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Q2NKX8

- ERC6L_HUMAN

UniProt

Q2NKX8 - ERC6L_HUMAN

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Protein
DNA excision repair protein ERCC-6-like
Gene
ERCC6L, PICH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

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

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
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

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.5 Publications

GO - Cellular componenti

  1. condensed chromosome kinetochore Source: UniProtKB-SubCell
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1293GKT → AAA: Abolishes chromatin association. 1 Publication
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-like
PRO_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.

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.

Family & Domainsi

Domains and Repeats

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

Motif

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

Sequence similaritiesi

Contains 2 TPR repeats.

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.

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 90 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

Dasty 3

Similar proteinsi