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Protein

Serine/threonine-protein kinase 38

Gene

STK38

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Activated by binding of S100B which releases autoinhibitory N-lobe interactions, enabling ATP to bind and the autophosphorylation of Ser-281. Thr-444 then undergoes calcium-dependent phosphorylation by STK24/MST3. Interactions between phosphorylated Thr-444 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 STK38.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei118 – 1181ATPPROSITE-ProRule annotation2 Publications
Active sitei212 – 2121Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi95 – 1039ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. intracellular signal transduction Source: UniProtKB
  3. negative regulation of MAP kinase activity Source: UniProtKB
  4. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
SignaLinkiQ15208.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 38 (EC:2.7.11.1)
Alternative name(s):
NDR1 protein kinase
Nuclear Dbf2-related kinase 1
Gene namesi
Name:STK38Imported
Synonyms:NDR11 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:17847. STK38.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. MLL5-L complex Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741T → A: Decreases autophosphorylation and kinase activity. Reduced binding of S100B. 1 Publication
Mutagenesisi118 – 1181K → A: Loss of autophosphorylation and kinase activity. 2 Publications
Mutagenesisi281 – 2811S → A: Loss of autophosphorylation and kinase activity. 1 Publication
Mutagenesisi444 – 4441T → A: Decreases autophosphorylation and kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA38251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 465464Serine/threonine-protein kinase 38PRO_0000086718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei74 – 741Phosphothreonine1 Publication
Modified residuei264 – 2641Phosphoserine1 Publication
Modified residuei281 – 2811Phosphoserine; by autocatalysis1 Publication
Modified residuei444 – 4441Phosphothreonine; by STK24/MST31 Publication

Post-translational modificationi

ISGylated.1 Publication
Phosphorylated by STK3/MST2 and this is enhanced by MOBKL1B.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15208.
PaxDbiQ15208.
PRIDEiQ15208.

PTM databases

PhosphoSiteiQ15208.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels observed in peripheral blood leukocytes.2 Publications

Gene expression databases

BgeeiQ15208.
CleanExiHS_STK38.
ExpressionAtlasiQ15208. baseline and differential.
GenevestigatoriQ15208.

Organism-specific databases

HPAiCAB004673.
HPA038623.

Interactioni

Subunit structurei

Interacts with MICAL1; leading to inhibit the protein kinase activity by antagonizing activation by MST1/STK4 (By similarity). Homodimeric S100B binds two molecules of STK38. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with MOB1 and MOB2. Interacts with MAP3K1 and MAP3K2 (via the kinase catalytic domain). Forms a tripartite complex with MOBKL1B and STK3/MST2.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB1P494073EBI-458376,EBI-743313
ARRB2P321213EBI-458376,EBI-714559
HSP90AB1P082382EBI-458376,EBI-352572
MOB1AQ9H8S92EBI-458376,EBI-748229
S100BP026383EBI-458376,EBI-458452From a different organism.

Protein-protein interaction databases

BioGridi116457. 38 interactions.
IntActiQ15208. 12 interactions.
MINTiMINT-1217042.
STRINGi9606.ENSP00000229812.

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi74 – 8512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PSBNMR-C/D62-87[»]
ProteinModelPortaliQ15208.
SMRiQ15208. Positions 19-449.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15208.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 382294Protein kinasePROSITE-ProRule annotationImportedAdd
BLAST
Domaini383 – 45573AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 8726Interaction with S100BAdd
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.
InParanoidiQ15208.
KOiK08790.
OMAiLTFQNMN.
OrthoDBiEOG7BZVS1.
PhylomeDBiQ15208.
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]

Sequencei

Sequence statusi: Complete.

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

Q15208-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMTGSTPCS SMSNHTKERV TMTKVTLENF YSNLIAQHEE REMRQKKLEK
60 70 80 90 100
VMEEEGLKDE EKRLRRSAHA RKETEFLRLK RTRLGLEDFE SLKVIGRGAF
110 120 130 140 150
GEVRLVQKKD TGHVYAMKIL RKADMLEKEQ VGHIRAERDI LVEADSLWVV
160 170 180 190 200
KMFYSFQDKL NLYLIMEFLP GGDMMTLLMK KDTLTEEETQ FYIAETVLAI
210 220 230 240 250
DSIHQLGFIH RDIKPDNLLL DSKGHVKLSD FGLCTGLKKA HRTEFYRNLN
260 270 280 290 300
HSLPSDFTFQ NMNSKRKAET WKRNRRQLAF STVGTPDYIA PEVFMQTGYN
310 320 330 340 350
KLCDWWSLGV IMYEMLIGYP PFCSETPQET YKKVMNWKET LTFPPEVPIS
360 370 380 390 400
EKAKDLILRF CCEWEHRIGA PGVEEIKSNS FFEGVDWEHI RERPAAISIE
410 420 430 440 450
IKSIDDTSNF DEFPESDILK PTVATSNHPE TDYKNKDWVF INYTYKRFEG
460
LTARGAIPSY MKAAK
Length:465
Mass (Da):54,190
Last modified:November 1, 1996 - v1
Checksum:i7262221DBFFAF83C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181E → K in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041196
Natural varianti145 – 1451D → N.1 Publication
Corresponds to variant rs56005153 [ dbSNP | Ensembl ].
VAR_041197
Natural varianti267 – 2671K → R.1 Publication
Corresponds to variant rs56105564 [ dbSNP | Ensembl ].
VAR_041198

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35102 mRNA. Translation: CAA84485.1.
Z85986 Genomic DNA. Translation: CAB39180.1.
BC012085 mRNA. Translation: AAH12085.1.
BC095413 mRNA. Translation: AAH95413.1.
CCDSiCCDS4822.1.
PIRiI38133.
RefSeqiNP_009202.1. NM_007271.2.
XP_005248896.1. XM_005248839.1.
XP_006715051.1. XM_006714988.1.
XP_006715052.1. XM_006714989.1.
UniGeneiHs.409578.

Genome annotation databases

EnsembliENST00000229812; ENSP00000229812; ENSG00000112079.
GeneIDi11329.
KEGGihsa:11329.
UCSCiuc003omg.3. human.

Polymorphism databases

DMDMi56749457.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35102 mRNA. Translation: CAA84485.1.
Z85986 Genomic DNA. Translation: CAB39180.1.
BC012085 mRNA. Translation: AAH12085.1.
BC095413 mRNA. Translation: AAH95413.1.
CCDSiCCDS4822.1.
PIRiI38133.
RefSeqiNP_009202.1. NM_007271.2.
XP_005248896.1. XM_005248839.1.
XP_006715051.1. XM_006714988.1.
XP_006715052.1. XM_006714989.1.
UniGeneiHs.409578.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PSBNMR-C/D62-87[»]
ProteinModelPortaliQ15208.
SMRiQ15208. Positions 19-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116457. 38 interactions.
IntActiQ15208. 12 interactions.
MINTiMINT-1217042.
STRINGi9606.ENSP00000229812.

Chemistry

BindingDBiQ15208.
ChEMBLiCHEMBL1075155.
GuidetoPHARMACOLOGYi1517.

PTM databases

PhosphoSiteiQ15208.

Polymorphism databases

DMDMi56749457.

Proteomic databases

MaxQBiQ15208.
PaxDbiQ15208.
PRIDEiQ15208.

Protocols and materials databases

DNASUi11329.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229812; ENSP00000229812; ENSG00000112079.
GeneIDi11329.
KEGGihsa:11329.
UCSCiuc003omg.3. human.

Organism-specific databases

CTDi11329.
GeneCardsiGC06M036461.
HGNCiHGNC:17847. STK38.
HPAiCAB004673.
HPA038623.
MIMi606964. gene.
neXtProtiNX_Q15208.
PharmGKBiPA38251.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000233033.
HOVERGENiHBG104247.
InParanoidiQ15208.
KOiK08790.
OMAiLTFQNMN.
OrthoDBiEOG7BZVS1.
PhylomeDBiQ15208.
TreeFamiTF105337.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
SignaLinkiQ15208.

Miscellaneous databases

ChiTaRSiSTK38. human.
EvolutionaryTraceiQ15208.
GeneWikiiSTK38.
GenomeRNAii11329.
NextBioi43035.
PROiQ15208.
SOURCEiSearch...

Gene expression databases

BgeeiQ15208.
CleanExiHS_STK38.
ExpressionAtlasiQ15208. baseline and differential.
GenevestigatoriQ15208.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a conserved nuclear serine/threonine protein kinase."
    Millward T.A., Cron P., Hemmings B.A.
    Proc. Natl. Acad. Sci. U.S.A. 92:5022-5026(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-118.
    Tissue: Fetal brainImported.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta and UterusImported.
  4. Bienvenut W.V., Calvo F., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 25-44; 51-63; 72-78; 82-97; 110-118; 122-159; 182-239; 248-266; 277-301; 334-391; 394-402 AND 437-454, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  5. "Mechanism of Ca2+-mediated regulation of NDR protein kinase through autophosphorylation and phosphorylation by an upstream kinase."
    Tamaskovic R., Bichsel S.J., Rogniaux H., Stegert M.R., Hemmings B.A.
    J. Biol. Chem. 278:6710-6718(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-74; SER-281 AND THR-444, MUTAGENESIS OF THR-74; LYS-118; SER-281 AND THR-444.
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH MOB1 AND MOB2.
  7. "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein."
    Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.
    J. Biol. Chem. 279:35228-35235(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION, INTERACTION WITH MOB1 AND MOB2.
  8. "Identification and Herc5-mediated ISGylation of novel target proteins."
    Takeuchi T., Inoue S., Yokosawa H.
    Biochem. Biophys. Res. Commun. 348:473-477(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION.
  9. "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."
    Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., Kawata A., Ohno K., Hata Y.
    Oncogene 27:4281-4292(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STK3/MST2 AND MOBKL1B, SUBCELLULAR LOCATION, PHOSPHORYLATION BY STK3/MST2.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
    Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
    Nature 459:455-459(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
  12. "Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38)."
    Enomoto A., Kido N., Ito M., Morita A., Matsumoto Y., Takamatsu N., Hosoi Y., Miyagawa K.
    Oncogene 27:1930-1938(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K1 AND MAP3K2.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase."
    Bhattacharya S., Large E., Heizmann C.W., Hemmings B.A., Chazin W.J.
    Biochemistry 42:14416-14426(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 62-84, ENZYME REGULATION, INTERACTION WITH S100B.
  17. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-18; ASN-145 AND ARG-267.

Entry informationi

Entry nameiSTK38_HUMAN
AccessioniPrimary (citable) accession number: Q15208
Secondary accession number(s): Q503A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 143 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.