wanglab/gogpt-training-data huggingface dataset:
Protein: Protein sneaky (Q9VU52)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the sperm acrosome membrane. Required for breakdown of the sperm plasma membrane after sperm entry into the egg, which is an essential prerequisite for successful fertilization.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:17092953}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:17092953}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17092953}; Multi-pass membrane protein {ECO:0000255}. Note=Has diffuse cytoplasmic expression in primary spermatocytes. In post-meiotic spermatids, detected in clusters of vesicle-like structures adjacent to the nucleus. In late spermatids, a single vesicle-like spot is found near the nucleus, which probably corresponds to the acroblast. In mature sperm, localizes to the apical tip of the sperm head (acrosome). {ECO:0000269|PubMed:17092953}.
Interaction partners:
- Misfire, isoform F
- Uncharacterized protein
Sequence:
MLSLLTRPFLPIFCFLYGPQSEGSTRIQCLRRFVTFLLGLVLGFLLWKLAALNFTLGRLFVNGATDLYVFIIFVLVTGTIFMLSLPVRAVILLIFVALVGKSGRTYLRAVAFAFIISGPIANLVENAGEVARVFVCTTVLTYNLSKTRFDLMAKPFTNTLKHMRGDVEEIRHTFYELQEVLVDLKYAVENSDIEDEKYGDKNTKPIYERWGRETSRMNVSEIGNGGKELPTPAAVQERFQRNMRNRCKHQLRSGHRACLEVFRNGYRKCTTNFPSMIAKAICWPYRVDIICELDLFGNPDKICDPSAVVPQNFGETYVELLKAEKKLFDNSSQIVVNYEIKDEQFAKSQLKSAERTGQAFKEDFERQKRIFNKVMGILQKILCLFMLRMVYVSINYYVKYLNDVEFDNFYITKYFKHVDQRRKEQRIDAILPLRTYEKSKYIDVDHIFSRTHHESTTVCFNLLQFLLELVTAGLFILIDHLVVELLQIVRKRSKIVYQQDGEHEVRFNISGVGQMARLLRTTMHNFNIHEKVSTSLSNKECLPNAHVLPKKMYYQLILLYLIIIVLIYQSTTFLRMRRVICSFFYYKREKQRILFLYNRILRNRLRSLEFLIHDAEDNLATHRIQQQVNVFLWLRFSCPVAFGWIRHFKFAKRTCMICRGLEDSTFTVCGNCGLPYCDDCAEDLNSVCFQCGVVLTRGAEGSESSVEVYTYRKEK
Protein: HTH-type transcriptional regulator YdeO (P76135)
Organism: Escherichia coli (strain K12)
Function: Induces the expression of gadE and mdtEF. Could also regulate the expression of other genes involved in acid resistance.
Interaction partners:
- Protein YdeP
- Two-component-system connector protein SafA
- Formyl-CoA:oxalate CoA-transferase
- DNA-binding transcriptional activator EvgA
- Probable multidrug resistance protein EmrK
- Transcriptional regulator GadE
- Sensor protein EvgS
- Protein YfdX
- Protein HdeD
- Glutamate/gamma-aminobutyrate antiporter
Sequence:
MSLVCSVIFIHHAFNANILDKDYAFSDGEILMVDNAVRTHFEPYERHFKEIGFTENTIKKYLQCTNIQTVTVPVPAKFLRASNVPTGLLNEMIAYLNSEERNHHNFSELLLFSCLSIFAACKGFITLLTNGVLSVSGKVRNIVNMKPAHPWKLKDICDCLYISESLLKKKLKQEQTTFSQILLDARMQHAKNLIRVEGSVNKIAEQCGYASTSYFIYAFRKHFGNSPKRVSKEYRCQSHTGMNTGNTMNALAI
Protein: Potassium transport protein 2 (Q10065)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Together with TRK1, defines the major, high-affinity potassium influx transport system. Involved in maintenance of the proper sodium/potassium ratio in the cell and in regulating the plasma membrane potential.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- K
