wanglab/gogpt-training-data huggingface dataset:
Protein: Cytokinin riboside 5'-monophosphate phosphoribohydrolase (EC 3.2.2.n1) (AMP nucleosidase) (EC 3.2.2.4) (PaLOG) (P48636)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the hydrolytic removal of ribose 5'-monophosphate from nitrogen N6-modified adenosines, the final step of bioactive cytokinin synthesis (Probable). Exhibits phosphoribohydrolase activity against AMP in vitro.
Interaction partners:
Sequence:
MTLRSVCVFCGASPGASPVYQEAAVALGRHLAERGLTLVYGGGAVGLMGTVADAALAAGGEVIGIIPQSLQEAEIGHKGLTRLEVVDGMHARKARMAELADAFIALPGGLGTLEELFEVWTWGQLGYHAKPLGLLEVNGFYDPLLTFLDHLVDERFVRAEHRGMLQRGASPEALLDALAAWTPSVAPKWVDRTPQ
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q7YU14)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADEKAKESFRERQAQELEVIKSIFGCDVEDLRPQANPSLWKPTDIRIQLTPLRDSSNGLETYVCTKLHVTCPSKYPKLPPKISLEESKGMSDQLLEALRNQLQAQSQELRGEVMIYELAQTVQAFLLEHNKPPKGSFYDQMLQDKQKRDQELQDLPALGALVESLMPTNSYEMRDFVDKCNSDRTLSASELLEHPFLRFYVDNGQQQVMPLPQQQHPNTVQRTGSAMPYQIPTLALSQSRLRTEFEVLMYLGKGAFGDVLKVRNILDNREYAIKRIPLPARSRQLYKKMTREVELLSRLNHENVVRYFNSWIESVDDADAAEMDKLLGGEWSQSQQDLSVKPAKSPQLGPTLEEDEDEEDSSSSMWNGYIPNMEDSDSDGIEFVDSNGKVAVYDDEEQEDSTRGKTNSPKPLMQVMYIQMEFCEKCTLRTAIDDNLFNDTDRLWRLFREIAEGLAHIHQQGIIHRDLKPVNIFLDSHDQIKIGDFGLATTSFLALQAHDAAPAPVNQITSAEDGTGTGKVGTTLYVAPELTGNASKSVYNQKVDMYTLGIILFEMCQPPFDTSMERAQTIMALRNVSINIPDAMLKDPKYEKTVKMLQWLLNHDPAQRPTAEELLISDLVPPAQLEANELQEMLRHALANPQSKAYKNLVARCLQQESDEVLEHTYHLGSSRAMKSWNSAIIIDDIVSLNPVIEFVKAKVVNLFRKHGAIEVDSPLLSPLSARNSTANANANAVHLMTHSGCVVVLPCDLRTQFARHVTMNSVNLIRRYCVDRVYREERVFNFHPKQSYDCSFDIIAPTTGSHLVDAELLSLAFEITSELPRLREKNLAIRMNHTNLLRAILIFCNVPKAQYGALFEGTMDFIESRISRFQFHSSITGIMEKSRTSAQTLMDMLLANFLLTGSRSTVDDSALKSLMRGKGEAASLARGALRELETVVGLAYSLGVKCPIHIWAGLPISFDRASNGGIVWQMTADLKPNRSGHPSVLAIGERYDSMLHEFQKQAQKFNPAMPARGVLSGAGLTFSLDKLVAAVGVEYAKDCRAIDVGICVCGTRPPLKDVTYIMRLLWSVGIRCGIVEAASELGDEAQDLARLGALHVILVAENGSLRVRSFERERFQERHLTRTELVEFIQKMLRSDGLNGTTVDNFSQLSALGSGDNRSSGGKERERGENGLSTSASNATIKNNYSQLPNLQVTFLTHDKPTANYKRRLENQVAQQMSSTLSQFLKKETFVVLVVELPPAVVNAIVGAINPREIRKRETEPEINYVIERFSKYKRYISEINEEVVDYLSDAKTPIVALYSISDSYYRVII
Protein: HTH-type transcriptional regulator HdiR (A2RKI6)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
Interaction partners:
- Protein RecA
- Pyridoxal-phosphate dependent aminotransferase
- Phage protein
Sequence:
