wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-like protein 7 (Bone marrow stromal cell ubiquitin-like protein) (BMSC-UbP) (Ubiquitin-like protein SB132) (Q96S82)
Organism: Homo sapiens (Human)
Interaction partners:
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin conjugation factor E4 B
- Ubiquilin-2
- Ubiquilin-1
- DNA excision repair protein ERCC-1
- UV excision repair protein RAD23 homolog B
- Zinc finger protein 428
Sequence:
MSLSDWHLAVKLADQPLTPKSILRLPETELGEYSLGGYSISFLKQLIAGKLQESVPDPELIDLIYCGRKLKDDQTLDFYGIQPGSTVHVLRKSWPEPDQKPEPVDKVAAMREFRVLHTALHSSSSYREAVFKMLSNKESLDQIIVATPGLSSDPIALGVLQDKDLFSVFADPNMLDTLVPAHPALVNAIVLVLHSVAGSAPMPGTDSSSRSMPSSSYRDMPGGFLFEGLSDDEDDFHPNTRSTPSSSTPSSRPASLGYSGAAGPRPITQSELATALALASTPESSSHTPTPGTQGHSSGTSPMSSGVQSGTPITNDLFSQALQHALQASGQPSLQSQWQPQLQQLRDMGIQDDELSLRALQATGGDIQAALELIFAGGAP
Protein: Embryonic polyadenylate-binding protein A (Embryonic poly(A)-binding protein A) (ePAB-A) (ePABP-A) (XePABP-A) (Q98SP8)
Organism: Xenopus laevis (African clawed frog)
Function: Binds and protects the poly(A) tail of mRNA with or without an AU-rich element (ARE) and prevents mRNA deadenylation. Stimulates the translation of mRNAs to which it is bound during early development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11274061, ECO:0000269|PubMed:15713657}. Note=Associated with polysomes.
Interaction partners:
Sequence:
MNATGAGYPLASLYIGDLHPDVTEAMLYEKFSPAGPIMSIRVCRDIATRRSLSYAYINFQQPADAERALDTMNFEVIKGRPIRIMWSQRDPGLRKSGVGNVFIKNLDESIDNKALYDTFSAFGNILSCKVVCDEHGSRGYGFVHFETHEAANRAIQTMNGMLLNDRKVFVGHFKSRRERELEYGAKVMEFTNVYIKNFGEDMDDKRLREIFSAFGNTLSVKVMMDDSGRSRGFGFVNYGNHEEAQKAVSEMNGKEVNGRMIYVGRAQKRIERQSELKRKFEQIKQERINRYQGVNLYVKNLDDGIDDDRLRKEFLPYGTITSAKVMTEGGHSKGFGFVCFSSPEEATKAVTEMNGRIVSTKPLYVALAQRKEERKAILTNQYMQRLATMRAMPGPLLGSFQQPANYFLSAMPQPPNRTFYSPNPVAPVRPAPQWASHQSRPPQYQPPTPLMRAVQPRRMSSNISTMKQASTQVPRVAQHSQRVANIGTQTAGARAQVNPSMMRTMPHYKYSCGVRNVQPIVSSTHLQQVMEPAVLMQGQEPLTASLLAGAPPQEQKQMLGERIYPVIHEMHPTLAGKITGMLLEIDNSELLHMLESPESLHSKVEEAVAVLQAHQAKENAQKSAQPSLI
Protein: Transcription factor MYB28 (Myb-related protein 28) (AtMYB28) (Protein HIGH ALIPHATIC GLUCOSINOLATE 1) (Protein PRODUCTION OF METHIONINE-DERIVED GLUCOSINOLATE 1) (Q9SPG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Major regulator of short-chained aliphatic glucosinolates (GLSs) biosynthesis. Together with MYB29/HAG3 and MYB76/HAG2, promotes aliphatic glucosinolate biosynthesis but represses indolic glucosinolate biosynthesis. Prevents insect performance (e.g. lepidopteran insect Mamestra brassicae and Spodoptera exigua) by promoting glucosinolates.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:17521412}.
Interaction partners:
- Cytochrome P450 83A1
- Transcription factor MYC2
- Methylthioalkylmalate synthase 1, chloroplastic
- Methylthioalkylmalate synthase 3, chloroplastic
- Dihomomethionine N-hydroxylase
- S-alkyl-thiohydroximate lyase SUR1
- Cytosolic sulfotransferase 18
- Methionine aminotransferase BCAT4
- Probable inactive 2-oxoglutarate-dependent dioxygenase AOP2
- Cytosolic sulfotransferase 17
Sequence:
MSRKPCCVGEGLKKGAWTTEEDKKLISYIHDHGEGGWRDIPQKAGLKRCGKSCRLRWTNYLKPEIKRGEFSSEEEQIIIMLHASRGNKWSVIARHLPRRTDNEIKNYWNTHLKKRLMEQGIDPVTHKPLASSSNPTVDENLNSPNASSSDKQYSRSSSMPFLSRPPPSSCNMVSKVSELSSNDGTPIQGSSLSCKKRFKKSSSTSRLLNKVAAKATSIKDILSASMEGSLSATTISHASFFNGFTEQIRNEEDSSNTSLTNTLAEFDPFSPSSLYPEHEINATSDLNMDQDYDFSQFFEKFGGDNHNEENSMNDLLMSDVSQEVSSTSVDDQDNMVGNFEGWSNYLLDHTNFMYDTDSDSLEKHFI
Protein: Solute carrier family 52, riboflavin transporter, member 3 (Riboflavin transporter 2) (rRFT2) (Q4FZU9)
Organism: Rattus norvegicus (Rat)
Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19122205}; Multi-pass membrane protein {ECO:0000269|PubMed:19122205}.
Interaction partners:
Sequence:
MAFLTHLLVCVFGMGSWVAINGLWVELPLLVTKLPEGWYLPSYLTVVIQLANTGPLLVTLMHRFRPGCLSEVPVIFLILCVGTTACILLAFLWSMTSWIQGRQHSVAFIVLTFFLALVDCTSSVTFLPFMSQLPTYYLTTFFIGEGLSGLLPALVALVQGSGITTCVNVTETPGTTLNPVTTMETSITQRTLSPSLTPLTWHLESRYLAPRFSPLLFFLLLSFLMGCCLVAFFLLQRQPWGRQGSIEDLLHSQVTLHSIKPRDTEDTGSVGAPVSSPGKGSVEVSVASLRPAQLAFIYSVVAFVNALTNGVLPSVQTYSCLPYGPVAYHLSATLSSVASPLACFLPIFLPNRSLLFLGVLTVLGTGFGTYNMAMAAMSPCPILQGHWGGEVLIVLSWMLFVACLSYVKVMLGVILRDRSRSALLWCGAAVQLGSLIGALLMFPLVNVLKLFSSADYCSLDCSA
Protein: Transforming acidic coiled-coil protein D-TACC (Q9NJH5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MEFDDAENGLGMGFGGRGVLREINKNDGGIKLSPLAVKPSPKPTSMDQQKAMAAALGHQTAVPGGLKPEDDLVPKFGGLPEFDETQIPELAPLSTDMDTQLKSNHSDSDVFVECLSLHSERYTGDRSELEAYSSALNDVLEQQLSMTSVSTLGAEFNDPLAVSQHNNVSYEAMDVDDLNETMEMLKDVLNAEEPSSYANAYSQRTQSKPENNFVHYHPNQEQNRVELDQLAKHSKPNSDAKESESLVESVLSEESGTQSFEPKLTLSALDSTKDLAKHQEEMQTNTKDIFQKEKHHPVSSAQVKDAQNPKEPEKALNLKEASSELSTKSAKSLEYPNQEKQFSVAVESMERPCTAISLEQNASPAMEATEDRTVEELDQMDVDESMKVDDATVLNSCRQEQINAHSPVSSKFFLKLCVQNDTDCQDNKMDQKTAGKESALKMTEIELPVESVPSASLSPPTPALQAKMIELSLSPPIPTHRPKTAEELEFLALRELPLPDGVSTAGKVECKQLSHGLVPIVAVLPTPLYLDLKGNTTTASLPEPTSPSFPIKEPAEKQSHFPRSPRAQLEQKDMPYLEEAVVERSSHRKQSDFGVIAKSPIVFELTQPSPEKQHLNETLPMSEISPTSSNMTFYSGSITEDKSQKGTENIEPSSTLAVSLGSVDDKQRRTFSVVQPTKEEEEAKSRRTFCMENENPRRTFCMQQNASPAVEATEDTGADEVMDVDISMRADEVAVMKSHQQTWKERQAPISNSPPIPTHQRLNRPPEAISPVSPLGNGTVVLEEQTLSAKEQATLSASDEKDDVFLEHFGAISPVSDDMFKTSSASNNQAKFRVNADEETGGKGASAMIRKRSGTAGEQEEIFDAEFHDGVNNQNLILNSSDFDYLYTKGSNSVPIDRSSLLLKFDPLLGAPVPVNHPNQQEQALQNILGSNQHQNRLLSPTLEEHETSDGNQSFGVISSAKDTAKKWDFKPPVDRTKHVKMSVDVIDNDCNKTFDNSNTNTEDKTHNYNDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKKLDTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELIYGKGQGGSS
Protein: Extender of the chronological lifespan protein 2 (C6Y4C5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in chronological cell aging.
Subcellular location: Nucleus {ECO:0000269|PubMed:19352039}.
Interaction partners:
- Extender of the chronological lifespan protein ecl3
Sequence:
MDLDYCIICGKPTTGNLYCSRECHLQDCPGCGSTSEQCSYSKSADLHMLSSQYLDHFRRRSSMPSPSTSSSLLNGFVASRLAVL
Protein: Protein Wnt-10a (P43446)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Required for normal tooth development. Regulates the expression of genes involved in tooth development.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9GZT5}. Secreted {ECO:0000250|UniProtKB:Q9GZT5}.
Interaction partners:
- Frizzled class receptor 1
- Wnt inhibitory factor 1
- Frizzled-4
- Frizzled-5
- Frizzled class receptor 2
- Secreted frizzled-related protein 1
- Frizzled class receptor 6
- Secreted frizzled-related protein 2
- Low density lipoprotein receptor-related protein 5
- Secreted frizzled-related protein 5.
Sequence:
MSSHDISWHSPASVYFSSDLDVKRIAGKLRGCWTDLLLRQESCCERVLQKSSSSMDYFLFRLFCSLALASLLVQRADSNEILGLKIPFDPILNANTVCLTLPGLTKKQLDVCMRNPDVTASAIQGIQIAIHECQHQFRGHRWNCSSLETRNKIPYESVVFSRGFRESAFAYAIAAAGVVHAVSNACAMGKLKACGCDEKRRGDEEALRIKLNRLQLEAINRGKGMVHGVMEHFPAEALGPQDSWEWGGCSPNVEYGERFSKDFLDSRETYRDIHSRMRLHNNRVGRQVVVDHMRRKCKCHGTSGSCQLKTCWQVTPEFRTVGSLLKERLNVATLIKAHNRNTGQVENAHHTHRRRANINDLVYFEKSPDFCERDLGSDSAGTQGRICNKTSQGMDNCESLCCGRGHNILQQTRSERCNCKFHWCCYVVCEECRITEWVSVCK
Protein: Eukaryotic translation initiation factor 4 gamma 1 (C9JWW9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGE
Protein: Midnolin homolog (Protein stuxnet) (Q8SXD4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Facilitates ubiquitin-independent proteasomal degradation of polycomb protein Pc by interacting directly with the proteasome and recruiting Pc to it.
Subcellular location: Nucleus {ECO:0000269|PubMed:27326929}.
Interaction partners:
Sequence:
MDKSAATNSATADGQNEAAAAAAAAATAAGCGSNNSSSTSSSNNTANSNNALQRLATTTSAVVASPMTINLNISTTTGGNFGVSVEPHISVESLKKIIAKKLKVAKDRICLLHREKELQDGTLRDHNLMDGSKIILIPNVETGLLAQRPENTVMQALESLNDAQVNDFLSGKTPLNLSMRLGDHMMLIQLQLSTVNPAGGGAATVAPVAGGASGSSINAAASTTSTVPVMPAGTGCSGANSTSLSSSAVLAAAAAGVGGSTGTSGSGTSSSSSSTSSSSSSSSSSSRTRSSGQRSSGRIGHGHVHSHQHPSLHAANWHGFSHGHGHGHSHGNGHGHHHHHHHHHHHHHHHHNASAVAAGSGGGMSSLRKMYGDLPSSSGASGSAPATGTGQSQSSSTLNGPDLTKLLIKGGIQNIVNSFALKDAGANARPVANGGSGSSPGKPVLEQSPIKSLSNLVSSPIKMTTIKNIPLPTTAATSSSSSCNCSSAAPSSSSSTSSGACATGGCQQDPIAAKLTSCLCTRLPTPSVAPPVATLVAPAPVARSGSTSSPSKCPESSCSGANAGFAARSTLAGTRVTFSGNSMLHKTGNNRITRTKHRHYHGQGHGHGHGNGHSSSSSSSSSSSSSHFFNHACAGNQPSVNAAAFATSSSSSSSSPSSSSSSPSKRRKLEQGMGAGAVGATAATATAAATVALPASTSATTAEPDDSLLGVSDTRTLAEASRNLTQTLRKLSKEVFTNKIDLSGAGVVSSGRSSSSGATSSGAASGEEAPRKSGSGAVIESMKNHGKGIYSGTFSGTLNPALQDRFGRPKRDISTVIHILNDLLSATPQYGRGARISFEAPTTGSVSGSGSGSGSSGSSSTTSSGSGLHHGSRSKMYSSKHHNCAKCNSRAQQQQQQSATLASGSGGSCSFRDCPSYHSSSAATKASTSSKSSSHSCCQTAEAPSSMTSQSNGCTCRYRRDDGQGEREREHTCQKCTVELANMKTRSKMDQLRLVMQQHKQKREARKLKSGPYATAASASAADSLSSIAAGGTAAVPMGAAAQYSAVSALVATPLQPAAVPVQTGKAAPANSITGNSSNANVNGNTSTAPATAATSAAAAPTAAPPSEVSPNHIVEEVDTAA
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (F1LUT4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
- Cell cycle control protein 50A
- ATPase phospholipid transporting 8A1
- Cell cycle control protein
- Phospholipid-transporting ATPase
- Phospholipid-transporting ATPase
- Phospholipid-transporting ATPase
- Phospholipid-transporting ATPase
- Phospholipid-transporting ATPase
- Phospholipid-transporting ATPase
- Phospholipid-transporting ATPase
Sequence:
MAFWDLLAGSEPQAMCYIETSNLDGETNLKIRQGLPATSDIKDIDSLMRISGRIECESPNRHLYDFVGNIRLDGHGTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILILFCILIAMSLVCSVGSAIWNRRHSGKDWYLHLHYGGASNFGLNFLTFIILFNNLIPISLLVTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQFKKCTIAGVAYGQSSQFGDEKTFNDPSLLENLQNNHPTAPIICEFLTMMAVCHTAVPERDGEKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEERYELLNVLEFTSSRKRMSVVVRTPSGKLRLYCKGADTVIYERLAESSKYKEITLKHLEQFATEGLRTLCFAVAEISESDFEEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIEDKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCRLLRRNMGMIVINEGSLDGTRETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQKSEVVEMVKKQVKVITLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYLKNLLMVHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMFTAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPLKALQYGTVFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVVFFGIYSSLWPAVPMAPDMSGEAAMLFSSGVFWVGLLSIPVASLLLDVLYKVIKRTAFKTLVDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQDENGIVSQSEVIRAYDTTKQRPDEW
Protein: DnaJ homolog subfamily B member 6 (Heat shock protein J2) (HSJ-2) (MRJ) (mDj4) (O54946)
Organism: Mus musculus (Mouse)
Function: Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Also reduces cellular toxicity and caspase-3 activity (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1B
- Heat shock 70 kDa protein 4
- Stress-70 protein, mitochondrial
- Heat shock 70 kDa protein 14
- Heat shock 70 kDa protein 1A
- BAG family molecular chaperone regulator 3
- Endoplasmic reticulum chaperone BiP
- Heat shock-related 70 kDa protein 2
- Schlafen family member 1
Sequence:
MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGIHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGNRSRGAGSFFSTFSGFPSFGSGFPAFDTGFTPFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALAEECQRRGQPTPALAPGPAPAPVRVPSQARPLAPTPAPTPAPTPAPAPAQTPAPSVSTRPQKPPRPAPTAKLGSKSNWEDDEQDRQRVPGNWDAPMTSAGLKEGGKRKKQKQKEDLKKKKSTKGNH
Protein: Extra-large guanine nucleotide-binding protein 1 (Extra-large GTP-binding protein 1) (Extra-large G-protein 1) (O80462)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (By similarity). Binds GTP with specificity. Plays a role in the root morphogenesis by regulation of the cell proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:17999646}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- Guanine nucleotide-binding protein subunit gamma 2
- Guanine nucleotide-binding protein subunit gamma 1
- Guanine nucleotide-binding protein subunit gamma 3
- AUGMIN subunit 6
- Regulator of G-protein signaling 1
- SKU5 similar 16
- U-box domain-containing protein 2
- Protein RALF-like 1
- Ubiquitin carboxyl-terminal hydrolase 3
Sequence:
MPLKEDDCCLFAEEYDGPPLSYNIPCAVPINVEKIPVAAVVSPVCISDNMSFPVIQPILSVESKKFLIDSVSPTSVIANCGSNQLELVSDSITVSPTSVIEHTEEEEEEEGGDGEDCELSSSGELLLRSCSVKESLDLNESSSNPLVPDWESNESVLSMDYPSSRVTGDCVSETNGDGKKQPVVTFLGIASDDGFEEEESCSNLRRVRVVPVKKQPQTKGKKGSCYRCFKGSRFTEKEVCLVCDAKYCNSCVLRAMGSMPEGRKCVTCIGFPIDESKRGSLGKCSRMLKRLLNDLEVKQIMKTERFCEANQLPAEYVYVNGQPLYPEELVTLQTCSNPPKKLKPGDYWYDKVSGLWGKEGEKPYQIISPHLNVGGPISPEASNGNTQVFINGREITKVELRMLQLAGVQCAGNPHFWVNEDGSYQEEGQKNTKGYIWGKAGTKLLCAVLSLPVPSKSTANASGEQLYSANSRSILDHLEHRTLQKILLVGNSGSGTSTIFKQAKILYKDVPFLEDERENIKVIIQTNVYGYLGMLLEGRERFEEEALALRNTKQCVLENIPADEGDAKSNDKTVTMYSIGPRLKAFSDWLLKTMAAGNLGVIFPAASREYAPLVEELWRDAAIQATYKRRSELGLLPSVASYFLERAIDVLTPDYEPSDLDILYAEGVTSSSGLACLDFSFPQTASEENLDPSDHHDSLLRYQLIRVPSRGLGENCKWIDMFEDVGMVVFVVSMSDYDQVSEDGTNKMLLTKKLFESIITHPIFENMDFLLILNKYDLLEEKVERVPLARCEWFQDFNPVVSRHRGSNNGNPTLGQLAFHFMAVKFKRFYSSLTGKKLFVSSSKSLDPNSVDSSLKLAMEILKWSEERTNICMSEYSMYSTEPSSFSN
Protein: G1/S-specific cyclin-E1 (P47794)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Essential for the control of the cell cycle at the G1/S (start) transition.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P24864}.
