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O60244

- MED14_HUMAN

UniProt

O60244 - MED14_HUMAN

Protein

Mediator of RNA polymerase II transcription subunit 14

Gene

MED14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.3 Publications

    GO - Molecular functioni

    1. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    2. receptor activity Source: UniProtKB
    3. RNA polymerase II transcription cofactor activity Source: UniProtKB
    4. thyroid hormone receptor binding Source: UniProtKB
    5. transcription coactivator activity Source: MGI
    6. transcription cofactor activity Source: UniProtKB
    7. vitamin D receptor binding Source: UniProtKB

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. gene expression Source: Reactome
    3. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
    4. positive regulation of transcription, DNA-templated Source: UniProtKB
    5. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    6. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    7. stem cell maintenance Source: Ensembl
    8. transcription initiation from RNA polymerase II promoter Source: UniProtKB

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_12627. Generic Transcription Pathway.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinkiO60244.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mediator of RNA polymerase II transcription subunit 14
    Alternative name(s):
    Activator-recruited cofactor 150 kDa component
    Short name:
    ARC150
    Cofactor required for Sp1 transcriptional activation subunit 2
    Short name:
    CRSP complex subunit 2
    Mediator complex subunit 14
    RGR1 homolog
    Short name:
    hRGR1
    Thyroid hormone receptor-associated protein complex 170 kDa component
    Short name:
    Trap170
    Transcriptional coactivator CRSP150
    Vitamin D3 receptor-interacting protein complex 150 kDa component
    Short name:
    DRIP150
    Gene namesi
    Name:MED14
    Synonyms:ARC150, CRSP2, CXorf4, DRIP150, EXLM1, RGR1, TRAP170
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2370. MED14.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. mediator complex Source: UniProtKB
    2. membrane Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26890.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14541454Mediator of RNA polymerase II transcription subunit 14PRO_0000079357Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei617 – 6171Phosphoserine2 Publications
    Modified residuei986 – 9861Phosphoserine1 Publication
    Modified residuei1112 – 11121Phosphoserine2 Publications
    Modified residuei1119 – 11191Phosphoserine1 Publication
    Modified residuei1128 – 11281Phosphoserine3 Publications
    Modified residuei1136 – 11361Phosphoserine3 Publications
    Modified residuei1144 – 11441Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO60244.
    PaxDbiO60244.
    PRIDEiO60244.

    PTM databases

    PhosphoSiteiO60244.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiO60244.
    BgeeiO60244.
    CleanExiHS_MED14.
    GenevestigatoriO60244.

    Interactioni

    Subunit structurei

    Interacts with GATA1 By similarity. Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with AR, ESR1, SREBF1 and STAT2.By similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005191EBI-394489,EBI-375543
    FYNP062411EBI-394489,EBI-515315
    GRB2P629931EBI-394489,EBI-401755
    NCK1P163331EBI-394489,EBI-389883

    Protein-protein interaction databases

    BioGridi114699. 56 interactions.
    DIPiDIP-31460N.
    IntActiO60244. 19 interactions.
    MINTiMINT-2796527.
    STRINGi9606.ENSP00000323720.

    Structurei

    3D structure databases

    ProteinModelPortaliO60244.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni188 – 566379Interaction with STAT2Add
    BLAST
    Regioni500 – 824325Interaction with SREBF1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi69 – 735LXXLL motif 1
    Motifi1182 – 11865LXXLL motif 2

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1002 – 1165164Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Mediator complex subunit 14 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG281210.
    HOGENOMiHOG000045361.
    HOVERGENiHBG104308.
    InParanoidiO60244.
    KOiK15156.
    OMAiKPLQISH.
    OrthoDBiEOG7SR4KK.
    PhylomeDBiO60244.
    TreeFamiTF314388.