MNFGQNLKKLRKEAKLTQSQLADKLGMKQNAYVLWEQKATNPTLELLEKLADIYDLPIQELIKNPDNGAEKQLIDNYRSLTGEQQESVINFTDFLIEQNKADLIDLKTYRRSSLQYAVVEDEALSAGFGQTANNTGGHYRAYTTENLGRYDGAARVKGESMEPDFPNFSIATFLHTGFGRSGDVYAIAEGDLGEERLYIKQVFEEEDGNFRIHSLNPDPQYKDFYLGQEDNFRIIGPVVDNFEEIEESQIID
Protein: BarH-like 2 homeobox protein (Bar-class homeodomain protein MBH1) (Homeobox protein B-H1) (Q8VIB5)
Organism: Mus musculus (Mouse)
Function: Potential regulator of neural basic helix-loop-helix genes. It may down-regulate expression of ASCL1 and, within the thalamus, up-regulate NGN2, thereby regulating distinct patterns of neuronal differentiation (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MTAMEGASGSSFGIDTILSGAGSGSPGMMNGDFRSLGEARTTDFRSQATPSPCSEIDTVGTAPSSPISVTLEPPEPHLVTDGPQHHHHLHHSQQPPPPSAVPAQSLQPSPQQQPPPQPQSAAQQLGSAAAAPRTSTSSFLIKDILGDSKPLAACAPYSTSVSSPHHTPKQESNAAHESFRPKLEQEDGKTKLDKREDPQSDIKCHGTKEEGDREITSSRESPPVRAKKPRKARTAFSDHQLNQLERSFERQKYLSVQDRMDLAAALNLTDTQVKTWYQNRRTKWKRQTAVGLELLAEAGNYSALQRMFPSPYFYHPSLLGSMDSTTAAAAAAAMYSSMYRTPPAPHPQLQRPLVPRVLIHGLGPGGQPALNPLSNPIPGTPHPR
Protein: Glycoprotein hormone beta-5 (Thyrostimulin subunit beta) (Q812B2)
Organism: Mus musculus (Mouse)
Function: Functions as a heterodimeric glycoprotein hormone with GPHA2 able to bind and activate the thyroid-stimulating hormone receptor (TSHR), leading to increased cAMP production. Plays a central role in controlling thyroid cell metabolism.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Glycoprotein hormone alpha-2
- Thyrotropin receptor
- Glycoprotein hormones alpha chain
Sequence:
MKLVYLVLGAVALLLLGGPDSVLSSSSGNLHTFVGCAVREFTFMAKKPGCRGLRITTDACWGRCETWEKPILEPPYIEAYHRVCTYNETRQVTVKLPNCAPGVDPFYTYPMAVRCDCGACSTATTECETI
Protein: Uncharacterized protein At1g21520 (Q8GYE6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative small RNA degrading nuclease 4
- Uncharacterized protein T2H7.3
- Amino acid transporter AVT1J
- Transcription regulator-like
- Peroxidase 38
- Probable dihydroneopterin aldolase 3
- Chromatin remodeling 34
- Large ribosomal subunit protein uL18c
- Dihydroneopterin aldolase 1
- Dihydroneopterin aldolase 2
Sequence:
MSSGELKPFKKKEGSVIPKERELVKTKAAKAIFSLFRPSCDGKQSSQPSRDGDGDHDGKRVYPTRY
Protein: Cno (Q24279)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSHDKKMLDREAVRSVIQQWNANRLDLFALSEPDENLLFHGVMRFYFQDAGQKVATKCIRVASDATVTDVIDTLIEKFRPDMRMLSVPNYALYEVHANGEERRLNADEKPLLVQLNWHIDDREGRFLLKNIDQKTTPIEQTDLNFKRKLSKREKKEQKKKDKMAKLSSDPPTSNGSHLGLGNGVGASSGSAHMNGNAGGTGGDSSDAVAGKLYTELPETSFTRSISNPEAVMRRRRQQKLEKKLQQFRSRDGGPDTGGTLKIYGESLCQDVPYKTLLLSIRDCAQAVVREMLTKYGLEKADPLHYCLVQVNSDGTEYILDDDECPLSILMNHPTSRGSIMFHVRRRPADSQPRRRKKKPLGAANGANHISGDREGPVLVEVTHSGDGGRRIKLGSDPVEVGSANTNCLQLFGPSIQPRHCLISLLEGVCTVTPLHTDALTFVNGHHISQPTILHNGSVVMFGRVASYRFLDSPTDGRYNLALSQSQLDSACLYERYRASTHYRPELQPTERAHKLTMFLHHVANLVYSVVQEQYTDPRILAFWMANSSEFLHFLKSDRHISAFSVQAQEVLAEAVQTAFRNLVNCFRLELSQTLNQFLSENIDHDSAAGLVLTVLGSAMALLRRCRVNAALTIQLFSQLFHYINVICFNTIVANSQMCTGDWGKVMTERLQLLELWAERQGLELAADCHLAKINQCAQFLQAPKSSVEEIQQLACSCFRLNSLQMAALLQQEKLPRNLVDTAIRMAESVADELTRADGREVRLEESPELHLALLLPDDGFSCDVVRGIPTGLVDFLNPLQQQGMCRLAAQPTSIGLWTVYMHQFNARSSSAMSNKLPQPELQLIKLHKNSNGMGLSIVASKGAGQEKLGIYIKSVVPGGAADADGRLQAGDQLLRVDGQSLIGITQERAADYLVRTGPVVSLEVAKQGAIYHGLATLLQQPSPVIQRGNRRMSERDLTRMGGAESTKSLGPLIANNHPNHSLSLSQHLNNSHNNTLGNSNNSSIINPLAAHLPNSKSVPALHHHTGSGTISLANSKSRSTHSLHNNTSGMGGIGGAAAGGMLGQPNGSQNNANGNGNGNEQGFYQNLSVYRAQNQSQPILNERPPIAAHAAMNAYNGSSPLAPQQQPQQQQQSPYQQQQQQQHMQANANLPPTRPVSAYYHSQQSAQQQLQQQQQQQQQHSLQQQQFALSSGNLNGQQQQQQQHQHQLTLNNRTKSQQNFQHTLRMQQMMAPSMPNISNMYHHQQQHQQQLPLQQQQQQQQQPLMSSSQSMQNVNDFAGGYQNGSLEYRRSQLHDPSTLYEIQQQQLQQQQQQQQQQQQQQQASPNFIALPPKPLGSLQSPNKPNVPPSTAPKPQQQQQRYLGQSLPAEDKPPLPPTATHPLFKATQQIAPGMNYVASTLDPPKGSYVASNQGNNRPLHSGSNPWEREEREKDLEMRREHIRQWREQQISELSQIVSRSPMQEEQLKTLILERDFERRAQELQEQEEQDQEQQYDKENVQELFRLAGGGQVSAIQTPITSYRQTEIKLAEMPDSNSLVDSVPPQPPAPTAQPLSSNTQQPKSILKHNRYSEGGVGPSGAPSSPSKSQKSASFANERHLHTEHPISNLAKELNQLTMLDKDNNNETLDAVVPPPPPPERNSSYLIMSQQKLRGSTGNATSSMGLLKTATSNQAAAAVEIKKASLLNTQTNNNNNLSGSLNNNTMHGSPLSAMELNAAYVSATGTGIIGGLGTPPPPPPLMQRDNKRVSFHDEENNFVSGNSQQQQLQQQYIMDNYGMEHQDLDTIREDTSYLQHNLDASMLPSMPATPDAALWNTSVQSTPGVIGAQEVYRDPRTRRLAEKQQQQQQQRAGDAVPEKLSFKEKMKMFALESGEDKTPKDKLKISRAQRDIDAVH
Protein: T-complex protein 1 subunit alpha (TCP-1-alpha) (CCT-alpha) (Chaperonin containing T-complex polypeptide 1 subunit 1) (P17987)
Organism: Homo sapiens (Human)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:1630492}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}.
Interaction partners:
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit zeta-2
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit beta
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
- Cell division cycle protein 20 homolog
Sequence:
MEGPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGSYEDAVHSGALND
Protein: Myosin-7B (Myosin cardiac muscle beta chain) (Myosin heavy chain 7B, cardiac muscle beta isoform) (A2AQP0)
Organism: Mus musculus (Mouse)
Function: Involved in muscle contraction.