- Serine/threonine-protein kinase hal4
- rRNA-processing protein fyv7
- V-type proton ATPase subunit d
Sequence:
MQLSGFSTNGSGSLNTIVCEKLLFKPNFVQDSFIIGMTILCSVILYGSGNLRYIDALLLASGSCTQTGLQPVDLTQISIYQQLTILLFGVLSTPITVNLGLTLFKLYFYNKRYDMVITNNKLRMTYTYHTVRRRDTPEPSKVGNRKIRVLLDQGNQMHRPVAPETKAEEAEHQENEKHHRHHFRLRKFANAIDRPSFFRGNTMPALPSYAGVRNSQENEDRTEALSPALGKRRMASIDNGSLSVVQNNARNNPVDFYIPSSFEESSFQTIPEDFEPQVHDHENQTQLNHHLDNNSSISSHNPSLETANDGNQETVSSSNSNYSTTRVDNDPHVASYSPQNSNFDHQAAATTNDAHQNVVRGSAITIAPTPVPRHNRRPIYFADDTNGAEQEKGAHRLDGRGRKRGKSFAVTPTLHRNERSMSVLPFQLAKSFTSALPRRLTFNRTHTKASTMSLPYLSYNATVGRNSAFYALTPVEREELAGIEYESLRILTVILVVYFLFWHILGLVAFLIFIYTAKTSGRVVTDGGINRGWWAAFTSSSLFDNLGYSLNSDSLNSFQKAIFPQVLGTILIFLGNTFFPIMLRFIIWIMIRTTRFSPNFQQALYFLFEHPRRSFTLLFPSKTTWVLFLNLTLLNFASFFFFMVLDLGNSYVDKIPVGYRIMNAIFQNAATRSAGFTVVDLSQIAPAVMVTYMFMMYISAYPIAMSIRQTNVYEERSLGIYAADTENDDDNNINNNNNDNNTPKRKNFLMDHIQRQLSHDLWYLFLGYFIITIVEGRRLESEAEPQFTLFAILFEVISGYGTVGLSLGYKNDPSLTAQFRKISKLVMVALQIRGRHRGLPSALDRAVLMPSDKNFDREEEDYMRRHGKKNTNRADPVPSS
Protein: cDNA, FLJ96701 (B2RDP1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASDDFDIVIEAMLEAPYKKEEDEQQRKEVKKDYPSNTTSSTSNSGNETSGSSTIGETSNRSRDRDRYRRRNSRSRSPGRQCRHRSRSWDRRHGSESRSRDHRREDRVHYRSPPLATGYRYGHSKSPHFREKSPVREPVDNLSPEERDARTVFCMQLAARIRPRDLEDFFSAVGKVRDVRIISDRNSRRSKGIAYVEFCEIQSVPLAIGLTGQRLLGVPIIVQASQAEKNRLAAMANNLQKGNGGPMRLYVGSLHFNITEDMLRGIFEPFGKIDNIVLMKDSDTGRSKGYGFITFSDSECARRALEQLNGFELAGRPMRVGHVTERLDGGTDITFPDGDQELDLGSAGGRFQLMAKLAEGAGIQLPSTAAAAAAAAAAQAAALQLNGAVPLGALNPAALTALSPALNLASQCFQLSSLFTPQTM
Protein: Sterol regulatory element-binding protein 1 (SREBP-1) (Sterol regulatory element-binding transcription factor 1) [Cleaved into: Processed sterol regulatory element-binding protein 1 (Transcription factor SREBF1)] (Q9WTN3)
Organism: Mus musculus (Mouse)
Function: Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 1), which is embedded in the endoplasmic reticulum membrane. Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis and lipid homeostasis.
Subcellular location: [Sterol regulatory element-binding protein 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21459323}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:21459323}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:21459323}; Multi-pass membrane protein {ECO:0000255}. Note=At high sterol concentrations, the SCAP-SREBP is retained in the endoplasmic reticulum (PubMed:21459323). Low sterol concentrations promote recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi, where it is processed (PubMed:21459323). {ECO:0000269|PubMed:21459323}.; SUBCELLULAR LOCATION: [Processed sterol regulatory element-binding protein 1]: Nucleus {ECO:0000269|PubMed:21459323, ECO:0000269|PubMed:8833906, ECO:0000269|PubMed:9062341}.
