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)

Q9UHV7

- MED13_HUMAN

UniProt

Q9UHV7 - MED13_HUMAN

Protein

Mediator of RNA polymerase II transcription subunit 13

Gene

MED13

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 126 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 Publication

    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. transcription initiation from RNA polymerase II promoter Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Repressor

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mediator of RNA polymerase II transcription subunit 13
    Alternative name(s):
    Activator-recruited cofactor 250 kDa component
    Short name:
    ARC250
    Mediator complex subunit 13
    Thyroid hormone receptor-associated protein 1
    Thyroid hormone receptor-associated protein complex 240 kDa component
    Short name:
    Trap240
    Vitamin D3 receptor-interacting protein complex component DRIP250
    Short name:
    DRIP250
    Gene namesi
    Name:MED13
    Synonyms:ARC250, KIAA0593, THRAP1, TRAP240
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:22474. MED13.

    Subcellular locationi

    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

    PharmGKBiPA162395168.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21742174Mediator of RNA polymerase II transcription subunit 13PRO_0000065584Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei500 – 5001Phosphoserine1 Publication
    Modified residuei504 – 5041Phosphoserine1 Publication
    Modified residuei537 – 5371Phosphoserine1 Publication
    Modified residuei1029 – 10291Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UHV7.
    PaxDbiQ9UHV7.
    PRIDEiQ9UHV7.

    PTM databases

    PhosphoSiteiQ9UHV7.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9UHV7.
    BgeeiQ9UHV7.
    CleanExiHS_MED13.
    GenevestigatoriQ9UHV7.

    Interactioni

    Subunit structurei

    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.5 Publications

    Protein-protein interaction databases

    BioGridi115294. 33 interactions.
    DIPiDIP-31468N.
    IntActiQ9UHV7. 15 interactions.
    MINTiMINT-4329245.
    STRINGi9606.ENSP00000380888.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UHV7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1188 – 11925LXXLL motif 1
    Motifi1279 – 12835LXXLL motif 2

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1508 – 157366Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Mediator complex subunit 13 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG304462.
    HOGENOMiHOG000012893.
    HOVERGENiHBG058069.
    KOiK15164.
    OMAiFHHRVSV.
    OrthoDBiEOG73FQKS.
    PhylomeDBiQ9UHV7.
    TreeFamiTF316867.

    Family and domain databases

    InterProiIPR009401. Mediator_Med13.
    IPR021643. Mediator_Med13_N_met/fun.
    [Graphical view]
    PfamiPF06333. Med13_C. 1 hit.
    PF11597. Med13_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UHV7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSASFVPNGA SLEDCHCNLF CLADLTGIKW KKYVWQGPTS APILFPVTEE     50
    DPILSSFSRC LKADVLGVWR RDQRPGRREL WIFWWGEDPS FADLIHHDLS 100
    EEEDGVWENG LSYECRTLLF KAVHNLLERC LMNRNFVRIG KWFVKPYEKD 150
    EKPINKSEHL SCSFTFFLHG DSNVCTSVEI NQHQPVYLLS EEHITLAQQS 200
    NSPFQVILCP FGLNGTLTGQ AFKMSDSATK KLIGEWKQFY PISCCLKEMS 250
    EEKQEDMDWE DDSLAAVEVL VAGVRMIYPA CFVLVPQSDI PTPSPVGSTH 300
    CSSSCLGVHQ VPASTRDPAM SSVTLTPPTS PEEVQTVDPQ SVQKWVKFSS 350
    VSDGFNSDST SHHGGKIPRK LANHVVDRVW QECNMNRAQN KRKYSASSGG 400
    LCEEATAAKV ASWDFVEATQ RTNCSCLRHK NLKSRNAGQQ GQAPSLGQQQ 450
    QILPKHKTNE KQEKSEKPQK RPLTPFHHRV SVSDDVGMDA DSASQRLVIS 500
    APDSQVRFSN IRTNDVAKTP QMHGTEMANS PQPPPLSPHP CDVVDEGVTK 550
    TPSTPQSQHF YQMPTPDPLV PSKPMEDRID SLSQSFPPQY QEAVEPTVYV 600
    GTAVNLEEDE ANIAWKYYKF PKKKDVEFLP PQLPSDKFKD DPVGPFGQES 650
    VTSVTELMVQ CKKPLKVSDE LVQQYQIKNQ CLSAIASDAE QEPKIDPYAF 700
    VEGDEEFLFP DKKDRQNSER EAGKKHKVED GTSSVTVLSH EEDAMSLFSP 750
    SIKQDAPRPT SHARPPSTSL IYDSDLAVSY TDLDNLFNSD EDELTPGSKK 800
    SANGSDDKAS CKESKTGNLD PLSCISTADL HKMYPTPPSL EQHIMGFSPM 850
    NMNNKEYGSM DTTPGGTVLE GNSSSIGAQF KIEVDEGFCS PKPSEIKDFS 900
    YVYKPENCQI LVGCSMFAPL KTLPSQYLPP IKLPEECIYR QSWTVGKLEL 950
    LSSGPSMPFI KEGDGSNMDQ EYGTAYTPQT HTSFGMPPSS APPSNSGAGI 1000
    LPSPSTPRFP TPRTPRTPRT PRGAGGPASA QGSVKYENSD LYSPASTPST 1050
    CRPLNSVEPA TVPSIPEAHS LYVNLILSES VMNLFKDCNF DSCCICVCNM 1100
    NIKGADVGVY IPDPTQEAQY RCTCGFSAVM NRKFGNNSGL FLEDELDIIG 1150
    RNTDCGKEAE KRFEALRATS AEHVNGGLKE SEKLSDDLIL LLQDQCTNLF 1200
    SPFGAADQDP FPKSGVISNW VRVEERDCCN DCYLALEHGR QFMDNMSGGK 1250
    VDEALVKSSC LHPWSKRNDV SMQCSQDILR MLLSLQPVLQ DAIQKKRTVR 1300
    PWGVQGPLTW QQFHKMAGRG SYGTDESPEP LPIPTFLLGY DYDYLVLSPF 1350
    ALPYWERLML EPYGSQRDIA YVVLCPENEA LLNGAKSFFR DLTAIYESCR 1400
    LGQHRPVSRL LTDGIMRVGS TASKKLSEKL VAEWFSQAAD GNNEAFSKLK 1450
    LYAQVCRYDL GPYLASLPLD SSLLSQPNLV APTSQSLITP PQMTNTGNAN 1500
    TPSATLASAA SSTMTVTSGV AISTSVATAN STLTTASTSS SSSSNLNSGV 1550
    SSNKLPSFPP FGSMNSNAAG SMSTQANTVQ SGQLGGQQTS ALQTAGISGE 1600
    SSSLPTQPHP DVSESTMDRD KVGIPTDGDS HAVTYPPAIV VYIIDPFTYE 1650
    NTDESTNSSS VWTLGLLRCF LEMVQTLPPH IKSTVSVQII PCQYLLQPVK 1700
    HEDREIYPQH LKSLAFSAFT QCRRPLPTST NVKTLTGFGP GLAMETALRS 1750
    PDRPECIRLY APPFILAPVK DKQTELGETF GEAGQKYNVL FVGYCLSHDQ 1800
    RWILASCTDL YGELLETCII NIDVPNRARR KKSSARKFGL QKLWEWCLGL 1850
    VQMSSLPWRV VIGRLGRIGH GELKDWSCLL SRRNLQSLSK RLKDMCRMCG 1900
    ISAADSPSIL SACLVAMEPQ GSFVIMPDSV STGSVFGRST TLNMQTSQLN 1950
    TPQDTSCTHI LVFPTSASVQ VASATYTTEN LDLAFNPNND GADGMGIFDL 2000
    LDTGDDLDPD IINILPASPT GSPVHSPGSH YPHGGDAGKG QSTDRLLSTE 2050
    PHEEVPNILQ QPLALGYFVS TAKAGPLPDW FWSACPQAQY QCPLFLKASL 2100
    HLHVPSVQSD ELLHSKHSHP LDSNQTSDVL RFVLEQYNAL SWLTCDPATQ 2150
    DRRSCLPIHF VVLNQLYNFI MNML 2174
    Length:2,174
    Mass (Da):239,297
    Last modified:January 11, 2011 - v3
    Checksum:i0FA54C84FE2C91E2
    GO

    Sequence cautioni

    The sequence AAD22032.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061V → M in AAD22032. (PubMed:10198638)Curated
    Sequence conflicti392 – 3921R → K in AAD22032. (PubMed:10198638)Curated
    Sequence conflicti467 – 4671K → E in AAD22032. (PubMed:10198638)Curated
    Sequence conflicti712 – 7121K → A AA sequence (PubMed:10198638)Curated
    Sequence conflicti800 – 8001K → R in AAD22032. (PubMed:10198638)Curated
    Sequence conflicti930 – 9301P → L in AAD22032. (PubMed:10198638)Curated
    Sequence conflicti984 – 9841F → C in AAD22032. (PubMed:10198638)Curated
    Sequence conflicti1090 – 10901F → S in AAD22032. (PubMed:10198638)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1370 – 13701A → P.
    Corresponds to variant rs34805963 [ dbSNP | Ensembl ].
    VAR_057792
    Natural varianti1385 – 13851A → P.
    Corresponds to variant rs35996128 [ dbSNP | Ensembl ].
    VAR_057793

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117754 mRNA. Translation: AAD22032.1. Frameshift.
    AC008158 Genomic DNA. No translation available.
    AC018628 Genomic DNA. No translation available.
    AC060798 Genomic DNA. No translation available.
    CH471179 Genomic DNA. Translation: EAW51438.1.
    BC140891 mRNA. Translation: AAI40892.1.
    AB011165 mRNA. Translation: BAA25519.2.
    CCDSiCCDS42366.1.
    PIRiT01238.
    RefSeqiNP_005112.2. NM_005121.2.
    UniGeneiHs.282678.

    Genome annotation databases

    EnsembliENST00000397786; ENSP00000380888; ENSG00000108510.
    GeneIDi9969.
    KEGGihsa:9969.
    UCSCiuc002izo.3. human.

    Polymorphism databases

    DMDMi317373421.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117754 mRNA. Translation: AAD22032.1 . Frameshift.
    AC008158 Genomic DNA. No translation available.
    AC018628 Genomic DNA. No translation available.
    AC060798 Genomic DNA. No translation available.
    CH471179 Genomic DNA. Translation: EAW51438.1 .
    BC140891 mRNA. Translation: AAI40892.1 .
    AB011165 mRNA. Translation: BAA25519.2 .
    CCDSi CCDS42366.1.
    PIRi T01238.
    RefSeqi NP_005112.2. NM_005121.2.
    UniGenei Hs.282678.

    3D structure databases

    ProteinModelPortali Q9UHV7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115294. 33 interactions.
    DIPi DIP-31468N.
    IntActi Q9UHV7. 15 interactions.
    MINTi MINT-4329245.
    STRINGi 9606.ENSP00000380888.

    PTM databases

    PhosphoSitei Q9UHV7.

    Polymorphism databases

    DMDMi 317373421.

    Proteomic databases

    MaxQBi Q9UHV7.
    PaxDbi Q9UHV7.
    PRIDEi Q9UHV7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397786 ; ENSP00000380888 ; ENSG00000108510 .
    GeneIDi 9969.
    KEGGi hsa:9969.
    UCSCi uc002izo.3. human.

    Organism-specific databases

    CTDi 9969.
    GeneCardsi GC17M060019.
    H-InvDB HIX0014059.
    HGNCi HGNC:22474. MED13.
    MIMi 603808. gene.
    neXtProti NX_Q9UHV7.
    PharmGKBi PA162395168.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304462.
    HOGENOMi HOG000012893.
    HOVERGENi HBG058069.
    KOi K15164.
    OMAi FHHRVSV.
    OrthoDBi EOG73FQKS.
    PhylomeDBi Q9UHV7.
    TreeFami TF316867.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi MED13. human.
    GeneWikii MED13.
    GenomeRNAii 9969.
    NextBioi 37622.
    PROi Q9UHV7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHV7.
    Bgeei Q9UHV7.
    CleanExi HS_MED13.
    Genevestigatori Q9UHV7.

    Family and domain databases

    InterProi IPR009401. Mediator_Med13.
    IPR021643. Mediator_Med13_N_met/fun.
    [Graphical view ]
    Pfami PF06333. Med13_C. 1 hit.
    PF11597. Med13_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators."
      Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S., Fu Z.-Y., Zhang X., Qin J., Roeder R.G.
      Mol. Cell 3:361-370(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 696-713, TISSUE SPECIFICITY, IDENTIFICATION IN TRAP COMPLEX.
      Tissue: Cervix carcinoma.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-2174.
      Tissue: Brain.
    6. Ohara O., Nagase T., Ishikawa K.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    7. "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: PROTEIN SEQUENCE OF 1401-1408 AND 1358-1367, IDENTIFICATION IN ARC COMPLEX.
      Tissue: Cervix carcinoma.
    8. "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: IDENTIFICATION IN ARC COMPLEX, PROTEIN SEQUENCE OF 1429-1438; 1772-1783 AND 2073-2084.
    9. "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, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
    10. "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; MED18; MED21; MED28; MED29 AND MED30, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
    11. "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.
    12. "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-500 AND SER-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiMED13_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHV7
    Secondary accession number(s): B2RU05, O60334
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2003
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 126 of the entry and version 3 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 17
      Human chromosome 17: 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