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STK38L

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

STK38L

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
1PSB

Identifiers

Aliases

STK38L, NDR2, serine/threonine kinase 38 like

External IDs

OMIM:615836;MGI:1922250;HomoloGene:56299;GeneCards:STK38L;OMA:STK38L - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12p11.23	Start	27,243,968bp^[1]
Band	12p11.23	End	27,325,959bp^[1]

Gene location (Mouse)

Chr.	Chromosome 6 (mouse)^[2]

Band	6\|6 G3	Start	146,626,493bp^[2]
Band	6\|6 G3	End	146,680,310bp^[2]

RNA expression pattern

Bgee

Human

Mouse (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

tail of embryo

facial motor nucleus

secondary oocyte

otolith organ

utricle

zygote

blastocyst

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

Species

Human

Mouse

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 Mb

Chr 6: 146.63 – 146.68 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Serine/threonine-protein kinase 38-like is anenzyme that in humans is encoded by theSTK38Lgene.^[5]^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000211455 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000001630 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.
^"Entrez Gene: STK38L serine/threonine kinase 38 like".

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.Bibcode:2004CBio...14.1436J.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.

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-
Tropomyosin kinase (EC 2.7.11.28)	-
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-
Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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