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Q15648

- MED1_HUMAN

UniProt

Q15648 - MED1_HUMAN

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Protein

Mediator of RNA polymerase II transcription subunit 1

Gene

MED1

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.11 Publications

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. chromatin DNA binding Source: Ensembl
  3. core promoter binding Source: UniProtKB
  4. estrogen receptor binding Source: UniProtKB
  5. LBD domain binding Source: UniProtKB
  6. ligand-dependent nuclear receptor binding Source: UniProtKB
  7. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  8. mediator complex binding Source: UniProtKB
  9. nuclear hormone receptor binding Source: UniProtKB
  10. peroxisome proliferator activated receptor binding Source: UniProtKB
  11. receptor activity Source: UniProtKB
  12. retinoic acid receptor binding Source: UniProtKB
  13. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  14. RNA polymerase II transcription cofactor activity Source: UniProtKB
  15. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  16. thyroid hormone receptor binding Source: UniProtKB
  17. thyroid hormone receptor coactivator activity Source: UniProtKB
  18. transcription coactivator activity Source: UniProtKB
  19. transcription cofactor activity Source: UniProtKB
  20. transcription factor binding Source: UniProtKB
  21. vitamin D receptor binding Source: UniProtKB

GO - Biological processi

  1. androgen biosynthetic process Source: UniProtKB
  2. androgen receptor signaling pathway Source: UniProtKB
  3. angiogenesis Source: UniProtKB
  4. brain development Source: Ensembl
  5. cell morphogenesis Source: UniProtKB
  6. cellular lipid metabolic process Source: Reactome
  7. cellular response to epidermal growth factor stimulus Source: UniProtKB
  8. cellular response to hepatocyte growth factor stimulus Source: Ensembl
  9. cellular response to steroid hormone stimulus Source: UniProtKB
  10. cellular response to thyroid hormone stimulus Source: UniProtKB
  11. embryonic heart tube development Source: Ensembl
  12. embryonic hemopoiesis Source: Ensembl
  13. embryonic hindlimb morphogenesis Source: Ensembl
  14. embryonic placenta development Source: Ensembl
  15. enucleate erythrocyte development Source: Ensembl
  16. epithelial cell proliferation involved in mammary gland duct elongation Source: Ensembl
  17. ERK1 and ERK2 cascade Source: UniProtKB
  18. erythrocyte development Source: UniProtKB
  19. fat cell differentiation Source: MGI
  20. gene expression Source: Reactome
  21. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
  22. keratinocyte differentiation Source: UniProtKB
  23. lactation Source: Ensembl
  24. lens development in camera-type eye Source: UniProtKB
  25. liver development Source: Ensembl
  26. mammary gland branching involved in pregnancy Source: Ensembl
  27. mammary gland branching involved in thelarche Source: Ensembl
  28. megakaryocyte development Source: UniProtKB
  29. monocyte differentiation Source: Ensembl
  30. mRNA transcription from RNA polymerase II promoter Source: UniProtKB
  31. negative regulation of apoptotic process Source: UniProtKB
  32. negative regulation of keratinocyte proliferation Source: UniProtKB
  33. negative regulation of neuron differentiation Source: UniProtKB
  34. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  35. organ regeneration Source: Ensembl
  36. peroxisome proliferator activated receptor signaling pathway Source: Ensembl
  37. positive regulation of G0 to G1 transition Source: Ensembl
  38. positive regulation of gene expression Source: UniProtKB
  39. positive regulation of hepatocyte proliferation Source: Ensembl
  40. positive regulation of interferon-gamma-mediated signaling pathway Source: Ensembl
  41. positive regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
  42. positive regulation of keratinocyte differentiation Source: UniProtKB
  43. positive regulation of mammary gland epithelial cell proliferation Source: Ensembl
  44. positive regulation of protein import into nucleus, translocation Source: Ensembl
  45. positive regulation of receptor activity Source: UniProtKB
  46. positive regulation of transcription, DNA-templated Source: UniProtKB
  47. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  48. regulation of cell cycle Source: UniProtKB
  49. regulation of RNA biosynthetic process Source: UniProtKB
  50. regulation of transcription from RNA polymerase I promoter Source: UniProtKB
  51. regulation of vitamin D receptor signaling pathway Source: Ensembl
  52. retinal pigment epithelium development Source: Ensembl
  53. small molecule metabolic process Source: Reactome
  54. thyroid hormone generation Source: Ensembl
  55. thyroid hormone mediated signaling pathway Source: UniProtKB
  56. transcription initiation from RNA polymerase II promoter Source: UniProtKB
  57. ventricular trabecula myocardium morphogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118789. REV-ERBA represses gene expression.
REACT_12627. Generic Transcription Pathway.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_15525. Nuclear Receptor transcription pathway.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_267716. Orphan transporters.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ15648.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 1
Alternative name(s):
Activator-recruited cofactor 205 kDa component
Short name:
ARC205
Mediator complex subunit 1
Peroxisome proliferator-activated receptor-binding protein
Short name:
PBP
Short name:
PPAR-binding protein
Thyroid hormone receptor-associated protein complex 220 kDa component
Short name:
Trap220
Thyroid receptor-interacting protein 2
Short name:
TR-interacting protein 2
Short name:
TRIP-2
Vitamin D receptor-interacting protein complex component DRIP205
p53 regulatory protein RB18A
Gene namesi
Name:MED1
Synonyms:ARC205, CRSP1, CRSP200, DRIP205, DRIP230, PBP, PPARBP, PPARGBP, RB18A, TRAP220, TRIP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9234. MED1.

Subcellular locationi

Nucleus 3 Publications
Note: A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3.

GO - Cellular componenti

  1. chromatin Source: Ensembl
  2. mediator complex Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nucleolus Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
  7. protein-DNA complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi599 – 61214SQNPI…LQITG → EKHKILHRLLQDSS: Enhances interaction with ESR1. 1 PublicationAdd
BLAST
Mutagenesisi600 – 61213QNPIL…LQITG → RHKILHRLLQEGS: Enhances interaction with ESR1. 1 PublicationAdd
BLAST
Mutagenesisi604 – 6041L → A: Impairs interaction with ESR2; when associated with A-607; A-645 and A-648. 1 Publication
Mutagenesisi607 – 6082LL → AA: Impairs interaction with ESR1, PPARG, RXRA and THRB. Impairs interaction with THRA; when associated with 648-A-A-649. 6 Publications
Mutagenesisi607 – 6071L → A: Impairs interaction with ESR2; when associated with A-604; A-645 and A-648. 1 Publication
Mutagenesisi639 – 65315TKNHP…LKDNP → VSRHKILHRLLQEGS: Enhances interaction with ESR1. 1 PublicationAdd
BLAST
Mutagenesisi645 – 6451L → A: Impairs interaction with ESR2; when associated with A-604; A-607 and A-648. 1 Publication
Mutagenesisi648 – 6492LL → AA: Impairs interaction with ESR1, PPARG, THRB and VDR. Impairs interaction with THRA; when associated with 607-A-A-608. 6 Publications
Mutagenesisi648 – 6481L → A: Impairs interaction with ESR2; when associated with A-604; A-607 and A-645. 1 Publication
Mutagenesisi1032 – 10321T → A: Enhances protein stability; when associated with A-1457. 1 Publication
Mutagenesisi1457 – 14571T → A: Enhances protein stability; when associated with A-1032. 1 Publication

Organism-specific databases

PharmGKBiPA33556.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15811581Mediator of RNA polymerase II transcription subunit 1PRO_0000058552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei664 – 6641Phosphoserine3 Publications
Modified residuei795 – 7951Phosphoserine1 Publication
Modified residuei805 – 8051Phosphothreonine4 Publications
Modified residuei953 – 9531PhosphoserineBy similarity
Modified residuei1032 – 10321Phosphothreonine; by MAPK1 or MAPK31 Publication
Modified residuei1051 – 10511Phosphothreonine3 Publications
Modified residuei1057 – 10571Phosphothreonine5 Publications
Modified residuei1156 – 11561Phosphoserine1 Publication
Modified residuei1177 – 11771N6-acetyllysine1 Publication
Modified residuei1207 – 12071Phosphoserine4 Publications
Modified residuei1215 – 12151Phosphothreonine5 Publications
Modified residuei1223 – 12231Phosphoserine1 Publication
Modified residuei1347 – 13471Phosphoserine1 Publication
Modified residuei1403 – 14031Phosphoserine1 Publication
Modified residuei1433 – 14331Phosphoserine1 Publication
Modified residuei1457 – 14571Phosphothreonine; by MAPK1 or MAPK31 Publication
Modified residuei1463 – 14631Phosphoserine2 Publications
Modified residuei1479 – 14791Phosphoserine3 Publications
Modified residuei1481 – 14811Phosphoserine2 Publications
Modified residuei1482 – 14821Phosphoserine2 Publications
Modified residuei1529 – 15291N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may enhance protein stability and promote entry into the nucleolus.8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15648.
PaxDbiQ15648.
PRIDEiQ15648.

PTM databases

PhosphoSiteiQ15648.

Expressioni

Tissue specificityi

Ubiquitously expressed.2 Publications

Gene expression databases

BgeeiQ15648.
CleanExiHS_MED1.
ExpressionAtlasiQ15648. baseline and differential.
GenevestigatoriQ15648.

Organism-specific databases

HPAiCAB017696.
HPA052818.

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. This subunit specifically interacts with a number of nuclear receptors in a ligand-dependent fashion including AR, ESR1, ESR2, PPARA, PPARG, RORA, RXRA, RXRG, THRA, THRB and VDR. Interacts with CTNNB1, GABPA, GLI3, PPARGC1A and TP53. Interacts with GATA1 and YWHAH.22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RARAP102762EBI-394459,EBI-413374
THRAP108275EBI-394459,EBI-286285

Protein-protein interaction databases

BioGridi111465. 94 interactions.
DIPiDIP-24212N.
IntActiQ15648. 25 interactions.
MINTiMINT-1345780.
STRINGi9606.ENSP00000300651.

Structurei

Secondary structure

1
1581
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi643 – 6497Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJKX-ray1.99C640-652[»]
1RK3X-ray2.20C640-652[»]
1RKGX-ray1.90C640-652[»]
1RKHX-ray2.28C640-652[»]
2O4JX-ray1.74C640-652[»]
2O4RX-ray1.98C640-652[»]
2ZFXX-ray1.99C640-652[»]
3A2HX-ray2.50B640-652[»]
3AUNX-ray1.81B640-652[»]
3VJSX-ray1.93C640-652[»]
3VJTX-ray2.00C640-652[»]
3VRTX-ray2.40C640-652[»]
3VRUX-ray2.00C640-652[»]
3VRVX-ray1.90C640-652[»]
3VRWX-ray2.40C640-652[»]
3W0GX-ray1.94C640-652[»]
3W0HX-ray1.80C640-652[»]
3W0IX-ray1.90C640-652[»]
3W0JX-ray1.84C640-652[»]
3W5PX-ray1.90C640-652[»]
3W5QX-ray1.90C640-652[»]
3W5RX-ray2.20C640-652[»]
3W5TX-ray2.29C640-652[»]
3WT5X-ray1.90C640-652[»]
3WT6X-ray2.00C640-652[»]
3WT7X-ray2.40C640-652[»]
ProteinModelPortaliQ15648.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15648.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 670670Interaction with the Mediator complex and THRAAdd
BLAST
Regioni16 – 590575Interaction with ESR1Add
BLAST
Regioni108 – 212105Interaction with the Mediator complexAdd
BLAST
Regioni215 – 390176Interaction with the Mediator complexAdd
BLAST
Regioni405 – 644240Interaction with THRAAdd
BLAST
Regioni542 – 789248Interaction with VDRAdd
BLAST
Regioni622 – 70180Interaction with PPARGC1A and THRAAdd
BLAST
Regioni637 – 71680Interaction with GATA1By similarityAdd
BLAST
Regioni656 – 1066411Interaction with ESR1Add
BLAST
Regioni1249 – 1421173Interaction with TP53Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi604 – 6085LXXLL motif 1
Motifi645 – 6495LXXLL motif 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1078 – 1482405Ser-richAdd
BLAST
Compositional biasi1496 – 152934Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the Mediator complex subunit 1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00660000095569.
HOVERGENiHBG101127.
InParanoidiQ15648.
KOiK15144.
OMAiPKHQTED.
OrthoDBiEOG7R830S.
PhylomeDBiQ15648.
TreeFamiTF324954.

