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Protein

BRCA1-A complex subunit RAP80

Gene

UIMC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-binding protein (PubMed:24627472). Specifically recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19328070, Ref. 36). 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 NCOR1.12 Publications

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • K63-linked polyubiquitin binding Source: UniProtKB

GO - Biological processi

  • double-strand break repair Source: UniProtKB
  • double-strand break repair via nonhomologous end joining Source: Reactome
  • G2 DNA damage checkpoint Source: UniProtKB
  • histone H2A K63-linked deubiquitination Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: HGNC
  • positive regulation of DNA repair Source: UniProtKB
  • response to ionizing radiation Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-5689901. Metalloprotease DUBs.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-69473. G2/M DNA damage checkpoint.
SIGNORiQ96RL1.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:30298. UIMC1.

Subcellular locationi

GO - Cellular componenti

  • BRCA1-A complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9K → A: Does not affect symoylation; when associated with A-19; A-31; A-52 and A-61. 1 Publication1
Mutagenesisi19K → A: Does not affect symoylation; when associated with A-9; A-31; A-52 and A-61. 1 Publication1
Mutagenesisi31K → A: Does not affect symoylation; when associated with A-9; A-19; A-52 and A-61. 1 Publication1
Mutagenesisi52K → A: Does not affect symoylation; when associated with A-9; A-19; A-31 and A-61. 1 Publication1
Mutagenesisi61K → A: Does not affect symoylation; when associated with A-9; A-19; A-31 and A-52. 1 Publication1
Mutagenesisi81Missing : Strongly reduces ubiquitin binding via UIM 1. 1 Publication1
Mutagenesisi88A → G or S: Impairs localization to DNA damages sites; when associated with A-92; S-113 and A-117. 3 Publications1
Mutagenesisi92S → A: Impairs localization to DNA damages sites; when associated with S-88; S-113 and A-117. 2 Publications1
Mutagenesisi97 – 103REVNSQE → AA: Impairs the selectivity for 'K-63'-linked ubiquitin. 1 Publication7
Mutagenesisi97 – 103REVNSQE → AAAAAAA: Increases the selectivity for 'K-63'-linked ubiquitin. 1 Publication7
Mutagenesisi97 – 103REVNSQE → AAAAAAAAA: Impairs the selectivity for 'K-63'-linked ubiquitin. 1 Publication7
Mutagenesisi101S → A or E: Slightly impairs the selectivity for 'K-63'-linked ubiquitin. 1 Publication1
Mutagenesisi113A → G or S: Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88; A-92 and A-117. 3 Publications1
Mutagenesisi117S → A: Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88; A-92 and S-113. 2 Publications1
Mutagenesisi205S → G: Abolishes phosphorylation at this position. 1 Publication1
Mutagenesisi508C → A: Abolishes interaction with histone monoubiquitinated H2B without affecting the interaction with H2A. 1 Publication1

Organism-specific databases

DisGeNETi51720.
OpenTargetsiENSG00000087206.
PharmGKBiPA162408624.

Polymorphism and mutation databases

BioMutaiUIMC1.
DMDMi60390957.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000975471 – 719BRCA1-A complex subunit RAP80Add BLAST719

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei29PhosphoserineCombined sources1
Cross-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei44PhosphoserineCombined sources1
Modified residuei46PhosphoserineCombined sources1
Modified residuei101PhosphoserineCombined sources2 Publications1
Modified residuei140PhosphoserineCombined sources1 Publication1
Modified residuei205Phosphoserine2 Publications1
Modified residuei379PhosphoserineBy similarity1
Cross-linki382Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei402Phosphoserine2 Publications1
Modified residuei419Phosphoserine1 Publication1
Modified residuei466PhosphoserineCombined sources1
Cross-linki544Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki562Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki607Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei627PhosphoserineCombined sources1
Modified residuei653PhosphoserineCombined sources1
Modified residuei677PhosphoserineCombined sources1

Post-translational modificationi

Sumoylated.1 Publication
Phosphorylated upon DNA damage by ATM or ATR.5 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96RL1.
MaxQBiQ96RL1.
PaxDbiQ96RL1.
PeptideAtlasiQ96RL1.
PRIDEiQ96RL1.

PTM databases

iPTMnetiQ96RL1.
PhosphoSitePlusiQ96RL1.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000087206.
CleanExiHS_UIMC1.
ExpressionAtlasiQ96RL1. baseline and differential.
GenevisibleiQ96RL1. HS.

Organism-specific databases

HPAiHPA037503.
HPA037504.

Interactioni

Subunit structurei

Interacts with TSP57 (By similarity). Component of the ARISC complex, at least composed of UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1 (PubMed:24075985). 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

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • K63-linked polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119697. 70 interactors.
DIPiDIP-29936N.
IntActiQ96RL1. 48 interactors.
MINTiMINT-1197441.
STRINGi9606.ENSP00000366434.

Structurei

Secondary structure

1719
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 43Combined sources4
Helixi82 – 94Combined sources13
Helixi101 – 119Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MKFNMR-A74-131[»]
2MKGNMR-A74-131[»]
2N9ENMR-A37-49[»]
2RR9NMR-C79-124[»]
ProteinModelPortaliQ96RL1.
SMRiQ96RL1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96RL1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 99UIM 1PROSITE-ProRule annotationAdd BLAST20
Domaini105 – 124UIM 2PROSITE-ProRule annotationAdd BLAST20

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 101Necessary for transcriptional repressionAdd BLAST101
Regioni97 – 103UIM-linker7
Regioni100 – 200Necessary for interaction with NR6A1 N-terminusAdd BLAST101
Regioni270 – 400AIRAdd BLAST131
Regioni400 – 500Necessary for interaction with NR6A1 C-terminusAdd BLAST101
Regioni505 – 582Zinc-finger-like regionAdd BLAST78

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi60 – 78LR motifAdd BLAST19

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi81 – 108Glu-richAdd BLAST28

Domaini

The tandem UIM domains form a continuous 60 Angstrom-long alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and UIM2 bind to the proximal and distal ubiquitin moieties and recognize an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM domains determines the selectivity for 'Lys-63'-linkage, and its length is very important for specificity.By similarity3 Publications
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) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IGE5. Eukaryota.
ENOG4111MI8. LUCA.
GeneTreeiENSGT00390000007635.
HOVERGENiHBG056783.
InParanoidiQ96RL1.
KOiK20775.
OMAiMGDEDKE.
OrthoDBiEOG091G07P7.
PhylomeDBiQ96RL1.
TreeFamiTF336575.

Family and domain databases

InterProiIPR003903. UIM_dom.
[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. AlignAdd to basket