Interaction partners:
- Sterol regulatory element-binding protein cleavage-activating protein
- Prelamin-A/C
- Peroxisome proliferator-activated receptor gamma coactivator 1-beta
- Fatty acid synthase
- Sterol regulatory element-binding protein 2
- Acetyl-CoA carboxylase 1
- Acyl-CoA desaturase 1
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Histone acetyltransferase p300
- Peroxisome proliferator-activated receptor alpha
Sequence:
MDELAFGEAALEQTLAEMCELDTAVLNDIEDMLQLINNQDSDFPGLFDAPYAGGETGDTGPSSPGANSPESFSSASLASSLEAFLGGPKVTPAPLSPPPSAPAALKMYPSVSPFSPGPGIKEEPVPLTILQPAAPQPSPGTLLPPSFPAPPVQLSPAPVLGYSSLPSGFSGTLPGNTQQPPSSLPLAPAPGVLPTPALHTQVQSLASQQPLPASAAPRTNTVTSQVQQVPVVLQPHFIKADSLLLTAVKTDAGATVKTAGISTLAPGTAVQAGPLQTLVSGGTILATVPLVVDTDKLPIHRLAAGSKALGSAQSRGEKRTAHNAIEKRYRSSINDKIVELKDLVVGTEAKLNKSAVLRKAIDYIRFLQHSNQKLKQENLTLRSAHKSKSLKDLVSACGSGGGTDVSMEGMKPEVVETLTPPPSDAGSPSQSSPLSFGSRASSSGGSDSEPDSPAFEDSQVKAQRLPSHSRGMLDRSRLALCVLAFLCLTCNPLASLFGWGILTPSDATGTHRSSGRSMLEAESRDGSNWTQWLLPPLVWLANGLLVLACLALLFVYGEPVTRPHSGPAVHFWRHRKQADLDLARGDFPQAAQQLWLALQALGRPLPTSNLDLACSLLWNLIRHLLQRLWVGRWLAGQAGGLLRDRGLRKDARASARDAAVVYHKLHQLHAMGKYTGGHLAASNLALSALNLAECAGDAISMATLAEIYVAAALRVKTSLPRALHFLTRFFLSSARQACLAQSGSVPLAMQWLCHPVGHRFFVDGDWAVHGAPPESLYSVAGNPVDPLAQVTRLFREHLLERALNCIAQPSPGAADGDREFSDALGYLQLLNSCSDAAGAPACSFSVSSSMAATTGPDPVAKWWASLTAVVIHWLRRDEEAAERLYPLVEHIPQVLQDTERPLPRAALYSFKAARALLDHRKVESSPASLAICEKASGYLRDSLASTPTGSSIDKAMQLLLCDLLLVARTSLWQRQQSPASVQVAHGTSNGPQASALELRGFQHDLSSLRRLAQSFRPAMRRVFLHEATARLMAGASPARTHQLLDRSLRRRAGSSGKGGTTAELEPRPTWREHTEALLLASCYLPPAFLSAPGQRMSMLAEAARTVEKLGDHRLLLDCQQMLLRLGGGTTVTSS
Protein: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (GMPMT) (EC 2.4.99.16) ((1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase) ((1->4)-alpha-D-glucan:phosphate alpha-D-maltosyltransferase) (P9WQ17)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Essential maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP5 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Exhibits an alpha-retaining catalytic mechanism. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
Interaction partners:
- Maltokinase
- 1,4-alpha-glucan branching enzyme GlgB
- Alpha-maltose-1-phosphate synthase
- Malto-oligosyltrehalose trehalohydrolase
- Glycogen phosphorylase
- Trehalose synthase/amylase TreS
- Glycogen synthase
- Putative maltooligosyl trehalose synthase
- Probable 1,4-alpha-glucan branching enzyme Rv3031
- 4-alpha-glucanotransferase
Sequence:
MSGRAIGTETEWWVPGRVEIDDVAPVVSCGVYPAKAVVGEVVPVSAAVWREGHEAVAATLVVRYLGVRYPHLTDRPRARVLPTPSEPQQRVKPLLIPMTSGQEPFVFHGQFTPDRVGLWTFRVDGWGDPIHTWRHGLIAKLDAGQGETELSNDLLVGAVLLERAATGVPRGLRDPLLAAAAALRTPGDPVTRTALALTPEIEELLADYPLRDLVTRGEQFGVWVDRPLARFGAWYEMFPRSTGGWDDDGNPVHGTFATAAAELPRIAGMGFDVVYLPPIHPIGKVHRKGRNNSPTAAPTDVGSPWAIGSDEGGHDTVHPSLGTIDDFDDFVSAARDLGMEVALDLALQCAPDHPWAREHRQWFTELPDGTIAYAENPPKKYQDIYPLNFDNDPEGLYDEVLRVVQHWVNHGVKFFRVDNPHTKPPNFWAWLIAQVKTVDPDVLFLSEAFTPPARQYGLAKLGFTQSYSYFTWRTTKWELTEFGNQIAELADYRRPNLFVNTPDILHAVLQHNGPGMFAIRAVLAATMSPAWGMYCGYELFEHRAVREGSEEYLDSEKYELRPRDFASALDQGRSLQPFITRLNIIRRLHPAFQQLRTIHFHHVDNDALLAYSKFDPATGDCVLVVVTLNAFGPEEATLWLDMAALGMEDYDRFWVRDEITGEEYQWGQANYIRIDPARAVAHIINMPAVPYESRNTLLRRR
Protein: Olfactory receptor 10G4 (Olfactory receptor OR11-278) (Q8NGN3)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Olfactory receptor 10G7
- Guanine nucleotide-binding protein G
Sequence:
MSNASLVTAFILTGLPHAPGLDALLFGIFLVVYVLTVLGNLLILLVIRVDSHLHTPMYYFLTNLSFIDMWFSTVTVPKMLMTLVSPSGRAISFHSCVAQLYFFHFLGSTECFLYTVMSYDRYLAISYPLRYTSMMSGSRCALLATGTWLSGSLHSAVQTILTFHLPYCGPNQIQHYFCDAPPILKLACADTSANVMVIFVDIGIVASGCFVLIVLSYVSIVCSILRIRTSDGRRRAFQTCASHCIVVLCFFVPCVVIYLRPGSMDAMDGVVAIFYTVLTPLLNPVVYTLRNKEVKKAVLKLRDKVAHPQRK
Protein: PDZ and LIM domain protein 3 (A0A087WYF8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPQTVILPGPAPWGFRLSGGIDFNQPLVITRITPGSKAAAANLCPGDVILAIDGFGTESMTHADAQDRIKAAAHQLCLKIDRGETHLWSPQVSEDGKAHPFKINLESEPQDGNYFEHKHNIRPKPFVIPGRSSEPTASVPPESDVYRMLHDNRNEPTQPRQSGSFRVLQGMVDDGSDDRPAGTRSVRAPVTKVHGGSGGAQRMPLCDKCGSGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFIEGELYCETHARARTKPPEGYDTVTLYPKA
Protein: Taste receptor type 2 (A0A090C7S0)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}.
Interaction partners:
Sequence:
MLSALQLIRMVMLIVTWPCGTILNSSIIAVYLSDWKKGVKLGECDQISLSMGCNYLLLQCFVTLGVAFISYGLHLPFASKVSLAVGAVLWFSVFLSFWLTASLSICYCLRLVNTLSKCFIHLKRRLSHIVTPLLLWSVAISFIITVPINATVGMATDQNITTNYHYIISSVIFMILDGAFGIGFPTLITSICIVLSLISLLRHIRRMKQNTQFGSPQLKTLIGACRTMILLMALNSILFLVILRSMLPPYNVETIWQTVMFSCVMLNPSGQAVVLIFGNSKLLSAWTKTLVPQG
Protein: Axin interactor, dorsalization-associated protein (Axin interaction partner and dorsalization antagonist) (Q6PBN2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as a ventralizing factor during embryogenesis. Inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by axin/JNK-signaling.
