PAGE4_HUMAN
ID PAGE4_HUMAN Reviewed; 102 AA.
AC O60829; B2R529; D3DX68; Q6IBI1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=P antigen family member 4;
DE Short=PAGE-4;
DE AltName: Full=G antigen family C member 1;
DE AltName: Full=PAGE-1;
GN Name=PAGE4; Synonyms=GAGEC1; ORFNames=JM27;
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], AND TISSUE SPECIFICITY.
RX PubMed=9724777; DOI=10.1073/pnas.95.18.10757;
RA Brinkmann U., Vasmatzis G., Lee B., Yerushalmi N., Essand M., Pastan I.;
RT "PAGE-1, an X chromosome-linked GAGE-like gene that is expressed in normal
RT and neoplastic prostate, testis, and uterus.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10757-10762(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
RA Meindl A.;
RT "Transcription map in Xp11.23.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12489849;
RA Iavarone C., Wolfgang C., Kumar V., Duray P., Willingham M., Pastan I.,
RA Bera T.K.;
RT "PAGE4 is a cytoplasmic protein that is expressed in normal prostate and in
RT prostate cancers.";
RL Mol. Cancer Ther. 1:329-335(2002).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=21357425; DOI=10.1074/jbc.m110.210765;
RA Zeng Y., He Y., Yang F., Mooney S.M., Getzenberg R.H., Orban J.,
RA Kulkarni P.;
RT "The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly
RT intrinsically disordered protein.";
RL J. Biol. Chem. 286:13985-13994(2011).
RN [11]
RP FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=25374899;
RA Zeng Y., Gao D., Kim J.J., Shiraishi T., Terada N., Kakehi Y., Kong C.,
RA Getzenberg R.H., Kulkarni P.;
RT "Prostate-associated gene 4 (PAGE4) protects cells against stress by
RT elevating p21 and suppressing reactive oxygen species production.";
RL Am. J. Clin. Exp. Urol. 1:39-52(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51, AND IDENTIFICATION BY
RP 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 [13]
RP FUNCTION, PHOSPHORYLATION AT THR-51, MUTAGENESIS OF THR-51, INTERACTION
RP WITH JUN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24559171; DOI=10.1021/bi500013w;
RA Mooney S.M., Qiu R., Kim J.J., Sacho E.J., Rajagopalan K., Johng D.,
RA Shiraishi T., Kulkarni P., Weninger K.R.;
RT "Cancer/testis antigen PAGE4, a regulator of c-Jun transactivation, is
RT phosphorylated by homeodomain-interacting protein kinase 1, a component of
RT the stress-response pathway.";
RL Biochemistry 53:1670-1679(2014).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP JUN.
RX PubMed=24263171; DOI=10.1016/j.bbadis.2013.11.014;
RA Rajagopalan K., Qiu R., Mooney S.M., Rao S., Shiraishi T., Sacho E.,
RA Huang H., Shapiro E., Weninger K.R., Kulkarni P.;
RT "The Stress-response protein prostate-associated gene 4, interacts with c-
RT Jun and potentiates its transactivation.";
RL Biochim. Biophys. Acta 1842:154-163(2014).
RN [15]
RP PHOSPHORYLATION AT SER-9 AND THR-51, AND INTERACTION WITH JUN.
RX PubMed=26242913; DOI=10.1074/jbc.m115.658583;
RA He Y., Chen Y., Mooney S.M., Rajagopalan K., Bhargava A., Sacho E.,
RA Weninger K., Bryan P.N., Kulkarni P., Orban J.;
RT "Phosphorylation-induced conformational ensemble switching in an
RT intrinsically disordered cancer/testis antigen.";
RL J. Biol. Chem. 290:25090-25102(2015).
RN [16]
RP REVIEW.
RX PubMed=27270343; DOI=10.4103/1008-682x.181818;
RA Kulkarni P., Dunker A.K., Weninger K., Orban J.;
RT "Prostate-associated gene 4 (PAGE4), an intrinsically disordered
RT cancer/testis antigen, is a novel therapeutic target for prostate cancer.";
RL Asian J. Androl. 18:695-703(2016).
RN [17]
RP FUNCTION, AND PHOSPHORYLATION AT SER-7; SER-9; THR-51; THR-71; SER-73;
RP SER-79; THR-85 AND THR-94.
RX PubMed=28289210; DOI=10.1073/pnas.1700082114;
RA Kulkarni P., Jolly M.K., Jia D., Mooney S.M., Bhargava A., Kagohara L.T.,
RA Chen Y., Hao P., He Y., Veltri R.W., Grishaev A., Weninger K., Levine H.,
RA Orban J.;
RT "Phosphorylation-induced conformational dynamics in an intrinsically
RT disordered protein and potential role in phenotypic heterogeneity.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E2644-E2653(2017).
RN [18]
RP FUNCTION, AND INDUCTION.
RX PubMed=30658679; DOI=10.1186/s13046-019-1032-3;
RA Lv C., Fu S., Dong Q., Yu Z., Zhang G., Kong C., Fu C., Zeng Y.;
RT "PAGE4 promotes prostate cancer cells survive under oxidative stress
RT through modulating MAPK/JNK/ERK pathway.";
RL J. Exp. Clin. Cancer Res. 38:24-24(2019).
CC -!- FUNCTION: Intrinsically disordered protein that potentiates the
CC transcriptional activator activity of JUN (PubMed:24263171,
CC PubMed:28289210). Protects cells from stress-induced apoptosis by
CC inhibiting reactive oxygen species (ROS) production and via regulation
CC of the MAPK signaling pathway (PubMed:21357425, PubMed:25374899,
CC PubMed:30658679). {ECO:0000269|PubMed:21357425,
CC ECO:0000269|PubMed:24263171, ECO:0000269|PubMed:25374899,
CC ECO:0000269|PubMed:28289210, ECO:0000269|PubMed:30658679}.
CC -!- SUBUNIT: Interacts with JUN. {ECO:0000269|PubMed:24263171,
CC ECO:0000269|PubMed:24559171, ECO:0000269|PubMed:26242913}.
CC -!- INTERACTION:
CC O60829; P05412: JUN; NbExp=2; IntAct=EBI-27085632, EBI-852823;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12489849,
CC ECO:0000269|PubMed:24559171, ECO:0000269|PubMed:25374899}. Nucleus
CC {ECO:0000269|PubMed:24559171}. Mitochondrion
CC {ECO:0000269|PubMed:25374899}. Note=Translocates to mitochondria in
CC response to stress. {ECO:0000269|PubMed:25374899}.
CC -!- TISSUE SPECIFICITY: Expressed at basal lvels in the adult normal
CC prostate gland but is highly up-regulated in the fetal prostate and
CC prostate cancer cells (PubMed:12489849, PubMed:25374899,
CC PubMed:24559171, PubMed:24263171). Preferentially expressed in normal
CC male and female reproductive tissues, testis, fallopian tube, uterus,
CC and placenta, as well as in testicular cancer, uterine cancer, cervical
CC cancer and kidney cancer (PubMed:9724777, PubMed:12489849).
CC {ECO:0000269|PubMed:12489849, ECO:0000269|PubMed:24263171,
CC ECO:0000269|PubMed:24559171, ECO:0000269|PubMed:25374899,
CC ECO:0000269|PubMed:9724777}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the earlier stages of fetal
CC development, expression decreases dramatically by the time the pre-
CC pubertal prostate buds are developed (36 weeks).
CC {ECO:0000269|PubMed:24263171}.
CC -!- INDUCTION: Up-regulated in response to a variety of stress factors.
CC {ECO:0000269|PubMed:25374899, ECO:0000269|PubMed:30658679}.
CC -!- PTM: HIPK1-mediated phosphorylation at Thr-51 leads to the compaction
CC of its intrinsically disordered conformation and is critical for its
CC ability to potentiate the transcriptional activator activity of JUN
CC inspite of a reduced interaction with JUN (PubMed:24559171,
CC PubMed:26242913). CLK2-mediated phosphorylation at multiple Ser and Thr
CC residues attenuates its ability to potentiate JUN transcriptional
CC activator activity (PubMed:28289210). {ECO:0000269|PubMed:24559171,
CC ECO:0000269|PubMed:26242913, ECO:0000269|PubMed:28289210}.
CC -!- SIMILARITY: Belongs to the GAGE family. {ECO:0000305}.
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DR EMBL; AF275258; AAF88037.1; -; mRNA.
DR EMBL; AJ005894; CAA06751.1; -; mRNA.
DR EMBL; CR456823; CAG33104.1; -; mRNA.
DR EMBL; CR542183; CAG46980.1; -; mRNA.
DR EMBL; AK312039; BAG34976.1; -; mRNA.
DR EMBL; AF238380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471180; EAW89932.1; -; Genomic_DNA.
DR EMBL; CH471180; EAW89933.1; -; Genomic_DNA.
DR EMBL; BC010897; AAH10897.1; -; mRNA.
DR CCDS; CCDS35274.1; -.
DR RefSeq; NP_001305806.1; NM_001318877.1.
DR RefSeq; NP_008934.1; NM_007003.4.
DR PDB; 6URQ; X-ray; 2.05 A; C/D=1-102.
DR PDBsum; 6URQ; -.
DR AlphaFoldDB; O60829; -.
DR SMR; O60829; -.
