Q7TSE6 (ST38L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase 38-like
EC=2.7.11.1

Alternative name(s):
NDR2 protein kinase
Nuclear Dbf2-related kinase 2

Gene names

Name:	Stk38l
Synonyms:	Ndr2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the regulation of structural processes in differentiating and mature neuronal cells. Ref.2 Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity. UniProtKB Q9Y2H1
Enzyme regulation	Activated by binding of S100B which releases autoinhibitory N-lobe interactions, enabling ATP to bind and the autophosphorylation of Ser-282. Thr-442 then undergoes calcium-dependent phosphorylation by STK24/MST3. Interactions between phosphorylated Thr-442 and the N-lobe promote additional structural changes that complete the activation of the kinase. Autoinhibition is also released by the binding of MOB1/MOBKL1A and MOB2 to the N-terminal of STK38L By similarity. UniProtKB Q9Y2H1
Subunit structure	Homodimeric S100B binds two molecules of STK38L. Interacts with MOB1 and MOB2 By similarity. Interacts with MICAL1; leading to inhibit the protein kinase activity by antagonizing activation by MST1/STK4. Ref.8
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Membrane. Note: Associated with the actin cytoskeleton. Co-localizes with STK24/MST3 in the membrane. Ref.2
Tissue specificity	Highly expressed in the large and small intestine, stomach and testis. High levels also present in the brain, in particular the neurocortex, basal forebrain, hippocampus, the amygdala, cerebellum and brainstem. Ref.1 Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Actin-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular protein kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB regulation of cellular component organization Inferred from direct assay Ref.2. Source: UniProtKB
Cellular_component	actin cytoskeleton Inferred from direct assay Ref.2. Source: UniProtKB cytoplasm Inferred from direct assay Ref.2. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q7TSE6-1)

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.

Isoform 2 (identifier: Q7TSE6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     423-423: V → VAFFLFLV

