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Protein

Serine/threonine-protein kinase 4

Gene

STK4

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

Functioni

Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes.By similarity16 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Inhibited by the C-terminal non-catalytic region. Activated by caspase-cleavage. Full activation also requires homodimerization and autophosphorylation of Thr-183. Activated by RASSF1 which acts by preventing its dephosphorylation.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei59ATP1
Active sitei149Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 44ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein homodimerization activity Source: MGI
  • protein kinase activity Source: MGI
  • protein serine/threonine kinase activator activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: UniProtKB
  • receptor signaling protein serine/threonine kinase activity Source: GO_Central
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cell differentiation involved in embryonic placenta development Source: Ensembl
  • cell morphogenesis Source: MGI
  • central nervous system development Source: Ensembl
  • endocardium development Source: Ensembl
  • hepatocyte apoptotic process Source: Ensembl
  • hippo signaling Source: UniProtKB
  • intracellular signal transduction Source: UniProtKB
  • keratinocyte differentiation Source: Ensembl
  • negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of organ growth Source: Ensembl
  • neural tube formation Source: Ensembl
  • patterning of blood vessels Source: Ensembl
  • peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  • positive regulation of fat cell differentiation Source: Ensembl
  • positive regulation of peptidyl-serine phosphorylation Source: MGI
  • positive regulation of protein binding Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • primitive hemopoiesis Source: Ensembl
  • protein autophosphorylation Source: MGI
  • protein phosphorylation Source: UniProtKB
  • protein stabilization Source: MGI
  • regulation of cell differentiation involved in embryonic placenta development Source: Ensembl
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:HS02194-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-2028269. Signaling by Hippo.
SignaLinkiQ13043.
SIGNORiQ13043.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 4 (EC:2.7.11.1)
Alternative name(s):
Mammalian STE20-like protein kinase 1
Short name:
MST-1
STE20-like kinase MST1
Serine/threonine-protein kinase Krs-2
Cleaved into the following 2 chains:
Gene namesi
Name:STK4
Synonyms:KRS2, MST1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11408. STK4.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: The caspase-cleaved form cycles between the nucleus and cytoplasm.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

T-cell immunodeficiency, recurrent infections, and autoimmunity with or without cardiac malformations (TIIAC)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA primary T-cell immunodeficiency syndrome characterized by progressive loss of naive T-cells, recurrent bacterial, viral, and fungal infections, warts, and abscesses, autoimmune manifestations, and cardiac malformations, including atrial septal defect.
See also OMIM:614868

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59K → R: Loss of activity. 2 Publications1
Mutagenesisi175T → A: No effect on activity. 1 Publication1
Mutagenesisi177T → A: No effect on activity. 1 Publication1
Mutagenesisi183T → A: Loss of activity. 1 Publication1
Mutagenesisi326D → N: Resistant to proteolytic cleavage by caspase during apoptosis; when associated with N-349. 1 Publication1
Mutagenesisi349D → N: Resistant to proteolytic cleavage by caspase during apoptosis; when associated with N-326. 1 Publication1
Mutagenesisi444L → P: Loss of homodimerization, activation, and autophosphorylation. 1 Publication1

Organism-specific databases

DisGeNETi6789.
MalaCardsiSTK4.
MIMi614868. phenotype.
OpenTargetsiENSG00000101109.
Orphaneti314689. Combined immunodeficiency due to STK4 deficiency.
PharmGKBiPA36215.

Chemistry databases

ChEMBLiCHEMBL4598.
GuidetoPHARMACOLOGYi2225.

Polymorphism and mutation databases

BioMutaiSTK4.
DMDMi13124559.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866911 – 487Serine/threonine-protein kinase 4Add BLAST487
ChainiPRO_00004137351 – 326Serine/threonine-protein kinase 4 37kDa subunitAdd BLAST326
ChainiPRO_0000413736327 – 487Serine/threonine-protein kinase 4 18kDa subunitAdd BLAST161

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei3PhosphothreonineCombined sources1
Modified residuei120Phosphothreonine; by PKB/AKT11 Publication1
Modified residuei183Phosphothreonine; by autocatalysis1 Publication1
Modified residuei265PhosphoserineCombined sources1
Modified residuei320PhosphoserineCombined sources1
Modified residuei340PhosphothreonineCombined sources1
Modified residuei367PhosphothreonineCombined sources1
Modified residuei387Phosphothreonine; by PKB/AKT1Combined sources1 Publication1
Modified residuei410PhosphoserineCombined sources1
Modified residuei414PhosphoserineCombined sources1
Modified residuei433PhosphotyrosineBy similarity1

Post-translational modificationi

Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-120 and Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3.4 Publications
Proteolytically cleaved by caspase-3 during apoptosis at Asp-326 and Asp-349 resulting in a 37 kDa or a 39 kDa subunit respectively. The 39 kDa subunit is further cleaved into the 37 kDa form. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). It is less likely that cleavage at Asp-349 is a prerequisite for activation as this site is not conserved in the murine ortholog.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei326 – 327Cleavage; by caspase-32
Sitei349 – 350Cleavage; by caspase-32

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13043.
MaxQBiQ13043.
PaxDbiQ13043.
PeptideAtlasiQ13043.
PRIDEiQ13043.