    Family and domain databases

    InterProiIPR013947. Mediator_Med14.
    [Graphical view]
    PfamiPF08638. Med14. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O60244-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPVQLENHQ LVPPGGGGGG SGGPPSAPAP PPPGAAVAAA AAAAASPGYR     50
    LSTLIEFLLH RAYSELMVLT DLLPRKSDVE RKIEIVQFAS RTRQLFVRLL 100
    ALVKWANNAG KVEKCAMISS FLDQQAILFV DTADRLASLA RDALVHARLP 150
    SFAIPYAIDV LTTGSYPRLP TCIRDKIIPP DPITKIEKQA TLHQLNQILR 200
    HRLVTTDLPP QLANLTVANG RVKFRVEGEF EATLTVMGDD PDVPWRLLKL 250
    EILVEDKETG DGRALVHSMQ ISFIHQLVQS RLFADEKPLQ DMYNCLHSFC 300
    LSLQLEVLHS QTLMLIRERW GDLVQVERYH AGKCLSLSVW NQQVLGRKTG 350
    TASVHKVTIK IDENDVSKPL QIFHDPPLPA SDSKLVERAM KIDHLSIEKL 400
    LIDSVHARAH QKLQELKAIL RGFNANENSS IETALPALVV PILEPCGNSE 450
    CLHIFVDLHS GMFQLMLYGL DQATLDDMEK SVNDDMKRII PWIQQLKFWL 500
    GQQRCKQSIK HLPTISSETL QLSNYSTHPI GNLSKNKLFI KLTRLPQYYI 550
    VVEMLEVPNK PTQLSYKYYF MSVNAADRED SPAMALLLQQ FKENIQDLVF 600
    RTKTGKQTRT NAKRKLSDDP CPVESKKTKR AGEMCAFNKV LAHFVAMCDT 650
    NMPFVGLRLE LSNLEIPHQG VQVEGDGFSH AIRLLKIPPC KGITEETQKA 700
    LDRSLLDCTF RLQGRNNRTW VAELVFANCP LNGTSTREQG PSRHVYLTYE 750
    NLLSEPVGGR KVVEMFLNDW NSIARLYECV LEFARSLPDI PAHLNIFSEV 800
    RVYNYRKLIL CYGTTKGSSI SIQWNSIHQK FHISLGTVGP NSGCSNCHNT 850
    ILHQLQEMFN KTPNVVQLLQ VLFDTQAPLN AINKLPTVPM LGLTQRTNTA 900
    YQCFSILPQS STHIRLAFRN MYCIDIYCRS RGVVAIRDGA YSLFDNSKLV 950
    EGFYPAPGLK TFLNMFVDSN QDARRRSVNE DDNPPSPIGG DMMDSLISQL 1000
    QPPPQQQPFP KQPGTSGAYP LTSPPTSYHS TVNQSPSMMH TQSPGNLHAA 1050
    SSPSGALRAP SPASFVPTPP PSSHGISIGP GASFASPHGT LDPSSPYTMV 1100
    SPSGRAGNWP GSPQVSGPSP AARMPGMSPA NPSLHSPVPD ASHSPRAGTS 1150
    SQTMPTNMPP PRKLPQRSWA ASIPTILTHS ALNILLLPSP TPGLVPGLAG 1200
    SYLCSPLERF LGSVIMRRHL QRIIQQETLQ LINSNEPGVI MFKTDALKCR 1250
    VALSPKTNQT LQLKVTPENA GQWKPDELQV LEKFFETRVA GPPFKANTLI 1300
    AFTKLLGAPT HILRDCVHIM KLELFPDQAT QLKWNVQFCL TIPPSAPPIA 1350
    PPGTPAVVLK SKMLFFLQLT QKTSVPPQEP VSIIVPIIYD MASGTTQQAD 1400
    IPRQQNSSVA APMMVSNILK RFAEMNPPRQ GECTIFAAVR DLMANLTLPP 1450
    GGRP 1454
    Length:1,454
    Mass (Da):160,607
    Last modified:April 17, 2007 - v2
    Checksum:i144308E3F08D3D9B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti309 – 3102HS → LT in AAD24360. (PubMed:10024883)Curated
    Sequence conflicti1265 – 12651V → L in BAA28626. (PubMed:9598311)Curated
    Sequence conflicti1265 – 12651V → L in AAD12725. (PubMed:9989412)Curated
    Sequence conflicti1265 – 12651V → L in AAG22547. (PubMed:10235266)Curated
    Sequence conflicti1451 – 14511G → V in BAA28626. (PubMed:9598311)Curated
    Sequence conflicti1451 – 14511G → V in AAD12725. (PubMed:9989412)Curated
    Sequence conflicti1451 – 14511G → V in AAG22547. (PubMed:10235266)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1325 – 13251F → L in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036608

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006651 mRNA. Translation: BAA28626.1.
    AB006652 Genomic DNA. Translation: BAA28627.1.
    AF104256 mRNA. Translation: AAD12725.1.
    AF304448 mRNA. Translation: AAG22547.1.
    AF135802 mRNA. Translation: AAD24360.1.
    BC098377 mRNA. Translation: AAH98377.1.
    BC132672 mRNA. Translation: AAI32673.1.
    BC132674 mRNA. Translation: AAI32675.1.
    CCDSiCCDS14254.1.
    RefSeqiNP_004220.2. NM_004229.3.
    UniGeneiHs.407604.

    Genome annotation databases

    EnsembliENST00000324817; ENSP00000323720; ENSG00000180182.
    GeneIDi9282.
    KEGGihsa:9282.
    UCSCiuc004dex.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006651 mRNA. Translation: BAA28626.1 .
    AB006652 Genomic DNA. Translation: BAA28627.1 .
    AF104256 mRNA. Translation: AAD12725.1 .
    AF304448 mRNA. Translation: AAG22547.1 .
    AF135802 mRNA. Translation: AAD24360.1 .
    BC098377 mRNA. Translation: AAH98377.1 .
    BC132672 mRNA. Translation: AAI32673.1 .
    BC132674 mRNA. Translation: AAI32675.1 .
    CCDSi CCDS14254.1.
    RefSeqi NP_004220.2. NM_004229.3.
    UniGenei Hs.407604.

    3D structure databases

    ProteinModelPortali O60244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114699. 56 interactions.
    DIPi DIP-31460N.
    IntActi O60244. 19 interactions.
    MINTi MINT-2796527.
    STRINGi 9606.ENSP00000323720.

    PTM databases

    PhosphoSitei O60244.

    Proteomic databases

    MaxQBi O60244.
    PaxDbi O60244.
    PRIDEi O60244.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324817 ; ENSP00000323720 ; ENSG00000180182 .
    GeneIDi 9282.
    KEGGi hsa:9282.
    UCSCi uc004dex.4. human.

    Organism-specific databases

    CTDi 9282.
    GeneCardsi GC0XM040507.
    HGNCi HGNC:2370. MED14.
    MIMi 300182. gene.
    neXtProti NX_O60244.
    PharmGKBi PA26890.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG281210.
    HOGENOMi HOG000045361.
    HOVERGENi HBG104308.
    InParanoidi O60244.
    KOi K15156.
    OMAi KPLQISH.
    OrthoDBi EOG7SR4KK.
    PhylomeDBi O60244.
    TreeFami TF314388.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_12627. Generic Transcription Pathway.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki O60244.

    Miscellaneous databases

    ChiTaRSi MED14. human.
    GeneWikii MED14.
    GenomeRNAii 9282.
    NextBioi 34783.
    PROi O60244.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60244.
    Bgeei O60244.
    CleanExi HS_MED14.
    Genevestigatori O60244.

    Family and domain databases

    InterProi IPR013947. Mediator_Med14.
    [Graphical view ]
    Pfami PF08638. Med14. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Detection and isolation of a novel human gene located on Xp11.2-p11.4 that escapes X-inactivation using a two-dimensional DNA mapping method."
      Yoshikawa H., Fujiyama A., Nakai K., Inazawa J., Matsubara K.
      Genomics 49:237-246(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1."
      Ryu S., Zhou S., Ladurner A.G., Tjian R.
      Nature 397:446-450(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex."
      Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M., Erdjument-Bromage H., Tempst P., Freedman L.P.
      Nature 398:824-828(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 250-263 AND 1106-1146, IDENTIFICATION IN ARC COMPLEX.
      Tissue: Cervix carcinoma.
    4. "A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation."
      Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., Qin J., Roeder R.G.
      Mol. Cell 3:97-108(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SMCC COMPLEX.
    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: Placenta.
    6. "NAT, a human complex containing Srb polypeptides that functions as a negative regulator of activated transcription."
      Sun X., Zhang Y., Cho H., Rickert P., Lees E., Lane W.S., Reinberg D.
      Mol. Cell 2:213-222(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A FORM OF THE MEDIATOR COMPLEX.
    7. "Composite co-activator ARC mediates chromatin-directed transcriptional activation."
      Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.
      Nature 398:828-832(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 4-13 AND 1256-1264, IDENTIFICATION IN ARC COMPLEX.
    8. "A coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expression."
      Wang Q., Sharma D., Ren Y., Fondell J.D.
      J. Biol. Chem. 277:42852-42858(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AR.
    9. "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro."
      Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.
      Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
    10. "Role of metazoan mediator proteins in interferon-responsive transcription."
      Lau J.F., Nusinzon I., Burakov D., Freedman L.P., Horvath C.M.
      Mol. Cell. Biol. 23:620-628(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAT2.
    11. "A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology."
      Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B., Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W., Conaway R.C.
      Mol. Cell 14:685-691(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX.
    12. "Selective coactivator interactions in gene activation by SREBP-1a and -1c."
      Toth J.I., Datta S., Athanikar J.N., Freedman L.P., Osborne T.F.
      Mol. Cell. Biol. 24:8288-8300(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SREBF1.
    13. "DRIP150 coactivation of estrogen receptor alpha in ZR-75 breast cancer cells is independent of LXXLL motifs."
      Lee J.E., Kim K., Sacchettini J.C., Smith C.V., Safe S.
      J. Biol. Chem. 280:8819-8830(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ESR1.
    14. "MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation enriched in RNA polymerase II and is required for ER-mediated transcription."
      Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T., Roeder R.G.
      Mol. Cell 19:89-100(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MED1 AND MED10, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
    15. "Human Mediator enhances basal transcription by facilitating recruitment of transcription factor IIB during preinitiation complex assembly."
      Baek H.J., Kang Y.K., Roeder R.G.
      J. Biol. Chem. 281:15172-15181(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MED1 AND MED10.
    16. "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-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1128; SER-1136 AND SER-1144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617 AND SER-986, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-1112; SER-1128 AND SER-1136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1112; SER-1119; SER-1128 AND SER-1136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-1325.

    Entry informationi

    Entry nameiMED14_HUMAN
    AccessioniPrimary (citable) accession number: O60244
    Secondary accession number(s): Q4KMR7, Q9UNB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2003
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 132 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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