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Protein

RNA/RNP complex-1-interacting phosphatase

Gene

DUSP11

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

Functioni

Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. In addition, has phosphatase activity with ATP, ADP and O-methylfluorescein phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA metabolism.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521Phosphocysteine intermediatePROSITE-ProRule annotation1 Publication
Active sitei158 – 1581Proton donor/acceptorSequence analysis

GO - Molecular functioni

  • nucleotide phosphatase activity, acting on free nucleotides Source: UniProtKB
  • phosphatase activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • polynucleotide 5'-phosphatase activity Source: UniProtKB
  • protein tyrosine/serine/threonine phosphatase activity Source: InterPro
  • protein tyrosine phosphatase activity Source: ProtInc
  • RNA binding Source: ProtInc

GO - Biological processi

  • peptidyl-tyrosine dephosphorylation Source: GOC
  • polynucleotide 5' dephosphorylation Source: UniProtKB
  • RNA metabolic process Source: UniProtKB
  • RNA processing Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA/RNP complex-1-interacting phosphatase (EC:3.1.3.-)
Alternative name(s):
Dual specificity protein phosphatase 11
Phosphatase that interacts with RNA/RNP complex 1
Gene namesi
Name:DUSP11
Synonyms:PIR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3066. DUSP11.

Subcellular locationi

  • Nucleus 1 Publication
  • Nucleus speckle 1 Publication

GO - Cellular componenti

  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi119 – 1191H → G: No effect on phosphatase activity with ATP and ADP. 1 Publication
Mutagenesisi152 – 1521C → S: Loss of activity. No effect in RNA-binding. 3 Publications
Mutagenesisi154 – 1541H → A: Strongly decreases phosphatase activity with ATP and ADP. 1 Publication
Mutagenesisi157 – 1571N → A: Strongly decreases phosphatase activity with ATP and ADP. 1 Publication
Mutagenesisi192 – 1921R → K: Slightly decreases phosphatase activity with ATP. Strongly decreases phosphatase activity with ADP. 1 Publication

Organism-specific databases

PharmGKBiPA27521.

Polymorphism and mutation databases

BioMutaiDUSP11.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330RNA/RNP complex-1-interacting phosphatasePRO_0000094816Add
BLAST

Proteomic databases

EPDiO75319.
MaxQBiO75319.
PaxDbiO75319.
PRIDEiO75319.

PTM databases

DEPODiO75319.
PhosphoSiteiO75319.

Expressioni

Gene expression databases

BgeeiO75319.
CleanExiHS_DUSP11.
ExpressionAtlasiO75319. baseline and differential.
GenevisibleiO75319. HS.

Organism-specific databases

HPAiHPA056973.

Interactioni

Subunit structurei

May interact with SFRS7 and SFRS9/SRP30C.1 Publication

Protein-protein interaction databases

BioGridi114024. 23 interactions.
IntActiO75319. 5 interactions.
MINTiMINT-1401557.
STRINGi9606.ENSP00000272444.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 373Combined sources
Beta strandi48 – 536Combined sources
Helixi59 – 646Combined sources
Helixi67 – 693Combined sources
Helixi73 – 8210Combined sources
Beta strandi87 – 926Combined sources
Helixi102 – 1043Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi118 – 1203Combined sources
Helixi124 – 13916Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi153 – 1564Combined sources
Helixi157 – 17115Combined sources
Helixi175 – 18612Combined sources
Helixi193 – 2019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JMJX-ray2.38A28-208[»]
4MBBX-ray1.85A29-207[»]
4NYHX-ray1.20A/B/C29-205[»]
ProteinModelPortaliO75319.
SMRiO75319. Positions 29-205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini128 – 19770Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni153 – 1586Substrate bindingCurated

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2386. Eukaryota.
COG5226. LUCA.
HOGENOMiHOG000112295.
HOVERGENiHBG051420.
InParanoidiO75319.
KOiK14165.
OrthoDBiEOG72VH64.
PhylomeDBiO75319.
TreeFamiTF105124.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 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: O75319-1) [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
MSQWHHPRSG WGRRRDFSGR SSAKKKGGNH IPERWKDYLP VGQRMPGTRF
60 70 80 90 100
IAFKVPLQKS FEKKLAPEEC FSPLDLFNKI REQNEELGLI IDLTYTQRYY
110 120 130 140 150
KPEDLPETVP YLKIFTVGHQ VPDDETIFKF KHAVNGFLKE NKDNDKLIGV
160 170 180 190 200
HCTHGLNRTG YLICRYLIDV EGVRPDDAIE LFNRCRGHCL ERQNYIEDLQ
210 220 230 240 250
NGPIRKNWNS SVPRSSDFED SAHLMQPVHN KPVKQGPRYN LHQIQGHSAP
260 270 280 290 300
RHFHTQTQSL QQSVRKFSEN PHVYQRHHLP PPGPPGEDYS HRRYSWNVKP
310 320 330
NASRAAQDRR RWYPYNYSRL SYPACWEWTQ
Length:330
Mass (Da):38,939
Last modified:November 1, 1998 - v1
Checksum:i0C397F43043B450A
GO
Isoform 2 (identifier: O75319-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     166-226: YLIDVEGVRP...DFEDSAHLMQ → RSRALSPRLE...IFSRDVVSPC
     227-330: Missing.

