wanglab/gogpt-training-data huggingface dataset:
Protein: Pyridoxal phosphate phosphatase YigL (EC 3.1.3.74) (PLP phosphatase) (Sugar phosphatase) (EC 3.1.3.23) (P27848)
Organism: Escherichia coli (strain K12)
Function: Catalyzes Strongly the dephosphorylation of pyridoxal-phosphate (PLP) and moderately the dephosphorylation of 2-deoxyglucose 6-phosphate (2bGLU6P) and beta-glucose 6-phosphate (bGlu6P). Also hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary substrates.
Interaction partners:
- Lysophospholipase L2
- Biotin transporter
- Putative inhibitor of glucose uptake transporter SgrT
- PTS system glucose-specific EIICB component
Sequence:
MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFAHNLDRDIASDLFGVVNDNPDIITNVYRDDEWFMNRHRPEEMRFFKEAVFQYALYEPGLLEPEGVSKVFFTCDSHEQLLPLEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKDLHPELEVIGTNADDAVPHYLRKLYLS
Protein: Matrix protein 2 (Proton channel protein M2) (O70632)
Organism: Influenza A virus (strain A/Hong Kong/156/1997 H5N1 genotype Gs/Gd)
Function: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}.
Interaction partners:
Sequence:
MSLLTEVETLTRNGWGCRCSDSSDPLVVAASIIGILHLILWILDRLFFKCIYRRFKYGLKRGPSTEGVPESMREEYRQEQQNAVDVDDGHFVNIELE
Protein: Protein DGCR6 (DiGeorge syndrome critical region 6) (Q14129)
Organism: Homo sapiens (Human)
Function: May play a role in neural crest cell migration into the third and fourth pharyngeal pouches.
Subcellular location: Nucleus {ECO:0000269|PubMed:15821931}. Note=Predominantly nuclear.
Interaction partners:
- Proline dehydrogenase
- Integral membrane protein DGCR2/IDD
- Zinc finger protein 74
- Proline dehydrogenase 1, mitochondrial
- Protein HIRA
- T-box transcription factor TBX1
Sequence:
MERYAGALEEVADGARQQERHYQLLSALQSLVKELPSSFQQRLSYTTLSDLALALLDGTVFEIVQGLLEIQHLTEKSLYNQRLRLQNEHRVLRQALRQKHQEAQQACRPHNLPVLQAAQQRELEAVEHRIREEQRAMDQKIVLELDRKVADQQSTLEKAGVAGFYVTTNPQELMLQMNLLELIRKLQQRGCWAGKAALGLGGPWQLPAAQCDQKGSPVPP
Protein: Splicing factor 3B subunit 1 domain-containing protein (G5EEQ8)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- PSP proline-rich domain-containing protein
- Splicing factor 3B subunit 6-like protein
- Splicing factor 3B subunit 4
- Splicing factor 3B subunit 3
- PHD finger-like domain-containing protein 5A
- Splicing factor U2AF 65 kDa subunit
- Probable U2 small nuclear ribonucleoprotein A'
- RNA helicase
- Pre-RNA processing 21
- Splicing factor 3A subunit 2
Sequence:
MSRSGEAYAQELNRKRVANQRAAAAEDNDENKGNGNKVAFGAAGNFDTDVYGSVRGENRDSYLDSIGTGEEDDVDEDSMPSVQKKSTNYAQPHKFIEEVAAASEDTDPFADTRTKTIAERQSKYHERAMRRQISPDRADAFVDQTPDNRNRGYAEVMRDQMYHEEKGRVERELADRAKAGELHVTGQPEKKKGRWDAEAPSTDASSDNLGAASATPSQGSAPRKRLGFSKISADAATPRAARWDETPAHSTGAADATPSVDKWSTTPAAQTPRRNRWDETPKENLNDGSMTPGWGMETPARGGSDDVKIEDTPSASKRRSRWDLTPSQTPNVAAATPLHSGLQTPSFTPSHPSQTPIGAMTPGGATPIGTAAMGMKTPAPHMIPMTPEQMQIYRWEKEIDDRNRPLTDEELDSLFPPGYKVLVPPMNYIPLRTPSRKLMATPTPMGGAAGGGFFMPGTPDRDGIGEKGVGGLVDTQPKNAELPPLKPDDMQYFDKLLMDVDESQLTKEEKNEREIMEHLLKIKNGTPPMRKSGLRKITENARKYGAGPLFNQILPLLMSPSLEDQERHLMVKVIDRILYKLDDLVRPYVHKILVVIEPLLIDEDYYARVEGREIISNLAKAAGLATMISTMRPDIDNVDEYVRNTTARAFAVVASALGIPALLPFLKAVCKSKKSWQARHTGIKIVQQMAILMGCAVLPHLKALVDIVESGLDDEQQKVRTITALCLAALAEASSPYGIEAFDSVLKPLWKGIRMHRGKGLAAFLKAIGYLIPLMDAEYASYYTREVMLILIREFASPDEEMKKIVLKVVKQCCATDGVEASYIRDEVLPSFFKAFWNQRMAMDRRNYRQLVDTTVEIAQKVGCVEMIARIVDDLKDENEQYRKMVMETIENIVALQGATDIDARLEEQLIDGLLYAFQEQTQEDSVMLDGFGTICSSLGRRAKAYIPQICGTILWRLNNKSAKVRQQAADLIARIAPVMHMCEEEKMMGHMGVVLYEYLGEEYPEVLGSILGALKAICNVIGMTKMTPPIKDLLPRLTPILKNRHEKVQENCIDLVGAIADRGSEFVSAREWMRICFELLELLKAHKKSIRRAAINTFGFIAKAIGPHDVLATLLNNLKVQERQLRVCTTVAIAIVSETCAPFTVLPAIMNEYRVPEINVQNGVLKALSFMFEYIGEMAKDYIYAVVPLLIDALMERDQVHRQIAVDAVAHLAIGVYGFGCEDALIHLLNYVWPNMLENSPHLIQRWVFACEGMRVSLGPIKVLQYCLQALWHPARKVREPVWKVFNNLILGSADALIAAYPRIENTPTNQYVRYELDYNL
Protein: Elongation of very long chain fatty acids protein 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL2) (ELOVL fatty acid elongase 2) (ELOVL FA elongase 2) (Very long chain 3-ketoacyl-CoA synthase 2) (Very long chain 3-oxoacyl-CoA synthase 2) (A0A068CAR2)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03202}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03202}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEHLKAFDQEVNAFVDYMFGPRDSRVRGWLLLDSYLPTFFLTVAYLLSIWLGNKFMKNRQPFSLRAHLIVYNLGITLLSLYMLIELILATWEGGYNLQCQNLHSAGEADIRVAKVLWWYYFSKVIEFADTIFFVLRKKSSQITFLHVYHHATMFNIWWCVLNWIPCGQSFFGPTLNSFIHVLMYSYYGLSVIPSMRKYLWWKKYLTQAQLIQFLLTIVHTLSAAVKPCGFPFGCLMFQSSYMATLVILFINFYIKTYQKAPSRTAAKETPVTTEVKNGFHKNYFAASNGFLNNKKAQ
