PRR14_HUMAN
ID PRR14_HUMAN Reviewed; 585 AA.
AC Q9BWN1; Q8WTX2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Proline-rich protein 14;
GN Name=PRR14;
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 [LARGE SCALE MRNA].
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-359.
RC TISSUE=Eye, and Pancreas;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 54-VAL-VAL-55.
RX PubMed=24209742; DOI=10.1016/j.celrep.2013.09.024;
RA Poleshko A., Mansfield K.M., Burlingame C.C., Andrake M.D., Shah N.R.,
RA Katz R.A.;
RT "The human protein PRR14 tethers heterochromatin to the nuclear lamina
RT during interphase and mitotic exit.";
RL Cell Rep. 5:292-301(2013).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CBX5, AND MUTAGENESIS OF
RP 54-VAL-VAL-55.
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).
RN [9]
RP FUNCTION, INTERACTION WITH GRB2, AND MUTAGENESIS OF SER-101 AND GLU-566.
RX PubMed=27041574; DOI=10.1038/onc.2016.93;
RA Yang M., Lewinska M., Fan X., Zhu J., Yuan Z.M.;
RT "PRR14 is a novel activator of the PI3K pathway promoting lung
RT carcinogenesis.";
RL Oncogene 35:5527-5538(2016).
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 (PubMed:24209742). Might play a
CC role in reattaching heterochromatin to the nuclear lamina at mitotic
CC exit (PubMed:24209742). Promotes myoblast differentiation during
CC skeletal myogenesis, possibly by stimulating transcription factor MyoD
CC activity via binding to CBX5/HP1 alpha (PubMed:25906157). Involved in
CC the positive regulation of the PI3K-Akt-mTOR signaling pathway and in
CC promoting cell proliferation, possibly via binding to GRB2
CC (PubMed:27041574). {ECO:0000269|PubMed:24209742,
CC ECO:0000269|PubMed:25906157, ECO:0000269|PubMed:27041574}.
CC -!- SUBUNIT: Interacts (via proline-rich region) with GRB2 (via SH3 domain
CC 2) (PubMed:27041574). Interacts (via N-terminus) with CBX5
CC (PubMed:25906157). {ECO:0000269|PubMed:25906157,
CC ECO:0000269|PubMed:27041574}.
CC -!- INTERACTION:
CC Q9BWN1; Q13185: CBX3; NbExp=6; IntAct=EBI-748167, EBI-78176;
CC Q9BWN1; P45973: CBX5; NbExp=10; IntAct=EBI-748167, EBI-78219;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:24209742}. Nucleus
CC {ECO:0000269|PubMed:25906157}. Nucleus lamina
CC {ECO:0000269|PubMed:24209742}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24209742}. 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:0000269|PubMed:24209742}.
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DR EMBL; AK074783; BAC11207.1; -; mRNA.
DR EMBL; CH471192; EAW52222.1; -; Genomic_DNA.
DR EMBL; BC000119; AAH00119.1; -; mRNA.
DR EMBL; BC021934; AAH21934.1; -; mRNA.
DR EMBL; BC050677; AAH50677.1; -; mRNA.
DR CCDS; CCDS10687.1; -.
DR RefSeq; NP_001307393.1; NM_001320464.1.
DR RefSeq; NP_076936.1; NM_024031.3.
DR AlphaFoldDB; Q9BWN1; -.
DR BioGRID; 122465; 38.
DR IntAct; Q9BWN1; 22.
DR MINT; Q9BWN1; -.
DR STRING; 9606.ENSP00000441641; -.
DR iPTMnet; Q9BWN1; -.
DR PhosphoSitePlus; Q9BWN1; -.
DR BioMuta; PRR14; -.
DR DMDM; 74733447; -.
DR EPD; Q9BWN1; -.
DR jPOST; Q9BWN1; -.
DR MassIVE; Q9BWN1; -.
DR MaxQB; Q9BWN1; -.
DR PaxDb; Q9BWN1; -.
DR PeptideAtlas; Q9BWN1; -.
DR PRIDE; Q9BWN1; -.
DR ProteomicsDB; 79294; -.
DR Antibodypedia; 66800; 74 antibodies from 19 providers.
DR DNASU; 78994; -.
DR Ensembl; ENST00000300835.9; ENSP00000300835.4; ENSG00000156858.12.
DR Ensembl; ENST00000542965.2; ENSP00000441641.2; ENSG00000156858.12.
DR GeneID; 78994; -.
DR KEGG; hsa:78994; -.
DR MANE-Select; ENST00000300835.9; ENSP00000300835.4; NM_024031.5; NP_076936.1.
DR UCSC; uc002dyy.4; human.
DR CTD; 78994; -.
