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Q9P289

- STK26_HUMAN

UniProt

Q9P289 - STK26_HUMAN

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Protein

Serine/threonine-protein kinase 26

Gene

STK26

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

Functioni

Mediator of cell growth. Modulates apoptosis.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+By similarity

Enzyme regulationi

Interaction with Golgi matrix protein GOLGA2 leads to autophosphorylation on Thr-178, possibly as a consequence of stabilization of dimer formation. May also be activated by C-terminal cleavage.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531ATPPROSITE-ProRule annotation
Active sitei144 – 1441Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. magnesium ion binding Source: UniProtKB
  4. protein kinase activity Source: UniProtKB
  5. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  3. protein phosphorylation Source: UniProtKB
  4. regulation of apoptotic process Source: UniProtKB
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

ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
SignaLinkiQ9P289.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 26Curated (EC:2.7.11.11 Publication)
Alternative name(s):
MST3 and SOK1-related kinase1 Publication
Mammalian STE20-like protein kinase 41 Publication
Short name:
MST-4Curated
Short name:
STE20-like kinase MST4Curated
Serine/threonine-protein kinase MASKCurated
Gene namesi
Name:STK26Imported
Synonyms:MASK1 Publication, MST41 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:18174. STK26.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. Golgi apparatus Source: HPA
  6. membrane Source: UniProtKB-KW
  7. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Serine/threonine-protein kinase 26PRO_0000086404Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei178 – 1781Phosphothreonine; by autocatalysis1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9P289.
PaxDbiQ9P289.
PRIDEiQ9P289.

PTM databases

PhosphoSiteiQ9P289.

Miscellaneous databases

PMAP-CutDBQ9P289.

Expressioni

Gene expression databases

BgeeiQ9P289.
ExpressionAtlasiQ9P289. baseline and differential.
GenevestigatoriQ9P289.

Organism-specific databases

HPAiHPA059921.

Interactioni

Subunit structurei

Homodimer. Interacts with PDCD10 and GOLGA2. Interacts with CTTNBP2NL.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-618239,EBI-618239
CAB39Q9Y3766EBI-618239,EBI-306905
CTTNBP2NLQ9P2B44EBI-618239,EBI-1774273
STRIP1Q5VSL92EBI-618239,EBI-1773588

Protein-protein interaction databases

BioGridi119722. 51 interactions.
DIPiDIP-34049N.
IntActiQ9P289. 28 interactions.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 234Combined sources
Beta strandi24 – 329Combined sources
Beta strandi34 – 4310Combined sources
Turni44 – 463Combined sources
Beta strandi49 – 568Combined sources
Turni58 – 603Combined sources
Helixi63 – 7412Combined sources
Beta strandi85 – 917Combined sources
Beta strandi94 – 1007Combined sources
Beta strandi104 – 1063Combined sources
Helixi107 – 1115Combined sources
Helixi118 – 13215Combined sources
Beta strandi138 – 1425Combined sources
Helixi147 – 1493Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi158 – 1614Combined sources
Turni162 – 1643Combined sources
Turni172 – 1743Combined sources
Turni176 – 1783Combined sources
Helixi188 – 1914Combined sources
Helixi199 – 21416Combined sources
Turni218 – 2214Combined sources
Helixi224 – 23310Combined sources
Beta strandi241 – 2433Combined sources
Helixi245 – 25410Combined sources
Helixi259 – 2613Combined sources
Helixi265 – 2695Combined sources
Helixi272 – 2776Combined sources
Helixi281 – 2844Combined sources
Helixi285 – 29612Combined sources
Helixi346 – 3505Combined sources
Helixi352 – 3554Combined sources
Helixi357 – 36610Combined sources
Turni367 – 3704Combined sources
Helixi372 – 39120Combined sources
Helixi395 – 40915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GGFX-ray2.35A/B1-300[»]
3W8IX-ray2.40B346-416[»]
4FZAX-ray3.15B18-297[»]
4FZDX-ray3.25B18-297[»]
C323-327[»]
4FZFX-ray3.64B18-297[»]
4GEHX-ray1.95B/D325-413[»]
ProteinModelPortaliQ9P289.
SMRiQ9P289. Positions 17-331, 344-412.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P289.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 274251Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091192.
HOGENOMiHOG000234203.
HOVERGENiHBG108518.
InParanoidiQ9P289.
KOiK08838.
PhylomeDBiQ9P289.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. 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.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9P289-1) [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
MAHSPVAVQV PGMQNNIADP EELFTKLERI GKGSFGEVFK GIDNRTQQVV
60 70 80 90 100
AIKIIDLEEA EDEIEDIQQE ITVLSQCDSS YVTKYYGSYL KGSKLWIIME
110 120 130 140 150
YLGGGSALDL LRAGPFDEFQ IATMLKEILK GLDYLHSEKK IHRDIKAANV
160 170 180 190 200
LLSEQGDVKL ADFGVAGQLT DTQIKRNTFV GTPFWMAPEV IQQSAYDSKA
210 220 230 240 250
DIWSLGITAI ELAKGEPPNS DMHPMRVLFL IPKNNPPTLV GDFTKSFKEF
260 270 280 290 300
IDACLNKDPS FRPTAKELLK HKFIVKNSKK TSYLTELIDR FKRWKAEGHS
310 320 330 340 350
DDESDSEGSD SESTSRENNT HPEWSFTTVR KKPDPKKVQN GAEQDLVQTL
360 370 380 390 400
SCLSMIITPA FAELKQQDEN NASRNQAIEE LEKSIAVAEA ACPGITDKMV
410
KKLIEKFQKC SADESP
Length:416
Mass (Da):46,529
Last modified:October 1, 2001 - v2
Checksum:i3E31B7E3CBDA5768
GO
Isoform 2 (identifier: Q9P289-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     15-91: Missing.

