wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent RNA helicase TDRD9 (EC 3.6.4.13) (Tudor domain-containing protein 9) (Q14BI7)
Organism: Mus musculus (Mouse)
Function: ATP-binding RNA helicase which plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Acts downstream of piRNA biogenesis: exclusively required for transposon silencing in the nucleus, suggesting that it acts as a nuclear effector in the nucleus together with PIWIL4.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20011505, ECO:0000269|PubMed:20059948, ECO:0000269|PubMed:28633017}. Nucleus {ECO:0000269|PubMed:20059948, ECO:0000269|PubMed:28633017}. Note=Component of the nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to piP-bodies, a subset of the nuage which contains secondary piRNAs. PIWIL2 is required for its localization to piP-bodies. {ECO:0000269|PubMed:20059948}.
Interaction partners:
- Piwi-like protein 4
- Protein maelstrom homolog
- Piwi-like protein 2
- Tudor and KH domain-containing protein
- Piwi-like protein 1
- Tudor domain-containing protein 7
- Inactive peptidyl-prolyl cis-trans isomerase FKBP6
- Mitochondrial cardiolipin hydrolase
- Small RNA 2'-O-methyltransferase
- Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1
Sequence:
MLRKLTVDQINDWFTIGKTVTNVELLGLPPAFPAEAPREEVQRSEEVPNEDPTAQAQVPVKATAPARPASTSGRSLSQRSSEMEYINKYRQLEEQELDIYGQDQPPSGPGLRSPLAKLSNVACIPETTYKYPDLPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATINCKQFADYFAVPVQNKMNPAYVFEVEGKPHAIEEYYLNDLGHIYHSGLPYRLEEPVITKDVYEVAVSLIQMFDDLDMKESGNKTWSGAQFVSERSSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAIPDHVVPEMLRCPLGSTILKVKLLDMGEPRALLATALSPPSLSDIERTILLLKEVGALAVSGQREDENPHDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLDGYRNKVHFSGSSRSDCLALVEAFRAWQACRQRGELRRPKDELDWGRLNYIQIKRIREVAELYEELKNRISQFNMFVGPHHPVLDQEYPYKQRFILQVVLAGAFYPNYFTFGQPDEEMAVRELAGKDPKTTVVLKHIPPYGFLYYKQLQSLFRQCGQVKSIVFDGAKAFVEFSRNPTERFKTLPAVNLAVKMSQLKVSLELSVHAAEEIEGKVQGGSVSKLRNTRVNVDFQKQTVDPMQVSFNTLDRPRTVADLLLTIDVTEVVEVGHFWGYRIDERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKESYFRAQILYVSGNSAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRPSAKSLICGEHWSGGAHGRFAALVGGCPLLVKVFSIVHSVLHVDVYRYSGAQDAVNVRDVLIREGYAELAEESYESKQSYEVLKGFFAKSVDTMPDGSVSSPLKDDEKHLLRILLESFASNRLGAPNCKAVLHGPFNPYELKCHSLTRISKFRCVWIEKESINSVVISDSPADLHQRMLVAASLSVNETGSTMLLRETSLMPHIPGLPALLSMLFAPVMELRVDREGKCYTGVLCGLGWNSATEAPILPEHDIELAFDVRLNVEDIVEINILRAAINKLVCDGPNGSKYLGPERIAQLQENARQKLLGLFCRLKPREKITPQWHEKPYEWNQVDPRLIMEQAEPEGSPGKSTSLYQLHTPVVLSP
Protein: CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase (EC 2.4.3.-) (Alpha-2,8-sialyltransferase 8D) (Polysialyltransferase-1) (Sialyltransferase 8D) (SIAT8-D) (Sialyltransferase St8Sia IV) (ST8SiaIV) (Q64692)
Organism: Mus musculus (Mouse)
Function: Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92187}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q92187}. Secreted {ECO:0000250|UniProtKB:Q92187}.
Interaction partners:
- Neural cell adhesion molecule 1
Sequence:
MRSIRKRWTICTISLLLIFYKTKEIARTEEHQETQLIGDGELCLSRSLVNSSDKIIRKAGSTIFQHSVQGWKINSSLVLEIRKNILRFLDAERDVSVVKSSFKPGDVIHYVLDRRRTLNISHNLHSLLPEVSPMKNRRFKTCAVVGNSGILLDSGCGKEIDSHNFVIRCNLAPVVEFAADVGTKSDFITMNPSVVQRAFGGFRNESDREKFVHRLSMLNDSVLWIPAFMVKGGEKHVEWVNALILKNKLQVRTAYPSLRLIHAVRGYWLTNKVPIKRPSTGLLMYTLATRFCDEIHLYGFWPFPKDLNGKAVKYHYYDDLKYRYFSNASPHRMPLEFKTLNVLHNRGALKLTTGKCMKQ
Protein: Transcriptional activator protein TraR (P54294)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Positive regulation of conjugal transfer of Ti plasmids. TraR activates target genes in the presence of AAI and also activates traR and traI themselves.
Interaction partners:
Sequence:
MQHWLDKLTDLAAIQGDECILKDGLADLAEHFGFTGYAYLHIQHKHTIAVTNYHRDWRSAYFENNFDKLDPVVKRAKSRKHVFAWSGEQERSRLSKEERAFYAHAADFGIRSGITIPIKTANGSMSMFTLASERPAIDLDREIDAAAAAGAVGQLHARISFLQTTPTVEDAAWLDPKEATYLRWIAVGMTMEEVADVEGVKYNSVRVKLREAMKRFDVRSKAHLTALAIRRKLI
Protein: Trans-aconitate 3-methyltransferase (EC 2.1.1.145) (P32643)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized protein YGL117W
Sequence:
MSTFSASDFNSERYSSSRPSYPSDFYKMIDEYHDGERKLLVDVGCGPGTATLQMAQELKPFEQIIGSDLSATMIKTAEVIKEGSPDTYKNVSFKISSSDDFKFLGADSVDKQKIDMITAVECAHWFDFEKFQRSAYANLRKDGTIAIWGYADPIFPDYPEFDDLMIEVPYGKQGLGPYWEQPGRSRLRNMLKDSHLDPELFHDIQVSYFCAEDVRDKVKLHQHTKKPLLIRKQVTLVEFADYVRTWSAYHQWKQDPKNKDKEDVADWFIKESLRRRPELSTNTKIEVVWNTFYKLGKRV
Protein: Formate dehydrogenase iron-sulfur subunit (Q9HUZ8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
- Nitrate-inducible formate dehydrogenase, gamma subunit
- Formate dehydrogenase-O, major subunit
- Protein FdhE homolog
- Periplasmic nitrate reductase
- Probable oxidoreductase
- Glutathione-independent formaldehyde dehydrogenase
- N-formylglutamate deformylase
- Formyltetrahydrofolate deformylase
- Kynurenine formamidase
- Formyltetrahydrofolate deformylase
Sequence:
MSSQDIHARSATTTPMPSVRNQEEVAKLIDVSKCIGCKACQVACSEWNELRDEVGHNHGTYDNPMDLTADSWTVMRFTEHENEAGNLEWLIRKDGCMHCAEPGCLKACPSPGAIVKYANGIVDFNQDKCIGCGYCITGCPFDIPRISQKDHKAYKCSLCSDRVSVGMEPACVKTCPTGAIVFGSKEDMKEHAAERIVDLKSRGYENAGLYDPEGVGGTHVMYVLHHADKPSLYAGLADQPSVSPLVSLWKGVTKPLALLAMGATVLAGFFHYVRVGPNRADDEEDHGQAEAPVHQVDPSVHTFDPHERR
Protein: Protein RecA (Recombinase A) (Q0P7V6)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
- DNA polymerase I
- Beta sliding clamp
- DNA topoisomerase 1
- DNA repair protein RecN
- DNA 3'-5' helicase
- DNA polymerase III subunit delta
- DNA 3'-5' helicase
- DNA processing protein A
- DNA-directed RNA polymerase subunit beta
- DNA repair protein RadA
Sequence:
MDDNKRKSLDAALKSLDKTFGKGTILRLGDKEVEQIDSIGTGSVGLDLALGIGGVPKGRIIEIYGPESSGKTTLTLHIIAECQKAGGVCAFIDAEHALDVKYAKNLGVNTDDLYVSQPDFGEQALEIVETIARSGAVDLIVVDSVAALTPKAEIEGDMGDQHVGLQARLMSQALRKLTGIVHKMNTTVIFINQIRMKIGAMGYGTPETTTGGNALKFYASVRLDVRKVATLKQNEEPIGNRVKVKVVKNKVAPPFRQAEFDVMFGEGLSREGELIDYGVKLDIVDKSGAWFSYKDKKLGQGRENSKAFLKENPEIADEITKAIQNSMGIEGMISGSEDDEGEE
Protein: Olfactory receptor (Q8VGP6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
- Receptor-transporting protein 2
- Guanine nucleotide-binding protein G
Sequence:
MGGNQTLITQFILLGFPLSPRMQMLLFALFSLFYAFTLLGNGTILGLICLDSRLHTPMYFFLSHLAIVDIAYACNTVPQMLVNLMDPAKPISFAGCMTQTFLFLTFAHTECLLLVVMSYDRYVAICHPLRYTAIMSWRVCVILVLTSWILGVLLALVHLVLLLPLPFCGSQKVNHFFCEIIAVLKLACSDTRINELMVLAGAVSVLVGPFSSIVVSYAHILCAILKIKSQQGRQKAFSTCSSHLCVVGLFYGTAIVMYIGPQHGKSNEQKKYLLLFHSLFNPMLNPLIYSLRNKEVKSALKRTLLKEDTS
Protein: Neuronal acetylcholine receptor subunit beta-4 (Neuronal acetylcholine receptor non-alpha-2 chain) (N-alpha 2) (P12392)
Organism: Rattus norvegicus (Rat)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:P04757}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P04757}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-3
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit alpha-5
- Acetylcholine receptor subunit alpha
- Neuronal acetylcholine receptor subunit beta-2
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit alpha-9
- Acetylcholine receptor subunit delta
- Acetylcholine receptor subunit beta
- Acetylcholine receptor subunit epsilon
Sequence:
MRGTPLLLVSLFSLLQDGDCRLANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIRLELSLSQLISVNEREQIMTTSIWLKQEWTDYRLAWNSSCYEGVNILRIPAKRVWLPDIVLYNNADGTYEVSVYTNVIVRSNGSIQWLPPAIYKSACKIEVKHFPFDQQNCTLKFRSWTYDHTEIDMVLKSPTAIMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDIPLIGKYLLFTMVLVTFSIVTTVCVLNVHHRSPSTHTMASWVKECFLHKLPTFLFMKRPGLEVSLVRVPHPSQLHLATADTAATSALGPTSPSNLYGSSMYFVNPVPAAPKSAVSSHTAGLPRDARLRSSGRFREDLQEALEGVSFIAQHLESDDRDQSVIEDWKFVAMVVDRLFLWVFVFVCILGTMGLFLPPLFQIHAPSKDS
Protein: Zgc:153049 (Q08BP6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MIHYLRWTGFLWIVNSIPFASGMAVNERIDHTCPPLKLEDKWHTNVNLHRELTGFDLAEKFLLRKGTVTDSDTPLFRLGSKPLFKPTESVFPNGLSHEYSIVATFRIRKTTKKDRWFVLQIFDKGGTSQVSLIVDGAKKSVEFLALGFLKNSLLYVFKNRDLHALFDRQFHKLGVSVESNAVSIYLDCELIERQVTAERSGIDVSGRTFITTRLEDGKPVDVELQEILVFCDSRIADLDRCCDSPGAMCEPTVTHNPTAIPLVTGYLQKMLSMPAQLPTDRCHCPALKVL