Family and domain databases

InterProiIPR019680. Mediator_Med1_met/fun.
[Graphical view]
PfamiPF10744. Med1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15648-1) [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

        10         20         30         40         50
MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM
60 70 80 90 100
SSGGHQHLVS CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE
110 120 130 140 150
CYITSDMFYV EVQLDPAGQL CDVKVAHHGE NPVSCPELVQ QLREKNFDEF
160 170 180 190 200
SKHLKGLVNL YNLPGDNKLK TKMYLALQSL EQDLSKMAIM YWKATNAGPL
210 220 230 240 250
DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI ILHENNVSRS
260 270 280 290 300
LGMNASVTIE GTSAVYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP
310 320 330 340 350
ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK
360 370 380 390 400
DPDPIPLNHN MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH
410 420 430 440 450
PGRVPLILNL IRHQVAYNTL IGSCVKRTIL KEDSPGLLQF EVCPLSESRF
460 470 480 490 500
SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY KGLSDALICT DDFIAKVVQR
510 520 530 540 550
CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL PPASSPGYGM
560 570 580 590 600
TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ
610 620 630 640 650
NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK
660 670 680 690 700
DNPAQDFSTL YGSSPLERQN SSSGSPRMEI CSGSNKTKKK KSSRLPPEKP
710 720 730 740 750
KHQTEDDFQR ELFSMDVDSQ NPIFDVNMTA DTLDTPHITP APSQCSTPPT
760 770 780 790 800
TYPQPVPHPQ PSIQRMVRLS SSDSIGPDVT DILSDIAEEA SKLPSTSDDC
810 820 830 840 850
PAIGTPLRDS SSSGHSQSTL FDSDVFQTNN NENPYTDPAD LIADAAGSPS
860 870 880 890 900
SDSPTNHFFH DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS
910 920 930 940 950
QALNTLGVPM LGGDNGETKF KGNNQADTVD FSIISVAGKA LAPADLMEHH
960 970 980 990 1000
SGSQGPLLTT GDLGKEKTQK RVKEGNGTSN STLSGPGLDS KPGKRSRTPS
1010 1020 1030 1040 1050
NDGKSKDKPP KRKKADTEGK SPSHSSSNRP FTPPTSTGGS KSPGSAGRSQ
1060 1070 1080 1090 1100
TPPGVATPPI PKITIQIPKG TVMVGKPSSH SQYTSSGSVS SSGSKSHHSH
1110 1120 1130 1140 1150
SSSSSSSAST SGKMKSSKSE GSSSSKLSSS MYSSQGSSGS SQSKNSSQSG
1160 1170 1180 1190 1200
GKPGSSPITK HGLSSGSSST KMKPQGKPSS LMNPSLSKPN ISPSHSRPPG
1210 1220 1230 1240 1250
GSDKLASPMK PVPGTPPSSK AKSPISSGSG GSHMSGTSSS SGMKSSSGLG
1260 1270 1280 1290 1300
SSGSLSQKTP PSSNSCTASS SSFSSSGSSM SSSQNQHGSS KGKSPSRNKK
1310 1320 1330 1340 1350
PSLTAVIDKL KHGVVTSGPG GEDPLDGQMG VSTNSSSHPM SSKHNMSGGE
1360 1370 1380 1390 1400
FQGKREKSDK DKSKVSTSGS SVDSSKKTSE SKNVGSTGVA KIIISKHDGG
1410 1420 1430 1440 1450
SPSIKAKVTL QKPGESSGEG LRPQMASSKN YGSPLISGST PKHERGSPSH
1460 1470 1480 1490 1500
SKSPAYTPQN LDSESESGSS IAEKSYQNSP SSDDGIRPLP EYSTEKHKKH
1510 1520 1530 1540 1550
KKEKKKVKDK DRDRDRDKDR DKKKSHSIKP ESWSKSPISS DQSLSMTSNT
1560 1570 1580
ILSADRPSRL SPDFMIGEED DDLMDVALIG N
Length:1,581
Mass (Da):168,478
Last modified:September 11, 2007 - v4
Checksum:iFCE0FE87EF08B887
GO
Isoform 2 (identifier: Q15648-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     548-556: YGMTTGNNP → SKNPELGSG
     557-1581: Missing.

