinated H2B without affecting the interaction with H2A. Ref.25
Sequence conflict1871E → K in AAH06078. Ref.7
Sequence conflict1921E → G in BAG51153. Ref.4
Sequence conflict2471V → C in AAG59851. Ref.3
Sequence conflict3471E → G in AAK61871. Ref.1
Sequence conflict5181E → G in AAK61871. Ref.1
Sequence conflict6341H → R in AAG59855. Ref.3
Sequence conflict6381D → N in BAG51153. Ref.4
Sequence conflict6941D → V in AAG59855. Ref.3

Secondary structure

..... 719
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2005. Version 2.
Checksum: 56B7699E42395861

FASTA71979,727
        10         20         30         40         50         60 
MPRRKKKVKE VSESRNLEKK DVETTSSVSV KRKRRLEDAF IVISDSDGEE PKEENGLQKT 

        70         80         90        100        110        120 
KTKQSNRAKC LAKRKIAQMT EEEQFALALK MSEQEAREVN SQEEEEEELL RKAIAESLNS 

       130        140        150        160        170        180 
CRPSDASATR SRPLATGPSS QSHQEKTTDS GLTEGIWQLV PPSLFKGSHI SQGNEAEERE 

       190        200        210        220        230        240 
EPWDHTEKTE EEPVSGSSGS WDQSSQPVFE NVNVKSFDRC TGHSAEHTQC GKPQESTGRG 

       250        260        270        280        290        300 
SAFLKAVQGS GDTSRHCLPT LADAKGLQDT GGTVNYFWGI PFCPDGVDPN QYTKVILCQL 

       310        320        330        340        350        360 
EVYQKSLKMA QRQLLNKKGF GEPVLPRPPS LIQNECGQGE QASEKNECIS EDMGDEDKEE 

       370        380        390        400        410        420 
RQESRASDWH SKTKDFQESS IKSLKEKLLL EEEPTTSHGQ SSQGIVEETS EEGNSVPASQ 

       430        440        450        460        470        480 
SVAALTSKRS LVLMPESSAE EITVCPETQL SSSETFDLER EVSPGSRDIL DGVRIIMADK 

       490        500        510        520        530        540 
EVGNKEDAEK EVAISTFSSS NQVSCPLCDQ CFPPTKIERH AMYCNGLMEE DTVLTRRQKE 

       550        560        570        580        590        600 
AKTKSDSGTA AQTSLDIDKN EKCYLCKSLV PFREYQCHVD SCLQLAKADQ GDGPEGSGRA 

       610        620        630        640        650        660 
CSTVEGKWQQ RLKNPKEKGH SEGRLLSFLE QSEHKTSDAD IKSSETGAFR VPSPGMEEAG 

       670        680        690        700        710 
CSREMQSSFT RRDLNESPVK SFVSISEATD CLVDFKKQVT VQPGSRTRTK AGRGRRRKF 

« Hide

Isoform 2 [UniParc].

Checksum: 61E2037D20BB900B
Show »

FASTA55361,325
Isoform 3 (XHRIP110) [UniParc].

Checksum: 62A782DFDA0E30AD
Show »

FASTA64170,744
Isoform 4 (X2HRIP110) [UniParc].

Checksum: F6A39455A3642247
Show »

FASTA34938,477
Isoform 5 [UniParc].

Checksum: C0CB4F0EBE4ADA49
Show »

FASTA15217,412

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4408.1. [Q96RL1-1]
RefSeqNP_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]
UniGeneHs.232721.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MKFNMR-A74-131[»]
2MKGNMR-A74-131[»]
2RR9NMR-C79-124[»]
ProteinModelPortalQ96RL1.
SMRQ96RL1. Positions 79-124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119697. 57 interactions.
DIPDIP-29936N.
IntActQ96RL1. 46 interactions.
MINTMINT-1197441.

PTM databases

PhosphoSiteQ96RL1.

Polymorphism databases

DMDM60390957.

Proteomic databases

MaxQBQ96RL1.
PaxDbQ96RL1.
PRIDEQ96RL1.

Protocols and materials databases

DNASU51720.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377227; ENSP00000366434; ENSG00000087206. [Q96RL1-1]
ENST00000506128; ENSP00000427480; ENSG00000087206. [Q96RL1-2]
ENST00000511320; ENSP00000421926; ENSG00000087206. [Q96RL1-1]
GeneID51720.
KEGGhsa:51720.
UCSCuc003mfd.2. human. [Q96RL1-4]
uc011dfq.2. human. [Q96RL1-5]
uc021yil.1. human. [Q96RL1-1]

Organism-specific databases

CTD51720.
GeneCardsGC05M176265.
H-InvDBHIX0005450.
HGNCHGNC:30298. UIMC1.
HPAHPA037503.
HPA037504.
MIM609433. gene.
neXtProtNX_Q96RL1.
PharmGKBPA162408624.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72551.
HOVERGENHBG056783.
OrthoDBEOG74XS6K.
PhylomeDBQ96RL1.
TreeFamTF336575.

Gene expression databases

ArrayExpressQ96RL1.
BgeeQ96RL1.
CleanExHS_UIMC1.
GenevestigatorQ96RL1.

Family and domain databases

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

Other

ChiTaRSUIMC1. human.
EvolutionaryTraceQ96RL1.
GeneWikiUIMC1.
GenomeRNAi51720.
NextBio55772.
PROQ96RL1.
SOURCESearch...

Entry information

Entry nameUIMC1_HUMAN
AccessionPrimary (citable) accession number: Q96RL1
Secondary accession number(s): A8MSA1 expand/collapse secondary AC list , B3KMZ1, B4E3N2, Q5XKQ1, Q7Z3W7, Q8N5B9, Q9BZR1, Q9BZR5, Q9UHX7
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM