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Protein

Crossover junction endonuclease MUS81

Gene

MUS81

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

Functioni

Interacts with EME1 and EME2 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks.9 Publications

Cofactori

Mg2+1 Publication

GO - Molecular functioni

GO - Biological processi

  • DNA catabolic process, endonucleolytic Source: MGI
  • DNA repair Source: UniProtKB
  • double-strand break repair via break-induced replication Source: GO_Central
  • interstrand cross-link repair Source: Reactome
  • intra-S DNA damage checkpoint Source: GO_Central
  • mitotic G2 DNA damage checkpoint Source: GO_Central
  • replication fork processing Source: GO_Central
  • resolution of meiotic recombination intermediates Source: GO_Central
  • response to intra-S DNA damage checkpoint signaling Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172732-MONOMER.
ReactomeiR-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-6783310. Fanconi Anemia Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Crossover junction endonuclease MUS81 (EC:3.1.22.-)
Gene namesi
Name:MUS81
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:29814. MUS81.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi306 – 307GD → AE: Loss of activity. 1 Publication2
Mutagenesisi333 – 334ER → AG: Loss of activity. 1 Publication2
Mutagenesisi338 – 339DD → AA: Loss of activity. 2 Publications2

Organism-specific databases

DisGeNETi80198.
OpenTargetsiENSG00000172732.
PharmGKBiPA134881809.

Polymorphism and mutation databases

BioMutaiMUS81.
DMDMi166898077.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988581 – 551Crossover junction endonuclease MUS81Add BLAST551

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei95PhosphoserineCombined sources1
Modified residuei101PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96NY9.
MaxQBiQ96NY9.
PaxDbiQ96NY9.
PeptideAtlasiQ96NY9.
PRIDEiQ96NY9.

PTM databases

iPTMnetiQ96NY9.
PhosphoSitePlusiQ96NY9.

Expressioni

Tissue specificityi

Widely expressed.

Developmental stagei

Expressed in S phase and G2 phase.1 Publication

Inductioni

Up-regulated in cells treated with agents that damage DNA or block replication. This up-regulation seems to be independent of transcription.1 Publication

Gene expression databases

BgeeiENSG00000172732.
CleanExiHS_MUS81.
ExpressionAtlasiQ96NY9. baseline and differential.
GenevisibleiQ96NY9. HS.

Organism-specific databases

HPAiHPA059530.

Interactioni

Subunit structurei

May self-associate. Interacts with EME1, EME2 and CHEK2. Interacts with BLM, and this interaction may stimulate the endonuclease activity of MUS81. Interacts with SLX4/BTBD12; this interaction is direct and links the MUS81-EME1 complex to SLX4, which may coordinate the action of the structure-specific endonuclease during DNA repair. Interacts with DCLRE1B/Apollo.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EME1Q96AY25EBI-2370806,EBI-2370825
FEN1P397485EBI-2370806,EBI-707816
SLX4Q8IY9210EBI-2370806,EBI-2370740

Protein-protein interaction databases

BioGridi123170. 77 interactors.
DIPiDIP-48630N.
IntActiQ96NY9. 9 interactors.
MINTiMINT-3056813.
STRINGi9606.ENSP00000307853.

