ID E1JGN0_DROME Unreviewed; 1141 AA. AC E1JGN0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 31-JUL-2019, entry version 81. DE RecName: Full=Non-specific serine/threonine protein kinase {ECO:0000256|SAAS:SAAS00804148}; DE EC=2.7.11.1 {ECO:0000256|SAAS:SAAS00804148}; GN Name=par-1 {ECO:0000313|EMBL:ACZ94480.1, GN ECO:0000313|FlyBase:FBgn0260934}; GN Synonyms=27C1 {ECO:0000313|EMBL:ACZ94480.1}, anon-WO0210402.19 GN {ECO:0000313|EMBL:ACZ94480.1}, BcDNA:RH48823 GN {ECO:0000313|EMBL:ACZ94480.1}, CG11960 {ECO:0000313|EMBL:ACZ94480.1}, GN CG16701 {ECO:0000313|EMBL:ACZ94480.1}, CG30131 GN {ECO:0000313|EMBL:ACZ94480.1}, CG30132 {ECO:0000313|EMBL:ACZ94480.1}, GN dMARK {ECO:0000313|EMBL:ACZ94480.1}, Dmel\CG8201 GN {ECO:0000313|EMBL:ACZ94480.1}, DPAR-1 {ECO:0000313|EMBL:ACZ94480.1}, GN dPAR-1 {ECO:0000313|EMBL:ACZ94480.1}, dPar-1 GN {ECO:0000313|EMBL:ACZ94480.1}, DPar1 {ECO:0000313|EMBL:ACZ94480.1}, GN dPAR1 {ECO:0000313|EMBL:ACZ94480.1}, dPar1 GN {ECO:0000313|EMBL:ACZ94480.1}, EMK {ECO:0000313|EMBL:ACZ94480.1}, GN l(2)27C1 {ECO:0000313|EMBL:ACZ94480.1}, l(2)k06323 GN {ECO:0000313|EMBL:ACZ94480.1}, MARK {ECO:0000313|EMBL:ACZ94480.1}, GN PAR-1 {ECO:0000313|EMBL:ACZ94480.1}, Par-1 GN {ECO:0000313|EMBL:ACZ94480.1}, PAR1 {ECO:0000313|EMBL:ACZ94480.1}, GN Par1 {ECO:0000313|EMBL:ACZ94480.1}, par1 GN {ECO:0000313|EMBL:ACZ94480.1}; GN ORFNames=CG8201 {ECO:0000313|EMBL:ACZ94480.1, GN ECO:0000313|FlyBase:FBgn0260934}, Dmel_CG8201 GN {ECO:0000313|EMBL:ACZ94480.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., RA Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002). RN [5] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:ACZ94480.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000256|SAAS:SAAS01117232}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000256|SAAS:SAAS01117231}; 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; AE013599; ACZ94480.1; -; Genomic_DNA. DR RefSeq; NP_001163208.1; NM_001169737.2. DR STRING; 7227.FBpp0290718; -. DR PRIDE; E1JGN0; -. DR EnsemblMetazoa; FBtr0301503; FBpp0290718; FBgn0260934. DR GeneID; 2768852; -. DR CTD; 2768852; -. DR FlyBase; FBgn0260934; par-1. DR GeneTree; ENSGT00940000166198; -. DR InParanoid; E1JGN0; -. DR SignaLink; E1JGN0; -. DR ChiTaRS; par-1; fly. DR GenomeRNAi; 2768852; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0260934; Expressed in 32 organ(s), highest expression level in head. DR ExpressionAtlas; E1JGN0; differential. DR Genevisible; E1JGN0; DM. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase. DR GO; GO:0005938; C:cell cortex; IDA:FlyBase. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0045169; C:fusome; IDA:FlyBase. DR GO; GO:0045172; C:germline ring canal; IDA:FlyBase. DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase. DR GO; GO:0061174; C:type I terminal bouton; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase. DR GO; GO:0050321; F:tau-protein kinase activity; IDA:FlyBase. DR GO; GO:0009948; P:anterior/posterior axis specification; TAS:FlyBase. DR GO; GO:0019730; P:antimicrobial humoral response; IMP:FlyBase. DR GO; GO:0009798; P:axis specification; IMP:FlyBase. DR GO; GO:0030709; P:border follicle cell delamination; IMP:FlyBase. DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase. DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase. DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase. DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; IMP:FlyBase. DR GO; GO:0009994; P:oocyte differentiation; TAS:FlyBase. DR GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase. DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase. DR GO; GO:0045451; P:pole plasm oskar mRNA localization; TAS:FlyBase. DR GO; GO:0007318; P:pole plasm protein localization; IMP:FlyBase. DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase. DR GO; GO:0030860; P:regulation of polarized epithelial cell differentiation; IMP:FlyBase. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase. DR GO; GO:0051124; P:synaptic growth at neuromuscular junction; IMP:FlyBase. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR001772; KA1_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR015940; UBA. DR Pfam; PF02149; KA1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00165; UBA; 1. DR SUPFAM; SSF103243; SSF103243; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50032; KA1; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50030; UBA; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|SAAS:SAAS00804144}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Kinase {ECO:0000256|SAAS:SAAS00804143}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00804159}; KW Proteomics identification {ECO:0000213|PeptideAtlas:E1JGN0}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00804166}; KW Transferase {ECO:0000256|SAAS:SAAS00804145, KW ECO:0000313|EMBL:ACZ94480.1}. FT DOMAIN 481 732 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT DOMAIN 751 793 UBA. {ECO:0000259|PROSITE:PS50030}. FT DOMAIN 1092 1141 KA1. {ECO:0000259|PROSITE:PS50032}. FT REGION 1 131 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 279 329 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 359 439 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 796 861 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 920 969 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 38 62 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 63 97 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 300 329 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 363 381 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 404 418 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 802 853 Polar. {ECO:0000256|SAM:MobiDB-lite}. SQ SEQUENCE 1141 AA; 124626 MW; 0798140BE6A3764F CRC64; MEATTTTTPD LNRGDATRKS VRLYAARKGA APAPPKLSVA PSSNQNSNHS SNNNNSSSNL PETEKEMELR QTHLANKDLD GATEDDSIVE LRRRDAQATP LPRIAVSALP TLQPHPTPKE RQKPPMPRLL STEDDAGVSF ALGSIEKHIH NVEESFKQQQ QNQQSQSSMD VMKLEIKRKQ SKRYGETENL LRPGISDMSS ENDFQYLGGR RAGELDDSNE LMLSEFQRGS DGRNSIGAYS KNSAAAANGA NAVKAKLART ASDTKNNDTV LAMRATFKQK QHLQDEKQPA VWRPAGTGPT PAARSSSSTT STSGSASRGG SSSSVVDGVA PSKLTATTIS ASKRREENLR QFEALLAQKS SHRHGASGAS GTGSNAASSK RRSDRPIVAP IPPYNSSRAE HVTSSTRHSV DPRSHSGHES RSGTASTHPP VGHHPTSRVP SVVANRSNVY SNNAAQGSPN MQMRSSAPMR WRATEEHIGK YKLIKTIGKG NFAKVKLAKH LPTGKEVAIK IIDKTQLNPG SLQKLFREVR IMKMLDHPNI VKLFQVIETE KTLYLIMEYA SGGEVFDYLV LHGRMKEKEA RVKFRQIVSA VQYCHQKRII HRDLKAENLL LDSELNIKIA DFGFSNEFTP GSKLDTFCGS PPYAAPELFQ GKKYDGPEVD VWSLGVILYT LVSGSLPFDG STLRELRERV LRGKYRIPFY MSTDCENLLR KFLVLNPAKR ASLETIMGDK WMNMGFEEDE LKPYIEPKAD LADPKRIGKT EALVAMGYNR SEIEASLSQV RYDDVFATYL LLGRKSTDPE SDGSRSGSSL SLRNISGNDA GANAGSASVQ SPTHRGVHRS ISASSTKPSR RASSGAETLR VGPTNAAATV AAATGAVGAV NPSNNYNAAG SAADRASVGS NFKRQNTIDS ATIKENTARL AAQNQRPASA TQKMLTTADT TLNSPAKPRT ATKYDPTNGN RTVSGTSGII PRRSTTLYEK TSSTEKTNVI PAETKARNNT ALEYSGTSGA SGDSSHPGRM SFFSKLSSRF SKRPTIADEA AKPRVLRFTW SMKTTSPLMP DQIMQKIREV LDQNNCDYEQ RERFVLWCVH GDPNTDSLVQ WEIEVCKLPR LSLNGVRFKR ISGTSIGFKN IASRIAFDLK L //