PJA2_HUMAN
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 03-AUG-2022, entry version 179.
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 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, 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, SUBCELLULAR LOCATION, INTERACTION WITH PRKAR1A; PRKAR2A AND
RP PRKAR2B, AND PHOSPHORYLATION AT SER-342 AND 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).
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 (PubMed:28471450).
CC {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175,
CC ECO:0000269|PubMed:28471450}.
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 (PubMed:28471450). {ECO:0000269|PubMed:12036302,
CC ECO:0000269|PubMed:21423175, ECO:0000269|PubMed:28471450}.
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}. Postsynaptic
CC density {ECO:0000250}. Note=Localizes at the cytoplasmic side of
CC endoplasmic reticulum and Golgi apparatus. Expressed in the
CC postsynaptic density region of synapses (By similarity). Colocalizes
CC with PRKAR2A and PRKAR2B in the cytoplasm and the cell membrane.
CC {ECO:0000250}.
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};
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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. [O43164-1]
DR AlphaFoldDB; O43164; -.
DR SMR; O43164; -.
DR BioGRID; 115200; 78.
DR DIP; DIP-47040N; -.
DR IntAct; O43164; 39.
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; O43164; -.
DR PeptideAtlas; O43164; -.
DR PRIDE; O43164; -.
DR ProteomicsDB; 48781; -. [O43164-1]
DR ProteomicsDB; 48782; -. [O43164-2]
DR Antibodypedia; 25290; 231 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 CTD; 9867; -.
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; HFSAREK; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; O43164; -.
DR TreeFam; TF330711; -.
DR PathwayCommons; O43164; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O43164; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 9867; 10 hits in 1119 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 209 other tissues.
DR Genevisible; O43164; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0035329; P:hippo signaling; IEA:InterPro.
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: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 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: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 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
