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Q2NKX8

- ERC6L_HUMAN

UniProt

Q2NKX8 - ERC6L_HUMAN

Protein

DNA excision repair protein ERCC-6-like

Gene

ERCC6L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (07 Feb 2006)
      Previous versions | rss
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    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.1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi122 – 1298ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. helicase activity Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. mitotic cell cycle Source: Reactome
    2. mitotic nuclear division Source: UniProtKB-KW

    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

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. 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
    PLK1-interacting checkpoint helicase
    Tumor antigen BJ-HCC-15
    Gene namesi
    Name:ERCC6L
    Synonyms:PICH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:20794. ERCC6L.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi127 – 1293GKT → AAA: Abolishes chromatin association.
    Mutagenesisi1063 – 10631T → A: Induces a decrease in phosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA162385290.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12501250DNA excision repair protein ERCC-6-likePRO_0000328831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphoserine3 Publications
    Modified residuei755 – 7551Phosphoserine1 Publication
    Modified residuei774 – 7741Phosphoserine1 Publication
    Modified residuei807 – 8071Phosphoserine1 Publication
    Modified residuei810 – 8101Phosphoserine2 Publications
    Modified residuei813 – 8131Phosphothreonine1 Publication
    Modified residuei820 – 8201Phosphoserine2 Publications
    Modified residuei995 – 9951Phosphoserine1 Publication
    Modified residuei1028 – 10281Phosphoserine4 Publications
    Modified residuei1063 – 10631Phosphothreonine; by PLK11 Publication
    Modified residuei1069 – 10691Phosphoserine1 Publication
    Modified residuei1098 – 10981Phosphoserine1 Publication
    Modified residuei1181 – 11811Phosphoserine1 Publication
    Modified residuei1188 – 11881Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation by PLK1 prevents the association with chromosome arms and restricts its localization to the kinetochore-centromere region.6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ2NKX8.
    PaxDbiQ2NKX8.
    PeptideAtlasiQ2NKX8.
    PRIDEiQ2NKX8.

    PTM databases

    PhosphoSiteiQ2NKX8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ2NKX8.
    BgeeiQ2NKX8.
    CleanExiHS_ERCC6L.
    GenevestigatoriQ2NKX8.

    Organism-specific databases

    HPAiHPA050492.

    Interactioni

    Subunit structurei

    Interacts with PLK1, which phosphorylates it. Both proteins are mutually dependent on each other for correct subcellular localization.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428582EBI-1042535,EBI-466029

    Protein-protein interaction databases

    BioGridi120176. 10 interactions.
    IntActiQ2NKX8. 9 interactions.
    STRINGi9606.ENSP00000334675.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2NKX8.
    SMRiQ2NKX8. Positions 92-632.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati21 – 5434TPR 1Add
    BLAST
    Domaini109 – 277169Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini464 – 620157Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Repeati1200 – 123334TPR 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi228 – 2314DEAH box

