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Protein

Dual specificity protein phosphatase 10

Gene

DUSP10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei408 – 4081Phosphocysteine intermediate2 Publications

GO - Molecular functioni

  • MAP kinase phosphatase activity Source: UniProtKB
  • MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  • phosphatase activity Source: UniProtKB
  • phosphoprotein phosphatase activity Source: ProtInc
  • protein tyrosine/serine/threonine phosphatase activity Source: GO_Central
  • protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAi3.1.3.16. 2681.
3.1.3.48. 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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3065. DUSP10.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • Golgi apparatus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
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.

Polymorphism and mutation databases

BioMutaiDUSP10.
DMDMi20138090.

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiQ9Y6W6.
PRIDEiQ9Y6W6.

PTM databases

DEPODiQ9Y6W6.
PhosphoSiteiQ9Y6W6.

Expressioni

Tissue specificityi

Detected in brain.1 Publication

Gene expression databases

BgeeiQ9Y6W6.
CleanExiHS_DUSP10.
GenevisibleiQ9Y6W6. HS.

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 – 1609Combined sources
Beta strandi173 – 1764Combined sources
Helixi180 – 1856Combined sources
Beta strandi186 – 1883Combined sources
Helixi199 – 2068Combined sources
Helixi212 – 2176Combined sources
Helixi224 – 2307Combined sources
Beta strandi233 – 2364Combined sources
Helixi243 – 2453Combined sources
Beta strandi248 – 2503Combined sources
Helixi251 – 26111Combined sources
Beta strandi267 – 2693Combined sources
Helixi272 – 2765Combined sources
Turni277 – 2793Combined sources
Helixi281 – 2833Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi323 – 3264Combined sources
Beta strandi329 – 3324Combined sources
Helixi336 – 3383Combined sources
Helixi340 – 3456Combined sources
Beta strandi348 – 3536Combined sources
Beta strandi356 – 3583Combined sources
Helixi363 – 3653Combined sources
Beta strandi368 – 3725Combined sources
Beta strandi378 – 3803Combined sources
Helixi384 – 3863Combined sources
Helixi387 – 39913Combined sources
Beta strandi403 – 4075Combined sources
Beta strandi409 – 4135Combined sources
Helixi414 – 42613Combined sources
Helixi431 – 44111Combined sources
Helixi449 – 46315Combined sources
Helixi478 – 4825Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6W6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 285118RhodanesePROSITE-ProRule annotationAdd
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.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
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. AlignAdd to basket

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

        10         20         30         40         50
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSANPGSN SHPPVIATTV
60 70 80 90 100
VSLKAANLTY MPSSSGSARS LNCGCSSASC CTVATYDKDN QAQTQAIAAG
110 120 130 140 150
TTTTAIGTST TCPANQMVNN NENTGSLSPS SGVGSPVSGT PKQLASIKII
160 170 180 190 200
YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF MEYNKSHIQG AVHINCADKI
210 220 230 240 250
SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT NEPSRVMPSQ
260 270 280 290 300
PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREVGGGA
310 320 330 340 350
SAASSLLPQP IPTTPDIENA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY
360 370 380 390 400
VINVTTHLPL YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC
410 420 430 440 450
GKGLLIHCQA GVSRSATIVI AYLMKHTRMT MTDAYKFVKG KRPIISPNLN
460 470 480
FMGQLLEFEE DLNNGVTPRI LTPKLMGVET VV
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. 2 PublicationsVSP_036549Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000366899; ENSP00000355866; ENSG00000143507. [Q9Y6W6-1]
GeneIDi11221.
KEGGihsa:11221.
UCSCiuc001hmx.2. human. [Q9Y6W6-2]
uc001hmy.2. human. [Q9Y6W6-1]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiQ9Y6W6.
ChEMBLiCHEMBL2396511.

PTM databases

DEPODiQ9Y6W6.
PhosphoSiteiQ9Y6W6.

Polymorphism and mutation databases

BioMutaiDUSP10.
DMDMi20138090.

Proteomic databases

PaxDbiQ9Y6W6.
PRIDEiQ9Y6W6.

Protocols and materials databases

DNASUi11221.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366899; ENSP00000355866; ENSG00000143507. [Q9Y6W6-1]
GeneIDi11221.
KEGGihsa:11221.
UCSCiuc001hmx.2. human. [Q9Y6W6-2]
uc001hmy.2. human. [Q9Y6W6-1]

Organism-specific databases

CTDi11221.
GeneCardsiGC01M221874.
HGNCiHGNC:3065. DUSP10.
HPAiHPA016758.
MIMi608867. gene.
neXtProtiNX_Q9Y6W6.
PharmGKBiPA27520.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000069871.
HOVERGENiHBG102158.
InParanoidiQ9Y6W6.
KOiK04459.
OMAiTCPANQM.
OrthoDBiEOG75QR5B.
PhylomeDBiQ9Y6W6.
TreeFamiTF105122.

Enzyme and pathway databases

BRENDAi3.1.3.16. 2681.
3.1.3.48. 2681.
SignaLinkiQ9Y6W6.

Miscellaneous databases

ChiTaRSiDUSP10. human.
EvolutionaryTraceiQ9Y6W6.
GeneWikiiDUSP10.
GenomeRNAii11221.
NextBioi42707.
PROiQ9Y6W6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y6W6.
CleanExiHS_DUSP10.
GenevisibleiQ9Y6W6. HS.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 142 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.