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Q8IZD4

- DCP1B_HUMAN

UniProt

Q8IZD4 - DCP1B_HUMAN

Protein

mRNA-decapping enzyme 1B

Gene

DCP1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

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

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    mRNA-decapping enzyme 1B (EC:3.-.-.-)
    Gene namesi
    Name:DCP1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:24451. DCP1B.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. intracellular membrane-bounded organelle Source: HPA
    4. membrane Source: UniProtKB
    5. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134889143.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 617616mRNA-decapping enzyme 1BPRO_0000402799Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei191 – 1911Phosphotyrosine1 Publication
    Modified residuei448 – 4481Phosphoserine1 Publication
    Modified residuei511 – 5111Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8IZD4.
    PaxDbiQ8IZD4.
    PRIDEiQ8IZD4.

    PTM databases

    PhosphoSiteiQ8IZD4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IZD4.
    BgeeiQ8IZD4.
    CleanExiHS_DCP1B.
    GenevestigatoriQ8IZD4.

    Organism-specific databases

    HPAiHPA039709.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DCP2Q8IU603EBI-521595,EBI-521577
    EDC3Q96F863EBI-521595,EBI-997311

    Protein-protein interaction databases

    BioGridi128216. 16 interactions.
    DIPiDIP-31289N.
    IntActiQ8IZD4. 13 interactions.
    MINTiMINT-1190113.
    STRINGi9606.ENSP00000280665.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IZD4.
    SMRiQ8IZD4. Positions 13-134, 573-606.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi252 – 26110Poly-Gln

    Sequence similaritiesi

    Belongs to the DCP1 family.Curated

    Phylogenomic databases

    eggNOGiNOG314415.
    HOGENOMiHOG000090228.
    HOVERGENiHBG103159.
    InParanoidiQ8IZD4.
    KOiK12611.
    OMAiDEYTKCK.
    OrthoDBiEOG75QR3K.
    PhylomeDBiQ8IZD4.
    TreeFamiTF320504.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IZD4-1) [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

    MAAVAAGGLV GKGRDISLAA LQRHDPYINR IVDVASQVAL YTFGHRANEW    50
    EKTDVEGTLF VYTRSASPKH GFTIMNRLSM ENRTEPITKD LDFQLQDPFL 100
    LYRNARLSIY GIWFYDKEEC QRIAELMKNL TQYEQLKAHQ GTGAGISPVI 150
    LNSGEGKEVD ILRMLIKAKD EYTKCKTCSE PKKITSSSAI YDNPNLIKPI 200
    PVKPSENQQQ RIPQPNQTLD PEPQHLSLTA LFGKQDKATC QETVEPPQTL 250
    HQQQQQQQQQ QEKLPIRQGV VRSLSYEEPR RHSPPIEKQL CPAIQKLMVR 300
    SADLHPLSEL PENRPCENGS THSAGEFFTG PVQPGSPHNI GTSRGVQNAS 350
    RTQNLFEKLQ STPGAANKCD PSTPAPASSA ALNRSRAPTS VTPVAPGKGL 400
    AQPPQAYFNG SLPPQTVGHQ AHGREQSTLP RQTLPISGSQ TGSSGVISPQ 450
    ELLKKLQIVQ QEQQLHASNR PALAAKFPVL AQSSGTGKPL ESWINKTPNT 500
    EQQTPLFQVI SPQRIPATAA PSLLMSPMVF AQPTSVPPKE RESGLLPVGG 550
    QEPPAAATSL LLPIQSPEPS VITSSPLTKL QLQEALLYLI QNDDNFLNII 600
    YEAYLFSMTQ AAMKKTM 617
    Length:617
    Mass (Da):67,723
    Last modified:January 11, 2011 - v2
    Checksum:i00B9D9592BAC3B64
    GO
    Isoform 2 (identifier: Q8IZD4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-107: MAAVAAGGLV...PFLLYRNARL → MQIKV

    Note: No experimental confirmation available.

    Show »
    Length:515
    Mass (Da):56,273
    Checksum:i200E0AAD38984003
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511H → HQ in AAN62764. (PubMed:12417715)Curated
    Sequence conflicti251 – 2511H → HQ in BAB71118. (PubMed:14702039)Curated
    Sequence conflicti251 – 2511H → HQ in AAH15368. (PubMed:15489334)Curated
    Sequence conflicti251 – 2511H → HQ in AAH43437. (PubMed:15489334)Curated
    Sequence conflicti426 – 4261Q → R in BAB71118. (PubMed:14702039)Curated
    Sequence conflicti435 – 4351P → A in AAH43437. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti195 – 1951N → D.
    Corresponds to variant rs12423058 [ dbSNP | Ensembl ].
    VAR_047395
    Natural varianti216 – 2161N → S.
    Corresponds to variant rs34730825 [ dbSNP | Ensembl ].
    VAR_047396
    Natural varianti301 – 3011S → T.
    Corresponds to variant rs2470449 [ dbSNP | Ensembl ].
    VAR_047397
    Natural varianti344 – 3441R → H.
    Corresponds to variant rs715146 [ dbSNP | Ensembl ].
    VAR_047398

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 107107MAAVA…RNARL → MQIKV in isoform 2. 1 PublicationVSP_056044Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY146652 mRNA. Translation: AAN62764.1.
    AK056200 mRNA. Translation: BAB71118.1.
    AK299203 mRNA. Translation: BAG61243.1.
    AC005342 Genomic DNA. No translation available.
    BC015368 mRNA. Translation: AAH15368.2. Different initiation.
    BC043437 mRNA. Translation: AAH43437.1.
    CCDSiCCDS31727.1.
    RefSeqiNP_689853.3. NM_152640.3.
    XP_006719034.1. XM_006718971.1.
    XP_006719035.1. XM_006718972.1.
    UniGeneiHs.130934.

    Genome annotation databases

    EnsembliENST00000280665; ENSP00000280665; ENSG00000151065.
    ENST00000397173; ENSP00000380358; ENSG00000151065.
    GeneIDi196513.
    KEGGihsa:196513.
    UCSCiuc001qjx.1. human.

    Polymorphism databases

    DMDMi317373353.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY146652 mRNA. Translation: AAN62764.1 .
    AK056200 mRNA. Translation: BAB71118.1 .
    AK299203 mRNA. Translation: BAG61243.1 .
    AC005342 Genomic DNA. No translation available.
    BC015368 mRNA. Translation: AAH15368.2 . Different initiation.
    BC043437 mRNA. Translation: AAH43437.1 .
    CCDSi CCDS31727.1.
    RefSeqi NP_689853.3. NM_152640.3.
    XP_006719034.1. XM_006718971.1.
    XP_006719035.1. XM_006718972.1.
    UniGenei Hs.130934.

    3D structure databases

    ProteinModelPortali Q8IZD4.
    SMRi Q8IZD4. Positions 13-134, 573-606.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128216. 16 interactions.
    DIPi DIP-31289N.
    IntActi Q8IZD4. 13 interactions.
    MINTi MINT-1190113.
    STRINGi 9606.ENSP00000280665.

    PTM databases

    PhosphoSitei Q8IZD4.

    Polymorphism databases

    DMDMi 317373353.

    Proteomic databases

    MaxQBi Q8IZD4.
    PaxDbi Q8IZD4.
    PRIDEi Q8IZD4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280665 ; ENSP00000280665 ; ENSG00000151065 .
    ENST00000397173 ; ENSP00000380358 ; ENSG00000151065 .
    GeneIDi 196513.
    KEGGi hsa:196513.
    UCSCi uc001qjx.1. human.

    Organism-specific databases

    CTDi 196513.
    GeneCardsi GC12M002055.
    H-InvDB HIX0201841.
    HGNCi HGNC:24451. DCP1B.
    HPAi HPA039709.
    MIMi 609843. gene.
    neXtProti NX_Q8IZD4.
    PharmGKBi PA134889143.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314415.
    HOGENOMi HOG000090228.
    HOVERGENi HBG103159.
    InParanoidi Q8IZD4.
    KOi K12611.
    OMAi DEYTKCK.
    OrthoDBi EOG75QR3K.
    PhylomeDBi Q8IZD4.
    TreeFami TF320504.

    Enzyme and pathway databases

    Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.

    Miscellaneous databases

    GeneWikii DCP1B.
    GenomeRNAii 196513.
    NextBioi 89512.
    PROi Q8IZD4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IZD4.
    Bgeei Q8IZD4.
    CleanExi HS_DCP1B.
    Genevestigatori Q8IZD4.

    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] (ISOFORM 1), 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.
      , 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] (ISOFORMS 1 AND 2).
      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.
      , 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] (ISOFORM 1).
      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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDCP1B_HUMAN
    AccessioniPrimary (citable) accession number: Q8IZD4
    Secondary accession number(s): B4DRD1
    , Q86XH9, Q96BP8, Q96MZ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 104 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3