Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

O96017 · CHK2_HUMAN

  • Protein
    Serine/threonine-protein kinase Chk2
  • Gene
    CHEK2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest, activation of DNA repair and apoptosis in response to the presence of DNA double-strand breaks. May also negatively regulate cell cycle progression during unperturbed cell cycles. Following activation, phosphorylates numerous effectors preferentially at the consensus sequence [L-X-R-X-X-S/T] (PubMed:37943659).
Regulates cell cycle checkpoint arrest through phosphorylation of CDC25A, CDC25B and CDC25C, inhibiting their activity. Inhibition of CDC25 phosphatase activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. May also phosphorylate NEK6 which is involved in G2/M cell cycle arrest. Regulates DNA repair through phosphorylation of BRCA2, enhancing the association of RAD51 with chromatin which promotes DNA repair by homologous recombination. Also stimulates the transcription of genes involved in DNA repair (including BRCA2) through the phosphorylation and activation of the transcription factor FOXM1. Regulates apoptosis through the phosphorylation of p53/TP53, MDM4 and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 may alleviate inhibition by MDM2, leading to accumulation of active p53/TP53. Phosphorylation of MDM4 may also reduce degradation of p53/TP53. Also controls the transcription of pro-apoptotic genes through phosphorylation of the transcription factor E2F1. Tumor suppressor, it may also have a DNA damage-independent function in mitotic spindle assembly by phosphorylating BRCA1. Its absence may be a cause of the chromosomal instability observed in some cancer cells. Promotes the CCAR2-SIRT1 association and is required for CCAR2-mediated SIRT1 inhibition (PubMed:25361978).
Under oxidative stress, promotes ATG7 ubiquitination by phosphorylating the E3 ubiquitin ligase TRIM32 at 'Ser-55' leading to positive regulation of the autophagosme assembly (PubMed:37943659).
(Microbial infection) Phosphorylates herpes simplex virus 1/HHV-1 protein ICP0 and thus activates its SUMO-targeted ubiquitin ligase activity.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Activated through phosphorylation at Thr-68 by ATM in response to DNA double-strand breaks. Activation is modulated by several mediators including MDC1 and TP53BP1. Induces homodimerization with exchange of the T-loop/activation segment between protomers and transphosphorylation of the protomers. The autophosphorylated kinase dimer is fully active. Negatively regulated by PPM1D through dephosphorylation of Thr-68.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site227-234ATP (UniProtKB | ChEBI)
Binding site249ATP (UniProtKB | ChEBI)
Binding site302-308ATP (UniProtKB | ChEBI)
Active site347Proton acceptor
Binding site351-352ATP (UniProtKB | ChEBI)
Binding site368ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentGolgi apparatus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentPML body
Molecular FunctionATP binding
Molecular Functionhistone H2AS1 kinase activity
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functionprotein homodimerization activity
Molecular Functionprotein kinase binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionubiquitin protein ligase binding
Biological Processcell division
Biological Processcellular response to gamma radiation
Biological Processcellular response to stress
Biological ProcessDNA damage checkpoint signaling
Biological ProcessDNA damage response
Biological ProcessDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
Biological ProcessDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator
Biological Processdouble-strand break repair
Biological ProcessG2/M transition of mitotic cell cycle
Biological Processintrinsic apoptotic signaling pathway in response to DNA damage
Biological Processintrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
Biological Processmitotic DNA damage checkpoint signaling
Biological Processmitotic intra-S DNA damage checkpoint signaling
Biological Processmitotic spindle assembly
Biological Processpositive regulation of DNA-templated transcription
Biological Processprotein autophosphorylation
Biological Processprotein catabolic process
Biological Processprotein phosphorylation
Biological Processprotein stabilization
Biological Processregulation of autophagosome assembly
Biological Processregulation of DNA-templated transcription
Biological Processregulation of protein catabolic process
Biological Processregulation of signal transduction by p53 class mediator
Biological Processreplicative senescence
Biological Processsignal transduction in response to DNA damage
Biological Processthymocyte apoptotic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase Chk2
  • EC number
  • Alternative names
    • CHK2 checkpoint homolog
    • Cds1 homolog (Hucds1; hCds1)
    • Checkpoint kinase 2

Gene names

    • Name
      CHEK2
    • Synonyms
      CDS1, CHK2, RAD53

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O96017
  • Secondary accessions
    • A8K3Y9
    • B7ZBF3
    • B7ZBF4
    • B7ZBF5
    • Q6QA03

Proteomes

Organism-specific databases

Subcellular Location

Note: Recruited into PML bodies together with TP53.

Isoform 2

Note: Isoform 10 is present throughout the cell.

