Q9P289 (MST4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MST4
Synonyms:	MASK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Apoptosis
Cellular component	Cytoplasm Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome regulation of apoptotic process Inferred from direct assay Ref.3. Source: UniProtKB
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from direct assay Ref.1. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.1. Source: UniProtKB protein kinase activity Inferred from direct assay Ref.1. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-618239,EBI-618239
CTTNBP2NL	Q9P2B4	4	EBI-618239,EBI-1774273
STRIP1	Q5VSL9	2	EBI-618239,EBI-1773588

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 416

416

Serine/threonine-protein kinase MST4

PRO_0000086404

Regions

Domain

24 – 274

251

Protein kinase

Nucleotide binding

30 – 38

9

ATP By similarity

Sites

Active site

144

1

Proton acceptor By similarity

Binding site

53

1

ATP By similarity

Amino acid modifications

Modified residue

178

1

Phosphothreonine; by autocatalysis

Natural variations

Alternative sequence

15 – 91

77

Missing in isoform 2.

VSP_041469

Alternative sequence

200 – 261

62

Missing in isoform 3.

VSP_041470

Natural variant

9

1

Q → R. Ref.14
Corresponds to variant rs56035648 [ dbSNP | Ensembl ].

VAR_040844

Natural variant

36

1

G → W in a gastric adenocarcinoma sample; somatic mutation. Ref.14

VAR_040845

Natural variant

45

1

R → C. Ref.14
Corresponds to variant rs56044451 [ dbSNP | Ensembl ].

VAR_040846

Secondary structure

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416

Helix Strand Turn

Details...

Helix

20 – 23

4

Beta strand

24 – 32

9

Beta strand

34 – 43

10

Turn

44 – 46

3

Beta strand

49 – 56

8

Helix

63 – 74

12

Beta strand

85 – 91

7

Beta strand

94 – 100

7

Beta strand

104 – 106

3

Helix

107 – 111

5

Helix

118 – 132

15

Beta strand

138 – 142

5

Helix

147 – 149

3

Beta strand

150 – 152

3

Beta strand

158 – 161

4

Turn

172 – 174

3

Turn

176 – 178

3

Helix

188 – 191

4

Helix

199 – 214

16

Turn

218 – 221

4

Helix

224 – 233

10

Beta strand

241 – 243

3

Helix

245 – 254

10

Helix

259 – 261

3

Helix

265 – 269

5

Helix

272 – 277

6

Helix

281 – 284

4

Helix

285 – 296

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2001. Version 2. Checksum: 3E31B7E3CBDA5768	FASTA	416	46,529
	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
	Isoform 2 [UniParc]. Checksum: E80868882811C8DE	FASTA	339	37,770
	10 20 30 40 50 60 MAHSPVAVQV PGMQGSKLWI IMEYLGGGSA LDLLRAGPFD EFQIATMLKE ILKGLDYLHS 70 80 90 100 110 120 EKKIHRDIKA ANVLLSEQGD VKLADFGVAG QLTDTQIKRN TFVGTPFWMA PEVIQQSAYD 130 140 150 160 170 180 SKADIWSLGI TAIELAKGEP PNSDMHPMRV LFLIPKNNPP TLVGDFTKSF KEFIDACLNK 190 200 210 220 230 240 DPSFRPTAKE LLKHKFIVKN SKKTSYLTEL IDRFKRWKAE GHSDDESDSE GSDSESTSRE 250 260 270 280 290 300 NNTHPEWSFT TVRKKPDPKK VQNGAEQDLV QTLSCLSMII TPAFAELKQQ DENNASRNQA 310 320 330 IEELEKSIAV AEAACPGITD KMVKKLIEKF QKCSADESP
	Isoform 3 (MST4a) [UniParc]. Checksum: 34BF60E79E9A42B4	FASTA	354	39,658
	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 IQQSAYDSKR PTAKELLKHK FIVKNSKKTS YLTELIDRFK RWKAEGHSDD 250 260 270 280 290 300 ESDSEGSDSE STSRENNTHP EWSFTTVRKK PDPKKVQNGA EQDLVQTLSC LSMIITPAFA 310 320 330 340 350 ELKQQDENNA SRNQAIEELE KSIAVAEAAC PGITDKMVKK LIEKFQKCSA DESP

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. , 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.

IPI

IPI00182383.
IPI00292827.
IPI00760722.

RefSeq

NP_001035917.1. NM_001042452.1.
NP_001035918.1. NM_001042453.1.
NP_057626.2. NM_016542.3.

UniGene

Hs.444247.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GGF	X-ray	2.35	A/B	1-300	[»]
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	[»]

ProteinModelPortal

Q9P289.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9P289. 23 interactions.

PTM databases

PhosphoSite

Q9P289.

Polymorphism databases

DMDM

73621232.

Proteomic databases

PaxDb

Q9P289.

PRIDE

Q9P289.

Protocols and materials databases

DNASU

51765.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

51765.

KEGG

hsa:51765.

UCSC

uc004ewk.1. human.
uc004ewl.1. human.
uc004ewm.1. human.

Organism-specific databases

CTD

51765.

GeneCards

GC0XP131158.

MIM

300547. gene.

neXtProt

NX_Q9P289.

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000234203.

HOVERGEN

HBG108518.

InParanoid

Q9P289.

KO

K16314.

OrthoDB

EOG4MPHQB.

PhylomeDB

Q9P289.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.

SignaLink

Q9P289.

Gene expression databases

ArrayExpress

Q9P289.

Bgee

Q9P289.

Genevestigator

Q9P289.

GermOnline

ENSG00000134602. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9P289.

ChEMBL

CHEMBL5941.

EvolutionaryTrace

Q9P289.

GenomeRNAi

51765.

NextBio

55887.

PMAP-CutDB

Q9P289.

SOURCE

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Entry information

Entry name

MST4_HUMAN

Accession

Primary (citable) accession number: Q9P289
Secondary accession number(s): B2RAU2 , Q3ZB77, Q8NC04, Q9BXC3, Q9BXC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	October 1, 2001
Last modified:	May 29, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.