DR DisGeNET; 78994; -.
DR GeneCards; PRR14; -.
DR HGNC; HGNC:28458; PRR14.
DR HPA; ENSG00000156858; Low tissue specificity.
DR MIM; 617423; gene.
DR neXtProt; NX_Q9BWN1; -.
DR OpenTargets; ENSG00000156858; -.
DR PharmGKB; PA144596393; -.
DR VEuPathDB; HostDB:ENSG00000156858; -.
DR eggNOG; ENOG502RJ6E; Eukaryota.
DR GeneTree; ENSGT00520000055626; -.
DR HOGENOM; CLU_489653_0_0_1; -.
DR InParanoid; Q9BWN1; -.
DR OMA; VWSSQAR; -.
DR OrthoDB; 484832at2759; -.
DR PhylomeDB; Q9BWN1; -.
DR TreeFam; TF328446; -.
DR PathwayCommons; Q9BWN1; -.
DR SignaLink; Q9BWN1; -.
DR BioGRID-ORCS; 78994; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; PRR14; human.
DR GenomeRNAi; 78994; -.
DR Pharos; Q9BWN1; Tbio.
DR PRO; PR:Q9BWN1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BWN1; protein.
DR Bgee; ENSG00000156858; Expressed in granulocyte and 195 other tissues.
DR ExpressionAtlas; Q9BWN1; baseline and differential.
DR Genevisible; Q9BWN1; HS.
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; IDA:HPA.
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..585
FT /note="Proline-rich protein 14"
FT /id="PRO_0000307269"
FT REGION 1..135
FT /note="Sufficient for heterochromatin association in
FT interphase and chromatin association in anaphase"
FT /evidence="ECO:0000269|PubMed:24209742"
FT REGION 23..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..378
FT /note="Required for the interaction with GRB2 and
FT sufficient to promote the phosphorylation of AKT and cell
FT proliferation"
FT /evidence="ECO:0000269|PubMed:25906157,
FT ECO:0000269|PubMed:27041574"
FT REGION 136..365
FT /note="Required for nuclear lamina association"
FT /evidence="ECO:0000269|PubMed:24209742"
FT REGION 189..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..535
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000269|PubMed:24209742"
FT REGION 525..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 359
FT /note="P -> L (in dbSNP:rs3747481)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035389"
FT MUTAGEN 54..55
FT /note="VV->AA: Loss of heterochromatin association. Loss of
FT interaction with CBX5."
FT /evidence="ECO:0000269|PubMed:24209742,
FT ECO:0000269|PubMed:25906157"
FT MUTAGEN 54..55
FT /note="VV->EE: Loss of heterochromatin association during
FT interphase and loss of chromatin association during
FT anaphase."
FT /evidence="ECO:0000269|PubMed:24209742"
FT MUTAGEN 101
FT /note="S->C: Increased binding to GRB2 and enhanced cell
FT proliferation."
FT /evidence="ECO:0000269|PubMed:27041574"
FT MUTAGEN 566
FT /note="E->K: Increased binding to GRB2 and enhanced cell
FT proliferation."
FT /evidence="ECO:0000269|PubMed:27041574"
SQ SEQUENCE 585 AA; 64328 MW; EE706853CE2D2742 CRC64;
MDLPGDSSPP GQPRLCRQPL TRALWGARSP KRPRLQLPGA PSPLEKASRR VLAVVLEDVM
AVHMVPVVPS KQTSIPQHHS YHQDPVHRQP PASPPRQAGW SSQARPPDPL CLCREPLSRI
HRTSSTLRRR SRTTPGPEEG PSQKVDRAPQ PTLVVMLEDI ASPRPPAEGF IDETPNFIIP
AQRAEPMRIV RQPTPPPGDL EPPFQPSALP ADPLESPPTA PDPALELPST PPPSSLLRPR
LSPWGLAPLF RSVRSKLESF ADIFLTPNKT PQPPPPSPPM KLELKIAISE AEQSGAAEGT
ASVSPRPPIR QWRTQDHNTP ALLPKPSLGR SYSCPDLGPP GPGTCTWPPA PPQPSRPRPR
RHTVGGGEMA RAPPPPRPCL RKEVFPLGGV GASPSLTTSC SSTASTSFSE PAEPRLGSTK
GKEPRASKDQ VLSEPETKTM GKVSRFRIRR TPARPQLNLT PMGLPRPIRL NKKEFSLEEI
YTNKNYQSPT TRRTFETIFE EPRERNGTLI FTSSRKLRRA VEFRDSSLPR SRRPSRGVRA
AGGRTVPPNV APSPDVGPLL QQRLEELDAL LLEEETVDRE QPHWT
