ID PJA2_HUMAN Reviewed; 708 AA. AC O43164; A8K6U4; D3DSZ5; Q68D49; Q8N1G5; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 4. DT 27-MAR-2024, entry version 188. DE RecName: Full=E3 ubiquitin-protein ligase Praja-2; DE Short=Praja2; DE EC=2.3.2.27 {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175}; 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 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] (ISOFORM 1), AND VARIANT ARG-297. RC TISSUE=Brain; RX PubMed=9455477; DOI=10.1093/dnares/4.5.307; RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VIII. 78 RT new cDNA clones from brain which code for large proteins in vitro."; RL DNA Res. 4:307-313(1997). RN [2] RP SEQUENCE REVISION. RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-297. RC TISSUE=Brain; 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 PROTEIN SEQUENCE OF 2-18; 24-34; 59-73; 193-207; 241-258; 388-404 AND RP 583-610, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 456-708 (ISOFORM 2). RC TISSUE=Liver; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, INTERACTION RP WITH PRKAR1A; PRKAR2A AND PRKAR2B, AND PHOSPHORYLATION AT SER-342 AND RP THR-389. RX PubMed=21423175; DOI=10.1038/ncb2209; RA Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R., RA Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A.; RT "Control of PKA stability and signalling by the RING ligase praja2."; RL Nat. Cell Biol. 13:412-422(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-253 AND SER-309, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246, 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 [18] RP FUNCTION, AND INTERACTION WITH MFHAS1. RX PubMed=28471450; DOI=10.1038/cddis.2017.102; RA Zhong J., Wang H., Chen W., Sun Z., Chen J., Xu Y., Weng M., Shi Q., Ma D., RA Miao C.; RT "Ubiquitylation of MFHAS1 by the ubiquitin ligase praja2 promotes M1 RT macrophage polarization by activating JNK and p38 pathways."; RL Cell Death Dis. 8:E2763-E2763(2017). RN [19] RP FUNCTION, INTERACTION WITH TBC1D31, SUBCELLULAR LOCATION, AND REGION. RX PubMed=33934390; DOI=10.15252/embj.2020106503; RA Senatore E., Chiuso F., Rinaldi L., Intartaglia D., Delle Donne R., RA Pedone E., Catalanotti B., Pirone L., Fiorillo B., Moraca F., Giamundo G., RA Scala G., Raffeiner A., Torres-Quesada O., Stefan E., Kwiatkowski M., RA van Pijkeren A., Morleo M., Franco B., Garbi C., Conte I., Feliciello A.; RT "The TBC1D31/praja2 complex controls primary ciliogenesis through PKA- RT directed OFD1 ubiquitylation."; RL EMBO J. 40:e106503-e106503(2021). CC -!- FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity CC (PubMed:12036302, PubMed:21423175). Responsible for ubiquitination of CC cAMP-dependent protein kinase type I and type II-alpha/beta regulatory CC subunits and for targeting them for proteasomal degradation. Essential CC for PKA-mediated long-term memory processes (PubMed:21423175). Through CC the ubiquitination of MFHAS1, positively regulates the TLR2 signaling CC pathway that leads to the activation of the downstream p38 and JNK MAP CC kinases and promotes the polarization of macrophages toward the pro- CC inflammatory M1 phenotype (PubMed:28471450). Plays a role in CC ciliogenesis by ubiquitinating OFD1 (PubMed:33934390). CC {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175, CC ECO:0000269|PubMed:28471450, ECO:0000269|PubMed:33934390}. 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; Evidence={ECO:0000269|PubMed:12036302, CC ECO:0000269|PubMed:21423175}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175}. 