Interaction partners:
- cyclin-dependent kinase
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase inhibitor 1C
- Cyclin-dependent kinase inhibitor 1B
- Retinoblastoma 1.
- S-phase kinase-associated protein 1
- Cyclin-dependent kinase inhibitor 1B
- Retinoblastoma-like protein 2
- S-phase kinase-associated protein 2
- Retinoblastoma-like 1
Sequence:
MPSKKVLQTEHINTTDEAPKTTSVRPRKRKADVAIHLQDPDEEVTEMTRKKQCASQACWNPDTGYTSPCRRIPTPDEVEEPVAFGSVGFTQYASESIFITPTRSTPLPALCWASKDEVWNNLLGKDKLYLRDTRVMERHPNLQPKMRAILLDWLMEVCEVYKLHRETFYLGQDYFDRFMATQENVLKTTLQLIGISCLFIAAKMEEIYPPKVHQFAYVTDGACTEDDILSMEIIIMKELNWSLSPLTPVAWLNIYMQMAYLKETAEVLTAQYPQATFVQIAELLDLCILDVRSLEFSYSLLAASALFHFSSLELVIKVSGLKWCDLEECVRWMVPFAMSIREAGSSALKTFKGIAADDMHNIQTHVPYLEWLGKVHSYQLVDIESSQRSPVPTGVLTPPPSSEKPESTIS
Protein: Ras-related protein Rab-5A (EC 3.6.5.2) (O96193)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- GDP dissociation inhibitor, putative
- Vacuolar protein sorting-associated protein 9, putative
Sequence:
MEKKSSYKTVLLGESSVGKSSIVLRLTKDTFHENTNTTIGASFCTYVVNLNDINIKNNSNNEKNNNINSINDDNNVIITNQHNNYNENLCNIKFDIWDTAGQERYASIVPLYYRGATCAIVVFDISNSNTLDRAKTWVNQLKISSNYIIILVANKIDKNKFQVDILEVQKYAQDNNLLFIQTSAKTGTNIKNIFYMLAEEIYKNIINNNNTSKNKTVNKNLINLDNQTLSKKGCC
Protein: Arginine--tRNA ligase, mitochondrial (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) (P38714)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Lysine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, mitochondrial
- Glutamine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, mitochondrial
- Serine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, mitochondrial
Sequence:
MFGIVYLKNRSLLCKNPFSSYPRYGFMPSFDTQFSNQFRKLEINIGRKRYSSKTLNTKYTDQPEGPIYPLDVLRLDISKALHDISGIDHSLILNALESTNSMDRGDLLLPLPKIKVADPVAVANRWAIELSTHGCIGKVCAKGPFLQFFLDQRYLIQSTVPNILLQKGKYGQKKSRHQKKVVVEFSSPNIAKPFHAGHLRSTIIGGFLSNLYEAMGWSVTRMNYLGDWGRQFGLLAVGFKRYGDEKTLQKQPIQHLFDVYVKINMDLAKEEINGNSKCGISGEARSFFKNLENGDENAIKIWNRFRSLSIHHYIQTYSRLNINFDIFSGESQVSKESMNEALDIFRKNNLVKEIDGALVIDLTQWSKRLGRVVVQKSDGTTLYLTRDVGAAIERKKNLHFDKMVYVISSQQDLYMSQFFMILKKMNFEWAKDLQHINFGMVQGMSTRKGNVVFLDTILDEARDKALQIMENNKMKISQVDNPQRVADLIGVSAIIIQDMKSKRINNYEFNWNRMLSFEGDTGPYLQYTHSRLRSLERTSSDFTTDMLIHADFSNLNEPQLVELVRLLAQYPDVLRRAFETQEPATIVTYLFKVCHQVSSCYKKIWVSGKPADIAIPRLAVYSASRQVLHNAMSLLGLVPVDRM
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC2 (RNA polymerases I, II, and III subunit ABC2) (DNA-directed RNA polymerase II subunit F) (DNA-directed RNA polymerases I, II, and III 14.4 kDa polypeptide) (RPABC14.4) (RPB14.4) (RPB6 homolog) (RPC15) (P61218)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:9852112}. Nucleus, nucleolus {ECO:0000305|PubMed:34887565, ECO:0000305|PubMed:36271492}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC10
