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Q9Y2H1

- ST38L_HUMAN

UniProt

Q9Y2H1 - ST38L_HUMAN

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Protein
Serine/threonine-protein kinase 38-like
Gene
STK38L, KIAA0965, NDR2
Organism
Homo sapiens (Human)
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 By similarity.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.2 Publications

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/HCCA2 to the N-terminal of STK38L.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191ATP1 Publication
Active sitei213 – 2131Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 1049ATP By similarityBy similarity

GO - Molecular functioni

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

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

Enzyme and pathway databases

SignaLinkiQ9Y2H1.

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:STK38L
Synonyms:KIAA0965, NDR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:17848. STK38L.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeleton. Membrane
Note: Associated with the actin cytoskeleton. Co-localizes with STK24/MST3 in the membrane.3 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi75 – 751T → A: Decreased kinase activity. Reduced binding of S100B. 1 Publication
Mutagenesisi119 – 1191K → A: Loss of autophosphorylation and kinase activity. 1 Publication
Mutagenesisi282 – 2821S → A: Loss of autophosphorylation and kinase activity. 1 Publication
Mutagenesisi442 – 4421T → A: Decreased kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA38252.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 464463Serine/threonine-protein kinase 38-like
PRO_0000086720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei75 – 751Phosphothreonine1 Publication
Modified residuei282 – 2821Phosphoserine; by autocatalysis1 Publication
Modified residuei442 – 4421Phosphothreonine; by STK24/MST32 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y2H1.
PaxDbiQ9Y2H1.
PeptideAtlasiQ9Y2H1.
PRIDEiQ9Y2H1.

PTM databases

PhosphoSiteiQ9Y2H1.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels observed in the thymus.1 Publication

Gene expression databases

ArrayExpressiQ9Y2H1.
BgeeiQ9Y2H1.
CleanExiHS_STK38L.
GenevestigatoriQ9Y2H1.

Organism-specific databases

HPAiHPA038623.

Interactioni

Subunit structurei

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 MOB2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MOB1AQ9H8S93EBI-991501,EBI-748229

Protein-protein interaction databases

BioGridi116654. 13 interactions.
IntActiQ9Y2H1. 7 interactions.
MINTiMINT-1631355.
STRINGi9606.ENSP00000373684.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2H1.
SMRiQ9Y2H1. Positions 71-443.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 383294Protein kinase
Add
BLAST
Domaini384 – 45370AGC-kinase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 8826S100B binding By similarityBy similarity
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233033.
HOVERGENiHBG104247.
InParanoidiQ9Y2H1.
KOiK08790.
OMAiYMKAGKA.
PhylomeDBiQ9Y2H1.
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_dom.
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]

Sequencei

Sequence statusi: Complete.

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

Q9Y2H1-1 [UniParc]FASTAAdd to Basket

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MAMTAGTTTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE    50
VAMEEEGLAD EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA 100
FGEVRLVQKK DTGHIYAMKI LRKSDMLEKE QVAHIRAERD ILVEADGAWV 150
VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM KKDTLTEEET QFYISETVLA 200
IDAIHQLGFI HRDIKPDNLL LDAKGHVKLS DFGLCTGLKK AHRTEFYRNL 250
THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY 300
NKLCDWWSLG VIMYEMLIGY PPFCSETPQE TYRKVMNWKE TLVFPPEVPI 350
SEKAKDLILR FCIDSENRIG NSGVEEIKGH PFFEGVDWEH IRERPAAIPI 400
EIKSIDDTSN FDDFPESDIL QPVPNTTEPD YKSKDWVFLN YTYKRFEGLT 450
QRGSIPTYMK AGKL 464
Length:464
Mass (Da):54,003
Last modified:December 21, 2004 - v3
Checksum:i71347E80BC3ADCB3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991G → A in a aLL TEL/AML1+ sample; somatic mutation. 1 Publication
VAR_041199

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023182 mRNA. Translation: BAA76809.2.
AK291055 mRNA. Translation: BAF83744.1.
CH471094 Genomic DNA. Translation: EAW96549.1.
BC028603 mRNA. Translation: AAH28603.1.
CCDSiCCDS31761.1.
RefSeqiNP_055815.1. NM_015000.3.
XP_006719121.1. XM_006719058.1.
UniGeneiHs.184523.

Genome annotation databases

EnsembliENST00000389032; ENSP00000373684; ENSG00000211455.
GeneIDi23012.
KEGGihsa:23012.
UCSCiuc001rhr.3. human.

Polymorphism databases

DMDMi56749668.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023182 mRNA. Translation: BAA76809.2 .
AK291055 mRNA. Translation: BAF83744.1 .
CH471094 Genomic DNA. Translation: EAW96549.1 .
BC028603 mRNA. Translation: AAH28603.1 .
CCDSi CCDS31761.1.
RefSeqi NP_055815.1. NM_015000.3.
XP_006719121.1. XM_006719058.1.
UniGenei Hs.184523.

3D structure databases

ProteinModelPortali Q9Y2H1.
SMRi Q9Y2H1. Positions 71-443.
ModBasei Search...

Protein-protein interaction databases

BioGridi 116654. 13 interactions.
IntActi Q9Y2H1. 7 interactions.
MINTi MINT-1631355.
STRINGi 9606.ENSP00000373684.

Chemistry

BindingDBi Q9Y2H1.
ChEMBLi CHEMBL4851.
GuidetoPHARMACOLOGYi 1518.

PTM databases

PhosphoSitei Q9Y2H1.

Polymorphism databases

DMDMi 56749668.

Proteomic databases

MaxQBi Q9Y2H1.
PaxDbi Q9Y2H1.
PeptideAtlasi Q9Y2H1.
PRIDEi Q9Y2H1.

Protocols and materials databases

DNASUi 23012.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389032 ; ENSP00000373684 ; ENSG00000211455 .
GeneIDi 23012.
KEGGi hsa:23012.
UCSCi uc001rhr.3. human.

Organism-specific databases

CTDi 23012.
GeneCardsi GC12P027396.
HGNCi HGNC:17848. STK38L.
HPAi HPA038623.
neXtProti NX_Q9Y2H1.
PharmGKBi PA38252.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233033.
HOVERGENi HBG104247.
InParanoidi Q9Y2H1.
KOi K08790.
OMAi YMKAGKA.
PhylomeDBi Q9Y2H1.
TreeFami TF105337.

Enzyme and pathway databases

SignaLinki Q9Y2H1.

Miscellaneous databases

ChiTaRSi STK38L. human.
GeneWikii STK38L.
GenomeRNAii 23012.
NextBioi 43932.
PROi Q9Y2H1.

Gene expression databases

ArrayExpressi Q9Y2H1.
Bgeei Q9Y2H1.
CleanExi HS_STK38L.
Genevestigatori Q9Y2H1.

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_dom.
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], 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.
    , 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. 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. 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.
    , 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.

Entry informationi

Entry nameiST38L_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2H1
Secondary accession number(s): A8K4U0, Q8TBX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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