Protein: Pdcd6ip protein (Q80Y09)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MASFIWVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRSALGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHIKDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNVASRYDEYVNVKDFSDKINRALTAAKKDNDFIYHDRVPDLKDLDPIGKATLVKPTPVNVPVSQKFTDLFEKMVPVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIKELPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDTIALLCKPEPELNAAIPSANPAKTMQGSEVVSVLKSLLSNLDEIKKERESLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTERDELLKDLQQSIAREPSAPSIPPPAYQSSPAAGHAAAPPTPAPRTMPVSTPAKPQPPARPPPPVLPANRVPPASAAAAPAGVGTASAAPPQTPGSAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPTYPFPQPPQQSYYPQQ
Protein: Proteasome assembly chaperone 3 (Q586K0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPAPSLATRHFTFTHEVPADDVFELEENAPRRVPIACVTLQMVSFNRRCFWFHIAMTREGFSAPPPPFGACAVSFSGVSGDSAATTLVDDTALPQLGFKEAQHEVGVGAPNPQAVFADSLARRLSRRLEREFTSGVAVYVACGIIGENQSDLLGTPAGYGSEVTRRFGAEVFKHAMDLICEEGLGKATAA
Protein: Cullin 4B (K4DI93)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKSVCPVTSGFSSPSPSAAAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSSNSSNEREDFDSTSSSSSTPPLQPRDSASPSTSSFCLGVSVAASSHVPIQKKLRFEDTLEFVGFDAKMAEESSSSSSSSSPTAATSQQQQLKNKSILISSVASVHHANGLAKSSTTVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDICFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTLVLLMFNEGEEFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA
Protein: Alpha-1,6-rhamnosyltransferase MigA (Q9I5M1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- GDP-6-deoxy-D-mannose reductase
- dTDP-4-dehydrorhamnose 3,5-epimerase
Sequence:
MIEEATSSKHSGTTDAPLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHGFQLYRQQNQGVSAALNFGLRHARGDYVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIYIDSEGQETKRQNGNRIRQLDFDYLLGNAYVCGAPVSLYRMEALRAAGFYDPEIKVQDFQMTLRIASQGYQIHKLPVLVTRYRRHPDNLSRRYKVLLDADLRTIAPYQSHPAYERGRTELVNKALKYAVVADKRHAWQLLRSLPLRQWNRTTFRRLKRFLLHHES
Protein: U6 snRNA-associated Sm-like protein LSm7 (O74499)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Probable component of the spliceosome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- LSM1-LSM7 complex subunit lsm1
- LSM complex subunit lsm4
- LSM complex subunit lsm5
- LSM complex subunit lsm6
- LSM complex subunit lsm3
- LSM2-LSM8 complex subunit lsm8
- LSM complex subunit lsm2
- Deadenylation-dependent mRNA-decapping factor pdc2
- Small nuclear ribonucleoprotein Sm D2
- U4/U6 snRNA-associated-splicing factor prp24
Sequence:
MSSLQKRPGPGNSSQPTERPRKESILDLSRYQDQRIQATFTGGRQITGILKGFDQLMNLVLDDVEEQLRNPEDGKLTGAIRKLGLVVVRGTTLVLIAPMDGSEEIPNPFVQAE