Protein: Conserved protein (O53777)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MTDQSYAVDIAHPPAALLRLVNPILRSLLHTPLAGPLRTQLMVVSFTGRKTGRHFSIPLSAHVIDNDLYALTEAGWKHNFSDGAAAQVVYDGKTTAMRGELIRDRAVVSELFLRAAQAYGVKRGQRMLGLSFRDRRIPTLEEFAEAVDRLKLVAIRLTPADNS
Protein: Insulin-like peptide INSL5 (Insulin-like peptide 5) (Relaxin/insulin-like factor 2) (Relaxin/insulin-like protein) [Cleaved into: Insulin-like peptide INSL5 B chain; Insulin-like peptide INSL5 A chain] (Q9WUG6)
Organism: Mus musculus (Mouse)
Function: May have a role in gut contractility or in thymic development and regulation. Activates RXFP4 with high potency and appears to be the endogenous ligand for this receptor (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Relaxin-3 receptor 2
- Relaxin-3 receptor 1
- Insulin-like 3
- Relaxin receptor 1
- Relaxin receptor 2
- Prorelaxin 1
- Relaxin-3
- Insulin-like peptide INSL6
Sequence:
MKGPTLALFLLLVLLAVVEVRSRQTVKLCGLDYVRTVIYICASSRWRRHLEGHFHSQQAETRNYLQLLDRHEPSKKTLEHSLPKTDLSGQELVRDPQAPKEGLWELKKHSVVSRRDLQALCCREGCSMKELSTLC
Protein: Bub3 interacting GLEBS and zinc finger domain protein, isoform G (X2JED0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKKKKASKPWCWYCNREFDDEKILVQHQKAKHFKCHICHKKLYTGPGLSIHCMQVHKETVDKVPNSLPNRSNIEVEIFGMDGIPAEDLRDHERQKNGGKSDSDDDEPVAKKKVEYAMSVPPPMMMPPNMMPPHMLGQYGMGMMQHMPPLPPYPVPMMPHMMPPRPLFPAAMATTSAAAAAAAAHHHHAAAMAQQKPTFPAYSNATISAPPTTNHAGGASSAPPSGPPDAQQHQQRPPAPPAASGTSAAAVTTKIMHPQEDLSLEELRARQPKIQARLAAALASLANPQSRKSPSNNGGPSTSIPTTPPPPSLAGISPTGSNSSSGMANSIVVSAAMSKAQENAALVAVAQAQAHAHAHAAQVQAQAQAQAVVQAQVQAAHVAHAVAAQQQAVQQQQAAQQQQQAAVQQQAAVQQQQQQQQAAVQQQQAAQQQVKQLEELNRAVMLQRFQAARQPGNPGAAAAAAAAAAVGMVSL
Protein: O-methyltransferase 12 (EC 2.1.1.-) (Q54B59)
Organism: Dictyostelium discoideum (Social amoeba)
Function: S-adenosyl-L-methionine dependent O-methyltransferase that may be involved in modifying resorcinol ring to synthesize a variant of 4-methyl-5-pentylbenzene-1,3-diol.
Interaction partners:
Sequence:
MSDWDKTMDLLFGFVTGHIHSRMFETILKFSICDLLEDGPKHYSEISKIIGFKNESYCYRLMRYFVPYKLFNESVVQVGLFSKTPSSTQFSKNGTLKNLGRFHCQDHHYRIFESLPKTLEMGKNQGPSSIGLSSFWEHFETDESYKQLFHNAMKDYTSLIIDRLISKISLSPNFKTVVDIGGSHGFLIGKLLESNPNIHGINFDLENIINSSTSKNENFQHPRLKHVSGDFFNSVPEADCYILKYILHDWSDEKCITILNNIHKSLKPNGKLFINDLVLDPSNYTKEAVFKDILMMQYFDAKERSINEWHQLFEKCGFKIDSVDTSISPQLMIVSKINSSNINLNDCTNFNSEIVEEKLKNSLPQFVNC
Protein: Kcnk6 protein (Q14BF9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLLLTASAQRLSLLLTHAPLSWLSLHWGWPPQRAARWHLVALLMVIVAIFFLVPAAVFAYLEEAWSFLDAFYFCFISLSTIGLGDYVPGEAPGQPYRALYKVLVTAYLFLGLVAMVLVLQTFRRVSDLHGLTELILLPDPDPASLSQDEDDQVAVLDARTDLHQHLSAASHADYASIPR
Protein: Myosin XI-2 (B0CN59)
Organism: Nicotiana benthamiana
Interaction partners:
Sequence:
MAASVSLPVGSLVWVEDPHEAWIDGEVLEVNGSDIKVLCTSGKTVVVKSSNVYAKDAEAPPSGVDDMTKLAYLHEPGVLHNLKARYDINEIYTYTGNILIAVNPFRRLPHLYDTHMMAQYKGAAFGELSPHPYAVADAAYRLMINEGVSQSILVSGESGAGKTESTKQLMRYLAYMGGRAAAEGSRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQKGRISGAAVRTYLLERSRVCQVSDPERNYHCFYMICAAPPEDIKRFKLGNPRTFHYLNQTNCFQLDEIDDSKEYLATRRAMDVVGISSEEQDAIFRVVAAILHLGNIEFAKGKEIDSSVPKDEKSWFHLRTAAELFMCDVKALEDSLCKRVIVTRDETITKWLDPEAAVTSRDALAKVVYSRLFDWLVDKINSSIGQDPNSKSLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEINWSYIEFIDNQDILDLIEKKPGGIIALLDEACMFPRSTHDTFAQKLYQTFKNHKRFCKPKLARSDFTICHYAGDVTYQTELFLEKNKDYVIAEHQALLSASTCSFVSGLFPTSNEESSKQSKFSSIGTRFKQQLQSLLETLSATEPHYIRCVKPNNLLKPAIFENHNVLQQLRCGGVMEAIRISMAGYPTRKPFYEFLDRFGILSPEVLDGSTDEVAACKRLLEKVGLEGYQIGKTKVFLRAGQMAELDGRRTEVLGRSASIIQRKVRSYMARRSFTLLRRSTIQIQSLCRGELARRVYESLRREAASLRIQTNVRMHLSRKAYKELLSSAVSIQTGLRGMAARDELRFRRQNKAAIIIQSHCRKFLAYSKFKKLKKAAITTQCAWRGRVARKELKKLKMAARETGALQAAKNKLEKQVEELTWRLQLEKRMRADLEEAKTQENAKLQSAFQELQVQFKETKEMLVKERENAKRAAEQIPIVQEVPVIDHELMNKLSIENENLKSMVSSLEKKIGETETKYEETNKLSEERLKQAMEAESKIVQLKTTMQRLEEKIFDMESENQILRQQALLTPAKRVSEHSPSPASKIVENGYHLNDENRTNDAPSFTPSKNYETPDSKLRRSPIDRQHEDVDALIDCVMKDVGFSQGKPVAAFTIYKCLLNWKSFEAERTSVFDRLIQMIGSAIENQESNDHMAYWLSNTSTLLFLIQKSLKSGGAVGATPTRKPQPPTSLFGRMTMGFRSSPSAVNLAAAAAALVVRQVEAKYPALLFKQQLTAYVEKIYGIIRDNLKKELGSLLSLCIQAPRTSKGSLRSGRSFGKDSSTNHWQRIIECLNSLLCTLKENFVPPILVQKIFTQTFSYINVQLFNSLLLRRECCTFSNGEYVKAGLAELELWCCQAKEEYAGSSWDELKHIRQAVGFLVIHQKYRISYDEITNDLCPILSVQQLYRICTLYWDDNYNTRSVSPDVISSMRVLMTEDSNNAESNSFLLDDNSSIPFSIDEVSESLQVKDFADVKAATQLLENPAFQFLHE
Protein: Centractin (Actin-like protein) (Actin-related protein 1) (P38696)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding (By similarity). The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. Required for proper orientation of the mitotic spindle.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:16291862}. Membrane {ECO:0000269|PubMed:16291862}. Note=Membrane-associated.
Interaction partners:
- Nuclear migration protein JNM1
- Protein NIP100
- Actin-like protein ARP10
- Protein LDB18
- Dynein heavy chain, cytoplasmic
- Myosin-1
- Fimbrin
- Actin-related protein 4
- Karyogamy protein KAR9
- Actin-related protein 3
Sequence:
MDQLSDSYALYNQPVVIDNGSGIIKAGFSGEERPKALEYCLVGNTKYDKVMLEGLQGDTFIGNNAQKLRGLLKLRYPIKHGVVEDWDSMELIWSYVLNEVLQLQNIGEHPLLITEAPMNPLKNREQMAQVLFETFDVSALYVSNPAVLSLYASGRTTGCVVDCGEGYCSTVPIYDGFALPASMMRMDIGGADITEQLQFQLRKSAGVSLFSSSEREIVRTMKEKVCYLAKNIKKEEEKYLQGTQDLISTFKLPDGRCIEVGNDRYRAPEILFSPQIIGLGYDGLSDMCMQSIWKVDLDLRKPLLSSIILSGGTTTLKGFGDRMLWDLEALTKGTSKIKIIAPSERKYTTWIGGSILTGLSTFQRLWTKKSDWLEDSTRVYSNLM
Protein: Heat shock protein beta-1 (HspB1) (Heat shock 27 kDa protein) (HSP 27) (P42930)
Organism: Rattus norvegicus (Rat)
Function: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04792}. Nucleus {ECO:0000250|UniProtKB:P04792}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04792}. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000250|UniProtKB:P04792}.
Interaction partners:
- non-specific serine/threonine protein kinase
- MAP kinase-activated protein kinase 5
- Cytochrome c, somatic
- MAP kinase-activated protein kinase 3
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 4
- RAC-alpha serine/threonine-protein kinase
- Heat shock 70 kDa protein 1A
- Plectin
- Eukaryotic translation initiation factor 4 gamma 1
Sequence:
MTERRVPFSLLRSPSWEPFRDWYPAHSRLFDQAFGVPRFPDEWSQWFSSAGWPGYVRPLPAATAEGPAAVTLARPAFSRALNRQLSSGVSEIRQTADRWRVSLDVNHFAPEELTVKTKEGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQSAEITIPVTFEARAQIGGPESEQSGAK
Protein: Ribonuclease T (EC 3.1.13.-) (Exoribonuclease T) (RNase T) (P30014)
Organism: Escherichia coli (strain K12)
Function: Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis, especially in strains lacking other exoribonucleases.
Interaction partners:
- Ribonuclease D
- Oligoribonuclease
- Ribonuclease R
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease E
- Ribonuclease BN
- Exoribonuclease 2
- Multifunctional CCA protein
- Cell division protein DedD
- Poly
Sequence:
MSDNAQLTGLCDRFRGFYPVVIDVETAGFNAKTDALLEIAAITLKMDEQGWLMPDTTLHFHVEPFVGANLQPEALAFNGIDPNDPDRGAVSEYEALHEIFKVVRKGIKASGCNRAIMVAHNANFDHSFMMAAAERASLKRNPFHPFATFDTAALAGLALGQTVLSKACQTAGMDFDSTQAHSALYDTERTAVLFCEIVNRWKRLGGWPLSAAEEV
Protein: C2H2-type domain-containing protein (Putative MAP-like protein) (G5EF29)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSDDEDEGRLQIDESPSDSEDKPSISAPPPLPPPLQETPEFQTTYDAHDQAETSGKEDGELDEDDENDDIEPMEIDEEIQLEIDEKPEDLVKDEQISEPTDKMREEFLKVEKTDENAVVESTSSFSPKLIDEQDLKVEEMSDEKHAQSPVSSDMTTSKSPTPSKKENGLMKPPQSTEKAQRKRKESTDIFSSEKRKLSLETVASSSSSSGSSNLSTTPQRSKRSSSHMATIAISACFTDEDIVSVPMMPIQKTPDTAPHSKRAKRDIGTNVITTRSTDTSGLLCNEAIMDTPPGSQMTLEVTVMYRTKNSLAFRVKGCDLIGFIGDGLPPMASSLTNNIASSMGNNNNKKKTASSSGNEEGKDGRSSSASSNGRGARGGSVLKDGKEDENQNNEQYGSKKCELVEVDVAQLHDCHYDGCEKRFQKTTDLEYHISKNHKRRVMMYESICTQTSISSLETQNNSTQIDDDLPPMPQMPILKKEVPIKTPIGNVYEDLSDDDSETKPTDLVLKTPSSSASSAVATLMGIAQVSSSTTSATTSVVPPVGAQRSTPATPVSAKIGINPSMVANALAEKNKQQQQQQQKLNQLQPPHNPSLSTAPSSSSAQPPTMIQAHPMAGVFIPPPFHPAMMNPQMAAMMDQQRIAVAMSQQQQMSRTPSRQTISVSDSHKIHELAKSRENQQRQQSATPKTPSESVSTTGVVTPQRQFLPPQMMQPGTPQSILLQQQQQQQQQQQQAAAQHQIIQQMQMQMQRGMAPQMANQELLMMMMGMPHMVQGVPGFPGVPQLPPK
Protein: Contig An02c0120, genomic contig (A2QCP4)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MSLLHNEDFTIWQLRTSYLSTIKDGIGDRLINVNNTVLNTPGFRAAGWSSASTNPNTQSAAAHIKRTNSPPIPTTTAVTSEYYQLGVARDDAQRFGLVDEGDDDEGGMVTGKTNTDLIGRRNRGKRVHRRERQQHEQQKHREAEEDDSSDLSDESDDDGDSARSAANQIKFTKMPIRTRAGSSPIRSSDRQESPQVMVTSPSHPTMGTHYRTGSLGTAVSSINERPRRDTTTTASSDISSDNDLDASAFRRRQISFSGHDQVIEPARKRNGPPGPRDLEELHEQAEDSGAESVGSALSSDFDATAGSASLLAGVGITGSLDSSSPVALMHKLQNGTGSQTASPRKPRAPAPELQDLPPPRPISTVQPVSLLSKALNARKKAPTNPVEKFAVLSGKGLTDVLNIKLYLPFSADPDEPLDLPIARESKLAEQPAPVTVVEAIGLALWRYSEEGREPAVERSKLTVNMWTLRMVEDGEVEYDFPALGRTSPIADFTSNNNRAAGRRTRGKQYDEFALVEASKAEFEANERQFPQYSQTAASEDSGEAPAPTSAPTSQTVPQSKAPRPNPILGQPFSSALNDNTLTPADRPAVPTSHATPRLGVSKTLKIRFINVEASTQVTTLNTSTDSYIAEILDSVCKRWGLDKGNYLLKVMGSNTIAPLDRTVEALGNITELDLVRRRFGPQSLTGSPGSSSPNAPLLIDSNSAPSKKGKKSGQRMLHPLTQKQDLIGGYYRRYYVWRKQSMGFTQSNHRILTFDNDYMHIMPADTGKTASDTKTRSISFNDVVGCKVSRRHLKNFRVVVLRGNDANEQKRYDFEARNALEAVEIVDEIKKNMAHYRI
Protein: Interleukin-18 (IL-18) (Q6IT44)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR015162}.
Interaction partners:
Sequence:
MSCEEIAVCAVRLRENLCLYFEELECDAFCKDKTIKRFFRNVNSQLLVVRPDLNVAAFEDVTDQEVKSGSGMYFDIHCYKTTAPSAGMPVAFSVQVEDKSYYMCCEKEHGKMVVRFREGEVPKDIPGESNIIFFKKTFTSCSSKAFKFEYSLEQGMFLAFEEEDSLRKLILKKLPREDEVDETTKFVTSHNERHNL
Protein: POU domain protein (O13007)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MTKTAPIAAMDYSHLWLPDIRMSKPIEVENPAADSPMENTGDSERNGSDSNNQIPSMKISPFSLSPTLSASNKAKLEECGEMSPASVQATPTQTPLSHTQLMLTGSQLAGDIQQLLQLQQLVLVPGHPLSSPAQFLLPQAQQGQQGLLQTPNLIPLPQQNQGGLLSAPPALGLQAQQREKVMESSVSTVTPVTSHAEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLTDAETMSMDSTLPSPSSLSSPSLGFEGLPARRRKKRTSIETNVRVALERSFSTNQKPTSEEILLIAEQLNMEKEVIRVWFCNRRQKEKRINPSSATPPLPSQPQPASHKPPCYSPHMMQGQGPSQPVTSLSTAATTMSSVCPLTPTGPSSSSTPSPVTPSPRSDASPVPATHTLNLNTGSWRHKNGDVSNYITDFAANLSSGSQWWSNHHFQS
Protein: Large ribosomal subunit protein eL27 (60S ribosomal protein L27) (P61358)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit (By similarity). Required for proper rRNA processing and maturation of 28S and 5.8S rRNAs (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61353}. Cytoplasm {ECO:0000269|PubMed:36517592}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:A1XQU5}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:A1XQU5, ECO:0000250|UniProtKB:P61353}.
Interaction partners:
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL13
Sequence:
MGKFMKPGKVVLVLAGRYSGRKAVIVKNIDDGTSDRPYSHALVAGIDRYPRKVTAAMGKKKIAKRSKIKSFVKVYNYNHLMPTRYSVDIPLDKTVVNKDVFRDPALKRKARREAKVKFEERYKTGKNKWFFQKLRF
Protein: Nck-associated protein 1 (NAP 1) (Membrane-associated protein HEM-2) (p125Nap1) (P55161)
Organism: Rattus norvegicus (Rat)
Function: Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1 (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P28660}; Single-pass membrane protein {ECO:0000250|UniProtKB:P28660}; Cytoplasmic side {ECO:0000250|UniProtKB:P28660}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P28660}; Single-pass membrane protein {ECO:0000250|UniProtKB:P28660}; Cytoplasmic side {ECO:0000250|UniProtKB:P28660}. Note=At the interface between the lamellipodial actin meshwork and the membrane. {ECO:0000250|UniProtKB:P28660}.
Interaction partners:
- Actin-binding protein WASF1
- Abl interactor 1
- Cytoplasmic FMR1-interacting protein
- Protein BRICK1
- Cytoplasmic FMR1-interacting protein
- Abl-interactor 2
- Wiskott-Aldrich syndrome protein family member
- ABI gene family member 3
- Ras-related C3 botulinum toxin substrate 1
- small monomeric GTPase
Sequence:
MSRSVLQPSQQKLAEKLTILNDRGVGMLTRLYNIKKACGDPKAKPSYLIDKNLESAVKFIVRKFPAVETRNNNQQLAQLQKEKSEILKNLALYYFTFVDVMEFKDHVCDLLNTIDVCQVFFDITVNFDLTKNYLDLTVTYTTLMILLSRIEERKAIIGLYNYAHEMTHGASDREYPRLGQMIVDYEHPLKKMMEEFVPHSKSLSDALISLQMVYPRRNLSADQWRNAQLLSLISAPSTMLNPAQSDTMPCEYLSLDAMEKWIIFGFILCHGMLNTEATALNLWKLALQSSSCLSLFRDEVFHIHKAAEDLFVNIRGYNKRINDIRECKEAAVSHAGSMHRERRKFLRSALKELATVLSDQPGLLGPKALFVFMALSFARDEIIWLLRHADNMPKKSADDFIDKHIAELIFYMEELRAHVRKYGPVMQRYYVQYLSGFDAVVLNELVQNLSVCPEDESIIMSSFVNTMTSLSVKQVEDGEVFDFRGMRLDWFRLQAYTSVSKASLSLADHRELGKMMNTIIFHTKMVDSLVEMLVETSDLSIFCFYSRAFEKMFQQCLELPSQSRYSIAFPLLCTHFMSCTHELCPEERHHIGDRSLSLCNMFLDEMAKQARNLITDICTEQCTLSDQLLPKHCAKTISQAVNKKSKKQTGKKGEPEREKPGVESMRKNRLVVTNLDKLHTALSELCFSINYVPNMAVWEHTFTPREYLTSHLEIRFTKSIVGMTMYNQATQEIAKPSELLTSVREYMTVLQSIENYVQIDITRVFNNVLLQQTQHLDSHGEPTITSLYTNWYLETLLRQVSNGHIAYFPAMKAFVNLPTENELTFNAEEYSDISEMRSLSELLGPYGMKFLSESLMWHISSQVAELKKLVVENVDVLTQMRTSFDKPDQMAALFKRLSSVDSVLKRMTIIGVILSFRSLAQEALRDVLSYHIPFLVSSIEDFKDHIPRETDMKVAMNVYELSSAAGLPCEIDPALVVALSSQKSENISPEEEYKIACLLMVFVAVSLPTLASNVMSQYSPAIEGHCNNIHCLAKAINQIAAALFTIHKGSIEDRLKEFLALASSSLLKIGQETDKTTTRNRESVYLLLDMIVQESPFLTMDLLESCFPYVLLRNAYHAVYKQSVTSSA
Protein: Oligogalacturonide ABC transporter, ATPase component (EC 3.6.3.19) (E0SDC8)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Oligogalacturonide ABC transporter, permease component
- Oligogalacturonide ABC transporter, permease component
- Predicted rhamnose oligosaccharide ABC transport system, substrate-binding component
- Galactan ABC transport system, permease component
- Predicted rhamnose oligosaccharide ABC transport system, substrate-binding component
- ABC-type sugar transport systems, permease component
- Multiple sugar ABC transporter, membrane-spanning permease protein MsmF
- ABC transporter, inner membrane component
- ABC transporter, membrane spanning protein
- Maltose/maltodextrin ABC transporter, permease protein MalG
Sequence:
MAEVIFNKLEKVYSNGFKAVHGIDLTIKDGEFMVIVGPSGCAKSTTLRMLAGLETISGGEVRIGEKIVNNLAPKDRGIAMVFQNYALYPHMTVRENLAFGLKLSKMPKDKIEAQVNEAAKILELEELMDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQLKKSGHPATSVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHFPKNMFVAGFIGAPEMNIKPGKLLEENGQITLQVGQYTMSLNQAKQDKVRGYVGKDICFGVRPEYVTVSEAPFDGGHFQGELVRAENMGHEFFMYIKVDGFELTSRMPSDEARVIINNRMNSKVYFKFDMDKCHIFDAKTEQNISL
Protein: Ran guanine nucleotide release factor (RanGNRF) (Ran-binding protein MOG1) (A3KPP3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May regulate the intracellular trafficking of RAN. Promotes guanine nucleotide release from RAN and inhibits binding of new GTP. Plays a role in the regulation of the levels of GTP-bound RAN in the nucleus (By similarity). Required for normal expression of the ion channel hcn4 and for normal expression of the cardiac transcription factors nkx2.5, gata4 and hand2 during embryonic development. Required for normal embryonic heart development and normal heart rate.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD47}. Cell membrane {ECO:0000250|UniProtKB:Q9HD47}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HD47}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9HD47}. Note=May shuttle between the nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q9HD47}.
Interaction partners:
- Adhesion G protein-coupled receptor D1
- GTP-binding nuclear protein Ran
- Sodium channel regulatory subunit beta-3
- Sodium channel subunit beta-2
Sequence:
MSRPLFGGALSAVFPSSVMDISELRQIPDNQEVFAHSQTDQSIIIELLEYQSQVQDADAARYHFEDVAGSNKAIENGTWEVRVVEQVPQSEISMQECSSAWLLSGAQLVSKFNEEAKNTVNVHQCLFRLPQFTTDILMTFNDPVFINPLSSSAAGNMEAIPWTLQDFQGVLQSLRLLDSGVFG