Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NPI6

- DCP1A_HUMAN

UniProt

Q9NPI6 - DCP1A_HUMAN

Protein

mRNA-decapping enzyme 1A

Gene

DCP1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1.2 Publications

    GO - Molecular functioni

    1. hydrolase activity Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
    6. RNA metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nonsense-mediated mRNA decay

    Enzyme and pathway databases

    ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Protein family/group databases

    TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    mRNA-decapping enzyme 1A (EC:3.-.-.-)
    Alternative name(s):
    Smad4-interacting transcriptional co-activator
    Transcription factor SMIF
    Gene namesi
    Name:DCP1A
    Synonyms:SMIF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:18714. DCP1A.

    Subcellular locationi

    CytoplasmP-body. Nucleus
    Note: Co-localizes with NANOS3 in the processing bodies By similarity. Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4.By similarity

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201D → A: Lowers decapping activity. 1 Publication
    Mutagenesisi59 – 591R → A: Lowers decapping activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134931379.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 582582mRNA-decapping enzyme 1APRO_0000189632Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei142 – 1421Phosphoserine1 Publication
    Modified residuei180 – 1801Phosphoserine1 Publication
    Modified residuei315 – 3151Phosphoserine6 Publications
    Modified residuei319 – 3191Phosphoserine3 Publications
    Modified residuei334 – 3341Phosphoserine2 Publications
    Modified residuei353 – 3531Phosphoserine4 Publications
    Modified residuei401 – 4011Phosphothreonine1 Publication
    Modified residuei422 – 4221Phosphoserine1 Publication
    Modified residuei522 – 5221Phosphoserine2 Publications
    Modified residuei523 – 5231Phosphoserine2 Publications
    Modified residuei525 – 5251Phosphoserine2 Publications
    Modified residuei531 – 5311Phosphothreonine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NPI6.
    PaxDbiQ9NPI6.
    PRIDEiQ9NPI6.

    PTM databases

    PhosphoSiteiQ9NPI6.

    Expressioni

    Tissue specificityi

    Detected in heart, brain, placenta, lung, skeletal muscle, liver, kidney and pancreas.1 Publication

    Gene expression databases

    CleanExiHS_DCP1A.
    GenevestigatoriQ9NPI6.

    Organism-specific databases

    HPAiHPA013202.

    Interactioni

    Subunit structurei

    Forms a complex with EDC3, DCP2, DDX6 and EDC4/HEDLS, within this complex directly interacts with EDC3. Binds DCP1B, UPF1 and SMAD4. Part of a cytoplasmic complex containing proteins involved in mRNA decay, including XRN1 and LSM1. Interacts with PNRC2. Interacts with DDX17 in an RNA-independent manner. Interacts with ZC3HAV1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-374238,EBI-374238
    BAG4O954293EBI-374238,EBI-2949658
    DCP2Q8IU607EBI-374238,EBI-521577
    DDX6P261965EBI-374238,EBI-351257
    UPF1Q9290013EBI-374238,EBI-373471
    ZFP36P266512EBI-374238,EBI-374248

    Protein-protein interaction databases

    BioGridi120914. 24 interactions.
    DIPiDIP-31292N.
    IntActiQ9NPI6. 16 interactions.
    MINTiMINT-5005647.
    STRINGi9606.ENSP00000294241.

    Structurei

    Secondary structure

    582
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 1919
    Beta strandi23 – 3917
    Turni40 – 434
    Beta strandi44 – 6320
    Beta strandi65 – 717
    Beta strandi78 – 814
    Beta strandi87 – 915
    Beta strandi94 – 985
    Beta strandi104 – 1118
    Helixi112 – 12615
    Helixi539 – 55719
    Helixi559 – 57113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WX3X-ray2.31A/B/C539-582[»]
    4B6HX-ray2.60A/B1-130[»]
    ProteinModelPortaliQ9NPI6.
    SMRiQ9NPI6. Positions 1-129, 539-582.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NPI6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DCP1 family.Curated

    Phylogenomic databases

    eggNOGiNOG314415.
    HOVERGENiHBG051320.
    InParanoidiQ9NPI6.
    KOiK12610.
    PhylomeDBiQ9NPI6.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR010334. DCP1.
    IPR011993. PH_like_dom.
    [Graphical view]
    PANTHERiPTHR16290. PTHR16290. 1 hit.
    PfamiPF06058. DCP1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NPI6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEALSRAGQE MSLAALKQHD PYITSIADLT GQVALYTFCP KANQWEKTDI    50
    EGTLFVYRRS ASPYHGFTIV NRLNMHNLVE PVNKDLEFQL HEPFLLYRNA 100
    SLSIYSIWFY DKNDCHRIAK LMADVVEEET RRSQQAARDK QSPSQANGCS 150
    DHRPIDILEM LSRAKDEYER NQMGDSNISS PGLQPSTQLS NLGSTETLEE 200
    MPSGSQDKSA PSGHKHLTVE ELFGTSLPKE QPAVVGLDSE EMERLPGDAS 250
    QKEPNSFLPF PFEQLGGAPQ SETLGVPSAA HHSVQPEITT PVLITPASIT 300
    QSNEKHAPTY TIPLSPVLSP TLPAEAPTAQ VPPSLPRNST MMQAVKTTPR 350
    QRSPLLNQPV PELSHASLIA NQSPFRAPLN VTNTAGTSLP SVDLLQKLRL 400
    TPQHDQIQTQ PLGKGAMVAS FSPAAGQLAT PESFIEPPSK TAAARVAASA 450
    SLSNMVLAPL QSMQQNQDPE VFVQPKVLSS AIQVAGAPLV TATTTAVSSV 500
    LLAPSVFQQT VTRSSDLERK ASSPSPLTIG TPESQRKPSI ILSKSQLQDT 550
    LIHLIKNDSS FLSTLHEVYL QVLTKNKDNH NL 582
    Length:582
    Mass (Da):63,309
    Last modified:May 18, 2010 - v2
    Checksum:iD218180ABA7FD768
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti483 – 4831Q → P in AAN62763. (PubMed:12417715)Curated
    Sequence conflicti483 – 4831Q → P in CAB77023. (PubMed:11836524)Curated
    Sequence conflicti483 – 4831Q → P in BAA92008. (PubMed:14702039)Curated
    Sequence conflicti483 – 4831Q → P in AAH07439. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY146651 mRNA. Translation: AAN62763.1.
    AJ275986 mRNA. Translation: CAB77023.1.
    AK001969 mRNA. Translation: BAA92008.1.
    AC097015 Genomic DNA. No translation available.
    AC112218 Genomic DNA. No translation available.
    BC007439 mRNA. Translation: AAH07439.1.
    RefSeqiNP_001277134.1. NM_001290205.1.
    NP_001277135.1. NM_001290206.1.
    NP_060873.4. NM_018403.6.
    UniGeneiHs.476353.

