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Q9UHV7

- MED13_HUMAN

UniProt

Q9UHV7 - MED13_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UHV7.
CleanExiHS_MED13.
ExpressionAtlasiQ9UHV7. baseline and differential.
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. 36 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.
GeneTreeiENSGT00390000013680.
HOGENOMiHOG000012893.
HOVERGENiHBG058069.
InParanoidiQ9UHV7.
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

        10         20         30         40         50
MSASFVPNGA SLEDCHCNLF CLADLTGIKW KKYVWQGPTS APILFPVTEE
60 70 80 90 100
DPILSSFSRC LKADVLGVWR RDQRPGRREL WIFWWGEDPS FADLIHHDLS
110 120 130 140 150
EEEDGVWENG LSYECRTLLF KAVHNLLERC LMNRNFVRIG KWFVKPYEKD
160 170 180 190 200
EKPINKSEHL SCSFTFFLHG DSNVCTSVEI NQHQPVYLLS EEHITLAQQS
210 220 230 240 250
NSPFQVILCP FGLNGTLTGQ AFKMSDSATK KLIGEWKQFY PISCCLKEMS
260 270 280 290 300
EEKQEDMDWE DDSLAAVEVL VAGVRMIYPA CFVLVPQSDI PTPSPVGSTH
310 320 330 340 350
CSSSCLGVHQ VPASTRDPAM SSVTLTPPTS PEEVQTVDPQ SVQKWVKFSS
360 370 380 390 400
VSDGFNSDST SHHGGKIPRK LANHVVDRVW QECNMNRAQN KRKYSASSGG
410 420 430 440 450
LCEEATAAKV ASWDFVEATQ RTNCSCLRHK NLKSRNAGQQ GQAPSLGQQQ
460 470 480 490 500
QILPKHKTNE KQEKSEKPQK RPLTPFHHRV SVSDDVGMDA DSASQRLVIS
510 520 530 540 550
APDSQVRFSN IRTNDVAKTP QMHGTEMANS PQPPPLSPHP CDVVDEGVTK
560 570 580 590 600
TPSTPQSQHF YQMPTPDPLV PSKPMEDRID SLSQSFPPQY QEAVEPTVYV
610 620 630 640 650
GTAVNLEEDE ANIAWKYYKF PKKKDVEFLP PQLPSDKFKD DPVGPFGQES
660 670 680 690 700
VTSVTELMVQ CKKPLKVSDE LVQQYQIKNQ CLSAIASDAE QEPKIDPYAF
710 720 730 740 750
VEGDEEFLFP DKKDRQNSER EAGKKHKVED GTSSVTVLSH EEDAMSLFSP
760 770 780 790 800
SIKQDAPRPT SHARPPSTSL IYDSDLAVSY TDLDNLFNSD EDELTPGSKK
810 820 830 840 850
SANGSDDKAS CKESKTGNLD PLSCISTADL HKMYPTPPSL EQHIMGFSPM
860 870 880 890 900
NMNNKEYGSM DTTPGGTVLE GNSSSIGAQF KIEVDEGFCS PKPSEIKDFS
910 920 930 940 950
YVYKPENCQI LVGCSMFAPL KTLPSQYLPP IKLPEECIYR QSWTVGKLEL
960 970 980 990 1000
LSSGPSMPFI KEGDGSNMDQ EYGTAYTPQT HTSFGMPPSS APPSNSGAGI
1010 1020 1030 1040 1050
LPSPSTPRFP TPRTPRTPRT PRGAGGPASA QGSVKYENSD LYSPASTPST
1060 1070 1080 1090 1100
CRPLNSVEPA TVPSIPEAHS LYVNLILSES VMNLFKDCNF DSCCICVCNM
1110 1120 1130 1140 1150
NIKGADVGVY IPDPTQEAQY RCTCGFSAVM NRKFGNNSGL FLEDELDIIG
1160 1170 1180 1190 1200
RNTDCGKEAE KRFEALRATS AEHVNGGLKE SEKLSDDLIL LLQDQCTNLF
1210 1220 1230 1240 1250
SPFGAADQDP FPKSGVISNW VRVEERDCCN DCYLALEHGR QFMDNMSGGK
1260 1270 1280 1290 1300
VDEALVKSSC LHPWSKRNDV SMQCSQDILR MLLSLQPVLQ DAIQKKRTVR
1310 1320 1330 1340 1350
PWGVQGPLTW QQFHKMAGRG SYGTDESPEP LPIPTFLLGY DYDYLVLSPF
1360 1370 1380 1390 1400
ALPYWERLML EPYGSQRDIA YVVLCPENEA LLNGAKSFFR DLTAIYESCR
1410 1420 1430 1440 1450
LGQHRPVSRL LTDGIMRVGS TASKKLSEKL VAEWFSQAAD GNNEAFSKLK
1460 1470 1480 1490 1500
LYAQVCRYDL GPYLASLPLD SSLLSQPNLV APTSQSLITP PQMTNTGNAN
1510 1520 1530 1540 1550
TPSATLASAA SSTMTVTSGV AISTSVATAN STLTTASTSS SSSSNLNSGV
1560 1570 1580 1590 1600
SSNKLPSFPP FGSMNSNAAG SMSTQANTVQ SGQLGGQQTS ALQTAGISGE
1610 1620 1630 1640 1650
SSSLPTQPHP DVSESTMDRD KVGIPTDGDS HAVTYPPAIV VYIIDPFTYE
1660 1670 1680 1690 1700
NTDESTNSSS VWTLGLLRCF LEMVQTLPPH IKSTVSVQII PCQYLLQPVK
1710 1720 1730 1740 1750
HEDREIYPQH LKSLAFSAFT QCRRPLPTST NVKTLTGFGP GLAMETALRS
1760 1770 1780 1790 1800
PDRPECIRLY APPFILAPVK DKQTELGETF GEAGQKYNVL FVGYCLSHDQ
1810 1820 1830 1840 1850
RWILASCTDL YGELLETCII NIDVPNRARR KKSSARKFGL QKLWEWCLGL
1860 1870 1880 1890 1900
VQMSSLPWRV VIGRLGRIGH GELKDWSCLL SRRNLQSLSK RLKDMCRMCG
1910 1920 1930 1940 1950
ISAADSPSIL SACLVAMEPQ GSFVIMPDSV STGSVFGRST TLNMQTSQLN
1960 1970 1980 1990 2000
TPQDTSCTHI LVFPTSASVQ VASATYTTEN LDLAFNPNND GADGMGIFDL
2010 2020 2030 2040 2050
LDTGDDLDPD IINILPASPT GSPVHSPGSH YPHGGDAGKG QSTDRLLSTE
2060 2070 2080 2090 2100
PHEEVPNILQ QPLALGYFVS TAKAGPLPDW FWSACPQAQY QCPLFLKASL
2110 2120 2130 2140 2150
HLHVPSVQSD ELLHSKHSHP LDSNQTSDVL RFVLEQYNAL SWLTCDPATQ
2160 2170
DRRSCLPIHF VVLNQLYNFI MNML
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 36 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.
GeneTreei ENSGT00390000013680.
HOGENOMi HOG000012893.
HOVERGENi HBG058069.
InParanoidi Q9UHV7.
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

Bgeei Q9UHV7.
CleanExi HS_MED13.
ExpressionAtlasi Q9UHV7. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 127 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