wanglab/gogpt-training-data huggingface dataset:
Protein: (-)-alpha pinene synthase 1, chloroplastic (EC 4.2.3.119) ((-)-beta pinene synthase 1, chloroplastic) (EC 4.2.3.120) (Terpene synthase (-)alphapin1) (PcTPS-(-)alphapin1) (R9QMR3)
Organism: Pinus contorta (Shore pine) (Lodgepole pine)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-alpha-pinene and, to a lower extent, to (-)-beta-pinene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSPVSVISLPSDLCLPTSFIDRSGRELNPLHITIPNVAMRRQGKLMTRASMSVNLRTAVSDDAVIRRRGDFHSNLWDDDFIQSLSSHYGEPSYRERAERLIGEVKNSFNSVSNEDGESITPLDDLIQRLWMVDSVERLGIDRHFKKEIKSALDHVYSYWSEKGIGCGRESVVTDLNSTALGLRTLRLHGYDVSAEVLNHFKNQSGQFACTLKQTEDQIRTVLNLYRASLIAFPGEKVMDEAETFSAKYLKDALQKIPVSSLSREIGDVLEYGWHTYLPRLEARNYIDVFGQDTENSKSYMKTEKLLELAKLEFNIFHALQKRELEYLVRWWKGSGSPQMTFCRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITVLDDMYDTFGTLDELELFTSAIKRWDPSATECLPEYMKGVYMIVYNTVNEMSQEADKAQGRDTLNYCRQAWEEYIDAYMQEAKWIASGEVPTFEEYYENGKVSSGHRVSALQPILTTDIPFPEHVLKEVDIPSKLNDLASAILRLRGDTRCYQADRARGEEASCISCYMKDNPGTTEEDALNHINAMISDVIKGLNWELLKPNSSVPISAKKHAFDISRAFHYGYKYRDGYSVASIETKSLVKRTVIDPVTL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4HSE1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MIYLHRIYFIIVLFTLIFHGRLGFSDNNKLHEAEVRALKEIGKKLGKKDWDFNKDPCSGEGTWIVTTYTTKGFESNITCDCSFLPQNSSCHVIRIGNLVGRALKSQNLTGIVPPEFSKLRHLKVLDLSRNSLTGSIPKEWASMRLEDLSFMGNRLSGPFPKVLTRLTMLRNLSLEGNQFSGPIPPDIGQLVHLEKLHLPSNAFTGPLTEKLGLLKNLTDMRISDNNFTGPIPDFISNWTRILKLQMHGCGLDGPIPSSISSLTSLTDLRISDLGGKPSSFPPLKNLESIKTLILRKCKIIGPIPKYIGDLKKLKTLDLSFNLLSGEIPSSFENMKKADFIYLTGNKLTGGVPNYFVERNKNVDVSFNNFTDESSIPSHDCNRVTSNLVESFALGNKSHKGSTCFLQRMPCVHPKRYHLYKLYINCGGGEVKVDKEITYQADDEPKGASMYVLGANKRWALSSTGNFMDNDDDADEYTVQNTSRLSVNASSPSFGLYRTARVSPLSLTYYGICLGNGNYTVNLHFAEIIFTDDNTLYSLGKRLFDIYVQDQLVIKNFNIQEAARGSGKPIIKSFLVNVTDHTLKIGLRWAGKGTTGIPIRGVYGPMISAISVEPNFKPPVYYDTKDIILKVGVPVAAATLLLFIIVGVFWKKRRDKNDIDKELRGLDLQTGTFTLRQIKAATDNFDVTRKIGEGGFGSVYKGELSEGKLIAVKQLSAKSRQGNREFVNEIGMISALQHPNLVKLYGCCVEGNQLILVYEYLENNCLSRALFGKDESSRLKLDWSTRKKIFLGIAKGLTFLHEESRIKIVHRDIKASNVLLDKDLNAKISDFGLAKLNDDGNTHISTRIAGTIGYMAPEYAMRGYLTEKADVYSFGVVALEIVSGKSNTNFRPTEDFVYLLDWAYVLQERGSLLELVDPTLASDYSEEEAMLMLNVALMCTNASPTLRPTMSQVVSLIEGKTAMQELLSDPSFSTVNPKLKALRNHFWQNELSRSLSFSTSGPRTASANSLVDAEEKTGLLD
Protein: Ribonucleases P/MRP protein subunit POP7 (EC 3.1.26.5) (RNA-processing protein POP7) (O94251)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease MRP protein subunit rmp1
- Probable ribonucleases P protein subunit pop8
- Ribonuclease P protein subunit rpr2
- Probable ribonuclease P protein subunit 1
- Probable ribonuclease P protein subunit 3
- Uncharacterized protein C6C3.09
- Ribonucleases P/MRP protein subunit pop1
- Ribonucleases P/MRP protein subunit pop3
- Uncharacterized protein C16C4.19
Sequence:
MSVERIKRAPAFRKGIIIRRKTHLIAMIRRMRKKLDIDGSILYQATGMAIPHLVELSDKYKRQGYNISMDTATVEFMDEIVDEVSIQNKNRLGNVLLLRVSR
Protein: EEF1A lysine methyltransferase 1 (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 2) (Protein-lysine N-methyltransferase N6AMT2) (eEF1A-KMT) (Q8WVE0)
Organism: Homo sapiens (Human)
Function: Protein N-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03187}.
