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Q9Y2H1 (ST38L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:KIAA0965, NDR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of structural processes in differentiating and mature neuronal cells By similarity. Ref.1 Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium. Ref.1 Ref.8

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/HCCA2 to the N-terminal of STK38L. Ref.1 Ref.8 Ref.9 UniProtKB Q15208

Subunit structure

Homodimeric S100B binds two molecules of STK38L. Interacts with MICAL1; leading to inhibit the protein kinase activity by antagonizing activation by MST1/STK4 By similarity. Interacts with MOB1 and MOB2. Ref.1 Ref.8

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Membrane. Note: Associated with the actin cytoskeleton. Co-localizes with STK24/MST3 in the membrane. Ref.1 Ref.8 Ref.9

Tissue specificity

Ubiquitously expressed with highest levels observed in the thymus. Ref.8

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MOB1AQ9H8S93EBI-991501,EBI-748229

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 464463Serine/threonine-protein kinase 38-like
PRO_0000086720

Regions

Domain90 – 383294Protein kinase
Domain384 – 45370AGC-kinase C-terminal
Nucleotide binding96 – 1049ATP By similarity UniProtKB O95835
Region63 – 8826S100B binding By similarity UniProtKB Q15208

Sites

Active site2131Proton acceptor By similarity UniProtKB O95835
Binding site1191ATP Ref.1

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue751Phosphothreonine Ref.1
Modified residue2821Phosphoserine; by autocatalysis Ref.1
Modified residue4421Phosphothreonine; by STK24/MST3 Ref.1 Ref.9

Natural variations

Natural variant991G → A in a aLL TEL/AML1+ sample; somatic mutation. Ref.12
VAR_041199

Experimental info

Mutagenesis751T → A: Decreased kinase activity. Reduced binding of S100B. Ref.1
Mutagenesis1191K → A: Loss of autophosphorylation and kinase activity. Ref.1
Mutagenesis2821S → A: Loss of autophosphorylation and kinase activity. Ref.1
Mutagenesis4421T → A: Decreased kinase activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y2H1 [UniParc].

Last modified December 21, 2004. Version 3.
Checksum: 71347E80BC3ADCB3

FASTA46454,003
        10         20         30         40         50         60 
MAMTAGTTTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE VAMEEEGLAD 

        70         80         90        100        110        120 
EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA FGEVRLVQKK DTGHIYAMKI 

       130        140        150        160        170        180 
LRKSDMLEKE QVAHIRAERD ILVEADGAWV VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM 

       190        200        210        220        230        240 
KKDTLTEEET QFYISETVLA IDAIHQLGFI HRDIKPDNLL LDAKGHVKLS DFGLCTGLKK 

       250        260        270        280        290        300 
AHRTEFYRNL THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY 

       310        320        330        340        350        360 
NKLCDWWSLG VIMYEMLIGY PPFCSETPQE TYRKVMNWKE TLVFPPEVPI SEKAKDLILR 

       370        380        390        400        410        420 
FCIDSENRIG NSGVEEIKGH PFFEGVDWEH IRERPAAIPI EIKSIDDTSN FDDFPESDIL 

       430        440        450        460 
QPVPNTTEPD YKSKDWVFLN YTYKRFEGLT QRGSIPTYMK AGKL 

« Hide

References

« Hide '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], FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, INTERACTION WITH S100, PHOSPHORYLATION AT THR-75; SER-282 AND THR-442, MUTAGENESIS OF THR-75; LYS-119; SER-282 AND THR-442.
Tissue: Brain.
[2]"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."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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].
Tissue: Testis.
[7]Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-18; 26-42; 48-64; 73-79; 83-98; 123-161; 213-224; 229-240; 249-266; 340-392 AND 433-460, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma and Lung carcinoma.
[8]"Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases."
Devroe E., Erdjument-Bromage H., Tempst P., Silver P.A.
J. Biol. Chem. 279:24444-24451(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION, INTERACTION WITH MOB1 AND MOB2.
[9]"Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3."
Stegert M.R., Hergovich A., Tamaskovic R., Bichsel S.J., Hemmings B.A.
Mol. Cell. Biol. 25:11019-11029(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-442, ENZYME REGULATION, SUBCELLULAR LOCATION.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-99.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023182 mRNA. Translation: BAA76809.2.
AK291055 mRNA. Translation: BAF83744.1.
CH471094 Genomic DNA. Translation: EAW96549.1.
BC028603 mRNA. Translation: AAH28603.1.
RefSeqNP_055815.1. NM_015000.3.
UniGeneHs.184523.

3D structure databases

ProteinModelPortalQ9Y2H1.
SMRQ9Y2H1. Positions 79-454.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116654. 13 interactions.
IntActQ9Y2H1. 7 interactions.
MINTMINT-1631355.
STRING9606.ENSP00000373684.

Chemistry

BindingDBQ9Y2H1.
ChEMBLCHEMBL4851.
GuidetoPHARMACOLOGY1518.

PTM databases

PhosphoSiteQ9Y2H1.

Polymorphism databases

DMDM56749668.

Proteomic databases

PaxDbQ9Y2H1.
PeptideAtlasQ9Y2H1.
PRIDEQ9Y2H1.

Protocols and materials databases

DNASU23012.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389032; ENSP00000373684; ENSG00000211455.
GeneID23012.
KEGGhsa:23012.
UCSCuc001rhr.3. human.

Organism-specific databases

CTD23012.
GeneCardsGC12P027396.
HGNCHGNC:17848. STK38L.
HPAHPA038623.
neXtProtNX_Q9Y2H1.
PharmGKBPA38252.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233033.
HOVERGENHBG104247.
InParanoidQ9Y2H1.
KOK08790.
OMAYMKAGKA.
PhylomeDBQ9Y2H1.
TreeFamTF105337.

Enzyme and pathway databases

SignaLinkQ9Y2H1.

Gene expression databases

ArrayExpressQ9Y2H1.
BgeeQ9Y2H1.
CleanExHS_STK38L.
GenevestigatorQ9Y2H1.

Family and domain databases

InterProIPR000961. 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_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSSTK38L. human.
GeneWikiSTK38L.
GenomeRNAi23012.
NextBio43932.
PROQ9Y2H1.

Entry information

Entry nameST38L_HUMAN
AccessionPrimary (citable) accession number: Q9Y2H1
Secondary accession number(s): A8K4U0, Q8TBX7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM