Reviewed, UniProtKB/Swiss-Prot Q96RL1 (UIMC1_HUMAN)

Names and origin

Protein names

Recommended name:
    BRCA1-A complex subunit RAP80
Alternative name(s):
    Receptor-associated protein 80
    Ubiquitin interaction motif-containing protein 1
    Retinoid X receptor-interacting protein 110

Gene names

Name:	UIMC1
Synonyms:	RAP80, RXRIP110

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	719 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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 MERIT40/NBA1. In the BRCA1-A complex, interacts directly with FAM175A/Abraxas. Interacts with ESR1, NR6A1 and UBE2I.
Subcellular location	Nucleus. Note: Localizes at sites of DNA damage at double-strand breaks (DSBs). Ref.1
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. The Abraxas-interacting region (AIR) mediates the interaction with FAM175A/Abraxas.
Post-translational modification	Sumoylated. Phosphorylated upon DNA damage by ATM or ATR.
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 process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Chromatin regulator
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	G2/M transition DNA damage checkpoint Ref.12 Ref.17 Ref.18 Ref.19 Ref.24 Inferred from mutant phenotype. Source: UniProtKB double-strand break repair Ref.12 Ref.17 Ref.18 Ref.19 Ref.24 Inferred from mutant phenotype. Source: UniProtKB negative regulation of transcription Ref.1 Inferred from direct assay. Source: HGNC positive regulation of DNA repair Ref.12 Ref.17 Ref.18 Ref.19 Ref.24 Inferred from mutant phenotype. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to ionizing radiation Ref.12 Ref.17 Ref.18 Ref.19 Ref.24 Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	BRCA1-A complex Ref.17 Ref.18 Ref.19 Ref.22 Ref.23 Ref.24 Inferred from direct assay. Source: UniProtKB
Molecular function	K63-linked polyubiquitin binding Ref.18 Ref.19 Ref.23 Inferred from direct assay. Source: UniProtKB histone binding Ref.18 Ref.19 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRCA1	P38398	4	EBI-725300,EBI-349905
FAM175A	Q6UWZ7	3	EBI-725300,EBI-1263451

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 719	719	BRCA1-A complex subunit RAP80		PRO_0000097547
Regions
	Repeat	79 – 96	18	UIM 1
	Repeat	104 – 124	21	UIM 2
	Region	1 – 101	101	Necessary for transcriptional repression
	Region	97 – 103	7	UIM-linker
	Region	100 – 200	101	Necessary for interaction with NR6A1 N-terminus
	Region	270 – 400	131	AIR
	Region	400 – 500	101	Necessary for interaction with NR6A1 C-terminus
	Region	505 – 582	78	Zinc-finger-like region
	Compositional bias	81 – 108	28	Glu-rich
Amino acid modifications
	Modified residue	44	1	Phosphoserine Ref.9 Ref.21
	Modified residue	46	1	Phosphoserine Ref.9 Ref.21
	Modified residue	101	1	Phosphoserine
	Modified residue	140	1	Phosphoserine Ref.16
	Modified residue	205	1	Phosphoserine
	Modified residue	402	1	Phosphoserine Ref.16
	Modified residue	415	1	Phosphoserine Ref.16
	Modified residue	419	1	Phosphoserine Ref.16
	Modified residue	597	1	Phosphoserine Ref.8
	Modified residue	627	1	Phosphoserine Ref.21
	Modified residue	653	1	Phosphoserine Ref.8 Ref.21
	Modified residue	677	1	Phosphoserine Ref.8 Ref.21
Natural variations
	Alternative sequence	1 – 370	370	Missing in isoform 4.		VSP_012933
	Alternative sequence	1 – 78	78	Missing in isoform 3.		VSP_012932
	Alternative sequence	120 – 152	33	SCRPS…TDSGL → VNMPCCKSLWRLISYIFDFC GVVVALGTSCSHL in isoform 5.		VSP_037264
	Alternative sequence	153 – 719	567	Missing in isoform 5.		VSP_037265
	Alternative sequence	234 – 399	166	Missing in isoform 2.		VSP_012935
	Alternative sequence	371 – 400	30	SKTKD…TSHGQ → MLPLPDLDLWPLDRLPSPIK RKPQTLGSLK in isoform 4.		VSP_012934
	Natural variant	15	1	R → W Common polymorphism not associated with susceptibility to breast cancer. dbSNP rs13167812.		VAR_051469
	Natural variant	353	1	M → T Common polymorphism not associated with susceptibility to breast cancer.		VAR_055328
	Natural variant	435	1	P → L Common polymorphism not associated with susceptibility to breast cancer. dbSNP rs3733876.		VAR_051470
	Natural variant	511	1	C → R Common polymorphism not associated with susceptibility to breast cancer. dbSNP rs13360277.		VAR_051471
	Natural variant	596	1	G → E: dbSNP rs10475633.		VAR_051472
Experimental info
	Mutagenesis	9	1	K → A: Does not affect symoylation; when associated with A-19, A-31, A-52 and A-61.
	Mutagenesis	19	1	K → A: Does not affect symoylation; when associated with A-9, A-31, A-52 and A-61.
	Mutagenesis	31	1	K → A: Does not affect symoylation; when associated with A-9, A-19, A-52 and A-61.
	Mutagenesis	52	1	K → A: Does not affect symoylation; when associated with A-9, A-19, A-31 and A-61.
	Mutagenesis	61	1	K → A: Does not affect symoylation; when associated with A-9, A-19, A-31 and A-52.
	Mutagenesis	88	1	A → G or S: Impairs localization to DNA damages sites; when associated with A-92, S-113 and A-117.
	Mutagenesis	92	1	S → A: Impairs localization to DNA damages sites; when associated with S-88, S-113 and A-117.
	Mutagenesis	97 – 103	7	REVNSQE → AA: Impairs the selectivity for 'Lys-63'-linked ubiquitin.
	Mutagenesis	97 – 103	7	REVNSQE → AAAAAAA: Increases the selectivity for 'Lys-63'-linked ubiquitin.
	Mutagenesis	97 – 103	7	REVNSQE → AAAAAAAAA: Impairs the selectivity for 'Lys-63'-linked ubiquitin.
	Mutagenesis	101	1	S → A or E: Slightly impairs the selectivity for 'Lys-63'-linked ubiquitin.
	Mutagenesis	113	1	A → G or S: Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88, A-92 and A-117.
	Mutagenesis	117	1	S → A: Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88, A-92 and S-113.
	Mutagenesis	205	1	S → G: Abolishes phosphorylation at this position.
	Mutagenesis	508	1	C → A: Abolishes interaction with histone monoubiquitinated H2B without affecting the interaction with H2A.
	Sequence conflict	187	1	E → K in AAH06078. Ref.7
	Sequence conflict	192	1	E → G in BAG51153. Ref.4
	Sequence conflict	247	1	V → C in AAG59851. Ref.3
	Sequence conflict	347	1	E → G in AAK61871. Ref.1
	Sequence conflict	518	1	E → G in AAK61871. Ref.1
	Sequence conflict	634	1	H → R in AAG59855. Ref.3
	Sequence conflict	638	1	D → N in BAG51153. Ref.4
	Sequence conflict	694	1	D → V in AAG59855. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2005. Version 2. Checksum: 56B7699E42395861	FASTA	719	79,727
	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
	Isoform 2. Checksum: 61E2037D20BB900B	FASTA	553	61,325
	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 GKPQSSQGIV 250 260 270 280 290 300 EETSEEGNSV PASQSVAALT SKRSLVLMPE SSAEEITVCP ETQLSSSETF DLEREVSPGS 310 320 330 340 350 360 RDILDGVRII MADKEVGNKE DAEKEVAIST FSSSNQVSCP LCDQCFPPTK IERHAMYCNG 370 380 390 400 410 420 LMEEDTVLTR RQKEAKTKSD SGTAAQTSLD IDKNEKCYLC KSLVPFREYQ CHVDSCLQLA 430 440 450 460 470 480 KADQGDGPEG SGRACSTVEG KWQQRLKNPK EKGHSEGRLL SFLEQSEHKT SDADIKSSET 490 500 510 520 530 540 GAFRVPSPGM EEAGCSREMQ SSFTRRDLNE SPVKSFVSIS EATDCLVDFK KQVTVQPGSR 550 TRTKAGRGRR RKF
	Isoform 3 (XHRIP110). Checksum: 62A782DFDA0E30AD	FASTA	641	70,744
	10 20 30 40 50 60 MTEEEQFALA LKMSEQEARE VNSQEEEEEE LLRKAIAESL NSCRPSDASA TRSRPLATGP 70 80 90 100 110 120 SSQSHQEKTT DSGLTEGIWQ LVPPSLFKGS HISQGNEAEE REEPWDHTEK TEEEPVSGSS 130 140 150 160 170 180 GSWDQSSQPV FENVNVKSFD RCTGHSAEHT QCGKPQESTG RGSAFLKAVQ GSGDTSRHCL 190 200 210 220 230 240 PTLADAKGLQ DTGGTVNYFW GIPFCPDGVD PNQYTKVILC QLEVYQKSLK MAQRQLLNKK 250 260 270 280 290 300 GFGEPVLPRP PSLIQNECGQ GEQASEKNEC ISEDMGDEDK EERQESRASD WHSKTKDFQE 310 320 330 340 350 360 SSIKSLKEKL LLEEEPTTSH GQSSQGIVEE TSEEGNSVPA SQSVAALTSK RSLVLMPESS 370 380 390 400 410 420 AEEITVCPET QLSSSETFDL EREVSPGSRD ILDGVRIIMA DKEVGNKEDA EKEVAISTFS 430 440 450 460 470 480 SSNQVSCPLC DQCFPPTKIE RHAMYCNGLM EEDTVLTRRQ KEAKTKSDSG TAAQTSLDID 490 500 510 520 530 540 KNEKCYLCKS LVPFREYQCH VDSCLQLAKA DQGDGPEGSG RACSTVEGKW QQRLKNPKEK 550 560 570 580 590 600 GHSEGRLLSF LEQSEHKTSD ADIKSSETGA FRVPSPGMEE AGCSREMQSS FTRRDLNESP 610 620 630 640 VKSFVSISEA TDCLVDFKKQ VTVQPGSRTR TKAGRGRRRK F
	Isoform 4 (X2HRIP110). Checksum: F6A39455A3642247	FASTA	349	38,477
	10 20 30 40 50 60 MLPLPDLDLW PLDRLPSPIK RKPQTLGSLK SSQGIVEETS EEGNSVPASQ SVAALTSKRS 70 80 90 100 110 120 LVLMPESSAE EITVCPETQL SSSETFDLER EVSPGSRDIL DGVRIIMADK EVGNKEDAEK 130 140 150 160 170 180 EVAISTFSSS NQVSCPLCDQ CFPPTKIERH AMYCNGLMEE DTVLTRRQKE AKTKSDSGTA 190 200 210 220 230 240 AQTSLDIDKN EKCYLCKSLV PFREYQCHVD SCLQLAKADQ GDGPEGSGRA CSTVEGKWQQ 250 260 270 280 290 300 RLKNPKEKGH SEGRLLSFLE QSEHKTSDAD IKSSETGAFR VPSPGMEEAG CSREMQSSFT 310 320 330 340 RRDLNESPVK SFVSISEATD CLVDFKKQVT VQPGSRTRTK AGRGRRRKF
	Isoform 5. Checksum: C0CB4F0EBE4ADA49	FASTA	152	17,412
	10 20 30 40 50 60 MPRRKKKVKE VSESRNLEKK DVETTSSVSV KRKRRLEDAF IVISDSDGEE PKEENGLQKT 70 80 90 100 110 120 KTKQSNRAKC LAKRKIAQMT EEEQFALALK MSEQEAREVN SQEEEEEELL RKAIAESLNV 130 140 150 NMPCCKSLWR LISYIFDFCG VVVALGTSCS HL

