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   24-JAN-2024, entry version 175.
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,
RC   Spleen, and 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; 12.
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; 10090-ENSMUSP00000022816; -.
DR   PeptideAtlas; P11031; -.
DR   ProteomicsDB; 263092; -.
DR   Pumba; P11031; -.
DR   Antibodypedia; 681; 318 antibodies from 32 providers.
DR   DNASU; 20024; -.
DR   Ensembl; ENSMUST00000022816.15; ENSMUSP00000022816.9; ENSMUSG00000022205.16.
DR   Ensembl; ENSMUST00000110504.2; ENSMUSP00000106130.2; ENSMUSG00000022205.16.
DR   GeneID; 20024; -.
DR   KEGG; mmu:20024; -.
DR   UCSC; uc007vhj.1; mouse.
DR   AGR; MGI:104811; -.
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; 5489415at2759; -.
DR   PhylomeDB; P11031; -.
DR   TreeFam; TF313859; -.
DR   BioGRID-ORCS; 20024; 17 hits in 79 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 256 other cell types or tissues.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:1905463; P:negative regulation of DNA duplex unwinding; 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 by RNA polymerase II; IEA:InterPro.
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:0001111; P:RNA polymerase II promoter clearance; ISO:MGI.
DR   InterPro; IPR003173; PC4_C.
DR   InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
DR   InterPro; IPR045125; Sub1/Tcp4-like.
DR   PANTHER; PTHR13215:SF0; ACTIVATED RNA POLYMERASE II TRANSCRIPTIONAL COACTIVATOR P15; 1.
DR   PANTHER; PTHR13215; RNA POLYMERASE II TRANSCRIPTIONAL COACTIVATOR; 1.
DR   Pfam; PF02229; PC4; 1.
DR   SUPFAM; SSF54447; ssDNA-binding transcriptional regulator domain; 1.
DR   Genevisible; P11031; MM.
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
//