Show »
Length:339
Mass (Da):37,770
Checksum:iE80868882811C8DE
GO
Isoform 3 (identifier: Q9P289-3) [UniParc]FASTAAdd to Basket

Also known as: MST4a

The sequence of this isoform differs from the canonical sequence as follows:
     200-261: Missing.

Show »
Length:354
Mass (Da):39,658
Checksum:i34BF60E79E9A42B4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91Q → R.1 Publication
Corresponds to variant rs56035648 [ dbSNP | Ensembl ].
VAR_040844
Natural varianti36 – 361G → W in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040845
Natural varianti45 – 451R → C.1 Publication
Corresponds to variant rs56044451 [ dbSNP | Ensembl ].
VAR_040846

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei15 – 9177Missing in isoform 2. 1 PublicationVSP_041469Add
BLAST
Alternative sequencei200 – 26162Missing in isoform 3. 1 PublicationVSP_041470Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF231012 mRNA. Translation: AAK38484.1.
AF344882 mRNA. Translation: AAK29620.1.
AF344883 mRNA. Translation: AAK29621.1.
AB040057 mRNA. Translation: BAA92785.2.
BT020099 mRNA. Translation: AAV38902.1.
AK075107 mRNA. Translation: BAC11406.1.
AK314356 mRNA. Translation: BAG36989.1.
AL109749 Genomic DNA. Translation: CAI42079.1.
CH471107 Genomic DNA. Translation: EAX11786.1.
CH471107 Genomic DNA. Translation: EAX11787.1.
BC098315 mRNA. Translation: AAH98315.1.
BC103503 mRNA. Translation: AAI03504.1.
CCDSiCCDS14631.1. [Q9P289-1]
CCDS43995.1. [Q9P289-3]
CCDS48168.1. [Q9P289-2]
RefSeqiNP_001035917.1. NM_001042452.1. [Q9P289-3]
NP_001035918.1. NM_001042453.1. [Q9P289-2]
NP_057626.2. NM_016542.3. [Q9P289-1]
UniGeneiHs.444247.

Genome annotation databases

GeneIDi51765.
KEGGihsa:51765.
UCSCiuc004ewk.1. human. [Q9P289-1]
uc004ewl.1. human. [Q9P289-2]
uc004ewm.1. human. [Q9P289-3]

Polymorphism databases

DMDMi73621232.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF231012 mRNA. Translation: AAK38484.1 .
AF344882 mRNA. Translation: AAK29620.1 .
AF344883 mRNA. Translation: AAK29621.1 .
AB040057 mRNA. Translation: BAA92785.2 .
BT020099 mRNA. Translation: AAV38902.1 .
AK075107 mRNA. Translation: BAC11406.1 .
AK314356 mRNA. Translation: BAG36989.1 .
AL109749 Genomic DNA. Translation: CAI42079.1 .
CH471107 Genomic DNA. Translation: EAX11786.1 .
CH471107 Genomic DNA. Translation: EAX11787.1 .
BC098315 mRNA. Translation: AAH98315.1 .
BC103503 mRNA. Translation: AAI03504.1 .
CCDSi CCDS14631.1. [Q9P289-1 ]
CCDS43995.1. [Q9P289-3 ]
CCDS48168.1. [Q9P289-2 ]
RefSeqi NP_001035917.1. NM_001042452.1. [Q9P289-3 ]
NP_001035918.1. NM_001042453.1. [Q9P289-2 ]
NP_057626.2. NM_016542.3. [Q9P289-1 ]
UniGenei Hs.444247.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GGF X-ray 2.35 A/B 1-300 [» ]
3W8I X-ray 2.40 B 346-416 [» ]
4FZA X-ray 3.15 B 18-297 [» ]
4FZD X-ray 3.25 B 18-297 [» ]
C 323-327 [» ]
4FZF X-ray 3.64 B 18-297 [» ]
4GEH X-ray 1.95 B/D 325-413 [» ]
ProteinModelPortali Q9P289.
SMRi Q9P289. Positions 17-331, 344-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119722. 51 interactions.
DIPi DIP-34049N.
IntActi Q9P289. 28 interactions.

