Q96RN5 (MED15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MED15
Synonyms:	ARC105, CTG7A, PCQAP, TIG1, TNRC7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	788 AA.
Sequence status	Complete.
Protein existence	Evidence 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 cholesterol-dependent gene regulation. Positively regulates the Nodal signaling pathway. Ref.9 Ref.13 Ref.14
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 SMAD2, SMAD3, SREBF1 and SREBF2. Interacts with WWTR1. Interacts with TRIM11. Ref.9 Ref.12 Ref.14 Ref.15
Subcellular location	Cytoplasm. Nucleus Ref.1 Ref.12.
Tissue specificity	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. Ref.1
Induction	By 12-O-tetradecanoylphorbol-13-acetate (TPA). Ref.1
Post-translational modification	Ubiquitinated by TRIM11, leading to proteasomal degradation. Ref.12
Polymorphism	The poly-Gln region from amino acids 235-262 of PCQAP is polymorphic. There are from 15 to 18 repeats in the Italian population.
Sequence similarities	Belongs to the Mediator complex subunit 15 family.
Sequence caution	The sequence AAC12944.1 differs from that shown. Reason: Frameshift at positions 13, 600 and 749. The sequence BAB85034.1 differs from that shown. Reason: Several sequencing errors. The sequence BAC03446.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism Triplet repeat expansion
Molecular function	Activator
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA mediator complex Inferred from electronic annotation. Source: InterPro
Molecular function	RNA polymerase II transcription cofactor activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.15. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SREBF1	P36956-1	6	EBI-394506,EBI-948328

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96RN5-1)

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: Q96RN5-2)

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

Isoform 3 (identifier: Q96RN5-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 788

788

Mediator of RNA polymerase II transcription subunit 15

PRO_0000058264

Regions

Region

9 – 73

65

Interaction with SREBF1

Motif

547 – 564

18

Nuclear localization signal Potential

Compositional bias

161 – 174

14

Poly-Gln

Compositional bias

178 – 193

16

Poly-Gln

Compositional bias

205 – 218

14

Poly-Gln

Compositional bias

226 – 239

14

Poly-Gln

Compositional bias

243 – 262

20

Poly-Gln

Compositional bias

266 – 515

250

Pro-rich

Compositional bias

360 – 367

8

Poly-Gln

Compositional bias

449 – 456

8

Poly-Pro

Compositional bias

602 – 611

10

Poly-Pro

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.17

Modified residue

603

1

Phosphothreonine Ref.16 Ref.17 Ref.18

Natural variations

Alternative sequence

80 – 151

72

DPMNA…ATPQT → A in isoform 3.

VSP_013024

Alternative sequence

385 – 424

40

Missing in isoform 2 and isoform 3.

VSP_003922

Natural variant

261 – 262

2

Missing.

VAR_013136

Experimental info

Mutagenesis

42

1

E → A: Abrogates interaction with SREBF1. Ref.14

Mutagenesis

58

1

L → D: Abrogates interaction with SREBF1. Ref.14

Mutagenesis

60

1

A → D: Abrogates interaction with SREBF1. Ref.14

Sequence conflict

12

1

S → R in AAC12944. Ref.1

Sequence conflict

116

1

L → F in AAC12944. Ref.1

Sequence conflict

154

1

Q → H in BAC03446. Ref.3

Sequence conflict

161

1

Q → R in BAB85034. Ref.3

Sequence conflict

185 – 186

2

QQ → EL in AAB91443. Ref.7

Sequence conflict

186 – 187

2

Missing in CAG30423. Ref.4

Sequence conflict

218

1

Missing in CAG30423. Ref.4

Sequence conflict

232 – 287

56

Missing in BAB85034. Ref.3

Sequence conflict

265

1

Q → E in AAC12944. Ref.1

Sequence conflict

265

1

Q → E in AAB91443. Ref.7

Sequence conflict

572 – 573

2

IL → GI in AAB91443. Ref.7

Sequence conflict

685

1

L → V in BAB85034. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

788

Helix Strand Turn

Details...

Helix

13 – 30

18

Helix

38 – 48

11

Helix

52 – 71

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 10, 2003. Version 2. Checksum: BB6AC6C63ED2F97E	FASTA	788	86,753
	10 20 30 40 50 60 MDVSGQETDW RSTAFRQKLV SQIEDAMRKA GVAHSKSSKD MESHVFLKAK TRDEYLSLVA 70 80 90 100 110 120 RLIIHFRDIH NKKSQASVSD PMNALQSLTG GPAAGAAGIG MPPRGPGQSL GGMGSLGAMG 130 140 150 160 170 180 QPMSLSGQPP PGTSGMAPHS MAVVSTATPQ TQLQLQQVAL QQQQQQQQFQ QQQQAALQQQ 190 200 210 220 230 240 QQQQQQQQFQ AQQSAMQQQF QAVVQQQQQL QQQQQQQQHL IKLHHQNQQQ IQQQQQQLQR 250 260 270 280 290 300 IAQLQLQQQQ QQQQQQQQQQ QQALQAQPPI QQPPMQQPQP PPSQALPQQL QQMHHTQHHQ 310 320 330 340 350 360 PPPQPQQPPV AQNQPSQLPP QSQTQPLVSQ AQALPGQMLY TQPPLKFVRA PMVVQQPPVQ 370 380 390 400 410 420 PQVQQQQTAV QTAQAAQMVA PGVQMITEAL AQGGMHIRAR FPPTTAVSAI PSSSIPLGRQ 430 440 450 460 470 480 PMAQVSQSSL PMLSSPSPGQ QVQTPQSMPP PPQPSPQPGQ PSSQPNSNVS SGPAPSPSSF 490 500 510 520 530 540 LPSPSPQPSQ SPVTARTPQN FSVPSPGPLN TPVNPSSVMS PAGSSQAEEQ QYLDKLKQLS 550 560 570 580 590 600 KYIEPLRRMI NKIDKNEDRK KDLSKMKSLL DILTDPSKRC PLKTLQKCEI ALEKLKNDMA 610 620 630 640 650 660 VPTPPPPPVP PTKQQYLCQP LLDAVLANIR SPVFNHSLYR TFVPAMTAIH GPPITAPVVC 670 680 690 700 710 720 TRKRRLEDDE RQSIPSVLQG EVARLDPKFL VNLDPSHCSN NGTVHLICKL DDKDLPSVPP 730 740 750 760 770 780 LELSVPADYP AQSPLWIDRQ WQYDANPFLQ SVHRCMTSRL LQLPDKHSVT ALLNTWAQSV HQACLSAA
	Isoform 2 [UniParc]. Checksum: 436AD762713DCC63	FASTA	748	82,581
	10 20 30 40 50 60 MDVSGQETDW RSTAFRQKLV SQIEDAMRKA GVAHSKSSKD MESHVFLKAK TRDEYLSLVA 70 80 90 100 110 120 RLIIHFRDIH NKKSQASVSD PMNALQSLTG GPAAGAAGIG MPPRGPGQSL GGMGSLGAMG 130 140 150 160 170 180 QPMSLSGQPP PGTSGMAPHS MAVVSTATPQ TQLQLQQVAL QQQQQQQQFQ QQQQAALQQQ 190 200 210 220 230 240 QQQQQQQQFQ AQQSAMQQQF QAVVQQQQQL QQQQQQQQHL IKLHHQNQQQ IQQQQQQLQR 250 260 270 280 290 300 IAQLQLQQQQ QQQQQQQQQQ QQALQAQPPI QQPPMQQPQP PPSQALPQQL QQMHHTQHHQ 310 320 330 340 350 360 PPPQPQQPPV AQNQPSQLPP QSQTQPLVSQ AQALPGQMLY TQPPLKFVRA PMVVQQPPVQ 370 380 390 400 410 420 PQVQQQQTAV QTAQAAQMVA PGVQVSQSSL PMLSSPSPGQ QVQTPQSMPP PPQPSPQPGQ 430 440 450 460 470 480 PSSQPNSNVS SGPAPSPSSF LPSPSPQPSQ SPVTARTPQN FSVPSPGPLN TPVNPSSVMS 490 500 510 520 530 540 PAGSSQAEEQ QYLDKLKQLS KYIEPLRRMI NKIDKNEDRK KDLSKMKSLL DILTDPSKRC 550 560 570 580 590 600 PLKTLQKCEI ALEKLKNDMA VPTPPPPPVP PTKQQYLCQP LLDAVLANIR SPVFNHSLYR 610 620 630 640 650 660 TFVPAMTAIH GPPITAPVVC TRKRRLEDDE RQSIPSVLQG EVARLDPKFL VNLDPSHCSN 670 680 690 700 710 720 NGTVHLICKL DDKDLPSVPP LELSVPADYP AQSPLWIDRQ WQYDANPFLQ SVHRCMTSRL 730 740 LQLPDKHSVT ALLNTWAQSV HQACLSAA
	Isoform 3 [UniParc]. Checksum: C5DBE759F22901CB	FASTA	677	75,927
	10 20 30 40 50 60 MDVSGQETDW RSTAFRQKLV SQIEDAMRKA GVAHSKSSKD MESHVFLKAK TRDEYLSLVA 70 80 90 100 110 120 RLIIHFRDIH NKKSQASVSA QLQLQQVALQ QQQQQQQFQQ QQQAALQQQQ QQQQQQQFQA 130 140 150 160 170 180 QQSAMQQQFQ AVVQQQQQLQ QQQQQQQHLI KLHHQNQQQI QQQQQQLQRI AQLQLQQQQQ 190 200 210 220 230 240 QQQQQQQQQQ QALQAQPPIQ QPPMQQPQPP PSQALPQQLQ QMHHTQHHQP PPQPQQPPVA 250 260 270 280 290 300 QNQPSQLPPQ SQTQPLVSQA QALPGQMLYT QPPLKFVRAP MVVQQPPVQP QVQQQQTAVQ 310 320 330 340 350 360 TAQAAQMVAP GVQVSQSSLP MLSSPSPGQQ VQTPQSMPPP PQPSPQPGQP SSQPNSNVSS 370 380 390 400 410 420 GPAPSPSSFL PSPSPQPSQS PVTARTPQNF SVPSPGPLNT PVNPSSVMSP AGSSQAEEQQ 430 440 450 460 470 480 YLDKLKQLSK YIEPLRRMIN KIDKNEDRKK DLSKMKSLLD ILTDPSKRCP LKTLQKCEIA 490 500 510 520 530 540 LEKLKNDMAV PTPPPPPVPP TKQQYLCQPL LDAVLANIRS PVFNHSLYRT FVPAMTAIHG 550 560 570 580 590 600 PPITAPVVCT RKRRLEDDER QSIPSVLQGE VARLDPKFLV NLDPSHCSNN GTVHLICKLD 610 620 630 640 650 660 DKDLPSVPPL ELSVPADYPA QSPLWIDRQW QYDANPFLQS VHRCMTSRLL QLPDKHSVTA 670 LLNTWAQSVH QACLSAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11024300] [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: 11414760] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Hepatoma and Spleen.
[4]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]	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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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]	"cDNAs with long CAG trinucleotide repeats from human brain." Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S., Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A. Hum. Genet. 100:114-122(1997) [PubMed: 9225980] [Abstract] 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: 10235267] [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: 12167862] [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: 15175163] [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: 15989967] [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: 16904669] [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: 16630888] [Abstract] Cited for: FUNCTION.
[14]	"An ARC/Mediator subunit required for SREBP control of cholesterol and lipid homeostasis." Yang F., Vought B.W., Satterlee J.S., Walker A.K., Jim Sun Z.-Y., Watts J.L., DeBeaumont R., Saito R.M., Hyberts S.G., Yang S., Macol C., Iyer L., Tjian R., van den Heuvel S., Hart A.C., Wagner G., Naeaer A.M. Nature 442:700-704(2006) [PubMed: 16799563] [Abstract] Cited for: FUNCTION, INTERACTION WITH SREBF1 AND SREBF2, MUTAGENESIS OF GLU-42; LEU-58 AND ALA-60.
[15]	"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: 18568018] [Abstract] Cited for: INTERACTION WITH WWTR1.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00107693.
IPI00220307.
IPI00554734.

