wanglab/gogpt-training-data huggingface dataset:
Protein: Heterogeneous nuclear ribonucleoprotein H2 (hnRNP H2) (FTP-3) (Heterogeneous nuclear ribonucleoprotein H') (hnRNP H') [Cleaved into: Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed] (P55795)
Organism: Homo sapiens (Human)
Function: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG).
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:24644279}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein A3
- Serine/arginine-rich splicing factor 2
- Interleukin enhancer-binding factor 3
- Heterogeneous nuclear ribonucleoprotein H
- Probable ATP-dependent RNA helicase DDX5
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoproteins C1/C2
Sequence:
MMLSTEGREGFVVKVRGLPWSCSADEVMRFFSDCKIQNGTSGIRFIYTREGRPSGEAFVELESEEEVKLALKKDRETMGHRYVEVFKSNSVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGMTLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMAMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYGGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSSFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPMRVHIEIGPDGRVTGEADVEFATHEDAVAAMAKDKANMQHRYVELFLNSTAGTSGGAYDHSYVELFLNSTAGASGGAYGSQMMGGMGLSNQSSYGGPASQQLSGGYGGGYGGQSSMSGYDQVLQENSSDYQSNLA
Protein: ATP-dependent RNA helicase DeaD (EC 3.6.4.13) (Cold-shock DEAD box protein A) (P9WH05)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00964}.
Interaction partners:
- Ribonuclease PH
- Bifunctional NAD
- Probable cold shock-like protein B CspB
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL3
- Probable acyltransferase
- Polyribonucleotide nucleotidyltransferase
- Probable helicase
- Conserved protein similar to jag protein
Sequence:
MAFPEYSPAASAATFADLQIHPRVLRAIGDVGYESPTAIQAATIPALMAGSDVVGLAQTGTGKTAAFAIPMLSKIDITSKVPQALVLVPTRELALQVAEAFGRYGAYLSQLNVLPIYGGSSYAVQLAGLRRGAQVVVGTPGRMIDHLERATLDLSRVDFLVLDEADEMLTMGFADDVERILSETPEYKQVALFSATMPPAIRKLSAKYLHDPFEVTCKAKTAVAENISQSYIQVARKMDALTRVLEVEPFEAMIVFVRTKQATEEIAEKLRARGFSAAAISGDVPQAQRERTITALRDGDIDILVATDVAARGLDVERISHVLNYDIPHDTESYVHRIGRTGRAGRSGAALIFVSPRELHLLKAIEKATRQTLTEAQLPTVEDVNTQRVAKFADSITNALGGPGIELFRRLVEEYEREHDVPMADIAAALAVQCRGGEAFLMAPDPPLSRRNRDQRRDRPQRPKRRPDLTTYRVAVGKRHKIGPGAIVGAIANEGGLHRSDFGQIRIGPDFSLVELPAKLPRATLKKLAQTRISGVLIDLRPYRPPDAARRHNGGKPRRKHVG
Protein: 23S rRNA 5-hydroxycytidine C2501 synthase (Large subunit ribosomal RNA hydroxylation A) (P76104)
Organism: Escherichia coli (strain K12)
Function: Responsible for the formation of the 5-hydroxycytidine modification at the C2501 position (ho5C2501) of 23S rRNA. May be a Fe-S protein that catalyzes ho5C2501 formation using prephenate as a hydroxyl group donor.
Interaction partners:
- Ubiquinone biosynthesis protein UbiV
- HTH-type transcriptional regulator SutR
- Uncharacterized protein YhaB
- Probable electron transfer flavoprotein-quinone oxidoreductase YgcN
Sequence:
MTVSSHRLELLSPARDAAIAREAILHGADAVYIGGPGFGARHNASNSLKDIAELVPFAHRYGAKIFVTLNTILHDDELEPAQRLITDLYQTGVDALIVQDMGILELDIPPIELHASTQCDIRTVEKAKFLSDVGFTQIVLARELNLDQIRAIHQATDATIEFFIHGALCVAYSGQCYISHAQTGRSANRGDCSQACRLPYTLKDDQGRVVSYEKHLLSMKDNDQTANLGALIDAGVRSFKIEGRYKDMSYVKNITAHYRQMLDAIIEERGDLARASSGRTEHFFVPSTEKTFHRGSTDYFVNARKGDIGAFDSPKFIGLPVGEVVKVAKDHLDVAVTEPLANGDGLNVLIKREVVGFRANTVEKTGENQYRVWPNEMPADLHKIRPHHPLNRNLDHNWQQALTKTSSERRVAVDIELGGWQEQLILTLTSEEGVSITHTLDGQFDEANNAEKAMNNLKDGLAKLGQTLYYARDVQINLPGALFVPNSLLNQFRREAADMLDAARLASYQRGSRKPVADPAPVYPQTHLSFLANVYNQKAREFYHRYGVQLIDAAYEAHEEKGEVPVMITKHCLRFAFNLCPKQAKGNIKSWKATPMQLVNGDEVLTLKFDCRPCEMHVIGKIKNHILKMPLPGSVVASVSPDELLKTLPKRKG
Protein: Putative HIG1 domain family member 2B (HIG1 domain family member 2B pseudogene) (Q4VC39)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836}.
