PJA1_MOUSE
ID PJA1_MOUSE Reviewed; 578 AA.
AC O55176; Q8CFU2; Q99MJ1; Q99MJ2; Q99MJ3; Q9DB04;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=E3 ubiquitin-protein ligase Praja-1;
DE Short=Praja1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase Praja-1 {ECO:0000305};
GN Name=Pja1;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=9393880; DOI=10.1038/sj.onc.1201405;
RA Mishra L., Tully R.E., Monga S.P.S., Yu P., Cai T., Makalowski W.,
RA Mezey E., Pavan W.J., Mishra B.;
RT "Praja1, a novel gene encoding a RING-H2 motif in mouse development.";
RL Oncogene 15:2361-2368(1997).
RN [2]
RP SEQUENCE REVISION.
RA Mishra L.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Amygdala;
RX PubMed=11533224; DOI=10.1101/lm.39401;
RA Stork O., Stork S., Pape H.-C., Obata K.;
RT "Identification of genes expressed in the amygdala during the formation of
RT fear memory.";
RL Learn. Memory 8:209-219(2001).
RN [4]
RP SEQUENCE REVISION TO C-TERMINUS (ISOFORMS 1 AND 3).
RA Stork O., Stork S.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [7]
RP FUNCTION AS A UBIQUITATION LIGASE, AND MUTAGENESIS OF HIS-553.
RX PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.;
RT "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN [8]
RP FUNCTION, AND INTERACTION WITH UBE2D2.
RX PubMed=12036302; DOI=10.1006/geno.2002.6770;
RA Yu P., Chen Y., Tagle D.A., Cai T.;
RT "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X
RT chromosome gene abundantly expressed in brain.";
RL Genomics 79:869-874(2002).
RN [9]
RP INTERACTION WITH MAGED1, AND MUTAGENESIS OF CYS-533.
RX PubMed=11959851; DOI=10.1074/jbc.m109728200;
RA Sasaki A., Masuda Y., Iwai K., Ikeda K., Watanabe K.;
RT "A RING finger protein Praja1 regulates Dlx5-dependent transcription
RT through its ubiquitin ligase activity for the Dlx/Msx-interacting
RT MAGE/Necdin family protein, Dlxin-1.";
RL J. Biol. Chem. 277:22541-22546(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-231; SER-317 AND SER-319, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, 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).
CC -!- FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity.
CC Ubiquitinates MAGED1 antigen leading to its subsequent degradation by
CC proteasome. May be involved in protein sorting.
CC {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:12036302}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBUNIT: Binds ubiquitin-conjugating enzymes (E2s). Binds, in vitro and
CC in vivo, the MAGE conserved domain of MAGED1. Binds weakly Necdin, in
CC vitro. Interacts with UBE2D2. {ECO:0000269|PubMed:11959851,
CC ECO:0000269|PubMed:12036302}.
CC -!- INTERACTION:
CC O55176-2; Q9QYH6: Maged1; NbExp=2; IntAct=EBI-1801670, EBI-1801274;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Alternative splicing appears to be tissue-specific.;
CC Name=1; Synonyms=Praja1a;
CC IsoId=O55176-3; Sequence=Displayed;
CC Name=2;
CC IsoId=O55176-2; Sequence=VSP_007519;
CC Name=3; Synonyms=Praja1c;
CC IsoId=O55176-4; Sequence=VSP_007521;
CC Name=4; Synonyms=Praja1d;
CC IsoId=O55176-5; Sequence=VSP_022011, VSP_007520;
CC -!- TISSUE SPECIFICITY: Expressed in brain, liver, kidney. Highest levels
CC in brain where it is found in many regions including cortical and
CC subcortical areas and in neurons of the amygdala. Weak expression also
CC found in testis. Also expressed in developing embryo.
CC -!- INDUCTION: By fear memory. Differential induction of isoforms.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC conjugating enzyme (E2) and facilitates ubiquitination.
CC -!- PTM: Substrate for E2-dependent ubiquitination.
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DR EMBL; U06944; AAC00205.2; -; mRNA.
DR EMBL; AF335250; AAK15764.2; -; mRNA.
DR EMBL; AF335251; AAK15765.2; -; mRNA.
DR EMBL; AF335252; AAK15766.1; -; mRNA.
DR EMBL; AK005373; BAB23982.1; -; mRNA.
DR EMBL; BC037616; AAH37616.1; -; mRNA.
DR CCDS; CCDS41070.1; -. [O55176-3]
DR RefSeq; NP_001076579.1; NM_001083110.2. [O55176-3]
DR RefSeq; NP_032879.2; NM_008853.3.
DR AlphaFoldDB; O55176; -.
DR BMRB; O55176; -.
DR SMR; O55176; -.
DR BioGRID; 202189; 3.
DR IntAct; O55176; 3.
DR iPTMnet; O55176; -.
DR PhosphoSitePlus; O55176; -.
DR jPOST; O55176; -.
DR MaxQB; O55176; -.
DR PaxDb; O55176; -.
DR PeptideAtlas; O55176; -.
DR PRIDE; O55176; -.
DR ProteomicsDB; 287740; -. [O55176-3]
DR ProteomicsDB; 287741; -. [O55176-2]
DR ProteomicsDB; 287742; -. [O55176-4]
DR ProteomicsDB; 287743; -. [O55176-5]
DR Antibodypedia; 402; 164 antibodies from 32 providers.
DR DNASU; 18744; -.
DR Ensembl; ENSMUST00000036354; ENSMUSP00000109420; ENSMUSG00000034403. [O55176-3]
DR Ensembl; ENSMUST00000113792; ENSMUSP00000109423; ENSMUSG00000034403. [O55176-3]
DR Ensembl; ENSMUST00000167246; ENSMUSP00000132393; ENSMUSG00000034403. [O55176-3]
DR GeneID; 18744; -.
DR KEGG; mmu:18744; -.
DR UCSC; uc009tvl.1; mouse. [O55176-3]
DR CTD; 64219; -.
DR MGI; MGI:1101765; Pja1.
DR VEuPathDB; HostDB:ENSMUSG00000034403; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000154585; -.
DR HOGENOM; CLU_026830_1_0_1; -.
DR InParanoid; O55176; -.
DR OMA; FNHDVRE; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; O55176; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 18744; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Pja1; mouse.
DR PRO; PR:O55176; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O55176; protein.
DR Bgee; ENSMUSG00000034403; Expressed in substantia propria of cornea and 280 other tissues.
DR ExpressionAtlas; O55176; baseline and differential.
DR Genevisible; O55176; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0030163; P:protein catabolic process; IDA:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031227; PJA1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710:SF2; PTHR15710:SF2; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..578
FT /note="E3 ubiquitin-protein ligase Praja-1"
FT /id="PRO_0000056000"
FT ZN_FING 530..571
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 60..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9393880"
FT /id="VSP_007519"
FT VAR_SEQ 185..187
FT /note="ARP -> PLF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11533224"
FT /id="VSP_022011"
FT VAR_SEQ 188..578
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11533224"
FT /id="VSP_007520"
FT VAR_SEQ 197..411
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11533224"
FT /id="VSP_007521"
FT MUTAGEN 533
FT /note="C->A: No effect on MAGED1 binding. Decrease in
FT ubiquitination of MAGED1. No inhibition of DLX5-dependent
FT transcriptional activity."
FT /evidence="ECO:0000269|PubMed:11959851"
FT MUTAGEN 553
FT /note="H->S: Loss of ubiquitination activity."
FT /evidence="ECO:0000269|PubMed:10500182"
FT CONFLICT 236
FT /note="D -> DD (in Ref. 3; AAK15764)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="I -> M (in Ref. 5; BAB23982)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="A -> T (in Ref. 3; AAK15764/AAK15765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 63906 MW; 11B2D3C1F8982143 CRC64;
MSHQERIASQ RRTTAEVPMH RSTANQSKRS RSPFASTRRR WDDSESSGAS LAVESEDYSR
YPPREYRASG SRRGLAYGHI DTVVARDSEE EGAGPVDRLP VRGKAGKFKD DPEKGARSSR
FTSVNHDAKE ECGKVESPPA ARCSARRAEL SKQNGSSASQ ISSAEGRAAA KGNNSLERER
QNLPARPSRA PVSICGGGEN TPKSAEEPVV RPKVRNVATP NCMKPKVFFD TDDDDDVPHS
TSRWRDAADA EEAHAEGLAR RGRGEAASSS EPRYAEDQDA RSEQAKADKV PRRRRTMADP
DFWAYTDDYY RYYEEDSDSD KEWMAALRRK YRSREQPQSS SGESWELLPG KEELERQQAG
AGSLASAGSN GSGYPEEVQD PSLQEEEQAS LEEGEIPWLR YNENESSSEG DNESTHELIQ
PGMFMLDGNN NLEDDSSVSE DLEVDWSLFD GFADGLGVAE AISYVDPQFL TYMALEERLA
QAMETALAHL ESLAVDVEVA NPPASKESID ALPEILVTED HGAVGQEMCC PICCSEYVKG
EVATELPCHH YFHKPCVSIW LQKSGTCPVC RCMFPPPL