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Myosin light chain 3
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin light chain 6B
- Myosin light chain 4
- Myosin regulatory light polypeptide 9
- Myosin light polypeptide 6
- Troponin I, slow skeletal muscle
- Myosin, light chain 12A, regulatory, non-sarcomeric
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin-7
Sequence:
MMDMSELGESACYLRQGYQEMMKVHTVPWDGKKRVWVPDEQDAYVEAEVKTEATGGKVTVETKDQKVLTVRETEMQPMNPPRFDLLEDMAMMTHLNEAAVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTAAVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFKAGLLGILEELRDQRLAKVLTLLQARSRGRLMRLEYQRMLGGRDALFTIQWNIRAFNAVKNWSWMKLFFKMKPLLRSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELDDAEERADMAETQANKLRARSRDALGPKHKE
Protein: Stromal cell-derived factor 1 (SDF-1) (hSDF-1) (C-X-C motif chemokine 12) (Intercrine reduced in hepatomas) (IRH) (hIRH) (Pre-B cell growth-stimulating factor) (PBSF) [Cleaved into: SDF-1-beta(3-72); SDF-1-alpha(3-67)] (P48061)
Organism: Homo sapiens (Human)
Function: Chemoattractant active on T-lymphocytes and monocytes but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. Binds to the allosteric site (site 2) of integrins and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 in a CXCR4-independent manner. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. Stimulates the proliferation of bone marrow-derived B-cell progenitors in the presence of IL7 as well as growth of stromal cell-dependent pre-B-cells (By similarity).
Subcellular location: Secreted.
Interaction partners:
- C-X-C motif chemokine 11
- Atypical chemokine receptor 3
- C-X-C motif chemokine 6
- C-X-C motif chemokine 10
- C-X-C motif chemokine 9
- C-X-C motif chemokine 2
- C-X-C chemokine receptor type 4
- Platelet factor 4
- C-C motif chemokine 20
- Platelet basic protein
Sequence:
MNAKVVVVLVLVLTALCLSDGKPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQEYLEKALNKRFKM
Protein: Mevalonate kinase (MK) (EC 2.7.1.36) (Q09780)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosphomevalonate kinase
- Diphosphomevalonate decarboxylase
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Acetyl-CoA acetyltransferase
- Hydroxymethylglutaryl-CoA synthase
- Lanosterol synthase erg7
- 3-keto-steroid reductase erg27
- Squalene synthase
- Isopentenyl-diphosphate delta-isomerase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Sequence:
MSKSLIVSSPGKTILFGEHAVVYGATALAAAVSLRSYCKLQTTNNNEIVIVMSDIGTERRWNLQSLPWQHVTVENVQHPASSPNLDLLQGLGELLKNEENGLIHSAMLCTLYLFTSLSSPSQGCTLTISSQVPLGAGLGSSATISVVVATSLLLAFGNIEPPSSNSLQNNKALALIEAWSFLGECCIHGTPSGIDNAVATNGGLIAFRKATAHQSAMKEFLKPKDTLSVMITDTKQPKSTKKLVQGVFELKERLPTVIDSIIDAIDGISKSAVLALTSESDKNSSAKKLGEFIVLNQKLLECLGVSHYSIDRVLQATKSIGWTKLTGAGGGGCTITLLTPECKEEEFKLCKESLLAHKNSIYDVQLGGPGVSVVTDSDSFFPQYESDFDFKKLNLLSKFNKYYI
Protein: Beta-conglycinin beta subunit 1 (CG-beta-1) (Beta-conglycinin beta subunit) (allergen Gly m 5) (P25974)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.
Subcellular location: Vacuole, aleurone grain {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:15447650}. Protein storage vacuole {ECO:0000269|PubMed:15447650, ECO:0000269|Ref.6}. Note=Localizes in protein storage vacuoles in cotyledons of developing and mature beans (PubMed:15447650, Ref.6). Synthesized and assembled into trimers in the endoplasmic reticulum, and transported to the protein storage vacuoles by the dense vesicles (PubMed:15447650). {ECO:0000269|PubMed:15447650, ECO:0000269|Ref.6}.
Interaction partners:
- Glycinin G1
- Glycinin G2
- Glycinin G4
- Basic 7S globulin 2
Sequence:
MMRVRFPLLVLLGTVFLASVCVSLKVREDENNPFYLRSSNSFQTLFENQNGRIRLLQRFNKRSPQLENLRDYRIVQFQSKPNTILLPHHADADFLLFVLSGRAILTLVNNDDRDSYNLHPGDAQRIPAGTTYYLVNPHDHQNLKIIKLAIPVNKPGRYDDFFLSSTQAQQSYLQGFSHNILETSFHSEFEEINRVLFGEEEEQRQQEGVIVELSKEQIRQLSRRAKSSSRKTISSEDEPFNLRSRNPIYSNNFGKFFEITPEKNPQLRDLDIFLSSVDINEGALLLPHFNSKAIVILVINEGDANIELVGIKEQQQKQKQEEEPLEVQRYRAELSEDDVFVIPAAYPFVVNATSNLNFLAFGINAENNQRNFLAGEKDNVVRQIERQVQELAFPGSAQDVERLLKKQRESYFVDAQPQQKEEGSKGRKGPFPSILGALY
Protein: Folliculin (Q9VS33)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004656}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- GH04846p
- GH16429p
- RE13835p
- Cuticular protein 73D, isoform B
- Ragulator complex protein LAMTOR3 homolog
- Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
- Ragulator complex protein LAMTOR2 homolog
- Ragulator complex protein LAMTOR1
- Ragulator complex protein LAMTOR4 homolog
- GATOR complex protein NPRL2
Sequence:
MNAVIALCHFCEAHGPCAIFCTQTLRDTKLEDLSLEQQTQKTCSACNYSMGKNNNAIYSRDTESGATFVSTKVAVLPEVASLVKQAAVLSLSNGTDASKDGEFVFFGDSSRGHILSHTFRVSDLQARGYSQLFSIIVLMKDKYFLLNIKPFLAEHLKKVSSELQAAAKKTKETEEQTYSERQRRLSGAQFLMPTSRALLELTGEEHIFAQLHSHFSWLLLAGSRFLTEHVTFGNLPWLPPQSSGRPPAQRLTYNSSTLPMIESIDDPDLEEFFSLRHLKSVVRKEEFATVCYCALTGVKIVVRGDPRKTFRFMVCLKKLLPEPMHNLMRIDAQHQHSISSEYKIISVSNDIAVPMASSSVYRIDFLDKHVNGHEVSVKWPGELPRKLPDLMVKLLKAVEEKNFTELVLNKQTKVLIEEWKNKVTCLNHAKSTSVQGKLKKVLGVQPHDQPIINYWSTHLH
Protein: 18S rRNA aminocarboxypropyltransferase (EC 2.5.1.157) (20S rRNA accumulation protein 3) (ScTsr3) (Q12094)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Required for processing 35S pre-rRNA at site D.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03146, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:27084949}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03146, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosomal RNA small subunit methyltransferase NEP1
- tRNA wybutosine-synthesizing protein 2
- Putative uncharacterized protein YIL025C
- 18S rRNA
- EKC/KEOPS complex subunit BUD32
- U3 small nucleolar RNA-associated protein 25
- 20S rRNA accumulation protein 4
- UPF0743 protein YCR087C-A
- rRNA biogenesis protein RRP36
- 20S-pre-rRNA D-site endonuclease NOB1
Sequence:
MGKGKNKMHEPKNGRPQRGANGHSSRQNHRRMEMKYDNSEKMKFPVKLAMWDFDHCDPKRCSGKKLERLGLIKSLRVGQKFQGIVVSPNGKGVVCPDDLEIVEQHGASVVECSWARLEEVPFNKIGGKHERLLPYLVAANQVNYGRPWRLNCVEALAACFAIVGRMDWASELLSHFSWGMGFLELNKELLEIYQQCTDCDSVKRAEEEWLQKLEKETQERKSRAKEEDIWMMGNINRRGNGSQSDTSESEENSEQSDLEGNNQCIEYDSLGNAIRIDNMKSREAQSEESEDEESGSKENGEPLSYDPLGNLIR