Show »
Length:556
Mass (Da):61,563
Checksum:i1E8BBE45A2629DB1
GO

Sequence cautioni

The sequence AAC39854.1 differs from that shown. Reason: Frameshift at positions 543 and 545. Curated
The sequence AAH06517.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence CAA73867.1 differs from that shown. Reason: Frameshift at position 4. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861R → G in CAA73867. (PubMed:9444950)Curated
Sequence conflicti147 – 1471F → S in CAA73867. (PubMed:9444950)Curated
Sequence conflicti471 – 4722DS → GL in CAA73867. (PubMed:9444950)Curated
Sequence conflicti563 – 5631P → S in CAA73867. (PubMed:9444950)Curated
Sequence conflicti563 – 5631P → S in AAF98352. (PubMed:10733574)Curated
Sequence conflicti573 – 5731T → A in CAA73867. (PubMed:9444950)Curated
Sequence conflicti573 – 5731T → A in AAF98352. (PubMed:10733574)Curated
Sequence conflicti651 – 6511D → N in AAH06517. (PubMed:15489334)Curated
Sequence conflicti673 – 6731S → F in AAC41736. (PubMed:7776974)Curated
Sequence conflicti702 – 7087Missing in AAC41736. (PubMed:7776974)Curated
Sequence conflicti721 – 7211N → K in AAC39854. (PubMed:9653119)Curated
Sequence conflicti728 – 7281M → R in AAF98352. (PubMed:10733574)Curated
Sequence conflicti756 – 7616VPHPQP → FYLTPQ in AAH06517. (PubMed:15489334)Curated
Sequence conflicti1388 – 13881G → S in AAC39854. (PubMed:9653119)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti753 – 7531P → T.
Corresponds to variant rs1139825 [ dbSNP | Ensembl ].
VAR_053955
Natural varianti1240 – 12401S → G.
Corresponds to variant rs35668211 [ dbSNP | Ensembl ].
VAR_034938

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei548 – 5569YGMTTGNNP → SKNPELGSG in isoform 2. 1 PublicationVSP_027906
Alternative sequencei557 – 15811025Missing in isoform 2. 1 PublicationVSP_027907Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13467 mRNA. Translation: CAA73867.1. Frameshift.
AF055994 mRNA. Translation: AAC39854.1. Frameshift.
CH471152 Genomic DNA. Translation: EAW60575.1.
BC006517 mRNA. Translation: AAH06517.1. Different termination.
BC060758 mRNA. Translation: AAH60758.1.
BC131783 mRNA. Translation: AAI31784.1.
AF283812 mRNA. Translation: AAF98352.1.
L40366 mRNA. Translation: AAC41736.1.
CCDSiCCDS11336.1. [Q15648-1]
RefSeqiNP_004765.2. NM_004774.3. [Q15648-1]
UniGeneiHs.643754.

Genome annotation databases

EnsembliENST00000300651; ENSP00000300651; ENSG00000125686. [Q15648-1]
ENST00000394287; ENSP00000377828; ENSG00000125686. [Q15648-3]
GeneIDi5469.
KEGGihsa:5469.
UCSCiuc002hru.2. human. [Q15648-3]
uc002hrv.4. human. [Q15648-1]

Polymorphism databases

DMDMi158518535.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13467 mRNA. Translation: CAA73867.1 . Frameshift.
AF055994 mRNA. Translation: AAC39854.1 . Frameshift.
CH471152 Genomic DNA. Translation: EAW60575.1 .
BC006517 mRNA. Translation: AAH06517.1 . Different termination.
BC060758 mRNA. Translation: AAH60758.1 .
BC131783 mRNA. Translation: AAI31784.1 .
AF283812 mRNA. Translation: AAF98352.1 .
L40366 mRNA. Translation: AAC41736.1 .
CCDSi CCDS11336.1. [Q15648-1 ]
RefSeqi NP_004765.2. NM_004774.3. [Q15648-1 ]
UniGenei Hs.643754.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RJK X-ray 1.99 C 640-652 [» ]
1RK3 X-ray 2.20 C 640-652 [» ]
1RKG X-ray 1.90 C 640-652 [» ]
1RKH X-ray 2.28 C 640-652 [» ]
2O4J X-ray 1.74 C 640-652 [» ]
2O4R X-ray 1.98 C 640-652 [» ]
2ZFX X-ray 1.99 C 640-652 [» ]
3A2H X-ray 2.50 B 640-652 [» ]
3AUN X-ray 1.81 B 640-652 [» ]
3VJS X-ray 1.93 C 640-652 [» ]
3VJT X-ray 2.00 C 640-652 [» ]
3VRT X-ray 2.40 C 640-652 [» ]
3VRU X-ray 2.00 C 640-652 [» ]
3VRV X-ray 1.90 C 640-652 [» ]
3VRW X-ray 2.40 C 640-652 [» ]
3W0G X-ray 1.94 C 640-652 [» ]
3W0H X-ray 1.80 C 640-652 [» ]
3W0I X-ray 1.90 C 640-652 [» ]
3W0J X-ray 1.84 C 640-652 [» ]
3W5P X-ray 1.90 C 640-652 [» ]
3W5Q X-ray 1.90 C 640-652 [» ]
3W5R X-ray 2.20 C 640-652 [» ]
3W5T X-ray 2.29 C 640-652 [» ]
3WT5 X-ray 1.90 C 640-652 [» ]
3WT6 X-ray 2.00 C 640-652 [» ]
3WT7 X-ray 2.40 C 640-652 [» ]
ProteinModelPortali Q15648.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111465. 94 interactions.
DIPi DIP-24212N.
IntActi Q15648. 25 interactions.
MINTi MINT-1345780.
STRINGi 9606.ENSP00000300651.

PTM databases

PhosphoSitei Q15648.

Polymorphism databases

DMDMi 158518535.

Proteomic databases

MaxQBi Q15648.
PaxDbi Q15648.
PRIDEi Q15648.

Protocols and materials databases

DNASUi 5469.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300651 ; ENSP00000300651 ; ENSG00000125686 . [Q15648-1 ]
ENST00000394287 ; ENSP00000377828 ; ENSG00000125686 . [Q15648-3 ]
GeneIDi 5469.
KEGGi hsa:5469.
UCSCi uc002hru.2. human. [Q15648-3 ]
uc002hrv.4. human. [Q15648-1 ]

Organism-specific databases

CTDi 5469.
GeneCardsi GC17M037560.
HGNCi HGNC:9234. MED1.
HPAi CAB017696.
HPA052818.
MIMi 604311. gene.
neXtProti NX_Q15648.
PharmGKBi PA33556.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00660000095569.
HOVERGENi HBG101127.
InParanoidi Q15648.
KOi K15144.
OMAi PKHQTED.
OrthoDBi EOG7R830S.
PhylomeDBi Q15648.
TreeFami TF324954.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118789. REV-ERBA represses gene expression.
REACT_12627. Generic Transcription Pathway.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_15525. Nuclear Receptor transcription pathway.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_267716. Orphan transporters.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki Q15648.

Miscellaneous databases

ChiTaRSi MED1. human.
EvolutionaryTracei Q15648.
GeneWikii MED1.
GenomeRNAii 5469.
NextBioi 21174.
PROi Q15648.
SOURCEi Search...

Gene expression databases

Bgeei Q15648.
CleanExi HS_MED1.
ExpressionAtlasi Q15648. baseline and differential.
Genevestigatori Q15648.