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 (PubMed:28471450). Interacts with TBC1D31; the interaction is direct CC and recruits PJA2 to centrosomes (PubMed:33934390). CC {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175, CC ECO:0000269|PubMed:28471450, ECO:0000269|PubMed:33934390}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell CC membrane {ECO:0000269|PubMed:21423175}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:21423175}; Peripheral membrane protein CC {ECO:0000269|PubMed:21423175}. Golgi apparatus membrane CC {ECO:0000269|PubMed:21423175}; Peripheral membrane protein CC {ECO:0000269|PubMed:21423175}. Synapse {ECO:0000250|UniProtKB:Q63364}. CC Postsynaptic density {ECO:0000250|UniProtKB:Q63364}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:33934390}. Note=Localizes at the cytoplasmic side CC of endoplasmic reticulum and Golgi apparatus (PubMed:21423175). CC Expressed in the postsynaptic density region of synapses (By CC similarity). Colocalizes with PRKAR2A and PRKAR2B in the cytoplasm and CC the cell membrane (PubMed:21423175). {ECO:0000250|UniProtKB:Q63364, CC ECO:0000269|PubMed:21423175}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O43164-1; Sequence=Displayed; CC Name=2; CC IsoId=O43164-2; Sequence=VSP_023198; CC -!- SEQUENCE CAUTION: CC Sequence=BAA23710.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AB007898; BAA23710.2; ALT_INIT; mRNA. DR EMBL; AK291759; BAF84448.1; -; mRNA. DR EMBL; AC008467; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471086; EAW49050.1; -; Genomic_DNA. DR EMBL; CH471086; EAW49051.1; -; Genomic_DNA. DR EMBL; BC030826; AAH30826.1; -; mRNA. DR EMBL; CR749579; CAH18371.1; -; mRNA. DR CCDS; CCDS4099.1; -. [O43164-1] DR PIR; T00064; T00064. DR RefSeq; NP_055634.3; NM_014819.4. [O43164-1] DR RefSeq; XP_016865588.1; XM_017010099.1. DR AlphaFoldDB; O43164; -. DR SMR; O43164; -. DR BioGRID; 115200; 143. DR DIP; DIP-47040N; -. DR IntAct; O43164; 44. DR MINT; O43164; -. DR STRING; 9606.ENSP00000354775; -. DR iPTMnet; O43164; -. DR PhosphoSitePlus; O43164; -. DR BioMuta; PJA2; -. DR EPD; O43164; -. DR jPOST; O43164; -. DR MassIVE; O43164; -. DR MaxQB; O43164; -. DR PaxDb; 9606-ENSP00000354775; -. DR PeptideAtlas; O43164; -. DR ProteomicsDB; 48781; -. [O43164-1] DR ProteomicsDB; 48782; -. [O43164-2] DR Pumba; O43164; -. DR Antibodypedia; 25290; 261 antibodies from 31 providers. DR DNASU; 9867; -. DR Ensembl; ENST00000361189.7; ENSP00000354775.2; ENSG00000198961.10. [O43164-1] DR Ensembl; ENST00000361557.4; ENSP00000355284.3; ENSG00000198961.10. [O43164-1] DR GeneID; 9867; -. DR KEGG; hsa:9867; -. DR MANE-Select; ENST00000361189.7; ENSP00000354775.2; NM_014819.5; NP_055634.3. DR UCSC; uc003kos.5; human. [O43164-1] DR AGR; HGNC:17481; -. DR DisGeNET; 9867; -. DR GeneCards; PJA2; -. DR HGNC; HGNC:17481; PJA2. DR HPA; ENSG00000198961; Low tissue specificity. DR MIM; 619341; gene. DR neXtProt; NX_O43164; -. DR OpenTargets; ENSG00000198961; -. DR PharmGKB; PA134873520; -. DR VEuPathDB; HostDB:ENSG00000198961; -. DR eggNOG; KOG0800; Eukaryota. DR GeneTree; ENSGT00940000154585; -. DR HOGENOM; CLU_026830_1_0_1; -. DR InParanoid; O43164; -. DR OMA; NHSEGEC; -. DR OrthoDB; 5474929at2759; -. DR PhylomeDB; O43164; -. DR TreeFam; TF330711; -. DR PathwayCommons; O43164; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; O43164; -. DR SIGNOR; O43164; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 9867; 10 hits in 1197 CRISPR screens. DR ChiTaRS; PJA2; human. DR GeneWiki; PJA2; -. DR GenomeRNAi; 9867; -. DR Pharos; O43164; Tbio. DR PRO; PR:O43164; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; O43164; Protein. DR Bgee; ENSG00000198961; Expressed in cortical plate and 211 other cell types or tissues. DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; ISS:UniProt. DR