RefSeq

NP_001003891.1. NM_001003891.1.
NP_056973.2. NM_015889.3.

UniGene

Hs.517421.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GUT	NMR	-	A	5-78	[»]

ProteinModelPortal

Q96RN5.

SMR

Q96RN5. Positions 5-78.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32908N.

IntAct

Q96RN5. 18 interactions.

MINT

MINT-243991.

STRING

Q96RN5.

PTM databases

PhosphoSite

Q96RN5.

Polymorphism databases

DMDM

27734440.

Proteomic databases

PRIDE

Q96RN5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263205; ENSP00000263205; ENSG00000099917.

GeneID

51586.

KEGG

hsa:51586.

UCSC

uc002zsp.1. human.
uc002zsq.1. human.

Organism-specific databases

CTD

51586.

GeneCards

GC22P020850.

HGNC

HGNC:14248. MED15.

HPA

HPA003179.

MIM

607372. gene.

neXtProt

NX_Q96RN5.

PharmGKB

PA162395367.
PA33088.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00600000084417.

HOVERGEN

HBG053529.

InParanoid

Q96RN5.

OMA

AFRQKLV.

PhylomeDB

Q96RN5.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_111045. Developmental Biology.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q96RN5.

Bgee

Q96RN5.

CleanEx

HS_MED15.

Genevestigator

Q96RN5.

GermOnline

ENSG00000099917. Homo sapiens.

Family and domain databases

InterPro

IPR019087. Mediator_Med15_met.
[Graphical view]

KO

K15157.

Pfam

PF09606. Med15. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

55423.

SOURCE

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Entry information

Entry name

MED15_HUMAN

Accession

Primary (citable) accession number: Q96RN5
Secondary accession number(s): D3DX31 , D3DX32, O15413, Q6IC31, Q8NF16, Q96CT0, Q96IH7, Q9P1T3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	January 10, 2003
Last modified:	January 25, 2012
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.