wanglab/gogpt-training-data huggingface dataset:
Protein: Kinase superfamily with octicosapeptide/Phox/Bem1p domain-containing protein (Q9LRY7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein
- Leucine-rich repeat protein 1
Sequence:
MSDRWARQNAERPATTLAERRNVNKNVSLQTGEEFSMEFLKDHTPVQSPIVAGRTHNDVHRFGDLYYQNQPQGYDSAARFHELRRIESECPSDAYDFGRDPRSTIRLENGGYMPHFNAYHNVGCDKEVITRKAFGEINSNRGDVTGMSAPCVFLPERTQSNNFTGGGGDFDRFGKVKFLCSFGGRIMPRSTDEKLKYVGGETHIISIRKNLSWEELKKKTSAICQQLHSIKYQLPGDELDSLISVSSDEDLQNMIEEYNGLERLEGSQRPRLFLIPIGEPERKAQQNIPDCQYAAALNCNADPNPRNISDGQTLAGDSRYHINNLDRNPSFCKRTPGQMLRLDATAMRPNPLFNGVQYNMASYPSPPVSPSPFQQRDSNGAYSQFHGNNSSSESNNSFTPAQQDTSIFEVIDSKYHQQRPLPSVNYQSNKQEAENLYGIQFQNGFNDKPVTPNLGHVDNLCFNPERSANNGRVFYDKVSMPEESKVSFSGSTNSNDSCLGIPHSYSDSTLEITGGHSSYFSQERQQSPSSTLNFTKKQTQEKQVQVHRNNDLADRRTQSDILDMKSTEGGETMFKFSPSPRGPRLSGENKTLHIDISAAGNHYDEIYLNQETKNQGGNSDTIFHLGGKVLGTRAMPTDMEGKKLPIYGNQTSVVVDPWKQIKQDNERLMAGAGTSSANLISLEEGIAANTPNEEPESRAARERNLEVSGIFISKRVVSDENFLFSIASESPNSKIVHETQKNRTEREGGLGHVRIPIMDLNQPAPATASETYSLKTPREDSPQSIPHAKITSGDTIFLSEEAEANTGQKENSFKDTLFVEMEASVYGLQIIKNADLEDLTELGSGTYGTVYHGTWRGTDVAIKRIRNSCFAGRSSEQERLTKDFWREAQILSNLHHPNVVAFYGIVPDGTGGTLATVTEFMVNGSLRHALLKKDRLLDTRKKIIIAMDAAFGMEYLHSKNIVHFDLKCENLLVNLRDPQRPICKVGDLGLSRIKRNTLVSGGVRGTLPWMAPELLNGSSTRVSEKVDVFSYGISLWEILTGEEPYADMHCGAIIGGIVKNTLRPPIPKSCSPEWKKLMEQCWSVDPDSRPPFTEITCRLRSMSMEVVTKSKRRENKP
Protein: C5a anaphylatoxin chemotactic receptor 1 (C5a anaphylatoxin chemotactic receptor) (C5a-R) (C5aR) (Q6UNA4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14628104}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21730}.
Interaction partners:
Sequence:
MDDMCSILTEEELSLYNITDCEFVKPGGLGPVLGPRHLSALVFYGLVFLLGVPGNALVVWVTGFRMPRSVTSLWFLNLALADLLCCLSLPLLMVPLAMDQHWPFGPVACKLLKGLLYLIMFCSVLLLVLISLDRFLLVSWPVWCQNWRRPRKAGWVCVGVWLLALLGSIPQFVYVKEVQLSTSKSECLGLYTVASAWANTTARFLVGFVLPFITIVTCHWVVYSRARRGSGVGPGRVSEARSRRTLRVIVAVSLSFFLCWFPLHILDFLVLSTPRHSSHSANIQLAHTLALCLAYCNSCLNPLLYVCLGRGFKQNINRSLRNMFNFATEESVTRQSMFKSTSERTQEMNM
Protein: Dynactin subunit 4 (A0A0S2Z5D5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000256|ARBA:ARBA00004529}. Cytoplasm, myofibril, sarcomere {ECO:0000256|ARBA:ARBA00004204}.
Interaction partners:
Sequence:
MASLLQSDRVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEMCQLF
Protein: Sulfate permease 2 (High-affinity sulfate transporter 2) (Q12325)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High affinity uptake of sulfate into the cell.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Sulfate permease 1
- Vacuolar basic amino acid transporter VSB1
- Homoserine O-acetyltransferase
- Sulfite reductase subunit beta
- Sulfate adenylyltransferase
- Sulfite reductase flavoprotein component
- Phosphoadenosine phosphosulfate reductase
- Adenylyl-sulfate kinase
- GTP-binding protein YPT1
- Uroporphyrinogen-III C-methyltransferase
Sequence:
MSREGYPNFEEVEIPDFQETNNTVPDLDDLELEYDQYKNNENNDTFNDKDLESNSVAKHNAVNSSKGVKGSKIDYFNPSDVSLYDNSVSQFEETTVSLKEYYDHSIRSHLTVKGACSYLKSVFPIINWLPHYNFSWFTADLIAGITIGCVLVPQSMSYAQVATLPAQYGLYSSFIGAYSYSFFATSKDVCIGPVAVMSLQTAKVIADVTAKYPDGDSAITGPVIATTLALLCGIISAAVGFLRLGFLVELISLNAVAGFMTGSAFNILWGQVPALMGYNSLVNTRAATYKVVIETLKHLPDTKLDAVFGLIPLFLLYVWKWWCGTYGPRLNDRYNSKNPRLHKIIKWTYFYAQASRNGIIIIVFTCIGWAITRGKSKSERPISILGSVPSGLKEVGVFHVPPGLMSKLGPNLPASIIVLLLEHIAISKSFGRINDYKVVPDQELIAIGVSNLLGTFFNAYPATGSFSRSALKAKCNVRTPLSGLFSGSCVLLALYCLTGAFFYIPKATLSAVIIHAVSDLLASYQTTWNFWKMNPLDFICFIVTVLITVFASIEDGIYFAMCWSCAMLILKVAFPAGKFLGRVEVAEVTDAYVRPDSDVVSYVSENNNGISTLEDGGEDDKESSTKYVTNSSKKIETNVQTKGFDSPSSSISQPRIKYHTKWIPFDHKYTRELNPDVQILPPPDGVLVYRLSESYTYLNCSRHYNIITEEVKKVTRRGQLIRHRKKSDRPWNDPGPWEAPAFLKNLKFWKKRENDPESMENAPSTSVDVERDDRPLLKILCLDFSQVAQTDATALQSLVDLRKAINQYADRQVEFHFVGIISPWVKRGLISRGFGTLNEEYSDESIVAGHTSYHVARVPQGEENPEKYSVYTASGTNLPFFHIDIPDFAKWDI
Protein: Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1) (Q60591)
Organism: Mus musculus (Mouse)
Function: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11030334, ECO:0000269|PubMed:24970700}. Nucleus {ECO:0000269|PubMed:11030334, ECO:0000269|PubMed:24970700}. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. The subcellular localization of NFATC plays a key role in the regulation of gene transcription.
Interaction partners:
- Transcription factor Jun
- Forkhead box protein P3
- Protein c-Fos
- Nuclear factor of activated T-cells, cytoplasmic 1
- Protein phosphatase 3 catalytic subunit alpha
- Calcineurin subunit B type 1
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Cyclic AMP-responsive element-binding protein 1
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Glycogen synthase kinase-3 beta
Sequence:
MDVPEPQPDPDGGDGPGHEPGGSPQDELDFSILFDYDYLNPIEEEPIAHKAISSPSGLAYPDDVLDYGLKPCNPLASLSGEPPGRFGEPDSIGFQNFLSPVKPAGASGPSPRIEITPSHELMQAGGALRGRDAGLSPEQPALALAGVAASPRFTLPVPGYEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNAGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVAPLPAASPQRSRSPSPQPSPHVALQDDSIPAGYPPTAGSAVLMDALNTLATDSPCGIPSKIWKTSPDPTPVSTAPSKAGLARHIYPTVEFLGPCEQEERRNSAPESILLVPPTWPKQLVPAIPICSIPVTASLPPLEWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPIECSQRSAHELPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKVNFYVINGKRKRSQPQHFTYHPVPAIKTEPSDEYEPSLICSPAHGGLGSQPYYPQHPMLAESPSCLVATMAPCQQFRSGLSSPDARYQQQSPAAALYQRSKSLSPGLLGYQQPSLLAAPLGLADAHRSVLVHAGSQGQGQGSTLPHTSSASQQASPVIHYSPTNQQLRGGGHQEFQHIMYCENFGPSSARPGPPPINQGQRLSPGAYPTVIQQQTAPSQRAAKNGPSDQKEALPTGVTVKQEQNLDQTYLDDVNEIIRKEFSGPPSRNQT
Protein: GID complex subunit 9 (EC 2.3.2.27) (Function required for yeast viability protein 10) (Glucose-induced degradation protein 9) (Probable E3 ubiquitin-protein ligase GID9) (P40492)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1). May catalyze ubiquitination of target proteins in complex with RMD5 (Probable). Required for survival upon exposure to K1 killer toxin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- GID complex substrate-recognition subunit 4
- GID complex subunit 5
- E3 ubiquitin-protein ligase RMD5
- GID complex subunit 1
- GID complex subunit 8
- GID complex subunit 7
- Fructose-1,6-bisphosphatase
- GID complex substrate-recognition subunit 10
- Protein yippee-like MOH1
- GID complex associated protein 12
Sequence:
MAEKSIFNEPDVDFHLKLNQQLFHIPYELLSKRIKHTQAVINKETKSLHEHTAALNQIFEHNDVEHDELALAKITEMIRKVDHIERFLNTQIKSYCQILNRIKKRLEFFHELKDIKSQNSGTSHNGNNEGTRTKLIQWYQSYTNILIGDYLTRNNPIKYNSETKDHWNSGVVFLKQSQLDDLIDYDVLLEANRISTSLLHERNLLPLISWINENKKTLTKKSSILEFQARLQEYIELLKVDNYTDAIVCFQRFLLPFVKSNFTDLKLASGLLIFIKYCNDQKPTSSTSSGFDTEEIKSQSLPMKKDRIFQHFFHKSLPRITSKPAVNTTDYDKSSLINLQSGDFERYLNLLDDQRWSVLNDLFLSDFYSMYGISQNDPLLIYLSLGISSLKTRDCLHPSDDENGNQETETATTAEKEVEDLQLFTLHSLKRKNCPVCSETFKPITQALPFAHHIQSQLFENPILLPNGNVYDSKKLKKLAKTLKKQNLISLNPGQIMDPVDMKIFCESDSIKMYPT
Protein: Centrosomal protein of 120 kDa (Cep120) (Coiled-coil domain-containing protein 100) (Q7TSG1)
Organism: Mus musculus (Mouse)
Function: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors and for proper positioning of neurons during brain development. Also implicated in the migration and selfrenewal of neural progenitors. Required for centriole duplication and maturation during mitosis and subsequent ciliogenesis. Required for the recruitment of CEP295 to the proximal end of new-born centrioles at the centriolar microtubule wall during early S phase in a PLK4-dependent manner (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17920017}. Note=Regulates the localization of TACC3 to the centrosome in neural progenitors in vivo. {ECO:0000269|PubMed:17920017}.
Interaction partners:
- Spindle and centriole-associated protein 1
- Protein TALPID3
- Centrosomal protein of 290 kDa
- Centrosomal protein of 164 kDa
- Centrobin
- Centriolar coiled-coil protein of 110 kDa
- Centrosomal P4.1-associated protein
- Centrosomal protein POC5
- Centrosomal protein of 135 kDa
- POC1 centriolar protein homolog B
Sequence:
MVPKSDQLLIVVSILEGRHFPKRPKHLLVVEAKFDGEQLATDPVDHTDQPEFATELAWEIDRKVLHQHRLQRTPIKLQCFALDPQTSAKETVGYIVLDLRTAQETKQAPKWYQLLSNKYTKFKAEVQISLTLETDTKAQVDSYKAKAAPPRDGKVLASLAGVDPKDIVAVLNEEGGYHQIGPAEHCTDPFILSVTIAFATQLEQLIPCTMKLPERQPEFFFYYSLLGNDVTNEPFSDLINPNFEPERASVRIRSSVEILRVYLALHSKLQIHLCCGDQSLGSTEIPLNGLLKKGSTEINQHPVTVEGAFTLDPPNRAKQKLAPVPLDLAPTVGVSVALQREGIDSQSLIELKTQNGHEAEHSQKRVLTPIKEKTLTGPKSPRESPAPPPPPNQTPPTKDDATESEVESLQYDKDPKPTVKGIGSVPASLAQPEATCGASEVVTSGQKIAVPAASHHFCFSVDLRSVHDLELSFPVNCILRYSYPFFGSAAPIMTNPPVEVRKNMEVFLPQSYCAFDFATMPHQLQDTFLRIPLLVELWHKDKMSKDLLLGVARIQLSNILSSEKTRFLGANGEQCWRQTYSESVPVIAAQGSNNRILDLSYTMTLEDYGLVKMREIFVSESSQGVPAVDQKPSSPPPAPCPSEIQMEPRETLEYKAALELEMWKEMQEDIFESQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYSILEGKLQKALTELETREQQLASAEAELQRERKELQLERERNLQELQDSVRRARDDCVYQVELERLKLKQLEEDKQRLQQQLNDAGNKYKTLEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKETVRTEQQELLDIRNELNRLRQQEQNQYQDCKEIASGKLGSPRGSGLEEGLDDYLTRLIEERDTLMRTGVYNHEDRIISELDRQIREVLTKNSAS
Protein: Cleavage and polyadenylation specificity factor subunit 5 (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) (Q9CQF3)
Organism: Mus musculus (Mouse)
Function: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7. Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (By similarity). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function. Binds to chromatin. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18032416}. Cytoplasm {ECO:0000250|UniProtKB:O43809}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm). In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles. {ECO:0000250|UniProtKB:O43809}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 7
- Cleavage and polyadenylation specificity factor subunit 6
- Pre-mRNA 3'-end-processing factor FIP1
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage stimulation factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 2
- Protein virilizer homolog
- Cleavage and polyadenylation specificity factor subunit 3
- Pre-mRNA cleavage complex 2 protein Pcf11
Sequence:
MSVVPPNRSQTGWPRGVNQFGNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDKIGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYN
Protein: RE16905p (Q8SZ50)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDETKDMRYSLEIDEDLRRPLEARAKKVLAVNSASQRTVNLGEDTMYEAGDLEHLDDGDDSFSAFERMCDKTGSDPDSTLFQYLHSEDRSQVMARARDHSTDDQKEIDALRRMLEAVGTEDDLLENESPVKGAECTHLEDIEAPSRFWDNTLAGMDETSSDSGLTPKALTKVSPVKMVGLLRPSTIIEDSELESSDVSSHTSFQSARTLKTNASSSYETATDTSLSGTLLNVDELFYAAIAKAKPPGMSKGEELELLSDLHGSLRELASLPKDEVEEEEDDIEDTIIELSSSDDEEVQLVPEVKQEDTSRVSSVHGKDHTEQKPAEKSVENKENSLHFNDTMEEMEYMMQKGMEYMAGGAPSVAAVKADCPVLPKTKQSTFVVSPKPEPKSPAVAFLQPSIPLRSSNQPQTVVGSSSTGRKPLNVGLTMEWTKKKFFSAASGIPQRRQNQIKQPYANIVSPIRTYTQKSGTAPLMSTFRPTSSDMLSTLAISELEQESRLCHPKALFAAKDETPKSSEAESLIINGIDSAADLLPKKAYISSEIKHVVDERTPLPMPKVPQIQKYLNSAVEPTVMRHDGKMKMPGEAVRNPSSSHIPRRANHSLADLSLASGDVSLYTIRDAQKF
Protein: Lectin 6 (MtLec6) (Agglutinin LEC6) (A9YWS4)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi.
Interaction partners:
Sequence:
MTLSSALIKIFITFLFLQNHVNSQYSSPSKPQPSLGSTISFSITKFDDESPNIFVKGDTSISNGVLSLTKTDKYSGKPLQKSVGHATHLTPIHIWDETSGELADFSTSFSFIVNTNGSSLHGDGFTFFLGPLHFDLPKNSSGGYLGLFNPETALIASQNPIVAIEFDSFTNGWDPASPSQYTHIGIDVGSIDSVSTADWPLNVLPRNALGEARINYNSESKRLSAFVDYPGLGESTGVSFVVDLRSVLPEWVRVGFSAATGELVETHDIINWSFEAAL
Protein: Peroxidase (EC 1.11.1.7) (Q8RVP5)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362060}.
Interaction partners:
Sequence:
MKTMGFVFLLLPFFAIGVVQGQLRVGFYSNTCPDAESIVSSVVRNAAQSISNIPPVLLRLHFHDCFVEGCDGSILIENGPKAERHAFGHQGVGGFEVIEQAKAQLEATCPGVVSCADIVALAARDAIALANGPSYEVPTGRRDGRVSDVSLAANMPDVSDSIQQLKAKFLQKGLSEKDLVLLSAAHTIGTTACFFMTKRLYKFSPAGGSDPAISPDFLPQLQSICPQNGDVNVRLPMDRGSERTFDKQILDNIRNGFAVLESDARLYDDETTRMVVDSYFGILTPIFGPSFESDFVDSIVKMGQIGVKTGSKGEIRRVCTAFN
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (Q4GZG4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase, putative
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Phosphoglycerate kinase
- Phosphoglycerate kinase
- Glucose-6-phosphate isomerase
- Phosphotransferase
Sequence:
MTLNEKKSINECDLKGKKVLIRVDFNVPVKNGKITNDYRIRSALPTLKKVLTEGGSCVLMSHLGRPKGIPMAQADKIRSTGGVPGFQQKATLKPVAKRLSELLLRPVTFAPDCLNAADVVSKMSPGDVVLLENVRFYKEEGSKKAKEREAMAKILASYGDVYISDAFGTAHRDSATMTGIPKILGNGAAGYLMEKEISYFAKVLGNPPRPLVAIVGGAKVSDKIQLLDNMLQRIDYLLIGGAMAYTFLKAQGYSIGKSKCEESKLEFARSLLKKAEDRKVQVILPIDHVCHTEFKAVDSPLITEDQNIPEGHMALDIGPKTIEKYVQTIGKCKSAIWNGPMGVFEMVPYSKGTFAIAKAMGRGTHEHGLMSIIGGGDSASAAELSGEAKRMSHVSTGGGASLELLEGKTLPGVAVLDEKSAVVSYASAGTGTLSNRWSSL
Protein: C3H1-type domain-containing protein (H2KZI4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MADVYTPTKTMDGAFLPAVGSPNTSIDSPAVYVPTPLTAPSTSKTTPVKPEDQTTRQKYGGTWKLRHLGMRWRCALPTRRFPLSQPLFLCSVDTTIHILMNYRTLQNFSKILKGLGKMGKCNFKSGQKPRFIIKKRLWIPGNYGHSYGSLFSIVNPHHFSDSPISCSPCFFYVSDFFFFSIFLCVRSFFADALSFIWNILQWFRLQSRAKWRRRYI
Protein: Cytosolic neutral trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) (O42777)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Hydrolyzes intracellular trehalose to glucose (Probable). The disaccharide trehalose serves as a storage carbohydrate that is mobilized during conidial germination. Regulates the level of trehalose as a protectant for cell integrity during heat stress.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P32356}.
Interaction partners:
- Large subunit of trehalose 6-phosphate synthase
- Alpha,alpha-trehalose-phosphate synthase
- Trehalose-6-phosphate phosphatase
- Acid trehalase
- UDP-glucose 4-epimerase
- Phosphoglucomutase
- Synthase subunit of trehalose-6-phosphate synthase/phosphatase complex
- 1,4-alpha-glucan-branching enzyme
Sequence:
MDDSALPSNTSNGINGRTAHRRSSSGGDPFQHPDIYYGNPESVERIKNRRRAFSSSLKSFNRQDFHEMLGDRNTRRGSMDPTSGNPRKFLIDVDATLHSLLEREDSDRNMQITIEDVGPKVFSLGTAASHGYNRFDVRGTYMLSNLLQELTIAKDYGRKQIVLDEERLSENPVSRLSRLIKNSFWNSLTRRIDGRNIEVAGRDPKDWTDDPRPRIYVPPGAPEQLEYYRRIAEEKPELRLDVQELAAEITPEYVRDLNEKPGLLALAMEEKYDEKTGKTDFAGVPFVVPGGRFNELYGWDSYMESLGLLASNRVDLAKAMVINFCFCIKHYGKILNANRSYYLTRSQPPFLTDMALRVYDRIQNEPGAMDFLRHAILAAIKEYYSVWMAEPRLDPVSGLSRYRSPGIGVPPETEASHFLHLLTPYAEKHGMEFKEFVQAYNYGKVKEPELDEYFMHDRAVRESGHDTSYRLERVCGNLATVDLNSLLYKYEVDIARVIRVYFKDKLEIPVEFRTPATKDIQSESSSVWDRRARRRKMRMDTYLWDEEKGMYFDYDTVKQERTNYESATTLWAMWAGLVTPRQASAMITKALPRFEEFGGIVSGTEESRGAVGLNRPTRQWDYPYGWAPQQMLAWTGFARYGYQEEAERLAYKWLYMITKAFVDFNGVVVEKYDVTRPIDPHRVDAEYGNQGVDFKGAPREGFGWVNASYVYGLEMLNAHQRRALGAVTPWETYSKAVSAQGSDTVLENRSE
Protein: Transcription and mRNA export factor sus1 (Q7LL15)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. May also be involved in cytoplasmic mRNA decay by interaction with components of P-bodies (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03046}. Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03046}.
Interaction partners:
- SAGA complex subunit Spt7
- SAGA complex subunit Sgf11
- SAGA complex subunit Sgf29
- SAGA complex subunit Sgf73
- Probable ubiquitin carboxyl-terminal hydrolase 8
- Cell division control protein 31
- SAGA complex subunit Ngg1
- Histone acetyltransferase gcn5
- SAGA complex subunit Ada2
- SAGA complex/transcription factor TFIID complex subunit Taf12
Sequence:
MYDLIFSTKMTTEKIVEQLYETGDYERLANELEYKLESCGWTTQLRDYTRGIVNSDSKIDFQKLYESALQSATESIPDSVKMDLLKDIKTCVLKLANPPESANGGNKM
Protein: Lysine-rich nucleolar protein 1 (Protein FAM191A) (Testis-specific gene 118 protein) (Q1ED39)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- IQ domain-containing protein K
- Zinc finger protein 106
Sequence:
MITKTHKVDLGLPEKKKKKKVVKEPETRYSVLNNDDYFADVSPLRATSPSKSVAHGQAPEMPLVKKKKKKKKGVSTLCEEHVEPETTLPARRTEKSPSLRKQVFGHLEFLSGEKKNKKSPLAMSHASGVKTSPDPRQGEEETRVGKKLKKHKKEKKGAQDPTAFSVQDPWFCEAREARDVGDTCSVGKKDEEQAALGQKRKRKSPREHNGKVKKKKKIHQEGDALPGHSKPSRSMESSPRKGSKKKPVKVEAPEYIPISDDPKASAKKKMKSKKKVEQPVIEEPALKRKKKKKRKESGVAGDPWKEETDTDLEVVLEKKGNMDEAHIDQVRRKALQEEIDRESGKTEASETRKWTGTQFGQWDTAGFENEDQKLKFLRLMGGFKNLSPSFSRPASTIARPNMALGKKAADSLQQNLQRDYDRAMSWKYSRGAGLGFSTAPNKIFYIDRNASKSVKLED
Protein: Diuretic hormone 31 receptor, isoform C (A0A0B4KF12)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Diuretic hormone 44, isoform A
- DNA-directed RNA polymerase III subunit RPC9
- Cardioacceleratory peptide receptor
Sequence:
MSDQIGNPNATFSGSGSGSGTNVASIAESVAESGPDFDALRAACETRLNASGQLAGSGGPGAEAGTHCAGTFDGWLCWPDTAVGTSAYELCPDFITGFDPARYAHKECGLDGEWFKHPLTNKTWSNYTTCVNLEDLNWRHTVNLISEVGYGTSLLAILLSLAILGYFKSLKCARITLHMNLFASFAANNSLWLVWYLLVMPNSELLHQSPMRCVALHITLHYFLLSNYSWMLCEGFYLHTVLVAAFISEKRLVKWLIAFGWGSPAIVIFVYSMARGLGGTPEDNRHCWMNQTNYQNILMVPVCISMFLNLLFLCNIVRVVLLKLNAPASIQGSCGPSRTVLQAFRATLLLVPLLGLQYILTPFRPAPKHPWENTYEIISAFTASFQGLCVAILFCFCNGEVIAQMKRKWRMMCFSNRPRTNSYTATQVSFVRCGPPLPGEEKVXLKDMSAKRRASAGPQHHQPHHQSHQLSTDQQRARSQSLASSSSFLEGWRDRMPFLKRRQTIDHSRQSQPLMEEGGETVGQAKSAPGAVDRPTLMTTIAEDVAETGTAATSHAASTSDAAAAAAVGAGGATGAEEGHPNGMGTVIVRMERAGQQHMADEAL
Protein: Baculoviral IAP repeat-containing protein 1a (Neuronal apoptosis inhibitory protein 1) (Q9QWK5)
Organism: Mus musculus (Mouse)
Function: Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals (By similarity).
