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Q8IZD4 (DCP1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
mRNA-decapping enzyme 1B

EC=3.-.-.-
Gene names
Name:DCP1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP By similarity.

Subunit structure

Binds DCP1A. Part of a complex containing enzymes involved in mRNA decay, including DCP2, LSM1, LSM3 and CNOT6.

Subcellular location

Cytoplasm. Nucleus By similarity Ref.5.

Sequence similarities

Belongs to the DCP1 family.

Sequence caution

The sequence AAH15368.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DCP2Q8IU603EBI-521595,EBI-521577

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 617616mRNA-decapping enzyme 1B
PRO_0000402799

Regions

Compositional bias252 – 26110Poly-Gln

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.11 Ref.12
Modified residue1911Phosphotyrosine Ref.6
Modified residue4481Phosphoserine Ref.8
Modified residue5111Phosphoserine Ref.8

Natural variations

Natural variant1951N → D.
Corresponds to variant rs12423058 [ dbSNP | Ensembl ].
VAR_047395
Natural variant2161N → S.
Corresponds to variant rs34730825 [ dbSNP | Ensembl ].
VAR_047396
Natural variant3011S → T.
Corresponds to variant rs2470449 [ dbSNP | Ensembl ].
VAR_047397
Natural variant3441R → H.
Corresponds to variant rs715146 [ dbSNP | Ensembl ].
VAR_047398

Experimental info

Sequence conflict2511H → HQ in AAN62764. Ref.1
Sequence conflict2511H → HQ in BAB71118. Ref.2
Sequence conflict2511H → HQ in AAH15368. Ref.4
Sequence conflict2511H → HQ in AAH43437. Ref.4
Sequence conflict4261Q → R in BAB71118. Ref.2
Sequence conflict4351P → A in AAH43437. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8IZD4 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 00B9D9592BAC3B64

FASTA61767,723
        10         20         30         40         50         60 
MAAVAAGGLV GKGRDISLAA LQRHDPYINR IVDVASQVAL YTFGHRANEW EKTDVEGTLF 

        70         80         90        100        110        120 
VYTRSASPKH GFTIMNRLSM ENRTEPITKD LDFQLQDPFL LYRNARLSIY GIWFYDKEEC 

       130        140        150        160        170        180 
QRIAELMKNL TQYEQLKAHQ GTGAGISPVI LNSGEGKEVD ILRMLIKAKD EYTKCKTCSE 

       190        200        210        220        230        240 
PKKITSSSAI YDNPNLIKPI PVKPSENQQQ RIPQPNQTLD PEPQHLSLTA LFGKQDKATC 

       250        260        270        280        290        300 
QETVEPPQTL HQQQQQQQQQ QEKLPIRQGV VRSLSYEEPR RHSPPIEKQL CPAIQKLMVR 

       310        320        330        340        350        360 
SADLHPLSEL PENRPCENGS THSAGEFFTG PVQPGSPHNI GTSRGVQNAS RTQNLFEKLQ 

       370        380        390        400        410        420 
STPGAANKCD PSTPAPASSA ALNRSRAPTS VTPVAPGKGL AQPPQAYFNG SLPPQTVGHQ 

       430        440        450        460        470        480 
AHGREQSTLP RQTLPISGSQ TGSSGVISPQ ELLKKLQIVQ QEQQLHASNR PALAAKFPVL 

       490        500        510        520        530        540 
AQSSGTGKPL ESWINKTPNT EQQTPLFQVI SPQRIPATAA PSLLMSPMVF AQPTSVPPKE 

       550        560        570        580        590        600 
RESGLLPVGG QEPPAAATSL LLPIQSPEPS VITSSPLTKL QLQEALLYLI QNDDNFLNII 

       610 
YEAYLFSMTQ AAMKKTM 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay."
Lykke-Andersen J.
Mol. Cell. Biol. 22:8114-8121(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DCP1A.
[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. expand/collapse author list , 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].
Tissue: Teratocarcinoma.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Testis and Uterus.
[5]"Cytoplasmic foci are sites of mRNA decay in human cells."
Cougot N., Babajko S., Seraphin B.
J. Cell Biol. 165:31-40(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DCP1A.
[6]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY146652 mRNA. Translation: AAN62764.1.
AK056200 mRNA. Translation: BAB71118.1.
AC005342 Genomic DNA. No translation available.
BC015368 mRNA. Translation: AAH15368.2. Different initiation.
BC043437 mRNA. Translation: AAH43437.1.
RefSeqNP_689853.3. NM_152640.3.
UniGeneHs.130934.

3D structure databases

ProteinModelPortalQ8IZD4.
SMRQ8IZD4. Positions 13-134, 574-611.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128216. 13 interactions.
DIPDIP-31289N.
IntActQ8IZD4. 8 interactions.
MINTMINT-1190113.
STRING9606.ENSP00000280665.

PTM databases

PhosphoSiteQ8IZD4.

Polymorphism databases

DMDM317373353.

Proteomic databases

PaxDbQ8IZD4.
PRIDEQ8IZD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000280665; ENSP00000280665; ENSG00000151065.
GeneID196513.
KEGGhsa:196513.
UCSCuc001qjx.1. human.

Organism-specific databases

CTD196513.
GeneCardsGC12M002055.
H-InvDBHIX0201841.
HGNCHGNC:24451. DCP1B.
HPAHPA039709.
MIM609843. gene.
neXtProtNX_Q8IZD4.
PharmGKBPA134889143.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314415.
HOGENOMHOG000090228.
HOVERGENHBG103159.
InParanoidQ8IZD4.
KOK12611.
OMADEYTKCK.
OrthoDBEOG75QR3K.
PhylomeDBQ8IZD4.
TreeFamTF320504.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ8IZD4.
BgeeQ8IZD4.
CleanExHS_DCP1B.
GenevestigatorQ8IZD4.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR010334. DCP1.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERPTHR16290. PTHR16290. 1 hit.
PfamPF06058. DCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDCP1B.
GenomeRNAi196513.
NextBio89512.
PROQ8IZD4.
SOURCESearch...

Entry information

Entry nameDCP1B_HUMAN
AccessionPrimary (citable) accession number: Q8IZD4
Secondary accession number(s): Q86XH9, Q96BP8, Q96MZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM