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Protein
Submitted name:

Serine/threonine-protein kinase Chk1

Gene

CHEK1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

SignaLinkiE7EPP6.

Names & Taxonomyi

Protein namesi
Submitted name:
Serine/threonine-protein kinase Chk1Imported
Gene namesi
Name:CHEK1Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:1925. CHEK1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Expressioni

Gene expression databases

BgeeiE7EPP6.
ExpressionAtlasiE7EPP6. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000388648.

Structurei

3D structure databases

ProteinModelPortaliE7EPP6.
SMRiE7EPP6. Positions 65-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00730000111032.
PhylomeDBiE7EPP6.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E7EPP6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSAVLKSLQ PGSLPDCKAA LGGSGNISTS PFWSRRHSEG QDTGTRAVLL
60 70 80 90 100
YGAGARVCGS VTPSSFGGKS AAFGFLQWWA KDSPPRCSVE SWQCPLWKTG
110 120 130 140 150
TWCKPWEKVP MEKPDIGMPE PDAQRFFHQL MAGVVYLHGI GITHRDIKPE
160 170 180 190 200
NLLLDERDNL KISDFGLATV FRYNNRERLL NKMCGTLPYV APELLKRREF
210 220 230 240 250
HAEPVDVWSC GIVLTAMLAG ELPWDQPSDS CQEYSDWKEK KTYLNPWKKI
260 270 280 290 300
DSAPLALLHK ILVENPSARI TIPDIKKDRW YNKPLKKGAK RPRVTSGGVS
310 320 330 340 350
ESPSGFSKHI QSNLDFSPVN SASSEENVKY SSSQPEPRTG LSLWDTSPSY
360 370 380 390 400
IDKLVQGISF SQPTCPDHML LNSQLLGTPG SSQNPWQRLV KRMTRFFTKL
410 420 430 440 450
DADKSYQCLK ETCEKLGYQW KKSCMNQVTI STTDRRNNKL IFKVNLLEMD
460 470 480 490
DKILVDFRLS KGDGLEFKRH FLKIKGKLID IVSSQKIWLP AT
Length:492
Mass (Da):55,518
Last modified:March 8, 2011 - v1
Checksum:i0EF4C429D747EEA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP001132 Genomic DNA. No translation available.
KF455559 Genomic DNA. No translation available.
RefSeqiXP_011540862.1. XM_011542560.1.
XP_011540863.1. XM_011542561.1.
UniGeneiHs.24529.
Hs.595920.

Genome annotation databases

EnsembliENST00000427383; ENSP00000391090; ENSG00000149554.
GeneIDi1111.
UCSCiuc010sbh.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP001132 Genomic DNA. No translation available.
KF455559 Genomic DNA. No translation available.
RefSeqiXP_011540862.1. XM_011542560.1.
XP_011540863.1. XM_011542561.1.
UniGeneiHs.24529.
Hs.595920.

3D structure databases

ProteinModelPortaliE7EPP6.
SMRiE7EPP6. Positions 65-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000388648.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000427383; ENSP00000391090; ENSG00000149554.
GeneIDi1111.
UCSCiuc010sbh.2. human.

Organism-specific databases

HGNCiHGNC:1925. CHEK1.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00730000111032.
PhylomeDBiE7EPP6.

Enzyme and pathway databases

SignaLinkiE7EPP6.

Miscellaneous databases

ChiTaRSiCHEK1. human.
NextBioi35499778.

Gene expression databases

BgeeiE7EPP6.
ExpressionAtlasiE7EPP6. baseline and differential.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiE7EPP6_HUMAN
AccessioniPrimary (citable) accession number: E7EPP6
Entry historyi
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: July 22, 2015
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

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 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.