Interaction partners:
- EH domain-binding protein 1
Sequence:
MSDVNKTVQKWHASFKKGTDFDSWGQLVEAIDEYQILARQLQKEVQSSNSHDFTEEQKKTLGKFATCLEMRSAALQCTQSQEEFKLEDLKKLEPIIKNILTYNKDFPFDVQPVPLRKILAPGEEENLDVEEDLDAGTGAGSTPSFTSRLPGSLLPRLPSEPGMTLLTLTIEKIGLKDAGQCIDPYITVSVKDLNGIDLNPVQDTPVATRKEDTYIHFSVDVEIQRHLEKLPKGAAIFFEFKHYKPKKRFTSTKCFAFMEMDEIKPGPIVIELYKKPTDFKRKKLNLLTKKPLYLHLNQTLHKD
Protein: Homeotic protein caudal (P09085)
Organism: Drosophila melanogaster (Fruit fly)
Function: Caudal (cad) is one of a number of transcription factors controlling segmentation of the embryo. Further transcriptional regulation via a 5' flanking region containing DNA replication-related elements (DRE) and by dref also regulated by trh and tgo via the CNS midline element. Alongside Bicoid (bcd), caudal forms concentration gradients down the anterior-posterior (A-P) axis providing positional information and subsequent induction of the gap genes. Plays a role in gastrulation/germ band extension, hindgut morphogenesis, positive regulation of cell proliferation, genital disk development and pattern formation. Acts as a key regulator of the Hox gene network and activates transcription via the downstream core promoter element (DPE) relative to the TATA box. Plays a role in the establishment of the hindgut and in the invagination of the hindgut primordium during gastrulation. These effects on the gut are achieved by acting combinatorially at the posterior of the embryo to activate transcription of different targets including fog, fkh and wg. Caudal is involved in regulation of proliferation through transactivation of the E2F gene. Postembryonically its function is mostly restricted to the intestine where it regulates antimicrobial peptide (AMP) levels preserving the normal gut flora.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:2433048}.
Interaction partners:
Sequence:
MVSHYYNTLPYTQKHSAANLAYASAAGQPWNWTPNYHHTPPNHQFLGDVDSSHAAHHAAAAHQMYYNSHHMFHSAAAASAGEWHSPASSTADNFVQNVPTSAHQLMQQHHHHHAHASSSSASSGSSSSGGAPGAPQLNETNSSIGVGGAGGGGGVGGATDGGPGSAPPNHQQHIAEGLPSPPITVSGSEISSPGAPTSASSPHHHLAHHLSAVANNNNNNNNNNNSPSTHNNNNNNNSVSNNNRTSPSKPPYFDWMKKPAYPAQPQPGKTRTKDKYRVVYTDFQRLELEKEYCTSRYITIRRKSELAQTLSLSERQVKIWFQNRRAKERKQNKKGSDPNVMGVGVQHADYSQLLDAKAKLEPGLHLSHSLAHSMNPMAAMNIPAMRLHPHLAAHSHSLAAVAAHSHQLQQQHSAQMSAAAAVGTLSM
Protein: PYD and CARD domain containing (G3V8L1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Inflammasome {ECO:0000256|ARBA:ARBA00004110}.
Interaction partners:
- NACHT, LRR and PYD domains-containing protein 3
- Caspase-1
- Absent in melanoma 2
- NLR family CARD domain-containing protein 4
- NLR family, pyrin domain-containing 1A.
