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Q9Y6W6

- DUS10_HUMAN

UniProt

Q9Y6W6 - DUS10_HUMAN

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Protein

Dual specificity protein phosphatase 10

Gene
DUSP10, MKP5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.2 Publications
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei408 – 4081Phosphocysteine intermediate Inferred

GO - Molecular functioni

  1. MAP kinase phosphatase activity Source: UniProtKB
  2. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  3. phosphatase activity Source: UniProtKB
  4. phosphoprotein phosphatase activity Source: ProtInc
  5. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  6. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. inactivation of MAPK activity Source: UniProtKB
  2. JNK cascade Source: ProtInc
  3. negative regulation of JNK cascade Source: RefGenome
  4. negative regulation of JUN kinase activity Source: RefGenome
  5. negative regulation of respiratory burst involved in inflammatory response Source: Ensembl
  6. protein dephosphorylation Source: UniProtKB
  7. regulation of adaptive immune response Source: Ensembl
  8. response to lipopolysaccharide Source: Ensembl
  9. response to stress Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
SignaLinkiQ9Y6W6.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 10 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Mitogen-activated protein kinase phosphatase 5
Short name:
MAP kinase phosphatase 5
Short name:
MKP-5
Gene namesi
Name:DUSP10
Synonyms:MKP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3065. DUSP10.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. Golgi apparatus Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi180 – 1812FM → DD: Reduced enzyme activity with MAPK14. 1 Publication
Mutagenesisi203 – 2042RR → AA: Strongly reduced affinity for MAPK14. Almost abolishes enzyme activity with MAPK14. 1 Publication

Organism-specific databases

PharmGKBiPA27520.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Dual specificity protein phosphatase 10PRO_0000094813Add
BLAST

Proteomic databases

PaxDbiQ9Y6W6.
PRIDEiQ9Y6W6.

PTM databases

PhosphoSiteiQ9Y6W6.

Expressioni

Tissue specificityi

Detected in brain.1 Publication

Gene expression databases

BgeeiQ9Y6W6.
CleanExiHS_DUSP10.
GenevestigatoriQ9Y6W6.

Organism-specific databases

HPAiHPA016758.

Interactioni

Subunit structurei

Monomer. Interacts with MAPK14.3 Publications

Protein-protein interaction databases

BioGridi116389. 11 interactions.
IntActiQ9Y6W6. 10 interactions.
MINTiMINT-8208613.
STRINGi9606.ENSP00000355866.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi152 – 1609
Beta strandi173 – 1764
Helixi180 – 1856
Beta strandi186 – 1883
Helixi199 – 2068
Helixi212 – 2176
Helixi224 – 2307
Beta strandi233 – 2364
Helixi243 – 2453
Beta strandi248 – 2503
Helixi251 – 26111
Beta strandi267 – 2693
Helixi272 – 2765
Turni277 – 2793
Helixi281 – 2833
Beta strandi284 – 2863
Beta strandi323 – 3264
Beta strandi329 – 3324
Helixi336 – 3383
Helixi340 – 3456
Beta strandi348 – 3536
Beta strandi356 – 3583
Helixi363 – 3653
Beta strandi368 – 3725
Beta strandi378 – 3803
Helixi384 – 3863
Helixi387 – 39913
Beta strandi403 – 4075
Beta strandi409 – 4135
Helixi414 – 42613
Helixi431 – 44111
Helixi449 – 46315
Helixi478 – 4825

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZZWX-ray1.60A/B320-467[»]
2OUCX-ray2.20A/B148-287[»]
2OUDX-ray2.80A315-482[»]
3TG1X-ray2.71B139-288[»]
ProteinModelPortaliQ9Y6W6.
SMRiQ9Y6W6. Positions 148-287, 315-482.

Miscellaneous databases

EvolutionaryTraceiQ9Y6W6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 285118RhodaneseAdd
BLAST
Domaini384 – 45370Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 21517Interaction with MAP kinasesAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000069871.
HOVERGENiHBG102158.
InParanoidiQ9Y6W6.
KOiK04459.
OMAiTCPANQM.
OrthoDBiEOG75QR5B.
PhylomeDBiQ9Y6W6.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y6W6-1) [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

MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSANPGSN SHPPVIATTV    50
VSLKAANLTY MPSSSGSARS LNCGCSSASC CTVATYDKDN QAQTQAIAAG 100
TTTTAIGTST TCPANQMVNN NENTGSLSPS SGVGSPVSGT PKQLASIKII 150
YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF MEYNKSHIQG AVHINCADKI 200
SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT NEPSRVMPSQ 250
PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREVGGGA 300
SAASSLLPQP IPTTPDIENA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY 350
VINVTTHLPL YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC 400
GKGLLIHCQA GVSRSATIVI AYLMKHTRMT MTDAYKFVKG KRPIISPNLN 450
FMGQLLEFEE DLNNGVTPRI LTPKLMGVET VV 482
Length:482
Mass (Da):52,642
Last modified:November 1, 1999 - v1
Checksum:iA8CB74ABF9498CD4
GO
Isoform 2 (identifier: Q9Y6W6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-342: Missing.

Show »
Length:140
Mass (Da):16,110
Checksum:iCE151F365D042516
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 342342Missing in isoform 2. VSP_036549Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB026436 mRNA. Translation: BAA81668.1.
AF179212 mRNA. Translation: AAD51857.1.
AK022513 mRNA. Translation: BAB14070.1.
AL590966 Genomic DNA. Translation: CAH71120.1.
CH471100 Genomic DNA. Translation: EAW93283.1.
CH471100 Genomic DNA. Translation: EAW93285.1.
CH471100 Genomic DNA. Translation: EAW93286.1.
CH471100 Genomic DNA. Translation: EAW93287.1.
BC020608 mRNA. Translation: AAH20608.1.
BC031405 mRNA. Translation: AAH31405.1.
BC063826 mRNA. Translation: AAH63826.1.
CCDSiCCDS1528.1. [Q9Y6W6-1]
RefSeqiNP_009138.1. NM_007207.5. [Q9Y6W6-1]
UniGeneiHs.497822.
Hs.732301.

