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Q9P289

- MST4_HUMAN

UniProt

Q9P289 - MST4_HUMAN

Protein

Serine/threonine-protein kinase MST4

Gene

MST4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (01 Oct 2001)
      Previous versions | rss
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    Functioni

    Mediator of cell growth. Modulates apoptosis.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.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 binding Source: UniProtKB
    5. protein kinase activity Source: UniProtKB
    6. 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

    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 MST4 (EC:2.7.11.1)
    Alternative name(s):
    Mammalian STE20-like protein kinase 4
    Short name:
    MST-4
    Mst3 and SOK1-related kinase
    STE20-like kinase MST4
    Serine/threonine-protein kinase MASK
    Gene namesi
    Name:MST4
    Synonyms:MASK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: HPA
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. Golgi apparatus Source: HPA
    5. Golgi membrane Source: UniProtKB-SubCell
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Serine/threonine-protein kinase MST4PRO_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

    ArrayExpressiQ9P289.
    BgeeiQ9P289.
    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. 47 interactions.
    DIPiDIP-34049N.
    IntActiQ9P289. 28 interactions.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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_dom.
    [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

    MAHSPVAVQV PGMQNNIADP EELFTKLERI GKGSFGEVFK GIDNRTQQVV    50
    AIKIIDLEEA EDEIEDIQQE ITVLSQCDSS YVTKYYGSYL KGSKLWIIME 100
    YLGGGSALDL LRAGPFDEFQ IATMLKEILK GLDYLHSEKK IHRDIKAANV 150
    LLSEQGDVKL ADFGVAGQLT DTQIKRNTFV GTPFWMAPEV IQQSAYDSKA 200
    DIWSLGITAI ELAKGEPPNS DMHPMRVLFL IPKNNPPTLV GDFTKSFKEF 250
    IDACLNKDPS FRPTAKELLK HKFIVKNSKK TSYLTELIDR FKRWKAEGHS 300
    DDESDSEGSD SESTSRENNT HPEWSFTTVR KKPDPKKVQN GAEQDLVQTL 350
    SCLSMIITPA FAELKQQDEN NASRNQAIEE LEKSIAVAEA ACPGITDKMV 400
    KKLIEKFQKC SADESP 416
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 47 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.
    HPAi HPA059921.
    MIMi 300547. gene.
    neXtProti NX_Q9P289.

    Phylogenomic databases

    eggNOGi COG0515.
    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

    ArrayExpressi Q9P289.
    Bgeei Q9P289.
    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_dom.
    [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

    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).
    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 nameiMST4_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: October 1, 2014
    This is version 119 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