Interaction partners:
- NLR family CARD domain-containing protein 4
- NACHT, LRR and PYD domains-containing protein 1a
- Interferon-inducible protein AIM2
- Caspase-1
- Pyrin
- NACHT, LRR and PYD domains-containing protein 3
- NACHT, LRR and PYD domains-containing protein 12
- Caspase-4
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 6
Sequence:
MAEHGESSEDRISEIDYEFLPELSALLGVDAVQLAKSQEEEEHKERMKMKKGFNSQMRSEAKRLKTFETYDTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQGKDVGNIGKYDIRVKSPEKMLRGGKARYHEEEARLESFEDWPFYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQSKKSSEEIAQYIQGYEGFVHVTGEHFVNSWVRRELPMVSAYCNDSVFANEELRMDTFKDWPHESPVAVDALVRAGLFYTGKKGIVQCFSCGGCMEKCTEGDDPIQEHNKFFPNCVFLQTPKSSAEVIPALQSHCALPEAMETTSESNHDDPAAVHSTVVGLGRSEAQWFQEARSLSEQLRDNYTKATFRHMNLPEVCSSLGTDHLIGCDVSIISKHISQPVQGALTIPEVFSNLSSVMCVEGETGSGKTTFLKRIAFLWASGCCPLLYRFQLVFYLSLSSITPDQGLANIICAQLLGAGGCISEVCLSSIIQQLQHQVLFLLDDYSGLASLPQALHTLITKNYLSRTCLLIAVHTNRVRGIRSYLDTSLEIKEFPLSNTVYILKKFFSHNIKRLLEFMVYFGQNEDLQGIHKTPLFVAAVCTDWFENPSDQPFQDMALFKSYMQYLSLKHKGAAKPLQATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDEELTTCLMSKFTAQRLRPVYRFLGPLFQEFLAAMRLTELLSSDRQEDQDLGLYYLRQINSPLKALTTYNNFLKYVFSHPSSKAGPTVVSHLLHLVDETELLENTYKNEDYVNHPPGTSRIMKGLKELWLLSPEYYSSFVSEHLLRIALNFAYESNTVAECSPFILQFLRGRTLALKVLNLQYFRDHPESLLLVKSLEVSINGNKVPKVVDYSVMEKSFETLQPPTIDQDYASAFEQMKEHEKNLSENEETIKSIKNIFPLQPPKISSGYWKLSPKPCKIPRLEVGVTNMGPADQALLQVLMEVFSASQSIEFRLSDSSGFLESIRPALELSKASVTKCSMSRLELSRAEQELLLTLPALQSLEVSETNQLPDQLFHNLHKFLGLKELCVRLDGKPDVLSVLPGEFPNLLHMEKLSIRTSMESDLSKLVKLIQNSPNLHVFHLKCDFLSNCDSLMAVLASCKKLREIEFSGRCFEAMPFVNILPNFISLKILNLISQQFPDKETSEKFAQALGSLRNLEELLVPTGDGIHQVAKLIVRQCLQLPCLRVLAFHYILDNDSVIEIARVATSGGFQKLEKLDLSMNHKITEEGYRNFFQALDNLPNLQNLNICRHIPECIQVQATTVKALGQCVSRLPSLTRLHMLSWLLDEEDMKVINDVKERHPQSKRLIIFWKWIVPFSPVVLE