Q96C86 (DCPS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Scavenger mRNA-decapping enzyme DcpS
EC=3.-.-.-

Alternative name(s):
DCS-1
Hint-related 7meGMP-directed hydrolase
Histidine triad protein member 5
Short name=HINT-5

Gene names

Name:	DCPS
Synonyms:	DCS1, HINT5
ORF Names:	HSPC015

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	337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Necessary for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA fragments shorter than 10 nucleotides that are produced by 3'->5' exosome-mediated mRNA decay. Releases m7GMP. Can also degrade m7GDP to m7GMP. Has no activity towards mRNA molecules longer than 25 nucleotides. Ref.2 Ref.3 Ref.7 Ref.8 Ref.9
Subunit structure	Homodimer. Associates with components of the exosome multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Ref.2 Ref.13
Subcellular location	Cytoplasm. Nucleus Ref.3 Ref.9.
Tissue specificity	Detected in liver, brain, kidney, testis and prostate. Ref.3
Sequence similarities	Belongs to the HIT family.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	deadenylation-dependent decapping of nuclear-transcribed mRNA Inferred from electronic annotation. Source: InterPro exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Traceable author statement. Source: Reactome nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 337

336

Scavenger mRNA-decapping enzyme DcpS

PRO_0000109794

Regions

Region

268 – 279

12

Substrate binding

Motif

275 – 279

5

Histidine triad motif

Sites

Active site

277

1

Nucleophile

Binding site

185

1

Substrate

Binding site

207

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6 Ref.10

Modified residue

138

1

N6-acetyllysine Ref.11

Modified residue

142

1

N6-acetyllysine Ref.11

Natural variations

Natural variant

73

1

G → E. Ref.5
Corresponds to variant rs11557735 [ dbSNP | Ensembl ].

VAR_027958

Experimental info

Mutagenesis

58

1

R → A: Increases decapping activity to 125% of wild-type. Ref.13

Mutagenesis

61

1

I → A: No effect. Ref.13

Mutagenesis

63

1

F → A: No effect. Ref.13

Mutagenesis

83

1

I → A: Strongly reduces decapping activity. Ref.13

Mutagenesis

85

1

E → A: Reduces decapping activity. Ref.13

Mutagenesis

108

1

F → A: Reduces decapping activity. Ref.13

Mutagenesis

110

1

N → A: Loss of decapping activity. Ref.13

Mutagenesis

113

1

Y → A: Loss of decapping activity. Ref.13

Mutagenesis

128

1

K → A: No effect. Ref.13

Mutagenesis

138

1

K → D: Increases decapping activity to 250% of wild-type. Ref.13

Mutagenesis

145

1

R → A: Increases decapping activity to 180% of wild-type. Ref.13

Mutagenesis

146

1

Q → P: Increases decapping activity to 140% of wild-type. Ref.13

Mutagenesis

175

1

W → A: Loss of decapping activity. Ref.13

Mutagenesis

185

1

E → A: Loss of decapping activity. Ref.13

Mutagenesis

204

1

P → A: Reduces decapping activity. Ref.13

Mutagenesis

205

1

D → A: Reduces decapping activity. Ref.13

Mutagenesis

206

1

L → A: No effect. Ref.13

Mutagenesis

207

1

K → A: Reduces decapping activity. Ref.13

Mutagenesis

207

1

K → R: No effect. Ref.13

Mutagenesis

217

1

Y → A: No effect. Ref.13

Mutagenesis

217

1

Y → F: Reduces decapping activity. Ref.13

Mutagenesis

268

1

H → N: Loss of decapping activity. Ref.13

Mutagenesis

272

1

S → A: No effect. Ref.13

Mutagenesis

277

1

H → N: Loss of decapping activity. Ref.2 Ref.13

Mutagenesis

279

1

H → N: Loss of decapping activity. Ref.13

Mutagenesis

294

1

R → A or K: No effect. Ref.13

Mutagenesis

322

1

R → A: No effect. Ref.13

Sequence conflict

69

1

N → K in AAK91763. Ref.1

Secondary structure

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337

Helix Strand Turn

Details...