Structurei

Secondary structure

1551
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi137 – 149Combined sources13
Helixi152 – 154Combined sources3
Helixi160 – 170Combined sources11
Helixi184 – 190Combined sources7
Beta strandi193 – 195Combined sources3
Beta strandi198 – 200Combined sources3
Beta strandi203 – 205Combined sources3
Helixi207 – 219Combined sources13
Turni220 – 222Combined sources3
Beta strandi224 – 226Combined sources3
Beta strandi266 – 274Combined sources9
Beta strandi275 – 277Combined sources3
Helixi287 – 293Combined sources7
Beta strandi298 – 301Combined sources4
Beta strandi307 – 316Combined sources10
Beta strandi325 – 336Combined sources12
Helixi337 – 345Combined sources9
Helixi348 – 357Combined sources10
Turni358 – 360Combined sources3
Beta strandi363 – 369Combined sources7
Beta strandi371 – 373Combined sources3
Helixi381 – 393Combined sources13
Beta strandi398 – 401Combined sources4
Helixi405 – 422Combined sources18
Turni423 – 425Combined sources3
Beta strandi428 – 430Combined sources3
Beta strandi452 – 455Combined sources4
Helixi456 – 462Combined sources7
Turni465 – 467Combined sources3
Helixi471 – 479Combined sources9
Helixi487 – 496Combined sources10
Helixi500 – 509Combined sources10
Helixi513 – 517Combined sources5
Turni518 – 522Combined sources5
Turni526 – 529Combined sources4
Helixi535 – 545Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MC3NMR-A127-230[»]
2ZIXX-ray3.50A246-551[»]
4P0PX-ray2.80A246-551[»]
4P0QX-ray2.85A246-551[»]
4P0RX-ray6.50A/C246-551[»]
4P0SX-ray6.00A/C/E/G246-551[»]
ProteinModelPortaliQ96NY9.
SMRiQ96NY9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96NY9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini270 – 372ERCC4Add BLAST103

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni125 – 244Interaction with BLM1 PublicationAdd BLAST120

Sequence similaritiesi

Belongs to the XPF family.Curated
Contains 1 ERCC4 domain.Curated

Phylogenomic databases

eggNOGiKOG2379. Eukaryota.
COG1948. LUCA.
GeneTreeiENSGT00390000005498.
HOGENOMiHOG000113699.
HOVERGENiHBG052538.
InParanoidiQ96NY9.
KOiK08991.
OMAiVLRTHQP.
OrthoDBiEOG091G09T6.
PhylomeDBiQ96NY9.
TreeFamiTF315113.

Family and domain databases

Gene3Di1.10.8.310. 1 hit.
3.40.50.10130. 1 hit.
InterProiIPR010996. DNA_pol_b-like_N.
IPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR033309. Mus81.
IPR027420. PolB_N.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]
PANTHERiPTHR13451:SF0. PTHR13451:SF0. 1 hit.
PfamiPF02732. ERCC4. 1 hit.
[Graphical view]
SMARTiSM00891. ERCC4. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

Q96NY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPVRLGRK RPLPACPNPL FVRWLTEWRD EATRSRRRTR FVFQKALRSL
60 70 80 90 100
RRYPLPLRSG KEAKILQHFG DGLCRMLDER LQRHRTSGGD HAPDSPSGEN
110 120 130 140 150
SPAPQGRLAE VQDSSMPVPA QPKAGGSGSY WPARHSGARV ILLVLYREHL
160 170 180 190 200
NPNGHHFLTK EELLQRCAQK SPRVAPGSAR PWPALRSLLH RNLVLRTHQP
210 220 230 240 250
ARYSLTPEGL ELAQKLAESE GLSLLNVGIG PKEPPGEETA VPGAASAELA
260 270 280 290 300
SEAGVQQQPL ELRPGEYRVL LCVDIGETRG GGHRPELLRE LQRLHVTHTV
310 320 330 340 350
RKLHVGDFVW VAQETNPRDP ANPGELVLDH IVERKRLDDL CSSIIDGRFR
360 370 380 390 400
EQKFRLKRCG LERRVYLVEE HGSVHNLSLP ESTLLQAVTN TQVIDGFFVK
410 420 430 440 450
RTADIKESAA YLALLTRGLQ RLYQGHTLRS RPWGTPGNPE SGAMTSPNPL
460 470 480 490 500
CSLLTFSDFN AGAIKNKAQS VREVFARQLM QVRGVSGEKA AALVDRYSTP
510 520 530 540 550
ASLLAAYDAC ATPKEQETLL STIKCGRLQR NLGPALSRTL SQLYCSYGPL

T
Length:551
Mass (Da):61,173
Last modified:February 5, 2008 - v3
Checksum:iD0F331CC2269D847
GO

