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)

Q6P2E9

- EDC4_HUMAN

UniProt

Q6P2E9 - EDC4_HUMAN

Protein

Enhancer of mRNA-decapping protein 4

Gene

EDC4

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 114 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro).1 Publication

    GO - Molecular functioni

    1. 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. RNA metabolic process Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enhancer of mRNA-decapping protein 4
    Alternative name(s):
    Autoantigen Ge-1
    Autoantigen RCD-8
    Human enhancer of decapping large subunit
    Short name:
    Hedls
    Gene namesi
    Name:EDC4
    Synonyms:HEDLS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:17157. EDC4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic mRNA processing body Source: MGI
    3. cytosol Source: Reactome
    4. intracellular membrane-bounded organelle Source: HPA
    5. membrane Source: UniProtKB
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA145148958.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 14011400Enhancer of mRNA-decapping protein 4PRO_0000278962Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei125 – 1251N6-acetyllysine1 Publication
    Modified residuei693 – 6931Phosphothreonine2 Publications
    Modified residuei723 – 7231Phosphoserine1 Publication
    Modified residuei725 – 7251Phosphoserine1 Publication
    Modified residuei729 – 7291Phosphoserine4 Publications
    Modified residuei741 – 7411Phosphoserine2 Publications
    Modified residuei821 – 8211Phosphothreonine1 Publication
    Modified residuei844 – 8441Phosphoserine2 Publications
    Modified residuei871 – 8711Phosphoserine2 Publications
    Modified residuei875 – 8751Phosphoserine1 Publication
    Modified residuei879 – 8791Phosphoserine3 Publications
    Modified residuei887 – 8871PhosphoserineBy similarity
    Modified residuei892 – 8921Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6P2E9.
    PaxDbiQ6P2E9.
    PRIDEiQ6P2E9.

    PTM databases

    PhosphoSiteiQ6P2E9.

    Miscellaneous databases

    PMAP-CutDBQ6P2E9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6P2E9.
    BgeeiQ6P2E9.
    CleanExiHS_EDC4.
    GenevestigatoriQ6P2E9.

    Organism-specific databases

    HPAiHPA041164.

    Interactioni

    Subunit structurei

    Part of a decapping complex consisting of DCP1A, DCP2, EDC3, EDC4 and probably DDX6. Part of a complex consisting of DCP1A, EDC3, EDC4 and DDX6. Part of a complex consisting of DCP1B, EDC3, EDC4 and DDX6. Interacts with DCP2. Interacts with RC3H1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COASYQ130573EBI-1006038,EBI-745967
    DCP2Q8IU604EBI-1006038,EBI-521577
    EIF2AK2P195252EBI-1006038,EBI-640775

    Protein-protein interaction databases

    BioGridi117171. 36 interactions.
    DIPiDIP-31192N.
    IntActiQ6P2E9. 23 interactions.
    MINTiMINT-5005241.
    STRINGi9606.ENSP00000351811.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6P2E9.
    SMRiQ6P2E9. Positions 298-325, 1268-1397.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati174 – 21441WD 1Add
    BLAST
    Repeati230 – 27748WD 2Add
    BLAST
    Repeati295 – 33440WD 3Add
    BLAST
    Repeati342 – 39352WD 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni913 – 93422Sufficient for nuclear localizationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili954 – 102572Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi602 – 67675Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat EDC4 family.Curated
    Contains 4 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, WD repeat

    Phylogenomic databases

    eggNOGiNOG270061.
    HOVERGENiHBG053855.
    InParanoidiQ6P2E9.
    KOiK12616.
    OMAiESPRNGL.
    OrthoDBiEOG72JWFV.
    PhylomeDBiQ6P2E9.
    TreeFamiTF350715.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    SMARTiSM00320. WD40. 3 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 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: Q6P2E9-1) [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

    MASCASIDIE DATQHLRDIL KLDRPAGGPS AESPRPSSAY NGDLNGLLVP     50
    DPLCSGDSTS ANKTGLRTMP PINLQEKQVI CLSGDDSSTC IGILAKEVEI 100
    VASSDSSISS KARGSNKVKI QPVAKYDWEQ KYYYGNLIAV SNSFLAYAIR 150
    AANNGSAMVR VISVSTSERT LLKGFTGSVA DLAFAHLNSP QLACLDEAGN 200
    LFVWRLALVN GKIQEEILVH IRQPEGTPLN HFRRIIWCPF IPEESEDCCE 250
    ESSPTVALLH EDRAEVWDLD MLRSSHSTWP VDVSQIKQGF IVVKGHSTCL 300
    SEGALSPDGT VLATASHDGY VKFWQIYIEG QDEPRCLHEW KPHDGRPLSC 350
    LLFCDNHKKQ DPDVPFWRFL ITGADQNREL KMWCTVSWTC LQTIRFSPDI 400
    FSSVSVPPSL KVCLDLSAEY LILSDVQRKV LYVMELLQNQ EEGHACFSSI 450
    SEFLLTHPVL SFGIQVVSRC RLRHTEVLPA EEENDSLGAD GTHGAGAMES 500
    AAGVLIKLFC VHTKALQDVQ IRFQPQLNPD VVAPLPTHTA HEDFTFGESR 550
    PELGSEGLGS AAHGSQPDLR RIVELPAPAD FLSLSSETKP KLMTPDAFMT 600
    PSASLQQITA SPSSSSSGSS SSSSSSSSSL TAVSAMSSTS AVDPSLTRPP 650
    EELTLSPKLQ LDGSLTMSSS GSLQASPRGL LPGLLPAPAD KLTPKGPGQV 700
    PTATSALSLE LQEVEPLGLP QASPSRTRSP DVISSASTAL SQDIPEIASE 750
    ALSRGFGSSA PEGLEPDSMA SAASALHLLS PRPRPGPELG PQLGLDGGPG 800
    DGDRHNTPSL LEAALTQEAS TPDSQVWPTA PDITRETCST LAESPRNGLQ 850
    EKHKSLAFHR PPYHLLQQRD SQDASAEQSD HDDEVASLAS ASGGFGTKVP 900
    APRLPAKDWK TKGSPRTSPK LKRKSKKDDG DAAMGSRLTE HQVAEPPEDW 950
    PALIWQQQRE LAELRHSQEE LLQRLCTQLE GLQSTVTGHV ERALETRHEQ 1000
    EQRRLERALA EGQQRGGQLQ EQLTQQLSQA LSSAVAGRLE RSIRDEIKKT 1050
    VPPCVSRSLE PMAGQLSNSV ATKLTAVEGS MKENISKLLK SKNLTDAIAR 1100
    AAADTLQGPM QAAYREAFQS VVLPAFEKSC QAMFQQINDS FRLGTQEYLQ 1150
    QLESHMKSRK AREQEAREPV LAQLRGLVST LQSATEQMAA TVAGSVRAEV 1200
    QHQLHVAVGS LQESILAQVQ RIVKGEVSVA LKEQQAAVTS SIMQAMRSAA 1250
    GTPVPSAHLD CQAQQAHILQ LLQQGHLNQA FQQALTAADL NLVLYVCETV 1300
    DPAQVFGQPP CPLSQPVLLS LIQQLASDLG TRTDLKLSYL EEAVMHLDHS 1350
    DPITRDHMGS VMAQVRQKLF QFLQAEPHNS LGKAARRLSL MLHGLVTPSL 1400
    P 1401
    Length:1,401
    Mass (Da):151,661
    Last modified:July 5, 2004 - v1
    Checksum:i0790BB8ADF488356
    GO
    Isoform 2 (identifier: Q6P2E9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-381: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,020
    Mass (Da):109,728
    Checksum:i45357808C08C8555
    GO

    Sequence cautioni

    The sequence AAA21833.1 differs from that shown. Reason: Frameshift at position 1189.
    The sequence AAB51444.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH53598.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti271 – 2722ML → IV in AAA21833. (PubMed:7520377)Curated
    Sequence conflicti621 – 6211S → N in AAB51444. (PubMed:9067524)Curated
    Sequence conflicti1018 – 10192QL → HW in AAA21833. (PubMed:7520377)Curated
    Sequence conflicti1160 – 11612KA → NG in AAA21833. (PubMed:7520377)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 381381Missing in isoform 2. 1 PublicationVSP_023412Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26339 mRNA. Translation: AAA21833.1. Frameshift.
    AK128582 mRNA. No translation available.
    AK291049 mRNA. Translation: BAF83738.1.
    AC040162 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83183.1.
    BC043616 mRNA. Translation: AAH43616.1.
    BC053598 mRNA. Translation: AAH53598.1. Different initiation.
    BC064567 mRNA. Translation: AAH64567.1.
    U17474 mRNA. Translation: AAB51444.1. Different initiation.
    CCDSiCCDS10849.1. [Q6P2E9-1]
    PIRiI52882.
    RefSeqiNP_055144.3. NM_014329.4. [Q6P2E9-1]
    UniGeneiHs.75682.

    Genome annotation databases

    EnsembliENST00000358933; ENSP00000351811; ENSG00000038358. [Q6P2E9-1]
    GeneIDi23644.
    KEGGihsa:23644.
    UCSCiuc002eur.3. human. [Q6P2E9-1]

    Polymorphism databases

    DMDMi74758241.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26339 mRNA. Translation: AAA21833.1 . Frameshift.
    AK128582 mRNA. No translation available.
    AK291049 mRNA. Translation: BAF83738.1 .
    AC040162 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83183.1 .
    BC043616 mRNA. Translation: AAH43616.1 .
    BC053598 mRNA. Translation: AAH53598.1 . Different initiation.
    BC064567 mRNA. Translation: AAH64567.1 .
    U17474 mRNA. Translation: AAB51444.1 . Different initiation.
    CCDSi CCDS10849.1. [Q6P2E9-1 ]
    PIRi I52882.
    RefSeqi NP_055144.3. NM_014329.4. [Q6P2E9-1 ]
    UniGenei Hs.75682.

    3D structure databases

    ProteinModelPortali Q6P2E9.
    SMRi Q6P2E9. Positions 298-325, 1268-1397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117171. 36 interactions.
    DIPi DIP-31192N.
    IntActi Q6P2E9. 23 interactions.
    MINTi MINT-5005241.
    STRINGi 9606.ENSP00000351811.

    PTM databases

    PhosphoSitei Q6P2E9.

    Polymorphism databases

    DMDMi 74758241.

    Proteomic databases

    MaxQBi Q6P2E9.
    PaxDbi Q6P2E9.
    PRIDEi Q6P2E9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358933 ; ENSP00000351811 ; ENSG00000038358 . [Q6P2E9-1 ]
    GeneIDi 23644.
    KEGGi hsa:23644.
    UCSCi uc002eur.3. human. [Q6P2E9-1 ]

    Organism-specific databases

    CTDi 23644.
    GeneCardsi GC16P067906.
    HGNCi HGNC:17157. EDC4.
    HPAi HPA041164.
    MIMi 606030. gene.
    neXtProti NX_Q6P2E9.
    PharmGKBi PA145148958.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270061.
    HOVERGENi HBG053855.
    InParanoidi Q6P2E9.
    KOi K12616.
    OMAi ESPRNGL.
    OrthoDBi EOG72JWFV.
    PhylomeDBi Q6P2E9.
    TreeFami TF350715.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GenomeRNAii 23644.
    NextBioi 46453.
    PMAP-CutDB Q6P2E9.
    PROi Q6P2E9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6P2E9.
    Bgeei Q6P2E9.
    CleanExi HS_EDC4.
    Genevestigatori Q6P2E9.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    SMARTi SM00320. WD40. 3 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The immunoreactive region in a novel autoantigen contains a nuclear localization sequence."
      Bloch D.B., Rabkina D., Quertermous T., Bloch K.D.
      Clin. Immunol. Immunopathol. 72:380-389(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    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: Trachea.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] (ISOFORM 1).
      Tissue: Duodenum, Skin and Testis.
    6. "Cytoplasmic detection of a novel protein containing a nuclear localization sequence by human autoantibodies."
      Garcia-Lozano J.R., Gonzalez-Escribano M.F., Wichmann I., Nunez-Roldan A.
      Clin. Exp. Immunol. 107:501-506(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 421-1401 (ISOFORMS 1/2), SUBCELLULAR LOCATION.
    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 DCP1A; DCP1B; DCP2; DDX6 AND EDC3, SUBCELLULAR LOCATION, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. "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-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    14. "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-729 AND SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723; SER-725; THR-821; SER-844; SER-871 AND SER-879, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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].
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-879, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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 THR-693; SER-729; SER-741; SER-875; SER-879 AND SER-892, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "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-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiEDC4_HUMAN
    AccessioniPrimary (citable) accession number: Q6P2E9
    Secondary accession number(s): A6NGM1
    , A8K4T4, Q13025, Q13826, Q6ZR12, Q7Z6H7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 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 16
      Human chromosome 16: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3