Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7TSE6

- ST38L_MOUSE

UniProt

Q7TSE6 - ST38L_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein kinase 38-like

Gene

Stk38l

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the regulation of structural processes in differentiating and mature neuronal cells.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191ATPBy similarityPROSITE-ProRule annotation
Active sitei213 – 2131Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 1049ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. intracellular signal transduction Source: UniProtKB
  2. protein phosphorylation Source: UniProtKB
  3. regulation of cellular component organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

Actin-binding, ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:Stk38lImported
Synonyms:Ndr21 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1922250. Stk38l.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication. Membrane 1 Publication
Note: Associated with the actin cytoskeleton. Co-localizes with STK24/MST3 in the membrane.

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 464463Serine/threonine-protein kinase 38-likePRO_0000086721Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei75 – 751PhosphothreonineBy similarity
Modified residuei282 – 2821Phosphoserine; by autocatalysisBy similarity
Modified residuei442 – 4421Phosphothreonine; by STK24/MST3By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7TSE6.
PaxDbiQ7TSE6.
PRIDEiQ7TSE6.

PTM databases

PhosphoSiteiQ7TSE6.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ7TSE6.
CleanExiMM_STK38L.
GenevestigatoriQ7TSE6.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi231267. 1 interaction.
IntActiQ7TSE6. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ7TSE6.
SMRiQ7TSE6. Positions 79-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 383294Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini384 – 45370AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 8926S100B bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000233033.
HOVERGENiHBG104247.
InParanoidiQ7TSE6.
KOiK08790.
OMAiYMKAGKA.
OrthoDBiEOG7BZVS1.
TreeFamiTF105337.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS51285. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7TSE6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAMTAGATTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE
60 70 80 90 100
VAMEEEGLAD EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA
110 120 130 140 150
FGEVRLVQKK DTGHIYAMKI LRKADMLEKE QVAHIRAERD ILVEADGAWV
160 170 180 190 200
VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM KKDTLTEEET QFYISETVLA
210 220 230 240 250
IDAIHQLGFI HRDVKPDNLL LDAKGHVKLS DFGLCTGLKK AHRTEFYRNL
260 270 280 290 300
THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY
310 320 330 340 350
NKLCDWWSLG VIMYEMLIGF PPFCSETPQE TYRKVMSWKE TLAFPPEVPV
360 370 380 390 400
SEKAKDLILR FCTDSENRIG NGGVEEIKGH PFFEGVDWGH IRERPAAIPI
410 420 430 440 450
EIRSIDDTSN FDDFPESDIL QPVPNTTEPD YKSKDWVFLN YTYKRFEGLT
460
QRGSIPTYMK AGKL
Length:464
Mass (Da):53,772
Last modified:July 27, 2011 - v2
Checksum:iBE7E0CECDB63A8FD
GO
Isoform 2 (identifier: Q7TSE6-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:471
Mass (Da):54,610
Checksum:iAE9B2D42B1351E75
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971G → A in AAP44998. (PubMed:15037617)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei423 – 4231V → VAFFLFLV in isoform 2. 1 PublicationVSP_012334

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS39712.1. [Q7TSE6-1]
RefSeqiNP_766322.1. NM_172734.3. [Q7TSE6-1]
XP_006536130.1. XM_006536067.1. [Q7TSE6-2]
UniGeneiMm.322121.

Genome annotation databases

EnsembliENSMUST00000001675; ENSMUSP00000001675; ENSMUSG00000001630. [Q7TSE6-1]
ENSMUST00000111644; ENSMUSP00000107271; ENSMUSG00000001630. [Q7TSE6-2]
GeneIDi232533.
KEGGimmu:232533.
UCSCiuc009esh.2. mouse. [Q7TSE6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS39712.1. [Q7TSE6-1 ]
RefSeqi NP_766322.1. NM_172734.3. [Q7TSE6-1 ]
XP_006536130.1. XM_006536067.1. [Q7TSE6-2 ]
UniGenei Mm.322121.

3D structure databases

ProteinModelPortali Q7TSE6.
SMRi Q7TSE6. Positions 79-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 231267. 1 interaction.
IntActi Q7TSE6. 1 interaction.

PTM databases

PhosphoSitei Q7TSE6.

Proteomic databases

MaxQBi Q7TSE6.
PaxDbi Q7TSE6.
PRIDEi Q7TSE6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001675 ; ENSMUSP00000001675 ; ENSMUSG00000001630 . [Q7TSE6-1 ]
ENSMUST00000111644 ; ENSMUSP00000107271 ; ENSMUSG00000001630 . [Q7TSE6-2 ]
GeneIDi 232533.
KEGGi mmu:232533.
UCSCi uc009esh.2. mouse. [Q7TSE6-1 ]

Organism-specific databases

CTDi 23012.
MGIi MGI:1922250. Stk38l.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118994.
HOGENOMi HOG000233033.
HOVERGENi HBG104247.
InParanoidi Q7TSE6.
KOi K08790.
OMAi YMKAGKA.
OrthoDBi EOG7BZVS1.
TreeFami TF105337.

Miscellaneous databases

ChiTaRSi STK38L. mouse.
NextBioi 381139.
PROi Q7TSE6.
SOURCEi Search...

Gene expression databases

Bgeei Q7TSE6.
CleanExi MM_STK38L.
Genevestigatori Q7TSE6.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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/6Imported.
    Tissue: BrainImported.
  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/6Imported.
    Tissue: BasophilImported.
  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. 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 jawImported and Fetal limbImported.
  7. Cited for: FUNCTION, INTERACTION WITH MICAL1.

Entry informationi

Entry nameiST38L_MOUSE
AccessioniPrimary (citable) accession number: Q7TSE6
Secondary accession number(s): B2KFR4, Q6P6K6, Q8BWK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3