Interaction partners:
Sequence:
MATLGFVTPEAPFESSKPPIFEGLSPTVYSNPEGFKEKFLRKTRENPVVPIGFLCTAAVLTNGLYCFHQGNSQCSRLMMHTQIAAQGFTIAAILLGLAATAMKSPP
Protein: Ubiquitin-like protein 4A (B2GV38)
Organism: Rattus norvegicus (Rat)
Function: As part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated and sorted to the proteasome. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P11441}. Nucleus {ECO:0000250|UniProtKB:P11441}.
Interaction partners:
- Small glutamine-rich tetratricopeptide repeat-containing protein alpha
- Large proline-rich protein BAG6
- Guided entry of tail-anchored proteins factor 4
- Next to BRCA1 gene 1 protein
- FAS-associated factor 2
- E3 ubiquitin-protein ligase TRIP12
- Ubiquitin conjugating enzyme E2 V1 like 1
- Uncharacterized protein
- E3 ubiquitin-protein ligase TRAF7
- Small glutamine-rich tetratricopeptide repeat-containing protein beta
Sequence:
MQLTVKALQGRECSLQVAEDELVSTLKHLVSDKLNVPVRQQRLLFKGKALADEKRLSDYNIGPNSKLNLVVKPLEKVLLEEGSAHRLVDSSATPIWQLISKVLARHFSIGDASRVLEQLQRDYDRSLSRLTLDDIERLASRFLHPEVTEAMEKGFCK
Protein: E3 ubiquitin-protein ligase CHIP (EC 2.3.2.27) (RING-type E3 ubiquitin transferase CHIP) (Q86DT5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
LKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAIKHLQRAYDLSKEQKQNFGDDITLQLRLARKKRWNVMEEKRIQQEIELQSYLNGLIKGDMESRLANLKLNGNVHDEQLKDKQQEIEQECDDHIKELNNIFSKVDERRKKREVPDFLCGKISFEILTDPVITPSGITYERKDIEEHLQRVGHFDPVTRVKLTQDQLIPNFSMKEVVDSFIA
Protein: Stimulator of interferon genes protein homolog (dSTING) (dmSTING) (A0A0B4LFY9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Facilitator of innate immune signaling that binds cyclic dinucleotides produced in response to infection by bacteria and/or viruses, and promotes the activation of the NF-kappa-B transcription factor Rel (Relish). Recognizes and binds cyclic di-GMP (c-di-GMP), a cyclic dinucleotide messenger produced by bacteria such as L.monocytogenes, leading to activation of the peptidoglycan recognition protein (IMD) signaling pathway and activation of Rel (Relish). Innate immune response is triggered in response to double-stranded RNA from viruses delivered to the cytoplasm: Sting acts by specifically binding cyclic dinucleotides 3',2'-cGAMP and 2',3'-cGAMP produced by cGlr1 and cGlr2 in response to RNA virus in the cytosol. Has a strong preference for 3',2'-cGAMP compared to other cyclic dinucleotides such as 2',3'-cGAMP or 3'3'-c-di-GMP. Upon binding to 3',2'-cGAMP, activates an antiviral immune response, leading to the activation of Rel (Relish). Activated in brain in response to Zika virus infection, leading to autophagy.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30119996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- FI05319p
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Protein Nazo
- Cyclic GMP-AMP synthase-like protein
- FI06716p
- Meiotic P26, isoform F
Sequence:
MAIASNVVEAGNAVRAEKGRKYFYFRKMIGDYIDTSIRIVATVFLADLLLRLYRCVVEYGSNGRYYLPEDRLWIILRRSCTYNNRSIYLIVGFLLVAFFRISVTGNYRNVMPTTLFLFQMPLYWIWSFTDMDQSTLSYSHWIRDSHGLDYAAGMASNYFHGYLKLSLPERKDDGLKHRLAMYEDKNNVTFGIKRLVILIPDEMFVNGVLESHLLDKAEPLETQFINRAGVYRPFKHDVYRMNKKVNGRTYYFAVEGATPMISFFDATYSNLSGTWQMQELKREIWIKFYKHLKELITTWPETRDLVELIIYNSHDSKGNLVDVGELLVAHMQNKTKTIDEISN
Protein: Replication protein E1 (EC 3.6.4.12) (ATP-dependent helicase E1) (P04014)
Organism: Human papillomavirus 11
Function: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:15564503}.
Interaction partners:
Sequence:
MADDSGTENEGSGCTGWFMVEAIVEHTTGTQISEDEEEEVEDSGYDMVDFIDDRHITQNSVEAQALFNRQEADAHYATVQDLKRKYLGSPYVSPISNVANAVESEISPRLDAIKLTTQPKKVKRRLFETRELTDSGYGYSEVEAATQVEKHGDPENGGDGQERDTGRDIEGEGVEHREAEAVDDSTREHADTSGILELLKCKDIRSTLHGKFKDCFGLSFVDLIRPFKSDRTTCADWVVAGFGIHHSIADAFQKLIEPLSLYAHIQWLTNAWGMVLLVLIRFKVNKSRCTVARTLGTLLNIPENHMLIEPPKIQSGVRALYWFRTGISNASTVIGEAPEWITRQTVIEHSLADSQFKLTEMVQWAYDNDICEESEIAFEYAQRGDFDSNARAFLNSNMQAKYVKDCAIMCRHYKHAEMKKMSIKQWIKYRGTKVDSVGNWKPIVQFLRHQNIEFIPFLSKLKLWLHGTPKKNCIAIVGPPDTGKSCFCMSLIKFLGGTVISYVNSCSHFWLQPLTDAKVALLDDATQPCWTYMDTYMRNLLDGNPMSIDRKHRALTLIKCPPLLVTSNIDISKEEKYKYLHSRVTTFTFPNPFPFDRNGNAVYELSDANWKCFFERLSSSLDIEDSEDEEDGSNSQAFRCVPGSVVRTL
Protein: Importin beta-like SAD2 (Protein ENHANCED MIRNA ACTIVITY 1) (Protein SUPER SENSITIVE TO ABA AND DROUGHT 2) (Protein UNARMED 9) (F4IRR2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions probably in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with other importin subunits (Probable). Involved in the regulation of the abscisic acid (ABA)-mediated pathway in response to cold or salt stress. Involved in UV-B responses by regulating accumulation of UV-absorbing pigments through mediation of MYB4 nuclear transport. Involved in trichome initiation by controlling GL1, GL2, GL3 and TTG1 transcription and may affect an upstream regulator of GL3 and disrupt complex function. Acts as negative regulator miRNA activity by regulating miRNA loading into AGO1 complexes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16889648}. Nucleus {ECO:0000269|PubMed:16889648}.
