wanglab/gogpt-training-data huggingface dataset:
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (CnSOD1) (J9VLJ9)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Destroys radicals produced by host defense mechanisms.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:33567338}. Mitochondrion {ECO:0000269|PubMed:33567338}. Cell membrane {ECO:0000269|PubMed:16524904}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to lipid rafts in the cell membrane. {ECO:0000269|PubMed:16524904}.
Interaction partners:
Sequence:
MVKAVVVLKGESYVHGTVCFTQESENAPVCITGEIKDMDADAKRGMHVHEFGDNTNGCTSAGPHYNPFKKHHGAPTDSERHVGDLGNIQTNSCGAAQLDFSDKIISLYGPHSIIGRSLVVHASTDDLGKGGNEESLKTGNAGARLACGVIGIST
Protein: Fucose-binding lectin PA-IIL (Q9HYN5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PA-I galactophilic lectin
- Elastase
- Protease LasA
- ATP-dependent RNA helicase RhlB
- chitinase
- Outer membrane porin F
- High-affinity zinc uptake system protein ZnuA
Sequence:
MATQGVFTLPANTRFGVTAFANSSGTQTVNVLVNNETAATFSGQSTNNAVIGTQVLNSGSSGKVQVQVSVNGRPSDLVSAQVILTNELNFALVGSEDGTDNDYNDAVVVINWPLG
Protein: Farnesyl pyrophosphate synthase (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase) (O14230)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Farnesyl pyrophosphate synthase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway. Fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Squalene synthase
- Isopentenyl-diphosphate delta-isomerase
- Diphosphomevalonate decarboxylase
- Geranylgeranyl pyrophosphate synthase
- Decaprenyl-diphosphate synthase subunit 1
- Dehydrodolichyl diphosphate synthase complex subunit SPAC4D7.04c-farnesyl diphosphate specific))
- Hydroxymethylglutaryl-CoA synthase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Dehydrodolichyl diphosphate synthase complex subunit nus1
- Protein farnesyltransferase subunit beta
Sequence:
MSAVDKRAKFESALPVFVDEIVNYLKTINIPDDVTEWYKNSLFHNTLGGKYNRGLSVIDSYEILLGHPLDEAAYMKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMPGVGNIAINDAFMVESAIYFLLKKHFRQESCYVDLIELFHDVTFQTELGQQLDLLTAPEDSVDLSKFSLQKHSFIVIYKTAFYSFYLPVALAMHLAGVATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGKIGTDILDNKCSWIINLALAKCTPEQRVILDDNYGRKDSESEKRVKAVFEELNIRGEFENYEESEVSEIKKLIDGVDESTGLKKSIFTTFLGKIYKRNK
Protein: 116 kDa U5 small nuclear ribonucleoprotein component (U5 snRNP-specific protein, 116 kDa) (A0A8I6A4V7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDTDLYDEFGNYIGPELDSDEDDDELGRETKDLDEMDEDEDEDDVGEHDDDHPGMEVVLHEDKKYYPTAEEVYGPEVETIVQEEDTQPLTEPIIKPVKTKKFTLMEQTLPVTVYEMDFLADLMDNSELIRNVTLCGHLHHGKTCFVDCLIEQTHPEIRKRYDQDLCYTDILFTEQERGVGIKSTPVTVVLPDTKGKSYLFNIMDTPGHVNFSDEVTAGLRISDGVVLFIDAAEGVMLNTERLIKHAVQERLAVTVCINKIDRLILELKLPPTDAYYKLRHIVDEVNGLISMYSTDENLILSPLLGNVCFSSSQYSICFTLGSFAKIYADTFGDINYQEFAKRLWGDIYFNPKTRKFTKKAPSSSSQRSFVEFILEPLYKILAQVVGDVDTSLPRTLDELGIHLTKEELKLNIRPLLRLVCKKFFGEFTGFVDMCVQHIPSPKVGAKPKIEHTYTGGVDSDLGEAMSDCDPDGPLMCHTTKMYSTDDGVQFHAFGRVLSGTIHAGQPVKVLGENYTLEDEEDSQICTVGRLWISVARYHIEVNRVPAGNWVLIEGVDQPIVKTATITEPRGNEEAQIFRPLKFNTTSVIKIAVEPVNPSELPKMLDGLRKVNKSYPSLTTKVEESGEHVILGTGELYLDCVMHDLRKMYSEIDIKVADPVVTFCETVVETSSLKCFAETPNKKNKITMIAEPLEKGLAEDIENEVVQITWNRKKLGEFFQTKYDWDLLAARSIWAFGPDDACGRLPNISVQVDKALLGSVKDSIVQGFQWGTREGPLCDELIRNVKFKILDAVVAQEPLHRGGGQIIPTARRVVYSAFLMATPRLMEPYYFVEVQAPADCVSAVYTVLARRRGHVTQDAPIPGSPLYTIKAFIPAIDSFGFETDLRTHTQGQAFSLSVFHHWQIVPGDPLDKSIVIRPLEPQPAPHLAREFMIKTRRRKGLSEDVSISKFFDDPMLLELAKQDVVLNYPM
Protein: Mnt, isoform I (M9NGP0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein max
- Paired amphipathic helix protein Sin3a
- Myc proto-oncogene protein
- FI24210p1
Sequence:
MSGIGGIGVLLEAAQFLEQHEKLPQAGGGGGSALGVGVALPQQQQQTVHCKSNSIINNNNSSQHNRNSSSSSNGIIATPPFTNGNGNGTVGVGNASAIFNVSVNANGNGLSNGHSSPRSQLAAAATAHDYEYSAAGVANGHSEGRPHVSEDDNSSINNNNNNNNTHPPQQQQHSAAGRTTTTRITTTPAILTKLMGNSVTPASNTTSLPTSTPSVTTSPPASTDFMLLAAAATSATSATPATATSAAATAASNPAKRKLSSIAEIPSKFLVVSDAKGVYSAHTHPNGFAADSLGVDNNETMIKKLMQNLQSQRQQQSLQQLRSLRPAEISLTPPPAATRKVDISNSRTRSYSLSNVSAARDQQDHPQHQQHANHMQIQQHYGYMRSNIGGVIYGLHKDSADSAASSACGAGAGAAAVGMSIASSAPAAGSQLSAHHHTGHGGRRRTTSSNSNGAGTREVHNKLEKERRAQLKECYDLLKKVLPMGDEDRKKTSNLTILDTAHKYVNSLSHEVCEQEAKIEKLAKQKIELQKRLKQLSLRRESPPTDQQIIPQADKVCLATTATTAPPTAASGHNGTTILFDAGNACATGQQLTTVINKTNGGATAAASSKHNGNHTGGATTTLTPAMGIMTIKNGNGSNGNMLAISPTGGHNHQLHQHHNGSPAGSPSGIGATTGATITRGSPTPSTPSPSPSSSSSGVSLSTSFMGGSSSSSSSSSSSSSSSSSSSSSSPTQQQQIITPTATARSVGLKFHGGAGAAVPAGGGSVNGFHQADKDRNYTFLRLSAGTTAQ
Protein: CRAL-TRIO domain-containing protein (Q57WJ6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSSSFLEELGPVAVSHRNELEEVKRQLGIERNELDCWIYAFLENKKFDIKETVAKLQRRFAMEVSEMAKYEVTESMRSSLRSGIIQAIGEDKCGRTVFYVTVSRDTSSEGTREEKKRTFDLIVSYGTRLRADNKRCQMVLLVNYENASMLSNVDMSLQMDVATRVSKFFPGCISKVLLCNMGSILCTFMKPVLGTMPASFSDTISLFSSNDVTNGSLLEYIDKSVLPVQLGGTNDCDDQVHWDRYADIIENYYRDMRIAIVERGLKVKDWELECLSANE
Protein: G-protein coupled receptor 176 (HB-954) (Q14439)
Organism: Homo sapiens (Human)
Function: Orphan receptor involved in normal circadian rhythm behavior. Acts through the G-protein subclass G(z)-alpha and has an agonist-independent basal activity to repress cAMP production.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q80WT4}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGHNGSWISPNASEPHNASGAEAAGVNRSALGEFGEAQLYRQFTTTVQVVIFIGSLLGNFMVLWSTCRTTVFKSVTNRFIKNLACSGICASLVCVPFDIILSTSPHCCWWIYTMLFCKVVKFLHKVFCSVTILSFPAIALDRYYSVLYPLERKISDAKSRELVMYIWAHAVVASVPVFAVTNVADIYATSTCTEVWSNSLGHLVYVLVYNITTVIVPVVVVFLFLILIRRALSASQKKKVIIAALRTPQNTISIPYASQREAELHATLLSMVMVFILCSVPYATLVVYQTVLNVPDTSVFLLLTAVWLPKVSLLANPVLFLTVNKSVRKCLIGTLVQLHHRYSRRNVVSTGSGMAEASLEPSIRSGSQLLEMFHIGQQQIFKPTEDEEESEAKYIGSADFQAKEIFSTCLEGEQGPQFAPSAPPLSTVDSVSQVAPAAPVEPETFPDKYSLQFGFGPFELPPQWLSETRNSKKRLLPPLGNTPEELIQTKVPKVGRVERKMSRNNKVSIFPKVDS
Protein: Calcineurin B-like protein 2 (SOS3-like calcium-binding protein 1) (Q8LAS7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Binds four calcium ions per subunit. Mediates the activation of AKT1 by CIPK proteins (CIPK6, CIPK16, and CIPK23) in response to low potassium conditions and in the context of stomatal movement. Mediates the inactivation of the proton pump AHA2 by CIPK11. Probably involved in regulating signaling responses to abscisic acid.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:18502848, ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:22547024, ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060, ECO:0000269|PubMed:23482856}; Lipid-anchor {ECO:0000269|PubMed:18502848, ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:22547024, ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060, ECO:0000269|PubMed:23482856}. Note=The tonoplast localization is S-acylation dependent and is abolished by 2-bromopalmitate (2-BP) treatment.
Interaction partners:
- CBL-interacting serine/threonine-protein kinase 14
- CBL-interacting serine/threonine-protein kinase 11
- CBL-interacting serine/threonine-protein kinase 9
- CBL-interacting serine/threonine-protein kinase 3
- CBL-interacting serine/threonine-protein kinase 21
- CBL-interacting serine/threonine-protein kinase 12
- CBL-interacting serine/threonine-protein kinase 6
- Protein S-acyltransferase 10
- CBL-interacting serine/threonine-protein kinase 24
- CBL-interacting serine/threonine-protein kinase 23
Sequence:
MSQCVDGIKHLCTSVLGCFDLDLYKQSGGLGDPELLARDTVFSVSEIEALYELFKKISSAVIDDGLINKEEFQLALFKTNKKESLFADRVFDLFDTKHNGILGFEEFARALSVFHPNAPIDDKIHFSFQLYDLKQQGFIERQEVKQMVVATLAESGMNLKDTVIEDIIDKTFEEADTKHDGKIDKEEWRSLVLRHPSLLKNMTLQYLKDITTTFPSFVFHSQVEDT
Protein: CG9886-like, isoform CRA_f (Glycerate kinase) (C9JA32)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLLKPHSRVQVFEGAEDNLPDRDALRAALAIQQLAEGLTADDLLLVLISGGGSALLPAPIPPVTLEEKQTLTRLLAARGATIQELNTIRKALSQLKGGGLAQAAYPAQVVSLILSDVVGDPVEVIASGPTVASSHNVQDCLHILNRYGLRAALPRSVKTVLSRADSDPHGPHTCGHVLNVIIGSNVLALAEAQRQAEALGYQAVVLSAAMQGWGTPAAHRDDRYQCHGHPPLVPAASVMA
Protein: Spermidine synthase (Q38BE3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVGKVEVIPNEDIVVGVKNEILRVYPFWKALVELRAVCKRKPALVSCNVRLLDREPCEIFSGVDVVWMRSDIVVSTRRTGTPGTVDIQGGVQCDEEVFGFGSMHFVHRDAHITGDDGSYNLQSVVFFQRQEQMQCVAGYMLHFAFLTHGMMQRCGVHEDEGSGRASFPSATTKVLILGMGGNSMEFGLRHILGVKAHISIVEIEPAVVRTCRRNNLLDGNPNTHIHVKTVEEALLDCPDDFNFIFMDVFEPKTGKMVNSHKLIEKAFAKLAPEGLLVMNEHCIPTASKLRELFRHIGTKCLQYINVKGWNESVITASKMGETRSESTKLYSKALAESVLHSYNAAFPGWMPTYTWIERTRGYTIKNGDEKLFVRQWVT
Protein: Sll1358 protein (P73510)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Kynurenine formamidase
- Formyltetrahydrofolate deformylase
- Sll1785 protein
- Sll1359 protein
- Fumarate hydratase class II
- Malic enzyme
- Malate dehydrogenase
- Phosphoenolpyruvate carboxylase
Sequence:
MVNSVIGWLRRRFLLVGLSVLLITFLGIFTPTIAQSEQWRSLSNVVWGKDLPAFTYAFSKTPLVLYDGGTTKQVGTYNFPVSKGMAGVYMSLEPGAIRELHWHANAAEWAYVMEGRTRITLTSPEGKVEIADVDKGGLWYFPRGWGHSIEGIGPDTAKFLLVFNDGTFSEGATFSVTDWLSHTPIAWVEENLGWTAAQVAQLPKKQVYISSYGPASGPLASATPQGQTAKIEVPHTHNLLGQQPLVSLGGNELRLASAKEFPGSFNMTGALIHLEPGAMRQLHWHPNADEWQYVLDGEMDLTVFASEGKASVSRLQQGDVGYVPKGYGHAIRNSSQKPLDIVVVFNDGDYQSIDLSTWLASNPSSVLGNTFQISPELTKKLPVQDTIFSLPTQP
Protein: Protein SOSEKI 2 (PpSOK2) (A0A2K1L2D9)
Organism: Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens)
Function: SOSEKI proteins locally interpret global polarity cues and can influence cell division orientation to coordinate cell polarization relative to body axes.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9SYJ8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9SYJ8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9SYJ8}.
Interaction partners:
Sequence:
MDSSSESYHKIEVIYLLSKGAEQDDHPHMIQVQYPSHQHAPTLRDVKFRLTALRGRGMPDSYSWSYKRSYKGTFIWCDVFDGDDILPLSESGEYVLKALEVMDSSEDACDRGVEHLGQEVARVLPTNRNGTSANFNEVHSIDDVRRVAPNKCVEVKRQFMGGSVHNNMTGKANRNEQGDAYGTTSRVPDPENCIENKRCLESMTGSDSSRSNISTDESYGLSFERDLKMDMKEMPACPATRSTDHGGMSSLAPRSSRLSRREYVKCKTWAVKEDENAALNHGRLSRRSSDTLRDSNSVGNTVDIPSSPVTRPCFPGDPLIFMLKKATKFHRSQLCRKAEVEGSPCATVGKPSSSRHTSKIRHGSGPLKAYHGPHSSKSATQNSRPVTYETSAKESERDIRSLCQFLGASNVGSVSQTINKEGTKKTGSARHIQAGSNDDFDFARHKEVAVDISEKLLLPEQVTGRYEKPSRMSKQLINKLDSKSLNMVTRPAVRLSSKLGSGQASESFSPASPHAPQRPIVSRPQEKAVNQLSLVAGFEDPQITSSDTSNAGLSCTSKASGLKAVKLPRNASNNCYFSLTIPDLEKRAADTKVYPWRENSAFNSIELYSGTLQKVDLAINTSFNGATLGELASGGC
Protein: Acyl-coenzyme A diphosphatase FITM2 (EC 3.6.1.-) (Fat storage-inducing transmembrane protein 2) (Fat-inducing protein 2) (Q52KL1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity). Required for lipid droplet accumulation in liver and intestine during embryogenesis. May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). May play a role in the regulation of cell morphology, ER morphology and cytoskeletal organization (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03230}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03230}.
Interaction partners:
- BSCL2 lipid droplet biogenesis-associated, seipin.
- Atlastin-1
Sequence:
MAAAVAGSLVDKLVCLWRQPYTRIYLPHLFFCISLVGSVLKNAELVPESYFSSSRNVLNLYFVKVSWGWTIVLLLPFIAYSNFYIKSHMFALRRLTSLLVATLVWYICTETFFYIEDITGSCYESNTMVVIRGEFDTKAACRKAGFFWDGFDISGHSFILSYSSLVIMEEMVPMLHIQPAYRNPPLDCLYLALNVIVAIWIWMFGCTSVYFHDIIDKILGTSCGILGWYMTYKVWYVKLFSPGLPPQPKQHT
Protein: Abscisic acid receptor PYL8 (ABI1-binding protein 1) (PYR1-like protein 8) (Regulatory components of ABA receptor 3) (Q9FGM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) in an ABA-independent manner but more efficiently when activated by ABA. Confers enhanced sensitivity to ABA. Can be activated by both (-)-ABA and (+)-ABA. Mediates crosstalk between ABA and auxin signaling to regulate lateral root growth. Required for lateral root growth suppression by ABA. In response to auxin, promotes lateral root growth by enhancing MYB77-dependent transcription of the auxin-responsive gene IAA19. Enhances the abilities of MYB44 and MYB73 to activate IAA19 gene.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:29928509}. Cytoplasm {ECO:0000269|PubMed:19889877, ECO:0000269|PubMed:22404835}. Nucleus {ECO:0000269|PubMed:19889877, ECO:0000269|PubMed:22404835, ECO:0000269|PubMed:24563205, ECO:0000269|PubMed:25465408}. Cell membrane {ECO:0000269|PubMed:25465408}. Note=Localizes at the plasma membrane in the presence of a CAR protein (e.g. CAR1 and CAR4). {ECO:0000269|PubMed:25465408}.
Interaction partners:
- Protein phosphatase 2C 16
- Transcription factor MYB77
- Protein phosphatase 2C 56
- Protein phosphatase 2C 37
- Protein phosphatase 2C 77
- Transcription factor MYB44
- Protein phosphatase 2C 7
- DET1- and DDB1-associated protein 1
- Protein phosphatase 2C 3
- Probable protein phosphatase 2C 75
Sequence:
MEANGIENLTNPNQEREFIRRHHKHELVDNQCSSTLVKHINAPVHIVWSLVRRFDQPQKYKPFISRCVVKGNMEIGTVREVDVKSGLPATRSTERLELLDDNEHILSIRIVGGDHRLKNYSSIISLHPETIEGRIGTLVIESFVVDVPEGNTKDETCYFVEALIKCNLKSLADISERLAVQDTTESRV
Protein: Transcriptional regulatory protein SEF1 (Q59UY7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor which plays an essential role in virulence by activating the transcription of iron uptake genes such as FRE7 in iron-poor environments such as the host bloodstream and internal organs. Promotes commensalism in a mouse model of gastrointestinal infection.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23133381}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:23133381}. Note=Interaction with SFU1 promotes cytoplasmic localization whereas interaction with SSN3 and subsequent phosphorylation promotes nuclear localization. Nuclear localization is associated with virulence.
Interaction partners:
- Suppressor of ferric uptake 1
- Hap43p
- High-affinity iron permease
- ferric-chelate reductase
Sequence:
