Q96C86 (DCPS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
m7GpppX diphosphatase
EC=3.6.1.59

Alternative name(s):
DCS-1
Decapping scavenger enzyme
Hint-related 7meGMP-directed hydrolase
Histidine triad nucleotide-binding protein 5
Histidine triad protein member 5
Short name=HINT-5
Scavenger mRNA-decapping enzyme DcpS

Gene names

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP (Ref.16). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP (Ref.8). Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death. Ref.2 Ref.3 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.16 Ref.18
Catalytic activity	M7G5'ppp5'N(3'ppp5'N)(n) + H2O = 7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)(n). Ref.9 Ref.10 Ref.16 Ref.19 7-methylguanosine 5'-diphosphate + H2O = 7-methylguanosine 5'-phosphate + phosphate. Ref.9 Ref.10 Ref.16 Ref.19
Enzyme regulation	The hydrolytic product 7-methylguanosine diphosphate (m7GDP) efficiently inhibits the decapping scavenger activity and acts as a competitive inhibitor in vitro. Inhibited by 2,4-diaminoquinazoline. Ref.16 Ref.19
Subunit structure	Homodimer. Associates with components of the exosome multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts with NDOR1. Ref.2 Ref.7 Ref.11 Ref.17 Ref.18
Subcellular location	Cytoplasm. Nucleus. Note: Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner. Ref.3 Ref.9 Ref.12
Tissue specificity	Detected in liver, brain, kidney, testis and prostate. Ref.3
Induction	Up-regulated by menadione. Up-regulated by the transcription factor LTF isoform delta-lactoferrin (at protein level). Ref.11 Ref.13 Ref.16 Ref.19
Domain	The C-terminal histidine triad (HIT) motif and the N-terminal domain are required for the decapping activity. The N-terminus is necessary but not sufficient for binding cap structures. Ref.9
Sequence similarities	Belongs to the HIT family.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
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	cellular response to menadione Inferred from direct assay Ref.11. Source: UniProtKB 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 mRNA cis splicing, via spliceosome Inferred from direct assay Ref.12. Source: UniProtKB negative regulation of programmed cell death Inferred from direct assay Ref.11. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.3PubMed 18441014. Source: UniProtKB
Molecular_function	RNA 7-methylguanosine cap binding Inferred from direct assay Ref.2Ref.10Ref.12PubMed 18441014Ref.16. Source: UniProtKB m7G(5')pppN diphosphatase activity Inferred from direct assay Ref.2Ref.10Ref.12PubMed 18441014Ref.19Ref.16. 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

m7GpppX diphosphatase

PRO_0000109794

Regions

Region

268 – 279

12

Substrate binding

Motif

10 – 13

4

nuclear localization signal (NLS)

Motif

142 – 154

13

nuclear export sequence (NES)

Motif

275 – 279

5

Histidine triad motif

Sites

Active site

277

1

Nucleophile

Binding site

175

1

Substrate

Binding site

185

1

Substrate

Binding site

205

1

Substrate

Binding site

207

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

138

1

N6-acetyllysine Ref.14

Modified residue

142

1

N6-acetyllysine Ref.14

Natural variations

Natural variant

73

1

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

VAR_027958

Experimental info

Mutagenesis

10 – 13

4

Missing: Increases cytoplasmic localization. Ref.12

Mutagenesis

58

1

R → A: Increases decapping activity to 125% of wild-type. Ref.17

Mutagenesis

61

1

I → A: No effect. Ref.17

Mutagenesis

63

1

F → A: No effect. Ref.17

Mutagenesis

83

1

I → A: Strongly reduces decapping activity. Ref.17

Mutagenesis

85

1

E → A: Reduces decapping activity. Ref.17

Mutagenesis

108

1

F → A: Reduces decapping activity. Ref.17

Mutagenesis

110

1

N → A: Loss of decapping activity. Ref.17

Mutagenesis

113

1

Y → A: Loss of decapping activity. Ref.17

Mutagenesis

128

1

K → A: No effect. Ref.17

Mutagenesis

138

1

K → D: Increases decapping activity to 250% of wild-type. Ref.17

Mutagenesis

145

1

R → A: Increases decapping activity to 180% of wild-type. Ref.17

Mutagenesis

146

1

Q → P: Increases decapping activity to 140% of wild-type. Ref.17

Mutagenesis

148

1

L → A: Inhibits nuclear export to the cytoplasm. Ref.12

Mutagenesis

150

1

L → A: Inhibits nuclear export to the cytoplasm. Ref.12

Mutagenesis

175

1

W → A: Loss of decapping activity. Ref.17

Mutagenesis

185

1

E → A: Loss of decapping activity. Ref.17

Mutagenesis

204

1

P → A: Reduces decapping activity. Ref.17

Mutagenesis

205

1

D → A: Reduces decapping activity. Ref.17

Mutagenesis

206

1

L → A: No effect. Ref.17

Mutagenesis

207

1

K → A: Reduces decapping activity. Ref.17

Mutagenesis

207

1

K → R: No effect. Ref.17

Mutagenesis

217

1

Y → A: No effect. Ref.17

Mutagenesis

217

1

Y → F: Reduces decapping activity. Ref.17

Mutagenesis

268

1

H → N: Loss of decapping activity. Ref.17

Mutagenesis

272

1

S → A: No effect. Ref.17

Mutagenesis

273

1

Y → A: Reduces decapping activity. Ref.18

Mutagenesis

273

1

Y → F: Activates decapping activity to 120% of wild-type. Ref.18

Mutagenesis

277

1

H → N: Loss of decapping activity. Does not inhibit cap structure and capped RNA binding. Preferentially hydrolyzes cap structure (m7GpppG) at least 2500-fold more efficiently than capped RNA (m7Gppp-RNA). Ref.2 Ref.9 Ref.17

Mutagenesis

279

1

H → N: Loss of decapping activity. Ref.17

Mutagenesis

294

1

R → A or K: No effect. Ref.17

Mutagenesis

322

1

R → A: No effect. Ref.17

Sequence conflict

69

1

N → K in AAK91763. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

337

Helix Strand Turn

Details...

Beta strand

43 – 45

3

Beta strand

48 – 56

9

Turn

57 – 60

4

Beta strand

61 – 67

7

Beta strand

79 – 86

8

Helix

91 – 98

8

Beta strand

103 – 110

8

Beta strand

113 – 119

7

Helix

122 – 124

3

Beta strand

127 – 132

6

Helix

137 – 143

7

Beta strand

148 – 153

6

Helix

155 – 160

6

Helix

162 – 167

6

Helix

174 – 180

7

Beta strand

183 – 185

3

Helix

186 – 188

3

Beta strand

191 – 193

3

Turn

196 – 198

3

Beta strand

200 – 204

5

Helix

213 – 215

3

Beta strand

217 – 225

9

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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-277.
[10]	"Nematode m7GpppG and m3(2,2,7)GpppG decapping: activities in Ascaris embryos and characterization of C. elegans scavenger DcpS." Cohen L.S., Mikhli C., Friedman C., Jankowska-Anyszka M., Stepinski J., Darzynkiewicz E., Davis R.E. RNA 10:1609-1624(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
[11]	"Role of a novel dual flavin reductase (NR1) and an associated histidine triad protein (DCS-1) in menadione-induced cytotoxicity." Kwasnicka-Crawford D.A., Vincent S.R. Biochem. Biophys. Res. Commun. 336:565-571(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CYTOTOXICITY INHIBITION, INDUCTION, INTERACTION WITH NDOR1.
[12]	"DcpS scavenger decapping enzyme can modulate pre-mRNA splicing." Shen V., Liu H., Liu S.W., Jiao X., Kiledjian M. RNA 14:1132-1142(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN SPLICING, MUTAGENESIS OF 10-LYS--ARG-13; LEU-148 AND LEU-150, SUBCELLULAR LOCATION.
[13]	"Proteomic approach to the identification of novel delta-lactoferrin target genes: Characterization of DcpS, an mRNA scavenger decapping enzyme." Mariller C., Hardiville S., Hoedt E., Benaissa M., Mazurier J., Pierce A. Biochimie 91:109-122(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138 AND LYS-142, MASS SPECTROMETRY.
[15]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"7-Methylguanosine diphosphate (m(7)GDP) is not hydrolyzed but strongly bound by decapping scavenger (dcpS) enzymes and potently inhibits their activity." Wypijewska A., Bojarska E., Lukaszewicz M., Stepinski J., Jemielity J., Davis R.E., Darzynkiewicz E. Biochemistry 51:8003-8013(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
[17]	"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] [Europe PMC] [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.
[18]	"Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping." Chen N., Walsh M.A., Liu Y., Parker R., Song H. J. Mol. Biol. 347:707-718(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION, SUBUNIT, MUTAGENESIS OF TYR-273.
[19]	"DcpS as a therapeutic target for spinal muscular atrophy." Singh J., Salcius M., Liu S.W., Staker B.L., Mishra R., Thurmond J., Michaud G., Mattoon D.R., Printen J., Christensen J., Bjornsson J.M., Pollok B.A., Kiledjian M., Stewart L., Jarecki J., Gurney M.E. ACS Chem. Biol. 3:711-722(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-337 IN COMPLEX WITH SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AH010984 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.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96C86. 4 interactions.

STRING

9606.ENSP00000263579.

PTM databases

PhosphoSite

Q96C86.

Polymorphism databases

DMDM

116241325.

2D gel databases

REPRODUCTION-2DPAGE

IPI00335385.

Proteomic databases

PaxDb

Q96C86.

PeptideAtlas

Q96C86.

PRIDE

Q96C86.

Protocols and materials databases

DNASU

28960.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263579; ENSP00000263579; ENSG00000110063.

GeneID

28960.

KEGG

hsa:28960.

UCSC

uc001qdp.3. human.

Organism-specific databases

CTD

28960.

GeneCards

GC11P126173.

HGNC

HGNC:29812. DCPS.

HPA

HPA039632.

MIM

610534. gene.

neXtProt

NX_Q96C86.

PharmGKB

PA134863866.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5075.

HOGENOM

HOG000182411.

HOVERGEN

HBG051322.

InParanoid

Q96C86.

KO

K12584.

OMA

GADSSHK.

OrthoDB

EOG48D0VP.

PhylomeDB

Q96C86.

Enzyme and pathway databases

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

Bgee

Q96C86.

CleanEx

HS_DCPS.

Genevestigator

Q96C86.

GermOnline

ENSG00000110063. Homo sapiens.

Family and domain databases

Gene3D

3.30.428.10. 1 hit.

InterPro

IPR008594. DcpS/DCS2.
IPR019808. Histidine_triad_CS.
IPR011146. HIT-like.
IPR011145. Scavenger_mRNA_decap_enz_N.
[Graphical view]

PANTHER

PTHR12978. PTHR12978. 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

BindingDB

Q96C86.

ChEMBL

CHEMBL1949488.

ChiTaRS

DCPS. human.

EvolutionaryTrace

Q96C86.

GenomeRNAi

28960.

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:	May 1, 2013
This is version 110 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.