Protein: Putative pyridoxal kinase C6F6.11c (EC 2.7.1.35) (O14242)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for synthesis of pyridoxal-5-phosphate from vitamin B6.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable pyridoxamine 5'-phosphate oxidase
- Putative pyridoxal kinase C18.10
- Uncharacterized glutaminase C222.08c
- Uncharacterized oxidoreductase C215.11c
- Probable pyridoxal reductase 2
- Pyridoxal reductase
- Uncharacterized oxidoreductase C3A11.11c
- Probable pyridoxal 5'-phosphate synthase subunit PDX1
- Proliferating cell nuclear antigen
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
Sequence:
MNTTKRILAIQSSVCHGYVGNRAATFPLQLLGWDVDAIPTVELSNHAGYPIVKGRTLSAEQILDLYKGVSAANPSGYECLLTGYARGIGSVKAIMEIVRSVKSKNKKAFWVFDPVLGDNGRLYVEESIIPLYREMLPFADLITPNGFEAEILSGMRINSIDTAFKCVECLQQKYKVPRVVISSFVVEENGVEKLYCIGSSIYSKSFFVLIPVIPGIFRGTGDLFTALMAAHIAESPDCTESLASIKEDKLKKSVEMALSSVHEVIQKTADRISALGVEEYHPAYAELCIVNSQNSIIAPSKLFEAVYYY
Protein: Bacterial surface antigen (D15) domain-containing protein (Q54XQ5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- SMP-LTD domain-containing protein
- SMP-LTD domain-containing protein
- Translocase of outer mitochondrial membrane
- Translocase of outer mitochondrial membrane
- Uncharacterized transmembrane protein DDB_G0283573
- Mitofilin
- Probable mitochondrial Rho GTPase gemA
- Uncharacterized protein
- Glutathione S-transferase domain-containing protein
- Reticulon-like protein
Sequence:
MKDYLQIVAEEIHYPSFPGPYHELTKDAQIRIDFIEEVQTGISLSLDKKKGGNNFSADCGLMPMFYRLEVGRDINDNQKLGAIIQPEKLELNYNFSPSKLLFGGILGGKSSRIGGDIYVGVPMTPQINFEKLVKKISTVGTITHETNKTSTEFKVSRIYMGDIDHRLAGLTFCYGLKPSLSLGFELYCKFIQGSGASIGGASLGARHRGRAMGIQYDLAGTCNIFGDLQLTSSIGIIPNRLSFSTRFNLNTSNIISNIQFGTRINGNPIIGNHEIPICLKLRTDTNFENAIALDIDTPFTSISIGCFGKKLDLFKNYGINFSF
Protein: Spliceosome-associated protein CWC27 homolog (Probable inactive peptidyl-prolyl cis-trans isomerase CWC27 homolog) (D6REK3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSNIYIQEPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVLFNPFDDIIPREIKRLKKEKPEEEVKKLKPKGTKNFSLLSFGEEAEEEEEEVNRVSQSMKGKSKSSHDLLKDDPHLSSVPVVESEKGDAPDLVDDGEDESAEHDEYIDGDEKNLMRERIAKKLKKDTSANVKSAGEGEVEKKSVSRSPPSLCLYLDYWIQLSRITQAYTSWYYYGFLDSSLSCVSSASLLLTRHNVYFTLQTHSTDHLAACFFMK
Protein: Uncharacterized protein (Q57Y66)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDSDTIYCDESSVASLSQPQGRPALRLDSLPPTPMVLTPCDSNVTASARKNQLKQQRHQHRSSFACTALTSPSLSQSDFIPETQSLTPPPRPGAVGPASGACDNEVEGGMDVSEANDNACADSSALSSGRPPVFSISRELNSTQSTEDRSSSPSSLLREPRATITPRNFPHLQLSDCEVSQGDNDEHVPDSQGSALEQEFQACLEGHGECFDAEAESAEVFGRQPLITSQEVYEEGCGSNAMRRSMLLPPGAALGAMSGGLTPPGEPTIHEEQLRPGCGKRVRSLQSSLLLCNGGISPLVGGASEVGTQVTNAPDEEDERKRFRPDAEAAQRRNEALMRTAATDVQQTQLSNSCLSGSWDVRLSPATEPRGRESLLLVSGSTPTPSLQVLTGTPVRDGAGCASEILDTRDSANANTSAPASTAPNNETSLVGSDYDSVWPRNVAAGDGTGEGECALRISDTTEECCDCKETLGNKAVGGFSGVGGNAERGPRSTDHRTVVPDGEGCAELVSSPRLSEEFRSFVEGARSEVRRASERLLAKLEEVSRTYSGSNVDGGAAADANGPSEAIQSASQDAVVAAEGRRVVRSLQLSLNRSSVVLGELELAQGRSTLSHSGSRGDSINSILSDTSSLRRQLATHAAAISRRLHGYDLDEAGTLPMIVVVRVVQQVLMIGSPSSVAPNSEEAADLSMCIASPSPVTKLQHQKSQSPMSVASPGTLHTISSGGVSSPSATHRSLWERMLNRRKASAMEDDAMKMYIGLWRCFHECFGERGVMERLGVQPSGEADDGSDGTDSEARLMTPTCLPLLRQQLNRLGCQQGRHRYHPPPLDVMVNYRVFAHSLAELW
Protein: CRS1C-3 (Defensin, alpha, 39) (Q9D848)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Alpha-defensin 29
Sequence:
MKTLVLLSALALLAFQVQADPIKNTDEETKTGEQPEEEDQAVSVSFGGTEGSALQYVAQRRFPWCRKCPVCQKCQVCQKCPVCPTCPQCPKLPLCKERQNKSAITTQAPNTQHKGC
Protein: Ethylene-responsive transcription factor ERF069 (Q8W4I5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Chaperone protein dnaJ 72
- Heavy metal-associated isoprenylated plant protein 4
- Purine permease 21
- Dof zinc finger protein DOF4.5
- Probable purine permease 10
- Putative purine permease 12
Sequence:
MKRIVRISFTDMEATDSSSSEDESPPSSRRRGKKLVKEIVIDHSDPPEVGKTRFKIRIPASLLAARNTTANKKKFRGVRQRPWGKWAAEIRCGRVKGRPERIWLGTFETAEEAALAYDNAAIQLIGPDAPTNFGRPDVDSAVVKKQDSDASGGASEEVV
Protein: Phosphoinositide phospholipase C 7 (EC 3.1.4.11) (Phosphoinositide phospholipase PLC7) (AtPLC10) (AtPLC7) (PI-PLC7) (Q9LY51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Inositol polyphosphate multikinase alpha
- Inositol polyphosphate multikinase beta
- Type I inositol polyphosphate 5-phosphatase 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phosphatidylinositol 3-kinase VPS34
- Multiple inositol polyphosphate phosphatase 1
- Phosphatidylinositol-3-phosphatase myotubularin-2
- Phosphatidylinositol-3-phosphatase myotubularin-1
- Type I inositol polyphosphate 5-phosphatase 2
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
Sequence:
MSKQTYKVCFCFRRRYRHTVSVAPAEIKTLFDNYSDKGLMTTDLLLRFLIDVQKQDKATKEEAQDIVNASSSLLHRNGLHLDAFFKYLFAVTNSPLSSLEVHQDMDAPLSHYFIYTGHNSYLTGNQLSSDCSELPIIEALKKGVRVIELDIWPNSDEDGIDVLHGRTLTSPVELIKCLRAIREHAFDVSDYPVVVTLEDHLTPKLQAKVAEMVTDIFGEMLFTPPSGECLKEFPSPAFLKKRIMISTKPPKEYKAATDDDLVKKGRDLGDKEVWGREVPSFIRRDRSVDKNDSNGDDDDDDDDDDDDDDGDDKIKKNAPPEYKHLIAIEAGKPKGGITECLKVDPDKVRRLSLSEEQLEKASEKYAKQIVRFTQRNLLRVYPKGTRITSSNYNPLIAWSHGAQMVAFNMQGLGRSLWVMQGMFRGNGGCGYIKKPDLLLKSNAVFDPEATLPVKTTLRVTIYMGEGWYYDFPHTHFDRYSPPDFYTRVGIAGVPADTVMKKTKTLEDNWIPAWDEVFEFPLTVPELALLRIEVHEYDMSEKDDFGGQICLPVWELRQGIRAVPLRNQDGVKCRSVKLLVRLEFV
