PRR14_MOUSE
ID PRR14_MOUSE Reviewed; 612 AA.
AC Q7TPN9; Q922N8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Proline-rich protein 14;
GN Name=Prr14;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Egg;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor, and Olfactory epithelium;
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 [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=25906157; DOI=10.1038/cddis.2015.103;
RA Yang M., Yuan Z.M.;
RT "A novel role of PRR14 in the regulation of skeletal myogenesis.";
RL Cell Death Dis. 6:E1734-E1734(2015).
CC -!- FUNCTION: Functions in tethering peripheral heterochromatin to the
CC nuclear lamina during interphase, possibly through the interaction with
CC heterochromatin protein CBX5/HP1 alpha (By similarity). Might play a
CC role in reattaching heterochromatin to the nuclear lamina at mitotic
CC exit (By similarity). Promotes myoblast differentiation during skeletal
CC myogenesis, possibly by stimulating transcription factor MyoD activity
CC via binding to CBX5/HP1 alpha (PubMed:25906157) (By similarity).
CC Involved in the positive regulation of the PI3K-Akt-mTOR signaling
CC pathway and in promoting cell proliferation, possibly via binding to
CC GRB2 (By similarity). {ECO:0000250|UniProtKB:Q9BWN1,
CC ECO:0000269|PubMed:25906157}.
CC -!- SUBUNIT: Interacts (via proline-rich region) with GRB2 (via SH3 domain
CC 2). Interacts (via N-terminus) with CBX5.
CC {ECO:0000250|UniProtKB:Q9BWN1}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q9BWN1}.
CC Nucleus {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus lamina
CC {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9BWN1}. Note=During interphase, associated with
CC peripheral heterochromatin at the nuclear lamina. Released from the
CC nuclear lamina in mitotic prophase and remains highly dispersed in
CC metaphase. Associates with chromatin at the onset of anaphase and
CC relocalizes to the nuclear lamina in telophase.
CC {ECO:0000250|UniProtKB:Q9BWN1}.
CC -!- DEVELOPMENTAL STAGE: Expressed in skeletal myocytes with increasing
CC expression during differentiation and in the gastrocnemius skeletal
CC muscle in newborn and at higher levels in 10 days old mice (at protein
CC level). {ECO:0000269|PubMed:25906157}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06909.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK139559; BAE24061.1; -; mRNA.
DR EMBL; AK145816; BAE26669.1; -; mRNA.
DR EMBL; AK151203; BAE30200.1; -; mRNA.
DR EMBL; BC006909; AAH06909.1; ALT_SEQ; mRNA.
DR EMBL; BC055033; AAH55033.1; -; mRNA.
DR CCDS; CCDS21868.1; -.
DR RefSeq; NP_663564.2; NM_145589.2.
DR RefSeq; XP_006507804.1; XM_006507741.3.
DR RefSeq; XP_006507805.1; XM_006507742.3.
DR AlphaFoldDB; Q7TPN9; -.
DR BioGRID; 231469; 2.
DR STRING; 10090.ENSMUSP00000033095; -.
DR iPTMnet; Q7TPN9; -.
DR PhosphoSitePlus; Q7TPN9; -.
DR EPD; Q7TPN9; -.
DR MaxQB; Q7TPN9; -.
DR PaxDb; Q7TPN9; -.
DR PeptideAtlas; Q7TPN9; -.
DR PRIDE; Q7TPN9; -.
DR ProteomicsDB; 291566; -.
DR Antibodypedia; 66800; 74 antibodies from 19 providers.
DR DNASU; 233895; -.
DR Ensembl; ENSMUST00000033095; ENSMUSP00000033095; ENSMUSG00000030822.
DR Ensembl; ENSMUST00000106292; ENSMUSP00000101899; ENSMUSG00000030822.
DR GeneID; 233895; -.
DR KEGG; mmu:233895; -.
DR UCSC; uc009jvo.1; mouse.
DR CTD; 78994; -.
DR MGI; MGI:2384565; Prr14.
DR VEuPathDB; HostDB:ENSMUSG00000030822; -.
DR eggNOG; ENOG502RJ6E; Eukaryota.
DR GeneTree; ENSGT00520000055626; -.
DR HOGENOM; CLU_489653_0_0_1; -.
DR InParanoid; Q7TPN9; -.
DR OMA; VWSSQAR; -.
DR OrthoDB; 484832at2759; -.
DR PhylomeDB; Q7TPN9; -.
DR TreeFam; TF328446; -.
DR BioGRID-ORCS; 233895; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Prr14; mouse.
DR PRO; PR:Q7TPN9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7TPN9; protein.
DR Bgee; ENSMUSG00000030822; Expressed in granulocyte and 250 other tissues.
DR ExpressionAtlas; Q7TPN9; baseline and differential.
DR Genevisible; Q7TPN9; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR InterPro; IPR026320; PRR14.
DR InterPro; IPR028149; Tantalus-like.
DR PANTHER; PTHR14522; PTHR14522; 1.
DR Pfam; PF15386; Tantalus; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Myogenesis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..612
FT /note="Proline-rich protein 14"
FT /id="PRO_0000307270"
FT REGION 1..135
FT /note="Sufficient for heterochromatin association in
FT interphase and chromatin association in anaphase"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..405
FT /note="Required for the interaction with GRB2 and
FT sufficient to promote the phosphorylation of AKT and cell
FT proliferation"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT REGION 119..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..392
FT /note="Required for nuclear lamina association"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT REGION 206..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..563
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT REGION 553..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..256
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWN1"
SQ SEQUENCE 612 AA; 67811 MW; F316E6431B8FF3BA CRC64;
MDLPGNSSPF TQPSLCRQPL SRASWEARSP KRPRLQPLGT PSSLEKASRR VLAVVLEDVM
TTNRVPLTHK EDTPSPLTHN HHQDPVCTQS PALPSQQVKW SMQARPPDPL HLCREPLTRA
RQSSPALRMR SRAASGPEES PSKKTDQVPQ PTLVVVLEDI ASGRQPAEGF DEDQPNLIVP
AQSTFRSLKG PGKHCHRRGL DLEARPTLTL SLHPRAEPVT KAGQPMPTPS DLEPPFQLST
LPADPPESPV PDPALETPVI PTSSSLLRPR LSPWGLAPLF RSVRSKLESF ADIFFTPNKT
PQPPPPSPPM KLELKIAISE AEQSRATEKI TSVSPRPPIR QWRTQCNSLA PVSKSSLGRS
YSCPDLGPPD PGSWPPVPSQ PSQSRPRRHT VGCGEMARTP PPPRPCLRKE VFPLGGVGVS
PSLTTSCSAN APASFFCEPA EPRLGSTKGK ELRASKDKVF SDPETKTMGK VSRFRIRRTP
VRLQPNLTPM GLPRPIRLNK KEFTLEEIYT NKNYQSPTTR RTFETIFEEP RERNGTLIFT
SSRKLRRAVE FRDSSLPRSR RPSRGVRTAA SRTLTPNLAP SQDVGSLLQE RLRELDALLL
EEETDKEHPC HL
