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Protein

Probable mediator of RNA polymerase II transcription subunit 37c

Gene

MED37D

Organism
Arabidopsis thaliana (Mouse-ear cress)
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. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).By similarity
In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to bacterium Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to heat Source: UniProtKB
  • response to virus Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:GQT-696-MONOMER.
ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.
R-ATH-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable mediator of RNA polymerase II transcription subunit 37c
Alternative name(s):
Heat shock 70 kDa protein 2
Heat shock cognate 70 kDa protein 2
Heat shock cognate protein 70-2
Short name:
AtHsc70-2
Heat shock protein 70-2
Short name:
AtHsp70-2
Gene namesi
Name:MED37D
Synonyms:HSC70-2, HSC70-G8, HSP70-2, MED37_3
Ordered Locus Names:At5g02490
ORF Names:T22P11.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G02490.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • cell wall Source: TAIR
  • cytosol Source: TAIR
  • Golgi apparatus Source: TAIR
  • nucleus Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 653652Probable mediator of RNA polymerase II transcription subunit 37cPRO_0000078345Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki457 – 457Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP22954.
PRIDEiP22954.

PTM databases

iPTMnetiP22954.

Expressioni

Developmental stagei

Down-regulated during seed maturation.1 Publication

Inductioni

By heat shock and by cold. Up-regulated by virus infection and by pathogen attack (P.syringae).3 Publications

Gene expression databases

GenevisibleiP22954. AT.

Interactioni

Subunit structurei

Component of the Mediator complex.1 Publication

Protein-protein interaction databases

BioGridi17132. 12 interactions.
IntActiP22954. 2 interactions.
STRINGi3702.AT5G02490.1.

Structurei

3D structure databases

ProteinModelPortaliP22954.
SMRiP22954. Positions 6-619.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
InParanoidiP22954.
KOiK03283.
OMAiCNITAYD.
PhylomeDBiP22954.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22954-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDS
60 70 80 90 100
ERLIGDAAKN QVAMNPVNTV FDAKRLIGRR FSDASVQSDR QLWPFTIISG
110 120 130 140 150
TAEKPMIVVE YKGEEKQFAA EEISSMVLIK MREIAEAFLG TTVKNAVVTV
160 170 180 190 200
PAYFNDSQRQ ATKDAGVIAG LNVLRIINEP TAAAIAYGLD KKATSVGEKN
210 220 230 240 250
VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD NRMVNHFVQE
260 270 280 290 300
FKRKNKQDIT GQPRALRRLR TACERAKRTL SSTAQTTIEI DSLYGGADFY
310 320 330 340 350
SPITRARFEE MNMDLFRKCM EPVEKCLRDA KMDKSTVHEI VLVGGSTRIP
360 370 380 390 400
KVQQLLQDFF NGKELCKSIN PDEAVAYGAA VQAAILSGEG NEKVQDLLLL
410 420 430 440 450
DVTPLSLGLE TAGGVMTTLI QRNTTIPTKK EQVFSTYSDN QPGVLIQVFE
460 470 480 490 500
GERARTKDNN LLGKFELSGI PPAPRGVPQI TVCFDIDANG ILNVSAEDKT
510 520 530 540 550
TGKKNKITIT NDKGRLSKED IEKMVQEAEK YKSEDEEHKK KVEAKNALEN
560 570 580 590 600
YAYNMRNTIR DEKIGEKLPA ADKKKVEDSI EEAIQWLDGN QLGEADEFED
610 620 630 640 650
KMKELESVCN PIIAKMYQGG AGGEAGGPGA SGMDEDEAPP ASGGAGPKIE

EVD
Length:653
Mass (Da):71,387
Last modified:December 1, 2000 - v2
Checksum:iEDEC254DB06D9966
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61E → K in CAA54420 (Ref. 6) Curated
Sequence conflicti100 – 1023GTA → ELQ in AAA32820 (PubMed:16666375).Curated
Sequence conflicti614 – 6141A → G in BAD94888 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL162971 Genomic DNA. Translation: CAB85986.1.
CP002688 Genomic DNA. Translation: AED90479.1.
AY093152 mRNA. Translation: AAM13151.1.
BT008411 mRNA. Translation: AAP37770.1.
AK222068 mRNA. Translation: BAD94888.1.
AK227090 mRNA. Translation: BAE99142.1.
M23106 Genomic DNA. Translation: AAA32820.1.
X77199 Genomic DNA. Translation: CAA54420.1.
Y08892 mRNA. Translation: CAA70105.1.
PIRiJA0170.
T48270.
RefSeqiNP_195869.1. NM_120327.4.
UniGeneiAt.5363.
At.74798.

Genome annotation databases

EnsemblPlantsiAT5G02490.1; AT5G02490.1; AT5G02490.
GeneIDi831856.
GrameneiAT5G02490.1; AT5G02490.1; AT5G02490.
KEGGiath:AT5G02490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL162971 Genomic DNA. Translation: CAB85986.1.
CP002688 Genomic DNA. Translation: AED90479.1.
AY093152 mRNA. Translation: AAM13151.1.
BT008411 mRNA. Translation: AAP37770.1.
AK222068 mRNA. Translation: BAD94888.1.
AK227090 mRNA. Translation: BAE99142.1.
M23106 Genomic DNA. Translation: AAA32820.1.
X77199 Genomic DNA. Translation: CAA54420.1.
Y08892 mRNA. Translation: CAA70105.1.
PIRiJA0170.
T48270.
RefSeqiNP_195869.1. NM_120327.4.
UniGeneiAt.5363.
At.74798.

3D structure databases

ProteinModelPortaliP22954.
SMRiP22954. Positions 6-619.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17132. 12 interactions.
IntActiP22954. 2 interactions.
STRINGi3702.AT5G02490.1.

PTM databases

iPTMnetiP22954.

Proteomic databases

PaxDbiP22954.
PRIDEiP22954.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G02490.1; AT5G02490.1; AT5G02490.
GeneIDi831856.
GrameneiAT5G02490.1; AT5G02490.1; AT5G02490.
KEGGiath:AT5G02490.

Organism-specific databases

TAIRiAT5G02490.

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
InParanoidiP22954.
KOiK03283.
OMAiCNITAYD.
PhylomeDBiP22954.

Enzyme and pathway databases

BioCyciARA:GQT-696-MONOMER.
ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.
R-ATH-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

PROiP22954.

Gene expression databases

GenevisibleiP22954. AT.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Characterization of an hsp70 cognate gene family in Arabidopsis."
    Wu C.H., Caspar T., Browse J., Lindquist S., Somerville C.R.
    Plant Physiol. 88:731-740(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
  6. King K.
    Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
    Strain: cv. Ostwestfalen.
    Tissue: Leaf.
  7. "Specific Hsp70s are expressed and accumulated during silique development in Arabidopsis."
    Wang Y.C., Lee S.P., Shieh K., Hu S.M., Wang C., Lin B.L.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 550-653.
    Strain: cv. Columbia.
    Tissue: Silique.
  8. "Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana."
    Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.
    Cell Stress Chaperones 6:201-208(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  9. "Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family."
    Sung D.Y., Vierling E., Guy C.L.
    Plant Physiol. 126:789-800(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNAK GENE SUBFAMILY, INDUCTION, DEVELOPMENTAL STAGE.
  10. "Virus induction of heat shock protein 70 reflects a general response to protein accumulation in the plant cytosol."
    Aparicio F., Thomas C.L., Lederer C., Niu Y., Wang D., Maule A.J.
    Plant Physiol. 138:529-536(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates Arabidopsis immune responses."
    Noel L.D., Cagna G., Stuttmann J., Wirthmueller L., Betsuyaku S., Witte C.P., Bhat R., Pochon N., Colby T., Parker J.E.
    Plant Cell 19:4061-4076(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY PATHOGEN.
  12. "Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
    Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
    Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-457.
  13. "AtHsp70-15-deficient Arabidopsis plants are characterized by reduced growth, a constitutive cytosolic protein response and enhanced resistance to TuMV."
    Jungkunz I., Link K., Vogel F., Voll L.M., Sonnewald S., Sonnewald U.
    Plant J. 66:983-995(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  14. "The Mediator complex in plants: structure, phylogeny, and expression profiling of representative genes in a dicot (Arabidopsis) and a monocot (rice) during reproduction and abiotic stress."
    Mathur S., Vyas S., Kapoor S., Tyagi A.K.
    Plant Physiol. 157:1609-1627(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, SUBUNIT, NOMENCLATURE.

Entry informationi

Entry nameiMD37D_ARATH
AccessioniPrimary (citable) accession number: P22954
Secondary accession number(s): O04293
, Q0WUQ6, Q56WH2, Q9LZ53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 1, 2000
Last modified: April 13, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.