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GRL1A_HUMAN
ID   GRL1A_HUMAN             Reviewed;         368 AA.
AC   P0CAP2; Q6EER8; Q6EES2; Q6EEV3; Q6EF00; Q6EF01; Q6EF02; Q6EF46; Q6EFN8;
AC   Q6EM48; Q6K046; Q6K050; Q6K051; Q6ZQZ3; Q8NC58; Q8NCF3; Q96DI5; Q96JB7;
AC   Q96NF5; Q9Y3V6;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=DNA-directed RNA polymerase II subunit GRINL1A;
DE   AltName: Full=DNA-directed RNA polymerase II subunit M;
DE   AltName: Full=Glutamate receptor-like protein 1A;
GN   Name=POLR2M; Synonyms=GRINL1A;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11474202; DOI=10.1159/000056971;
RA   Roginski R.S., Mohan Raj B.K., Finkernagel S.W., Sciorra L.J.;
RT   "Assignment of an ionotropic glutamate receptor-like gene (GRINL1A) to
RT   human chromosome 15q22.1 by in situ hybridization.";
RL   Cytogenet. Cell Genet. 93:143-144(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 11), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain, and Lung;
RX   PubMed=15233991; DOI=10.1016/j.ygeno.2004.04.004;
RA   Roginski R.S., Mohan Raj B.K., Birditt B., Rowen L.;
RT   "The human GRINL1A gene defines a complex transcription unit, an unusual
RT   form of gene organization in eukaryotes.";
RL   Genomics 84:265-276(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Heart;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain cortex;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-368.
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
RA   Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
RA   Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
RA   Conaway R.C.;
RT   "A set of consensus mammalian mediator subunits identified by
RT   multidimensional protein identification technology.";
RL   Mol. Cell 14:685-691(2004).
RN   [9]
RP   FUNCTION, AND RECONSTITUTION OF THE POL II(G) COMPLEX.
RX   PubMed=16769904; DOI=10.1073/pnas.0603702103;
RA   Hu X., Malik S., Negroiu C.C., Hubbard K., Velalar C.N., Hampton B.,
RA   Grosu D., Catalano J., Roeder R.G., Gnatt A.;
RT   "A Mediator-responsive form of metazoan RNA polymerase II.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9506-9511(2006).
CC   -!- FUNCTION: Isoform 1 appears to be a stable component of the Pol II(G)
CC       complex form of RNA polymerase II (Pol II). Pol II synthesizes mRNA
CC       precursors and many functional non-coding RNAs and is the central
CC       component of the basal RNA polymerase II transcription machinery.
CC       Isoform 1 may play a role in the Mediator complex-dependent regulation
CC       of transcription activation. Isoform 1 acts in vitro as a negative
CC       regulator of transcriptional activation; this repression is relieved by
CC       the Mediator complex, which restores Pol II(G) activator-dependent
CC       transcription to a level equivalent to that of Pol II.
CC       {ECO:0000269|PubMed:16769904}.
CC   -!- SUBUNIT: Isoform 1 is a component of the Pol II(G) complex, which
CC       contains the RNA polymerase II (Pol II) core complex subunits and
CC       POLR2M isoform 1. Pol II(G) appears to be an abundant form of Pol II.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=Gdown1;
CC         IsoId=P0CAP2-1; Sequence=Displayed;
CC       Name=2; Synonyms=Gdown6;
CC         IsoId=P0CAP2-2; Sequence=VSP_037387;
CC       Name=3;
CC         IsoId=P0CAP2-3; Sequence=VSP_037388;
CC       Name=4; Synonyms=Gdown4;
CC         IsoId=Q6EEV4-1; Sequence=External;
CC       Name=5; Synonyms=Gdown3;
CC         IsoId=Q6EEV4-2; Sequence=External;
CC       Name=11; Synonyms=Gcom1, GRINL1A complex locus protein 1;
CC         IsoId=P0CAP1-11; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Detected in adult an fetal brain. Detected in
CC       heart, kidney, skeletal muscle, small intestine, lung, prostate and
CC       testis. {ECO:0000269|PubMed:15233991}.
CC   -!- MISCELLANEOUS: The adjacent MYZAP and POLR2M genes are part of a
CC       complex transcription unit. The respective transcripts derive from
CC       different promoters and are alternatively spliced. In human, some
CC       transcripts of the upstream promoter of MYZAP use exons of the
CC       downstream POLR2M gene.
CC   -!- SIMILARITY: Belongs to the GRINL1 family. {ECO:0000305}.
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DR   EMBL; AF326773; AAK92284.2; -; mRNA.
DR   EMBL; AY207007; AAO39707.1; -; mRNA.
DR   EMBL; AY353061; AAQ76837.1; -; mRNA.
DR   EMBL; AK074767; BAC11193.1; -; mRNA.
DR   EMBL; AK074955; BAC11313.1; -; mRNA.
DR   EMBL; AK128618; BAC87533.1; -; mRNA.
DR   EMBL; AC090651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471082; EAW77525.1; -; Genomic_DNA.
DR   EMBL; BC001510; AAH01510.1; -; mRNA.
DR   EMBL; AL050091; CAB43263.1; -; mRNA.
DR   CCDS; CCDS32252.1; -. [P0CAP2-1]
DR   CCDS; CCDS42045.1; -. [P0CAP2-2]
DR   PIR; T08740; T08740.
DR   RefSeq; NP_001018112.1; NM_001018102.2. [P0CAP2-2]
DR   RefSeq; NP_056347.1; NM_015532.4. [P0CAP2-1]
DR   PDB; 6DRD; EM; 3.90 A; M=300-316.
