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Q2NKX8 (ERC6L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
PLK1-interacting checkpoint helicase
Tumor antigen BJ-HCC-15
Gene names
Name:ERCC6L
Synonyms:PICH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1250 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. Ref.1

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. Ref.1 Ref.8

Subcellular location

Chromosomecentromere. Chromosomecentromerekinetochore. 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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8

Post-translational modification

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

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.

Sequence caution

The sequence AAM82750.1 differs from that shown. Reason: Erroneous termination at position 803. Translated as Lys.

The sequence BAA90952.1 differs from that shown. Reason: Erroneous termination at position 803. Translated as Lys.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HTTP428582EBI-1042535,EBI-466029

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12501250DNA excision repair protein ERCC-6-like
PRO_0000328831

Regions

Repeat21 – 5434TPR 1
Domain109 – 277169Helicase ATP-binding
Domain464 – 620157Helicase C-terminal
Repeat1200 – 123334TPR 2
Nucleotide binding122 – 1298ATP Probable
Motif228 – 2314DEAH box

Amino acid modifications

Modified residue141Phosphoserine Ref.9 Ref.10 Ref.13
Modified residue7551Phosphoserine Ref.9
Modified residue7741Phosphoserine Ref.9
Modified residue8071Phosphoserine Ref.13
Modified residue8101Phosphoserine Ref.10 Ref.13
Modified residue8131Phosphothreonine Ref.10
Modified residue8201Phosphoserine Ref.10 Ref.15
Modified residue9951Phosphoserine Ref.13
Modified residue10281Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15
Modified residue10631Phosphothreonine; by PLK1 Ref.1
Modified residue10691Phosphoserine Ref.15
Modified residue10981Phosphoserine Ref.12
Modified residue11811Phosphoserine Ref.9
Modified residue11881Phosphoserine Ref.9

Experimental info

Mutagenesis127 – 1293GKT → AAA: Abolishes chromatin association. Ref.1
Mutagenesis10631T → A: Induces a decrease in phosphorylation. Ref.1
Sequence conflict1451V → M in BAC11160. Ref.3
Sequence conflict1721R → G in BAC11160. Ref.3
Sequence conflict8121A → T in BAA90952. Ref.3
Sequence conflict8121A → T in AAM82750. Ref.4
Sequence conflict8891I → V in BAC11160. Ref.3
Sequence conflict9891R → K in BAA90952. Ref.3
Sequence conflict9891R → K in AAM82750. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q2NKX8 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: C27DB2846F07C45D

FASTA1,250141,103
        10         20         30         40         50         60 
MEASRRFPEA EALSPEQAAH YLRYVKEAKE ATKNGDLEEA FKLFNLAKDI FPNEKVLSRI 

        70         80         90        100        110        120 
QKIQEALEEL AEQGDDEFTD VCNSGLLLYR ELHNQLFEHQ KEGIAFLYSL YRDGRKGGIL 

       130        140        150        160        170        180 
ADDMGLGKTV QIIAFLSGMF DASLVNHVLL IMPTNLINTW VKEFIKWTPG MRVKTFHGPS 

       190        200        210        220        230        240 
KDERTRNLNR IQQRNGVIIT TYQMLINNWQ QLSSFRGQEF VWDYVILDEA HKIKTSSTKS 

       250        260        270        280        290        300 
AICARAIPAS NRLLLTGTPI QNNLQELWSL FDFACQGSLL GTLKTFKMEY ENPITRAREK 

       310        320        330        340        350        360 
DATPGEKALG FKISENLMAI IKPYFLRRTK EDVQKKKSSN PEARLNEKNP DVDAICEMPS 

       370        380        390        400        410        420 
LSRKNDLIIW IRLVPLQEEI YRKFVSLDHI KELLMETRSP LAELGVLKKL CDHPRLLSAR 

       430        440        450        460        470        480 
ACCLLNLGTF SAQDGNEGED SPDVDHIDQV TDDTLMEESG KMIFLMDLLK RLRDEGHQTL 

       490        500        510        520        530        540 
VFSQSRQILN IIERLLKNRH FKTLRIDGTV THLLEREKRI NLFQQNKDYS VFLLTTQVGG 

       550        560        570        580        590        600 
VGLTLTAATR VVIFDPSWNP ATDAQAVDRV YRIGQKENVV VYRLITCGTV EEKIYRRQVF 

       610        620        630        640        650        660 
KDSLIRQTTG EKKNPFRYFS KQELRELFTI EDLQNSVTQL QLQSLHAAQR KSDIKLDEHI 

       670        680        690        700        710        720 
AYLQSLGIAG ISDHDLMYTC DLSVKEELDV VEESHYIQQR VQKAQFLVEF ESQNKEFLME 

       730        740        750        760        770        780 
QQRTRNEGAW LREPVFPSST KKKCPKLNKP QPQPSPLLST HHTQEEDISS KMASVVIDDL 

       790        800        810        820        830        840 
PKEGEKQDLS SIKVNVTTLQ DGKGTGSADS IATLPKGFGS VEELCTNSSL GMEKSFATKN 

       850        860        870        880        890        900 
EAVQKETLQE GPKQEALQED PLESFNYVLS KSTKADIGPN LDQLKDDEIL RHCNPWPIIS 

