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Protein

Mediator of RNA polymerase II transcription subunit 15

Gene

MED15

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 cholesterol-dependent gene regulation. Positively regulates the Nodal signaling pathway.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-212436. Generic Transcription Pathway.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 15
Alternative name(s):
Activator-recruited cofactor 105 kDa component
Short name:
ARC105
CTG repeat protein 7a
Mediator complex subunit 15
Positive cofactor 2 glutamine/Q-rich-associated protein
Short name:
PC2 glutamine/Q-rich-associated protein
TPA-inducible gene 1 protein
Short name:
TIG-1
Trinucleotide repeat-containing gene 7 protein
Gene namesi
Name:MED15
Synonyms:ARC105, CTG7A, PCQAP, TIG1, TNRC7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:14248. MED15.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • mediator complex Source: InterPro
  • membrane Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421E → A: Abrogates interaction with SREBF1. 1 Publication
Mutagenesisi58 – 581L → D: Abrogates interaction with SREBF1. 1 Publication
Mutagenesisi60 – 601A → D: Abrogates interaction with SREBF1. 1 Publication

Organism-specific databases

PharmGKBiPA33088.

Polymorphism and mutation databases

BioMutaiMED15.
DMDMi27734440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 788788Mediator of RNA polymerase II transcription subunit 15PRO_0000058264Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei603 – 6031PhosphothreonineCombined sources

Post-translational modificationi

Ubiquitinated by TRIM11, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96RN5.
MaxQBiQ96RN5.
PaxDbiQ96RN5.
PeptideAtlasiQ96RN5.
PRIDEiQ96RN5.

PTM databases

iPTMnetiQ96RN5.
PhosphoSiteiQ96RN5.

Expressioni

Tissue specificityi

Expressed in all tissues examined, including heart, brain, lung, spleen, thymus, pancreas, blood leukocyte and placenta. However, the level of expression varied, with highest expression in the placenta and peripheral blood and lowest in the pancreas and kidney.1 Publication

Inductioni

By 12-O-tetradecanoylphorbol-13-acetate (TPA).1 Publication

Gene expression databases

BgeeiQ96RN5.
CleanExiHS_MED15.
ExpressionAtlasiQ96RN5. baseline and differential.
GenevisibleiQ96RN5. HS.

Organism-specific databases

HPAiHPA003179.

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 SMAD2, SMAD3, SREBF1 and SREBF2. Interacts with WWTR1. Interacts with TRIM11.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428583EBI-394506,EBI-466029
MED14O602442EBI-394506,EBI-394489
MED25Q71SY52EBI-394506,EBI-394558
SREBF1P36956-16EBI-394506,EBI-948328
TRIM11Q96F445EBI-394506,EBI-851809

Protein-protein interaction databases

BioGridi119623. 64 interactions.
DIPiDIP-32908N.
IntActiQ96RN5. 34 interactions.
MINTiMINT-243991.
STRINGi9606.ENSP00000263205.

Structurei

Secondary structure

1
788
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 3018Combined sources
Helixi38 – 4811Combined sources
Helixi52 – 7120Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GUTNMR-A5-78[»]
ProteinModelPortaliQ96RN5.
SMRiQ96RN5. Positions 5-78.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96RN5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 7365Interaction with SREBF1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi547 – 56418Nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi161 – 17414Poly-GlnAdd
BLAST
Compositional biasi178 – 19316Poly-GlnAdd
BLAST
Compositional biasi205 – 21814Poly-GlnAdd
BLAST
Compositional biasi226 – 23914Poly-GlnAdd
BLAST
Compositional biasi243 – 26220Poly-GlnAdd
BLAST
Compositional biasi266 – 515250Pro-richAdd
BLAST
Compositional biasi360 – 3678Poly-Gln
Compositional biasi449 – 4568Poly-Pro
Compositional biasi602 – 61110Poly-Pro

Sequence similaritiesi

Belongs to the Mediator complex subunit 15 family.Curated

Phylogenomic databases

eggNOGiKOG4274. Eukaryota.
ENOG410YKAW. LUCA.
GeneTreeiENSGT00730000111140.
HOVERGENiHBG053529.
InParanoidiQ96RN5.
KOiK15157.
OMAiPPITXAN.
OrthoDBiEOG7353WV.
PhylomeDBiQ96RN5.
TreeFamiTF324988.

Family and domain databases

InterProiIPR019087. Med15.
[Graphical view]
PfamiPF09606. Med15. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96RN5-1) [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
MDVSGQETDW RSTAFRQKLV SQIEDAMRKA GVAHSKSSKD MESHVFLKAK
60 70 80 90 100
TRDEYLSLVA RLIIHFRDIH NKKSQASVSD PMNALQSLTG GPAAGAAGIG
110 120 130 140 150
MPPRGPGQSL GGMGSLGAMG QPMSLSGQPP PGTSGMAPHS MAVVSTATPQ
160 170 180 190 200
TQLQLQQVAL QQQQQQQQFQ QQQQAALQQQ QQQQQQQQFQ AQQSAMQQQF
210 220 230 240 250
QAVVQQQQQL QQQQQQQQHL IKLHHQNQQQ IQQQQQQLQR IAQLQLQQQQ
260 270 280 290 300
QQQQQQQQQQ QQALQAQPPI QQPPMQQPQP PPSQALPQQL QQMHHTQHHQ
310 320 330 340 350
PPPQPQQPPV AQNQPSQLPP QSQTQPLVSQ AQALPGQMLY TQPPLKFVRA
360 370 380 390 400
PMVVQQPPVQ PQVQQQQTAV QTAQAAQMVA PGVQMITEAL AQGGMHIRAR
410 420 430 440 450
FPPTTAVSAI PSSSIPLGRQ PMAQVSQSSL PMLSSPSPGQ QVQTPQSMPP
460 470 480 490 500
PPQPSPQPGQ PSSQPNSNVS SGPAPSPSSF LPSPSPQPSQ SPVTARTPQN
510 520 530 540 550
FSVPSPGPLN TPVNPSSVMS PAGSSQAEEQ QYLDKLKQLS KYIEPLRRMI
560 570 580 590 600
NKIDKNEDRK KDLSKMKSLL DILTDPSKRC PLKTLQKCEI ALEKLKNDMA
610 620 630 640 650
VPTPPPPPVP PTKQQYLCQP LLDAVLANIR SPVFNHSLYR TFVPAMTAIH
660 670 680 690 700
GPPITAPVVC TRKRRLEDDE RQSIPSVLQG EVARLDPKFL VNLDPSHCSN
710 720 730 740 750
NGTVHLICKL DDKDLPSVPP LELSVPADYP AQSPLWIDRQ WQYDANPFLQ
760 770 780
SVHRCMTSRL LQLPDKHSVT ALLNTWAQSV HQACLSAA
Length:788
Mass (Da):86,753
Last modified:January 10, 2003 - v2
Checksum:iBB6AC6C63ED2F97E
GO
Isoform 2 (identifier: Q96RN5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     385-424: Missing.

Show »
Length:748
Mass (Da):82,581
Checksum:i436AD762713DCC63
GO
Isoform 3 (identifier: Q96RN5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     80-151: DPMNALQSLTGGPAAGAAGIGMPPRGPGQSLGGMGSLGAMGQPMSLSGQPPPGTSGMAPHSMAVVSTATPQT → A
     385-424: Missing.

Note: No experimental confirmation available.
Show »
Length:677
Mass (Da):75,927
Checksum:iC5DBE759F22901CB
GO

Sequence cautioni

The sequence AAC12944.1 differs from that shown. Reason: Frameshift at positions 13, 600 and 749. Curated
The sequence BAB85034.1 differs from that shown.Several sequencing errors.Curated
The sequence BAC03446.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121S → R in AAC12944 (PubMed:11024300).Curated
Sequence conflicti116 – 1161L → F in AAC12944 (PubMed:11024300).Curated
Sequence conflicti154 – 1541Q → H in BAC03446 (PubMed:14702039).Curated
Sequence conflicti161 – 1611Q → R in BAB85034 (PubMed:14702039).Curated
Sequence conflicti185 – 1862QQ → EL in AAB91443 (PubMed:9225980).Curated
Sequence conflicti186 – 1872Missing in CAG30423 (PubMed:15461802).Curated
Sequence conflicti218 – 2181Missing in CAG30423 (PubMed:15461802).Curated
Sequence conflicti232 – 28756Missing in BAB85034 (PubMed:14702039).CuratedAdd
BLAST
Sequence conflicti265 – 2651Q → E in AAC12944 (PubMed:11024300).Curated
Sequence conflicti265 – 2651Q → E in AAB91443 (PubMed:9225980).Curated
Sequence conflicti572 – 5732IL → GI in AAB91443 (PubMed:9225980).Curated
Sequence conflicti685 – 6851L → V in BAB85034 (PubMed:14702039).Curated

Polymorphismi

The poly-Gln region from amino acids 235-262 of PCQAP is polymorphic. There are from 15 to 18 repeats in the Italian population.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti261 – 2622Missing .
VAR_013136

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei80 – 15172DPMNA…ATPQT → A in isoform 3. 1 PublicationVSP_013024Add
BLAST
Alternative sequencei385 – 42440Missing in isoform 2 and isoform 3. 6 PublicationsVSP_003922Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056191 mRNA. Translation: AAC12944.1. Frameshift.
AF328769 mRNA. Translation: AAK58423.1.
AK074268 mRNA. Translation: BAB85034.1. Sequence problems.
AK090465 mRNA. Translation: BAC03446.1. Different initiation.
CR456537 mRNA. Translation: CAG30423.1.
CH471176 Genomic DNA. Translation: EAX02951.1.
CH471176 Genomic DNA. Translation: EAX02952.1.
CH471176 Genomic DNA. Translation: EAX02954.1.
CH471176 Genomic DNA. Translation: EAX02956.1.
BC007529 mRNA. Translation: AAH07529.1.
BC013985 mRNA. Translation: AAH13985.1.
U80745 mRNA. Translation: AAB91443.1.
CCDSiCCDS13781.1. [Q96RN5-2]
CCDS33602.1. [Q96RN5-1]
CCDS74824.1. [Q96RN5-3]
RefSeqiNP_001003891.1. NM_001003891.2. [Q96RN5-1]
NP_001280164.1. NM_001293235.1.
NP_001280165.1. NM_001293236.1. [Q96RN5-3]
NP_056973.2. NM_015889.4. [Q96RN5-2]
UniGeneiHs.517421.

Genome annotation databases

EnsembliENST00000263205; ENSP00000263205; ENSG00000099917. [Q96RN5-1]
ENST00000292733; ENSP00000292733; ENSG00000099917. [Q96RN5-2]
ENST00000382974; ENSP00000372434; ENSG00000099917. [Q96RN5-3]
GeneIDi51586.
KEGGihsa:51586.
UCSCiuc002zsp.4. human. [Q96RN5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Triplet repeat expansion

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056191 mRNA. Translation: AAC12944.1. Frameshift.
AF328769 mRNA. Translation: AAK58423.1.
AK074268 mRNA. Translation: BAB85034.1. Sequence problems.
AK090465 mRNA. Translation: BAC03446.1. Different initiation.
CR456537 mRNA. Translation: CAG30423.1.
CH471176 Genomic DNA. Translation: EAX02951.1.
CH471176 Genomic DNA. Translation: EAX02952.1.
CH471176 Genomic DNA. Translation: EAX02954.1.
CH471176 Genomic DNA. Translation: EAX02956.1.
BC007529 mRNA. Translation: AAH07529.1.
BC013985 mRNA. Translation: AAH13985.1.
U80745 mRNA. Translation: AAB91443.1.
CCDSiCCDS13781.1. [Q96RN5-2]
CCDS33602.1. [Q96RN5-1]
CCDS74824.1. [Q96RN5-3]
RefSeqiNP_001003891.1. NM_001003891.2. [Q96RN5-1]
NP_001280164.1. NM_001293235.1.
NP_001280165.1. NM_001293236.1. [Q96RN5-3]
NP_056973.2. NM_015889.4. [Q96RN5-2]
UniGeneiHs.517421.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GUTNMR-A5-78[»]
ProteinModelPortaliQ96RN5.
SMRiQ96RN5. Positions 5-78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119623. 64 interactions.
DIPiDIP-32908N.
IntActiQ96RN5. 34 interactions.
MINTiMINT-243991.
STRINGi9606.ENSP00000263205.

PTM databases

iPTMnetiQ96RN5.
PhosphoSiteiQ96RN5.

Polymorphism and mutation databases

BioMutaiMED15.
DMDMi27734440.

Proteomic databases

EPDiQ96RN5.
MaxQBiQ96RN5.
PaxDbiQ96RN5.
PeptideAtlasiQ96RN5.
PRIDEiQ96RN5.