Interaction partners:
- Importin subunit beta-1
- Tetratricopeptide repeat protein SKI3
- Exosome complex component RRP4 homolog
- Ribosomal RNA-processing protein 42
- Ribosomal RNA-processing protein 43
- Nuclear nucleic acid-binding protein C1D
- Transportin-1
- GTP-binding nuclear protein Ran-1
- Exosome complex component RRP45B
- At5g38890
Sequence:
MDLHSLALILRTAALSPIPDERKVSEQQLNQLEHTPQHLVRLLQIAVDGNCDMAVRQIASIQFKNLIAKNWSPEDCGPAVRQQQIFESDKELVRDNILVYVTQVPTLLRSQLGESLKTIIYADYPEQWPRLLDWVKYNLQNQQIYGALFVLRILSRKYEFKSDEERTPVSRIVEETFPQLLTIFNGLIQIPNPSLEIAELMKLICKIFWSSIYLELPRQLFDLNVFNAWMVLFLSVSERPVPVEGQPMDPELRKSWGWWKVKKWTVHILNRLYSRFGDPKLQSPENKPFAQMFQKNYAGRILEGHLNFLNTIRVGGYLPDRVINLLLQYLSNSISKNSMYKLLLPRLDVLLFEIVFPLMCFNDNDQKLWEEDPHEYVRKGYNIIEDLYSPRTASMDFVNELVRKRGKENLPKFVKFVVEIFLSYEKATVEEKPYRQKDGAMLAVGALCDKLKQTDPYKSQLELMLVQHIFPDFNSPVGHLRAKAAWVAGQYAHINFSDQNNFRKALHSVVSGLRDPDLPVRVDSVFALRSFVEACKDLNEIRPILPQLLDEFFKLMNEVENEDLVFTLETIVDKFGEEMAPFAFGLCQNLAAAFWRCLNTSEANDDSDDMGALAAVGCLRAISTILESVSSLPQLFVEIEPTILPIMQKMLTTDGQEVFEEVLEIASYMTFYSPSISLDIWSLWPLMVEALVDWGIDFFPNILVPMDNFISRGTAHFLTCKEPDYQQSLYNVLSTLMTDRNIEDSEIESAPKLIEVVFQNCKGQVDQWVEPYLRLTVDRLQRAETSYVKSLLIQVVANMLYYNPGLTLGVLHNTGLASKVFDLWFQMLQQKRKSGLPANFKREHDKKVCCLGLTSLLALPGGQFPDEALQRVFRATLDLLVAYKNQLAEAAKETEVDYEEEMNGLQSSDDDYDDDGSDGEMDDTEEGDEAQSVKLQKLAAQAKAFHYDDDDDDDSDDDFSDEDEFQSPIDEVDAFVFFVDAIRVMQASDAQRFQNLNQSLDFTYQAIANGIAQHAELRRVEIEKEKQKKLAAASTPVTAL
Protein: Period circadian clock 1a (Period circadian protein homolog 1a) (Q7SZZ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTDNQSLCPGLNITNESQQTHSGDTDAQSSGIDSTERENDGRLGHGTSTCSSLHGKGSATETTESKSSNGNSPSPPSSSVSFSLLSGSSEQDHSTSQASNSDQPARLQTQRELLKVLRELKIHMPAERRRKGRSSTLASLQYALSCVKQVRANQEYYHQWSVEESHGCCLDLSSFTIEELDNVTSEYTLQNTDTFSVAVSFLSGKVVYISSQAASLLRCKAERLQGALFSELLAPQDVSTFYSSTAPSRLPPWSSCAGTSSQVDCAEEKSMFCRISRGRDSNGEVKYHPFRLTPYQLTLRDSDTSQPEPCCLLIAERVHSGYEAPRIPADKRIFTTSHTPNCLFQEIDERAVPLLGYLPQDLVGKPVLVYLHPEDRLLMVAIHKKILQFAGQPFDHSPLRMRARSGEYLTIDTSWSSFINPWSRKVAFIVGRHKVRTSPLNEDVFTAPEGEEMKTMSPDVPQLNELIHRFLVQPVYGGSSQGYGSLGSSGSHEHQQGATSSSESNGHTSEDQIKPRKPMTFEQICQDMHMVKTSGQQVFIESRNRPPALKQGSLEALAKAADTAEASARDGLASLALSSPPRKELPMIYSYQQINCLDSIVRYLESFNVPGTVKRKCGSSSCTTSSTSDDDKQREGAGATQAETLVVTEGSKVVPAAPAHPLTPLALHCKAESVVSATSQCSFSSTIVHVGDKKPPESAVHEKEKEKERRSGGSAGKGLTKAVLSAHTQQEEQAFLNRFRDLSQLRMVQPSGLPPPRRCTSIPGTKGVNSSQNYPSVGNTSSRRHGRGGKRQKHQVDGNIPNNTPISASGPYRGPNPAQIRPNFPSVQQSSNSWAPSAASQTNGAPVGTSFPPSYMTMFPTSSPFSVTQMGTDPSLQTGVPRFPAQGFPSVMPPVMTFMMPNYMFPQLSNPGSQLNPANSQLNAQMNSFGQFPPPVVQMSVPMFNPAMGQFYPLGSQMNPAMPAMIPQQFYNPNYQLNFSNSPSMPAANVSTTPHGQSRSSTPQSTGPQAGERDGAGSPLFQSRCSSPLNLLQLEELPSNRTDATQQTPPPGGSSNTSKYFGSIDSSENDQNHKPASGDLGGEQFIKFVLQDPIWLLMANTDDKIMMTYQIPIKDKDSVLKEDRDALKAAQKHQPHFTEEQKKELTQVHPWIQTGCLPKAINVTSCTGCESPPDSSTLPPFDLEFHEMDLNVVLREEAKQEDKLAETAFPLSPPSSDNEQRDNQANLST
