TCP4_MOUSE
ID TCP4_MOUSE Reviewed; 127 AA.
AC P11031; Q3UJR5; Q543N2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Activated RNA polymerase II transcriptional coactivator p15;
DE AltName: Full=Positive cofactor 4;
DE Short=PC4;
DE AltName: Full=SUB1 homolog;
DE AltName: Full=Single-stranded DNA-binding protein p9;
DE AltName: Full=p14;
GN Name=Sub1; Synonyms=Pc4, Rpo2tc1;
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], PROTEIN SEQUENCE OF 51-81 AND 108-127,
RP PROTEOLYTIC PROCESSING, AND DNA-BINDING.
RX PubMed=3372536; DOI=10.1016/s0021-9258(18)68498-4;
RA Ballard D.W., Philbrick W.M., Bothwell A.L.M.;
RT "Identification of a novel 9-kDa polypeptide from nuclear extracts. DNA
RT binding properties, primary structure, and in vitro expression.";
RL J. Biol. Chem. 263:8450-8457(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Bone marrow;
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].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: General coactivator that functions cooperatively with TAFs
CC and mediates functional interactions between upstream activators and
CC the general transcriptional machinery. May be involved in stabilizing
CC the multiprotein transcription complex. Binds single-stranded DNA. Also
CC binds, in vitro, non-specifically to double-stranded DNA (ds DNA).
CC -!- SUBUNIT: Homodimer. Interacts with CSTF2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Activity is controlled by protein kinases that target the
CC regulatory region. Phosphorylation inactivates both ds DNA-binding and
CC cofactor function, but does not affect binding to ssDNA (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transcriptional coactivator PC4 family.
CC {ECO:0000305}.
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DR EMBL; J03750; AAA37317.1; -; mRNA.
DR EMBL; AK048371; BAC33314.1; -; mRNA.
DR EMBL; AK049260; BAC33642.1; -; mRNA.
DR EMBL; AK132021; BAE20946.1; -; mRNA.
DR EMBL; AK146335; BAE27090.1; -; mRNA.
DR EMBL; AK151734; BAE30649.1; -; mRNA.
DR EMBL; AK154114; BAE32384.1; -; mRNA.
DR EMBL; BC010967; AAH10967.1; -; mRNA.
DR CCDS; CCDS27387.1; -.
DR PIR; A28084; A28084.
DR RefSeq; NP_035424.1; NM_011294.3.
DR RefSeq; XP_006520105.1; XM_006520042.3.
DR AlphaFoldDB; P11031; -.
DR SMR; P11031; -.
DR BioGRID; 202999; 11.
DR CORUM; P11031; -.
DR IntAct; P11031; 2.
DR MINT; P11031; -.
DR STRING; 10090.ENSMUSP00000022816; -.
DR iPTMnet; P11031; -.
DR PhosphoSitePlus; P11031; -.
DR EPD; P11031; -.
DR jPOST; P11031; -.
DR MaxQB; P11031; -.
DR PaxDb; P11031; -.
DR PeptideAtlas; P11031; -.
DR PRIDE; P11031; -.
DR ProteomicsDB; 263092; -.
DR Antibodypedia; 681; 283 antibodies from 32 providers.
DR DNASU; 20024; -.
DR Ensembl; ENSMUST00000022816; ENSMUSP00000022816; ENSMUSG00000022205.
DR Ensembl; ENSMUST00000110504; ENSMUSP00000106130; ENSMUSG00000022205.
DR GeneID; 20024; -.
DR KEGG; mmu:20024; -.
DR UCSC; uc007vhj.1; mouse.
DR CTD; 10923; -.
DR MGI; MGI:104811; Sub1.
DR VEuPathDB; HostDB:ENSMUSG00000022205; -.
DR eggNOG; KOG2712; Eukaryota.
DR GeneTree; ENSGT00390000008802; -.
DR HOGENOM; CLU_104273_1_1_1; -.
DR InParanoid; P11031; -.
DR OMA; WMNPDGE; -.
DR OrthoDB; 1616655at2759; -.
DR PhylomeDB; P11031; -.
DR TreeFam; TF313859; -.
DR BioGRID-ORCS; 20024; 16 hits in 74 CRISPR screens.
DR ChiTaRS; Sub1; mouse.
DR PRO; PR:P11031; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P11031; protein.
DR Bgee; ENSMUSG00000022205; Expressed in undifferentiated genital tubercle and 253 other tissues.
DR Genevisible; P11031; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0003678; F:DNA helicase activity; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0051053; P:negative regulation of DNA metabolic process; ISO:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
DR Gene3D; 2.30.31.10; -; 1.
DR InterPro; IPR003173; PC4_C.
DR InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
DR InterPro; IPR045125; Sub1/Tcp4-like.
DR PANTHER; PTHR13215; PTHR13215; 1.
DR Pfam; PF02229; PC4; 1.
DR SUPFAM; SSF54447; SSF54447; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..127
FT /note="Activated RNA polymerase II transcriptional
FT coactivator p15"
FT /id="PRO_0000023286"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..50
FT /note="Regulatory"
FT REGION 77..101
FT /note="Interaction with ssDNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 50..51
FT /note="Cleavage"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT CONFLICT 46
FT /note="S -> P (in Ref. 2; BAE27090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 14427 MW; 12D58716F40FEB1C CRC64;
MPKSKELVSS SSSGSDSDSE VEKKLKRKKQ AVPEKPVKKQ KPGETSRALA SSKQSSSSRD
DNMFQIGKMR YVSVRDFKGK ILIDIREYWM DSEGEMKPGR KGISLNMEQW SQLKEQISDI
DDAVRKL