Sequence cautioni

The sequence BAB14953 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02534037R → H.3 PublicationsCorresponds to variant rs13817dbSNPEnsembl.1
Natural variantiVAR_061988115S → F.Corresponds to variant rs34381357dbSNPEnsembl.1
Natural variantiVAR_038521180R → P.3 PublicationsCorresponds to variant rs545500dbSNPEnsembl.1
Natural variantiVAR_021990189L → F.Corresponds to variant rs2298447dbSNPEnsembl.1
Natural variantiVAR_038522350R → W.Corresponds to variant rs34891773dbSNPEnsembl.1
Natural variantiVAR_025341481Q → H.Corresponds to variant rs765593dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF425646 mRNA. Translation: AAL28065.1.
BC009999 mRNA. Translation: AAH09999.2.
AK024665 mRNA. Translation: BAB14953.1. Different initiation.
CCDSiCCDS8115.1.
RefSeqiNP_079404.3. NM_025128.4.
XP_011543572.1. XM_011545270.1.
UniGeneiHs.288798.

Genome annotation databases

EnsembliENST00000308110; ENSP00000307853; ENSG00000172732.
GeneIDi80198.
KEGGihsa:80198.
UCSCiuc001ofv.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF425646 mRNA. Translation: AAL28065.1.
BC009999 mRNA. Translation: AAH09999.2.
AK024665 mRNA. Translation: BAB14953.1. Different initiation.
CCDSiCCDS8115.1.
RefSeqiNP_079404.3. NM_025128.4.
XP_011543572.1. XM_011545270.1.
UniGeneiHs.288798.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MC3NMR-A127-230[»]
2ZIXX-ray3.50A246-551[»]
4P0PX-ray2.80A246-551[»]
4P0QX-ray2.85A246-551[»]
4P0RX-ray6.50A/C246-551[»]
4P0SX-ray6.00A/C/E/G246-551[»]
ProteinModelPortaliQ96NY9.
SMRiQ96NY9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123170. 77 interactors.
DIPiDIP-48630N.
IntActiQ96NY9. 9 interactors.
MINTiMINT-3056813.
STRINGi9606.ENSP00000307853.

PTM databases

iPTMnetiQ96NY9.
PhosphoSitePlusiQ96NY9.

Polymorphism and mutation databases

BioMutaiMUS81.
DMDMi166898077.

Proteomic databases

EPDiQ96NY9.
MaxQBiQ96NY9.
PaxDbiQ96NY9.
PeptideAtlasiQ96NY9.
PRIDEiQ96NY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308110; ENSP00000307853; ENSG00000172732.
GeneIDi80198.
KEGGihsa:80198.
UCSCiuc001ofv.5. human.

Organism-specific databases

CTDi80198.
DisGeNETi80198.
GeneCardsiMUS81.
H-InvDBHIX0009809.
HGNCiHGNC:29814. MUS81.
HPAiHPA059530.
MIMi606591. gene.
neXtProtiNX_Q96NY9.
OpenTargetsiENSG00000172732.
PharmGKBiPA134881809.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2379. Eukaryota.
COG1948. LUCA.
GeneTreeiENSGT00390000005498.
HOGENOMiHOG000113699.
HOVERGENiHBG052538.
InParanoidiQ96NY9.
KOiK08991.
OMAiVLRTHQP.
OrthoDBiEOG091G09T6.
PhylomeDBiQ96NY9.
TreeFamiTF315113.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172732-MONOMER.
ReactomeiR-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-6783310. Fanconi Anemia Pathway.

Miscellaneous databases

ChiTaRSiMUS81. human.
EvolutionaryTraceiQ96NY9.
GeneWikiiMUS81.
GenomeRNAii80198.
PROiQ96NY9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172732.
CleanExiHS_MUS81.
ExpressionAtlasiQ96NY9. baseline and differential.
GenevisibleiQ96NY9. HS.

Family and domain databases

Gene3Di1.10.8.310. 1 hit.
3.40.50.10130. 1 hit.
InterProiIPR010996. DNA_pol_b-like_N.
IPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR033309. Mus81.
IPR027420. PolB_N.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]
PANTHERiPTHR13451:SF0. PTHR13451:SF0. 1 hit.
PfamiPF02732. ERCC4. 1 hit.
[Graphical view]
SMARTiSM00891. ERCC4. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMUS81_HUMAN
AccessioniPrimary (citable) accession number: Q96NY9
Secondary accession number(s): Q9H7D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 5, 2008
Last modified: November 30, 2016
This is version 140 of the entry and version 3 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 11
    Human chromosome 11: 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.