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Q15648 (MED1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. 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 1
Alternative name(s):
Activator-recruited cofactor 205 kDa component
Short name=ARC205
Mediator complex subunit 1
Peroxisome proliferator-activated receptor-binding protein
Short name=PBP
Short name=PPAR-binding protein
Thyroid hormone receptor-associated protein complex 220 kDa component
Short name=Trap220
Thyroid receptor-interacting protein 2
Short name=TR-interacting protein 2
Short name=TRIP-2
Vitamin D receptor-interacting protein complex component DRIP205
p53 regulatory protein RB18A
Gene names
Name:MED1
Synonyms:ARC205, CRSP1, CRSP200, DRIP205, DRIP230, PBP, PPARBP, PPARGBP, RB18A, TRAP220, TRIP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1581 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. Ref.2 Ref.12 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.28

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. This subunit specifically interacts with a number of nuclear receptors in a ligand-dependent fashion including AR, ESR1, ESR2, PPARA, PPARG, RORA, RXRA, RXRG, THRA, THRB and VDR. Interacts with CTNNB1, GABPA, GLI3, PPARGC1A and TP53. Interacts with GATA1 and YWHAH. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28 Ref.29

Subcellular location

Nucleus. Note: A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3. Ref.22 Ref.26 Ref.28

Tissue specificity

Ubiquitously expressed. Ref.1 Ref.2

Post-translational modification

Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may enhance protein stability and promote entry into the nucleolus. Ref.26

Sequence similarities

Belongs to the Mediator complex subunit 1 family.

Sequence caution

The sequence AAC39854.1 differs from that shown. Reason: Frameshift at positions 543 and 545.

The sequence AAH06517.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence CAA73867.1 differs from that shown. Reason: Frameshift at position 4.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: Ensembl

ERK1 and ERK2 cascade

Inferred from direct assay PubMed 18391015. Source: UniProtKB

androgen biosynthetic process

Inferred from mutant phenotype PubMed 19497978. Source: UniProtKB

androgen receptor signaling pathway

Inferred from direct assay Ref.16. Source: UniProtKB

angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

brain development

Inferred from electronic annotation. Source: Ensembl

cell morphogenesis

Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to epidermal growth factor stimulus

Inferred from direct assay Ref.26. Source: UniProtKB

cellular response to hepatocyte growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to steroid hormone stimulus

Inferred from direct assay PubMed 18391015. Source: UniProtKB

cellular response to thyroid hormone stimulus

Inferred from direct assay PubMed 18391015. Source: UniProtKB

embryonic heart tube development

Inferred from electronic annotation. Source: Ensembl

embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

embryonic hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

enucleate erythrocyte development

Inferred from electronic annotation. Source: Ensembl

epithelial cell proliferation involved in mammary gland duct elongation

Inferred from electronic annotation. Source: Ensembl

erythrocyte development

Inferred from sequence or structural similarity. Source: UniProtKB

fat cell differentiation

Inferred from direct assay Ref.17. Source: MGI

gene expression

Traceable author statement. Source: Reactome

intracellular steroid hormone receptor signaling pathway

Inferred from direct assay Ref.18. Source: UniProtKB

keratinocyte differentiation

Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB

lactation

Inferred from electronic annotation. Source: Ensembl

lens development in camera-type eye

Inferred from sequence or structural similarity. Source: UniProtKB

liver development

Inferred from electronic annotation. Source: Ensembl

mRNA transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

mammary gland branching involved in pregnancy

Inferred from electronic annotation. Source: Ensembl

mammary gland branching involved in thelarche

Inferred from electronic annotation. Source: Ensembl

megakaryocyte development

Inferred from sequence or structural similarity. Source: UniProtKB

monocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of keratinocyte proliferation

Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB

negative regulation of neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

organ regeneration

Inferred from electronic annotation. Source: Ensembl

peroxisome proliferator activated receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of G0 to G1 transition

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from direct assay PubMed 17827210. Source: UniProtKB

positive regulation of hepatocyte proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of interferon-gamma-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of keratinocyte differentiation

Inferred from mutant phenotype PubMed 17082781. Source: UniProtKB

positive regulation of mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein import into nucleus, translocation

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor activity

Inferred from mutant phenotype PubMed 18391015. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17827210PubMed 19497978Ref.2. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10198638Ref.26. Source: UniProtKB

regulation of RNA biosynthetic process

Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB

regulation of cell cycle

Non-traceable author statement Ref.26. Source: UniProtKB

regulation of transcription from RNA polymerase I promoter

Inferred from direct assay Ref.26. Source: UniProtKB

regulation of vitamin D receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

retinal pigment epithelium development

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

thyroid hormone generation

Inferred from electronic annotation. Source: Ensembl

thyroid hormone mediated signaling pathway

Inferred from mutant phenotype Ref.26. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Inferred from direct assay Ref.16. Source: UniProtKB

ventricular trabecula myocardium morphogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromatin

Inferred from electronic annotation. Source: Ensembl

mediator complex

Inferred from direct assay PubMed 10198638. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.26. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.6Ref.26PubMed 17223341PubMed 17827210PubMed 19497978. Source: UniProtKB

protein-DNA complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionLBD domain binding

Inferred from physical interaction PubMed 17827210. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription cofactor activity

Inferred from direct assay PubMed 10198638. Source: UniProtKB

chromatin DNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from mutant phenotype PubMed 17641689. Source: UniProtKB

core promoter binding

Inferred from direct assay PubMed 17641689. Source: UniProtKB

estrogen receptor binding

Inferred from physical interaction Ref.2. Source: UniProtKB

ligand-dependent nuclear receptor binding

Inferred from direct assay PubMed 18391015. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from mutant phenotype PubMed 17641689. Source: UniProtKB

mediator complex binding

Inferred from direct assay PubMed 18391015. Source: UniProtKB

nuclear hormone receptor binding

Inferred from physical interaction Ref.13. Source: UniProtKB

peroxisome proliferator activated receptor binding

Inferred from physical interaction Ref.2. Source: UniProtKB

receptor activity

Inferred from direct assay Ref.16. Source: UniProtKB

retinoic acid receptor binding

Inferred from physical interaction Ref.2. Source: UniProtKB

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

thyroid hormone receptor binding

Inferred from direct assay PubMed 10198638. Source: UniProtKB

thyroid hormone receptor coactivator activity

Inferred from mutant phenotype PubMed 18391015. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.26PubMed 19497978Ref.2. Source: UniProtKB

transcription cofactor activity

Inferred from direct assay Ref.16. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 17641689PubMed 19497978. Source: UniProtKB

vitamin D receptor binding

Inferred from physical interaction Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15648-1)

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: Q15648-3)

The sequence of this isoform differs from the canonical sequence as follows:
     548-556: YGMTTGNNP → SKNPELGSG
     557-1581: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15811581Mediator of RNA polymerase II transcription subunit 1
PRO_0000058552

Regions

Region1 – 670670Interaction with the Mediator complex and THRA
Region16 – 590575Interaction with ESR1
Region108 – 212105Interaction with the Mediator complex
Region215 – 390176Interaction with the Mediator complex
Region405 – 644240Interaction with THRA
Region542 – 789248Interaction with VDR
Region622 – 70180Interaction with PPARGC1A and THRA
Region637 – 71680Interaction with GATA1 By similarity
Region656 – 1066411Interaction with ESR1
Region1249 – 1421173Interaction with TP53
Motif604 – 6085LXXLL motif 1
Motif645 – 6495LXXLL motif 2
Compositional bias1078 – 1482405Ser-rich
Compositional bias1496 – 152934Lys-rich

Amino acid modifications

Modified residue6641Phosphoserine Ref.33 Ref.36 Ref.38
Modified residue7951Phosphoserine Ref.30
Modified residue8051Phosphothreonine Ref.30 Ref.32 Ref.35 Ref.38
Modified residue9531Phosphoserine By similarity
Modified residue10321Phosphothreonine; by MAPK1 or MAPK3 Ref.26
Modified residue10511Phosphothreonine Ref.33 Ref.36 Ref.40
Modified residue10571Phosphothreonine Ref.30 Ref.32 Ref.33 Ref.36 Ref.38
Modified residue11561Phosphoserine Ref.40
Modified residue11771N6-acetyllysine Ref.37
Modified residue12071Phosphoserine Ref.32 Ref.33 Ref.38 Ref.40
Modified residue12151Phosphothreonine Ref.32 Ref.33 Ref.35 Ref.38 Ref.40
Modified residue12231Phosphoserine Ref.40
Modified residue13471Phosphoserine Ref.38
Modified residue14031Phosphoserine Ref.38
Modified residue14331Phosphoserine Ref.38
Modified residue14571Phosphothreonine; by MAPK1 or MAPK3 Ref.26
Modified residue14631Phosphoserine Ref.33 Ref.36
Modified residue14791Phosphoserine Ref.33 Ref.36 Ref.40
Modified residue14811Phosphoserine Ref.33 Ref.36
Modified residue14821Phosphoserine Ref.33 Ref.36
Modified residue15291N6-acetyllysine Ref.37

Natural variations

Alternative sequence548 – 5569YGMTTGNNP → SKNPELGSG in isoform 2.
VSP_027906
Alternative sequence557 – 15811025Missing in isoform 2.
VSP_027907
Natural variant7531P → T.
Corresponds to variant rs1139825 [ dbSNP | Ensembl ].
VAR_053955
Natural variant12401S → G.
Corresponds to variant rs35668211 [ dbSNP | Ensembl ].
VAR_034938

Experimental info

Mutagenesis599 – 61214SQNPI…LQITG → EKHKILHRLLQDSS: Enhances interaction with ESR1. Ref.2 Ref.7 Ref.14 Ref.15 Ref.21 Ref.24
Mutagenesis600 – 61213QNPIL…LQITG → RHKILHRLLQEGS: Enhances interaction with ESR1. Ref.2 Ref.7 Ref.14 Ref.21 Ref.24
Mutagenesis6041L → A: Impairs interaction with ESR2; when associated with A-607; A-645 and A-648. Ref.2 Ref.7 Ref.14 Ref.15 Ref.21 Ref.24
Mutagenesis607 – 6082LL → AA: Impairs interaction with ESR1, PPARG, RXRA and THRB. Impairs interaction with THRA; when associated with 648-A-A-649. Ref.2 Ref.7 Ref.14 Ref.15 Ref.21 Ref.24
Mutagenesis6071L → A: Impairs interaction with ESR2; when associated with A-604; A-645 and A-648. Ref.2 Ref.7 Ref.14 Ref.15 Ref.21 Ref.24
Mutagenesis639 – 65315TKNHP…LKDNP → VSRHKILHRLLQEGS: Enhances interaction with ESR1. Ref.2 Ref.7 Ref.14 Ref.20 Ref.21 Ref.24
Mutagenesis6451L → A: Impairs interaction with ESR2; when associated with A-604; A-607 and A-648. Ref.2 Ref.7 Ref.14 Ref.15 Ref.21 Ref.24
Mutagenesis648 – 6492LL → AA: Impairs interaction with ESR1, PPARG, THRB and VDR. Impairs interaction with THRA; when associated with 607-A-A-608. Ref.2 Ref.7 Ref.14 Ref.15 Ref.21 Ref.24
Mutagenesis6481L → A: Impairs interaction with ESR2; when associated with A-604; A-607 and A-645. Ref.2 Ref.7 Ref.14 Ref.15 Ref.21 Ref.24
Mutagenesis10321T → A: Enhances protein stability; when associated with A-1457. Ref.2 Ref.7 Ref.14 Ref.21 Ref.24 Ref.26
Mutagenesis14571T → A: Enhances protein stability; when associated with A-1032. Ref.2 Ref.7 Ref.14 Ref.21 Ref.24 Ref.26
Sequence conflict861R → G in CAA73867. Ref.1
Sequence conflict1471F → S in CAA73867. Ref.1
Sequence conflict471 – 4722DS → GL in CAA73867. Ref.1
Sequence conflict5631P → S in CAA73867. Ref.1
Sequence conflict5631P → S in AAF98352. Ref.7
Sequence conflict5731T → A in CAA73867. Ref.1
Sequence conflict5731T → A in AAF98352. Ref.7
Sequence conflict6511D → N in AAH06517. Ref.5
Sequence conflict6731S → F in AAC41736. Ref.9
Sequence conflict702 – 7087Missing in AAC41736. Ref.9
Sequence conflict7211N → K in AAC39854. Ref.2
Sequence conflict7281M → R in AAF98352. Ref.7
Sequence conflict756 – 7616VPHPQP → FYLTPQ in AAH06517. Ref.5
Sequence conflict13881G → S in AAC39854. Ref.2

Secondary structure

... 1581
Helix Strand Turn

Details...

Sequences

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

Last modified September 11, 2007. Version 4.
Checksum: FCE0FE87EF08B887

FASTA1,581168,478
        10         20         30         40         50         60 
MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS 

        70         80         90        100        110        120 
CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL 

       130        140        150        160        170        180 
CDVKVAHHGE NPVSCPELVQ QLREKNFDEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL 

       190        200        210        220        230        240 
EQDLSKMAIM YWKATNAGPL DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI 

       250        260        270        280        290        300 
ILHENNVSRS LGMNASVTIE GTSAVYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP 

       310        320        330        340        350        360 
ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK DPDPIPLNHN 

       370        380        390        400        410        420 
MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH PGRVPLILNL IRHQVAYNTL 

       430        440        450        460        470        480 
IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY 

       490        500        510        520        530        540 
KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL 

       550        560        570        580        590        600 
PPASSPGYGM TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ 

       610        620        630        640        650        660 
NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK DNPAQDFSTL 

       670        680        690        700        710        720 
YGSSPLERQN SSSGSPRMEI CSGSNKTKKK KSSRLPPEKP KHQTEDDFQR ELFSMDVDSQ 

       730        740        750        760        770        780 
NPIFDVNMTA DTLDTPHITP APSQCSTPPT TYPQPVPHPQ PSIQRMVRLS SSDSIGPDVT 

       790        800        810        820        830        840 
DILSDIAEEA SKLPSTSDDC PAIGTPLRDS SSSGHSQSTL FDSDVFQTNN NENPYTDPAD 

       850        860        870        880        890        900 
LIADAAGSPS SDSPTNHFFH DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS 

       910        920        930        940        950        960 
QALNTLGVPM LGGDNGETKF KGNNQADTVD FSIISVAGKA LAPADLMEHH SGSQGPLLTT 

       970        980        990       1000       1010       1020 
GDLGKEKTQK RVKEGNGTSN STLSGPGLDS KPGKRSRTPS NDGKSKDKPP KRKKADTEGK 

      1030       1040       1050       1060       1070       1080 
SPSHSSSNRP FTPPTSTGGS KSPGSAGRSQ TPPGVATPPI PKITIQIPKG TVMVGKPSSH 

      1090       1100       1110       1120       1130       1140 
SQYTSSGSVS SSGSKSHHSH SSSSSSSAST SGKMKSSKSE GSSSSKLSSS MYSSQGSSGS 

      1150       1160       1170       1180       1190       1200 
SQSKNSSQSG GKPGSSPITK HGLSSGSSST KMKPQGKPSS LMNPSLSKPN ISPSHSRPPG 

