Q05923 (DUS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 2
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
Dual specificity protein phosphatase PAC-1

Gene names

Name:	DUSP2
Synonyms:	PAC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subcellular location	Nucleus.
Tissue specificity	Expressed in hematopoietic tissues.
Induction	By mitogens.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 rhodanese domain. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Cellular component	Nucleus
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	endoderm formation Inferred from Biological aspect of Ancestor. Source: RefGenome inactivation of MAPK activity Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of apoptotic process Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	nucleoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Traceable author statement. Source: ProtInc protein tyrosine/threonine phosphatase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 314

314

Dual specificity protein phosphatase 2

PRO_0000094793

Regions

Domain

23 – 144

122

Rhodanese

Domain

237 – 302

66

Tyrosine-protein phosphatase

Sites

Active site

257

1

Phosphocysteine intermediate By similarity

Secondary structure

1

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314

Helix Strand Turn

Details...

Beta strand

174 – 176

3

Turn

177 – 179

3

Beta strand

180 – 182

3

Helix

188 – 197

10

Beta strand

200 – 204

5

Beta strand

206 – 213

8

Beta strand

215 – 221

7

Helix

236 – 248

13

Beta strand

253 – 255

3

Beta strand

258 – 262

5

Helix

263 – 274

12

Helix

279 – 287

9

Helix

305 – 311

7

Sequences

	Sequence		Length	Mass (Da)
	Q05923 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: FDD3543C6DE10CA5	FASTA	314	34,400
	10 20 30 40 50 60 MGLEAARELE CAALGTLLRD PREAERTLLL DCRPFLAFCR RHVRAARPVP WNALLRRRAR 70 80 90 100 110 120 GPPAAVLACL LPDRALRTRL VRGELARAVV LDEGSASVAE LRPDSPAHVL LAALLHETRA 130 140 150 160 170 180 GPTAVYFLRG GFDGFQGCCP DLCSEAPAPA LPPTGDKTSR SDSRAPVYDQ GGPVEILPYL 190 200 210 220 230 240 FLGSCSHSSD LQGLQACGIT AVLNVSASCP NHFEGLFRYK SIPVEDNQMV EISAWFQEAI 250 260 270 280 290 300 GFIDWVKNSG GRVLVHCQAG ISRSATICLA YLMQSRRVRL DEAFDFVKQR RGVISPNFSF 310 MGQLLQFETQ VLCH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase." Rohan P., Davis P., Moskaluk C.A., Kearns M., Krutzsch H., Siebenlist U., Kelly K. Science 259:1763-1766(1993) [PubMed: 7681221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic organization and chromosomal localization of the DUSP2 gene, encoding a MAP kinase phosphatase, to human 2p11.2-q11." Yi H., Morton C.C., Weremowicz S., McBride O.W., Kelly K. Genomics 28:92-96(1995) [PubMed: 7590752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: B-cell.
[6]	"Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP." Farooq A., Plotnikova O., Chaturvedi G., Yan S., Zeng L., Zhang Q., Zhou M.M. Structure 11:155-164(2003) [PubMed: 12575935] [Abstract] Cited for: STRUCTURE BY NMR OF 170-314.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L11329 mRNA. Translation: AAA50779.1.
U23853 Genomic DNA. Translation: AAA86112.1.
AC012307 Genomic DNA. Translation: AAY24222.1.
CH471207 Genomic DNA. Translation: EAW71385.1.
BC007771 mRNA. Translation: AAH07771.1.

IPI

IPI00016729.

PIR

A57126.

RefSeq

NP_004409.1. NM_004418.3.

UniGene

Hs.1183.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M3G	NMR	-	A	170-314	[»]

ProteinModelPortal

Q05923.

SMR

Q05923. Positions 1-148, 170-314.

ModBase

Search...

Protein-protein interaction databases

STRING

Q05923.

PTM databases

PhosphoSite

Q05923.

Polymorphism databases

DMDM

464334.

Proteomic databases

PRIDE

Q05923.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000288943; ENSP00000288943; ENSG00000158050.

GeneID

1844.

KEGG

hsa:1844.

UCSC

uc002svk.2. human.

Organism-specific databases

CTD

1844.

GeneCards

GC02M096808.

H-InvDB

HIX0002269.

HGNC

HGNC:3068. DUSP2.

MIM

603068. gene.

neXtProt

NX_Q05923.

PharmGKB

PA27525.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16280.

GeneTree

ENSGT00600000084364.

HOGENOM

HBG713414.

HOVERGEN

HBG007347.

InParanoid

Q05923.

OMA

AIGFIDW.

OrthoDB

EOG4K3KWW.

PhylomeDB

Q05923.

Gene expression databases

ArrayExpress

Q05923.

Bgee

Q05923.

CleanEx

HS_DUSP2.

Genevestigator

Q05923.

GermOnline

ENSG00000158050. Homo sapiens.

Family and domain databases

InterPro

IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR014393. Dual_MAP_Kinase_Phosphatase.
IPR008343. MAPK_phosph.
IPR001763. Rhodanese-like.
IPR000387. Tyr/Dual-specificity_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]

Gene3D

G3DSA:3.40.250.10. Rhodanese-like. 1 hit.

KO

K04459.

Pfam

PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]

PIRSF

PIRSF000939. MAPK_Ptase. 1 hit.

PRINTS

PR01764. MAPKPHPHTASE.

SMART

SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

NextBio

7551.

SOURCE

Search...

Entry information

Entry name

DUS2_HUMAN

Accession

Primary (citable) accession number: Q05923
Secondary accession number(s): Q53T45

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 123 of the entry and version 1 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.