Isoform 4

Isoform 7

Isoform 9

Isoform 12

Keywords

Disease & Variants

Involvement in disease

Tumor predisposition syndrome 4 (TPDS4)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A disorder characterized by an increased risk for developing various types of benign and/or malignant neoplasms that arise at an accelerated rate and in different organs.
  • See also
    MIM:609265
Natural variants in TPDS4
Variant IDPosition(s)ChangeDescription
VAR_008554145R>Win TPDS4; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation; dbSNP:rs137853007

Prostate cancer (PC)

  • Note
    • Disease susceptibility is associated with variants affecting the gene represented in this entry
  • Description
    A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.
  • See also
    MIM:176807

Osteogenic sarcoma (OSRC)

  • Note
    • The gene represented in this entry may be involved in disease pathogenesis
  • Description
    A sarcoma originating in bone-forming cells, affecting the ends of long bones.
  • See also
    MIM:259500

Breast cancer (BC)

  • Note
    • Disease susceptibility is associated with variants affecting the gene represented in this entry
  • Description
    A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.
  • See also
    MIM:114480
Natural variants in BC
Variant IDPosition(s)ChangeDescription
VAR_022461117R>Gin BC; dbSNP:rs28909982
VAR_073020390Y>Cin BC; does not phosphorylate p53/TP53; dbSNP:rs200928781

Features

Showing features for natural variant, mutagenesis.

Type
IDPosition(s)Description
Natural variantVAR_01910117found in an osteogenic sarcoma sample; somatic mutation; might influence susceptibility to breast cancer; dbSNP:rs137853008
Natural variantVAR_02663059in multiple cancers; dbSNP:rs149991239
Natural variantVAR_01910764in prostate cancer; somatic mutation; dbSNP:rs141568342
Mutagenesis68Loss of activation and phosphorylation.
Mutagenesis73Impaired activation, phosphorylation by ATM and G2/M transition checkpoint.
Natural variantVAR_01910285found in an osteogenic sarcoma sample; somatic mutation; dbSNP:rs17883862
Natural variantVAR_022461117in BC; dbSNP:rs28909982
Natural variantVAR_022462137might influence susceptibility to breast cancer; dbSNP:rs368570187
Natural variantVAR_019108145in prostate cancer; somatic mutation; dbSNP:rs587781667
Natural variantVAR_008554145in TPDS4; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation; dbSNP:rs137853007
Natural variantVAR_008555157might influence susceptibility to different types of cancer; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation; dbSNP:rs17879961
Natural variantVAR_019109167in prostate cancer; somatic mutation; dbSNP:rs72552322
Natural variantVAR_019103180in prostate cancer; somatic mutation; dbSNP:rs77130927
Natural variantVAR_019110180in prostate cancer; somatic mutation; dbSNP:rs137853009
Natural variantVAR_019104181in prostate cancer; somatic mutation; dbSNP:rs137853010
Natural variantVAR_019105181in prostate cancer; somatic mutation; dbSNP:rs121908701
Natural variantVAR_019106239in prostate cancer; germline mutation; dbSNP:rs121908702
Natural variantVAR_019111251in prostate cancer; uncertain significance; dbSNP:rs587780189
Natural variantVAR_019112318in prostate cancer; uncertain significance; somatic mutation; dbSNP:rs143611747
Natural variantVAR_019113323in prostate cancer; somatic mutation; dbSNP:rs750984976
Natural variantVAR_019114327in prostate cancer; uncertain significance; somatic mutation; dbSNP:rs587780194
Natural variantVAR_029154347in dbSNP:rs28909980
Mutagenesis347Loss of kinase activity and of the ability to phosphorylate CDC25A.
Mutagenesis368Loss of autophosphorylation activity.
Natural variantVAR_066012371confers a moderate risk of breast cancer; partially reduces kinase activity; dbSNP:rs531398630
Mutagenesis379Abrogates autophosphorylation at Ser-379 and prevents ubiquitination.
Mutagenesis383Loss of phosphorylation in response to ionizing radiation.
Mutagenesis387Loss of phosphorylation in response to ionizing radiation.
Natural variantVAR_073020390in BC; does not phosphorylate p53/TP53; dbSNP:rs200928781
Natural variantVAR_024572406in dbSNP:rs200649225
Natural variantVAR_022463428may increase breast cancer risk; dbSNP:rs137853011
Natural variantVAR_021117436in dbSNP:rs17882922
Natural variantVAR_021118446in dbSNP:rs17880867
Natural variantVAR_021119447in dbSNP:rs17881473
Natural variantVAR_021120448in dbSNP:rs17886163
Mutagenesis456Increased ubiquitination and degradation by the proteasome.
Natural variantVAR_019115476in prostate cancer; somatic mutation
Natural variantVAR_029155500in dbSNP:rs28909981
Natural variantVAR_021121501in dbSNP:rs17883172
Natural variantVAR_021122512in dbSNP:rs17882942

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 2,897 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

Type
IDPosition(s)Source
Description
ChainPRO_00000858581-543UniProtSerine/threonine-protein kinase Chk2
Modified residue62UniProtPhosphoserine; by PLK3
Modified residue68UniProtPhosphothreonine; by ATM and MAP3K20
Modified residue73UniProtPhosphoserine; by PLK3
Modified residue (large scale data)120PRIDEPhosphoserine
Modified residue (large scale data)225PRIDEPhosphothreonine
Modified residue (large scale data)260PRIDEPhosphoserine
Modified residue (large scale data)378PRIDEPhosphothreonine
Modified residue379UniProtPhosphoserine; by autocatalysis
Modified residue (large scale data)379PRIDEPhosphoserine
Modified residue383UniProtPhosphothreonine; by autocatalysis
Modified residue (large scale data)383PRIDEPhosphothreonine
Modified residue387UniProtPhosphothreonine; by autocatalysis
Modified residue (large scale data)389PRIDEPhosphothreonine
Modified residue456UniProtPhosphoserine

Post-translational modification

Phosphorylated. Phosphorylated at Ser-73 by PLK3 in response to DNA damage, promoting phosphorylation at Thr-68 by ATM and the G2/M transition checkpoint. Phosphorylation at Thr-68 induces homodimerization. Autophosphorylates at Thr-383 and Thr-387 in the T-loop/activation segment upon dimerization to become fully active and phosphorylate its substrates like for instance CDC25C. DNA damage-induced autophosphorylation at Ser-379 induces CUL1-mediated ubiquitination and regulates the pro-apoptotic function. Phosphorylation at Ser-456 also regulates ubiquitination. Phosphorylated by PLK4.
Ubiquitinated. CUL1-mediated ubiquitination regulates the pro-apoptotic function. Ubiquitination may also regulate protein stability. Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

High expression is found in testis, spleen, colon and peripheral blood leukocytes. Low expression is found in other tissues.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homodimer. Homodimerization is part of the activation process but the dimer may dissociate following activation. Interacts with PML. Interacts with TP53. Interacts with RB1; phosphorylates RB1. Interacts with BRCA1. Interacts (phosphorylated at Thr-68) with MDC1; requires ATM-mediated phosphorylation of CHEK2. Interacts with TP53BP1; modulates CHEK2 phosphorylation at Thr-68 in response to ionizing radiation. Interacts with CDC25A; phosphorylates CDC25A and mediates its degradation in response to ionizing radiation. Interacts with CUL1; mediates CHEK2 ubiquitination and regulation. Interacts with CDKN2AIP. Interacts (via protein kinase domain) with CCAR2 (via N-terminus). Interacts with SIRT1.

Binary interactions

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-66Disordered
Compositional bias7-66Polar residues
Domain113-175FHA
Domain220-486Protein kinase
Region368-394T-loop/activation segment
Region506-538Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

  • Sequence status
    Complete

This entry describes 13 isoforms produced by Alternative splicing.

O96017-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    1
  • Note
    Lacks enzymatic activity.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    543
  • Mass (Da)
    60,915
  • Last updated
    1999-05-01 v1
  • MD5 Checksum
    D4BFE45A8F3D01CBF5EAC244D893BA1A
MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAETTKRPAVCAAVL

O96017-2

  • Name
    2
  • Synonyms
    ins2
  • Note
    Lacks enzymatic activity.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 198-224: VFVFFDLTVDDQSVYPKALRDEYIMSK → EKILKIYSLSRFSKIRRGAVAHVFNPS
    • 228-234: SGACGEV → GRGWQIT
    • 235-543: Missing

O96017-3

  • Name
    3
  • Synonyms
    del2-12
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O96017-4

  • Name
    4
  • Synonyms
    del2-3
  • Note
    Lacks enzymatic activity.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O96017-5

  • Name
    5
  • Synonyms
    del4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O96017-6

  • Name
    6
  • Synonyms
    sub3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O96017-7

  • Name
    7
  • Synonyms
    del9-12
  • Note
    Lacks enzymatic activity.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O96017-8

  • Name
    8
  • Synonyms
    del7
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O96017-9

  • Name
    9
  • Synonyms
    insx
  • Note
    Retains low level of catalytic activity.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 107-107: E → ETESGHVTQSDLELLLSSDPPASASQSAGIRGVRHHPRPVCSLK

O96017-10

  • Name
    10
  • Synonyms
    iso2
  • Note
    Lacks enzymatic activity.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O96017-11

  • Name
    11
  • Synonyms
    iso1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O96017-12

  • Name
    12
  • Synonyms
    del9
  • Note
    Lacks enzymatic activity.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O96017-13

  • Name
    13
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 13 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A7P0MUT5A0A7P0MUT5_HUMANCHEK2476
F8WCV2F8WCV2_HUMANCHEK2161
B7ZBF2B7ZBF2_HUMANCHEK2121
B7ZBF7B7ZBF7_HUMANCHEK2295
B7ZBF8B7ZBF8_HUMANCHEK2162
C9JFD7C9JFD7_HUMANCHEK2207
H0Y820H0Y820_HUMANCHEK2276
H0Y4V6H0Y4V6_HUMANCHEK2144
A0AA34QVK6A0AA34QVK6_HUMANCHEK2337
H7BZ30H7BZ30_HUMANCHEK2167
H7C0V7H7C0V7_HUMANCHEK257
A0A3B3ITA7A0A3B3ITA7_HUMANCHEK2176
A0A087X102A0A087X102_HUMANCHEK2323

Features

Showing features for alternative sequence, compositional bias.

Type
IDPosition(s)Description
Alternative sequenceVSP_0451481-221in isoform 13
Compositional bias7-66Polar residues
Alternative sequenceVSP_01455675-392in isoform 11
Alternative sequenceVSP_014557107in isoform 9
Alternative sequenceVSP_014558107-197in isoform 4
Alternative sequenceVSP_014559107-487in isoform 3
Alternative sequenceVSP_014560131-147in isoform 10
Alternative sequenceVSP_014561148-543in isoform 10
Alternative sequenceVSP_014562150-165in isoform 6
Alternative sequenceVSP_014563166-543in isoform 6
Alternative sequenceVSP_014564198-224in isoform 2
Alternative sequenceVSP_014565199-203in isoform 5
Alternative sequenceVSP_014566204-543in isoform 5
Alternative sequenceVSP_014567228-234in isoform 2
Alternative sequenceVSP_014568235-543in isoform 2
Alternative sequenceVSP_014569283-289in isoform 8
Alternative sequenceVSP_014570290-543in isoform 8
Alternative sequenceVSP_014572337-339in isoform 7
Alternative sequenceVSP_014571337-365in isoform 12
Alternative sequenceVSP_014573340-543in isoform 7

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF086904
EMBL· GenBank· DDBJ
AAC83693.1
EMBL· GenBank· DDBJ
mRNA
AJ131197
EMBL· GenBank· DDBJ
CAA10319.1
EMBL· GenBank· DDBJ
mRNA
AF096279
EMBL· GenBank· DDBJ
AAD11784.1
EMBL· GenBank· DDBJ
mRNA
AY551295
EMBL· GenBank· DDBJ
AAS58456.1
EMBL· GenBank· DDBJ
mRNA
AY551296
EMBL· GenBank· DDBJ
AAS58457.1
EMBL· GenBank· DDBJ
mRNA
AY551297
EMBL· GenBank· DDBJ
AAS58458.1
EMBL· GenBank· DDBJ
mRNA
AY551298
EMBL· GenBank· DDBJ
AAS58459.1
EMBL· GenBank· DDBJ
mRNA
AY551299
EMBL· GenBank· DDBJ
AAS58460.1
EMBL· GenBank· DDBJ
mRNA
AY551300
EMBL· GenBank· DDBJ
AAS58461.1
EMBL· GenBank· DDBJ
mRNA
AY551301
EMBL· GenBank· DDBJ
AAS58462.1
EMBL· GenBank· DDBJ
mRNA
AY551302
EMBL· GenBank· DDBJ
AAS58463.1
EMBL· GenBank· DDBJ
mRNA
AY551303
EMBL· GenBank· DDBJ
AAS58464.1
EMBL· GenBank· DDBJ
mRNA
AY551304
EMBL· GenBank· DDBJ
AAS58465.1
EMBL· GenBank· DDBJ
mRNA
AY551305
EMBL· GenBank· DDBJ
AAS58466.1
EMBL· GenBank· DDBJ
mRNA
CR456418
EMBL· GenBank· DDBJ
CAG30304.1
EMBL· GenBank· DDBJ
mRNA
AF174135
EMBL· GenBank· DDBJ
AAD48504.1
EMBL· GenBank· DDBJ
mRNA
AB040105
EMBL· GenBank· DDBJ
BAB17231.1
EMBL· GenBank· DDBJ
mRNA
AK290754
EMBL· GenBank· DDBJ
BAF83443.1
EMBL· GenBank· DDBJ
mRNA
AF217975
EMBL· GenBank· DDBJ
AAG17218.1
EMBL· GenBank· DDBJ
mRNA
AY800241
EMBL· GenBank· DDBJ
AAV41895.1
EMBL· GenBank· DDBJ
Genomic DNA
AL117330
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL121825
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471095
EMBL· GenBank· DDBJ
EAW59755.1
EMBL· GenBank· DDBJ
Genomic DNA
BC004207
EMBL· GenBank· DDBJ
AAH04207.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help