PTM databases

iPTMnetiQ13043.
PhosphoSitePlusiQ13043.

Miscellaneous databases

PMAP-CutDBQ13043.

Expressioni

Tissue specificityi

Expressed in prostate cancer and levels increase from the normal to the malignant state (at protein level). Ubiquitously expressed.1 Publication

Inductioni

Activity increases during mitosis.

Gene expression databases

BgeeiENSG00000101109.
CleanExiHS_MST1.
HS_STK4.
ExpressionAtlasiQ13043. baseline and differential.
GenevisibleiQ13043. HS.

Organism-specific databases

HPAiCAB004038.
HPA015270.

Interactioni

Subunit structurei

Homodimer; mediated via the coiled-coil region. Interacts with NORE1, which inhibits autoactivation. Interacts with and stabilizes SAV1. Interacts with RASSF1. Interacts with FOXO3. Interacts with RASSF2 (via SARAH domain). Interacts with AR, PKB/AKT1, TNNI3 and SIRT1.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-367376,EBI-367376
AKT1P3174913EBI-367376,EBI-296087
GABARAPO951662EBI-367376,EBI-712001
GABARAPL1Q9H0R82EBI-367376,EBI-746969
GABARAPL2P605202EBI-367376,EBI-720116
MAP1LC3BQ9GZQ87EBI-367376,EBI-373144
MOB1AQ9H8S99EBI-367376,EBI-748229
MOB1BQ7L9L44EBI-367376,EBI-2558745
PRDX1Q0683011EBI-367376,EBI-353193
Prdx1P357003EBI-367376,EBI-444948From a different organism.
RASSF1Q9NS23-24EBI-367376,EBI-438698
RASSF2P5074915EBI-367376,EBI-960081
RASSF3Q86WH26EBI-367376,EBI-2845202
RASSF4Q9H2L56EBI-367376,EBI-2933362
RASSF5Q8WWW07EBI-367376,EBI-367390
RASSF5Q8WWW0-24EBI-367376,EBI-960502
RASSF5Q8WWW0-32EBI-367376,EBI-960507
RASSF6Q6ZTQ34EBI-367376,EBI-2933412
SAV1Q9H4B618EBI-367376,EBI-1017775
SLMAPQ14BN47EBI-367376,EBI-1043216
STK3Q1318817EBI-367376,EBI-992580
Stk38Q91VJ42EBI-367376,EBI-2527046From a different organism.

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB
  • protein homodimerization activity Source: MGI
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112665. 65 interactors.
DIPiDIP-32491N.
IntActiQ13043. 169 interactors.
MINTiMINT-4658525.
STRINGi9606.ENSP00000361892.

Chemistry databases

BindingDBiQ13043.

Structurei

Secondary structure

1487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 22Combined sources4
Beta strandi30 – 35Combined sources6
Beta strandi43 – 49Combined sources7
Turni50 – 52Combined sources3
Beta strandi55 – 62Combined sources8
Helixi68 – 78Combined sources11
Beta strandi88 – 94Combined sources7
Beta strandi97 – 103Combined sources7
Helixi110 – 117Combined sources8
Helixi123 – 142Combined sources20
Helixi152 – 154Combined sources3
Beta strandi155 – 157Combined sources3
Beta strandi163 – 165Combined sources3
Helixi188 – 190Combined sources3
Helixi193 – 196Combined sources4
Beta strandi197 – 199Combined sources3
Helixi205 – 219Combined sources15
Turni223 – 226Combined sources4
Helixi229 – 238Combined sources10
Helixi247 – 249Combined sources3
Helixi252 – 261Combined sources10
Turni266 – 268Combined sources3
Helixi272 – 275Combined sources4
Helixi279 – 282Combined sources4
Helixi287 – 290Combined sources4
Helixi291 – 297Combined sources7
Helixi433 – 436Combined sources4
Helixi441 – 478Combined sources38

