Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9P289 (MST4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MST4
Synonyms:MASK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediator of cell growth. Modulates apoptosis. Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

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.

Subunit structure

Homodimer. Interacts with PDCD10 and GOLGA2. Interacts with CTTNBP2NL. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Note: Localizes to the Golgi apparatus. Ref.9 Ref.12

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of apoptotic process

Inferred from direct assay Ref.3. Source: UniProtKB

regulation of cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transduction by phosphorylation

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

centrosome

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.3. Source: IntAct

magnesium ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

protein kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P289-1)

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.
Isoform 2 (identifier: Q9P289-2)

The sequence of this isoform differs from the canonical sequence as follows:
     15-91: Missing.
Isoform 3 (identifier: Q9P289-3)

Also known as: MST4a;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Serine/threonine-protein kinase MST4
PRO_0000086404

Regions

Domain24 – 274251Protein kinase
Nucleotide binding30 – 389ATP By similarity

Sites

Active site1441Proton acceptor By similarity
Binding site531ATP By similarity

Amino acid modifications

Modified residue1781Phosphothreonine; by autocatalysis

Natural variations

Alternative sequence15 – 9177Missing in isoform 2.
VSP_041469
Alternative sequence200 – 26162Missing in isoform 3.
VSP_041470
Natural variant91Q → R. Ref.14
Corresponds to variant rs56035648 [ dbSNP | Ensembl ].
VAR_040844
Natural variant361G → W in a gastric adenocarcinoma sample; somatic mutation. Ref.14
VAR_040845
Natural variant451R → C. Ref.14
Corresponds to variant rs56044451 [ dbSNP | Ensembl ].
VAR_040846

Secondary structure

.................................................................. 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2001. Version 2.
Checksum: 3E31B7E3CBDA5768

FASTA41646,529
        10         20         30         40         50         60 
MAHSPVAVQV PGMQNNIADP EELFTKLERI GKGSFGEVFK GIDNRTQQVV AIKIIDLEEA 

        70         80         90        100        110        120 
EDEIEDIQQE ITVLSQCDSS YVTKYYGSYL KGSKLWIIME YLGGGSALDL LRAGPFDEFQ 

       130        140        150        160        170        180 
IATMLKEILK GLDYLHSEKK IHRDIKAANV LLSEQGDVKL ADFGVAGQLT DTQIKRNTFV 

       190        200        210        220        230        240 
GTPFWMAPEV IQQSAYDSKA DIWSLGITAI ELAKGEPPNS DMHPMRVLFL IPKNNPPTLV 

       250        260        270        280        290        300 
GDFTKSFKEF IDACLNKDPS FRPTAKELLK HKFIVKNSKK TSYLTELIDR FKRWKAEGHS 

       310        320        330        340        350        360 
DDESDSEGSD SESTSRENNT HPEWSFTTVR KKPDPKKVQN GAEQDLVQTL SCLSMIITPA 

       370        380        390        400        410 
FAELKQQDEN NASRNQAIEE LEKSIAVAEA ACPGITDKMV KKLIEKFQKC SADESP 

« Hide

Isoform 2 [UniParc].

Checksum: E80868882811C8DE
Show »

FASTA33937,770
Isoform 3 (MST4a) [UniParc].

Checksum: 34BF60E79E9A42B4
Show »

FASTA35439,658

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"Structural comparison of human mammalian ste20-like kinases."
Record C.J., Chaikuad A., Rellos P., Das S., Pike A.C., Fedorov O., Marsden B.D., Knapp S., Lee W.H.
PLoS ONE 5:E11905-E11905(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-300 IN COMPLEX WITH QUINAZOLIN INHIBITOR, SUBUNIT.
[14]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001035917.1. NM_001042452.1.
NP_001035918.1. NM_001042453.1.
NP_057626.2. NM_016542.3.
UniGeneHs.444247.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9P289.
SMRQ9P289. Positions 17-331, 344-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119722. 129 interactions.
DIPDIP-34049N.
IntActQ9P289. 28 interactions.

Chemistry

BindingDBQ9P289.
ChEMBLCHEMBL5941.
GuidetoPHARMACOLOGY2287.

PTM databases

PhosphoSiteQ9P289.

Polymorphism databases

DMDM73621232.

Proteomic databases

PaxDbQ9P289.
PRIDEQ9P289.

Protocols and materials databases

DNASU51765.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID51765.
KEGGhsa:51765.
UCSCuc004ewk.1. human. [Q9P289-1]
uc004ewl.1. human. [Q9P289-2]
uc004ewm.1. human. [Q9P289-3]

Organism-specific databases

CTD51765.
GeneCardsGC0XP131158.
HPAHPA059921.
MIM300547. gene.
neXtProtNX_Q9P289.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234203.
HOVERGENHBG108518.
InParanoidQ9P289.
KOK08838.
PhylomeDBQ9P289.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
SignaLinkQ9P289.

Gene expression databases

ArrayExpressQ9P289.
BgeeQ9P289.
GenevestigatorQ9P289.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9P289.
GeneWikiMST4.
GenomeRNAi51765.
NextBio55887.
PMAP-CutDBQ9P289.
PROQ9P289.
SOURCESearch...

Entry information

Entry nameMST4_HUMAN
AccessionPrimary (citable) accession number: Q9P289
Secondary accession number(s): B2RAU2 expand/collapse secondary AC list , Q3ZB77, Q8NC04, Q9BXC3, Q9BXC4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2001
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM