STK38L

Protein-coding gene in the species Homo sapiens
STK38L
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1PSB

Identifiers
AliasesSTK38L, NDR2, serine/threonine kinase 38 like
External IDsOMIM: 615836; MGI: 1922250; HomoloGene: 56299; GeneCards: STK38L; OMA:STK38L - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for STK38L
Genomic location for STK38L
Band12p11.23Start27,243,968 bp[1]
End27,325,959 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for STK38L
Genomic location for STK38L
Band6|6 G3Start146,626,493 bp[2]
End146,680,310 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ascending aorta

  • popliteal artery

  • tibial arteries

  • Achilles tendon

  • right coronary artery

  • Descending thoracic aorta

  • saphenous vein

  • left coronary artery

  • epithelium of colon

  • monocyte
Top expressed in
  • ascending aorta

  • aortic valve

  • left colon

  • facial motor nucleus

  • secondary oocyte

  • otolith organ

  • utricle

  • blastocyst

  • anterior horn of spinal cord

  • Region I of hippocampus proper
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • kinase activity
  • transferase activity
  • nucleotide binding
  • actin binding
  • protein serine/threonine kinase activity
  • protein kinase activity
  • protein binding
  • ATP binding
  • magnesium ion binding
  • metal ion binding
Cellular component
  • cytoplasm
  • cytoskeleton
  • membrane
  • actin cytoskeleton
  • cytosol
Biological process
  • protein phosphorylation
  • regulation of cellular component organization
  • intracellular signal transduction
  • peptidyl-serine phosphorylation
  • phosphorylation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23012

232533

Ensembl

ENSG00000211455

ENSMUSG00000001630

UniProt

Q9Y2H1

Q7TSE6

RefSeq (mRNA)

NM_015000

NM_172734
NM_001346666

RefSeq (protein)

NP_055815

NP_001333595
NP_766322

Location (UCSC)Chr 12: 27.24 – 27.33 MbChr 6: 146.63 – 146.68 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Serine/threonine-protein kinase 38-like is an enzyme that in humans is encoded by the STK38L gene.[5][6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000211455 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001630 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Suzuki A, Ogura T, Esumi H (May 2006). "NDR2 acts as the upstream kinase of ARK5 during insulin-like growth factor-1 signaling". J Biol Chem. 281 (20): 13915–21. doi:10.1074/jbc.M511354200. PMID 16488889.
  6. ^ "Entrez Gene: STK38L serine/threonine kinase 38 like".

Further reading

  • Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
  • Nagase T, Ishikawa K, Suyama M, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID 10231032.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Stegert MR, Tamaskovic R, Bichsel SJ, et al. (2004). "Regulation of NDR2 protein kinase by multi-site phosphorylation and the S100B calcium-binding protein". J. Biol. Chem. 279 (22): 23806–12. doi:10.1074/jbc.M402472200. PMID 15037617.
  • Devroe E, Erdjument-Bromage H, Tempst P, Silver PA (2004). "Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases". J. Biol. Chem. 279 (23): 24444–51. doi:10.1074/jbc.M401999200. PMID 15067004.
  • Bichsel SJ, Tamaskovic R, Stegert MR, Hemmings BA (2005). "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein". J. Biol. Chem. 279 (34): 35228–35. doi:10.1074/jbc.M404542200. PMID 15197186.
  • Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Devroe E, Silver PA, Engelman A (2005). "HIV-1 incorporates and proteolytically processes human NDR1 and NDR2 serine-threonine kinases". Virology. 331 (1): 181–9. doi:10.1016/j.virol.2004.10.023. PMID 15582665.
  • Stegert MR, Hergovich A, Tamaskovic R, et al. (2006). "Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3". Mol. Cell. Biol. 25 (24): 11019–29. doi:10.1128/MCB.25.24.11019-11029.2005. PMC 1316964. PMID 16314523.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  • v
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
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IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
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Tropomyosin kinase (EC 2.7.11.28)
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Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
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Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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