PJA2_MOUSE
ID PJA2_MOUSE Reviewed; 707 AA.
AC Q80U04; Q3TH95; Q810E3; Q91W46; Q99KC0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=E3 ubiquitin-protein ligase Praja-2;
DE Short=Praja2;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 131;
DE AltName: Full=RING-type E3 ubiquitin transferase Praja-2 {ECO:0000305};
GN Name=Pja2; Synonyms=Kiaa0438, Rnf131;
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 1), AND FUNCTION.
RC STRAIN=129/SvJ;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 326-707 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 8-18, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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 Responsible for ubiquitination of cAMP-dependent protein kinase type I
CC and type II-alpha/beta regulatory subunits and for targeting them for
CC proteasomal degradation. Essential for PKA-mediated long-term memory
CC processes. Through the ubiquitination of MFHAS1, positively regulates
CC the TLR2 signaling pathway that leads to the activation of the
CC downstream p38 and JNK MAP kinases and promotes the polarization of
CC macrophages toward the pro-inflammatory M1 phenotype.
CC {ECO:0000250|UniProtKB:O43164, 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Binds ubiquitin-conjugating enzymes (E2s). In vitro, interacts
CC with the ubiquitin-conjugating enzyme, UBE2D2. The phosphorylated form
CC interacts with PRKAR1A, PRKAR2A and PRKAR2B. Binds the catalytic
CC subunits of cAMP-dependent protein kinase. Interacts with MFHAS1.
CC {ECO:0000250|UniProtKB:O43164}.
CC -!- INTERACTION:
CC Q80U04; P61809: Cdk5r1; NbExp=2; IntAct=EBI-1801691, EBI-7840438;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}.
CC Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi
CC apparatus membrane; Peripheral membrane protein. Synapse {ECO:0000250}.
CC Postsynaptic density {ECO:0000250}. Note=Localizes at the cytoplasmic
CC side of endoplasmic reticulum and Golgi apparatus. Expressed in the
CC postsynaptic density region of synapses. Co-localizes with PRKAR2A and
CC PRKAR2B in the cytoplasm and the cell membrane (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80U04-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U04-2; Sequence=VSP_023199;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65564.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF493070; AAO85470.1; -; mRNA.
DR EMBL; AK122282; BAC65564.1; ALT_INIT; mRNA.
DR EMBL; AK144586; BAE25949.1; -; mRNA.
DR EMBL; AK168371; BAE40303.1; -; mRNA.
DR EMBL; BC004742; AAH04742.1; -; mRNA.
DR EMBL; BC017130; AAH17130.1; -; mRNA.
DR CCDS; CCDS37674.1; -. [Q80U04-2]
DR CCDS; CCDS37675.1; -. [Q80U04-1]
DR RefSeq; NP_001020480.1; NM_001025309.1. [Q80U04-1]
DR RefSeq; NP_659108.1; NM_144859.2. [Q80U04-2]
DR AlphaFoldDB; Q80U04; -.
DR SMR; Q80U04; -.
DR BioGRID; 230345; 7.
DR DIP; DIP-47060N; -.
DR IntAct; Q80U04; 2.
DR STRING; 10090.ENSMUSP00000134380; -.
DR iPTMnet; Q80U04; -.
DR PhosphoSitePlus; Q80U04; -.
DR EPD; Q80U04; -.
DR jPOST; Q80U04; -.
DR MaxQB; Q80U04; -.
DR PaxDb; Q80U04; -.
DR PeptideAtlas; Q80U04; -.
DR PRIDE; Q80U04; -.
DR ProteomicsDB; 289651; -. [Q80U04-1]
DR ProteomicsDB; 289652; -. [Q80U04-2]
DR Antibodypedia; 25290; 231 antibodies from 31 providers.
DR DNASU; 224938; -.
DR Ensembl; ENSMUST00000024888; ENSMUSP00000024888; ENSMUSG00000024083. [Q80U04-1]
DR Ensembl; ENSMUST00000024889; ENSMUSP00000024889; ENSMUSG00000024083. [Q80U04-2]
DR Ensembl; ENSMUST00000172733; ENSMUSP00000133730; ENSMUSG00000024083. [Q80U04-2]
DR Ensembl; ENSMUST00000172818; ENSMUSP00000134380; ENSMUSG00000024083. [Q80U04-1]
DR GeneID; 224938; -.
DR KEGG; mmu:224938; -.
DR UCSC; uc008dfu.1; mouse. [Q80U04-1]
DR UCSC; uc008dfv.1; mouse. [Q80U04-2]
DR CTD; 9867; -.
DR MGI; MGI:2159342; Pja2.
DR VEuPathDB; HostDB:ENSMUSG00000024083; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000154585; -.
DR HOGENOM; CLU_026830_1_0_1; -.
DR InParanoid; Q80U04; -.
DR OMA; HFSAREK; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q80U04; -.
DR TreeFam; TF330711; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 224938; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Pja2; mouse.
DR PRO; PR:Q80U04; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q80U04; protein.
DR Bgee; ENSMUSG00000024083; Expressed in dorsal pancreas and 251 other tissues.
DR Genevisible; Q80U04; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISS:UniProtKB.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0035329; P:hippo signaling; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:UniProtKB.
DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0043030; P:regulation of macrophage activation; ISO:MGI.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR030639; Praja-2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710:SF5; PTHR15710:SF5; 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 Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Synapse;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43164"
FT CHAIN 2..707
FT /note="E3 ubiquitin-protein ligase Praja-2"
FT /id="PRO_0000278231"
FT ZN_FING 633..674
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..707
FT /note="Interaction with PRKAR1A, PRKAR2A and PRKAR2B"
FT /evidence="ECO:0000250"
FT REGION 685..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O43164"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43164"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43164"
FT MOD_RES 339
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O43164"
FT MOD_RES 385
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O43164"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43164"
FT VAR_SEQ 426..488
FT /note="SSECSDGEWSASLPHRFSGTEKDQSSSDDSWETLPGKDENDPELQSDSSGPE
FT EENQELSLQEG -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023199"
FT CONFLICT 230
FT /note="E -> A (in Ref. 3; BAE40303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 77958 MW; F0D45E2267CC7EAA CRC64;
MSQYTEKEPS VMDQESSKAA WPKPAGGYQT ITGRRYGRRH AYVSFKPCMT RHERSLGRAG
DDYEVLELDD VPKENTSGSS SLDQVHPALP NEPTVEKSET EISTCGPALN QSTESSPSIA
TVCHSEEVRE TLESNTNLHN RTETEHTPAV CNVSSVQNGI MLVHTDSYDP DSKHDENGSL
QLGAEAVEGG RHQKGLGRAV FELENGEAEI YADLSPSVPS LNGEISEAFE ELDSAPLEKS
STADAELVHQ NGQEFQRSSE DGVVRKRRQD DTDQGRQTEN STEDADCAPG HVEQNTSDRA
NHHGSSPEQV VRPKVRKVIS SSQVDQEIGF NRHEAKQRSV QRWREALEVE ECSSDDPIIK
CDDYDGDHDC MFLTPTYSRV TQRETERNRV TSENGATASG RQESRDNAFW NACGEYYQLF
DKDEDSSECS DGEWSASLPH RFSGTEKDQS SSDDSWETLP GKDENDPELQ SDSSGPEEEN
QELSLQEGEQ TSLEEGEIPW LQYNEVNESS SDEGNEPANE FAQPEAFMLD GNNNLEDDSS
VSEDLDVDWS LFDGFADGLG VAEAISYVDP QFLTYMALEE RLAQAMETAL AHLESLAVDV
EVANPPASKE SIDGLPETLV LEDHTAIGQE QCCPICCSEY IKDDIATELP CHHFFHKPCV
SIWLQKSGTC PVCRRHFPPA VIDASAAASS DPDPDASPAN DNAEEAP