GO; GO:0005737; C:cytoplasm; IDA: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; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA: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; IMP:UniProtKB. DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IMP:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB. DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB. DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB. DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB. DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IMP:UniProtKB. DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IMP:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0043030; P:regulation of macrophage activation; IMP:UniProtKB. DR GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:UniProtKB. DR CDD; cd16465; RING-H2_PJA1_2; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1. DR PANTHER; PTHR15710:SF5; E3 UBIQUITIN-PROTEIN LIGASE PRAJA-2; 1. DR Pfam; PF13639; zf-RING_2; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; O43164; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton; 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:0000269|Ref.7" FT CHAIN 2..708 FT /note="E3 ubiquitin-protein ligase Praja-2" FT /id="PRO_0000278230" FT ZN_FING 634..675 FT /note="RING-type; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 53..90 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 244..317 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 425..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 531..708 FT /note="Interaction with PRKAR1A, PRKAR2A and PRKAR2B" FT /evidence="ECO:0000269|PubMed:21423175" FT REGION 550..570 FT /note="Mediates interaction with TBC1D31" FT /evidence="ECO:0000269|PubMed:33934390" FT REGION 685..708 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..71 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 73..90 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 245..277 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 448..471 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 478..493 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.7" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 246 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 253 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 323 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 342 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:21423175" FT MOD_RES 389 FT /note="Phosphothreonine; by PKA" FT /evidence="ECO:0000269|PubMed:21423175" FT MOD_RES 432 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT VAR_SEQ 544..563 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_023198" FT VARIANT 176 FT /note="E -> G (in dbSNP:rs35224970)" FT /id="VAR_057215" FT VARIANT 297 FT /note="Q -> R (in dbSNP:rs1045706)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9455477" FT /id="VAR_030698" FT VARIANT 705 FT /note="A -> T (in dbSNP:rs246105)" FT /id="VAR_030699" SQ SEQUENCE 708 AA; 78214 MW; 719B4A367C411735 CRC64; MSQYTEKEPA AMDQESGKAV WPKPAGGYQT ITGRRYGRRH AYVSFKPCMT RHERSLGRAG DDYEVLELDD VPKENSSGSS PLDQVDSSLP SEPIFEKSET EIPTCGSALN QTTESSQSFV AVHHSEEGRD TLGSSTNLHN HSEGEYIPGA CSASSVQNGI ALVHTDSYDP DGKHGEDNDH LQLSAEVVEG SRYQESLGNT VFELENREAE AYTGLSPPVP SFNCEVRDEF EELDSVPLVK SSAGDTEFVH QNSQEIQRSS QDEMVSTKQQ NNTSQERQTE HSPEDAACGP GHICSEQNTN DREKNHGSSP EQVVRPKVRK LISSSQVDQE TGFNRHEAKQ RSVQRWREAL EVEESGSDDL LIKCEEYDGE HDCMFLDPPY SRVITQRETE NNQMTSESGA TAGRQEVDNT FWNGCGDYYQ LYDKDEDSSE CSDGEWSASL PHRFSGTEKD QSSSDESWET LPGKDENEPE LQSDSSGPEE ENQELSLQEG EQTSLEEGEI PWLQYNEVNE SSSDEGNEPA NEFAQPAFML DGNNNLEDDS SVSEDLDVDW SLFDGFADGL GVAEAISYVD PQFLTYMALE ERLAQAMETA LAHLESLAVD VEVANPPASK ESIDGLPETL VLEDHTAIGQ EQCCPICCSE YIKDDIATEL PCHHFFHKPC VSIWLQKSGT CPVCRRHFPP AVIEASAAPS SEPDPDAPPS NDSIAEAP //