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JO8NMR-A/B432-480[»]
3COMX-ray2.20A/B2-311[»]
4NR2X-ray2.00A/B/C/D/E/F/G/H432-480[»]
4OH8X-ray2.28A432-480[»]
ProteinModelPortaliQ13043.
SMRiQ13043.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 281Protein kinasePROSITE-ProRule annotationAdd BLAST252
Domaini433 – 480SARAHPROSITE-ProRule annotationAdd BLAST48

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili290 – 310Sequence analysisAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi373 – 378Poly-Glu6

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SARAH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0201. Eukaryota.
ENOG410XP9G. LUCA.
GeneTreeiENSGT00810000125395.
HOVERGENiHBG108518.
InParanoidiQ13043.
KOiK04411.
OMAiAMINEAM.
OrthoDBiEOG091G065P.
PhylomeDBiQ13043.
TreeFamiTF354217.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR024205. Mst1_SARAH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR011524. SARAH_dom.
[Graphical view]
PfamiPF11629. Mst1_SARAH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50951. SARAH. 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. AlignAdd to basket

Isoform 1 (identifier: Q13043-1) [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
METVQLRNPP RRQLKKLDED SLTKQPEEVF DVLEKLGEGS YGSVYKAIHK
60 70 80 90 100
ETGQIVAIKQ VPVESDLQEI IKEISIMQQC DSPHVVKYYG SYFKNTDLWI
110 120 130 140 150
VMEYCGAGSV SDIIRLRNKT LTEDEIATIL QSTLKGLEYL HFMRKIHRDI
160 170 180 190 200
KAGNILLNTE GHAKLADFGV AGQLTDTMAK RNTVIGTPFW MAPEVIQEIG
210 220 230 240 250
YNCVADIWSL GITAIEMAEG KPPYADIHPM RAIFMIPTNP PPTFRKPELW
260 270 280 290 300
SDNFTDFVKQ CLVKSPEQRA TATQLLQHPF VRSAKGVSIL RDLINEAMDV
310 320 330 340 350
KLKRQESQQR EVDQDDEENS EEDEMDSGTM VRAVGDEMGT VRVASTMTDG
360 370 380 390 400
ANTMIEHDDT LPSQLGTMVI NAEDEEEEGT MKRRDETMQP AKPSFLEYFE
410 420 430 440 450
QKEKENQINS FGKSVPGPLK NSSDWKIPQD GDYEFLKSWT VEDLQKRLLA
460 470 480
LDPMMEQEIE EIRQKYQSKR QPILDAIEAK KRRQQNF
Length:487
Mass (Da):55,630
Last modified:February 21, 2001 - v2
Checksum:i150758EBC5F77D5C
GO
Isoform 2 (identifier: Q13043-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     436-462: LKSWTVEDLQKRLLALDPMMEQEIEEI → KTSQEQQSGKDICIQNCQGNLLCRYAF
     463-487: Missing.

Note: No experimental confirmation available.
Show »
Length:462
Mass (Da):52,335
Checksum:i9CFFF2D1FBC316E8
GO

Sequence cautioni

The sequence AAH29511 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH58916 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti222P → R in AAA83254 (PubMed:7665586).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041123162H → N.1 PublicationCorresponds to variant rs55850759dbSNPEnsembl.1
Natural variantiVAR_041124310R → Q.1 PublicationCorresponds to variant rs35447878dbSNPEnsembl.1
Natural variantiVAR_027040312V → M.2 PublicationsCorresponds to variant rs17420378dbSNPEnsembl.1
Natural variantiVAR_041125355I → T.1 PublicationCorresponds to variant rs35944046dbSNPEnsembl.1
Natural variantiVAR_041126416P → L.1 PublicationCorresponds to variant rs33963346dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_019851436 – 462LKSWT…EIEEI → KTSQEQQSGKDICIQNCQGN LLCRYAF in isoform 2. CuratedAdd BLAST27
Alternative sequenceiVSP_019852463 – 487Missing in isoform 2. CuratedAdd BLAST25

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18297 mRNA. Translation: AAA83254.1.
U60207 mRNA. Translation: AAB17262.1.
AK315238 mRNA. Translation: BAG37665.1.
Z93016, AL109839 Genomic DNA. Translation: CAB07508.2.
AL109839, Z93016 Genomic DNA. Translation: CAI95633.1.
AL109839, Z93016 Genomic DNA. Translation: CAI95634.1.
Z93016, AL109839 Genomic DNA. Translation: CAI19815.1.
CH471077 Genomic DNA. Translation: EAW75882.1.
BC029511 mRNA. Translation: AAH29511.1. Sequence problems.
BC058916 mRNA. Translation: AAH58916.1. Sequence problems.
BC093768 mRNA. Translation: AAH93768.1.
CCDSiCCDS13341.1. [Q13043-1]
RefSeqiNP_006273.1. NM_006282.3. [Q13043-1]
XP_005260590.1. XM_005260533.2. [Q13043-2]
UniGeneiHs.472838.