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase I subunit RPA1
Sequence:
MSDNEDNFDGDDFDDVEEDEGLDDLENAEEEGQENVEILPSGERPQANQKRITTPYMTKYERARVLGTRALQIAMCAPVMVELEGETDPLLIAMKELKARKIPIIIRRYLPDGSYEDWGVDELIITD
Protein: DISCO interacting protein 1, isoform H (Disco-interacting protein) (DsRBD-containing protein dip1-a) (Q9TW12)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPVIIKEEPISVNDEPSVDNIEDNTSASTSASGIGGKIPFKKIFQKRKKSSERTRDKKLRQNRQLRKSMLPKNALMALNEVKGVTISDFTIDSNTDGGFTAVVTVNSNQYEGKGTSKMTAKNAACEKAWRDFIIAKMTPKPPRIHQVEMGSEPMDINEDEADAPDDDLPMLNLASFAIYKLFAEWEREGYVVPEMHPSANAAQQAGGDAGTPVPPVPKEPKKPPVRTELPSGWETMHPATILCIMRPGLNYVDYGSSGDKTNGMQHLGIMVDNQEFHANGRSKKIARRNVAVKVCNSLFGTNFTYSDTT
Protein: Wax ester synthase/diacylglycerol acyltransferase 7 (WS/DGAT 7) (Diacylglycerol O-acyltransferase WSD7) (EC 2.3.1.20) (Long-chain-alcohol O-fatty-acyltransferase WSD7) (EC 2.3.1.75) (Q94CK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional wax ester synthase/diacylglycerol acyltransferase that uses acyl-CoAs with 14, 16 and 18 carbons as substrates, preferably in combination with 16:0ol alcohol. Involved in cuticular wax biosynthesis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q5KS41}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:30729606}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:30729606}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Fatty alcohol:caffeoyl-CoA acyltransferase
- 3-ketoacyl-CoA synthase 8
Sequence:
MTYGEEEPVSPMARVFQSPGIDLCAVTIMGFKTKINPDVVLDALKQNVSKHPRFSSILSDNGAKWIETEVNVEDHVIVPYIDAEEIGEGGQSFIDDYMSRLTMIPLDRSRPLWDIHILNVKTSEAEAVGFIRSHHSLGDGMSLISLMLACTHKTSDPDMFSNAIPSMKRRATMSHSLKTKGWFLRSIFTIGSTMRLLWNTTIDMLLLLATVLFLKDTKTPLKAGADVRSNPKRFYHRIISLDDIKLIKNAMNMTINDVLFGITQASLSHYLNRQYGTKKEEDGALTSYRNNLPDGIRFRVACTVNLRSDIGFKPLADMMVKDSKCRWGNYFSFIFLPFTIGLQTDPLVYLKMSKSMMARKKHSYHAALVYFIIKIVLKVFGAKAAAELFDRPVRNTTTCVSNVIGPMEEISFRGHPVSYIAPSSYGHSHALLIHLMSYADKMIISLAYDPTVISDPHKICDDMEESLKAMKASLCERGLL
Protein: Interleukin-4 (IL-4) (B-cell IGG differentiation factor) (B-cell growth factor 1) (B-cell stimulatory factor 1) (BSF-1) (Lymphocyte stimulatory factor 1) (P20096)
Organism: Rattus norvegicus (Rat)
Function: Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-4 receptor subunit alpha
- Interleukin-2
- Interleukin-13 receptor subunit alpha-1
- Interleukin 2 receptor, gamma, isoform CRA_a.
- Signal transducer and activator of transcription
- Tyrosine-protein kinase
- Tyrosine-protein kinase JAK3
- Interleukin-7
- Interleukin 9
- T-cell surface glycoprotein CD4
Sequence:
MGLSPHLAVTLFCFLICTGNGIHGCNDSPLREIINTLNQVTEKGTPCTEMFVPDVLTATRNTTENELICRASRVLRKFYFPRDVPPCLKNKSGVLGELRKLCRGVSGLNSLRSCTVNESTLTTLKDFLESLKSILRGKYLQSCTSMS
Protein: Phospholipase Culp4 (EC 3.1.1.-) (Cutinase-like protein 4) (Culp4) (O06319)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A2-type phospholipase, which is probably involved in the degradation of macrophage membrane. Hydrolyzes dipalmitoylphosphatidylcholine. Also shows moderate esterase activity and hydrolyzes the p-nitrophenol-linked aliphatic ester pNP-butyrate (C4). Does not exhibit cutinase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17416658}. Secreted, cell wall {ECO:0000269|PubMed:17416658}.
Interaction partners:
- Carboxylesterase/lipase Culp6
- Esterase LipI
- Carboxylesterase NlhH
- Carboxylesterase B
- Carboxylic ester hydrolase LipN
- Probable carboxylesterase Culp3
Sequence:
MIPRPQPHSGRWRAGAARRLTSLVAAAFAAATLLLTPALAPPASAGCPDAEVVFARGTGEPPGLGRVGQAFVSSLRQQTNKSIGTYGVNYPANGDFLAAADGANDASDHIQQMASACRATRLVLGGYSQGAAVIDIVTAAPLPGLGFTQPLPPAADDHIAAIALFGNPSGRAGGLMSALTPQFGSKTINLCNNGDPICSDGNRWRAHLGYVPGMTNQAARFVASRI
Protein: Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase (EC 2.4.3.8) (Alpha-2,8-sialyltransferase 8A) (Ganglioside GD3 synthase) (Sialyltransferase 8A) (Sialyltransferase St8Sia I) (G3V7T2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
- Lactosylceramide alpha-2,3-sialyltransferase
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- Type 2 lactosamine alpha-2,3-sialyltransferase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Beta-hexosaminidase subunit alpha
- ST3 beta-galactoside alpha-2,3-sialyltransferase 1
- Alpha-
- Acetyl-coenzyme A transporter 1
- Alpha-
Sequence:
MSPCGRALHTSRGAMAMLARKFPRTRLPVGASALCVVVLCWLYVFPVYRLPNEKEIVQGVLAQRTAWRRNQTSARLFRKQMEDCCNPAHLFAMTKVNSPMGKSLWYDGEFLYSLTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKMSGCGRQIDEANFVMRCNLPPLSSEYTRDVGSKTQLVTANPSIIRQRFENLLWSRKKFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLKDAGANQTVLFANPNFLRNIGKFWKGRGIHAKRLSTGLFLVSAALGLCEEVSIYGFWPFSVNMQGEPISHHYYDNVLPFSGFHAMPEEFLQLWYLHKMGALRMQLDPCEEPSPPQPTS