Note: No experimental confirmation available.
Show »
Length:226
Mass (Da):25,892
Checksum:i04748C59187B7CDF
GO

Sequence cautioni

The sequence CAH10467.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651R → I in AAH00346 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei166 – 22661YLIDV…AHLMQ → RSRALSPRLECSGTISTHSK FCFPSSRRSPASASQVAGTT GARHHARLIFCIFSRDVVSP C in isoform 2. 1 PublicationVSP_014136Add
BLAST
Alternative sequencei227 – 330104Missing in isoform 2. 1 PublicationVSP_014137Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023917 mRNA. Translation: AAC39925.1.
AK315271 mRNA. Translation: BAG37685.1.
CR627368 mRNA. Translation: CAH10467.1. Different initiation.
AC092653 Genomic DNA. No translation available.
BC000346 mRNA. Translation: AAH00346.1.
RefSeqiNP_003575.2. NM_003584.2.
UniGeneiHs.14611.

Genome annotation databases

EnsembliENST00000272444; ENSP00000272444; ENSG00000144048.
GeneIDi8446.
KEGGihsa:8446.
UCSCiuc002sjp.4. human. [O75319-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023917 mRNA. Translation: AAC39925.1.
AK315271 mRNA. Translation: BAG37685.1.
CR627368 mRNA. Translation: CAH10467.1. Different initiation.
AC092653 Genomic DNA. No translation available.
BC000346 mRNA. Translation: AAH00346.1.
RefSeqiNP_003575.2. NM_003584.2.
UniGeneiHs.14611.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JMJX-ray2.38A28-208[»]
4MBBX-ray1.85A29-207[»]
4NYHX-ray1.20A/B/C29-205[»]
ProteinModelPortaliO75319.
SMRiO75319. Positions 29-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114024. 23 interactions.
IntActiO75319. 5 interactions.
MINTiMINT-1401557.
STRINGi9606.ENSP00000272444.

PTM databases

DEPODiO75319.
PhosphoSiteiO75319.

Polymorphism and mutation databases

BioMutaiDUSP11.

Proteomic databases

EPDiO75319.
MaxQBiO75319.
PaxDbiO75319.
PRIDEiO75319.

Protocols and materials databases

DNASUi8446.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272444; ENSP00000272444; ENSG00000144048.
GeneIDi8446.
KEGGihsa:8446.
UCSCiuc002sjp.4. human. [O75319-1]

Organism-specific databases

CTDi8446.
GeneCardsiDUSP11.
H-InvDBHIX0017827.
HGNCiHGNC:3066. DUSP11.
HPAiHPA056973.
MIMi603092. gene.
neXtProtiNX_O75319.
PharmGKBiPA27521.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2386. Eukaryota.
COG5226. LUCA.
HOGENOMiHOG000112295.
HOVERGENiHBG051420.
InParanoidiO75319.
KOiK14165.
OrthoDBiEOG72VH64.
PhylomeDBiO75319.
TreeFamiTF105124.

Miscellaneous databases

ChiTaRSiDUSP11. human.
GenomeRNAii8446.
NextBioi31602.
PROiO75319.
SOURCEiSearch...

Gene expression databases

BgeeiO75319.
CleanExiHS_DUSP11.
ExpressionAtlasiO75319. baseline and differential.
GenevisibleiO75319. HS.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PIR1, a novel phosphatase that exhibits high affinity to RNA ribonucleoprotein complexes."
    Yuan Y., Li D.-M., Sun H.
    J. Biol. Chem. 273:20347-20353(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SFRS7 AND SFRS9, MUTAGENESIS OF CYS-152, SUBCELLULAR LOCATION.
  2. "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 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cerebellum.
  4. "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] [Europe PMC] [Abstract]
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle.
  6. "Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA 5'-triphosphatase and diphosphatase activities."
    Deshpande T., Takagi T., Hao L., Buratowski S., Charbonneau H.
    J. Biol. Chem. 274:16590-16594(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-152, FUNCTION.
  7. "Structure of human PIR1, an atypical dual-specificity phosphatase."
    Sankhala R.S., Lokareddy R.K., Cingolani G.
    Biochemistry 53:862-871(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 29-205 OF MUTANT SER-152 IN COMPLEX WITH PHOSPHATE, MUTAGENESIS OF HIS-119; CYS-152; HIS-154; ASN-157 AND ARG-192, ACTIVE SITE, FUNCTION.

Entry informationi

Entry nameiDUS11_HUMAN
AccessioniPrimary (citable) accession number: O75319
Secondary accession number(s): B2RCT8, Q6AI47, Q9BWE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 136 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 2
    Human chromosome 2: 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

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 one 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.