Chemistry

BindingDBi Q9P289.
ChEMBLi CHEMBL5941.
GuidetoPHARMACOLOGYi 2287.

PTM databases

PhosphoSitei Q9P289.

Polymorphism databases

DMDMi 73621232.

Proteomic databases

MaxQBi Q9P289.
PaxDbi Q9P289.
PRIDEi Q9P289.

Protocols and materials databases

DNASUi 51765.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 51765.
KEGGi hsa:51765.
UCSCi uc004ewk.1. human. [Q9P289-1 ]
uc004ewl.1. human. [Q9P289-2 ]
uc004ewm.1. human. [Q9P289-3 ]

Organism-specific databases

CTDi 51765.
GeneCardsi GC0XP131158.
HGNCi HGNC:18174. STK26.
HPAi HPA059921.
MIMi 300547. gene.
neXtProti NX_Q9P289.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00640000091192.
HOGENOMi HOG000234203.
HOVERGENi HBG108518.
InParanoidi Q9P289.
KOi K08838.
PhylomeDBi Q9P289.

Enzyme and pathway databases

Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
SignaLinki Q9P289.

Miscellaneous databases

EvolutionaryTracei Q9P289.
GeneWikii MST4.
GenomeRNAii 51765.
NextBioi 55887.
PMAP-CutDB Q9P289.
PROi Q9P289.
SOURCEi Search...

Gene expression databases

Bgeei Q9P289.
ExpressionAtlasi Q9P289. baseline and differential.
Genevestigatori Q9P289.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "MST4, a new Ste20-related kinase that mediates cell growth and transformation via modulating ERK pathway."
    Lin J.-L., Chen H.-C., Fang H.-I., Robinson D., Kung H.-J., Shih H.-M.
    Oncogene 20:6559-6569(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY.
  2. "Cloning and characterization of MST4, a novel Ste20-like kinase."
    Qian Z., Lin C., Espinosa R., LeBeau M., Rosner M.R.
    J. Biol. Chem. 276:22439-22445(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    Tissue: Fetal brain.
  3. "Cloning of MASK, a novel member of the mammalian germinal center kinase III subfamily, with apoptosis-inducing properties."
    Dan I., Ong S.E., Watanabe N.M., Blagoev B., Nielsen M.M., Kajikawa E., Kristiansen T.Z., Mann M., Pandey A.
    J. Biol. Chem. 277:5929-5939(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Placenta.
  6. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1).
  9. "YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta."
    Preisinger C., Short B., De Corte V., Bruyneel E., Haas A., Kopajtich R., Gettemans J., Barr F.A.
    J. Cell Biol. 164:1009-1020(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-178, INTERACTION WITH GOLGA2, ENZYME REGULATION.
  10. "PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and transformation via modulation of the ERK pathway."
    Ma X., Zhao H., Shan J., Long F., Chen Y., Chen Y., Zhang Y., Han X., Ma D.
    Mol. Biol. Cell 18:1965-1978(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDCD10, FUNCTION, SUBCELLULAR LOCATION.
  11. "Functional analyses of human and zebrafish 18-amino acid in-frame deletion pave the way for domain mapping of the cerebral cavernous malformation 3 protein."
    Voss K., Stahl S., Hogan B.M., Reinders J., Schleider E., Schulte-Merker S., Felbor U.
    Hum. Mutat. 30:1003-1011(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDCD10.
  12. "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
    Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
    Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTTNBP2NL.
  13. "CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell orientation."
    Fidalgo M., Fraile M., Pires A., Force T., Pombo C., Zalvide J.
    J. Cell Sci. 123:1274-1284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDCD10 AND GOLGA2, SUBCELLULAR LOCATION.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-300 IN COMPLEX WITH QUINAZOLIN INHIBITOR, SUBUNIT.
  15. "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: VARIANTS [LARGE SCALE ANALYSIS] ARG-9; TRP-36 AND CYS-45.

Entry informationi

Entry nameiSTK26_HUMAN
AccessioniPrimary (citable) accession number: Q9P289
Secondary accession number(s): B2RAU2
, Q3ZB77, Q8NC04, Q9BXC3, Q9BXC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2001
Last modified: November 26, 2014
This is version 121 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, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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