Protocols and materials databases

DNASUi51586.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263205; ENSP00000263205; ENSG00000099917. [Q96RN5-1]
ENST00000292733; ENSP00000292733; ENSG00000099917. [Q96RN5-2]
ENST00000382974; ENSP00000372434; ENSG00000099917. [Q96RN5-3]
GeneIDi51586.
KEGGihsa:51586.
UCSCiuc002zsp.4. human. [Q96RN5-1]

Organism-specific databases

CTDi51586.
GeneCardsiMED15.
HGNCiHGNC:14248. MED15.
HPAiHPA003179.
MIMi607372. gene.
neXtProtiNX_Q96RN5.
PharmGKBiPA33088.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4274. Eukaryota.
ENOG410YKAW. LUCA.
GeneTreeiENSGT00730000111140.
HOVERGENiHBG053529.
InParanoidiQ96RN5.
KOiK15157.
OMAiPPITXAN.
OrthoDBiEOG7353WV.
PhylomeDBiQ96RN5.
TreeFamiTF324988.

Enzyme and pathway databases

ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-212436. Generic Transcription Pathway.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

ChiTaRSiMED15. human.
EvolutionaryTraceiQ96RN5.
GeneWikiiMED15.
GenomeRNAii51586.
PROiQ96RN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ96RN5.
CleanExiHS_MED15.
ExpressionAtlasiQ96RN5. baseline and differential.
GenevisibleiQ96RN5. HS.

Family and domain databases

InterProiIPR019087. Med15.
[Graphical view]
PfamiPF09606. Med15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel glutamine-rich putative transcriptional adaptor protein (TIG-1), preferentially expressed in placental and bone-marrow tissues."
    Abraham S., Solomon W.B.
    Gene 255:389-400(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    Tissue: Megakaryocyte and Placenta.
  2. "Isolation and characterization of a novel gene from the DiGeorge chromosomal region that encodes for a mediator subunit."
    Berti L., Mittler G., Przemeck G.K.H., Stelzer G., Guenzler B., Amati F., Conti E., Dallapiccola B., Hrabe' de Angelis M., Novelli G., Meisterernst M.
    Genomics 74:320-332(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), POLYMORPHISM OF POLY-GLN REGION.
    Tissue: Cervix carcinoma.
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Hepatoma and Spleen.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 405-788 (ISOFORM 1).
    Tissue: Eye and Kidney.
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 185-573 (ISOFORM 2).
    Tissue: Brain cortex.
  8. "Composite co-activator ARC mediates chromatin-directed transcriptional activation."
    Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.
    Nature 398:828-832(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN ARC COMPLEX, PROTEIN SEQUENCE OF 39-48 AND 525-536.
  9. "A component of the ARC/Mediator complex required for TGF beta/Nodal signalling."
    Kato Y., Habas R., Katsuyama Y., Naeaer A.M., He X.
    Nature 418:641-646(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SMAD1; SMAD2 AND SMAD3.
  10. "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.
  11. "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.
  12. "TRIM11 binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105) through the ubiquitin-proteasome system."
    Ishikawa H., Tachikawa H., Miura Y., Takahashi N.
    FEBS Lett. 580:4784-4792(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM11, UBIQUITINATION, SUBCELLULAR LOCATION.
  13. "Genome-wide location of the coactivator mediator: binding without activation and transient Cdk8 interaction on DNA."
    Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G., van de Peppel J., Werner M., Holstege F.C.P.
    Mol. Cell 22:179-192(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal."
    Varelas X., Sakuma R., Samavarchi-Tehrani P., Peerani R., Rao B.M., Dembowy J., Yaffe M.B., Zandstra P.W., Wrana J.L.
    Nat. Cell Biol. 10:837-848(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WWTR1.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. Cited for: STRUCTURE BY NMR OF 5-78, FUNCTION, INTERACTION WITH SREBF1 AND SREBF2, MUTAGENESIS OF GLU-42; LEU-58 AND ALA-60.

Entry informationi

Entry nameiMED15_HUMAN
AccessioniPrimary (citable) accession number: Q96RN5
Secondary accession number(s): D3DX31
, D3DX32, O15413, Q6IC31, Q8NF16, Q96CT0, Q96IH7, Q9P1T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: January 10, 2003
Last modified: July 6, 2016
This is version 152 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 22
    Human chromosome 22: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.