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Q71SY5 (MED25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MED25
Synonyms:ACID1, ARC92, PTOV2
ORF Names:TCBAP0758
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.3 Ref.13

Subunit structure

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. Ref.2 Ref.3 Ref.11 Ref.12 Ref.13

Subcellular location

Nucleus Ref.2.

Tissue specificity

Ubiquitously expressed. Highest levels in brain, heart, kidney, peripheral leukocytes, placenta, skeletal muscle and spleen. Ref.2 Ref.3

Involvement in disease

Charcot-Marie-Tooth disease 2B2 (CMT2B2) [MIM:605589]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Belongs to the Mediator complex subunit 25 family.

Sequence caution

The sequence AAG15589.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB66680.1 differs from that shown. Reason: Frameshift at position 567.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Neurodegeneration
Neuropathy
   Molecular functionActivator
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processgene expression

Traceable author statement. Source: Reactome

negative regulation of fibroblast proliferation

Inferred from mutant phenotype Ref.13. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of cell cycle arrest

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of chromatin binding

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of mediator complex assembly

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.13. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionretinoic acid receptor binding

Inferred from physical interaction Ref.13. Source: UniProtKB

retinoid X receptor binding

Inferred from physical interaction Ref.13. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RARAP1027610EBI-394558,EBI-413374
RXRAP197934EBI-394558,EBI-78598
RxraP287003EBI-394558,EBI-346715From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q71SY5-1)

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.
Isoform 2 (identifier: Q71SY5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     671-747: QPPGAPALLP...MEDDILMDLI → PSPGPHNFPL...ESPTPNKVPF
Isoform 3 (identifier: Q71SY5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     701-747: AQSWPAQLPP...MEDDILMDLI → PATRGSCAAA...VERIQPETPL
Note: No experimental confirmation available.
Isoform 4 (identifier: Q71SY5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     716-747: GQMLLSGGPRGPVPQPGLQPSVMEDDILMDLI → AAKRKREGEG...IRARPIWPDP
Note: No experimental confirmation available.
Isoform 5 (identifier: Q71SY5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     303-319: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q71SY5-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 747747Mediator of RNA polymerase II transcription subunit 25
PRO_0000304952

Regions

Region1 – 226226Interaction with the Mediator complex
Region389 – 543155Interaction with VP16
Region395 – 545151Interaction with CREBBP
Region564 – 65390Interaction with RARA
Region640 – 70768Interaction with RARA
Motif646 – 6505LXXLL motif
Compositional bias200 – 381182Pro-rich
Compositional bias565 – 735171Pro-rich

Natural variations

Alternative sequence61 – 273213Missing in isoform 6.
VSP_047570
Alternative sequence303 – 31917Missing in isoform 5.
VSP_028143
Alternative sequence671 – 74777QPPGA…LMDLI → PSPGPHNFPLGLHCQVRGPG GGQRSGLSVPAAPGLEHQDQ VLLGSKDIGSKNEGSPSRAC SPASWRTTSSWISSESPTPN KVPF in isoform 2.
VSP_028144
Alternative sequence701 – 74747AQSWP…LMDLI → PATRGSCAAASAAPGPGAAP VGAPTPASTTCPVLARTTSP SGSTASGKTKERRRGPCVSR KMGASLFLCGSEEHAYVFNM QTNRVCVERIQPETPL in isoform 3.
VSP_028145
Alternative sequence716 – 74732GQMLL…LMDLI → AAKRKREGEGRVFREKWERA YFFVEVKSMPMCLICKQIVS VLKEYNLKRHYESKHSKSYD QYTEQTRRIRARPIWPDP in isoform 4.
VSP_028146
Natural variant3351A → V in CMT2B2. Ref.16
Corresponds to variant rs145770066 [ dbSNP | Ensembl ].
VAR_063521

Experimental info

Mutagenesis6461L → A: Abrogates interaction with RARA. Ref.13
Mutagenesis649 – 6502LL → AA: Abrogates interaction with RARA.
Sequence conflict201F → S in AAM20739. Ref.1
Sequence conflict2361P → L in CAE84581. Ref.2
Sequence conflict2361P → L in CAB66680. Ref.4
Sequence conflict2681V → I in AAM20739. Ref.1
Sequence conflict5141L → M in AAS45401. Ref.3
Sequence conflict5361G → D in AAS45401. Ref.3
Sequence conflict7031S → F in AAM20739. Ref.1

Secondary structure

........................... 747
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 6FE13FB45786402D

FASTA74778,171
        10         20         30         40         50         60 
MVPGSEGPAR AGSVVADVVF VIEGTANLGP YFEGLRKHYL LPAIEYFNGG PPAETDFGGD 

        70         80         90        100        110        120 
YGGTQYSLVV FNTVDCAPES YVQCHAPTSS AYEFVTWLDG IKFMGGGGES CSLIAEGLST 

       130        140        150        160        170        180 
ALQLFDDFKK MREQIGQTHR VCLLICNSPP YLLPAVESTT YSGCTTENLV QQIGERGIHF 

       190        200        210        220        230        240 
SIVSPRKLPA LRLLFEKAAP PALLEPLQPP TDVSQDPRHM VLVRGLVLPV GGGSAPGPLQ 

       250        260        270        280        290        300 
SKQPVPLPPA APSGATLSAA PQQPLPPVPP QYQVPGNLSA AQVAAQNAVE AAKNQKAGLG 

       310        320        330        340        350        360 
PRFSPITPLQ QAAPGVGPPF SQAPAPQLPP GPPGAPKPPP ASQPSLVSTV APGSGLAPTA 

       370        380        390        400        410        420 
QPGAPSMAGT VAPGGVSGPS PAQLGAPALG GQQSVSNKLL AWSGVLEWQE KPKPASVDAN 

       430        440        450        460        470        480 
TKLTRSLPCQ VYVNHGENLK TEQWPQKLIM QLIPQQLLTT LGPLFRNSRM VQFHFTNKDL 

       490        500        510        520        530        540 
ESLKGLYRIM GNGFAGCVHF PHTAPCEVRV LMLLYSSKKK IFMGLIPYDQ SGFVNGIRQV 

       550        560        570        580        590        600 
ITNHKQVQQQ KLEQQQRGMG GQQAPPGLGP ILEDQARPSQ NLLQLRPPQP QPQGTVGASG 

       610        620        630        640        650        660 
ATGQPQPQGT AQPPPGAPQG PPGAASGPPP PGPILRPQNP GANPQLRSLL LNPPPPQTGV 

       670        680        690        700        710        720 
PPPQASLHHL QPPGAPALLP PPHQGLGQPQ LGPPLLHPPP AQSWPAQLPP RAPLPGQMLL 

       730        740 
SGGPRGPVPQ PGLQPSVMED DILMDLI 

« Hide

Isoform 2 [UniParc].

Checksum: 0E8022B21685A1EE
Show »

FASTA75478,882
Isoform 3 [UniParc].

Checksum: 930FD1BDBEED7BA1
Show »

FASTA79682,972
Isoform 4 [UniParc].

Checksum: 4F9597470EB0E517
Show »

FASTA79384,389
Isoform 5 [UniParc].

Checksum: 70D41D4F28B8A709
Show »

FASTA73076,512
Isoform 6 [UniParc].

Checksum: D49EA118755469AC
Show »

FASTA53455,456

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"NMR structure of the human Mediator MED25 ACID domain."
Bontems F., Verger A., Dewitte F., Lens Z., Baert J.L., Ferreira E., Launoit Y.D., Sizun C., Guittet E., Villeret V., Monte D.
J. Struct. Biol. 174:245-251(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
[17]Erratum
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. expand/collapse author list , 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 10:375-376(2009)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_112235.2. NM_030973.3.
UniGeneHs.656639.
Hs.745568.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KY6NMR-A391-553[»]
2L23NMR-A391-548[»]
2L6UNMR-A391-543[»]
2XNFNMR-A394-543[»]
ProteinModelPortalQ71SY5.
SMRQ71SY5. Positions 391-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123607. 43 interactions.
DIPDIP-31454N.
IntActQ71SY5. 15 interactions.
MINTMINT-5209896.

PTM databases

PhosphoSiteQ71SY5.

Polymorphism databases

DMDM158706143.

Proteomic databases

PaxDbQ71SY5.
PRIDEQ71SY5.

Protocols and materials databases

DNASU81857.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312865; ENSP00000326767; ENSG00000104973. [Q71SY5-1]
ENST00000538643; ENSP00000437496; ENSG00000104973. [Q71SY5-6]
GeneID81857.
KEGGhsa:81857.
UCSCuc002ppw.2. human. [Q71SY5-1]
uc002ppx.1. human. [Q71SY5-4]

Organism-specific databases

CTD81857.
GeneCardsGC19P050321.
H-InvDBHIX0015345.
HGNCHGNC:28845. MED25.
MIM605589. phenotype.
610197. gene.
neXtProtNX_Q71SY5.
Orphanet101101. Charcot-Marie-Tooth disease type 2B2.
PharmGKBPA134984839.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG79607.
HOVERGENHBG108127.
KOK15168.
OMAPGQMLLS.
OrthoDBEOG78H3SP.
PhylomeDBQ71SY5.
TreeFamTF329598.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ71SY5.
BgeeQ71SY5.
CleanExHS_MED25.
GenevestigatorQ71SY5.

Family and domain databases

InterProIPR021394. Mediator_Med25.
IPR021406. Mediator_Med25_NR-box.
IPR021397. Mediator_Med25_SD1.
IPR021419. Mediator_Med25_VWA.
IPR002035. VWF_A.
[Graphical view]
PfamPF11232. Med25. 1 hit.
PF11244. Med25_NR-box. 1 hit.
PF11235. Med25_SD1. 1 hit.
PF11265. Med25_VWA. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMED25. human.
EvolutionaryTraceQ71SY5.
GeneWikiMED25.
GenomeRNAi81857.
NextBio35482117.
PROQ71SY5.
SOURCESearch...

Entry information

Entry nameMED25_HUMAN
AccessionPrimary (citable) accession number: Q71SY5
Secondary accession number(s): A8K095 expand/collapse secondary AC list , B9TX30, O95783, Q6P143, Q6QMH5, Q707U4, Q8TB55, Q9H0L5, Q9HB34
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: April 16, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM