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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-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)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
Mutagenesisi81 – 811Missing : Strongly reduces ubiquitin binding via UIM 1. 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.

Polymorphism and mutation databases

BioMutaiUIMC1.
DMDMi60390957.

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
Cross-linki20 – 20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei29 – 291PhosphoserineCombined sources
Cross-linki31 – 31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei46 – 461PhosphoserineCombined sources
Modified residuei101 – 1011PhosphoserineCombined sources2 Publications
Modified residuei140 – 1401PhosphoserineCombined sources1 Publication
Modified residuei205 – 2051Phosphoserine2 Publications
Modified residuei379 – 3791PhosphoserineBy similarity
Cross-linki382 – 382Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei402 – 4021Phosphoserine2 Publications
Modified residuei419 – 4191Phosphoserine1 Publication
Modified residuei466 – 4661PhosphoserineCombined sources
Cross-linki544 – 544Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki562 – 562Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki607 – 607Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei627 – 6271PhosphoserineCombined sources
Modified residuei653 – 6531PhosphoserineCombined sources
Modified residuei677 – 6771PhosphoserineCombined sources

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.
PhosphoSiteiQ96RL1.

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 interactions.
DIPiDIP-29936N.
IntActiQ96RL1. 48 interactions.
MINTiMINT-1197441.
STRINGi9606.ENSP00000366434.

Structurei

Secondary structure

1
719
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 434Combined sources
Helixi82 – 9413Combined sources
Helixi101 – 11919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MKFNMR-A74-131[»]
2MKGNMR-A74-131[»]
2N9ENMR-A37-49[»]
2RR9NMR-C79-124[»]
ProteinModelPortaliQ96RL1.
SMRiQ96RL1. Positions 79-124.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96RL1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 9920UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini105 – 12420UIM 2PROSITE-ProRule annotationAdd
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 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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871E → K in AAH06078 (PubMed:15489334).Curated
Sequence conflicti192 – 1921E → G in BAG51153 (PubMed:14702039).Curated
Sequence conflicti247 – 2471V → C in AAG59851 (Ref. 3) Curated
Sequence conflicti347 – 3471E → G in AAK61871 (PubMed:12080054).Curated
Sequence conflicti518 – 5181E → G in AAK61871 (PubMed:12080054).Curated
Sequence conflicti634 – 6341H → R in AAG59855 (Ref. 3) Curated
Sequence conflicti638 – 6381D → N in BAG51153 (PubMed:14702039).Curated
Sequence conflicti694 – 6941D → V in AAG59855 (Ref. 3) Curated

Natural variant

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

Alternative sequence

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

Sequence databases

Select the link destinations:
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]
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]
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]
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]
UniGeneiHs.232721.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MKFNMR-A74-131[»]
2MKGNMR-A74-131[»]
2N9ENMR-A37-49[»]
2RR9NMR-C79-124[»]
ProteinModelPortaliQ96RL1.
SMRiQ96RL1. Positions 79-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ96RL1.
PhosphoSiteiQ96RL1.

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

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-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: September 7, 2016
This is version 127 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.