- C-X-C chemokine receptor type 5
- Interleukin-18
- NACHT, LRR and PYD domains-containing protein 12
- Pyrin
- Interleukin-1 beta
Sequence:
MGRARDAILDALENLTADEFKKFKMKLLTAPVREGYGRIPRGALLQMDPIDLTDKLVSYYLEGYGLELTMTVLRDMGIQELAEQLQKIMEESGAVATATSVPAQGTARTEVDGLLDALYGNVLTEGQYQAVRAETTNQNKMRKLFSFAPAWNLTCKNLFLEALRQTQPYLVTDLEQS
Protein: Ferrous iron transport protein B (Q9HW43)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|RuleBase:RU362098}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362098}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ferrous iron transporter FeoA-like domain-containing protein
- Transcriptional regulator HTH-type FeoC domain-containing protein
- Probable outer membrane protein
Sequence:
MTALTLGLIGNPNSGKTTLFNQLTGSRQRVGNWAGVTVERKEGAFHTVRHAVRLVDLPGTYSLTSVSAQASLDEQIACRYIASGEVDVLVNVVDAANLERNLYLTVQLREMGIPCIVALNMLDIARSQRIRIDIDGLARRLGCPVVPLVSTRADGIDELKAAIDSLQLPQAALAVDYPPAIQAQVGYLLETRAPAASAIEPRWLALQALEGDIFNGPALGLPPATLEQARRGCGEEPELAIVDARYRLIGEICAAVCDHQQAQPHRLTQWLDRVVLNRWLGLPIFLLVMYLMFFFAINIGGALQPIFDKGSSAIFIDGIQWLGIRFGLPDWLTVFLAQGIGGGVNTVLPLVPQIGLMYLFLSLLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFGCNVPSIMGARTLDAQRERLITIMMAPFMSCGARLAIFAVFAGAFFGQGGALVIFSLYLLGIVVAILTGLLLKHTLMRGEASPFVMELPLYHVPHLKSLLLQTWSRLRGFVVRAGKVIILVSLVIGGLNSITLDGKPVQGDIGHSALASVSQRLTPLLAPLGVQPDNWQATVGLVTGAMAKEVVVGTLNTLYTAEQIQGEAFDYEGYDLPGQLREALVETWDGLVDTFSLSVLANPVEASMADGDMETGSMGTMASKFGSPIAAYSYLVFVLLYVPCVTAMGAIARESSKGWMAFSVLWGLNVAYSLATLCYQVATFAAHPERSVLTIAVVLLFNLILMTCLRLFGREQVLQLPGRMADAPSGQGGCH
Protein: Pumilio/PUF RNA binding protein 4, putative (Q585G4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEASAEVTGVDGNLGNGKGCATAMVTRGGGDEFSERIWERRHNASLLGGPSAGNSPMDVKRCSLWGNSPPCPRSVGRPVDDNTFTRSIVGATTSLEVSPLAPEGGLLMVEGSSTFTPCAYRRRSCQHLGEPAEGSATTPSVSPTSVAAGLTPSVYSARATRSESAHGAAISGVAAIAAAAAANSTTVASANANNTAGITTQRTGEPLELAGDPSPGFIARLDWGDAVDQVTGGETKDVHASRSDAHCLNEAIGGINLLDELSPLCTPNTRRTSGRWGSNLGIRPTSDSSYSQLARPERLPPQESDLLLGGRSAGMADYQRQQQHQKQELHDTYPLRSGQPYERFTLSSAASGAVNRNPIMSHGSRNNSTIDMMQTSGTNPNRRISFMSGSEHQGKGWSGEKARDVHAAFADPTALLRAEEDADALMRLATKVVHHRHYSSHPVMQQRDLNVTALAGSMMSENGQSAAFTASGSQNSHDAAARSRAPVQMPLHGGRIVKLAADQQGCRMLQSVLERFPFHSSEVQKVISELLPVLTDVMKDPYGNFLVQKLLEVAPDEERMRLLDYHISASLCDVAISPHGNYAVQKLIDSLRSSQEVQVVCRALQRGTLQLMTDLNGGHVIQKLLQCISPKDLTFLYDVIVKDTVDVCNDKHGCCVVQKCMDHAINVHLQRTQKAILRHMLQLSLNPYGNYVVTHLISMCNSQSQRHVVNEAAHCAGPALELLCANKFASNVVEKIVQGCAPSAKLELCRFLFNRSTINTGMSARLMGMDYVLGEQDPQQRLMIQPAAAFVTPYQENTALETIVLNSYGNYVVQTMLDVLPISPELAQLLFLLHKLSPEIMKHNFGKRIASKMEQARERIITHLQERGVNAGEADLIGNRYTDRLADVSRSVIESSFHSNIPMDRPATNYNINGSGTAGETPQMKPQEVEIIKALLASLGSFAPAPPPPPASAAGSVRGPLADVQRAVDVISGPRSNKRKQTQRGRKG