    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

    eggNOGiCOG0553.
    HOGENOMiHOG000074172.
    HOVERGENiHBG107854.
    InParanoidiQ2NKX8.
    OMAiICEMPSL.
    PhylomeDBiQ2NKX8.
    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.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    [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.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2NKX8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEASRRFPEA EALSPEQAAH YLRYVKEAKE ATKNGDLEEA FKLFNLAKDI     50
    FPNEKVLSRI QKIQEALEEL AEQGDDEFTD VCNSGLLLYR ELHNQLFEHQ 100
    KEGIAFLYSL YRDGRKGGIL ADDMGLGKTV QIIAFLSGMF DASLVNHVLL 150
    IMPTNLINTW VKEFIKWTPG MRVKTFHGPS KDERTRNLNR IQQRNGVIIT 200
    TYQMLINNWQ QLSSFRGQEF VWDYVILDEA HKIKTSSTKS AICARAIPAS 250
    NRLLLTGTPI QNNLQELWSL FDFACQGSLL GTLKTFKMEY ENPITRAREK 300
    DATPGEKALG FKISENLMAI IKPYFLRRTK EDVQKKKSSN PEARLNEKNP 350
    DVDAICEMPS LSRKNDLIIW IRLVPLQEEI YRKFVSLDHI KELLMETRSP 400
    LAELGVLKKL CDHPRLLSAR ACCLLNLGTF SAQDGNEGED SPDVDHIDQV 450
    TDDTLMEESG KMIFLMDLLK RLRDEGHQTL VFSQSRQILN IIERLLKNRH 500
    FKTLRIDGTV THLLEREKRI NLFQQNKDYS VFLLTTQVGG VGLTLTAATR 550
    VVIFDPSWNP ATDAQAVDRV YRIGQKENVV VYRLITCGTV EEKIYRRQVF 600
    KDSLIRQTTG EKKNPFRYFS KQELRELFTI EDLQNSVTQL QLQSLHAAQR 650
    KSDIKLDEHI AYLQSLGIAG ISDHDLMYTC DLSVKEELDV VEESHYIQQR 700
    VQKAQFLVEF ESQNKEFLME QQRTRNEGAW LREPVFPSST KKKCPKLNKP 750
    QPQPSPLLST HHTQEEDISS KMASVVIDDL PKEGEKQDLS SIKVNVTTLQ 800
    DGKGTGSADS IATLPKGFGS VEELCTNSSL GMEKSFATKN EAVQKETLQE 850
    GPKQEALQED PLESFNYVLS KSTKADIGPN LDQLKDDEIL RHCNPWPIIS 900
    ITNESQNAES NVSIIEIADD LSASHSALQD AQASEAKLEE EPSASSPQYA 950
    CDFNLFLEDS ADNRQNFSSQ SLEHVEKENS LCGSAPNSRA GFVHSKTCLS 1000
    WEFSEKDDEP EEVVVKAKIR SKARRIVSDG EDEDDSFKDT SSINPFNTSL 1050
    FQFSSVKQFD ASTPKNDISP PGRFFSSQIP SSVNKSMNSR RSLASRRSLI 1100
    NMVLDHVEDM EERLDDSSEA KGPEDYPEEG VEESSGEASK YTEEDPSGET 1150
    LSSENKSSWL MTSKPSALAQ ETSLGAPEPL SGEQLVGSPQ DKAAEATNDY 1200
    ETLVKRGKEL KECGKIQEAL NCLVKALDIK SADPEVMLLT LSLYKQLNNN 1250
    Length:1,250
    Mass (Da):141,103
    Last modified:February 7, 2006 - v1
    Checksum:iC27DB2846F07C45D
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451V → M in BAC11160. (PubMed:14702039)Curated
    Sequence conflicti172 – 1721R → G in BAC11160. (PubMed:14702039)Curated
    Sequence conflicti812 – 8121A → T in BAA90952. (PubMed:14702039)Curated
    Sequence conflicti812 – 8121A → T in AAM82750. 1 PublicationCurated
    Sequence conflicti889 – 8891I → V in BAC11160. (PubMed:14702039)Curated
    Sequence conflicti989 – 9891R → K in BAA90952. (PubMed:14702039)Curated
    Sequence conflicti989 – 9891R → K in AAM82750. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS35329.1.
    RefSeqiNP_060139.2. NM_017669.2.
    UniGeneiHs.47558.

    Genome annotation databases

    EnsembliENST00000334463; ENSP00000334675; ENSG00000186871.
    GeneIDi54821.
    KEGGihsa:54821.
    UCSCiuc004eap.1. human.

    Polymorphism databases

    DMDMi121948339.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS35329.1.
    RefSeqi NP_060139.2. NM_017669.2.
    UniGenei Hs.47558.

    3D structure databases

    ProteinModelPortali Q2NKX8.
    SMRi Q2NKX8. Positions 92-632.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120176. 10 interactions.
    IntActi Q2NKX8. 9 interactions.
    STRINGi 9606.ENSP00000334675.

    PTM databases

    PhosphoSitei Q2NKX8.

    Polymorphism databases

    DMDMi 121948339.

    Proteomic databases

    MaxQBi Q2NKX8.
    PaxDbi Q2NKX8.
    PeptideAtlasi Q2NKX8.
    PRIDEi Q2NKX8.

    Protocols and materials databases

    DNASUi 54821.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334463 ; ENSP00000334675 ; ENSG00000186871 .
    GeneIDi 54821.
    KEGGi hsa:54821.
    UCSCi uc004eap.1. human.

    Organism-specific databases

    CTDi 54821.
    GeneCardsi GC0XM071424.
    H-InvDB HIX0016867.
    HGNCi HGNC:20794. ERCC6L.
    HPAi HPA050492.
    MIMi 300687. gene.
    neXtProti NX_Q2NKX8.
    PharmGKBi PA162385290.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOGENOMi HOG000074172.
    HOVERGENi HBG107854.
    InParanoidi Q2NKX8.
    OMAi ICEMPSL.
    PhylomeDBi Q2NKX8.
    TreeFami TF332843.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    GenomeRNAii 54821.
    NextBioi 57573.
    PROi Q2NKX8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q2NKX8.
    Bgeei Q2NKX8.
    CleanExi HS_ERCC6L.
    Genevestigatori Q2NKX8.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    3.40.50.300. 2 hits.
    InterProi IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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].

    Entry informationi

    Entry nameiERC6L_HUMAN
    AccessioniPrimary (citable) accession number: Q2NKX8
    Secondary accession number(s): Q8NCI1, Q96H93, Q9NXQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

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