      1210       1220       1230       1240       1250       1260 
GSDKLASPMK PVPGTPPSSK AKSPISSGSG GSHMSGTSSS SGMKSSSGLG SSGSLSQKTP 

      1270       1280       1290       1300       1310       1320 
PSSNSCTASS SSFSSSGSSM SSSQNQHGSS KGKSPSRNKK PSLTAVIDKL KHGVVTSGPG 

      1330       1340       1350       1360       1370       1380 
GEDPLDGQMG VSTNSSSHPM SSKHNMSGGE FQGKREKSDK DKSKVSTSGS SVDSSKKTSE 

      1390       1400       1410       1420       1430       1440 
SKNVGSTGVA KIIISKHDGG SPSIKAKVTL QKPGESSGEG LRPQMASSKN YGSPLISGST 

      1450       1460       1470       1480       1490       1500 
PKHERGSPSH SKSPAYTPQN LDSESESGSS IAEKSYQNSP SSDDGIRPLP EYSTEKHKKH 

      1510       1520       1530       1540       1550       1560 
KKEKKKVKDK DRDRDRDKDR DKKKSHSIKP ESWSKSPISS DQSLSMTSNT ILSADRPSRL 

      1570       1580 
SPDFMIGEED DDLMDVALIG N 

« Hide

Isoform 2 [UniParc].

Checksum: 1E8BBE45A2629DB1
Show »

FASTA55661,563

References

« Hide 'large scale' references
[1]"Identification of RB18A, a 205 kDa new p53 regulatory protein which shares antigenic and functional properties with p53."
Drane P., Barel M., Balbo M., Frade R.
Oncogene 15:3013-3024(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING, INTERACTION WITH TP53, TISSUE SPECIFICITY.
Tissue: Heart.
[2]"The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion."
Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.
Proc. Natl. Acad. Sci. U.S.A. 95:7939-7944(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 157-168; 943-952 AND 1432-1442, FUNCTION, INTERACTION WITH ESR1; PPARA; PPARG; RARA; RXRA; THRA AND VDR, TISSUE SPECIFICITY, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[3]Erratum
Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G.
Proc. Natl. Acad. Sci. U.S.A. 95:14584-14584(1998)
[4]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 (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 2).
Tissue: Colon and Testis.
[6]"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: PROTEIN SEQUENCE OF 1-13 AND 1452-1464, IDENTIFICATION IN THE ARC COMPLEX.
[7]"The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes."
Rachez C., Gamble M., Chang C.-P.B., Atkins G.B., Lazar M.A., Freedman L.P.
Mol. Cell. Biol. 20:2718-2726(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-1581 (ISOFORM 1), INTERACTION WITH VDR, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[8]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 307-315 AND 584-597, IDENTIFICATION IN THE DRIP COMPLEX, INTERACTION WITH VDR.
Tissue: Cervix carcinoma.
[9]"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 622-711.
[10]"A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation."
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., Qin J., Roeder R.G.
Mol. Cell 3:97-108(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SMCC COMPLEX.
[11]Erratum
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., Qin J., Roeder R.G.
Mol. Cell 3:541-541(1999)
[12]"Identification of mouse TRAP100: a transcriptional coregulatory factor for thyroid hormone and vitamin D receptors."
Zhang J., Fondell J.D.
Mol. Endocrinol. 13:1130-1140(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MED24; THRA; THRB AND VDR.
[13]"Coactivators for the orphan nuclear receptor RORalpha."
Atkins G.B., Hu X., Guenther M.G., Rachez C., Freedman L.P., Lazar M.A.
Mol. Endocrinol. 13:1550-1557(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RORA.
[14]"Functional interactions between the estrogen receptor and DRIP205, a subunit of the heteromeric DRIP coactivator complex."
Burakov D., Wong C.-W., Rachez C., Cheskis B.J., Freedman L.P.
J. Biol. Chem. 275:20928-20934(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ESR1; ESR2 AND VDR, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[15]"Differential recruitment of the mammalian mediator subunit TRAP220 by estrogen receptors ERalpha and ERbeta."
Waernmark A., Almloef T., Leers J., Gustafsson J.-A., Treuter E.
J. Biol. Chem. 276:23397-23404(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ESR1 AND ESR2, MUTAGENESIS OF 599-SER--GLY-612; LEU-604; LEU-607; LEU-645 AND LEU-648.
[16]"A coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expression."
Wang Q., Sharma D., Ren Y., Fondell J.D.
J. Biol. Chem. 277:42852-42858(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AR, ASSOCIATION WITH PROMOTER REGIONS.
[17]"Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis."
Ge K., Guermah M., Yuan C.-X., Ito M., Wallberg A.E., Spiegelman B.M., Roeder R.G.
Nature 417:563-567(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION OF THE MEDIATOR COMPLEX WITH PPARG.
[18]"The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro."
Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
[19]"Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo."
Sharma D., Fondell J.D.
Proc. Natl. Acad. Sci. U.S.A. 99:7934-7939(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH PROMOTER REGIONS.
[20]"An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220."
Coulthard V.H., Matsuda S., Heery D.M.
J. Biol. Chem. 278:10942-10951(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ESR1; PPARG; RARA; RXRA AND THRB, MUTAGENESIS OF 600-GLN--SER-612; 607-LEU-LEU-608; 639-THR--PRO-653 AND 648-LEU-LEU-649.
[21]"Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha."
Wallberg A.E., Yamamura S., Malik S., Spiegelman B.M., Roeder R.G.
Mol. Cell 12:1137-1149(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPARGC1A, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[22]"Vitamin D-interacting protein 205 (DRIP205) coactivation of estrogen receptor alpha (ERalpha) involves multiple domains of both proteins."
Wu Q., Burghardt R., Safe S.
J. Biol. Chem. 279:53602-53612(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ESR1, SUBCELLULAR LOCATION.
[23]"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.
[24]"Structural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptors."
Malik S., Guermah M., Yuan C.-X., Wu W., Yamamura S., Roeder R.G.
Mol. Cell. Biol. 24:8244-8254(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION OF THE MEDIATOR COMPLEX WITH THRA, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[25]"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: FUNCTION, ASSOCIATION WITH PROMOTER REGIONS, INTERACTION WITH CCNC; MED6; MED10; MED11; MED12; MED13; MED14; MED15; MED16; MED17; MED18; MED19; MED20; MED21; MED23; MED24; MED25; MED26; MED28; MED29 AND MED30, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[26]"Activation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-activated protein kinase-dependent phosphorylation."
Pandey P.K., Udayakumar T.S., Lin X., Sharma D., Shapiro P.S., Fondell J.D.
Mol. Cell. Biol. 25:10695-10710(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1032 AND THR-1457, MUTAGENESIS OF THR-1032 AND THR-1457.
[27]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Regulation of Aurora-A kinase gene expression via GABP recruitment of TRAP220/MED1."
Udayakumar T.S., Belakavadi M., Choi K.-H., Pandey P.K., Fondell J.D.
J. Biol. Chem. 281:14691-14699(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GABPA, ASSOCIATION WITH PROMOTER REGIONS, SUBCELLULAR LOCATION.
[29]"Mediator modulates Gli3-dependent Sonic hedgehog signaling."
Zhou H., Kim S., Ishii S., Boyer T.G.
Mol. Cell. Biol. 26:8667-8682(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK8.
[30]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-795; THR-805 AND THR-1057, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[32]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805; THR-1057; SER-1207 AND THR-1215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-1051; THR-1057; SER-1207; THR-1215; SER-1463; SER-1479; SER-1481 AND SER-1482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"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].
[35]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805 AND THR-1215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-1051; THR-1057; SER-1463; SER-1479; SER-1481 AND SER-1482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[37]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1177 AND LYS-1529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-805; THR-1057; SER-1207; THR-1215; SER-1347; SER-1403 AND SER-1433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[39]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1051; SER-1156; SER-1207; THR-1215; SER-1223 AND SER-1479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13467 mRNA. Translation: CAA73867.1. Frameshift.
AF055994 mRNA. Translation: AAC39854.1. Frameshift.
CH471152 Genomic DNA. Translation: EAW60575.1.
BC006517 mRNA. Translation: AAH06517.1. Different termination.
BC060758 mRNA. Translation: AAH60758.1.
BC131783 mRNA. Translation: AAI31784.1.
AF283812 mRNA. Translation: AAF98352.1.
L40366 mRNA. Translation: AAC41736.1.
RefSeqNP_004765.2. NM_004774.3.
UniGeneHs.643754.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJKX-ray1.99C640-652[»]
1RK3X-ray2.20C640-652[»]
1RKGX-ray1.90C640-652[»]
1RKHX-ray2.28C640-652[»]
2O4JX-ray1.74C640-652[»]
2O4RX-ray1.98C640-652[»]
2ZFXX-ray1.99C640-652[»]
3A2HX-ray2.50B640-652[»]
3AUNX-ray1.81B640-652[»]
3VJSX-ray1.93C640-652[»]
3VJTX-ray2.00C640-652[»]
3VRTX-ray2.40C640-652[»]
3VRUX-ray2.00C640-652[»]
3VRVX-ray1.90C640-652[»]
3VRWX-ray2.40C640-652[»]
3W0GX-ray1.94C640-652[»]
3W0HX-ray1.80C640-652[»]
3W0IX-ray1.90C640-652[»]
3W0JX-ray1.84C640-652[»]
3W5PX-ray1.90C640-652[»]
3W5QX-ray1.90C640-652[»]
3W5RX-ray2.20C640-652[»]
3W5TX-ray2.29C640-652[»]
ProteinModelPortalQ15648.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111465. 91 interactions.
DIPDIP-24212N.
IntActQ15648. 25 interactions.
MINTMINT-1345780.
STRING9606.ENSP00000300651.

PTM databases

PhosphoSiteQ15648.

Polymorphism databases

DMDM158518535.

Proteomic databases

PaxDbQ15648.
PRIDEQ15648.

Protocols and materials databases

DNASU5469.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300651; ENSP00000300651; ENSG00000125686. [Q15648-1]
ENST00000394287; ENSP00000377828; ENSG00000125686. [Q15648-3]
GeneID5469.
KEGGhsa:5469.
UCSCuc002hru.2. human. [Q15648-3]
uc002hrv.4. human. [Q15648-1]

Organism-specific databases

CTD5469.
GeneCardsGC17M037560.
HGNCHGNC:9234. MED1.
HPACAB017696.
HPA052818.
MIM604311. gene.
neXtProtNX_Q15648.
PharmGKBPA33556.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG101127.
InParanoidQ15648.
KOK15144.
OMAPKHQTED.
OrthoDBEOG7R830S.
PhylomeDBQ15648.
TreeFamTF324954.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.
REACT_71. Gene Expression.
SignaLinkQ15648.

Gene expression databases

ArrayExpressQ15648.
BgeeQ15648.
CleanExHS_MED1.
GenevestigatorQ15648.

Family and domain databases

InterProIPR019680. Mediator_Med1_met/fun.
[Graphical view]
PfamPF10744. Med1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMED1. human.
EvolutionaryTraceQ15648.
GeneWikiMED1.
GenomeRNAi5469.
NextBio21174.
PROQ15648.
SOURCESearch...

Entry information

Entry nameMED1_HUMAN
AccessionPrimary (citable) accession number: Q15648
Secondary accession number(s): A2RRQ6 expand/collapse secondary AC list , O43810, O75447, Q6P9H7, Q6PK58, Q9HD39
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 140 of the entry and version 4 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 17

Human chromosome 17: entries, gene names and cross-references to MIM