wanglab/gogpt-training-data huggingface dataset:
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1 (A0A8I6AJE1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAARAGFQSVAPSGGAGASGGAGVAAALGPGGTPGPPVRMGPAPGQGLYRSPMPGAAYPRPGMLPGSRMTPQGPSMGPPGYGGNPSVRPGLAQSGMDQSRKRPAPQQIQQVQQQAVQNRNHNAKKKKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRLDIQEALKRPIKSALSKYDATKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTATTQETDGFQVKRPGDVNVRCTVLLMLDYQPPQFKLDPRLARLLGIHTQTRPVIIQALWQYIKTHKLQDPHEREFVICDKYLQQIFESQRMKFSEIPQRLHALLMPPEPIIINHVISVDPNDQKKTACYDIDVEVDDTLKTQMNSFLLSTASQQEIATLDNKIHETIETINQLKTQREFMLSFARDPQGFINDWLQSQCRDLKTMTDVVGNPEEERRAEFYFQPWAQEAVCRYFYSKVQQRRQELEQALGIRNT
Protein: Fatty acid-binding protein, brain (Brain lipid-binding protein) (BLBP) (Brain-type fatty acid-binding protein) (B-FABP) (Fatty acid-binding protein 7) (P51880)
Organism: Mus musculus (Mouse)
Function: B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers.
Subcellular location: Cytoplasm.
Interaction partners:
- Nestin
- Glial fibrillary acidic protein
- Excitatory amino acid transporter 1
- Paired box protein Pax-6
- Transcription factor HES-5
- Tubulin beta-3 chain
Sequence:
MVDAFCATWKLTDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGGKVVIRTQCTFKNTEINFQLGEEFEETSIDDRNCKSVVRLDGDKLIHVQKWDGKETNCTREIKDGKMVVTLTFGDIVAVRCYEKA
Protein: DNA-directed RNA polymerase III subunit rpc31 (RNA polymerase III subunit C31) (DNA-directed RNA polymerase III 31 kDa polypeptide) (Q8WZJ8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit rpc5
- DNA-directed RNA polymerase III subunit rpc3
- Probable DNA-directed RNA polymerase III subunit rpc6
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase III subunit rpc8
- DNA-directed RNA polymerase III subunit rpc4
- DNA-directed RNA polymerase III subunit rpc9
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase III subunit rpc1
Sequence:
MRRGARGSTNLGGMTWQEVLEFNANSTPTKLYPDRDIPLQRSIRPEELLELRFYKEIRTSFLDESAFYIRRNPISVVQRNEDGLVRYSDRNKPKRKNDNLSLSDLDLDPKFFPEELRKTLGAASATGRKRARRKLDMKTFIDFTIKAQDLKDESSEAAHPNIEEEPDEGLEEEDEDFGDDDDNDYGENYFDNGEGDDYDDYDGDEGAIYE
Protein: DNA primase large subunit (DNA polymerase subunit beta) (Suppressor of fat facets 240) (Q9VPH2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulatory subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which play an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit PolA1, an accessory subunit PolA2 and two primase subunits, the catalytic subunit Prim1 and the regulatory subunit Prim2) is recruited to DNA at the replicative forks (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity). In the primase complex, both subunits are necessary for the initial di-nucleotide formation, but the extension of the primer depends only on the catalytic subunit. Stabilizes and modulates the activity of the catalytic subunit (By similarity).
Interaction partners:
- DNA polymerase alpha catalytic subunit
- DNA polymerase alpha subunit B
- DNA primase small subunit
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon catalytic subunit 1
- Replication factor C subunit 3
- DNA polymerase epsilon subunit 2
- DNA polymerase delta subunit 2
- DNA replication licensing factor Mcm2
- Proliferating cell nuclear antigen
Sequence:
MEFGLKKRARHEVKVEVASLETKYPHNVMLYHYPPTEDVHIDEFEELALERLRLLRVLDRASTRNLRVLSDEWKEIVSADLTREGLRSYLRLCSTGGSAKHEADIQTRRRDYLSHFILRLAYCRSEDLARWFVAREMELFRYKFAALSSFEVKQFLEANGFEIHPLTEAQKDEVKDGLYESTVGQSVAKIELLDFYKVPFTQVLDLVRGRRCFLKAGYAYVNTHDLVSLVGTKQQDEIEQGLQAAKTMVEDVEADERISRTLKALHNSYTGRDYTVCRDAAVPIESLDQLSKTSMPLCMRMCHEHIRANHHIKHSGRMQYGLFLKGIGVALEDSLRFWREEFTKKMDADKFTRSYEYNIYHNYGKKGSMVNYTPYSCAKIIKDVAGPGDCHGCPYKNMDQGSLKTKLSSYGLSASAIDEVMFFVSRGHYQIGCGKYFQLTHNSPVEPSINHPNNYFEESQIAMGNRQKRANGSAPPKARIRPDIKGHGDRSMLMGDDDDELWRIAETQERIMQSQKDISEAFNDDLDLTQIDY
Protein: Ion_trans_2 domain-containing protein (B2MZB8)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MHDEDNQLGELLARRKASPNGISPAPSTQQILEEVARMQYGEKKNIKHKLQQWFIENPSISARIRSCNVLIKLLTCILYCIRVVNDERSYPDDFPFSEEEAGKQDVTLYKYLLWVDFDFKIWFLQTMFACISMVYTILVFYLSYSGSVVRLLINIHFLLELITSFPFIISIFIPSLTYLYVPVFLNCWLAKGALQAMMNDLNRKSFISSSALFRQLLLLFSVLACLIFTGMCSIEHLQRARGKRIDLFTSFYFVMVTFSTVGYGDWYPDYWASQLCVVILICVALGLIPKQLDELGQTWSERQKSGTDFSSWNGVESHVVVTITTLEVEFIRDFLEEFYAHPENQRIQIVLLSPAELDNQTRMLLKIPLWNNRVHYVRGSSLRDEDLERANVATSKACFILSARHVNRKVATDEHTILRSWAIKDFAPNVKQYVQIFRAETKMHIEHAEVLICEDEFKYALLANNCICPGISTFITLLMHTSRGEEGQKSTEPWHKVYGFHSGNEMYQIKVQDSKFFCEYVGKSFSSTSFHAHKEYGIGLIAVSPDGDTSRMKLNPGSSHIIQPTDTVYYMGLTNEESLTDFRKGIRSQQKRANVASTIANIGTVAVDVPRSDKTELVGRKKKKRKEKAADEIHLIEVGEHVQSSRRPSIAMVTEGKIDSSSDSDQEEICDKCRGPCIQHKLQRTYPQVRTYIGTSNTVCHMMKERRSLCCLKLDEKCAHKSATSAHEYQWRNRPIILAADRTSSGMYNLVIPLRAYYRPVHDLHPIIILLELEEQDSLNDAFLDAISYFPDVYWMKGKVGNLDCLLRAGVSSAEHVVVVKETAVMAEEHTADCNTIITVQKIHRMFPRLRMITELTHATNMRFVQFNPHNAYSLAQSRFEKKERKRGSHMPFMFRLPFAQGGVFSANMLDRLLYQAIIKPFVVDLVRLLLGIDQHSDGGYLTSFVITSDDLWIRNYGRLYQKLCSSVADIPIGIFRTKKMDTKTVSLDLQEQCKDFENTEMGRNKDMYDHVKNRMRLLNIKDTHTFNWKYASRCRSTVLEGSDEKSQISYVIINPAQDLELESGDIVYVIRSPIRKDATNARINPRRGLRRSKNVSETIDSTNQVPTIVIDENNL
Protein: Protein MOS2 (Q9C801)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for innate and induced resistance to pathogens such as compatible and incompatible isolates of P.syringae and P.parasitica.
Subcellular location: Nucleus {ECO:0000269|PubMed:16271871}.
Interaction partners:
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH6
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH8
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH1
- At1g31870
- G patch domain-containing protein TGH
- Peptidyl-prolyl cis-trans isomerase CYP57
- Cell division cycle 5-like protein
- Peptidyl-prolyl cis-trans isomerase CYP65
- Protein pleiotropic regulatory locus 1
Sequence:
MKLSFSLPSKSKPKVTATTADGNNAVDDGTSKEFVTEFDPSKTLANSIPKYVIPPIENTWRPHKKMKNLDLPLQSGNAGSGLEFEPEVPLPGTEKPDNISYGLNLRQKVKDDSIGGDAVEERKVSMGEQLMLQSLRRDLMSLADDPTLEDFESVPVDGFGAALMAGYGWKPGKGIGKNAKEDVEIKEYKKWTAKEGLGFDPDRSKVVDVKAKVKESVKLDKKGVGINGGDVFFVGKEVRIIAGRDVGLKGKIVEKPGSDFFVIKISGSEEEVKVGVNEVADLGSKEEEKCLKKLKDLQLNDREKDKKTSGRGRGAERGSRSEVRASEKQDRGQTRERKVKPSWLRSHIKVRIVSKDWKGGRLYLKKGKVVDVVGPTTCDITMDETQELVQGVDQELLETALPRRGGPVLVLSGKHKGVYGNLVEKDLDKETGVVRDLDNHKMLDVRLDQVAEYMGDMDDIEY
Protein: Chaperone protein ClpB (Q9RA63)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MNLERWTQAAREALAQAQVLAQRMKHQAIDLPHLWAVLLKDERSLAWRLLEKAGADPKALKELQERELARLPKVEGAEVGQYLTSRLSGALNRAEALMEELKDRYVAVDTLVLALAEATPGLPGLEALKGALKELRGGRTVQTEHAESTYNALEQYGIDLTRLAAEGKLDPVIGRDEEIRRVIQILLRRTKNNPVLIGEPGVGKTAIVEGLAQRIVKGDVPEGLKGKRIVSLQMGSLLAGAKYRGEFEERLKAVIQEVVQSQGEVILFIDELHTVVGAGKAEGAVDAGNMLKPALARGELRLIGATTLDEYREIEKDPALERRFQPVYVDEPTVEETISILRGLKEKYEVHHGVRISDSAIIAAATLSHRYITERRLPDKAIDLIDEAAARLRMALESAPEEIDALERKKLQLEIEREALKKEKDPDSQERLKAIEAEIAKLTEEIAKLRAEWEREREILRKLREAQHRLDEVRREIELAERQYDLNRAAELRYGELPKLEAEVEALSEKLRGARFVRLEVTEEDIAEIVSRWTGIPVSKLLEGEREKLLRLEEELHKRVVGQDEAIRAVADAIRRARAGLKDPNRPIGSFLFLGPTGVGKTELAKTLAATLFDTEEAMIRIDMTEYMEKHAVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVILFDEIEKAHPDVFNILLQILDDGRLTDSHGRTVDFRNTVIILTSNLGSPLILEGLQKGWPYERIRDEVFKVLQQHFRPEFLNRLDEIVVFRPLTKEQIRQIVEIQLSYLRARLAEKRISLELTEAAKDFLAERGYDPVFGARPLRRVIQRELETPLAQKILAGEVKEGDRVQVDVGPAGLVFAVPARVEA
Protein: Arabinogalactan endo-beta-1,4-galactanase A (EC 3.2.1.89) (Endo-1,4-beta-galactanase A) (Galactanase A) (Q5B153)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- tRNA-specific adenosine-34 deaminase subunit Tad3, putative
- Flavoprotein, putative
Sequence:
MILSSLLPLSLVTLTSAALTYRGADISSLLIEEDSGVAYKNLNGETQAFELILANNGVNSIRQRIWVNPSDGSYNLEYNLELAKRVQDAGMSVYLDLHLSDTWADPGDQATPSGWSTTDIDTLAWQVYNYTLDVCNTFAENNVAVEIVSIGNEIRNGLLHPLGSTDHYDNIARLLHSGAWGVKDSSLSTTPKILFHLDNGWDWDAQKYFYDTVLATGTLLSTDFDLIGVSYYPFYNADATLSSLKTSLTNLKSNYGKNVLVVETDWPVQCSSPEYAFPSDLSSIPFSADGQETFLGRLADTLEDVGGVGIYYWEPGWVDNAGLGSSCEDNLMVDWRDRTVRESISVFGDL
Protein: 22.0 kDa heat shock protein (AtHsp22.0) (Q38806)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum {ECO:0000305|PubMed:7870826}.
Interaction partners:
- 23.6 kDa heat shock protein, mitochondrial
- Heat shock protein 90-1
- Heat shock 70 kDa protein 5
- Protein HEAT-STRESS-ASSOCIATED 32
- 23.5 kDa heat shock protein, mitochondrial
- Chaperone protein ClpB1
- Heat shock 70 kDa protein 4
- L-ascorbate peroxidase 2, cytosolic
- Heat shock protein 21, chloroplastic
- Heat stress transcription factor A-2
Sequence:
MMKHLLSIFFIGALLLGNIKTSEGSLSSALETTPGSLLSDLWLDRFPDPFKILERIPLGLERDTSVALSPARVDWKETAEGHEIMLDIPGLKKDEVKIEVEENGVLRVSGERKREEEKKGDQWHRVERSYGKFWRQFKLPDNVDMESVKAKLENGVLTINLTKLSPEKVKGPRVVNIAAEEDQTAKISSSESKEL
Protein: Grunge, isoform A (Q8IQA6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASTQGEIRVGPGHQVNDVYAKLPDYNPISSFPIDKETDERELEESRWSPGVVADGDLLMFLRAARSMAAFQGMCDGGLEDGCLAASRDDTTINALDVLHDSGYDPGKALQALVKCPVSKGIDKKWTEDETKKFIKGLRQFGKNFFRIHKDLLPHKDTPELVEFYYLWKKTPGANNNRPHRRRRQSALRRNRVTRANNSNSNTPPKKEDTPEPQTATTATAAATAASETASRSSPAVSKEENSSLTEDDASECDSDSSLTHKRDESPSRMRTRNKQQNNNSSTSSGNNTAGNGGGNATSISSGSTGGGAAGGNSSSKDQSANAVANGKRPKRGSETPDVSGGASVDSPKTPTKAVAESSANKRKGGKQDTPNKKKRTEQESNEPSAHEENAIKEKRKRPDSPVESMNSDSRPDSVLDDGESNTTDTTTAEQQSTKDSKETVSCKEEREMVTNDLEAKAEEKAIKAEALAEDSKDSAIKNMDEETNIQAPSSADTSLVDGPNPNALPSPVAAPITMKVPTIATVEALNASVDRKEAIEKMESCDSDPEMLKKLATIKQEVSPQQQQHMQQQSQQQMQQQLAPVGIPQPPSCPPSESVYIKKEPMEDSMDATCNQNSNEPQDLKVKIEIKNEDALKHSAGGLPPSGPCAPPSALHPLSGAPVESGQEPLHLQHMPHGQVTTQPPPGYLIDGQLKYGPSGQGVPPQPPQLHSDAAGGVSGAPPGAPTTPQKYPPEMEMKFAPQDLKYPPPPPLDALKYSQEMQAAAAAAAAAGKYDMKYMMEQQGKYNVELSAAHQPPSKPGYQDSLKIPDIKPGFGHLPHNVGSPLDAAHKYGPPPTSQESQQQQPQPPAHQVPPGATPPPGIAMPKPHYQHDVQTPPLGRPFEPTGLMLKYGDPLAAKYGPPQDLKYPMPPVSQAGPADVKPYGGENLIKSSPYGPPPESPIDASARSTPGQDSQGSNSNSQPPSMPPQPQQFQSPHPSPHMPSPAGGGLPPGMHPQNLIHGPPPGAAGGSGPQPPPPPTSLHQPTPTSAGPPSLQHGLHPGHQHSQLSVASSIPPSSIGIPPTLSTMAPSHMHPHLHPHAHLQGLHRPHDLPPSMHPHAPMPLSLQGHPQHGHGLPPSHTSQQQQQQQQQQQPGGPAGTVRTPSPAQQPPRSMHDPQSSREPPTSQPSTTMAGSSGPGGPPPQQSPHAHRTSPLPGLAGSGPPPPGLIGHPMAIHPHLAHLPPGHPAHAALAHPGHHLLSHSIAGLGPGGGPIALLAGPGGLGGIPESALSRRTPPSHLPHSHASSAPLTAHSVASMTSTSMSLTTSTVPSSAFSRASPSVQISSSGGGPSGPGSVGPGGMPNSSAAAAAAAAAHRAASPASSVSSLSRQSPLHPVPQSPLSHHPSSSALSAAAAAVAERDRHALMRQQSPHMTPPPVSNASLMASPLSKMYAPQPGQRGLGTSPPPHLRPGASPPVIRHPQMPLPLPLIAPGGGIPQIGVHPGQSPYPHPLLHPSVFYSPHHHPFNSPYGYAPYGPGFPAYMKPPPQPGQLDPAAVMAAHHAGLQGPPPQQMRQDEQNAAAAAAQAAAEKQHQAAAAAAAQQHKAPQQQQPGGMPPNKPPTPKTPQGPGGGMPPGMGGPGTPTGLPPGAYPGSHMPGYPQGPPHGSPFAPQDGQPHGLKPTSHMDALRAHAHSANSAGMGGGHHPTEPLPIDIEPDPEPEIPSPTHNIPRGPSPEAKPDDTECHRSQSAIFVRHIDRGDYNSCTRTDLIFKPVADSKLARKREERDRKLAEKERERRQQQQQQQQQQQQQQAAAAQQAAQQAKMKAELKPPYADTPALRQLSEYARPHVAFRELEEIKNAQAAAASQSRLDPHWMEYYRRGIHPSQFPLYANPAISQMERERLGIPPPHHVGLDPGEHMVRMPQPPEAGFQLPPNVGQYPRPNMLIPREPHSDVLLRMSYADQLQAAEFQRQSLHDQYFRQRPR
Protein: Transcriptional and immune response regulator (Q9D915)
Organism: Mus musculus (Mouse)
Function: Seems to be involved in the regulation of cell growth an differentiation, may play different and opposite roles depending on the tissue or cell type. May enhance the WNT-CTNNB1 pathway by relieving antagonistic activity of CBY1. Enhances the proliferation of follicular dendritic cells. Plays a role in the mitogen-activated MAPK2/3 signaling pathway, positively regulates G1-to-S-phase transition of the cell cycle. In endothelial cells, enhances key inflammatory mediators and inflammatory response through the modulation of NF-kappaB transcriptional regulatory activity. Involved in the regulation of heat shock response, seems to play a positive feedback with HSF1 to modulate heat-shock downstream gene expression (By similarity). Plays a role in the regulation of hematopoiesis even if the mechanisms are unknown. In cancers such as thyroid or lung cancer, it has been described as promoter of cell proliferation, G1-to-S-phase transition and inhibitor of apoptosis. However, it negatively regulates self-renewal of liver cancer cells via suppresion of NOTCH2 signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24937306}. Nucleus {ECO:0000269|PubMed:24937306}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NR00}. Nucleus speckle {ECO:0000250|UniProtKB:Q9NR00}. Note=Localizes in nucleus speckles in presence of CBY1. Translocates to the nucleus upon cellular stress such as H(2)O(2). {ECO:0000250|UniProtKB:Q9NR00}.
Interaction partners:
Sequence:
MKAKPSHQATSMSSSLRVSPSIHGYHFDTAARKKAVGNIFENIDQESLQRLFRNSGDKKAEERAKIIFAIDQDLEEKTRALMALKKRTKDKLLQFLKLRKYSIKVH
Protein: Probable electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF) (Altered inheritance rate of mitochondria protein 45) (Q12480)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Probable electron transfer flavoprotein subunit beta
- Probable electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
- DASH complex subunit SPC34
- Succinate--CoA ligase subunit alpha, mitochondrial
- D-lactate dehydrogenase [cytochrome] 1, mitochondrial
- Acetyl-CoA acetyltransferase
- 3-ketoacyl-CoA thiolase, peroxisomal
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2
- D-arabinono-1,4-lactone oxidase
- Small ribosomal subunit protein mS47
Sequence:
MFKSLAAVLPRASKAKFLQKNYASTLAFIESSKDGSVSRSSLSLLAAAQKLSNPITAVITGSKAEKTAEALKSSYSCSNLEKLVIFEDSKLDTCLPEQLTPLLVKLLKGGDYSHFVVSNSSVGKSVLPRVGALLDVQPVCEVTVIKDPKTFIRPIYAGNIISTIECQAEKKLLIIRASAFPPIAEGSMDSVTIEKRTDIPPCDLNVTWVKTILTKSERPELTSAQNVVTGGRALKDKETFEKLLSPLADVLHAAIGATRASVDNGLCDNSLQIGQTGKVVAPNLYIAIGVSGAVQHLAGMKDSKVIVAINNDPDAPIFNVADYGLQGDLYKIVPELTEKLGKYK
Protein: Endo-1,6-beta-D-glucanase neg1 (EC 3.2.1.75) (Beta-1,6-glucanase neg1) (Glucan endo-1,6-beta-glucosidase neg1) (Q4WBR2)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Endoglucanase that has highest activity on the linear beta-1,6-glucan pustulan and lower activity against laminarin (beta-1,3-glucans with beta-1,6-branches). Is active on C.albicans cell walls allowing the release of a previously described cell wall proteins.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRISVGALLGLTALSHATTEKRAASASAYCSNSAGNYKLSSIAAPVQGAGNPGSESTWQLTVDDTSSGHKQTIVGFGAAVTDATVTSFNTLSASVLQDLLNKLMTPAGANFALMRHTIGASDLSGDPAYTYDDNGGKADPSLSGFNLGDRGTAMAKMLATMKSLQPNLKILGSPWSAPGWMKLNGVLDGNTNNNNLNDGYLTSGGTGSTGYASQFAQYFVKYIQAYKNLGAHVDAITIQNEPLFSSAGYPTMYVYDYESAQLIQNYIGPALASAGLDTEIWAYDHNTDVPSYPQTVLNQAGQYVKSVAWHCYAPNVDWTVLSQFHNTNPGVKQYMTECWTPASGAWHQAADFTMGPLQNWASGVAAWTLGTNAQDGPHLSTGGCATCQGLVTINNGGYTLNTAYYMMAQFSKFMPPGAIVLNGSGSYTYSGGGGIQSVASLNPDGTRTVVIENTFGNDVYVTVTMKSGQKWSGNAPSQSVTTWVLPSA
Protein: Perilipin-1 homolog (Lipid droplet-associated protein) (A8WHP8)
Organism: Caenorhabditis elegans
Function: Lipid droplet-associated protein which plays a role in lipid droplet clustering.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:26025681, ECO:0000269|PubMed:26121959, ECO:0000269|PubMed:26357594}.
Interaction partners:
- TAR DNA-binding protein 43 N-terminal domain-containing protein
- Abhydrolase domain-containing protein lid-1
Sequence:
MTDVEQPVSVEDQQAQAQSYYDQVLGNAYVQTAINAYTKTKEFHPLLNSTLNSAEEKVSTVGNYAAQKAYDGYNSYYVKPKNTAYEAVSYGTERAKTAVESGKQAAIVGGTFGIGAAVVLTQFSLALSAGGAALVLEQVDSAKKLGSSAISTIKEAELAVEHRIFSALHQAQRIAMVPVEKITENTNSLLDILDGAVQKGLNIEVPPSVNLTIGQRVKNLASLIVQGVSNKLFKAHDHVIDPINERARNYLEQLSQSFVLLDIVREKKTWVIEKSNELSTSVFDFKKTLEEEAQKYKVAPEEMLMKHIQSTSEQLSTQLQSLREKGQNVFGDGTKIDSTIDYLENLKKNFTDAEDVYKVRDEVLNEGRQRIAELSTWTTSLLIISAEWQFEPEDLLIEELYFDAPPPVRTRNLYRNRA
Protein: SAGA-associated factor 29 homolog B (AtSGF29b) (29 kDa SAGA-associated factor homolog B) (Q500Z7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chromatin reader component of the transcription regulatory histone acetylation (HAT) complex SAGA.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SAGA-associated factor 11
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10
- Ubiquitin C-terminal hydrolase 22
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- Transcription initiation factor TFIID subunit 12b
- Transcription initiation factor TFIID subunit 12
- Transcription and mRNA export factor ENY2
- Transcription initiation factor TFIID subunit 6
Sequence:
MSSPDIVGILENTKELDRLRKDQEEVLVEINKMHKKLQASPEIVEKPGDISLAKLKNLYIQAKELSENEVTVSNILLTQLDLLLPYGPTGQQRRKLGVVAEGNDQKRKRMKVDSDVIRLSPSMRNQIEAYASLKGEQVAARVTAESADKDEWFVVKVIHFDRETKEVEVLDEEPGDDEEGSGQRTYKLPMLCILPFPKRNDPSNTQEFPPGKHVLAVYPGTTALYKATVVSTPRKRKSDEYLLEFDDDEEDGALPQRTVPFHKVVALPEGHRQ
Protein: Alkaline phosphatase (EC 3.1.3.1) (Q9W274)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Alkaline phosphatase
- 6-pyruvoyl tetrahydrobiopterin synthase
- GTP cyclohydrolase 1
- IP06402p
- Thiamine pyrophosphokinase 1
Sequence:
MHISQRRCLYPIFLFLLAFVGTALGRVQEVHNVLELTGQKASKLRFSTDVATGKYTPPEEMDPQFWYKLADEEIAKRLQLPQPNSDRAKNVIMFLGDGMPISTVTAARILKGQRQGNTGEESSLSFEKFPYSGLSRTYCANAQVPDSACTATAYLCGVKTNIINIGVSAAVNFNNCTASQDPANRLTSIAEWAQNAGKSTGFVTTTTLTHASPSGAYAKTANRMWQSDTDVTSYGVDASTCVDMATQLVTQTPGKNFEVMFGGGMGKFLPKTTKDSHGKYGERSDGVNLLSRWQGLHDKGVLVTNRKQLLNLDVSAASSIIGTFQSGLMDFHMDADPTYQPTLSELTEVAIKKLSHNENGYFVFIEGGLIDYGNHYTQAGYALDEALEFEKAIQLAREMTNISDTLIVVTADHGHAVSIAGYPGRGTPILGLNQHDTDINGVKYSVLNYAAGPNQYLDEHGQRIPLDDILGPDDAISPSYIDKEIGVHSGEDVGIWASGPQSHLFTGVMQQSTIPHLMAYASCVGSGKQVCGSSGRKT
Protein: Large ribosomal subunit protein eL6A (60S ribosomal protein L6-A) (L17) (RP18) (YL16) (Q02326)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein uL6A
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein uL13B
- Small ribosomal subunit protein eS24A
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS9A
Sequence:
MSAQKAPKWYPSEDVAALKKTRKAARPQKLRASLVPGTVLILLAGRFRGKRVVYLKHLEDNTLLISGPFKVNGVPLRRVNARYVIATSTKVSVEGVNVEKFNVEYFAKEKLTKKEKKEANLFPEQQNKEIKAERVEDQKVVDKALIAEIKKTPLLKQYLSASFSLKNGDKPHMLKF
Protein: Integrin subunit alpha L (A0A8I5ZT41)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
SLPGVNAWSYNLDTRHAQSFLTQAGRHFGYQVLQFGDGVVVGAPGEGNSTGSLYHCHPSSGSCQPVHLGSNHTSKYLGMTMVTDAAKGSLLACDPGLSRTCDQNPYLSGLCYLFSQSLGKPILQNRPAYQECMKGNVDLVFLFDGSQSLDKKDFEKIVDFMKDVMRKLSNTSYQFAAVQFSTECKTEFTFLDYIKLNKNPDVLLGNVTPMFLLTNTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNGNIDAAQDITRYIIGIGKHFSTTQKQEKLHIFASKPVEEFVKILDTFEKLKDLFTDLQRKIYAIEGTSKQDLASFNMELSSSGISADLSKGHAVVGAVGAKDWAGGFLDLHEDLEGATFVGQEPLTSDERGGYLGYTVAWLTSRSSRPLLAAGAPRYQHVGQVLLFQAPEAGGHWNQTQKIEGTQIGSYFGGELCSVDLHQDGETDLLLIGAPLFYGEQRGGRVSVYQRRRSLFEMVSELQGDPGYPLGRFGAAISALTDINGDGLTDVAVGAPLEEQGAVYIFNGKPGGFSSQSSQRIPGTQVSPGVRWFGRSIHGVKDLGGDRLADVVVGAEGQVIVLSSRPVVDIVTELSFSPDEIPVHEVECSYSASQEQKEGVKLKVCFQIRPLTSQFQGRLLANLSYTLQLDGHRTRSRGLFPGGSRELGGNTSVTPDKSCMDFHFHFPICIQDLISPINVSLNFSLLEEEGSPRDQKGGRDMQPILRPSIHAVTKEIPFEKNCGEDKKCEADLALSPPARSSVKRLHPWAVSTRRGTSFSKKASELFMLMTLQVMFNTLLNSSWGDFVELNGTVHWPRGFLGSGLHPFNTLSFHVSLHSQENSTLYISFTPKGPKTQQVQHIYKVRIQPSAYDHNMPALEALVEVPQPHSEGPIAHTWTVHTDPLVTCHREDLKKPTREAEQPCLPGVQFRCPIVFRQETFIRVAGTVELSEKIKVAPSRSCEVLRVGWLSRPQLALLPQVLMKVDMIYEKEMLHLYVLSGIGGLLLLSLIFLALYKVGFFKRKLKEKMEADGGVPNGSPGEDADPLAVPGEETKDMGCLEPLRESDKD
Protein: Bowman-Birk type proteinase inhibitor B4 (HOSPI-B4) (C0HLT0)
Organism: Hyacinthus orientalis (Common hyacinth)
Function: Serine protease inhibitor. Inhibits trypsin (Ki = 110 nM) and very weakly inhibits chymotrypsin (Ki =1200 nM). Does not inhibit bacterial subtilisin.
Interaction partners:
Sequence:
GQQPLCNDCFACARSLCICGDLVPQCHEGCQQCEKVDTLSGKPLYQCRSFEDYQCAN
Protein: IP13724p (Semaphorin 2b, isoform B) (Q29QV5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPLNAQLKIAQSVNKVTYAKVSDSNCCAKKQQKYSIADFSQAKRQAGSMCATGKGKHRLCSLSALLLVLVAQTVHVEYARADYENTWNLYYEPPCCTGSSAAHHLRHHKEHVQDFSCGPLHYKTFYMDERNNALYVGAMDRIFRLNLRNISQSICERDVLILEPTGSDILNCVSKGKREKVECRNHIRVIQPMNFNGQKLYVCGTNAHNPKDYVINANLTHLPRSQYVPGIGLGIGKCPYDPADNSTAVYVENGNPFGLPALYAGTNAEFTKADSVIFRSDLYNLTNGRKEANFKRTVKYDSKLLDKPNFVGSFEIGEFVYFFFREHAVEYINCGKAVYSRVARVCKNDRGGKYMISQNWATYLKARMNCSISSEFPFYFNEIQSVYKMPTDDTKFYATFTTNTNGLIGSAVCSYDIRDINAAFDGKFKEQATSNSAWLPVLNSKVPEPRPGTCHNDTATLPDSVLNFIRKHPLMDKAVDHEFGNPVFFKRDVILTKLVVDKIRIDKLNQEFLVYFVATTSGHIYKIVQFMHYGQRHSNLVDIFEASPHSEPIREMTLSHKTGSLYVATDHQVKQIDIAMCARRYDSCFRCVSDPYCGWDKDVNACRPYQLGLLQDVANETSGICDTSVLRKKVTSSYGQTLHLSCFVKMPEVLRKKQTRWYHHSTEKGRYEVRYTPTKYIDTNEGGLVLLAVNEGDGGRYDSYLDGTLLCSYGVTVDAHRCSPPSQKQDYQKIYSHWCNEFEKYKSAMKQWQAKQEQCGLKDKTGPISSNGKHVNDVFSNDALV