DR   PDBsum; 6DRD; -.
DR   AlphaFoldDB; P0CAP2; -.
DR   SMR; P0CAP2; -.
DR   BioGRID; 123498; 131.
DR   DIP; DIP-61933N; -.
DR   IntAct; P0CAP2; 61.
DR   MINT; P0CAP2; -.
DR   STRING; 9606.ENSP00000299638; -.
DR   GlyGen; P0CAP2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P0CAP2; -.
DR   PhosphoSitePlus; P0CAP2; -.
DR   BioMuta; POLR2M; -.
DR   DMDM; 238064986; -.
DR   EPD; P0CAP2; -.
DR   jPOST; P0CAP2; -.
DR   MassIVE; P0CAP2; -.
DR   MaxQB; P0CAP2; -.
DR   PaxDb; P0CAP2; -.
DR   PeptideAtlas; P0CAP2; -.
DR   PRIDE; P0CAP2; -.
DR   ProteomicsDB; 52428; -. [P0CAP2-1]
DR   ProteomicsDB; 52429; -. [P0CAP2-2]
DR   ProteomicsDB; 52430; -. [P0CAP2-3]
DR   Antibodypedia; 57855; 103 antibodies from 15 providers.
DR   DNASU; 81488; -.
DR   Ensembl; ENST00000299638.8; ENSP00000299638.3; ENSG00000255529.9. [P0CAP2-1]
DR   Ensembl; ENST00000380557.4; ENSP00000369930.4; ENSG00000255529.9. [P0CAP2-2]
DR   Ensembl; ENST00000482852.5; ENSP00000432615.1; ENSG00000255529.9. [P0CAP2-3]
DR   GeneID; 81488; -.
DR   KEGG; hsa:81488; -.
DR   MANE-Select; ENST00000299638.8; ENSP00000299638.3; NM_015532.5; NP_056347.1.
DR   UCSC; uc002aet.6; human. [P0CAP2-1]
DR   CTD; 81488; -.
DR   DisGeNET; 81488; -.
DR   GeneCards; POLR2M; -.
DR   HGNC; HGNC:14862; POLR2M.
DR   HPA; ENSG00000255529; Low tissue specificity.
DR   MIM; 606485; gene.
DR   neXtProt; NX_P0CAP2; -.
DR   OpenTargets; ENSG00000255529; -.
DR   PharmGKB; PA28986; -.
DR   VEuPathDB; HostDB:ENSG00000255529; -.
DR   eggNOG; ENOG502S3HI; Eukaryota.
DR   GeneTree; ENSGT00950000183065; -.
DR   HOGENOM; CLU_051512_0_0_1; -.
DR   InParanoid; P0CAP2; -.
DR   OMA; PRKQKFK; -.
DR   PhylomeDB; P0CAP2; -.
DR   TreeFam; TF332945; -.
DR   PathwayCommons; P0CAP2; -.
DR   SignaLink; P0CAP2; -.
DR   SIGNOR; P0CAP2; -.
DR   BioGRID-ORCS; 81488; 154 hits in 1035 CRISPR screens.
DR   ChiTaRS; POLR2M; human.
DR   GenomeRNAi; 81488; -.
DR   Pharos; P0CAP2; Tbio.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P0CAP2; protein.
DR   Bgee; ENSG00000255529; Expressed in germinal epithelium of ovary and 205 other tissues.
DR   ExpressionAtlas; P0CAP2; baseline and differential.
DR   Genevisible; P0CAP2; HS.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005635; C:nuclear envelope; IDA:LIFEdb.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IPI:FlyBase.
DR   GO; GO:0016591; C:RNA polymerase II, holoenzyme; IDA:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0051685; P:maintenance of ER location; IBA:GO_Central.
DR   InterPro; IPR026213; GRINL1.
DR   Pfam; PF15328; GCOM2; 1.
DR   PRINTS; PR02085; POLR2GRINL1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil;
KW   DNA-directed RNA polymerase; Nucleus; Reference proteome; Transcription.
FT   CHAIN           1..368
FT                   /note="DNA-directed RNA polymerase II subunit GRINL1A"
FT                   /id="PRO_5000089546"
FT   REGION          116..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          301..335
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        116..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         39..195
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15233991"
FT                   /id="VSP_037387"
FT   VAR_SEQ         323..368
FT                   /note="MQAKLAAQKLAERLNIKMRSYNPEGESSGRYREVRDEDDDWSSDEF -> RP
FT                   FYSPQYRSSMNLLSLAAAAKDTRGSKSGKMGSLALLTKL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_037388"
FT   CONFLICT        171
FT                   /note="H -> D (in Ref. 7; CAB43263)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  41740 MW;  B2F3ADAC21793D1E CRC64;
     MCSLPRGFEP QAPEDLAQRS LVELREMLKR QERLLRNEKF ICKLPDKGKK IFDSFAKLKA
     AIAECEEVRR KSELFNPVSL DCKLRQKAIA EVDVGTDKAQ NSDPILDTSS LVPGCSSVDN
     IKSSQTSQNQ GLGRPTLEGD EETSEVEYTV NKGPASSNRD RVPPSSEASE HHPRHRVSSQ
     AEDTSSSFDN LFIDRLQRIT IADQGEQQSE ENASTKNLTG LSSGTEKKPH YMEVLEMRAK
     NPVPQLRKFK TNVLPFRQND SSSHCQKSGS PISSEERRRR DKQHLDDITA ARLLPLHHMP
     TQLLSIEESL ALQKQQKQNY EEMQAKLAAQ KLAERLNIKM RSYNPEGESS GRYREVRDED
     DDWSSDEF
 
 
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