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Protein

Mediator of RNA polymerase II transcription subunit 25

Gene

MED25

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Required for RARA/RXRA-mediated transcription.3 Publications

GO - Molecular functioni

  1. retinoic acid receptor binding Source: UniProtKB
  2. retinoid X receptor binding Source: UniProtKB
  3. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. negative regulation of fibroblast proliferation Source: UniProtKB
  3. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  4. positive regulation of cell cycle arrest Source: UniProtKB
  5. positive regulation of chromatin binding Source: UniProtKB
  6. positive regulation of mediator complex assembly Source: UniProtKB
  7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  8. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 25
Alternative name(s):
Activator interaction domain-containing protein 1
Activator-recruited cofactor 92 kDa component
Short name:
ARC92
Mediator complex subunit 25
p78
Gene namesi
Name:MED25
Synonyms:ACID1, ARC92, PTOV2
ORF Names:TCBAP0758
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:28845. MED25.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease 2B21 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA recessive axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.

See also OMIM:605589
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti335 – 3351A → V in CMT2B2. 1 Publication
Corresponds to variant rs145770066 [ dbSNP | Ensembl ].
VAR_063521

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi646 – 6461L → A: Abrogates interaction with RARA. 1 Publication
Mutagenesisi649 – 6502LL → AA: Abrogates interaction with RARA. 1 Publication

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi605589. phenotype.
Orphaneti101101. Charcot-Marie-Tooth disease type 2B2.
PharmGKBiPA134984839.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747Mediator of RNA polymerase II transcription subunit 25PRO_0000304952Add
BLAST

Proteomic databases

MaxQBiQ71SY5.
PaxDbiQ71SY5.
PRIDEiQ71SY5.

PTM databases

PhosphoSiteiQ71SY5.

Expressioni

Tissue specificityi

Ubiquitously expressed. Highest levels in brain, heart, kidney, peripheral leukocytes, placenta, skeletal muscle and spleen.2 Publications

Gene expression databases

BgeeiQ71SY5.
CleanExiHS_MED25.
ExpressionAtlasiQ71SY5. baseline and differential.
GenevestigatoriQ71SY5.

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. Interacts with CREBBP. Interacts with ESR1, GR, RARA, RXRA and THRB in a ligand-dependent fashion. Binds the Herpes simplex virus activator VP16.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MED15Q96RN52EBI-394558,EBI-394506
MED16Q9Y2X02EBI-394558,EBI-394541
RARAP1027610EBI-394558,EBI-413374
RXRAP197934EBI-394558,EBI-78598
RxraP287003EBI-394558,EBI-346715From a different organism.

Protein-protein interaction databases

BioGridi123607. 42 interactions.
DIPiDIP-31454N.
IntActiQ71SY5. 20 interactions.
MINTiMINT-5209896.

Structurei

Secondary structure

1
747
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi396 – 40914Combined sources
Beta strandi414 – 4174Combined sources
Beta strandi424 – 43411Combined sources
Helixi441 – 4433Combined sources
Beta strandi446 – 4549Combined sources
Helixi455 – 4617Combined sources
Helixi462 – 4654Combined sources
Beta strandi466 – 47510Combined sources
Beta strandi476 – 4783Combined sources
Helixi480 – 49314Combined sources
Beta strandi494 – 4996Combined sources
Beta strandi504 – 5074Combined sources
Beta strandi510 – 5156Combined sources
Turni517 – 5193Combined sources
Beta strandi521 – 5299Combined sources
Helixi530 – 54516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KY6NMR-A391-553[»]
2L23NMR-A391-548[»]
2L6UNMR-A391-543[»]
2XNFNMR-A394-543[»]
ProteinModelPortaliQ71SY5.
SMRiQ71SY5. Positions 391-553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ71SY5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 226226Interaction with the Mediator complexAdd
BLAST
Regioni389 – 543155Interaction with VP16Add
BLAST
Regioni395 – 545151Interaction with CREBBPAdd
BLAST
Regioni564 – 65390Interaction with RARAAdd
BLAST
Regioni640 – 70768Interaction with RARAAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi646 – 6505LXXLL motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi200 – 381182Pro-richAdd
BLAST
Compositional biasi565 – 735171Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the Mediator complex subunit 25 family.Curated

Phylogenomic databases

eggNOGiNOG79607.
GeneTreeiENSGT00520000055653.
HOVERGENiHBG108127.
InParanoidiQ71SY5.
KOiK15168.
OMAiPRFSPIN.
OrthoDBiEOG78H3SP.
PhylomeDBiQ71SY5.
TreeFamiTF329598.

Family and domain databases

InterProiIPR021394. Mediator_Med25.
IPR021406. Mediator_Med25_NR-box.
IPR021397. Mediator_Med25_SD1.
IPR021419. Mediator_Med25_VWA.
IPR002035. VWF_A.
[Graphical view]
PfamiPF11232. Med25. 1 hit.
PF11244. Med25_NR-box. 1 hit.
PF11235. Med25_SD1. 1 hit.
PF11265. Med25_VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q71SY5-1) [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
MVPGSEGPAR AGSVVADVVF VIEGTANLGP YFEGLRKHYL LPAIEYFNGG
60 70 80 90 100
PPAETDFGGD YGGTQYSLVV FNTVDCAPES YVQCHAPTSS AYEFVTWLDG
110 120 130 140 150
IKFMGGGGES CSLIAEGLST ALQLFDDFKK MREQIGQTHR VCLLICNSPP
160 170 180 190 200
YLLPAVESTT YSGCTTENLV QQIGERGIHF SIVSPRKLPA LRLLFEKAAP
210 220 230 240 250
PALLEPLQPP TDVSQDPRHM VLVRGLVLPV GGGSAPGPLQ SKQPVPLPPA
260 270 280 290 300
APSGATLSAA PQQPLPPVPP QYQVPGNLSA AQVAAQNAVE AAKNQKAGLG
310 320 330 340 350
PRFSPITPLQ QAAPGVGPPF SQAPAPQLPP GPPGAPKPPP ASQPSLVSTV
360 370 380 390 400
APGSGLAPTA QPGAPSMAGT VAPGGVSGPS PAQLGAPALG GQQSVSNKLL
410 420 430 440 450
AWSGVLEWQE KPKPASVDAN TKLTRSLPCQ VYVNHGENLK TEQWPQKLIM
460 470 480 490 500
QLIPQQLLTT LGPLFRNSRM VQFHFTNKDL ESLKGLYRIM GNGFAGCVHF
510 520 530 540 550
PHTAPCEVRV LMLLYSSKKK IFMGLIPYDQ SGFVNGIRQV ITNHKQVQQQ
560 570 580 590 600
KLEQQQRGMG GQQAPPGLGP ILEDQARPSQ NLLQLRPPQP QPQGTVGASG
610 620 630 640 650
ATGQPQPQGT AQPPPGAPQG PPGAASGPPP PGPILRPQNP GANPQLRSLL
660 670 680 690 700
LNPPPPQTGV PPPQASLHHL QPPGAPALLP PPHQGLGQPQ LGPPLLHPPP
710 720 730 740
AQSWPAQLPP RAPLPGQMLL SGGPRGPVPQ PGLQPSVMED DILMDLI
Length:747
Mass (Da):78,171
Last modified:October 2, 2007 - v2
Checksum:i6FE13FB45786402D
GO
Isoform 2 (identifier: Q71SY5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     671-747: QPPGAPALLP...MEDDILMDLI → PSPGPHNFPL...ESPTPNKVPF

Show »
Length:754
Mass (Da):78,882
Checksum:i0E8022B21685A1EE
GO
Isoform 3 (identifier: Q71SY5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     701-747: AQSWPAQLPP...MEDDILMDLI → PATRGSCAAA...VERIQPETPL

Note: No experimental confirmation available.

Show »
Length:796
Mass (Da):82,972
Checksum:i930FD1BDBEED7BA1
GO
Isoform 4 (identifier: Q71SY5-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     716-747: GQMLLSGGPRGPVPQPGLQPSVMEDDILMDLI → AAKRKREGEG...IRARPIWPDP

Note: No experimental confirmation available.

Show »
Length:793
Mass (Da):84,389
Checksum:i4F9597470EB0E517
GO
Isoform 5 (identifier: Q71SY5-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     303-319: Missing.

Note: No experimental confirmation available.

Show »
Length:730
Mass (Da):76,512
Checksum:i70D41D4F28B8A709
GO
Isoform 6 (identifier: Q71SY5-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-273: Missing.

Show »
Length:534
Mass (Da):55,456
Checksum:iD49EA118755469AC
GO

Sequence cautioni

The sequence AAG15589.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB66680.1 differs from that shown. Reason: Frameshift at position 567. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201F → S in AAM20739. (PubMed:12163014)Curated
Sequence conflicti236 – 2361P → L in CAE84581. (PubMed:14657022)Curated
Sequence conflicti236 – 2361P → L in CAB66680. 1 PublicationCurated
Sequence conflicti268 – 2681V → I in AAM20739. (PubMed:12163014)Curated
Sequence conflicti514 – 5141L → M in AAS45401. (PubMed:14983011)Curated
Sequence conflicti536 – 5361G → D in AAS45401. (PubMed:14983011)Curated
Sequence conflicti703 – 7031S → F in AAM20739. (PubMed:12163014)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti335 – 3351A → V in CMT2B2. 1 Publication
Corresponds to variant rs145770066 [ dbSNP | Ensembl ].
VAR_063521

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei61 – 273213Missing in isoform 6. 1 PublicationVSP_047570Add
BLAST
Alternative sequencei303 – 31917Missing in isoform 5. 1 PublicationVSP_028143Add
BLAST
Alternative sequencei671 – 74777QPPGA…LMDLI → PSPGPHNFPLGLHCQVRGPG GGQRSGLSVPAAPGLEHQDQ VLLGSKDIGSKNEGSPSRAC SPASWRTTSSWISSESPTPN KVPF in isoform 2. 2 PublicationsVSP_028144Add
BLAST
Alternative sequencei701 – 74747AQSWP…LMDLI → PATRGSCAAASAAPGPGAAP VGAPTPASTTCPVLARTTSP SGSTASGKTKERRRGPCVSR KMGASLFLCGSEEHAYVFNM QTNRVCVERIQPETPL in isoform 3. 1 PublicationVSP_028145Add
BLAST
Alternative sequencei716 – 74732GQMLL…LMDLI → AAKRKREGEGRVFREKWERA YFFVEVKSMPMCLICKQIVS VLKEYNLKRHYESKHSKSYD QYTEQTRRIRARPIWPDP in isoform 4. 1 PublicationVSP_028146Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF261072 mRNA. Translation: AAM20739.1.
AJ617479 mRNA. Translation: CAE84581.1.
AY533507 mRNA. Translation: AAS45401.1.
AL136746 mRNA. Translation: CAB66680.1. Frameshift.
EU392500 mRNA. Translation: ACB88862.1.
AK289460 mRNA. Translation: BAF82149.1.
AC006942 Genomic DNA. Translation: AAD15565.1.
AC018766 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52546.1.
BC024312 mRNA. Translation: AAH24312.2.
BC065297 mRNA. Translation: AAH65297.1.
AF283769 mRNA. Translation: AAG15589.1. Different initiation.
CCDSiCCDS33075.1. [Q71SY5-1]
RefSeqiNP_112235.2. NM_030973.3. [Q71SY5-1]
UniGeneiHs.656639.
Hs.745568.

Genome annotation databases

EnsembliENST00000312865; ENSP00000326767; ENSG00000104973. [Q71SY5-1]
ENST00000538643; ENSP00000437496; ENSG00000104973. [Q71SY5-6]
GeneIDi81857.
KEGGihsa:81857.
UCSCiuc002ppw.2. human. [Q71SY5-1]
uc002ppx.1. human. [Q71SY5-4]

Polymorphism databases

DMDMi158706143.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF261072 mRNA. Translation: AAM20739.1.
AJ617479 mRNA. Translation: CAE84581.1.
AY533507 mRNA. Translation: AAS45401.1.
AL136746 mRNA. Translation: CAB66680.1. Frameshift.
EU392500 mRNA. Translation: ACB88862.1.
AK289460 mRNA. Translation: BAF82149.1.
AC006942 Genomic DNA. Translation: AAD15565.1.
AC018766 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52546.1.
BC024312 mRNA. Translation: AAH24312.2.
BC065297 mRNA. Translation: AAH65297.1.
AF283769 mRNA. Translation: AAG15589.1. Different initiation.
CCDSiCCDS33075.1. [Q71SY5-1]
RefSeqiNP_112235.2. NM_030973.3. [Q71SY5-1]
UniGeneiHs.656639.
Hs.745568.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KY6NMR-A391-553[»]
2L23NMR-A391-548[»]
2L6UNMR-A391-543[»]
2XNFNMR-A394-543[»]
ProteinModelPortaliQ71SY5.
SMRiQ71SY5. Positions 391-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123607. 42 interactions.
DIPiDIP-31454N.
IntActiQ71SY5. 20 interactions.
MINTiMINT-5209896.

PTM databases

PhosphoSiteiQ71SY5.

Polymorphism databases

DMDMi158706143.

Proteomic databases

MaxQBiQ71SY5.
PaxDbiQ71SY5.
PRIDEiQ71SY5.

Protocols and materials databases

DNASUi81857.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312865; ENSP00000326767; ENSG00000104973. [Q71SY5-1]
ENST00000538643; ENSP00000437496; ENSG00000104973. [Q71SY5-6]
GeneIDi81857.
KEGGihsa:81857.
UCSCiuc002ppw.2. human. [Q71SY5-1]
uc002ppx.1. human. [Q71SY5-4]

Organism-specific databases

CTDi81857.
GeneCardsiGC19P050321.
GeneReviewsiMED25.
H-InvDBHIX0015345.
HGNCiHGNC:28845. MED25.
MIMi605589. phenotype.
610197. gene.
neXtProtiNX_Q71SY5.
Orphaneti101101. Charcot-Marie-Tooth disease type 2B2.
PharmGKBiPA134984839.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG79607.
GeneTreeiENSGT00520000055653.
HOVERGENiHBG108127.
InParanoidiQ71SY5.
KOiK15168.
OMAiPRFSPIN.
OrthoDBiEOG78H3SP.
PhylomeDBiQ71SY5.
TreeFamiTF329598.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMED25. human.
EvolutionaryTraceiQ71SY5.
GeneWikiiMED25.
GenomeRNAii81857.
NextBioi35482117.
PROiQ71SY5.
SOURCEiSearch...

Gene expression databases

BgeeiQ71SY5.
CleanExiHS_MED25.
ExpressionAtlasiQ71SY5. baseline and differential.
GenevestigatoriQ71SY5.

Family and domain databases

InterProiIPR021394. Mediator_Med25.
IPR021406. Mediator_Med25_NR-box.
IPR021397. Mediator_Med25_SD1.
IPR021419. Mediator_Med25_VWA.
IPR002035. VWF_A.
[Graphical view]
PfamiPF11232. Med25. 1 hit.
PF11244. Med25_NR-box. 1 hit.
PF11235. Med25_SD1. 1 hit.
PF11265. Med25_VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A prostate-derived cDNA that is mapped to human chromosome 19 encodes a novel protein."
    Wang C., McCarty I.M., Balazs L., Li Y., Steiner M.S.
    Biochem. Biophys. Res. Commun. 296:281-287(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "A novel docking site on Mediator is critical for activation by VP16 in mammalian cells."
    Mittler G., Stuehler T., Santolin L., Uhlmann T., Kremmer E., Lottspeich F., Berti L., Meisterernst M.
    EMBO J. 22:6494-6504(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION WITH VP16, ASSOCIATION WITH PROMOTER REGIONS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  3. "The activator-recruited cofactor/Mediator coactivator subunit ARC92 is a functionally important target of the VP16 transcriptional activator."
    Yang F., DeBeaumont R., Zhou S., Naeaer A.M.
    Proc. Natl. Acad. Sci. U.S.A. 101:2339-2344(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PROTEIN SEQUENCE OF 1-11; 197-207; 241-254; 398-446 AND 520-530, FUNCTION, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION WITH VP16, TISSUE SPECIFICITY.
  4. "Alternative splicing as a prevalent mechanism in regulating mammalian mediator tail subcomplex activity."
    Kivil A., Kazantseva A., Vinkel K.J.M., Sadam H., Neuman T., Palm K.
    Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), ALTERNATIVE SPLICING.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-747 (ISOFORM 5).
    Tissue: Eye and Lung.
  10. "Pediatric leukemia cDNA sequencing project."
    Villalon D.K., Luna R.A., Margolin J.K., Tsang Y.T.M., Hale S.M., Mei G., Bouck J., Gibbs R.A.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-747 (ISOFORM 4).
    Tissue: Leukocyte.
  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. "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: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  13. "MED25 is distinct from TRAP220/MED1 in cooperating with CBP for retinoid receptor activation."
    Lee H.-K., Park U.-H., Kim E.-J., Um S.-J.
    EMBO J. 26:3545-3557(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH PROMOTER REGIONS, INTERACTION WITH CREBBP; ESR1; GR; MED1; MED6; RARA; RXRA AND THRB, MUTAGENESIS OF LEU-646 AND 649-LEU-LEU-650.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: STRUCTURE BY NMR OF 391-548.
  16. "Identification of the variant Ala335Val of MED25 as responsible for CMT2B2: molecular data, functional studies of the SH3 recognition motif and correlation between wild-type MED25 and PMP22 RNA levels in CMT1A animal models."
    Leal A., Huehne K., Bauer F., Sticht H., Berger P., Suter U., Morera B., Del Valle G., Lupski J.R., Ekici A., Pasutto F., Endele S., Barrantes R., Berghoff C., Berghoff M., Neundoerfer B., Heuss D., Dorn T.
    , Young P., Santolin L., Uhlmann T., Meisterernst M., Sereda M.W., Sereda M., Stassart R.M., Zu Horste G.M., Nave K.A., Reis A., Rautenstrauss B.
    Neurogenetics 10:275-287(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2B2 VAL-335.

Entry informationi

Entry nameiMED25_HUMAN
AccessioniPrimary (citable) accession number: Q71SY5
Secondary accession number(s): A8K095
, B9TX30, O95783, Q6P143, Q6QMH5, Q707U4, Q8TB55, Q9H0L5, Q9HB34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: January 7, 2015
This is version 87 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.