MKFEKGKVRILPKPSPTPTNPQTPLPLLPAQTKPVNSKRKSAASTPGNESKKSRKSNSTASTPNSATPTSVGTPPQKTSKPTGHRPVTSCTFCRQHKIKCNASDNYPNPCERCKKMGLKCEIDPEFRPRKGSQIQSLKSDVDELKAKIEMLTKNESLLTQALNQHNLNHASQQQQSSGSQSQQQHPPNPQRALSYTSANSSPQVAFSNASPIPSVTSIQQNAPLTHENSDNSPYALNTPENIEELQPISEFILGDVTLPLNRANELHDKFMTTHLPFLPIIISRSATELYHKSQLLFWAVILTASLSEPEPKLYMSLASLIKQLAIETCWIKTPRSTHVIQALIILSIWPLPNEKVLDDCSYRFVGLAKNLSLQLGLHRGGEFIQEFSRNQVSLGPDAERWRTRSWLAVFFCEQFWSSLLGLPPSINTTDYLLENARVDKSLPKNFRCLISLSIFQCKLVNIMGISVTRPDGLLEPSNRAGSLSLLDRELERLRFKLQFEEGGPIEVYYLYIKLMICCFAFLPGTPIEDQVKYVSFAYLSATRIVTIVSKMVNDISLIELPIYIRQAVTYSVFMLFKLHLSRYLIDKYVDSARQSIVTVHRLFRNTLSSWKDLQNDISRTAKVLENLNMVLYNYPEIFLNDSENEDSSIITRMRSHLTASLFYDLVWCVHEARRRSVLDKGKRQAQPNKKILPLPFYNQITKDDFKTITTTSPNGTTITTLVPTDQAMNQAKSKSFDSSKPLEINGIPLPMLEATGSTREVLDSLPSQSLPSQAPTLQQYPMQQDQQQQEPSQQQQQKHSQQSQQYQQQQQSNQQQPHLQHQRQFQQSPPPQFSMISSTPPLQQPPFILANSPLPQTYLPKIDEMNMSPEVKQENSVAPFASQITNFFDQQTSGWFNNDNQDDDFLGWFDVNMMQEK
Protein: CaM kinase II isoform (O15302)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYTNQAEQCRKISASLQSQSPEHLLPVLIQAAQLCREKQHTKAIELLQEFSDQHPENAAEIKLTMAQLKISQGNISKACLILRSIEELKHKPGMVSALVTMYSHEEDIDSAIEVFTQAIQWYQNHQPKSPXHLSLIREAANFKLKYGRKKEAISDLQQLWKQNPKDIHTLAQLISAYSLVDPEKAKALSKHLPSSDSMSLKVDVEALENSAGATYIRKKGGKVTGDSQPKEQGQGDLKK
Protein: 2-keto-3-deoxy-L-rhamnonate aldolase (KDR aldolase) (EC 4.1.2.53) (2-dehydro-3-deoxyrhamnonate aldolase) (2-keto-3-deoxy acid sugar aldolase) (P76469)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible retro-aldol cleavage of 2-keto-3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde. 2-keto-3-deoxy-L-mannonate, 2-keto-3-deoxy-L-lyxonate and 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) are also reasonably good substrates, although 2-keto-3-deoxy-L-rhamnonate is likely to be the physiological substrate.
Interaction partners:
- L-rhamnonate dehydratase
- Inner membrane transport protein RhmT
- L-fuculose phosphate aldolase
- Uncharacterized HTH-type transcriptional regulator RhmR
- Rhamnulose-1-phosphate aldolase
- Epimerase family protein YfcH
- 2-keto-4-pentenoate hydratase
- Uncharacterized sugar kinase YegV
Sequence:
MNALLSNPFKERLRKGEVQIGLWLSSTTAYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAVAPYASQPVIRPVEGSKPLIKQVLDIGAQTLLIPMVDTAEQARQVVSATRYPPYGERGVGASVARAARWGRIENYMAQVNDSLCLLVQVESKTALDNLDEILDVEGIDGVFIGPADLSASLGYPDNAGHPEVQRIIETSIRRIRAAGKAAGFLAVAPDMAQQCLAWGANFVAVGVDTMLYSDALDQRLAMFKSGKNGPRIKGSY
Protein: C-type lectin LmsL (CTL) (Galactose-specific lectin) (Mutina) (Q9PSM4)
Organism: Lachesis stenophrys (Central American bushmaster)
Function: Galactose-binding protein which recognizes specific carbohydrate structures and agglutinates a variety of animal cells by binding to cell-surface glycoproteins and glycolipids. Is a calcium-dependent lectin. Shows high hemagglutinating activity, that is inhibited by lactose, galactose and inositol.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
NNCPQDWLPMNGLCYKIFDEQKAWEDAEMFCRKYKPGCHLASFHRYGESLEIAEYISDYHKGQAEVWIGLWDKKKDFSWEWTDRSCTDYLTWDKNQPDHYEGKEFCVELVSLTGYRLWNDQVCESKNAFLCQCKF