DR BioGRID; 114884; 258.
DR IntAct; O60829; 1.
DR STRING; 9606.ENSP00000218068; -.
DR iPTMnet; O60829; -.
DR PhosphoSitePlus; O60829; -.
DR BioMuta; PAGE4; -.
DR jPOST; O60829; -.
DR MassIVE; O60829; -.
DR PaxDb; O60829; -.
DR PeptideAtlas; O60829; -.
DR PRIDE; O60829; -.
DR ProteomicsDB; 49621; -.
DR Antibodypedia; 12225; 92 antibodies from 20 providers.
DR DNASU; 9506; -.
DR Ensembl; ENST00000218068.7; ENSP00000218068.6; ENSG00000101951.17.
DR Ensembl; ENST00000376141.5; ENSP00000365311.1; ENSG00000101951.17.
DR GeneID; 9506; -.
DR KEGG; hsa:9506; -.
DR MANE-Select; ENST00000218068.7; ENSP00000218068.6; NM_007003.4; NP_008934.1.
DR UCSC; uc004don.3; human.
DR CTD; 9506; -.
DR DisGeNET; 9506; -.
DR GeneCards; PAGE4; -.
DR HGNC; HGNC:4108; PAGE4.
DR HPA; ENSG00000101951; Group enriched (epididymis, placenta).
DR MIM; 300287; gene.
DR neXtProt; NX_O60829; -.
DR OpenTargets; ENSG00000101951; -.
DR PharmGKB; PA28523; -.
DR VEuPathDB; HostDB:ENSG00000101951; -.
DR eggNOG; ENOG502TF3A; Eukaryota.
DR GeneTree; ENSGT00940000153097; -.
DR HOGENOM; CLU_150116_1_0_1; -.
DR InParanoid; O60829; -.
DR OMA; IEPGQEK; -.
DR OrthoDB; 949920at2759; -.
DR PhylomeDB; O60829; -.
DR TreeFam; TF340669; -.
DR PathwayCommons; O60829; -.
DR SignaLink; O60829; -.
DR SIGNOR; O60829; -.
DR BioGRID-ORCS; 9506; 11 hits in 694 CRISPR screens.
DR ChiTaRS; PAGE4; human.
DR GenomeRNAi; 9506; -.
DR Pharos; O60829; Tbio.
DR PRO; PR:O60829; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O60829; protein.
DR Bgee; ENSG00000101951; Expressed in corpus epididymis and 117 other tissues.
DR Genevisible; O60829; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; IDA:UniProtKB.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; TAS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IDA:UniProtKB.
DR DisProt; DP01435; -.
DR InterPro; IPR031320; GAGE.
DR InterPro; IPR008625; GAGE_fam.
DR PANTHER; PTHR14047; PTHR14047; 1.
DR Pfam; PF05831; GAGE; 1.
DR SMART; SM01379; GAGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..102
FT /note="P antigen family member 4"
FT /id="PRO_0000148348"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine; by CLK2"
FT /evidence="ECO:0000269|PubMed:28289210"
FT MOD_RES 9
FT /note="Phosphoserine; by HIPK1 and CLK2"
FT /evidence="ECO:0000269|PubMed:26242913,
FT ECO:0000269|PubMed:28289210"
FT MOD_RES 51
FT /note="Phosphothreonine; by HIPK1 and CLK2"
FT /evidence="ECO:0000269|PubMed:24559171,
FT ECO:0000269|PubMed:26242913, ECO:0000269|PubMed:28289210,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphothreonine; by CLK2"
FT /evidence="ECO:0000269|PubMed:28289210"
FT MOD_RES 73
FT /note="Phosphoserine; by CLK2"
FT /evidence="ECO:0000269|PubMed:28289210"
FT MOD_RES 79
FT /note="Phosphoserine; by CLK2"
FT /evidence="ECO:0000269|PubMed:28289210"
FT MOD_RES 85
FT /note="Phosphothreonine; by CLK2"
FT /evidence="ECO:0000269|PubMed:28289210"
FT MOD_RES 94
FT /note="Phosphothreonine; by CLK2"
FT /evidence="ECO:0000269|PubMed:28289210"
FT MUTAGEN 51
FT /note="T->A: Loss of phosphorylation and its ability to
FT potentiate JUN transcriptional activator activity."
FT /evidence="ECO:0000269|PubMed:24263171"
SQ SEQUENCE 102 AA; 11153 MW; CE5D07AFBF73301B CRC64;
MSARVRSRSR GRGDGQEAPD VVAFVAPGES QQEEPPTDNQ DIEPGQEREG TPPIEERKVE
GDCQEMDLEK TRSERGDGSD VKEKTPPNPK HAKTKEAGDG QP
