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Q8BHK9 (ERC6L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA excision repair protein ERCC-6-like

EC=3.6.4.12
Alternative name(s):
ATP-dependent helicase ERCC6-like
Gene names
Name:Ercc6l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1240 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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

Subcellular location

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.

Tissue specificity

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. Ref.5

Post-translational modification

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

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 2 TPR repeats.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Kinetochore
   DomainRepeat
TPR repeat
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12401240DNA excision repair protein ERCC-6-like
PRO_0000328832

Regions

Repeat21 – 5434TPR 1
Domain110 – 278169Helicase ATP-binding
Domain467 – 631165Helicase C-terminal
Repeat1191 – 122434TPR 2
Nucleotide binding123 – 1308ATP By similarity
Motif229 – 2324DEAH box

Amino acid modifications

Modified residue141Phosphoserine By similarity
Modified residue7551Phosphoserine By similarity
Modified residue7731Phosphoserine By similarity
Modified residue8211Phosphoserine By similarity
Modified residue10211Phosphoserine Ref.6
Modified residue10571Phosphothreonine By similarity
Modified residue10921Phosphoserine By similarity
Modified residue11721Phosphoserine By similarity

Experimental info

Sequence conflict12101A → S in BAC26244. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BHK9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 0B996A4286F51C27

FASTA1,240138,854
        10         20         30         40         50         60 
MEASQGLAEV ETLSPQLAES YLRYVQEAKE AAKNGDLEES LKLFNLAKDI FPTKKVMSRI 

        70         80         90        100        110        120 
QKLQEALEQL AEEEDDDEFI DVCSSGLLLY RELYEKLFEH QKEGIAFLYS LYKDGRKGGI 

       130        140        150        160        170        180 
LADDMGLGKT VQIIAFLSGM FDASLVNHVL LIMPTNLINT WVNEFAKWTP GMRVKTFHGS 

       190        200        210        220        230        240 
SKSERTRSLT RIQQRNGVVI TTYQMLLNNW QQLASFNGQA FVWDYVILDE AHKIKSASTK 

       250        260        270        280        290        300 
SAVCARAIPA SNRLLLTGTP VQNNLQELWS LFDFACQGSL LGTLKTFKME YEHPIIRARE 

       310        320        330        340        350        360 
KDATPGEKAL GLKISENLME IIKPYFLRRT KEEVQTKKAD NPEARLGEKN PAGEAICDMF 

       370        380        390        400        410        420 
SLARKNDLIV WIRLLPLQEE IYRKFVSLDH IKELLMETRS PLAELGVLKK LCDHPRLLSA 

       430        440        450        460        470        480 
RACRLLNLGT ATFSAQDENE QEDVSNMNSI DHLPDKTLIQ ESGKMIFLMS LLERLQDEGH 

       490        500        510        520        530        540 
QTLVFSQSIK ILNIIERLLK NKHFKTLRID GTVTHLWERE KRIQLFQQNK EYSVFLLTTQ 

       550        560        570        580        590        600 
VGGVGLTLTA ATRVVIFDPS WNPATDAQAV DRVYRIGQKE NVVVYRLITC GTVEEKIYRR 

       610        620        630        640        650        660 
QVFKDSLIRQ TTGEKKNPFR YFTKQELKEL FTVGDLQKSA TQMQLQCLHA AQRRSDEKLD 

       670        680        690        700        710        720 
EHIAYLHLLG IAGISDHDLM FTRDLSVKEE LDMLEDSQYI HQRVQKAQFL VESESQNTVQ 

       730        740        750        760        770        780 
RQTTGIEETW LKAQEFPSQQ KKKGTEFNKP QPQPSRLLTK PTQVEAISSQ MASITICDQS 

       790        800        810        820        830        840 
AESEPQEHSE VHDVTSLQGS HHFNSTSDAG TIASLPQGAE SIGEVSTDSL LSPAKGFAAE 

       850        860        870        880        890        900 
NDAMQKKGLQ ASPGQEAPSE NLGSFHYLPR ESSKASLGPN LDLQDSVVLY HRSPTANENQ 

       910        920        930        940        950        960 
NLESDVPMIE ISDDLSEPPS ALQGAQAIEA QLELKEDDPL KSPPQYACDF NLFLEDSADT 

       970        980        990       1000       1010       1020 
RQNLSSKFLE HVEKEKSLQS PAANSRAKSA LTLSLDSSPK SDEESEVISV KTKSKTRRIL 

      1030       1040       1050       1060       1070       1080 
SDDEDEDEED AFKGSHTNSI NISPFPFSSV KQFDASTPQS GSNPSRRFFS PKTPGEVNTS 

      1090       1100       1110       1120       1130       1140 
LHSRRSLASR RSLINVVLDD VEDMEERLDN SSEEESEPGL SEENNEEEAL ACTEEQPSGA 

      1150       1160       1170       1180       1190       1200 
TLASGNKSSN LTMSEPTSPA PQSSPCAPEP SSSDPMPDPP QDLAVEAGND YESLVARGKE 

      1210       1220       1230       1240 
LKECGKIQEA LNCLVKALDI KSADPEVMLM TLSLYKQLNI 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and expression analysis of mouse gene encoding the protein Ercc6l which is a novel member of SNF2 family."
Chen X.-G., Li Y., Zang M.-X., Pei X.-R., Xu Y.-J., Fang L.-F.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 31:443-448(2004)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Heart.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Heart and Skin.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"Ercc6l, a gene of SNF2 family, may play a role in the teratogenic action of alcohol."
Xu Y.-J., Chen X.-G., Li Y.
Toxicol. Lett. 157:233-239(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1021, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS30321.1.
RefSeqNP_666347.2. NM_146235.3.
UniGeneMm.31911.

3D structure databases

ProteinModelPortalQ8BHK9.
SMRQ8BHK9. Positions 100-630.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231820. 7 interactions.
IntActQ8BHK9. 7 interactions.

PTM databases

PhosphoSiteQ8BHK9.

Proteomic databases

MaxQBQ8BHK9.
PaxDbQ8BHK9.
PRIDEQ8BHK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056904; ENSMUSP00000050592; ENSMUSG00000051220.
GeneID236930.
KEGGmmu:236930.
UCSCuc009tyk.2. mouse.

Organism-specific databases

CTD54821.
MGIMGI:2654144. Ercc6l.

Phylogenomic databases

eggNOGCOG0553.
GeneTreeENSGT00590000083118.
HOGENOMHOG000074172.
HOVERGENHBG107854.
InParanoidQ8BHK9.
OMAICEMPSL.
OrthoDBEOG76DTRN.
PhylomeDBQ8BHK9.
TreeFamTF332843.

Gene expression databases

ArrayExpressQ8BHK9.
BgeeQ8BHK9.
GenevestigatorQ8BHK9.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio383173.
PROQ8BHK9.
SOURCESearch...

Entry information

Entry nameERC6L_MOUSE
AccessionPrimary (citable) accession number: Q8BHK9
Secondary accession number(s): Q8BGN1, Q8BRC9, Q8CE49
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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