Protein: Alpha N-terminal protein methyltransferase 1 (EC 2.1.1.244) (Translation associated element 1) (X-Pro-Lys N-terminal protein methyltransferase 1) (NTM1) (P38340)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Responsible for the N-terminal methylation of the ribosomal proteins RPL12A, RPL12B, RPS25A and RPS25B.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein arginine N-methyltransferase 2
- Ribosomal lysine N-methyltransferase 2
- Protein-lysine N-methyltransferase EFM4
- Histidine protein methyltransferase 1
- 25S rRNA
- Ribosomal lysine N-methyltransferase 3
- Protein-lysine N-methyltransferase EFM2
- Ribosomal lysine N-methyltransferase 1
- Protein-lysine N-methyltransferase EFM3
- 25S rRNA
Sequence:
MDVPADSHIKYEDAIDYWTDVDATVDGVLGGYGEGTVVPTMDVLGSNNFLRKLKSRMLPQENNVKYAVDIGAGIGRVSKTMLHKHAAKIDLVEPVKPFIEQMHVELAELKDKGQIGQIYEVGMQDWTPDAGKYWLIWCQWCVGHLPDAELVAFLKRCIVGLQPNGTIVVKENNTPTDTDDFDETDSSVTRSDAKFRQIFEEAGLKLIASERQRGLPRELYPVRMYALKPMPN
Protein: Bptf protein (Q8VDN7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
HASGPAEAQPQPAQPAAQPQPQPQPPAQPEVQTQPAVSSHVPSETQPSQAQTSKPLVATQCQPQSSVQGQSPVRVQSPPLTRICPSTPSQVTPGQQPQVQTTASQPIPIPPPTSLQAPSQGQPQSQPQVQSSTQTLSSGQTLNQVTVLSPSCPQPQPQVIAVPQLQQVQVLSQIQSQVVAQIQAQQSGVPQQIKLQLPIQVQQNSAAQTQSVVTVQAASVQEQLQRVQQLRDQQQKKKQQIETEREHTLQASNQSEIIQKQVVMKHNAVIEHLKQKKTMTPAEREENQRMIVCNQVMKYILDKIDKEEKQAAKKRKREESVEQKRSKQNASKLSALLFKHKEQLKAEILRKRALLDKELQIQVQEELKRDLKMKREREMAQAVQANAASVPTPSVPAPVPAPAPAAPPAPPRSPPPSTHSLPPAGHPTAPLPVTSQKRKREEEKDSKSKKKKMISTTSKEAKKDTRLYCICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEADLIDEYVCPQCQSTEDAMTVLTPLTEKDYEGLKRVLRSLQAHKMAWPFLEPVDPNDAPDYYGVIKEPMDLATMEERIQKRYYEKLTEFVADMTKIFDNCRYYNPRDTPFYQCAEVLESFFVQKLKGFKASRSHNNKLQSTAP
Protein: Prolyl 3-hydroxylase 1 (EC 1.14.11.7) (Growth suppressor 1) (Leucine- and proline-enriched proteoglycan 1) (Leprecan-1) (Q3V1T4)
Organism: Mus musculus (Mouse)
Function: Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9R1J8}. Note=Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG). {ECO:0000250|UniProtKB:Q9R1J8}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase B
- Cartilage-associated protein
- Collagen alpha-1
- Collagen alpha-2
- Serpin H1
- Peptidyl-prolyl cis-trans isomerase FKBP10
- Trimeric intracellular cation channel type B
- Protein disulfide-isomerase
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
Sequence:
MAVSERRLLAAMLAVAAAAALRVAAESEPGWDVAAPDLLYAEGTAAYSRGDWPGVVLNMERALRSRAALRALRLRCRTRCATELPWAPDLDLGPDPSLSQDPGAAALHDLRFFGAVLRRAACLRRCLGPPSAHLLSEELDLEFNKRSPYNYLQVAYFKINKLEKAVAAAHTFFVGNPEHMEMRQNLDYYQTMSGVKEADFRDLEAKPHMHEFRLGVRLYSEEKPQEAVPHLEAALQEYFVADEECRALCEGPYDYDGYNYLDYSADLFQAITDHYVQVLNCKQNCVTELASHPSREKPFEDFLPSHYNYLQFAYYNIGNYTQAIECAKTYLLFFPNDEVMHQNLAYYTAMLGEEEASSISPRENAEEYRRRSLLEKELLFFAYDIFGIPFVDPDSWTPEEVIPKRLQEKQKSERETAVRISQEIGNLMKEIETLVEEKTKESLDVSRLTREGGPLLYEGISLTMNSKVLNGSQRVVMDGVISDDECQELQRLTNAAATSGDGYRGQTSPHTPNEKFYGVTVLKALKLGQEGKVPLQSARMYYNVTEKVRRVMESYFRLDTPLYFSYSHLVCRTAIEESQAERKDSSHPVHVDNCILNAEALMCIKEPPAYTFRDYSAILYLNGDFDGGNFYFTELDAKTVTAEVQPQCGRAVGFSSGTENPHGVKAVTRGQRCAIALWFTLDPRHSERDRVQADDLVKMLFSPEEVDLPQEQPLPDQQGSPEPGEESLSDRGSLHKDEL