Protein: Bub3 interacting GLEBS and zinc finger domain protein, isoform B (Bub3 interacting GLEBS and zinc finger domain protein, isoform C) (Bub3 interacting GLEBS and zinc finger domain protein, isoform D) (A8DZ09)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKKKKASKPWCWYCNREFDDEKILVQHQKAKHFKCHICHKKLYTGPGLSIHCMQVHKETVDKVPNSLPNRSNIEVEIFGMDGIPAEDLRDHERQKNGGKSDSDDDEPVAKKKVEYAMSVPPPMMMPPNMMPPHMLGQYGMGMMQHMPPLPPYPVPMMPHMMPPRPLFPAAMATTSAAAAAAAAHHHHAAAMAQQKPTFPAYSNATISAPPTTNHAGGASSAPPSGPPDAQQHQQRPPAPPAASGTSAAAVTTKIMHPQEDLSLEELRARQPKIQARLAAALASLANPQSRKSPSNNGGPSTSIPTTPPPPSLAGISPTGSNSSSGMANSIVVSAAMSKAQENAALVAVAQAQAHAHAHAAQVQAQAQAQAVVQAQVQAAHVAHAVAAQQQAVQQQQAAQQQQQAAVQQQAAVQQQQQQQQAAVQQQQAAQQQVKQLEELNRAVMLQRFQAARQPGNPGAAAAAAAAAAVGMMPLPGHMQLMQPMLRPAMAIGPHGTLIGGNMLRAGGPGLHGMPAGLLPMQIGLPGMPGALPAGAMAMPGMGVMLQGHPNMLQMMQPRFR
Protein: Tyrosine--tRNA ligase, mitochondrial (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) (Q9Y2Z4)
Organism: Homo sapiens (Human)
Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:15779907, ECO:0000269|PubMed:30006346}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Pseudouridylate synthase 1 homolog
- Tryptophan--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, mitochondrial
- Alanine--tRNA ligase, cytoplasmic
- Probable proline--tRNA ligase, mitochondrial
- Tryptophan--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Asparaginyl-tRNA synthetase
Sequence:
MAAPILRSFSWGRWSGTLNLSVLLPLGLRKAHSGAQGLLAAQKARGLFKDFFPETGTKIELPELFDRGTASFPQTIYCGFDPTADSLHVGHLLALLGLFHLQRAGHNVIALVGGATARLGDPSGRTKEREALETERVRANARALRLGLEALAANHQQLFTDGRSWGSFTVLDNSAWYQKQHLVDFLAAVGGHFRMGTLLSRQSVQLRLKSPEGMSLAEFFYQVLQAYDFYYLFQRYGCRVQLGGSDQLGNIMSGYEFINKLTGEDVFGITVPLITSTTGAKLGKSAGNAVWLNRDKTSPFELYQFFVRQPDDSVERYLKLFTFLPLPEIDHIMQLHVKEPERRGPQKRLAAEVTKLVHGREGLDSAKRCTQALYHSSIDALEVMSDQELKELFKEAPFSEFFLDPGTSVLDTCRKANAIPDGPRGYRMITEGGVSINHQQVTNPESVLIVGQHILKNGLSLLKIGKRNFYIIKWLQL
Protein: Alternative oxidase (Q8WSV6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MFKYVTVLNKNNNLNKLLLNSISKGNTLNSNNGLASTSISINSSIRSFSSFSSSKVMLDKRSEKPQNPLYHRNSTLYSFTPRDVLIKIEKDFVMPPSYEAKSLSDNFAKFSVLFLRKFSNLFFKEKFLHYAIVLETVAAVPGLVAGMFLHLKTLRNMQSNNWIKILMDEMENERMHLLSFMELTKPTLLERGMVAVTQAIYWNLFLVFYVLSPKTAHRFTGYLEEQAVVTYTHMLEDIDSGKVPNYKAPQIAIEYWGLPEDATLRDLILVIRQDESDHRLVNHEISNKIVLNNNEPIILENHFHKPTIINPVGEEEIKEHSQEGIRIEKKINPTSEL
Protein: E3 ubiquitin-protein ligase SopA (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SopA) (Salmonella outer protein A) (Secreted effector protein SopA) (Q9S4P4)
Organism: Salmonella dublin
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway (By similarity). Required for inducing polymorphonuclear leukocytes migration across the intestinal epithelium.