Genome annotation databases

EnsembliENST00000372801; ENSP00000361887; ENSG00000101109. [Q13043-2]
ENST00000372806; ENSP00000361892; ENSG00000101109. [Q13043-1]
GeneIDi6789.
KEGGihsa:6789.
UCSCiuc002xnb.4. human. [Q13043-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18297 mRNA. Translation: AAA83254.1.
U60207 mRNA. Translation: AAB17262.1.
AK315238 mRNA. Translation: BAG37665.1.
Z93016, AL109839 Genomic DNA. Translation: CAB07508.2.
AL109839, Z93016 Genomic DNA. Translation: CAI95633.1.
AL109839, Z93016 Genomic DNA. Translation: CAI95634.1.
Z93016, AL109839 Genomic DNA. Translation: CAI19815.1.
CH471077 Genomic DNA. Translation: EAW75882.1.
BC029511 mRNA. Translation: AAH29511.1. Sequence problems.
BC058916 mRNA. Translation: AAH58916.1. Sequence problems.
BC093768 mRNA. Translation: AAH93768.1.
CCDSiCCDS13341.1. [Q13043-1]
RefSeqiNP_006273.1. NM_006282.3. [Q13043-1]
XP_005260590.1. XM_005260533.2. [Q13043-2]
UniGeneiHs.472838.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JO8NMR-A/B432-480[»]
3COMX-ray2.20A/B2-311[»]
4NR2X-ray2.00A/B/C/D/E/F/G/H432-480[»]
4OH8X-ray2.28A432-480[»]
ProteinModelPortaliQ13043.
SMRiQ13043.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112665. 65 interactors.
DIPiDIP-32491N.
IntActiQ13043. 169 interactors.
MINTiMINT-4658525.
STRINGi9606.ENSP00000361892.

Chemistry databases

BindingDBiQ13043.
ChEMBLiCHEMBL4598.
GuidetoPHARMACOLOGYi2225.

PTM databases

iPTMnetiQ13043.
PhosphoSitePlusiQ13043.

Polymorphism and mutation databases

BioMutaiSTK4.
DMDMi13124559.

Proteomic databases

EPDiQ13043.
MaxQBiQ13043.
PaxDbiQ13043.
PeptideAtlasiQ13043.
PRIDEiQ13043.

Protocols and materials databases

DNASUi6789.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372801; ENSP00000361887; ENSG00000101109. [Q13043-2]
ENST00000372806; ENSP00000361892; ENSG00000101109. [Q13043-1]
GeneIDi6789.
KEGGihsa:6789.
UCSCiuc002xnb.4. human. [Q13043-1]

Organism-specific databases

CTDi6789.
DisGeNETi6789.
GeneCardsiSTK4.
H-InvDBHIX0015851.
HGNCiHGNC:11408. STK4.
HPAiCAB004038.
HPA015270.
MalaCardsiSTK4.
MIMi604965. gene.
614868. phenotype.
neXtProtiNX_Q13043.
OpenTargetsiENSG00000101109.
Orphaneti314689. Combined immunodeficiency due to STK4 deficiency.
PharmGKBiPA36215.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0201. Eukaryota.
ENOG410XP9G. LUCA.
GeneTreeiENSGT00810000125395.
HOVERGENiHBG108518.
InParanoidiQ13043.
KOiK04411.
OMAiAMINEAM.
OrthoDBiEOG091G065P.
PhylomeDBiQ13043.
TreeFamiTF354217.

Enzyme and pathway databases

BioCyciZFISH:HS02194-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-2028269. Signaling by Hippo.
SignaLinkiQ13043.
SIGNORiQ13043.

Miscellaneous databases

ChiTaRSiSTK4. human.
EvolutionaryTraceiQ13043.
GeneWikiiSTK4.
GenomeRNAii6789.
PMAP-CutDBQ13043.
PROiQ13043.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101109.
CleanExiHS_MST1.
HS_STK4.
ExpressionAtlasiQ13043. baseline and differential.
GenevisibleiQ13043. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR024205. Mst1_SARAH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR011524. SARAH_dom.
[Graphical view]
PfamiPF11629. Mst1_SARAH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50951. SARAH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTK4_HUMAN
AccessioniPrimary (citable) accession number: Q13043
Secondary accession number(s): B2RCR8
, Q15802, Q4G156, Q5H982, Q6PD60, Q9BR32, Q9NTZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: November 30, 2016
This is version 179 of the entry and version 2 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 20
    Human chromosome 20: 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

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 one 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.