Beta strand

43 – 45

3

Beta strand

48 – 56

9

Turn

57 – 60

4

Beta strand

61 – 68

8

Beta strand

78 – 86

9

Helix

91 – 98

8

Beta strand

103 – 110

8

Beta strand

113 – 119

7

Helix

122 – 125

4

Beta strand

127 – 134

8

Helix

137 – 143

7

Beta strand

148 – 153

6

Helix

155 – 160

6

Turn

161 – 165

5

Helix

166 – 169

4

Helix

174 – 180

7

Beta strand

183 – 185

3

Helix

186 – 188

3

Beta strand

190 – 193

4

Turn

196 – 198

3

Beta strand

200 – 204

5

Beta strand

217 – 224

8

Helix

230 – 232

3

Helix

235 – 237

3

Helix

238 – 256

19

Helix

260 – 262

3

Beta strand

263 – 270

8

Beta strand

272 – 275

4

Beta strand

277 – 282

6

Turn

292 – 294

3

Beta strand

295 – 297

3

Helix

298 – 307

10

Helix

311 – 314

4

Beta strand

317 – 322

6

Helix

326 – 333

8

Turn

334 – 336

3

Sequences

	Sequence		Length	Mass (Da)
	Q96C86 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: C9C5A33C212D7A52	FASTA	337	38,609
	10 20 30 40 50 60 MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ KVLRESARDK 70 80 90 100 110 120 IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP 130 140 150 160 170 180 PRQLNDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL 190 200 210 220 230 240 DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL 250 260 270 280 290 300 LRNILHQGQE AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE 310 320 330 VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a novel member of the histidine triad protein family (HINT-5) in different vertebrate species." Huang C.-H., Peng J., Chen H., Chen Y. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases." Liu H., Rodgers N.D., Jiao X., Kiledjian M. EMBO J. 21:4699-4708(2002) [PubMed: 12198172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, MUTAGENESIS OF HIS-277, SUBUNIT.
[3]	"Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1." Kwasnicka D.A., Krakowiak A., Thacker C., Brenner C., Vincent S.R. J. Biol. Chem. 278:39051-39058(2003) [PubMed: 12871939] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Placenta.
[4]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[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], VARIANT GLU-73. Tissue: Bone marrow.
[6]	Bienvenut W.V. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11; 129-138 AND 243-255, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[7]	"Functional link between the mammalian exosome and mRNA decapping." Wang Z., Kiledjian M. Cell 107:751-762(2001) [PubMed: 11747811] [Abstract] Cited for: FUNCTION, INTERACTION WITH EXOSOME PROTEINS.
[8]	"DcpS can act in the 5'-3' mRNA decay pathway in addition to the 3'-5' pathway." van Dijk E., Le Hir H., Seraphin B. Proc. Natl. Acad. Sci. U.S.A. 100:12081-12086(2003) [PubMed: 14523240] [Abstract] Cited for: FUNCTION.
[9]	"Functional analysis of mRNA scavenger decapping enzymes." Liu S.-W., Jiao X., Liu H., Gu M., Lima C.D., Kiledjian M. RNA 10:1412-1422(2004) [PubMed: 15273322] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138 AND LYS-142, MASS SPECTROMETRY.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity." Gu M., Fabrega C., Liu S.-W., Liu H., Kiledjian M., Lima C.D. Mol. Cell 14:67-80(2004) [PubMed: 15068804] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT ASN-277 IN COMPLEX WITH SUBSTRATE, SUBUNIT, MUTAGENESIS OF ARG-58; ILE-61; PHE-63; ILE-83; GLU-85; PHE-108; ASN-110; TYR-113; LYS-128; LYS-138; ARG-145; GLN-146; TRP-175; GLU-185; PRO-204; ASP-205; LEU-206; LYS-207; TYR-217; HIS-268; SER-272; HIS-277; HIS-279; ARG-294 AND ARG-322.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY040773, AY040772 Genomic DNA. Translation: AAK91763.1.
AY040771 mRNA. Translation: AAK91765.1.
AF532613 mRNA. Translation: AAM90310.1.
AY077684 mRNA. Translation: AAL77216.1.
AF077201 mRNA. Translation: AAD26996.1.
BC014532 mRNA. Translation: AAH14532.1.

IPI

IPI00335385.

RefSeq

NP_054745.1. NM_014026.3.

UniGene

Hs.504249.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ST0	X-ray	1.90	A/B	1-337	[»]
1ST4	X-ray	2.02	A/B	1-337	[»]
1XML	X-ray	2.00	A/B	1-337	[»]
1XMM	X-ray	2.50	A/B/C/D	1-337	[»]
3BL7	X-ray	2.31	A/B	38-337	[»]
3BL9	X-ray	1.80	A/B	38-337	[»]
3BLA	X-ray	2.60	A/B	38-337	[»]

ProteinModelPortal

Q96C86.

SMR

Q96C86. Positions 38-337.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96C86. 4 interactions.

STRING

Q96C86.

PTM databases

PhosphoSite

Q96C86.

Polymorphism databases

DMDM

116241325.

2D gel databases

REPRODUCTION-2DPAGE

IPI00335385.

Proteomic databases

PeptideAtlas

Q96C86.

PRIDE

Q96C86.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263579; ENSP00000263579; ENSG00000110063.

GeneID

28960.

KEGG

hsa:28960.

UCSC

uc001qdp.1. human.

Organism-specific databases

CTD

28960.

GeneCards

GC11P126173.

H-InvDB

HIX0010255.

HGNC

HGNC:29812. DCPS.

HPA

HPA039632.

MIM

610534. gene.

neXtProt

NX_Q96C86.

PharmGKB

PA134863866.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000003924.

HOGENOM

HBG714525.

HOVERGEN

HBG051322.

InParanoid

Q96C86.

OMA

FSGFRLQ.

OrthoDB

EOG48D0VP.

PhylomeDB

Q96C86.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q96C86.

Bgee

Q96C86.

CleanEx

HS_DCPS.

Genevestigator

Q96C86.

GermOnline

ENSG00000110063. Homo sapiens.

Family and domain databases

InterPro

IPR011146. His_triad-like_motif.
IPR019808. Histidine_triad_CS.
IPR008594. Scavenger_mRNA_decap_enz.
IPR011145. Scavenger_mRNA_decap_enz_N.
[Graphical view]

KO

K12584.

PANTHER

PTHR12978. DcpS. 1 hit.

Pfam

PF05652. DcpS. 1 hit.
[Graphical view]

PIRSF

PIRSF028973. Scavenger_mRNA_decap_enz. 1 hit.

SUPFAM

SSF54197. His_triad-like_motif. 1 hit.
SSF102860. Scavenger_mRNA_decap_enz_N. 1 hit.

PROSITE

PS00892. HIT_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

51799.

SOURCE

Search...

Entry information

Entry name

DCPS_HUMAN

Accession

Primary (citable) accession number: Q96C86
Secondary accession number(s): Q8NHL8, Q9Y2S5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 95 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.