Protein: FI18602p1 (Straw, isoform F (EC 1.10.3.-, EC 1.16.3.1)) (A1Z6F6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYSFFDHSKNQPDLTPMGSFWQQHVATPSSSTPFDSPFFSATHGLVQTHPSIGGSHSGPAPLNGNSLGSGAPSSILAGTKPALTAGSGYLNSRGSLPTSARYPANKITGTVVEPNPKSPFRHLDFSTSATAELRRNPALSAPDECARACREGEPPRICYYHFTLEYYTVLGAACQVCTPNATNTVWSHCQCVLADGVERGILTANRMIPGPSIQVCENDKVVIDVENHMEGMEVTIHWHGIWQRGSQYYDGVPFVTQCPIQQGNTFRYQWTGNAGTHFWHAHTGLQKLDGLYGSVVVRQPPSRDPNSHLYDFDLTTHIMLISDWLHEDAAERYPGRLAVNTGQDPESMLINGKGQFRDPNTGFMTNTPLEIFTITPGRRYRFRMINAFASVCPAQVTIEGHGMTVIATDGEPVHPVDVNTIISFSGERYDFVISADQPVGAYWIQLRGLGECGIRRAQQLAILRYARGPYQPASSPPTYDVGIPQGVVMNPLDAQCNRQRNDAICVSQLKNALEIDRGILAEKPDVKIFLPFRFFVYRAEDLFQPNTYNRFLVAPTGDHVISLIDEISYLSAPAPLTSQYNDINPDQFCNGDNRPADCGPNCMCTHKIDIPLNAIVEVVLVDEVQQPNLSHPFHLHGYGFSVIGIGRSPDSSVKKINLKHALDLDRRGLLHRQYNLPPTKDTIAVPNNGYVVLRFRADNPGFWLFHCHFLFHIVIGMNLILQVGTNADLPPVPPGFPTCGDHTPSIPIN
Protein: Regulator of Vps4 activity in the MVB pathway protein (F4JNS8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA polymerase V family
- At4g14145
- NADP-dependent alkenal double bond reductase P2
- Chitinase family protein
- Chitinase family protein
- Inactive endochitinase At2g43600
- Endochitinase At2g43610
- chitinase
- At4g01700
- Endochitinase At2g43580
Sequence:
MTAAEVASAQTKKLMKFSLSLFRRGFNSSKCKTAAKMAVARIKLIRNKRLVVVKQMRRDIAVLLQSGQDATARIRVEHVIREQNIQAANEIIELFCELIVSRLTIITKQKQCPVDLKEGIASLIFAAPRCSEIPELGDLRDIFAKKYGKDFVSAATDLRPSCGVNRMLIDKLSVRNPGGEYKLKIMKEIAKEFQVDWDTTETEQELLKPQEESIDGPRKFVSASSLPVNRAAINEPIDPTKAVPRSTSSMSINTHYHDTESAAEAATELAKQAVAAAQVASLLATRRDSSNKEFSVSSDHSTHQKDSQYMDHHHHHPGSRRQSRDSETSSYYAKPGAENRGMGRRHSYNNPGINESDYEEEYTNTEAEAKETMRRRHSYNPRSVPPPATSEIKFDESDYYEEETEPDEPSQGRVSSLPPNRAPPQAPQSGESRQDSSGHQVHPKLPDYDILAARFEAIRHSKGPLI
Protein: HTH-type transcriptional regulator RpiR (Als operon repressor) (P0ACS7)
Organism: Escherichia coli (strain K12)
Function: Regulatory protein involved in rpiB gene repression. Also involved in als operon repression.
Interaction partners:
- D-allose transport system permease protein AlsC
- Ribose-5-phosphate isomerase B
- D-allose-binding periplasmic protein
- Glucokinase
- D-allose import ATP-binding protein AlsA
- D-allulose-6-phosphate 3-epimerase
- D-allose kinase
Sequence:
MSQSEFDSALPNGIGLAPYLRMKQEGMTENESRIVEWLLKPGNLSCAPAIKDVAEALAVSEAMIVKVSKLLGFSGFRNLRSALEDYFSQSEQVLPSELAFDEAPQDVVNKVFNITLRTIMEGQSIVNVDEIHRAARFFYQARQRDLYGAGGSNAICADVQHKFLRIGVRCQAYPDAHIMMMSASLLQEGDVVLVVTHSGRTSDVKAAVELAKKNGAKIICITHSYHSPIAKLADYIICSPAPETPLLGRNASARILQLTLLDAFFVSVAQLNIEQANINMQKTGAIVDFFSPGALK