Interaction partners:
- Elongation factor 1-alpha 1
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Exportin-4
- Tubulin--tyrosine ligase-like protein 12
- EEF1A lysine methyltransferase 2
- Elongation factor 1-alpha 2
Sequence:
MSDLEDDETPQLSAHALAALQEFYAEQKQQIEPGEDDKYNIGIIEENWQLSQFWYSQETALQLAQEAIAAVGEGGRIACVSAPSVYQKLRELCRENFSIYIFEYDKRFAMYGEEFIFYDYNNPLDLPERIAAHSFDIVIADPPYLSEECLRKTSETVKYLTRGKILLCTGAIMEEQAAELLGVKMCTFVPRHTRNLANEFRCYVNYDSGLDCGI
Protein: Structure-specific endonuclease subunit slx4 (Synthetic lethal of unknown function protein 4) (Q9P6M0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulatory subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. Has Holliday junction resolvase activity in vitro. Slx4 is required for efficient processing of DNA substrates.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:16467377, ECO:0000269|PubMed:16823372}. Note=Associates with chromatin at rDNA repeat protrusions. {ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:16467377, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Structure-specific endonuclease subunit slx1
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 3
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 1
- Actin-binding protein wsp1
- Uncharacterized protein C1322.02
Sequence:
MSAEEYIEVSSSPDIFTDDDDMITIEPELNKNPKDCNSKRKRSVTECCEIRLITSKCDFESTQQLVHHNCTGHKVHEHNLNAVDEEDFDTENLPLLFSSFSDNESDILEPDLNTRVAEDNDVLLSRYSKIKNSASCRNTFEHSAYHSNREEISSSGFYYHRKPQLFEKSLEKLGNKSIEANRSPLIKELCESANSTENVCFSVSTVDEIQQRHPSAGHSIDSTCQSNSFLEGDSATHKKKKTDNIKEFTSCEFNDRSRTLLNYAGYMDTNKNADNEAKSLKEKLENFPVEKLRAIAESYGFKSSDSKATLIKIVESCLDAIDSRSQSKKLGKETPHDYLITSTKTVLEFDDIVTQTHRAISQVVKQAKDNSVWIKILTYSAIDVEEFQLWLKRKNLNVSLDLIKSWCDKYGVLMKGSWH
Protein: calcium/calmodulin-dependent protein kinase (EC 2.7.11.17) (Q32PV2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLSGQEYAAKIINTKKLSTRDHQKLDREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKSKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSLEVLRKDPYGKAVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVECLKKFNARRKLKGAILTTMLATRNFSGGKSGVSKKTDGVKESSESTNTTIEDEDTRVRKQEIIKVTEQLIEAISNGDFESYTKMCDPSVTAFEPEALGNLVEGLDFHRFYFENLWSKNSKPVHTTILNPHIHLIGEEAACIAYIRITQYLDNNGMPCTAQSEETRIWHRKDGKWQIVHFHRSGSPAAIAK
Protein: Mannitol-1-phosphate 5-dehydrogenase (M1PDH) (MPD) (MPDH) (EC 1.1.1.17) (A2QD49)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the metabolism of mannitol. Has a strong preference for NADH over NADPH (By similarity).
Interaction partners:
Sequence:
MGKKAIQFGGGNIGRGFVAEFLHKAGYEVVFVDVMDKMVEALQQNKSYKVTEVSEEGEHTTTITNYRAINSKTHESDVIQEIATADVVTCAVGPNILKFIAPVIAKGIDARTESKPVAVIACENAIGATDTLHGFIKQHTSQDRVESLYDRAQFANSAIDRIVPQQAPNSGLDVRIEKFYEWAVEKTPFGSVGHPDIPAIHWVDNLEPYIERKLFTVNTSHATTAYFGHFRGKKMIADALEDKEIRGLVHKVLEETASLIVAKHDISEEEQKEYVEKIVSRISNPYLEDNVDRVGRAPLRKLSRKERFIGPASQLAERGMKYDSLMDAVEMALRFQNVPGDDESAELANILQEQPAEDATTNLTGLEKEHPLYPAVLDRVRKVQQGTK
Protein: SWI/SNF chromatin-remodeling complex subunit SNF5 (SWI/SNF complex subunit SNF5) (Transcription factor TYE4) (Transcription regulatory protein SNF5) (P18480)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- SWI/SNF chromatin-remodeling complex subunit SWI1
- SWI/SNF complex subunit SWI3
- Actin-like protein ARP9
- Transcription regulatory protein SNF2
- Transcription regulatory protein SNF12
- Transcription regulatory protein SNF6
- Actin-related protein 7
- Transcription initiation factor TFIID subunit 14
- SWI/SNF global transcription activator complex subunit SWP82
- Transcription regulatory protein SNF11
Sequence:
MNNQPQGTNSVPNSIGNIFSNIGTPSFNMAQIPQQLYQSLTPQQLQMIQQRHQQLLRSRLQQQQQQQQQTSPPPQTHQSPPPPPQQSQPIANQSATSTPPPPPAPHNLHPQIGQVPLAPAPINLPPQIAQLPLATQQQVLNKLRQQAIAKNNPQVVNAITVAQQQVQRQIEQQKGQQTAQTQLEQQRQLLVQQQQQQQLRNQIQRQQQQQFRHHVQIQQQQQKQQQQQQQHQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQGQIPQSQQVPQVRSMSGQPPTNVQPTIGQLPQLPKLNLPKYQTIQYDPPETKLPYPTYWSDKKADTDTLLYEQIIQRDKINKYSLIRETNGYDPFSIYGFSNKEYISRLWHTLKYYQDLKNTRMKSITSTSQKIPSASIWGNGYSGYGNGITNTTTRVIPQVEVGNRKHYLEDKLKVYKQAMNETSEQLVPIRLEFDQDRDRFFLRDTLLWNKNDKLIKIEDFVDDMLRDYRFEDATREQHIDTICQSIQEQIQEFQGNPYIELNQDRLGGDDLRIRIKLDIVVGQNQLIDQFEWDISNSDNCPEEFAESMCQELELPGEFVTAIAHSIREQVHMYHKSLALLGYNFDGSAIEDDDIRSRMLPTITLDDVYRPAAESKIFTPNLLQISAAELERLDKDKDRDTRRKRRQGRSNRRGMLALSGTSASNTSMNGVHNTVAAGNASSLPPGEILLPDIADIPRTFRTPVPSTLMPGGVDVGPSVESYELRNTTTYKSRPDRPKPVSPPCYIIDHIPGHSLLLSIKLPGKVNTKEEFAAAPNDTSSGTNAMLPSPESLKTKLNSNIRAGVTIPSIPNPIANHTVTNSPNPTLQPVIPGGAASKSVPTPSLPIAPPVAPHDSEATLLTNSNNGSSNNNTQNT
Protein: LD37351p (Q960S5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGIYNPQTNQQQRAPQVRVGNANPAPPPLQGLPPNANGGQTLMITPAPQPAPKVPTLVRLTFPNTPMGQARAQLQEQIFSAMDICTHLTGKVVSLTHSNAYNQVRSYLELKELYIHMSYLMTYAIGRFKNLQEKCLVDMREKGFKNDANSLENGQLAADKQASDDEDNEIEIVEPKTDTITIDSDNEDDMPSTSTATQQEQPQETAIMKITSVTSEASKKELQENNQADIDVAAFSSTILASLLEVEVNEGASEPKPVSPGQKKQPRKKTTNKPNPALLQLERQRMEDMKKSDAKLKMKVMVKLKRAEDEFEVARKWVEDMKQGQELATKIKDSKAATPSNKTQKPSENLKISEKGSSAKKESTKQHGEGDKENTKNKEKIGDILKAAIKAKIGENEKLMAEDVQLPVDELLTEKDKELDKETLTSTEPETNKKSGTEKGSDKKQHLTKENNVKGESKDESKTDQKSDCKKGPDSECTEIEEETEMLSEKGYGGSEKEQGDTENMEDETSSERPTLIGEIEKNLLKEGKEESSEKFDKEVEPSKDVGKDSPTTQGKGQDSDKLKNARAGLKNSTQDASNTVEPPVAASNENDQSSVGELIERMDVTELDEKPKELLDCALDEVIPMEGIELSDDTEDLIKALGSPSVLPSQNTKDNETDLDANDFIGNLPLETTEPPEILLKEDECKVEKTTGISQVGAPSPAENGDTEMESTLEASDSAPDEFATAEIVG
Protein: Glutamate decarboxylase 1 (EC 4.1.1.15) (67 kDa glutamic acid decarboxylase) (GAD-67) (Glutamate decarboxylase 67 kDa isoform) (P18088)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor.
Interaction partners:
- 4-aminobutyrate aminotransferase, mitochondrial
- Glutamate decarboxylase 2
- Vesicular inhibitory amino acid transporter
- Glutamate dehydrogenase 1, mitochondrial
- Glutamine synthetase
- Glutaminase kidney isoform, mitochondrial
- Parvalbumin alpha
- Glutaminase liver isoform, mitochondrial
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase, dimeric NADP-preferring
Sequence:
MASSTPSPATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEKSRLVSAFRERQASKNLLSCENSDPGARFRRTETDFSNLFAQDLLPAKNGEEQTVQFLLEVVDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIGWSNKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPERREKLHRVAPKIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
Protein: Tryptamine hydroxycinnamoyltransferase 2 (OsTHT2) (EC 2.3.1.-) (Q8LMI4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to tryptamine, to produce coumaroyl tryptamine. Serotonin and tyramine serve as acyl acceptors in vitro. Can use caffeoyl-CoA, and to a lesser extent feruloyl-CoA, as acyl donors.
Interaction partners:
- Nitrate reductase
- Nitrate reductase
- Nitrate reductase 1
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- 4-coumarate--CoA ligase
- 4-coumarate--CoA ligase-like 9
Sequence:
MAVAVEITRSEVLRPSETLAAGGGGKRSQLTVFDRAAMDWYIPAVFAWDGAAAPSNDEVKGGLAAVLARYPHLAGRFDVDERGRRCFNLNNAGVRVLEATVAADLADALAHDVAAHVNELYPKADMENADEPVFQVQLTRYACGGLVIGTACNHQVSDGQSMSFFYVAWAAAVRSAGATLPTPFVDRAAIAVPRGPPAPAFDHRNIEFKGEHSWTHSYGSLPLERIRNLAVHFPDEFVAGLKSHVGARCSTFQCLLAHAWKKITAARDLSPEEYTQVRVAVNCRGRASPAVPMDYFGNMVLWAFPRMRVRDLLSSSYAAVVGVIRNAVARVDEQYIQSFVDFGEVAAGDELTPTAAPPGTVFCPDLEVDSWLGFRFHDLDFGRGPPCAFLPPDVPVEGLLIFVPSCAAKGGVEMFMALDDVHVEAFRQICYSMD
Protein: UBX domain-containing protein 7 (O94888)
Organism: Homo sapiens (Human)
Function: Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates.
Subcellular location: Nucleus {ECO:0000269|PubMed:22537386}.