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4JE58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNVVRRLTSIASGRNFVSSDNVGETETPRSKPNQNREETESTETTSYEKDSVSSSENSDHLPKEIREVGLGDDKDMDCGIIKGNGTESGRIITTKKKGLNDQKDKTISYRAEHVIGTGSFGVVFQAKCLETEEKVAIKKVLQDKRYKNRELQIMRMLDHPNVVELKHSFFSTTEKDELYLNLVLEYVPETIYRASRSYTKMNQHMPLIYIQLYTYQICRAMNYLHQVVGVCHRDIKPQNLLVNNVTHEVKICDFGSAKMLIPGEPNISYICSRYYRAPELIFGATEYTSAIDMWSVGCVMAELFLGHPLFPGETSVDQLVEIIKILGTPAREEIKNMNPRYNDFKFPQIKAQPWHKIFRRQVSPEAMDLASRLLQYSPNLRCTALEACAHPFFDDLRDPRASLPNGRALPPLFDFTAQELAGASVELRHRLIPEHARK
Protein: Calcium-dependent protein kinase 1 (AtCDPK 1) (CDPK 1) (EC 2.7.11.1) (Calcium-dependent protein kinase isoform AK1) (Q06850)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger. Phosphorylates the Ca(2+)-ATPase ACA2 resulting in the inhibition of its calcium activation.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:12913141}; Lipid-anchor {ECO:0000269|PubMed:12913141}.
Interaction partners:
- Respiratory burst oxidase homolog protein D
- Calcium-binding protein CP1
- Respiratory burst oxidase homolog protein B
- Respiratory burst oxidase homolog protein F
- Protein DEHYDRATION-INDUCED 19 homolog 2
- Respiratory burst oxidase homolog protein A
- Respiratory burst oxidase homolog protein C
- Respiratory burst oxidase homolog protein E
Sequence:
MGNTCVGPSRNGFLQSVSAAMWRPRDGDDSASMSNGDIASEAVSGELRSRLSDEVQNKPPEQVTMPKPGTDVETKDREIRTESKPETLEEISLESKPETKQETKSETKPESKPDPPAKPKKPKHMKRVSSAGLRTESVLQRKTENFKEFYSLGRKLGQGQFGTTFLCVEKTTGKEFACKSIAKRKLLTDEDVEDVRREIQIMHHLAGHPNVISIKGAYEDVVAVHLVMECCAGGELFDRIIQRGHYTERKAAELTRTIVGVVEACHSLGVMHRDLKPENFLFVSKHEDSLLKTIDFGLSMFFKPDDVFTDVVGSPYYVAPEVLRKRYGPEADVWSAGVIVYILLSGVPPFWAETEQGIFEQVLHGDLDFSSDPWPSISESAKDLVRKMLVRDPKKRLTAHQVLCHPWVQVDGVAPDKPLDSAVLSRMKQFSAMNKFKKMALRVIAESLSEEEIAGLKEMFNMIDADKSGQITFEELKAGLKRVGANLKESEILDLMQAADVDNSGTIDYKEFIAATLHLNKIEREDHLFAAFTYFDKDGSGYITPDELQQACEEFGVEDVRIEELMRDVDQDNDGRIDYNEFVAMMQKGSITGGPVKMGLEKSFSIALKL
Protein: Eukaryotic translation initiation factor 5A-1 (AtELF5A-1) (eIF-5A-1) (Q9XI91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The precise role of eIF-5A in protein biosynthesis is not known but it may function as a bimodular protein capable of binding to both RNA and proteins. Involved in xylogenesis.