Subcellular location: Secreted {ECO:0000269|PubMed:11207586}. Host mitochondrion {ECO:0000269|PubMed:15866946}. Note=Secreted via type III secretion system 1 (SPI-1 T3SS), and delivered into the host cell via a Sip-dependent pathway. Localizes to the mitochondria of host cell. {ECO:0000269|PubMed:15866946}.
Interaction partners:
Sequence:
MKISSGAINFSTIPNQVKKLITSIREHTKNGLASKITSVKNTHTSLNEKFKTGKDSPIEFALPQKIKDFFQPKDKNTLNKTLITVKNIKDTNNAGKKNISAEDVSKMNAAFMRKHIANQTCDYNYRMTGAAPLPGGVSVSANNRPTVSEGRTPPVSPSLSLQATSSPSSPADWAKKLTDAVLRQKAGETLTAADRDFSNADFRNITFSKILPPSFMERDGDIIKGFNFSNSKFTYSDISHLHFDECRFTYSTLSDVVCSNTKFSNSDMNEVVLQYSITTQQQPSFIHTTLKNTLIRHKANLSGVILNEPHNSSPPSVSGGGNFIRLGDIWLQMPLLWTENAVDGFLNHEHNNGKSILMTIDSLPDKYSQEKVQAMEDLVKSLRGGRLTEACIRPVESSLVSVLAHPPYTQSALIREWLGPVQERFFAHQCQTYNDVPLPTPDTYYQQRILPVLLDSFDRNSAAMTTHSGLFNQVILHCMTGVDCTDGTRQKAAALYEQYLAHPAVSPHIHNGLFGNYDGSSDWTTRAADNFLLLSSQDSDTAMMLSTDTLLTMLNPTPDTAWDNFYLQRAGENVSTAQISPVELFRHDFPVFLAAFNQQATQRRFGELIDIILSTEEHGELNQQFLAATNQKHSTVKLIDDASVSRLATIFDPLLPEGKLSPAHYQHILSAYHLTDATPQKQAETLFCLSTAFARYSSSAIFGTEHDSPPALRGYAEALMQKAWELSPAIFPTSEQFTDWSDRFHGLHGAFTCTCVVADSMQRHARKYFPSVLSSILPLSWA
Protein: Osteopontin (Bone sialoprotein 1) (Nephropontin) (Secreted phosphoprotein 1) (SPP-1) (Urinary stone protein) (Uropontin) (P10451)
Organism: Homo sapiens (Human)
Function: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.
Subcellular location: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}.
Interaction partners:
- Integrin alpha-V
- CD44 antigen
- Stromelysin-1
- Integrin beta-1
- Fibronectin
- Integrin beta-3
- Osteocalcin
- Integrin-binding sialoprotein
- SPARC
- Glutathione S-transferase Mu 1
Sequence:
MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN
Protein: Protein sgm1 (Q9Y7Y1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000250}.
Interaction partners:
Sequence:
MENSKWGGFLKKAMSNVETSIDKVLDGNQIEEMSRGNAKSKDEIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVVRLTRQVETLSTQYSIQRSQWVREDEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDTNIRSNVKSKPKKIVTTGGIPENNDYTVGKVDTLKVTKEDEDPTTPTNAIPIPSSMSKRDEALENDKDNYFDDLHPLNISTSPQPSPLSFSEIPQSDTRNALENFLDNLPSPSEERSRISRSASEARKLGINAQSRYASISSAVLSPPSEASRKFSLYESEAISPTSGTPSNLEKGAGNVPDVSLLEQLATTIRRLEAELQTTKQQVAQLIIQRDQARQEIVDAYVNNDANEDSKKQVEELRLQLQNLEKEHASTLVTLKQKSDKVFELELDIKDMRELYVSQIDILAGRQ