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Protein

DNA excision repair protein ERCC-6-like

Gene

Ercc6l

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. Acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi123 – 130ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA excision repair protein ERCC-6-like (EC:3.6.4.12)
Alternative name(s):
ATP-dependent helicase ERCC6-like
Gene namesi
Name:Ercc6l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:2654144. Ercc6l.

Subcellular locationi

  • Chromosomecentromere By similarity
  • Chromosomecentromerekinetochore By similarity

  • Note: Localizes to kinetochores, inner centromeres and thin threads connecting separating chromosomes even during anaphase. In prometaphase cells, it mostly concentrates in between kinetochores. In metaphase, it localizes to numerous thin threads that stretch between sister kinetochores of the aligned chromosomes and are composed of catenated centromeric DNA. Evolution from inner centromeres to thin threads takes place in response to tension. Resolution of thin threads requires topoisomerase 2-alpha (TOP2A) after anaphase onset (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003288321 – 1240DNA excision repair protein ERCC-6-likeAdd BLAST1240

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineBy similarity1
Modified residuei755PhosphoserineBy similarity1
Modified residuei773PhosphoserineBy similarity1
Modified residuei821PhosphoserineBy similarity1
Modified residuei966PhosphoserineBy similarity1
Modified residuei998PhosphoserineCombined sources1
Modified residuei1001PhosphoserineCombined sources1
Modified residuei1021PhosphoserineCombined sources1
Modified residuei1057PhosphothreonineBy similarity1
Modified residuei1092PhosphoserineBy similarity1
Modified residuei1112PhosphoserineCombined sources1
Modified residuei1172PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation by PLK1 prevents the association with chromosome arms and restricts its localization to the kinetochore-centromere region.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BHK9.
MaxQBiQ8BHK9.
PaxDbiQ8BHK9.
PeptideAtlasiQ8BHK9.
PRIDEiQ8BHK9.

PTM databases

iPTMnetiQ8BHK9.
PhosphoSitePlusiQ8BHK9.

Expressioni

Tissue specificityi

Expressed mainly in the neural tube and heart of E10.5 embryo. Significantly down-regulated after alcohol exposure in embryonic brain and heart, but not in embryonic kidney, liver, or lung.1 Publication

Gene expression databases

BgeeiENSMUSG00000051220.
GenevisibleiQ8BHK9. MM.

Interactioni

Subunit structurei

Interacts with PLK1, which phosphorylates it. Both proteins are mutually dependent on each other for correct subcellular localization (By similarity).By similarity

Protein-protein interaction databases

BioGridi231820. 33 interactors.
IntActiQ8BHK9. 33 interactors.
STRINGi10090.ENSMUSP00000050592.

Structurei

3D structure databases

ProteinModelPortaliQ8BHK9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati21 – 54TPR 1Add BLAST34
Domaini110 – 278Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST169
Domaini467 – 631Helicase C-terminalPROSITE-ProRule annotationAdd BLAST165
Repeati1191 – 1224TPR 2Add BLAST34

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi229 – 232DEAH box4

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 2 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0387. Eukaryota.
ENOG410XP4Z. LUCA.
GeneTreeiENSGT00590000083118.
HOGENOMiHOG000074172.
HOVERGENiHBG107854.
InParanoidiQ8BHK9.
KOiK20093.
OMAiICEMPSL.
OrthoDBiEOG091G058Q.
PhylomeDBiQ8BHK9.
TreeFamiTF332843.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BHK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEASQGLAEV ETLSPQLAES YLRYVQEAKE AAKNGDLEES LKLFNLAKDI
60 70 80 90 100
FPTKKVMSRI QKLQEALEQL AEEEDDDEFI DVCSSGLLLY RELYEKLFEH
110 120 130 140 150
QKEGIAFLYS LYKDGRKGGI LADDMGLGKT VQIIAFLSGM FDASLVNHVL
160 170 180 190 200
LIMPTNLINT WVNEFAKWTP GMRVKTFHGS SKSERTRSLT RIQQRNGVVI
210 220 230 240 250
TTYQMLLNNW QQLASFNGQA FVWDYVILDE AHKIKSASTK SAVCARAIPA
260 270 280 290 300
SNRLLLTGTP VQNNLQELWS LFDFACQGSL LGTLKTFKME YEHPIIRARE
310 320 330 340 350
KDATPGEKAL GLKISENLME IIKPYFLRRT KEEVQTKKAD NPEARLGEKN
360 370 380 390 400
PAGEAICDMF SLARKNDLIV WIRLLPLQEE IYRKFVSLDH IKELLMETRS
410 420 430 440 450
PLAELGVLKK LCDHPRLLSA RACRLLNLGT ATFSAQDENE QEDVSNMNSI
460 470 480 490 500
DHLPDKTLIQ ESGKMIFLMS LLERLQDEGH QTLVFSQSIK ILNIIERLLK
510 520 530 540 550
NKHFKTLRID GTVTHLWERE KRIQLFQQNK EYSVFLLTTQ VGGVGLTLTA
560 570 580 590 600
ATRVVIFDPS WNPATDAQAV DRVYRIGQKE NVVVYRLITC GTVEEKIYRR
610 620 630 640 650
QVFKDSLIRQ TTGEKKNPFR YFTKQELKEL FTVGDLQKSA TQMQLQCLHA
660 670 680 690 700
AQRRSDEKLD EHIAYLHLLG IAGISDHDLM FTRDLSVKEE LDMLEDSQYI
710 720 730 740 750
HQRVQKAQFL VESESQNTVQ RQTTGIEETW LKAQEFPSQQ KKKGTEFNKP
760 770 780 790 800
QPQPSRLLTK PTQVEAISSQ MASITICDQS AESEPQEHSE VHDVTSLQGS
810 820 830 840 850
HHFNSTSDAG TIASLPQGAE SIGEVSTDSL LSPAKGFAAE NDAMQKKGLQ
860 870 880 890 900
ASPGQEAPSE NLGSFHYLPR ESSKASLGPN LDLQDSVVLY HRSPTANENQ
910 920 930 940 950
NLESDVPMIE ISDDLSEPPS ALQGAQAIEA QLELKEDDPL KSPPQYACDF
960 970 980 990 1000
NLFLEDSADT RQNLSSKFLE HVEKEKSLQS PAANSRAKSA LTLSLDSSPK
1010 1020 1030 1040 1050
SDEESEVISV KTKSKTRRIL SDDEDEDEED AFKGSHTNSI NISPFPFSSV
1060 1070 1080 1090 1100
KQFDASTPQS GSNPSRRFFS PKTPGEVNTS LHSRRSLASR RSLINVVLDD
1110 1120 1130 1140 1150
VEDMEERLDN SSEEESEPGL SEENNEEEAL ACTEEQPSGA TLASGNKSSN
1160 1170 1180 1190 1200
LTMSEPTSPA PQSSPCAPEP SSSDPMPDPP QDLAVEAGND YESLVARGKE
1210 1220 1230 1240
LKECGKIQEA LNCLVKALDI KSADPEVMLM TLSLYKQLNI
Length:1,240
Mass (Da):138,854
Last modified:March 1, 2003 - v1
Checksum:i0B996A4286F51C27
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1210A → S in BAC26244 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY172688 mRNA. Translation: AAN87172.1.
AK029015 mRNA. Translation: BAC26244.1.
AK045113 mRNA. Translation: BAC32227.2.
AK084617 mRNA. Translation: BAC39230.1.
AK084618 mRNA. Translation: BAC39231.1.
AL807784 Genomic DNA. Translation: CAM24634.1.
BC037660 mRNA. Translation: AAH37660.1.
CCDSiCCDS30321.1.
RefSeqiNP_666347.2. NM_146235.3.
UniGeneiMm.31911.

Genome annotation databases

EnsembliENSMUST00000056904; ENSMUSP00000050592; ENSMUSG00000051220.
GeneIDi236930.
KEGGimmu:236930.
UCSCiuc009tyk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY172688 mRNA. Translation: AAN87172.1.
AK029015 mRNA. Translation: BAC26244.1.
AK045113 mRNA. Translation: BAC32227.2.
AK084617 mRNA. Translation: BAC39230.1.
AK084618 mRNA. Translation: BAC39231.1.
AL807784 Genomic DNA. Translation: CAM24634.1.
BC037660 mRNA. Translation: AAH37660.1.
CCDSiCCDS30321.1.
RefSeqiNP_666347.2. NM_146235.3.
UniGeneiMm.31911.

3D structure databases

ProteinModelPortaliQ8BHK9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231820. 33 interactors.
IntActiQ8BHK9. 33 interactors.
STRINGi10090.ENSMUSP00000050592.

PTM databases

iPTMnetiQ8BHK9.
PhosphoSitePlusiQ8BHK9.

Proteomic databases

EPDiQ8BHK9.
MaxQBiQ8BHK9.
PaxDbiQ8BHK9.
PeptideAtlasiQ8BHK9.
PRIDEiQ8BHK9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056904; ENSMUSP00000050592; ENSMUSG00000051220.
GeneIDi236930.
KEGGimmu:236930.
UCSCiuc009tyk.2. mouse.

Organism-specific databases

CTDi54821.
MGIiMGI:2654144. Ercc6l.

Phylogenomic databases

eggNOGiKOG0387. Eukaryota.
ENOG410XP4Z. LUCA.
GeneTreeiENSGT00590000083118.
HOGENOMiHOG000074172.
HOVERGENiHBG107854.
InParanoidiQ8BHK9.
KOiK20093.
OMAiICEMPSL.
OrthoDBiEOG091G058Q.
PhylomeDBiQ8BHK9.
TreeFamiTF332843.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiErcc6l. mouse.
PROiQ8BHK9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000051220.
GenevisibleiQ8BHK9. MM.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERC6L_MOUSE
AccessioniPrimary (citable) accession number: Q8BHK9
Secondary accession number(s): Q8BGN1, Q8BRC9, Q8CE49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.