       910        920        930        940        950        960 
ITNESQNAES NVSIIEIADD LSASHSALQD AQASEAKLEE EPSASSPQYA CDFNLFLEDS 

       970        980        990       1000       1010       1020 
ADNRQNFSSQ SLEHVEKENS LCGSAPNSRA GFVHSKTCLS WEFSEKDDEP EEVVVKAKIR 

      1030       1040       1050       1060       1070       1080 
SKARRIVSDG EDEDDSFKDT SSINPFNTSL FQFSSVKQFD ASTPKNDISP PGRFFSSQIP 

      1090       1100       1110       1120       1130       1140 
SSVNKSMNSR RSLASRRSLI NMVLDHVEDM EERLDDSSEA KGPEDYPEEG VEESSGEASK 

      1150       1160       1170       1180       1190       1200 
YTEEDPSGET LSSENKSSWL MTSKPSALAQ ETSLGAPEPL SGEQLVGSPQ DKAAEATNDY 

      1210       1220       1230       1240       1250 
ETLVKRGKEL KECGKIQEAL NCLVKALDIK SADPEVMLLT LSLYKQLNNN 

« Hide

References

« Hide 'large scale' references
[1]"PICH, a centromere-associated SNF2 family ATPase, is regulated by Plk1 and required for the spindle checkpoint."
Baumann C., Koerner R., Hofmann K., Nigg E.A.
Cell 128:101-114(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1063, INTERACTION WITH PLK1, MUTAGENESIS OF 127-GLY--THR-129 AND THR-1063.
[2]"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].
Tissue: Ovary and Uterus.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-1250.
Tissue: Colon and Teratocarcinoma.
[4]"Cloning and identification of genes which are differentially expressed in carcinoma."
Xueyuan D., Weifeng C.
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 603-1250.
[5]"Persistence of DNA threads in human anaphase cells suggests late completion of sister chromatid decatenation."
Wang L.-H., Schwarzbraun T., Speicher M.R., Nigg E.A.
Chromosoma 117:123-135(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"BLM is required for faithful chromosome segregation and its localization defines a class of ultrafine anaphase bridges."
Chan K.-L., North P.S., Hickson I.D.
EMBO J. 26:3397-3409(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Depletion of topoisomerase IIalpha leads to shortening of the metaphase interkinetochore distance and abnormal persistence of PICH-coated anaphase threads."
Spence J.M., Phua H.-H., Mills W., Carpenter A.J., Porter A.C.G., Farr C.J.
J. Cell Sci. 120:3952-3964(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Use of the novel Plk1 inhibitor ZK-thiazolidinone to elucidate functions of Plk1 in early and late stages of mitosis."
Santamaria A., Neef R., Eberspaecher U., Eis K., Husemann M., Mumberg D., Prechtl S., Schulze V., Siemeister G., Wortmann L., Barr F.A., Nigg E.A.
Mol. Biol. Cell 18:4024-4036(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PLK1.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-755; SER-774; SER-1181 AND SER-1188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-810; THR-813; SER-820 AND SER-1028, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028 AND SER-1098, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-807; SER-810; SER-995 AND SER-1028, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820; SER-1028 AND SER-1069, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU069463 mRNA. Translation: ABU25227.1.
BC008808 mRNA. Translation: AAH08808.2.
BC111486 mRNA. Translation: AAI11487.1.
AK000112 mRNA. Translation: BAA90952.1. Sequence problems.
AK074719 mRNA. Translation: BAC11160.1.
AY121802 mRNA. Translation: AAM82750.1. Sequence problems.
CCDSCCDS35329.1.
RefSeqNP_060139.2. NM_017669.2.
UniGeneHs.47558.

3D structure databases

ProteinModelPortalQ2NKX8.
SMRQ2NKX8. Positions 92-632.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120176. 10 interactions.
IntActQ2NKX8. 9 interactions.
STRING9606.ENSP00000334675.

PTM databases

PhosphoSiteQ2NKX8.

Polymorphism databases

DMDM121948339.

Proteomic databases

MaxQBQ2NKX8.
PaxDbQ2NKX8.
PeptideAtlasQ2NKX8.
PRIDEQ2NKX8.

Protocols and materials databases

DNASU54821.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334463; ENSP00000334675; ENSG00000186871.
GeneID54821.
KEGGhsa:54821.
UCSCuc004eap.1. human.

Organism-specific databases

CTD54821.
GeneCardsGC0XM071424.
H-InvDBHIX0016867.
HGNCHGNC:20794. ERCC6L.
HPAHPA050492.
MIM300687. gene.
neXtProtNX_Q2NKX8.
PharmGKBPA162385290.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000074172.
HOVERGENHBG107854.
InParanoidQ2NKX8.
OMAICEMPSL.
PhylomeDBQ2NKX8.
TreeFamTF332843.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ2NKX8.
BgeeQ2NKX8.
CleanExHS_ERCC6L.
GenevestigatorQ2NKX8.

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.
IPR013026. TPR-contain_dom.
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.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi54821.
NextBio57573.
PROQ2NKX8.
SOURCESearch...

Entry information

Entry nameERC6L_HUMAN
AccessionPrimary (citable) accession number: Q2NKX8
Secondary accession number(s): Q8NCI1, Q96H93, Q9NXQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: February 7, 2006
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM