UniProtKB/Swiss-Prot Q9NVC6: Variant p.Glu69Asp

Mediator of RNA polymerase II transcription subunit 17
Gene: MED17
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Variant information Variant position:

69 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Glutamate (E) to Aspartate (D) at position 69 (E69D, p.Glu69Asp). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Similar physico-chemical property. Both residues are medium size and acidic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Other resources:

Links to websites of interest for the variant.

Variant rs2848477 [ dbSNP | Ensembl ]

Sequence information Variant position:

69 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

651 The length of the canonical sequence.
Location on the sequence:

FSQGSGSEEEEAAGTEGDAQ E WPGAGSSADQDDEEGVVKFQ The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         FSQGSG--------SEEEEAAGTEGDAQEWPGAGSSADQDDEEGVVK---------FQ

Mouse                         FSQGSG--------SEEEEAAGPDGDAPDWGGAG--ADQDD

Bovine                        FSQGSG--------SEEEEAAGAEGDAQDWAGAGSSADQDD

Chicken                       FSQGSG--------SEEDE-PGSAGRA--WAEP---SEAED

Xenopus tropicalis            FSQESG--------EEEAEAAREL----EW------AEQEE

Zebrafish                     FCQSSD--------SEEDGAERARAGREQWK-----QEPEE

Caenorhabditis elegans        WTKLVG--------TKSPYENSKVDPEDEL------DDENV

Drosophila                    FSKTSL--------DDLKKEEKSAA-----------AAADE

Slime mold                    HQKEIE-------QIKLNDNKNNENNNLQDKEKEKEKEKER

Baker's yeast                 RQRGPGFKFVDLNEKELQNEIKQLGSDSSDGHNSEKKDTDG

Fission yeast                 QERGPF--------RDLKEEDLQKELQKESIKDESSAKSSE

Sequence annotation in neighborhood:

The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:

Type: the type of sequence feature.
Positions: endpoints of the sequence feature.
Description: contains additional information about the feature.

Type	Positions	Description
Chain	1 – 651	Mediator of RNA polymerase II transcription subunit 17
Region	51 – 83	Disordered

Literature citations
Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators.
Ito M.; Yuan C.-X.; Malik S.; Gu W.; Fondell J.D.; Yamamura S.; Fu Z.-Y.; Zhang X.; Qin J.; Roeder R.G.;
Mol. Cell 3:361-370(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); PROTEIN SEQUENCE OF 306-319; 405-415 AND 592-602; TISSUE SPECIFICITY; IDENTIFICATION IN TRAP COMPLEX; VARIANT ASP-69; Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex.
Rachez C.; Lemon B.D.; Suldan Z.; Bromleigh V.; Gamble M.; Naeaer A.M.; Erdjument-Bromage H.; Tempst P.; Freedman L.P.;
Nature 398:824-828(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); PROTEIN SEQUENCE OF 88-99 AND 607-619; IDENTIFICATION IN ARC COMPLEX; VARIANT ASP-69; 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)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2); VARIANT ASP-69; 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)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANT ASP-69; Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
Daub H.; Olsen J.V.; Bairlein M.; Gnad F.; Oppermann F.S.; Korner R.; Greff Z.; Keri G.; Stemmann O.; Mann M.;
Mol. Cell 31:438-448(2008)
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-69; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; 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)
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-69; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];

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