Interaction partners:
- Nuclear protein localization protein 4 homolog
- Ubiquitin recognition factor in ER-associated degradation protein 1
- FAS-associated factor 2
- FAS-associated factor 1
- UBX domain-containing protein 1
- Transitional endoplasmic reticulum ATPase
- Tether containing UBX domain for GLUT4
- NSFL1 cofactor p47
- Deubiquitinating protein VCPIP1
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3
Sequence:
MAAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGLPAVDSEILEMPPEKADGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN
Protein: Forkhead box protein O (B3G3K1)
Organism: Ancylostoma caninum (Dog hookworm)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MSNHLSQTQCLPPQLPTFGVVPPLSFQPQCYISTSSSILPPGPPYPSLNTTSPSSDSLFSVSTSLNSLPSECPPRRSDLDLKMETPDGDDGDDFFDLEKHQKARSASFGGSTQYSSQLAIARHGLFAPSLDTIGSVASGLYDSAENLNSRLGATSVASSGALLHSPDGNNTFSPSSCNMSSPVMNDQLAPAGATDAGDGVAGAGAAKKSTTRRNAWGNLSYADLITQAIMQSPEKRLTLSQVYEWMVQNVPYFRDKGDSNSSAGWKNSIRHNLSLHSRFMRIQNEGAGKSSWWVINPDAKPGRNPRRVRASTLDTTSKATLSKKLKGARKRIHDIRAVSGLHSGVSSLAGSQASIMSHDIYGDEEAMQASFDPMFRPRTQSNLSVPGSSTRVSPSMEHPFDDFEFPSWVNDATAASAAANAAANAANHTGAAPIPTDILDRTDQMRIDSCRIMMNGVKQEPKPIKTESPVAPPPSYLELSSVRNQSQLQNPLLRTQLASVKFPTAGLPLPYQTYSPWPTHTPLLPPSSCAAVAQANSVAAAAALPSDLESLTLPDQPLMDFEVESLLRHELSQTTDHRLNFDNL
Protein: GH16993p (Q8T0N8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MATTASQSNCWLLQRRQLDSITTVLAEMIATAMLMFLGCMGSVENSVFTNSDFQSALNFGFVVLICIQCFGCVCGAHLNPAVTLATYVYNMISLPMALAYFVAQMVGAFIGYGLLKAVLPESAIYSAENPNGVCLTSLNSTLTPWQGLAVEFLITCVLISVCCGVWDPRNATKQDSLPVRFGLAIACLSLTAGQLTGASMNPVRSFAPAIWNGFWDDHWIYWVGPMAAALITSVIYKHAFRRELEESEVD
Protein: Ribonuclease Z 1 (RNase Z 1) (EC 3.1.26.11) (tRNA 3 endonuclease 1) (tRNase Z 1) (Q10155)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. May be involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21208191}. Cytoplasm.
Interaction partners:
- Ribonuclease Z 2, mitochondrial
- Small ribosomal subunit protein eS25B
- Nuclease 1, mitochondrial
- RNA exonuclease 3
- mRNA degradation protein pet127
- Uncharacterized exonuclease C637.09
- ATP-dependent RNA helicase suv3, mitochondrial
- Probable oligoribonuclease
Sequence:
MSKTVNFRATKNFYLQFVSVSSRDTSCIPCIHLFFDSKRYVFGSVGEGCQRAILSQQLRLSKIKDVFLMQGSSISSPDTYDSSSSSSTTSVSDMLQLDDRDKVIVSERNSMCSTVNYPTWWDSCGGFPGFLLSLNDISEPGETGEASPFVLHGPSEVHQFLSSMRHFTYHTNVNLTVQGYTSAEAPVFVDENICVTPVVVSLVKNSFKKRKHENINRGTNARPLKEDRANTSPHWYSHVSNDTSFVVENAMYNTPAPLEPDKPELFISYIVQSHPTPGKFDAAKAKSLGITKGLDCGRLARGEPVTLENGKTVYPKEVIGPSIPGSSFFIIHCPNELVIDLVIENHKWTNAPKPVCVIHSVTPEVYKNPRYQSWISSFPSEVSHLIASTEVNEVINYPRSAVAIATLNLLDSKVFPLGFNCYEVKNVQKNNRIAFAKPKLRFAFGKKTGIDDSEVGVSIEELKDKILKEKPDYKSFVEEAQKYVSDKPKAPSFAGSDIQICTLGTGSAMPSLYRNVSSTYVRIPVDKKCMEDSAISMKNILLDCGEGTLGRLSRQYGDNLKYEIASLRWIYISHMHADHHAGVIGVLKAWTKYSDGRSKLFITAPPQFEFWLLEYSRIDYLPLSNIVFISNSALRTDRKPSALESSRLSSLFKEFDLVSFRTVPAIHCPYSYCMEITNSSGWKIAYSGDTRPSEDFANIAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAKKAGTKNVILTHFSQRYPKLPDIDISTEDLHIALAFDGMTLKISDISLFRYFGKPLAYLFNEENLKEESDPLKF
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FSK6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- 13 kDa ribonucleoprotein-associated protein
- Candida glabrata strain CBS138 chromosome M complete sequence
Sequence:
MSCNTSSDICGSNYYSQLNLNSHKTKDIETWYIKLDMSNIRDIKVDLEFKDPNTGESAATILQKYQFQRNELVNVIPTAPDDVIDALEYIGESGTIDKEDDYGRRLRLAELLMEDELKRQLFQQWRDKRYKKEITQFTEDEDDEEFYTPASKDLISARQYILKNSIARANKRIAAQKTISQTYSIQNVLNKRRAANKYWCSFDLLATQVVSTRPISTVTFCNNGNYVASGSWNGEVSIIDSNTLEVTQTLQNHDGKVGGIAWTSNDSVLITGGEDHLITVSNRSDGEFITSNSIGGHEGRITDLQVHPSGKFIGTSSFDSTWRLWDIEKQKQLLLQEGHSKELYCLAFQADGALVSTAGTDKTAIIWDLRSGKAVSQLQGHAKTIYCMDWSIDGHTLATGGGDGVITIWDLRKSDKLTKITEHKSIVTSLKFDKANDHNLISSGYDRSIFVYSKDNYLKVSSLIGHADKVLTFDIDKNNKNLISGGWDRSVKHWSTVSTD
Protein: Ionotropic receptor 76a, isoform E (A8JNV9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ionotropic receptor 25a
- Ionotropic receptor 84a
- Ionotropic receptor 75d
- IP13856p
- Ionotropic receptor 75a
- Ionotropic receptor 8a
- Ionotropic receptor 21a
Sequence:
MENLLVESYYFSTVLSFFAQQFFADSHATCIFWHPAFDFRLETVHPMPLIIMDWHRWANRSDQDVYDYKIKEDEFEGKGIPYNDWTLRLTVAIERSHCETFIAFQEQIPEFARYFYHASIYSIWRSLRNRFMFVYTKEFEDKKDSYLSGYIFQDQPNILVITSQYLNSSTFEIKTNRFVGPRNFNKNPEPVEFYILQRFDAKGTKATWETQSAMSSKMRNLKGREVVIGIFDYKPFMLLDYEKPPLYYDRFMNTTDVTIDGTDIQLMLIFCELYNCTIQVDTSEPYDWGDIYLNASGYGLVGMILDRRNDYGVGGMYLWYEAYEYMDMTHFLGRSGVTCLVPAPNRLISWTLLLRPFQFVLWMCVMLCLLLESLALGITRRWEHSSVAAGNSWISSLRFGCISTLKLFVNQSTNYVTSSYALRTVLVASYMIDIILTTVYSGGLAAILTLPTLEEAADSRQRLFDHKLIWTGTSQAWITTIDERSADPVLLGLMEHYRVYDANLISAFSHTEQMGFVVERLQFGHLGNTELIENDALKRLKLMVDDIYFAFTVAFVPRLWPHLNAYNDFILAWHSSGFDKFWEWKIAAEYMNAHRQNRIVASEKTNLDIGPVKLGIDNFIGLILLWCFGMICSLLTFLGELWRGQG
Protein: Npl6p (A0A1D8PG62)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Bromo domain-containing protein
- Chromatin structure-remodeling complex protein RSC8
- Arp9p
- RFX-type winged-helix domain-containing protein
- Chromatin structure-remodeling complex subunit SFH1
- RSC chromatin remodeling complex ATPase subunit
- Chromatin structure-remodeling complex protein RSC58
- Chromatin structure-remodeling complex subunit RSC1
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MPRIKNQVEKEEQLIEEPKHERDNEYKDEQGVEPQEEEQDDDNDDDDEQLAEEDSEIAPARKRGRKRKITTVVEDEDNNTTKIRKKVKSEDDEGQAANENEEEDDDDDEEEEEADEEDDDDGETEGDGKKKRGRKKKPKVQLYGDDVFDDEGNPLIIENDEVVIPQEDPKGKEKIDELGYLQGDRKFRMKTFKLLGKGDRLYMISTEPARLVGFRDSYLLFKTHRTLFKKVADNDEKMDLIQRGIIPNSYKGRAVNLVTARSIFREFGSRMIENGKKVIDDFWEQRAIDNGDIPGELADPDQLYKTKLSNVLGDSGIVSTGHATPLTATPIVNYQGDPTWMYQIAKQTSEYNKKLYELRTNNMYKGYKDTYTNLTLYPQSTQPTQIKYSKFNNNNGKLVYDIVMTNKNIRKPITRLAKVPQAILNEIDDPEIKQAIIDQQEYEISAREI
Protein: Beta-tectorin (O08524)
Organism: Mus musculus (Mouse)
Function: One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted, extracellular space, extracellular matrix. Note=Found in the non-collagenous matrix of the tectorial membrane. {ECO:0000250}.
Interaction partners:
- Cell adhesion molecule CEACAM16
- Otogelin
- Otogelin-like protein
- Stereocilin
Sequence:
MVVRAFVLLALFAEASAKSCTPNKADVILVFCYPKTIITKIPECPYGWEVHQLALGGLCYNGVHEGGYYQFVIPDLSPKNKSYCGTQSEYKPPIYHFYSHIVSNDSTVIVKNQPVNYSFSCTYHSTYLVNQAAFDQRVATVHVKNGSMGTFESQLSLNFYTNAKFSTKKEAPFVLETSEIGSDLFAGVEAKGLSVRFKVVLNSCWATPSADFMYPLQWQLINKGCPTDETVLVHENGKDHRATFQFNAFRFQNIPKLSKVWLHCETFICDSEKLSCPVNCDKRKRMLRDQTGGVLVVELSLRSRAFSGLCDFSDVLLHLILMLGTWAVL
Protein: Beta-defensin 112 (Beta-defensin 12) (DEFB-12) (Defensin, beta 112) (Q30KQ8)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Beta-defensin 125
- Beta-defensin 129
- Beta-defensin 110
- Beta-defensin 126
- Beta-defensin 121
- Beta-defensin 127
- Beta-defensin 116
Sequence:
MKLLTTICRLKLEKMYSKTNTSSTIFEKARHGTEKISTARSEGHHITFSRWKSCTAIGGRCKNQCDDSEFRISYCARPTTHCCVTECDPTDPNNWIPKDSVGTQEWYPKDSRH
Protein: Sphingosine 1-phosphate receptor 1 (S1P receptor 1) (S1P1) (Sphingosine 1-phosphate receptor Edg-1) (S1P receptor Edg-1) (Q9DDK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Sphingosine 1-phosphate receptor 4
Sequence:
MDDLIARHYNFTGKFRKVHKDPGLKADSVVFIIVCCFIILENVLVLLTIWRTKKFHKPMYYFIGNLALSDLLAGVVYTANILLSGANTYKLTPTQWFFREGSMFVALAASVFSLLAIAIERHLTMLKMKLHNNGKTCRVFMLISTVWFIAAILGGLPVMGWNCIDSMNNCSTVLPLYHKAYILFCTTVFSVILMAIVILYARIYALVRTRSRKLVFRKVANGRGSNKSSEKSMALLKTVIIVLSCFIACWAPLFILLLLDVACQTLTCSILYKAEWFLALAVLNSAMNPLIYTLTSNEMRRAFIKMLNCGVCVQPSGKFSRPIMGAEFSRSKSDNSSHPNKDEPEYSPRETIVSSGNITSSS