Interaction partners:
- Deoxyhypusine synthase
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL21x/eL21w
- Large ribosomal subunit protein uL5z
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein bL31c
- Small ribosomal subunit protein eS1z
- Small ribosomal subunit protein eS1y
Sequence:
MSDEEHHFESSDAGASKTYPQQAGTIRKNGYIVIKNRPCKVVEVSTSKTGKHGHAKCHFVAIDIFTSKKLEDIVPSSHNCDVPHVNRTDYQLIDISEDGYVSLLTDNGSTKDDLKLPNDDTLLQQIKSGFDDGKDLVVSVMSAMGEEQINALKDIGPK
Protein: Cytochrome P450 710A4 (EC 1.14.19.41) (C-22 sterol desaturase) (Q9ZV28)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required to form the C-22 double bond in the sterol side chain. Possesses C-22 desaturase activity toward beta-sitosterol and produces stigmasterol.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Delta
- Cycloeucalenol cycloisomerase
- Methylsterol monooxygenase 2-1
- Delta
- Methylsterol monooxygenase 2-2
- Delta
- 24-methylenesterol C-methyltransferase 2
- Methylsterol monooxygenase 1-3
- Lanosterol synthase
- Ergosterol biosynthetic protein 28
Sequence:
MVSSVSLFASLTPYLVSALLLFLLLEQLFYRVKKRNLPGPLFVFPIIGNVVALIRDPTSFWDKQSAMADTSVGLSVNYLIGKFIIYIKDAELSNKVLSNIRPDAFQLTGHPFGKKLFGDHSLIFMFGEDHKSVRRQVAPNFTRKPLSAYSSLQQIVILRHLRQWEESFSSGSRPVSMRQLIRELNLETSQTVFVGPYLDKEVKKTICDDYSLLTLGTMAIPIDLPGFTFGEARQAVSRLVNTMSVCVGKSKAKMAAGENPTCLVDFWTHSIIEENPPPPHSKDKEISCVLVDFMFASQDASTSSLLWAVVMLESEPEVLRRVREDVARFWSSESNELITADQLAEMKYTRAVAREVLRYRPPASMIPHVAVSDFRLTESYTIPKGTIVFPSLFDASFQGFTEPDRFDPDRFSETRQEDEVFKRNFLTFGNGSHQCVGQRYAMNHLVLFIAMFSSMFDFKRVRSDGCDDIVHIPTMSPKDGCTVFLSSRLVTSP
Protein: Laccase-2 isoform A (Q58IU3)
Organism: Anopheles gambiae (African malaria mosquito)
Interaction partners:
Sequence:
MAIDWRNRVLSLGILLALAVAADGVRVQQHTSRRFKDESFGHDQTPAGSWWSSHLTEPPSNFYQATHGLLQTHPSVPSLKPVAGAPAAPGPSALPLSSRKSPTVSSAAALNSGFPSIANPNPRSPFRHLDFSTSATAELRRNPSLSAPDECARACREGEPPRICYYHFTVEYYTVLGAACQVCTPNATNTVWSHCQCVLADGVERGILTVNRMIPGPSIQVCENDRVVIDVENHMEGMELTIHWHGIWQRGTQYYDGVPFVTQCPIQQGNTFRYQWTGNAGTHFWHAHTGLQKLDGLYGSIVVRQPPSRDPNSHLYDFDLTTHIMLVSDWLHEDAAERYPGRLAVNTGQDPESLLINGKGQFRDPNTGFMTNTPLEIFTITPGRRYRFRMINAFASVCPAQVTIEGHALTVIATDGEPVHPAQVNTIISFSGERYDFVITADQPVGAYWIQLRGLGECGIKRAQQLAILRYARGPYQPASPPPTYDVGLPQGVVMNPLDAQCNVQRDDAICVSQLKNAKEIDRALLQDKPDVKIFLPFRFYLYRPEELFQPNTYNRFLVAPTGDHVISLIDEISYLSAPAPLLSQYDDINPEQFCNGDNRPADCGANCMCTHKVDIPLNAIVEVVLVDEVQQPNLSHPFHLHGYAYNVVGIGRSPDSNVKKINLKHALDLDRRGLLHRQYNLPPLKDTIAVPNNGYVVLRFRADNPGFWLFHCHFLFHIVIGMNLILQVGTHADLPPVPPNFPTCGDHLPPIN
Protein: Synaptogyrin-1 (O55100)
Organism: Mus musculus (Mouse)
Function: May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q62876}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62876}. Melanosome {ECO:0000250|UniProtKB:O43759}.
Interaction partners:
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- Synaptotagmin-1
- Ras-related protein Rab-3A
Sequence:
MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWVFSIVVFGSIVNEGYLNNPEEEEEFCIYNRNPNACSYGVTVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFFWFVGFCFLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWAGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPSAGSDPAGMGGTYQHPANAFDAEPQGYQSQGY
Protein: Fructose-1,6-bisphosphatase (FBPase) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (P09202)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable transketolase
- Fructose-bisphosphate aldolase
- ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- Transaldolase
- Probable 6-phosphofructo-2-kinase C222.13c
- Putative 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase C144.17c
- Hexokinase-2
- Hexokinase-1
- Probable 6-phosphofructo-2-kinase PB17E12.14c
Sequence:
MKKDLDEIDTDIVTLSSFILQEQRRYNQKHKNEEGKPCIIQEASGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEDLIVVDSNGSYAVTCDPIDGSSNIDAGVSVGTIFGIYKLRPGSQGDISDVLRPGKEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHLKESTPDKKPYSARYIGSMVADMHRTILYGGLFAYPCSKGNNGKLRLLYECFPMAFLVEQAGGIAVNDKGDRILDLVPKTLHGKSSIWLGSKHEVEEYINFIK
Protein: Cyclin-dependent kinase 11B (EC 2.7.11.22) (Zgc:101589) (Q5PRD1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGDEKETWKVKTLDEILQEKKRRRELEEKSDPKRIKNADDRELKRDTPEEGELRDHRMEITIRNSPYTREDSTEDRGEEDESLAIKPPQQMTRKDKNYHRKEEKRKDKRRRRSHSAEGAEKHPRTKDKEKERENERRKRQWHEDNKARQDYERQKRRDQARAHSRRERDRLEQLERKRERDRKLREQEQREQRELEERERRAKERRKDRDTRRDVPISHHRVAPAEEYTDKARLRHRSRSRSRSPVRLQRETKAESSEPRRAVREGKVDKDPLSDLQDISDSERKTSSPGSSLGSGSGSEAEEDEDNEEEESSSQTEGDEEGESGSESEGSEHSGGALSDEEPSEEEEEGEEEEERENGNHIPPVPESRFDHDSEVSAEEEEEEEEEVEEEEAVDVTPQSHAPSATPEERYIPESPPVSPVELKKELPKYLPALQGCRSVEEFQCLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPITSLREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYVEHDLKSLMETMKQPFLPGEVKTLMIQLLRGVRHLHDNWILHRDLKTSNLLLSHKGILKIGDFGLAREYGSPLKPYTPVVVTLWYRSPDLLLGAKEYSTAVDMWSVGCIFGELLTQKPLFPGKSEIDQINKIFKDLGSPSEKIWPGYSEPPAVKKMTFTEYPYNNLRKRFGALLSDQGFDLMNKFLTYCPAKRISADEALKHEYFRESPLPIDPSMFPTWPAKSEQQRVKRGTSPRAPEGGQDFSQLGDDDLKDTGFHLTTANKGASMAGPGFSLKF
Protein: D-mannonate dehydratase (ManD) (EC 4.2.1.8) (Q1NAJ2)
Organism: Sphingomonas sp. (strain SKA58)
Function: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- Putative D-mannonate oxidoreductase protein
- Altronate hydrolase
- 2-oxo-3-deoxygalactonate kinase
- 2-dehydro-3-deoxygluconokinase
- Uronate isomerase
- 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
- Beta-D-glucoside glucohydrolase
- Beta-D-glucoside glucohydrolase
Sequence:
MPKIIDAKVIITCPGRNFVTLKIMTDEGVYGLGDATLNGRELAVASYLTDHVIPCLIGRDAHRIEDLWQYLYKGAYWRRGPVTMTAIAAVDMALWDIKGKIAGLPVYQLLGGASREGVMVYGHANGTTIEDTVKVALDYQAQGYKAIRLQCGVPGMASTYGVSKDKYFYEPADADLPTENIWNTSKYLRIVPELFKAARESLGWDVHLLHDIHHRLTPIEAGRLGQDLEPYRPFWLEDATPAENQEAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQIRTGCHGATDLSPVCMAAALHFDLSVPNFGIQEYMRHMPETDAVFPHAYTFADGMMHPGDQPGLGVDIDEDLAAGYEYKRAFLPVNRLEDGTMFNW