wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein (Q57VV6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- T. brucei spp.-specific protein
- Uncharacterized protein
- EF-hand domain-containing protein
Sequence:
MEGQKYDWANAHARLWTSFKKSQESNDTPTARGDIRMHSSPTAPSVHLRNSAAVRDITTAVLAEAMGRGKADEPVFTEELEARIVWLLENEGVDSPMRDLLGAIMHLKKRIEMRGGEVAITSSRVADIVGETLYHLTGRKVSGHVNEGASTGKDFDDVNESPFLKVLMQVEKCKKTARKLAERNGICKSYDSESSLGEILDMMSSCRPCAVERTIDEDNKETLRQVMDILGASPGVPVGQAPSLTLKLTKDLEFARRDVHTCSALLHQYEKAAMSRFSSCGVVSPPTVEQERAILLSDRPNVSVSSNDQWIEREFKDVISIMTQVNQRFHLNIVPNHLRGWPTSSSAEVVFDHMRTSLESARDMIAALAEREQEVRSKLAEITRKLRHSDDRSASECSDDRFSRKLSDDTVVSGHSTAIEMAQHLGLLVDHQLKKEENVNQESLQGYRKKMREILMRILRWLPDGDGSSQGDTDPTCLSPTKAPQDEDALAGYVESVVQRFAAQSNVPDTLVPHIRELCTNVSQLADSLACGNVQCIDDSTMTTLLSTVDQLRRWVLGERCDTRSSADNALIQQCLCELAQLLPTGTSPSSCEGAVEIEPPVNNLLEMVQLLKRRQEQWVQEQHKHQASGANSRMEKARLEEIVREGGKQLVKRCKEILLISANSVEAEAVINALSDELTDDVPAVKDCAVDAAPGNNQGSTGAHSITLATTVFRDLDERMKLIKTRYHRLQHAYEANKVRLDNLIQSNIPRGKRWARICNTVGALCRAVGVEELAFRLEHDGRPESLQSPSAPTASASNTTSPAAVASAFKQTLRADLTKSDAGQSVTDGELLEALKLVESRLKDNTALCDRVSQQSRLLLLQEERKQWREEVVTFRQAIQVILQRLAEAGQRIKRSLYLLGTDECAEDDVVETVLREQECRDDDKSRLKQRQDEGDGGDPDSEWNGADEERLQKQQEVNEEALAVLLRKFGRWATRLHETTEDHLHTQKKLVKYFAAVHRFFCNANVAPPNLDSCTEALLDIDTTLMHFADGILPVLDRAIDAAQSKRKKRTGVTSCGNKALLNILNSGKSSADTGDSEACRTVTGEKDDADARNEVMSLLLQNAPADRILPADHRITRLYEMVGKLRTMVSGLLSVRYLAIPVAVGNRGSGGNSDELVFADGFGDDDYIELDLNTLRAVGGKGSKEGTAGIEGDHNSGSGAAANIESKGSDGATYVSDEKLLRIVESNVTAVYQALAKFSTDYKLAAILLQKDTESMQHFIAEMLKYYIELDVKRGFGQDPEMLRELYILIHERAKRQRGCYFFSRVGGEGPCVWSAALEQLSSGFIGILEKLHKRTETAAELRELVDDVVDICAMYVNWVDTTGATITSLHPLPEDVLTACIRQDVVAEEEVMSVVEGNQLQPHGNQSCDRCSDARDELEVEDVRDSGEEVPKPPLPPGHSRPKVSHFKKDDIVLKVIAHMFQVAQEVLSLSGSNSERTQQLEEQLQLLRESVAVAEQGRDKALSEAAVSRAELRRWRRQHHVPDDQLQPPPPLPIVQQHQQEKRPSGLERPVSPSPVTTITIDDEGIHPGVGRAPPPSAVAPGRDDALLHVAEVMKELTDELRGVCGRRGSDISYPPVATVLDSTSKTLTASEGSRRRVMMDTESDFYSGASVSTAAFQRGLATRGSTAGAPLVREQKGNAMQYGKSSPSFAPPTTPPRSGNKELSPMGEMSASPPSFQPPSQGLQIQQRPQGIIQSYDEGRHSPAARDTVVLASGGTKYTTRAPSTQHYRSHSEGVNAHERDVSTRQRHAGRSRGGAVSDMVGGLQTKSDGRRTTSATRAPVTRTPPSLSAALRGQSPQANPRTPVRVAASPSSLSSANAAAPTAAAPIRRSSPHSRKYRDGMEELMDGLYANYHAYHDCVCGNQPKGHHGSGVLKSTNRPAAVVASRQRARNRKPGTTGDRYCENVKRSPGGSLSVRTTVSGKSYAAGGGQARPRSSNEEDYTLHMSSLHNTGSSIVISPDSTAAYPDVGDTDASRRGRDRRQIGNEAQGLFFRGLEREESLRGPARPVISGTRSPSRARDGGGLRGILKQQHHQRQSTVTPTRRVSSLGYGVNDYAHGANSKQLLDVVARTKVGKRDEF
Protein: RanBP2-type domain-containing protein (P91457)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear pore complex protein Nup85
- Nuclear Pore complex Protein
- Nuclear pore protein
- Nuclear pore complex protein 5
- mRNA export factor rae-1
- Nuclear pore complex protein 14
- Nucleoporin NUP35
- Nuclear Pore complex Protein
- Nuclear pore complex protein Nup98-Nup96
- Nucleoporin Nup54 alpha-helical domain-containing protein
Sequence:
MSDKSGGFFSSVGRFFSVGASATKSKDGDKSNDEGTSNSSSKSSPSASPALKNILSVDNEAKIASDETSVNTSQNHRIGSRLRYLSPTALDRRTSASNGLEIDVDAVPDIFFSTPAVSTNRKRQLTELDKQILPQSFRSESVKRSRFLNRSLLEPTLNSSMNNERKMDMTWCGELTANHSPASSITNFSLLSRRSGATTNGSLSTRTQEIFKKLEGANTPAKEVQRMSMLRAGIARPEKWGSFSESKVPNGSATGTPPPPLKKAGDAIPSRIQLISKTMGMSARRAPYWTDLTRKRTSSKNGDTGSSDSMKSLNGNFATAELSSLFSLDLPAPKKTASTASTTTINSSNSRKQHASIMKGPDGKPVSRNTFKLSDDIEEVDEDSQKLPPIPTTTLQNPQPLKLAPEYAPKRGFLDDLAFSFTAPVDLVTAVGTAKTASTASSHKASESSSESNAESTEKQTSESSGNESDSEESEDSEVDVGEENGSEVKESRPQTSADTISSAGGSNQSSKDSSPKVAKDAEPVVVAPAPVVDAGSKKWECQSCFCSWDSTLSECGACGEARPGGSGTGPKSQPKPSEKQLVSNLSSFASNTPSTVKFGFGSGASTTTTIASTTSNTIPFGSGSSVAPLFGAPKTTAPPPTTVPATIPVAPTTIASAPVAAVTSSSNGTRVDWECPDCMVSNKASDDKCPCCSHVKYASAEASSNVFGNRAFKPLSSTGSTISFGVGGSTATTQPSAFAFGLSKTTEVAPTSTPAFGLSAKPAVSSAPVEKPSAPEVPKTAGSLFGNIAKPADSATTSFLAPGAASSTSSLAPTAGSSLFGGSTGSIFNLNKTNTTETAKPGLFGSILDKETHVTTTPVSVALPSSTDSTQSKSAIPTIAPTMSLFGNSSTGSFGGSSMFGNSKTELPKISSTLSFGNPTTAAAPVSTATAEAVKTNVFGSNSASASTSLFGAGSSSTATNLFTTKPADSTTSSIFGKPISFGDDSGTTTTDGAPAKRGLFSSDSQKLQFGGQQKVEMPKFTGFGNPASTASTTSGSLFGGASTNPPMFGGPSSSSIPAFSTSNSSSTSGFPSSTATPFGNAGTTSTSGVFGAFGNKPSQPGLSSSSSTNSLFGQAPADSSNPFGGTSNNGFNFGASSSTTGATAGGGGVFQFGNAATSAPAPTAAPGGGAFQFGGNMSVPQAPAPGGMENAFSYQAPSGVGARKMAMARRRNMRK
Protein: Fasciclin-like arabinogalactan protein 2 (Q9SU13)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a cell surface adhesion protein.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Fasciclin-like arabinogalactan protein 15
- Putative fasciclin-like arabinogalactan protein 20
- Probable methyltransferase PMT3
- Fasciclin-like arabinogalactan protein 21
- Fasciclin-like arabinogalactan protein 18
- Fasciclin-like arabinogalactan protein 19
- Classical arabinogalactan protein 9
- Non-classical arabinogalactan protein 30
Sequence:
MAYLRRAATALVLIFQLHLFLSLSNAHNITRILAKDPDFSTFNHYLSATHLADEINRRQTITVLAVDNSAMSSILSNGYSLYQIRNILSLHVLVDYFGTKKLHQITDGSTSTASMFQSTGSATGTSGYINITDIKGGKVAFGVQDDDSKLTAHYVKSVFEKPYNISVLHISQVLTSPEAEAPTASPSDLILTTILEKQGCKAFSDILKSTGADKTFQDTVDGGLTVFCPSDSAVGKFMPKFKSLSPANKTALVLYHGMPVYQSLQMLRSGNGAVNTLATEGNNKFDFTVQNDGEDVTLETDVVTAKVMGTLKDQEPLIVYKIDKVLLPREIYKAVKTSAPAPKSSKKKPKNAEADADGPSADAPSDDDVEVADDKNGAVSAMITRTSNVVTAIVGLCFGVWLM
Protein: Chaperone protein DNAJ, putative (Q381S2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MADLYDVLGILHDAEDDAIAKAYRRHSMAVNPQCNPDHPDPAALEKQFKHVSQAYVVLSNPKARGIYDLYGEEGVRHGGTGAQGIPGGIDLDAIDPYAVFRSFFGVDNPFQVIGEINGLRNNRHNFFSSTAVIPKSLVKAPSIEVQLPVTLEDVYYGAVRRASWKCSFVRQGNETVVEEFFELRVPKGAHAGDKFVVDGKGDWEEGRARGDVVVVLELLPHERFRREGDDLVVRVPITLREALCGVTLTVQTMEGTDVAVLIDEIVHPKYSRRVVGQGLPRNDEPSNPRGDLIVECDTTFPGFLTLEQKSELSRILDAK
Protein: BLOC-1-related complex subunit 5 (O01902)
Organism: Caenorhabditis elegans
Subcellular location: Lysosome membrane {ECO:0000256|ARBA:ARBA00004122}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004122}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004122}.
Interaction partners:
- BLOC-1-related complex subunit 7
- BLOC-1-related complex subunit 8 homolog
- KxDL domain-containing protein
- SNAPIN protein homolog
- Single-stranded DNA-binding protein homolog sam-10
- BLOC-1-related complex subunit 6 C-terminal helix domain-containing protein
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- ADP-ribosylation factor-like protein 8B
- Yip1 domain-containing protein
- BED-type domain-containing protein
Sequence:
MGNEQSSSTAGTSSNPQNQQSSFSFLTRASTKRSKGIITVKDGNIPQEKLEDDEIYKRFTEIPRFLPVIPAVIGKRDPQTNQGASYTHQKISSRPFFRLATRLQEHFAVNAKAVAADQAKIPATCKSVEAKMIRLIEETRAHKEQHDGFMAALSGLNQLHDDICSIQIILEDIVPMVETLNEILTPDERLPPLNLGSVLDRSPVPSSDSSLQSTPRHNQNIGHIDQIEPIEEIRVVDLPK
Protein: DBIRD complex subunit ZNF326 (Zinc finger protein 326) (Zinc finger protein interacting with mRNPs and DBC1) (Q5BKZ1)
Organism: Homo sapiens (Human)
Function: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro.
Subcellular location: Nucleus matrix {ECO:0000250}.
Interaction partners:
- Cell cycle and apoptosis regulator protein 2
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein H
- Matrin-3
- Heterogeneous nuclear ribonucleoproteins C1/C2
Sequence:
MDFEDDYTHSACRNTYQGFNGMDRDYGPGSYGGMDRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGGGSRFGPYESYDSRSSLGGRDLYRSGYGFNEPEQSRFGGSYGGRFESSYRNSLDSFGGRNQGGSSWEAPYSRSKLRPGFMEDRGRENYSSYSSFSSPHMKPAPVGSRGRGTPAYPESTFGSRNYDAFGGPSTGRGRGRGHMGDFGSIHRPGIVVDYQNKSTNVTVAAARGIKRKMMQPFNKPSGTFIKKPKLAKPMEKISLSKSPTKTDPKNEEEEKRRIEARREKQRRRREKNSEKYGDGYRMAFTCSFCKFRTFEEKDIELHLESSSHQETLDHIQKQTKFDKVVMEFLHECMVNKFKKTSIRKQQTNNQTEVVKIIEKDVMEGVTVDDHMMKVETVHCSACSVYIPALHSSVQQHLKSPDHIKGKQAYKEQIKRESVLTATSILNNPIVKARYERFVKGENPFEIQDHSQDQQIEGDEEDEEKIDEPIEEEEDEDEEEEAEEVGEVEEVEEVEEVREGGIEGEGNIQGVGEGGEVGVVGEVEGVGEVEEVEELEEETAKEEPADFPVEQPEEN
Protein: Inducible T cell costimulator ligand (Inducible T-cell co-stimulator ligand, isoform CRA_b) (K4DIA0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MRLGSPGLLFLLFSSLRADTQEKEVRAMVGSDVELSCACPEGSRFDLNDVYVYWQTSESKTVVTYHIPQNSSLENVDSRYRNRALMSPAGMLRGDFSLRLFNVTPQDEQKFHCLVLSQSLGFQEVLSVEVTLHVAANFSVPVVSAPHSPSQDELTFTCTSINGYPRPNVYWINKTDNSLLDQALQNDTVFLNMRGLYDVVSVLRIARTPSVNIGCCIENVLLQQNLTVGSQTGNDIGERDKITENPVSTGEKNAATWSILAVLCLLVVVAVAIGWVCRDRCLQHSYAGAWAVSPETELTGEFAVGSSRFWGAQGRLGCQLSFRVSKNFQKAKVPCLEQLLFLETQRSPRWCAWHFLQPPLGMGWHPGVHFVTLRWDFPNMHRSRETSARPPRSPVPSPDQGVQGGSRHRRPAPMGCPEWVQAPAPSPRGVSRAGPGTGAQPLWGVRSGSGHRQLLSVAATPAALVCPSVPGAT
Protein: Olfactory receptor 8D1 (OST004) (Olfactory receptor 8D3) (Olfactory receptor OR11-301) (Olfactory receptor-like protein JCG9) (Q8WZ84)
Organism: Homo sapiens (Human)
Function: Odorant receptor (Potential). May be involved in taste perception.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Olfactory receptor 8D2
Sequence:
MTMENYSMAAQFVLDGLTQQAELQLPLFLLFLGIYVVTVVGNLGMILLIAVSPLLHTPMYYFLSSLSFVDFCYSSVITPKMLVNFLGKKNTILYSECMVQLFFFVVFVVAEGYLLTAMAYDRYVAICSPLLYNAIMSSWVCSLLVLAAFFLGFLSALTHTSAMMKLSFCKSHIINHYFCDVLPLLNLSCSNTHLNELLLFIIAGFNTLVPTLAVAVSYAFILYSILHIRSSEGRSKAFGTCSSHLMAVVIFFGSITFMYFKPPSSNSLDQEKVSSVFYTTVIPMLNPLIYSLRNKDVKKALRKVLVGK
Protein: Alhambra, isoform J (A8JQU6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMMMDTMDTSQSQPMDVAPAVAVAATSGAALVDFTAAMVSMAATAEAESAESNNNHIDMAEYKEHRKNKKKKREKREREGKEHRHHKHRDREHREHRRHRDRDRDKERDREGHHHHPTHHHPNNSQHSTSASSSPSSASTTPSATIEYVGGSASASPSYLGGGATGTGAAVGATTTYPHNLKIRFLLSGQRTELSPPTHQTSATAEVNAPLASSTSASIAVTASATAASAPPATGTTTLGSSISGNAGSTSSGNSSGVSATGGAQSAVGSGGYPKTESSKSSGTASAGSGSGSSSNTSSTKHGSNIKDISSSSNQQASTASSSSAPSLYVSVPLSTANVPGINLPTSSTSSSTTSESHSASSRSSGAQSQHQQQLSNALVGPPMGGSAGAFHGGTTSAGSSSVIQQQSGKSSPALGTLVSGNSGGSIISASGFPLPSGNLTATTTESGNLKISYEKQTTRVQQLQEQEAPPARRSRTLDLSTASASSSSPSAVPATTSPLVVLSNQLPLNSVAASSSTGGLKFTYESQTQMDVPMMPVSAIKDSPPSSPGSEIGSAMHSATTAPGSLTGASTAATAQPGNVRKRGRKAKDATIAAAAAAAAAAAALSNSQQDLKDVRILQNGASNTPGNPAGSTPTPPATPASSNAVSSASSIITHTAAHMLGNQINPNSSVAQKLSEQLHMEVQDHSIYTPDSMNSQYAGVPFPGKQRNSTAVPSNATPAQNPLQSMFSGGGMNGNMPIPQSLEQLLERQWEQGSQFLMEQAQHFDIASLLNCLHQLQSENLRLEEHVTSLIARRDHLLAVNARLQIPLSTIASNTKAEAHAAISTTAAPTTTTTTSTTTATSTCTTSVISTIASSGNSSTSTIGLGSSTSALNAATTIAAAVSLATTAINTTIPTMANSRPTVAAASSSGVLDYRGPGATSNSSNSNSSNNTISNSVSNSSSNPTSSSSASVPPASSMSISGMSISNATNLGMRHVSAAHGSNNAGNSNSSVWSLTASSTVNSNSLHHQHSSQQQQQHQAQHQSHPLQQQQQQQQQVQHHLHQSHHTSAAVAAAHMLGVGMSLGAGGGAAGGIGRGGSATAMAATAATTTTTFTTTAGTGMGQQHHHPHPHQHPSIQIQVGGGGVGVDGLSSTSSSYAVHHAALYSTHHQSQLRRDDNLAKTSXKSHSEQVLQQPQQQIKLKRKQQSLAKRGARHSSTSTSSSSSNHGSKKLPQPSKYSKLSAAESSFRQLIDKNEDDLSSNSSSSTFSSSSQQQSSVDYEAEDENEDKQRRPLHKNDNDSLLHVQNFLKCFGPNAYASTKPSTPTPAIASKPLAIVKSSAGGQLRAWRQNYSSPINGVQAATSIATLQAAQSTTAVAENTSTSTAMFQAQASANQKPTKFQINTKFLRKPRNKLLKMLPTAAALAPGAATTEFKQQEEQLQQPQMFNDDSNAKFKDFSIDSLLNK
Protein: Ribosomal protein S3A (H0Y9Y4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
KRLTKGGKKGAKKKVVDPFSKKDWYDVKAPAMFNIRNIGKTLVTRTQGTKIASDGLKGRVFETMIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVRQIRKKMMEIMTREVQTNDLKEVVNKLIPDSIGKDIEKACQSIYPLHDVFVRKVKMLKKPKFELGKLMELHGEGSSSGKATGDETGAKVERADGYEPPVQESV
Protein: Probable ubiquitin-conjugating enzyme E2 17 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 17) (Ubiquitin carrier protein 17) (O23239)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Interaction partners:
- E3 ubiquitin-protein ligase UPL4
- E3 ubiquitin-protein ligase UPL3
- Probable ubiquitin-conjugating enzyme E2 26
- Probable ubiquitin-conjugating enzyme E2 33
- Probable ubiquitin-conjugating enzyme E2 25
- Probable ubiquitin-conjugating enzyme E2 23
- Ubiquitin-activating enzyme E1 1
- Ubiquitin-conjugating enzyme E2 34
- Membrane-anchored ubiquitin-fold protein 1
- Peptidyl-prolyl cis-trans isomerase CYP26-2, chloroplastic
Sequence:
MTSSSESTRKGLTKIATNRLQKEFMEWQTNPPSGFKHRVSDNLQRWIIEVHGVPGTLYANETYQLQVEFPEHYPMEAPQVIFQHPAPLHPHIYSNGHICLDVLYDSWSPAMRLSSICLSILSMLSSSSVKQKPKDNDHYLKNCKHGRSPKETRWRFHDDKV
Protein: Shaggy-related protein kinase alpha (EC 2.7.11.1) (ASK-alpha) (Shaggy-related protein kinase 11) (AtSK11) (P43288)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May mediate extracellular signals to regulate transcription in differentiating cells.
Interaction partners:
- Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein
- Transcription factor LRL2
- Extensin-like protein
Sequence:
MASVGIAPNPGARDSTGVDKLPEEMNDMKIRDDKEMEATVVDGNGTETGHIIVTTIGGRNGQPKQTISYMAERVVGHGSFGVVFQAKCLETGETVAIKKVLQDRRYKNRELQTMRLLDHPNVVSLKHCFFSTTEKDELYLNLVLEYVPETVHRVIKHYNKLNQRMPLIYVKLYTYQIFRALSYIHRCIGVCHRDIKPQNLLVNPHTHQVKLCDFGSAKVLVKGEPNISYICSRYYRAPELIFGATEYTTAIDVWSAGCVLAELLLGQPLFPGESGVDQLVEIIKVLGTPTREEIKCMNPNYTEFKFPQIKAHPWHKIFHKRMPPEAVDLVSRLLQYSPNLRSAALDTLVHPFFDELRDPNARLPNGRFLPPLFNFKPHELKGVPLEMVAKLVPEHARKQCPWLGL
Protein: Thiamine pyrimidine synthase (Q5LSI0)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
- ABC transporter, permease protein
- ABC transporter, permease protein
- ABC transporter, ATP-binding protein
- D-hydantoinase/dihydropyrimidinase
- ABC transporter, permease protein
- Sulfonate ABC transporter, permease protein, putative
- dihydrouracil dehydrogenase
Sequence:
MSPFGTLPKGVRLIPYPTRSRTEPGQRNRQPTRSEIMKKLMNGAALALALAAGPALAADEVKLQLQWVTQAQFAGYYVALDKGFYDEEGLDVTILPGGPDIAPPQVLAGGGADAMLNWMPSALAAREKGLPVVNIAQPFKSSGLMLTCWKDTGITGPQDFKGKTIGVWFFGNEYPFLSWMSQEGISTDGGADGVTVLKQGFNVDPLLQRQADCISTMTYNEYGQVLDAGVSEDELVTFKYEDMGVATLEDGIYVLEDNLKDEAFKDKMTRFVRASMKGWKYAEANPDEAAGIVLDNDATGAQTEAHQVRMMGEIAKLTAGSNGALDPADFDRTVGTLLAGGSDPVITKTPEGAWTHEITDAALK
Protein: Exostosin-like 3 (EC 2.4.1.223) (Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Multiple exostosis-like protein 3) (Q9WVL6)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase which regulates the biosynthesis of heparan sulfate (HS). Initiates HS synthesis by transferring the first N-acetyl-alpha-D-glucosamine (alpha-GlcNAc) residue (GlcNAcT-I activity) to the tetrasaccharide linker (GlcA-Gal-Gal-Xyl-)Ser core linker. May also transfer alpha-GlcNAc residues during HS elongation (GlcNAcT-II activity). Lacks glucuronyl transferase II (GlcAT-II) activity. Important for both skeletal development and hematopoiesis, through the formation of HS proteoglycans (HSPGs) (By similarity). Through the synthesis of HS, regulates postnatal pancreatic islet maturation and insulin secretion.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43909}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O43909}. Golgi apparatus {ECO:0000250|UniProtKB:O43909}. Cell membrane {ECO:0000250|UniProtKB:O43909}. Nucleus {ECO:0000250|UniProtKB:O43909}. Note=Interaction with REG3A induces its translocation to the nucleus. {ECO:0000250|UniProtKB:O43909}.
Interaction partners:
- Exostosin-like 1
- Exostosin-like 2
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Heparan sulfate 2-O-sulfotransferase 1
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Xylosyltransferase 2
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Beta-1,4-galactosyltransferase 7
- D-glucuronyl C5-epimerase
- Xylosyltransferase 1
Sequence:
MTGYTMLRNGGVGNGGQTCMLRWSNRIRLTWLSFTLFIILVFFPLIAHYYLTTLDEADEAGKRIFGPRAGSELCEVKHVLDLCRIRESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQPKLSLPIRLLPEKDDAGLPPPKVTRGCRLHNCFDYSRCPLTSGFPVYVYDSDQFAFGSYLDPLVKQAFQATVRANVYVTENAAIACLYVVLVGEMQEPTVLRPADLEKQLFSLPHWRTDGHNHVIINLSRKSDTQNLLYNVSTGRHVAQSTFYAAQYRAGFDLVVSPLVHAMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEARSFEEEMEGDPPADYDDRIIATLKAVQDSKLDQVLVEFTCKNQPKPSLPTEWALCGEREDRLELLKLSTFALIITPGDPHLLISSGCATRLFEALEVGAVPVVLGEQVQLPYHDMLQWNEAALVVPKPRVTEVHFLLRSLSDSDLLAMRRQGRFLWETYFSTADSIFNTVLAMIRTRIQIPAAPIREEVAAEIPHRSGKAAGTDPNMADNGDLDLGPVETEPPYASPKYLRNFTLTVTDCYRGWNSAPGPFHLFPHTPFDPVLPSEAKFLGSGTGFRPIGGGAGGSGKEFQAALGGNVQREQFTVVMLTYEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRTEKNSLNNRFLPWNEIETEAILSIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDIPHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAIRDMVDEYINCEDIAMNFLVSHITRKPPIKVTSRWTFRCPGCPQALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRVDSVLFKTRLPHDKTKCFKFI
Protein: ShKT domain-containing protein (O16225)
Organism: Caenorhabditis elegans
Interaction partners:
- Anoctamin
- TMhelix containing protein
- ShKT domain-containing protein
- EB domain-containing protein
- Prion-like-
- Kelch repeat and BTB domain-containing protein F47D12.7
- BPTI/Kunitz inhibitor domain-containing protein
- BTB domain-containing protein
- Flo11 domain-containing protein
- Carboxylic ester hydrolase
Sequence:
MIALFSVLIAFLTPQANAVISGELNCTTYNGTAFVYTPSATACSNAISDSSCAALYPASDPATGYPAPGNDVERPFACYTTATPTPAPVVPDMRSAALKNCARTCGLCCKTADFDCPNVQFPRLTCSTITNEQCRSSVWRTIIATDCPSACGFCNQGGCVDGVMDCANDLSICNSVGMQEFVNQYCQRTCNRCSSSTAATGTGGSCGGRYIADSSTACAAWKLNGFCTNTFYTAAQRRSYCATTCSLC
Protein: V-type proton ATPase 16 kDa proteolipid subunit c (V-ATPase 16 kDa proteolipid subunit c) (VHA16K) (Ductin) (Vacuolar H+ ATPase subunit 16-1) (Vacuolar proton pump 16 kDa proteolipid subunit c) (P23380)
Organism: Drosophila melanogaster (Fruit fly)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. In enterocytes, acts as part of a pHCl-2 sensory pathway which mediates Tor-dependent larval growth and metabolism in response to zinc availability. Likely acts in maintaining enterocyte lysosomal acidification which consequently promotes Tor activation at the lysosome membrane.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit H
- V-type proton ATPase subunit E
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit a
- V-type proton ATPase subunit G
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase subunit a
- V-type proton ATPase subunit C
- V-type proton ATPase catalytic subunit A isoform 1
Sequence:
MSSEVSSDNPIYGPFFGVMGAASAIIFSALGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGALEEPSKYSLYRGFIHLGAGLAVGFSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVAIYLYTK
Protein: Vomeronasal type-1 receptor (A0A2I3BPI9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}.
Interaction partners:
Sequence:
MDLISCQLTFVHIMMFLAGENFWLANIFESLNVENDFKCKATFYTKRVMRGLSICITCLLSVFQAVMISHRNSLLAKFKHKLKIYMINALFYIWTFNLSLSSNLIFYVGGFTNMSQTKQLKVTKSCSLIPMNYIIRGLILTVISSRDMFLVGVMLTTSTYMVIILCRHQRQCKHLHSTSHLRASPEKRATQTILLLVVFFVIMYWVDFIISSTSILLWMYDPVIMIVQKFVVNAYPAITPFVQISSDTRVIRVVKNWHS
Protein: Malonyl-CoA decarboxylase, mitochondrial (MCD) (EC 4.1.1.9) (Q920F5)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16298369}. Mitochondrion matrix {ECO:0000269|PubMed:16298369}. Peroxisome {ECO:0000250}. Peroxisome matrix {ECO:0000269|PubMed:16298369}. Note=Enzymatically active in all three subcellular compartments.
Interaction partners:
- Acetyl-CoA carboxylase 1
- Acetyl-CoA acetyltransferase, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Protein kinase AMP-activated non-catalytic subunit gamma 2
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- Protein kinase AMP-activated non-catalytic subunit gamma 3
- 5'-AMP-activated protein kinase subunit beta-2
- 5'-AMP-activated protein kinase subunit beta-1
- Fatty acid synthase
Sequence:
MRGLGPSLRARRLLPLRYPPRPPGPRGPRLCSGLTASAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAEAAQRAELLGRLAQGFGVDHGQVAEQSAGVLQLRQQSREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPHVREMNGVLKSMLSEWFSSGFLNLERVTWHSPCEVLQKISECEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGDPLVVLHVALTGDISNNIQSIVKECPPSETEEKNRIAAAVFYSISLTQQGLQGVELGTFLIKRVVKELQKEFPHLGAFSSLSPIPGFTKWLLGLLNVQGKEYGRNELFTDSECKEIAEVTGDPVHESLKGLLSSGEWAKSEKLAQALQGPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVMWRINWMADSSLKGLTSSCGLMVNYRYYLEETGPNSISYLGSKNIKASEQILSLVAQFQSNSKL
Protein: Somatostatin receptor subtype 5 (Q6YEY1)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MEPLFPATPPTSRNTSWAATSRGGGGGGGGENGTLAEPVPSPGARAVAVPVLYLLVCALGLGGNALVIYVVLRHAKMKTVTNIYILNLAVADVLLMLGLPFVATQNALSYWPFGPVLCRLVMTLDGINQFTSIFCLTVMSVDRYLAVVHPLRSARWRRPRVARLASAAVWAFSLVMSLPLVVFADVQEGWNTCNLSRPEPVGLWGAVFIIYTSVLGFFGPLLVICLCYLLIVVKLKASGVRVGSTRRRSERKVTRMVVVVVLVFVGCWLPSFIANLVNLAFVLPEEPASAGAYFFVVVLSYANSCANPLLYGFLSDNFRQSFRKVLCLRKGSGVEDANATKPRAGQSGRPPEAPVALRSHEANGLMQTSRL
Protein: Replication origin-binding protein (OBP) (OriBP) (P09299)
Organism: Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3)
Function: Functions as a docking protein to recruit essential components of the viral replication machinery to viral DNA origins. In the presence of the major DNA-binding protein, opens dsDNA leading to a conformational change in the origin that facilitates DNA unwinding and subsequent replication (By similarity).
Subcellular location: Host nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSPNTGESNAAVYASSTQLARALYGGDLVSWIKHTHPGISLELQLDVPVKLIKPGMSQTRPVTVVRAPMGSGKTTALLEWLQHALKADISVLVVSCRRSFTQTLIQRFNDAGLSGFVTYLTSETYIMGFKRLIVQLESLHRVSSEAIDSYDVLILDEVMSVIGQLYSPTMRRLSAVDSLLYRLLNRCSQIIAMDATVNSQFIDLISGLRGDENIHTIVCTYAGVGFSGRTCTILRDMGIDTLVRVIKRSPEHEDVRTIHQLRGTFFDELALRLQCGHNICIFSSTLSFSELVAQFCAIFTDSILILNSTRPLCNVNEWKHFRVLVYTTVVTVGLSFDMAHFHSMFAYIKPMSYGPDMVSVYQSLGRVRLLLLNEVLMYVDGSRTRCGPLFSPMLLNFTIANKFQWFPTHTQITNKLCCAFRQRCANAFTRSNTHLFSRFKYKHLFERCSLWSLADSINILQTLLASNQILVVLDGMGPITDVSPVQFCAFIHDLRHSANAVASCMRSLRQDNDSCLTDFGPSGFMADNITAFMEKYLMESINTEEQIKVFKALACPIEQPRLVNTAILGACIRIPEALEAFDVFQKIYTHYASGWFPVLDKTGEFSIATITTAPNLTTHWELFRRCAYIAKTLKWNPSTEGCVTQVLDTDINTLFNQHGDSLAQLIFEVMRCNVTDAKIILNRPVWRTTGFLDGCHNQCFRPIPTKHEYNIALFRLIWEQLFGARVTKSTQTFPGSTRVKNLKKKDLETLLDSINVDRSACRTYRQLYNLLMSQRHSFSQQRYKITAPAWARHVYFQAHQMHLAPHAEAMLQLALSELSPGSWPRINGAVNFESL