Genome annotation databases

EnsembliENST00000323825; ENSP00000322015; ENSG00000143507. [Q9Y6W6-2]
ENST00000366899; ENSP00000355866; ENSG00000143507. [Q9Y6W6-1]
ENST00000544095; ENSP00000441302; ENSG00000143507. [Q9Y6W6-2]
GeneIDi11221.
KEGGihsa:11221.
UCSCiuc001hmx.2. human. [Q9Y6W6-2]
uc001hmy.2. human. [Q9Y6W6-1]

Polymorphism databases

DMDMi20138090.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB026436 mRNA. Translation: BAA81668.1 .
AF179212 mRNA. Translation: AAD51857.1 .
AK022513 mRNA. Translation: BAB14070.1 .
AL590966 Genomic DNA. Translation: CAH71120.1 .
CH471100 Genomic DNA. Translation: EAW93283.1 .
CH471100 Genomic DNA. Translation: EAW93285.1 .
CH471100 Genomic DNA. Translation: EAW93286.1 .
CH471100 Genomic DNA. Translation: EAW93287.1 .
BC020608 mRNA. Translation: AAH20608.1 .
BC031405 mRNA. Translation: AAH31405.1 .
BC063826 mRNA. Translation: AAH63826.1 .
CCDSi CCDS1528.1. [Q9Y6W6-1 ]
RefSeqi NP_009138.1. NM_007207.5. [Q9Y6W6-1 ]
UniGenei Hs.497822.
Hs.732301.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZZW X-ray 1.60 A/B 320-467 [» ]
2OUC X-ray 2.20 A/B 148-287 [» ]
2OUD X-ray 2.80 A 315-482 [» ]
3TG1 X-ray 2.71 B 139-288 [» ]
ProteinModelPortali Q9Y6W6.
SMRi Q9Y6W6. Positions 148-287, 315-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116389. 11 interactions.
IntActi Q9Y6W6. 10 interactions.
MINTi MINT-8208613.
STRINGi 9606.ENSP00000355866.

Chemistry

ChEMBLi CHEMBL2396511.

PTM databases

PhosphoSitei Q9Y6W6.

Polymorphism databases

DMDMi 20138090.

Proteomic databases

PaxDbi Q9Y6W6.
PRIDEi Q9Y6W6.

Protocols and materials databases

DNASUi 11221.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323825 ; ENSP00000322015 ; ENSG00000143507 . [Q9Y6W6-2 ]
ENST00000366899 ; ENSP00000355866 ; ENSG00000143507 . [Q9Y6W6-1 ]
ENST00000544095 ; ENSP00000441302 ; ENSG00000143507 . [Q9Y6W6-2 ]
GeneIDi 11221.
KEGGi hsa:11221.
UCSCi uc001hmx.2. human. [Q9Y6W6-2 ]
uc001hmy.2. human. [Q9Y6W6-1 ]

Organism-specific databases

CTDi 11221.
GeneCardsi GC01M221874.
HGNCi HGNC:3065. DUSP10.
HPAi HPA016758.
MIMi 608867. gene.
neXtProti NX_Q9Y6W6.
PharmGKBi PA27520.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000069871.
HOVERGENi HBG102158.
InParanoidi Q9Y6W6.
KOi K04459.
OMAi TCPANQM.
OrthoDBi EOG75QR5B.
PhylomeDBi Q9Y6W6.
TreeFami TF105122.

Enzyme and pathway databases

BRENDAi 3.1.3.48. 2681.
SignaLinki Q9Y6W6.

Miscellaneous databases

EvolutionaryTracei Q9Y6W6.
GeneWikii DUSP10.
GenomeRNAii 11221.
NextBioi 42707.
PROi Q9Y6W6.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6W6.
CleanExi HS_DUSP10.
Genevestigatori Q9Y6W6.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view ]
PRINTSi PR01908. ADSPHPHTASE.
PR01764. MAPKPHPHTASE.
SMARTi SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5."
    Tanoue T., Moriguchi T., Nishida E.
    J. Biol. Chem. 274:19949-19956(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "MKP5, a new member of the MAP kinase phosphatase family, which selectively dephosphorylates stress-activated kinases."
    Theodosiou A., Smith A., Gillieron C., Arkinstall S., Ashworth A.
    Oncogene 18:6981-6988(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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] (ISOFORM 2).
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain, Lung, PNS and Testis.
  7. "Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase."
    Jeong D.G., Yoon T.S., Kim J.H., Shim M.Y., Jung S.K., Son J.H., Ryu S.E., Kim S.J.
    J. Mol. Biol. 360:946-955(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 320-467, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, ACTIVE SITE.
  8. "Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5."
    Tao X., Tong L.
    Protein Sci. 16:880-886(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 148-287, SUBUNIT, ACTIVE SITE.
  9. "A distinct interaction mode revealed by the crystal structure of the kinase p38alpha with the MAPK binding domain of the phosphatase MKP5."
    Zhang Y.Y., Wu J.W., Wang Z.X.
    Sci. Signal. 4:RA88-RA88(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 139-288 IN COMPLEX WITH MAPK14, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MAPK14, MUTAGENESIS OF 180-PHE-MET-181 AND 203-ARG-ARG-204.

Entry informationi

Entry nameiDUS10_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6W6
Secondary accession number(s): D3DTB4, Q6GSI4, Q9H9Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 132 of the entry and version 1 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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