ID B2RAG9_HUMAN Unreviewed; 1566 AA.
AC B2RAG9;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 1 {ECO:0000256|ARBA:ARBA00020612, ECO:0000256|RuleBase:RU364059};
DE AltName: Full=Mediator complex subunit 1 {ECO:0000256|ARBA:ARBA00031254, ECO:0000256|RuleBase:RU364059};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG36866.1};
RN [1] {ECO:0000313|EMBL:BAG36866.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:BAG36866.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA Isogai T.;
RT "NEDO functional analysis of protein and research application project.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors. {ECO:0000256|RuleBase:RU364059}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364059}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
CC {ECO:0000256|ARBA:ARBA00006210, ECO:0000256|RuleBase:RU364059}.
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DR EMBL; AK314185; BAG36866.1; -; mRNA.
DR PeptideAtlas; B2RAG9; -.
DR GO; GO:0016592; C:mediator complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0006702; P:androgen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; ISS:UniProtKB.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0002088; P:lens development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:2001141; P:regulation of RNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0002154; P:thyroid hormone mediated signaling pathway; ISS:UniProtKB.
DR InterPro; IPR019680; Mediator_Med1.
DR PANTHER; PTHR12881; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 1; 1.
DR PANTHER; PTHR12881:SF10; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 1; 1.
DR Pfam; PF10744; Med1; 1.
PE 2: Evidence at transcript level;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU364059};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364059};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU364059};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU364059}.
FT DOMAIN 45..411
FT /note="Mediator complex subunit Med1"
FT /evidence="ECO:0000259|Pfam:PF10744"
FT REGION 594..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1566 AA; 166646 MW; CA760D5C8E93FE86 CRC64;
MSSLLERLHA KFNQNRPWSE TIKLVRQVME KRVVMSSGGH QHLVSCLETL QKALKVTSLP
AMTDRLESIA RQNGLGSHLS ASGTECYITS DMFYVEVQLD PAGQLCDVKV AHHGENPVSC
PELVQQLREK NFDEFSKHLK GLVNLYNLPG DNKLKTKMCL ALQSLEQDLS KMAIMYWKAT
NAGPLDKILH GSVGYLTPRS GGHLMNLKYY VSPSDLLDDK TASPIILHEN NVSRSLGMNA
SVTIEGTSAV YKLPIAPLIM GSHPVDNKWT PSFSSITSAN SVDLPACFFL KFPQPIPVSR
AFVQKLQNCT GIPLFETQPT YAPLYELITQ FELSKDPDPI PLNHNMRFYA ALPGQQHCYF
LNKDAPLPDG QSLQGTLVSK ITFQHPGRVP LILNLIRHQV AYNTLIGSCV KRTILKEDSP
GLLQFEVCPL SESRFSVSFQ HPVNDSLVCV VMDVQDSTHV SCKLYKGLSD ALICTDDFIA
KVVQRCMSIP VTMRAIRRKA ETIQADTPAL SLIAETVEDM VKKNLPPASS PGYGMTTGNN
PMSGTTTPTN TFPGGPITTL FNMSMSIKDR HESVGHGEDF SKVSQNPILT SLLQITGNGG
STIGSSPTPP HHTPPPVSSM AGNTKNHPML MNLLKDNPAQ DFSTLYGSSP LERQNSSSGS
PRMEICSGSN KTKKKKSSRL PPEKPKHQTE DDFQRELFSM DVDSQNPIFD VNMTADTLGT
PHITPAPSQC STPPTTYPQP VPHPQPSIQR MVRLSSSDSI GPDVTDILSD IAEEASKLPS
TSDDCPAIGT PLRDSSSSGH SQSTLFDSDV FQTNNNENPY TDPADLIADA AGSPSSDSPT
NHFFHDGVDF NPDLLNSQSQ SGFGEEYFDE SSQSGDNDDF KGFASQALNT LGVPMLGGDN
GETKFKGNNQ ADTVDFSIIS VAGKALAPAD LMEHHSGSQG PLLTTGDLGK EKTQKRVKEG
NGTSNSTLSG PGLDSKPGKR SRTPSNDGKS KDKPPKRKKA DTEGKSPSHS SSNRPFTPPT
STGGSKSPGS AGRSQTPPGV ATPPIPKITI QIPKGTVMVG KPSSHSQYTS SGSVSSSGSK
SHHSHSSSSS SSASTSGKMK SSKSEGSSSS KLSSSMYSSQ GSSGSSQSKN SSQSGGKPGS
SPITKHGLSS GSSSTKMKPQ GKPSSLMNPS LSKPNISPSH SRPPGGSDKL ASPMKPVPGT
PPSSKAKSPI SSGSGGSHMS GTSSSSGMKS SSGLGSSGSL SQKTPPSSNS CTASSSSFSS
SGSSMSSSQN QHGSSKGKSP SRNKKPSLTA VIDKLKHGVV TSGPGGEDPL DGQMGVSTNS
SSQPMSSKHN MSGGEFQGKR EKSDKDKSKV STSGSSVDSS KKTSESKNVG STGVAKIIIS
KHDGGSPSIK AKVTLQKPGE SSGEGLRPQM ASSKNYGSPL ISGSTPKHER GSPSHSKSPA
YTPQNLDSES ESGSSIAEKS YQNSPSSDDG IRPLPEYSTE KHKKHKKEKK KVKDKDRDRD
RDKDRDKKKS HSIKPESWSK SPISSDQSLS MTSNTILSAD RPSRLSPDFM IGEEDDDLMD
VALIGN
//