Family and domain databases

InterProi IPR019680. Mediator_Med1_met/fun.
[Graphical view ]
Pfami PF10744. Med1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of RB18A, a 205 kDa new p53 regulatory protein which shares antigenic and functional properties with p53."
    Drane P., Barel M., Balbo M., Frade R.
    Oncogene 15:3013-3024(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING, INTERACTION WITH TP53, TISSUE SPECIFICITY.
    Tissue: Heart.
  2. "The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion."
    Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.
    Proc. Natl. Acad. Sci. U.S.A. 95:7939-7944(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 157-168; 943-952 AND 1432-1442, FUNCTION, INTERACTION WITH ESR1; PPARA; PPARG; RARA; RXRA; THRA AND VDR, TISSUE SPECIFICITY, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
  3. Erratum
    Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.
    Proc. Natl. Acad. Sci. U.S.A. 95:14584-14584(1998)
  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] (ISOFORMS 1 AND 2).
    Tissue: Colon and Testis.
  6. "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 1-13 AND 1452-1464, IDENTIFICATION IN THE ARC COMPLEX.
  7. "The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes."
    Rachez C., Gamble M., Chang C.-P.B., Atkins G.B., Lazar M.A., Freedman L.P.
    Mol. Cell. Biol. 20:2718-2726(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-1581 (ISOFORM 1), INTERACTION WITH VDR, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
  8. "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 307-315 AND 584-597, IDENTIFICATION IN THE DRIP COMPLEX, INTERACTION WITH VDR.
    Tissue: Cervix carcinoma.
  9. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
    Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
    Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 622-711.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SMCC COMPLEX.
  11. "Identification of mouse TRAP100: a transcriptional coregulatory factor for thyroid hormone and vitamin D receptors."
    Zhang J., Fondell J.D.
    Mol. Endocrinol. 13:1130-1140(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MED24; THRA; THRB AND VDR.
  12. Cited for: INTERACTION WITH RORA.
  13. "Functional interactions between the estrogen receptor and DRIP205, a subunit of the heteromeric DRIP coactivator complex."
    Burakov D., Wong C.-W., Rachez C., Cheskis B.J., Freedman L.P.
    J. Biol. Chem. 275:20928-20934(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ESR1; ESR2 AND VDR, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
  14. "Differential recruitment of the mammalian mediator subunit TRAP220 by estrogen receptors ERalpha and ERbeta."
    Waernmark A., Almloef T., Leers J., Gustafsson J.-A., Treuter E.
    J. Biol. Chem. 276:23397-23404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ESR1 AND ESR2, MUTAGENESIS OF 599-SER--GLY-612; LEU-604; LEU-607; LEU-645 AND LEU-648.
  15. "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: FUNCTION, INTERACTION WITH AR, ASSOCIATION WITH PROMOTER REGIONS.
  16. "Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis."
    Ge K., Guermah M., Yuan C.-X., Ito M., Wallberg A.E., Spiegelman B.M., Roeder R.G.
    Nature 417:563-567(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION OF THE MEDIATOR COMPLEX WITH PPARG.
  17. "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: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
  18. "Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo."
    Sharma D., Fondell J.D.
    Proc. Natl. Acad. Sci. U.S.A. 99:7934-7939(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PROMOTER REGIONS.
  19. "An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220."
    Coulthard V.H., Matsuda S., Heery D.M.
    J. Biol. Chem. 278:10942-10951(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ESR1; PPARG; RARA; RXRA AND THRB, MUTAGENESIS OF 600-GLN--SER-612; 607-LEU-LEU-608; 639-THR--PRO-653 AND 648-LEU-LEU-649.
  20. "Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha."
    Wallberg A.E., Yamamura S., Malik S., Spiegelman B.M., Roeder R.G.
    Mol. Cell 12:1137-1149(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPARGC1A, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
  21. "Vitamin D-interacting protein 205 (DRIP205) coactivation of estrogen receptor alpha (ERalpha) involves multiple domains of both proteins."
    Wu Q., Burghardt R., Safe S.
    J. Biol. Chem. 279:53602-53612(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ESR1, SUBCELLULAR LOCATION.
  22. "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.
  23. "Structural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptors."
    Malik S., Guermah M., Yuan C.-X., Wu W., Yamamura S., Roeder R.G.
    Mol. Cell. Biol. 24:8244-8254(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION OF THE MEDIATOR COMPLEX WITH THRA, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
  24. "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: FUNCTION, ASSOCIATION WITH PROMOTER REGIONS, INTERACTION WITH CCNC; MED6; MED10; MED11; MED12; MED13; MED14; MED15; MED16; MED17; MED18; MED19; MED20; MED21; MED23; MED24; MED25; MED26; MED28; MED29 AND MED30, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  25. "Activation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-activated protein kinase-dependent phosphorylation."
    Pandey P.K., Udayakumar T.S., Lin X., Sharma D., Shapiro P.S., Fondell J.D.
    Mol. Cell. Biol. 25:10695-10710(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1032 AND THR-1457, MUTAGENESIS OF THR-1032 AND THR-1457.
  26. "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.
  27. "Regulation of Aurora-A kinase gene expression via GABP recruitment of TRAP220/MED1."
    Udayakumar T.S., Belakavadi M., Choi K.-H., Pandey P.K., Fondell J.D.
    J. Biol. Chem. 281:14691-14699(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GABPA, ASSOCIATION WITH PROMOTER REGIONS, SUBCELLULAR LOCATION.
  28. "Mediator modulates Gli3-dependent Sonic hedgehog signaling."
    Zhou H., Kim S., Ishii S., Boyer T.G.
    Mol. Cell. Biol. 26:8667-8682(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK8.
  29. "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-795; THR-805 AND THR-1057, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  31. "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 THR-805; THR-1057; SER-1207 AND THR-1215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-1051; THR-1057; SER-1207; THR-1215; SER-1463; SER-1479; SER-1481 AND SER-1482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805 AND THR-1215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors."
    Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y., Makishima M.
    Mol. Pharmacol. 76:1360-1369(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RXRA.
  36. "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-664; THR-1051; THR-1057; SER-1463; SER-1479; SER-1481 AND SER-1482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  37. "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-1177 AND LYS-1529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. "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-664; THR-805; THR-1057; SER-1207; THR-1215; SER-1347; SER-1403 AND SER-1433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1051; SER-1156; SER-1207; THR-1215; SER-1223 AND SER-1479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMED1_HUMAN
AccessioniPrimary (citable) accession number: Q15648
Secondary accession number(s): A2RRQ6
, O43810, O75447, Q6P9H7, Q6PK58, Q9HD39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 11, 2007
Last modified: November 26, 2014
This is version 147 of the entry and version 4 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3