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MD13L_MOUSE
ID   MD13L_MOUSE             Reviewed;        2207 AA.
AC   Q6JPI3; Q3TRF4; Q3UQI8; Q80TM3; Q80WQ0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 13-like;
DE   AltName: Full=Mediator complex subunit 13-like;
DE   AltName: Full=Thyroid hormone receptor-associated protein 2;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 240 kDa component-like;
GN   Name=Med13l; Synonyms=Kiaa1025, Thrap2, Trap240l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15145061; DOI=10.1016/j.gene.2004.02.044;
RA   Musante L., Bartsch O., Ropers H.-H., Kalscheuer V.M.;
RT   "cDNA cloning and characterization of the human THRAP2 gene which maps to
RT   chromosome 12q24, and its mouse ortholog Thrap2.";
RL   Gene 332:119-127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-465 AND 1846-2207.
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 550-2207.
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1083-2207.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. This subunit may specifically
CC       regulate transcription of targets of the Wnt signaling pathway and SHH
CC       signaling pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC       MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC       MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC       MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC       CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC       module termed the CDK8 module. Mediator containing the CDK8 module is
CC       less active than Mediator lacking this module in supporting
CC       transcriptional activation. Individual preparations of the Mediator
CC       complex lacking one or more distinct subunits have been variously
CC       termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart and weakly expressed in
CC       brain, spleen, lung, liver, kidney and testis.
CC       {ECO:0000269|PubMed:15145061}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR08419.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY338464; AAR08419.1; ALT_FRAME; mRNA.
DR   EMBL; AK142391; BAE25053.1; -; mRNA.
DR   EMBL; AK162842; BAE37076.1; -; mRNA.
DR   EMBL; AK122419; BAC65701.1; -; mRNA.
DR   EMBL; BC052320; AAH52320.1; -; mRNA.
DR   CCDS; CCDS57375.1; -.
DR   RefSeq; NP_766012.3; NM_172424.4.
DR   AlphaFoldDB; Q6JPI3; -.
DR   BioGRID; 218020; 9.
DR   STRING; 10090.ENSMUSP00000098379; -.
DR   iPTMnet; Q6JPI3; -.
DR   PhosphoSitePlus; Q6JPI3; -.
DR   EPD; Q6JPI3; -.
DR   MaxQB; Q6JPI3; -.
DR   PaxDb; Q6JPI3; -.
DR   PRIDE; Q6JPI3; -.
DR   ProteomicsDB; 252756; -.
DR   DNASU; 76199; -.
DR   GeneID; 76199; -.
DR   KEGG; mmu:76199; -.
DR   CTD; 23389; -.
DR   MGI; MGI:2670178; Med13l.
DR   eggNOG; KOG3600; Eukaryota.
DR   InParanoid; Q6JPI3; -.
DR   PhylomeDB; Q6JPI3; -.
DR   BioGRID-ORCS; 76199; 6 hits in 72 CRISPR screens.
DR   ChiTaRS; Med13l; mouse.
DR   PRO; PR:Q6JPI3; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q6JPI3; protein.
DR   GO; GO:0016592; C:mediator complex; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IC:MGI.
DR   InterPro; IPR009401; Med13_C.
DR   InterPro; IPR021643; Mediator_Med13_N.
DR   InterPro; IPR041285; MID_MedPIWI.
DR   Pfam; PF06333; Med13_C; 1.
DR   Pfam; PF11597; Med13_N; 1.
DR   Pfam; PF18296; MID_MedPIWI; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..2207
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   13-like"
FT                   /id="PRO_0000076353"
FT   REGION          337..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1379..1400
FT                   /note="Leucine-zipper"
FT   REGION          1523..1652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2042..2077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           664..668
FT                   /note="LXXLL motif 1"
FT   MOTIF           1224..1228
FT                   /note="LXXLL motif 2"
FT   COMPBIAS        339..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..746
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1005..1033
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1091
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1533..1647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71F56"
FT   MOD_RES         555
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71F56"
FT   MOD_RES         812
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71F56"
FT   MOD_RES         821
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71F56"
FT   MOD_RES         918
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71F56"
FT   MOD_RES         2080
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71F56"
FT   CONFLICT        950
FT                   /note="T -> M (in Ref. 3; BAC65701)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1008
FT                   /note="V -> L (in Ref. 3; BAC65701)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1222
FT                   /note="V -> I (in Ref. 3; BAC65701)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2207 AA;  241758 MW;  CC4CE8B90CF30338 CRC64;
     MTAAANWVAN GASLEDCHSN LFSLAELTGI KWRRYNFGGH GDCGPIISAP AQDDPILLSF
     IRCLQANLLC VWRRDVKPDC KELWIFWWGD EPNLVGVIHH ELQVVEEGLW ENGLSYECRT
     LLFKAIHNLL ERCLMDKNFV RIGKWFVRPY DKDEKPVNKS EHLSCAFTFF LHGESNVCTS
     VEIAQHQPIY LINEEHLHMA QSSPAPFQVL VSPYGLNGTL TGHAYKMSDP AARKLIEEWH
     CFYPMVLRKR EEPREEAELG YDDDFPVAVE VIVGGVRMVY PSAFVLVSQN DIPVPQSGHG
     TVAQQGLGSV KDPSNCGMPL TPPTSPEQVV IGESGGVQSA ASHLGSQDGG MSTMHSPKRS
     RKTPPKLHSH MVRRVWRECI LSRAQSKRSQ MSTPTREEEA AHSPAAWDFV DPTQRVSCSC
     SRHKLLKRCA VGPSRPPAIS QPGFSAGLPS SSSLPPPASS KHKTTERQEK GDKLQKRPLV
     PFHHRPSVAE ELCVEQDAPG QKLGLAGIDA SLEVSNTRKY DKQMAVPSRN TSKQMNLNPM
     DSPHSPISPL PPTLSPQPRG QEAESLDPPS VPVNPALYGN GLDLQQLSTI EDRTVLVGQR
     LPLMAEASET ALYSGLRPSY TESSDRWWQS FRLPSSEDAE FRPPELQGER FDTALDLNPE
     STALQRLLAQ PNKRFKIWQD EQPQVQPLPF LDPSPLSQQP GDTLGEVNDP YTFEDGDIKY
     IFTANKKCKQ GTEKDSLKKN KSEDGFGTKD VTTPGHSTPV PDGKNAMSIF SSATKTDVRQ
     DSAAGRAGSG SLTQVTDLAP SLHDLDNIFD NSDDDELGAV SPALRSSKMP TVGTEERPPG
     KDGRAAGPYP PTVADLQRMF PTPPSLEQHP AFSPVMNYKD GVSSETVTAL GMMESPVVSM
     VPTHLTEFRM EVEDGLGSPK PEEIKDFSYV HKVPQFQPFV GSSMFAPLKT LPSHCLLPLK
     TPDACLFRPS WAVPPKMEQL PMPPAASSIR DGYNNVPSVG SLADPDYVNT PQMNTPVTLN
     SAAPASNSGA GVLPSPATPR FSVPTPRTPR TPRTPRGGGT ASGQGSVKYD STDQGSPAST
     PSTTRPLNSV EPATMQPIPE AHSLYVTLIL SDSVMNVFKD RNFDSCCICA CNMNIKGADV
     GLYIPDSSKE DQYRCTCGFS AIVNRKLGYN SGLFLEDELD IFGKNSDIGQ AAERRLMMCQ
     SSGQSTLLPQ VEGARKAPEP PVSLLLLLQN QHTQPFASLS FLDYISSANR HALPCVSWTY
     DRVQADNNDY WTECFNALEQ GRQYVDNPTG GKVDEALVRS ATVHCWPHSN VLDTSMLSSQ
     DVVRMLLSLQ PFLQDAIQKK RTGRTWENIQ HVQGPLTWQQ FHKMAGRGTY GSEESPEPLP
     IPTLLVGYDK EFLTISPFSL PFWERLLLEP YGGHRDVAYI VVCPENEALL EGAKTFFRDL
     SAVYEMCRLG QHKPICKVLR DGIMRVGKTV AQKLTEELVS EWFNQPWSSE ESDNHSRLKL
     YAQVCRHHLA PYLATLQLDS GLLMPPKHQS PPAEAQGQAT PGNAGSLPSN SGSGAPPAGS
     AFNPTSSSSA NPTTSSSSAS SGPPGSSAAS APGITQMNTT SSSGFGGGVG GQNPSAGGSS
     TDRTPGNVAC GDTEPGQSCT QSSQDGQDSV TERERIGIPT EPDSADSHAY PPAVVIYMVD
     PFTYTAEEDS SSGNFWLLSL MRCYTEMLDH LPEHMRSSFI LQIVPCQYML QTMKDEHVFY
     IQYLKSMAFS VYCQCRRPLP TQIHIKSLTG FGPAASIEMT LKNPERPSPI QLYSPPFILA
     PIKDKQTEPG ETFGEASQKY NVLFVGYCLS HDQRWLLASC TDLHGELLET CVVNIALPSR
     SRKSKVSARK VGLQKLWEWC LGIVQMTSLP WRVVIGRLGR LGHGELKDWS ILLGECSLQT
     ISKQLKDVCR MCGISAADSP SILSACLVAM EPQGSFVVMP DAVTMGSVFG RSTALNMQSS
     QLNTPQDASC THILVFPTSS TIQVAPANYP NEDGFSPNND DMFVDLPFPD DMDNDIGILM
     TGNLHSSPNS SPVPSPGSPS GIGVGSHFQH SRSQGERLLS REAPEELKQQ PLALGYFVST
     AKAENLPQWF WSSCPQARNQ CPLFLKASLH HHISVAQTDE LLPARTSQRA PHPLDSKTTS
     DVLRFVLEQY NALSWLTCNP ATQDRTSCLP VHFVVLTQLY NAIMNML
 
 
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