References

	« Hide 'large scale' referencesShow '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: 12080054] [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: 14702039] [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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Oesophageal 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: 15372022] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Ovary and Skin.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597; SER-653 AND SER-677, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"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: 17698038] [Abstract] Cited for: SUMOYLATION, INTERACTION WITH UBE2I, MUTAGENESIS OF LYS-9; LYS-19; LYS-31; LYS-52 AND LYS-61.
[11]	"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: 17621610] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ALA-88 AND ALA-113, PHOSPHORYLATION AT SER-205 AND SER-402.
[12]	"CCDC98 targets BRCA1 to DNA damage sites." Liu Z., Wu J., Yu X. Nat. Struct. Mol. Biol. 14:716-720(2007) [PubMed: 17643121] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FAM175A.
[13]	"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: 17643122] [Abstract] Cited for: INTERACTION WITH FAM175A.
[14]	"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: 17311814] [Abstract] Cited for: INTERACTION WITH ESR1.
[15]	"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: 18077395] [Abstract] Cited for: INTERACTION WITH FAM175A.
[16]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-402; SER-415 AND SER-419, MASS SPECTROMETRY.
[17]	"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: 17525340] [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.
[18]	"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: 17525341] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, UBIQUITIN-BINDING, PHOSPHORYLATION AT SER-101.
[19]	"Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response." Kim H., Chen J., Yu X. Science 316:1202-1205(2007) [PubMed: 17525342] [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.
[20]	"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: 18519686] [Abstract] Cited for: PHOSPHORYLATION AT SER-205, MUTAGENESIS OF SER-205.
[21]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-46; SER-627; SER-653 AND SER-677, MASS SPECTROMETRY.
[22]	"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: 19261746] [Abstract] Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
[23]	"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: 19261749] [Abstract] Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX, UBIQUITIN-BINDING, INTERACTION WITH FAM175A.
[24]	"MERIT40 facilitates BRCA1 localization and DNA damage repair." Feng L., Huang J., Chen J. Genes Dev. 23:719-728(2009) [PubMed: 19261748] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, INTERACTION WITH FAM175A.
[25]	"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: 19328070] [Abstract] Cited for: UBIQUITIN-BINDING, UIM-LINKER DOMAIN, MUTAGENESIS OF 97-ARG--GLU-103 AND SER-101.
[26]	"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: 19015238] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-508.
[27]	"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: 19202061] [Abstract] Cited for: FUNCTION.
[28]	"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. 0:0-0(2008) [PubMed: 18695986] [Abstract] Cited for: VARIANTS TRP-15; THR-353; LEU-435 AND ARG-511.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00328521. IPI00396071. IPI00552059. IPI00872390.
RefSeq	NP_057374.3.
UniGene	Hs.232721
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96RL1. 6 interactions.
PTM databases
PhosphoSite	Q96RL1.
Proteomic databases
PRIDE	Q96RL1.
Genome annotation databases
Ensembl	ENSG00000087206. Homo sapiens. [Contig view]
GeneID	51720.
KEGG	hsa:51720.
Organism-specific databases
GeneCards	GC05M176265.
HGNC	HGNC:30298. UIMC1.
MIM	609433. gene.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q96RL1.
Gene expression databases
ArrayExpress	Q96RL1.
Bgee	Q96RL1.
CleanEx	HS_UIMC1.
GermOnline	ENSG00000087206. Homo sapiens.
Family and domain databases
InterPro	IPR003903. Ubiquitin-int_motif. [Graphical view]
Pfam	PF02809. UIM. 1 hit. [Graphical view]
SMART	SM00726. UIM. 2 hits. [Graphical view]
PROSITE	PS50330. UIM. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	55772.
SOURCE	Search...

Entry information

Entry name

UIMC1_HUMAN

Accession

Primary (citable) accession number: Q96RL1
Secondary accession number(s): A8MSA1 , 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:	June 16, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)