    Genome annotation databases

    EnsembliENST00000610213; ENSP00000476386; ENSG00000272886.
    GeneIDi55802.
    KEGGihsa:55802.
    UCSCiuc021wzi.1. human.

    Polymorphism databases

    DMDMi296434475.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY146651 mRNA. Translation: AAN62763.1 .
    AJ275986 mRNA. Translation: CAB77023.1 .
    AK001969 mRNA. Translation: BAA92008.1 .
    AC097015 Genomic DNA. No translation available.
    AC112218 Genomic DNA. No translation available.
    BC007439 mRNA. Translation: AAH07439.1 .
    RefSeqi NP_001277134.1. NM_001290205.1.
    NP_001277135.1. NM_001290206.1.
    NP_060873.4. NM_018403.6.
    UniGenei Hs.476353.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WX3 X-ray 2.31 A/B/C 539-582 [» ]
    4B6H X-ray 2.60 A/B 1-130 [» ]
    ProteinModelPortali Q9NPI6.
    SMRi Q9NPI6. Positions 1-129, 539-582.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120914. 24 interactions.
    DIPi DIP-31292N.
    IntActi Q9NPI6. 16 interactions.
    MINTi MINT-5005647.
    STRINGi 9606.ENSP00000294241.

    Protein family/group databases

    TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    PTM databases

    PhosphoSitei Q9NPI6.

    Polymorphism databases

    DMDMi 296434475.

    Proteomic databases

    MaxQBi Q9NPI6.
    PaxDbi Q9NPI6.
    PRIDEi Q9NPI6.

    Protocols and materials databases

    DNASUi 55802.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000610213 ; ENSP00000476386 ; ENSG00000272886 .
    GeneIDi 55802.
    KEGGi hsa:55802.
    UCSCi uc021wzi.1. human.

    Organism-specific databases

    CTDi 55802.
    GeneCardsi GC03M053319.
    HGNCi HGNC:18714. DCP1A.
    HPAi HPA013202.
    MIMi 607010. gene.
    neXtProti NX_Q9NPI6.
    PharmGKBi PA134931379.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314415.
    HOVERGENi HBG051320.
    InParanoidi Q9NPI6.
    KOi K12610.
    PhylomeDBi Q9NPI6.

    Enzyme and pathway databases

    Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.
    REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
    REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi DCP1A. human.
    EvolutionaryTracei Q9NPI6.
    GeneWikii DCP1A.
    GenomeRNAii 55802.
    NextBioi 60947.
    PROi Q9NPI6.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_DCP1A.
    Genevestigatori Q9NPI6.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR010334. DCP1.
    IPR011993. PH_like_dom.
    [Graphical view ]
    PANTHERi PTHR16290. PTHR16290. 1 hit.
    Pfami PF06058. DCP1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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], FUNCTION, MUTAGENESIS OF ASP-20 AND ARG-59, INTERACTION WITH DCP1B AND DCP2, SUBCELLULAR LOCATION.
    2. "SMIF, a Smad4-interacting protein that functions as a co-activator in TGFbeta signalling."
      Bai R.-Y., Koester C., Ouyang T., Hahn S.A., Hammerschmidt M., Peschel C., Duyster J.
      Nat. Cell Biol. 4:181-190(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SMAD4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Pancreas.
    3. "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].
      Tissue: Placenta.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [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].
      Tissue: Muscle.
    6. "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci."
      Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.
      RNA 8:1489-1501(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH A COMPLEX CONTAINING ENZYMES INVOLVED IN MRNA DECAY.
    7. "Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping."
      Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.
      Mol. Cell 20:905-915(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EDC3; DCP2; EDC4 AND DDX6, SUBCELLULAR LOCATION.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-334 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-315; SER-319; SER-334; SER-353; THR-401; SER-522; SER-523; SER-525 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Human proline-rich nuclear receptor coregulatory protein 2 mediates an interaction between mRNA surveillance machinery and decapping complex."
      Cho H., Kim K.M., Kim Y.K.
      Mol. Cell 33:75-86(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PNRC2.
    14. "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-180; SER-315; SER-319; SER-522; SER-523; SER-525 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-353 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
      Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZC3HAV1 AND DDX17.
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDCP1A_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 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 3
      Human chromosome 3: 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

    External Data

    Dasty 3