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

        10         20         30         40         50
MPRRKKKVKE VSESRNLEKK DVETTSSVSV KRKRRLEDAF IVISDSDGEE
60 70 80 90 100
PKEENGLQKT KTKQSNRAKC LAKRKIAQMT EEEQFALALK MSEQEAREVN
110 120 130 140 150
SQEEEEEELL RKAIAESLNS CRPSDASATR SRPLATGPSS QSHQEKTTDS
160 170 180 190 200
GLTEGIWQLV PPSLFKGSHI SQGNEAEERE EPWDHTEKTE EEPVSGSSGS
210 220 230 240 250
WDQSSQPVFE NVNVKSFDRC TGHSAEHTQC GKPQESTGRG SAFLKAVQGS
260 270 280 290 300
GDTSRHCLPT LADAKGLQDT GGTVNYFWGI PFCPDGVDPN QYTKVILCQL
310 320 330 340 350
EVYQKSLKMA QRQLLNKKGF GEPVLPRPPS LIQNECGQGE QASEKNECIS
360 370 380 390 400
EDMGDEDKEE RQESRASDWH SKTKDFQESS IKSLKEKLLL EEEPTTSHGQ
410 420 430 440 450
SSQGIVEETS EEGNSVPASQ SVAALTSKRS LVLMPESSAE EITVCPETQL
460 470 480 490 500
SSSETFDLER EVSPGSRDIL DGVRIIMADK EVGNKEDAEK EVAISTFSSS
510 520 530 540 550
NQVSCPLCDQ CFPPTKIERH AMYCNGLMEE DTVLTRRQKE AKTKSDSGTA
560 570 580 590 600
AQTSLDIDKN EKCYLCKSLV PFREYQCHVD SCLQLAKADQ GDGPEGSGRA
610 620 630 640 650
CSTVEGKWQQ RLKNPKEKGH SEGRLLSFLE QSEHKTSDAD IKSSETGAFR
660 670 680 690 700
VPSPGMEEAG CSREMQSSFT RRDLNESPVK SFVSISEATD CLVDFKKQVT
710
VQPGSRTRTK AGRGRRRKF
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 differs from that shown. Reason: Erroneous termination at position 386. Translated as Glu.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti187E → K in AAH06078 (PubMed:15489334).Curated1
Sequence conflicti192E → G in BAG51153 (PubMed:14702039).Curated1
Sequence conflicti247V → C in AAG59851 (Ref. 3) Curated1
Sequence conflicti347E → G in AAK61871 (PubMed:12080054).Curated1
Sequence conflicti518E → G in AAK61871 (PubMed:12080054).Curated1
Sequence conflicti634H → R in AAG59855 (Ref. 3) Curated1
Sequence conflicti638D → N in BAG51153 (PubMed:14702039).Curated1
Sequence conflicti694D → V in AAG59855 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05146915R → W Common polymorphism not associated with susceptibility to breast cancer. 1 PublicationCorresponds to variant rs13167812dbSNPEnsembl.1
Natural variantiVAR_055328353M → T Common polymorphism not associated with susceptibility to breast cancer. 1 PublicationCorresponds to variant rs143282828dbSNPEnsembl.1
Natural variantiVAR_051470435P → L Common polymorphism not associated with susceptibility to breast cancer. 1 PublicationCorresponds to variant rs3733876dbSNPEnsembl.1
Natural variantiVAR_051471511C → R Common polymorphism not associated with susceptibility to breast cancer. 1 PublicationCorresponds to variant rs13360277dbSNPEnsembl.1
Natural variantiVAR_051472596G → E.Corresponds to variant rs10475633dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0129331 – 370Missing in isoform 4. 2 PublicationsAdd BLAST370
Alternative sequenceiVSP_0129321 – 78Missing in isoform 3. 1 PublicationAdd BLAST78
Alternative sequenceiVSP_037264120 – 152SCRPS…TDSGL → VNMPCCKSLWRLISYIFDFC GVVVALGTSCSHL in isoform 5. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_037265153 – 719Missing in isoform 5. 1 PublicationAdd BLAST567
Alternative sequenceiVSP_012935234 – 399Missing in isoform 2. 1 PublicationAdd BLAST166
Alternative sequenceiVSP_012934371 – 400SKTKD…TSHGQ → MLPLPDLDLWPLDRLPSPIK RKPQTLGSLK in isoform 4. 2 PublicationsAdd BLAST30

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS83050.1. [Q96RL1-2]
RefSeqiNP_001186226.1. NM_001199297.2. [Q96RL1-1]
NP_001186227.1. NM_001199298.1. [Q96RL1-1]
NP_001304890.1. NM_001317961.1. [Q96RL1-2]
NP_057374.3. NM_016290.4. [Q96RL1-1]
XP_005265987.1. XM_005265930.2. [Q96RL1-1]
XP_005265993.1. XM_005265936.2. [Q96RL1-4]
XP_006714934.1. XM_006714871.2. [Q96RL1-1]
XP_016865063.1. XM_017009574.1. [Q96RL1-3]
XP_016865067.1. XM_017009578.1. [Q96RL1-4]
XP_016865068.1. XM_017009579.1. [Q96RL1-4]
UniGeneiHs.232721.

Genome annotation databases

EnsembliENST00000377227; ENSP00000366434; ENSG00000087206. [Q96RL1-1]
ENST00000506128; ENSP00000427480; ENSG00000087206. [Q96RL1-2]
ENST00000510698; ENSP00000423717; ENSG00000087206. [Q96RL1-4]
ENST00000511320; ENSP00000421926; ENSG00000087206. [Q96RL1-1]
GeneIDi51720.
KEGGihsa:51720.
UCSCiuc063kam.1. human. [Q96RL1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS83050.1. [Q96RL1-2]
RefSeqiNP_001186226.1. NM_001199297.2. [Q96RL1-1]
NP_001186227.1. NM_001199298.1. [Q96RL1-1]
NP_001304890.1. NM_001317961.1. [Q96RL1-2]
NP_057374.3. NM_016290.4. [Q96RL1-1]
XP_005265987.1. XM_005265930.2. [Q96RL1-1]
XP_005265993.1. XM_005265936.2. [Q96RL1-4]
XP_006714934.1. XM_006714871.2. [Q96RL1-1]
XP_016865063.1. XM_017009574.1. [Q96RL1-3]
XP_016865067.1. XM_017009578.1. [Q96RL1-4]
XP_016865068.1. XM_017009579.1. [Q96RL1-4]
UniGeneiHs.232721.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MKFNMR-A74-131[»]
2MKGNMR-A74-131[»]
2N9ENMR-A37-49[»]
2RR9NMR-C79-124[»]
ProteinModelPortaliQ96RL1.
SMRiQ96RL1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119697. 70 interactors.
DIPiDIP-29936N.
IntActiQ96RL1. 48 interactors.
MINTiMINT-1197441.
STRINGi9606.ENSP00000366434.

PTM databases

iPTMnetiQ96RL1.
PhosphoSitePlusiQ96RL1.

Polymorphism and mutation databases

BioMutaiUIMC1.
DMDMi60390957.

Proteomic databases

EPDiQ96RL1.
MaxQBiQ96RL1.
PaxDbiQ96RL1.
PeptideAtlasiQ96RL1.
PRIDEiQ96RL1.

Protocols and materials databases

DNASUi51720.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377227; ENSP00000366434; ENSG00000087206. [Q96RL1-1]
ENST00000506128; ENSP00000427480; ENSG00000087206. [Q96RL1-2]
ENST00000510698; ENSP00000423717; ENSG00000087206. [Q96RL1-4]
ENST00000511320; ENSP00000421926; ENSG00000087206. [Q96RL1-1]
GeneIDi51720.
KEGGihsa:51720.
UCSCiuc063kam.1. human. [Q96RL1-1]

Organism-specific databases

CTDi51720.
DisGeNETi51720.
GeneCardsiUIMC1.
H-InvDBHIX0005450.
HGNCiHGNC:30298. UIMC1.
HPAiHPA037503.
HPA037504.
MIMi609433. gene.
neXtProtiNX_Q96RL1.
OpenTargetsiENSG00000087206.
PharmGKBiPA162408624.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGE5. Eukaryota.
ENOG4111MI8. LUCA.
GeneTreeiENSGT00390000007635.
HOVERGENiHBG056783.
InParanoidiQ96RL1.
KOiK20775.
OMAiMGDEDKE.
OrthoDBiEOG091G07P7.
PhylomeDBiQ96RL1.
TreeFamiTF336575.

Enzyme and pathway databases

ReactomeiR-HSA-5689901. Metalloprotease DUBs.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-69473. G2/M DNA damage checkpoint.
SIGNORiQ96RL1.

Miscellaneous databases

ChiTaRSiUIMC1. human.
EvolutionaryTraceiQ96RL1.
GeneWikiiUIMC1.
GenomeRNAii51720.
PROiQ96RL1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087206.
CleanExiHS_UIMC1.
ExpressionAtlasiQ96RL1. baseline and differential.
GenevisibleiQ96RL1. HS.

Family and domain databases

InterProiIPR003903. UIM_dom.
[Graphical view]
SMARTiSM00726. UIM. 2 hits.
[Graphical view]
PROSITEiPS50330. UIM. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 130 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.