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 464	463	Serine/threonine-protein kinase 38-like		PRO_0000086721
Regions
	Domain	90 – 383	294	Protein kinase
	Domain	384 – 453	70	AGC-kinase C-terminal
	Nucleotide binding	96 – 104	9	ATP By similarity UniProtKB O95835
	Region	64 – 89	26	S100B binding By similarity UniProtKB Q15208
Sites
	Active site	213	1	Proton acceptor By similarity UniProtKB O95835
	Binding site	119	1	ATP By similarity UniProtKB Q9Y2H1
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	75	1	Phosphothreonine By similarity UniProtKB Q9Y2H1
	Modified residue	282	1	Phosphoserine; by autocatalysis By similarity UniProtKB Q9Y2H1
	Modified residue	442	1	Phosphothreonine; by STK24/MST3 By similarity UniProtKB Q9Y2H1
	Modified residue	450	1	Phosphothreonine Ref.7
Natural variations
	Alternative sequence	423	1	V → VAFFLFLV in isoform 2.		VSP_012334
Experimental info
	Sequence conflict	97	1	G → A in AAP44998. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: BE7E0CECDB63A8FD	FASTA	464	53,772
	10 20 30 40 50 60 MAMTAGATTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE VAMEEEGLAD 70 80 90 100 110 120 EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA FGEVRLVQKK DTGHIYAMKI 130 140 150 160 170 180 LRKADMLEKE QVAHIRAERD ILVEADGAWV VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM 190 200 210 220 230 240 KKDTLTEEET QFYISETVLA IDAIHQLGFI HRDVKPDNLL LDAKGHVKLS DFGLCTGLKK 250 260 270 280 290 300 AHRTEFYRNL THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY 310 320 330 340 350 360 NKLCDWWSLG VIMYEMLIGF PPFCSETPQE TYRKVMSWKE TLAFPPEVPV SEKAKDLILR 370 380 390 400 410 420 FCTDSENRIG NGGVEEIKGH PFFEGVDWGH IRERPAAIPI EIRSIDDTSN FDDFPESDIL 430 440 450 460 QPVPNTTEPD YKSKDWVFLN YTYKRFEGLT QRGSIPTYMK AGKL
	Isoform 2 [UniParc]. Checksum: AE9B2D42B1351E75	FASTA	471	54,610
	10 20 30 40 50 60 MAMTAGATTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE VAMEEEGLAD 70 80 90 100 110 120 EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA FGEVRLVQKK DTGHIYAMKI 130 140 150 160 170 180 LRKADMLEKE QVAHIRAERD ILVEADGAWV VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM 190 200 210 220 230 240 KKDTLTEEET QFYISETVLA IDAIHQLGFI HRDVKPDNLL LDAKGHVKLS DFGLCTGLKK 250 260 270 280 290 300 AHRTEFYRNL THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY 310 320 330 340 350 360 NKLCDWWSLG VIMYEMLIGF PPFCSETPQE TYRKVMSWKE TLAFPPEVPV SEKAKDLILR 370 380 390 400 410 420 FCTDSENRIG NGGVEEIKGH PFFEGVDWGH IRERPAAIPI EIRSIDDTSN FDDFPESDIL 430 440 450 460 470 QPVAFFLFLV PNTTEPDYKS KDWVFLNYTY KRFEGLTQRG SIPTYMKAGK L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of NDR2 protein kinase by multi-site phosphorylation and the S100B calcium-binding protein." Stegert M.R., Tamaskovic R., Bichsel S.J., Hergovich A., Hemmings B.A. J. Biol. Chem. 279:23806-23812(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Brain.
[2]	"Neuronal functions of the novel serine/threonine kinase Ndr2." Stork O., Zhdanov A., Kudersky A., Yoshikawa T., Obata K., Pape H.-C. J. Biol. Chem. 279:45773-45781(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Basophil.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Fetal heart.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 2). Tissue: Fetal jaw and Fetal limb.
[7]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"MICAL-1 is a negative regulator of MST-NDR kinase signaling and apoptosis." Zhou Y., Adolfs Y., Pijnappel W.W., Fuller S.J., Van der Schors R.C., Li K.W., Sugden P.H., Smit A.B., Hergovich A., Pasterkamp R.J. Mol. Cell. Biol. 31:3603-3615(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MICAL1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY292400 mRNA. Translation: AAP44998.1. AY223819 mRNA. Translation: AAO66474.1. AK052288 mRNA. Translation: BAC34918.1. CU207394 Genomic DNA. Translation: CAQ51943.1. CH466572 Genomic DNA. Translation: EDL10715.1. BC062170 mRNA. Translation: AAH62170.1.
IPI	IPI00453705. IPI00515183.
RefSeq	NP_766322.1. NM_172734.3.
UniGene	Mm.322121.
3D structure databases
ProteinModelPortal	Q7TSE6.
SMR	Q7TSE6. Positions 71-443.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q7TSE6. 1 interaction.
PTM databases
PhosphoSite	Q7TSE6.
Proteomic databases
PaxDb	Q7TSE6.
PRIDE	Q7TSE6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000001675; ENSMUSP00000001675; ENSMUSG00000001630. ENSMUST00000111644; ENSMUSP00000107271; ENSMUSG00000001630.
GeneID	232533.
KEGG	mmu:232533.
Organism-specific databases
CTD	23012.
MGI	MGI:1922250. Stk38l.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104041.
HOGENOM	HOG000233033.
HOVERGEN	HBG104247.
KO	K08790.
OMA	DHPFFEG.
OrthoDB	EOG4XGZZX.
Gene expression databases
ArrayExpress	Q7TSE6.
Bgee	Q7TSE6.
CleanEx	MM_STK38L.
Genevestigator	Q7TSE6.
GermOnline	ENSMUSG00000001630. Mus musculus.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	STK38L. mouse.
NextBio	381139.
SOURCE	Search...

Entry information

Entry name

ST38L_MOUSE

Accession

Primary (citable) accession number: Q7TSE6
Secondary accession number(s): B2KFR4, Q6P6K6, Q8BWK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program