Protein: SR family splicing factor SC35, isoform A (Q7KTD2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDGRMLDGRELRVQMARYGRPSSPTRSSSGRRGGGGGGGSGGRRRSRSRSPMRRRSRSPRRRSYSRSRSPGSHSPERRSKFSRSPVRGDSRNGIGSGSGGLAPAASRSRSRS
Protein: Stathmin (Q9GQR4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVNNTVDTEATEIRCQEKSRGGLSYEVILAEPAPNVAVPKRPVTPGKNVSVEEIEQKLKAAEERRISLEAKKMADISTKLAKVEEATRKKDEITNEFITQTKEQLESKMELHVEKREAIISDMKEKLKIHAQDIEKTRETLEQQKANEQKAIEEKLKIAQSLRDENIKKMLDRL
Protein: Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase (EC 3.5.1.118) (Gamma-glutamyl hercynylcysteine S-oxide hydrolase) (O69670)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the hydrolysis of the gamma-glutamyl amide bond of hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide to produce hercynylcysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine. Ergothioneine is an antioxidant that protects mycobacteria from oxidative stress.
Interaction partners:
- Hercynine oxygenase
- Histidine N-alpha-methyltransferase
- Probable hercynylcysteine sulfoxide lyase
- Glutamate--cysteine ligase EgtA
Sequence:
MCRHLGWLGAQVAVSSLVLDPPQGLRVQSYAPRRQKHGLMNADGWGVGFFDGAIPRRWRSPAPLWGDTSFHSVAPALRSHCILAAVRSATVGMPIEVSATPPFTDGHWLLAHNGVVDRAVLPAGPAAESVCDSAILAATIFAHGLDALGDTIVKVGAADPNARLNILAANGSRLIATTWGDTLSILRRADGVVLASEPYDDDSGWGDVPDRHLVEVTQKGVTLTALDRAKGPR
Protein: Mediator-associated protein 3 (DEK-domain containing protein At5g42060) (KELP-like protein) (Q9FHX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 6
- F16B3.27 protein
- Gb|AAF32471.1
- Mediator-associated protein 2
- rRNA 2'-O-methyltransferase fibrillarin 2
- Mediator of RNA polymerase II transcription subunit 25
- ATP-dependent DNA helicase Q-like 2
- Mediator of RNA polymerase II transcription subunit 20a
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 17
Sequence:
MEEVAREEVEIDKDLRRKIKKTVKKILESSNLYKITEIKAREEASLKLDLDLSQDPYKVIVKEEVENFLEEAVKLIGNKLAMLPKRIESTSI
Protein: Zgc:136228 (Q58EJ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MYKNSYSQATFGLEAKKIHKAKKGKSCGYYMRIVFSFSSLIQSLFIASLVLFLVYGQPEKTAEEKRLEDLQQAYDTLSKDHTKLRKEKADLATALKTKSGEKDAADKEITKLKTDLNISIAGSKNWQRLNSQCEANAKLKLSSTRNTPLMCPPANPNQSGEVKTLNTLLDQQKALYGILKSNFSQTVEYLKSDLDHAVKDKNEHHSQVIKLRQENKDLKSQLDVYTKKCKEDFADSLQGIQTVTTAFLSKIDNFFTNSVTFHLTCPKQEEQMDRIRSNCSSLSRQVEDKFQSYLNNVGAKVSNIQKQSSWLEIQNEKLTSELDKCKTEAEKEASDSSKKLQDAQTTCDKQLEQLLKEQTRLRNAKDLVDTELSVKEATIISLQKGCTPQAKPSGFQPLGSAGQYPSTSG