wanglab/gogpt-training-data huggingface dataset:
Protein: ISWI chromatin-remodeling complex ATPase CHR17 (EC 3.6.4.-) (Protein CHROMATIN REMODELING 17) (F4JY24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses intrinsic ATP-dependent nucleosome-remodeling activity. Constitutes the catalytic subunit of several complexes capable of forming ordered nucleosome arrays on chromatin (By similarity). Involved in the formation of nucleosome distribution patterns. Required for the maintenance of the plant vegetative phase. In association with RLT1 or RLT2 may prevent the early activation of the vegetative-to-reproductive transition by regulating key genes that contribute to flower timing, such as FT, SEP1, SEP3, AGL8/FUL, SOC1 and FLC. Necessary to acquire heat stress (HS) memory.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
Interaction partners:
- Homeobox-DDT domain protein RLT1
- Histone H4
- DDT domain-containing protein
- Probable F-box protein At4g22060
- DNA polymerase II subunit B4
- Methyl-CpG-binding domain-containing protein 9
- Chromatin structure-remodeling complex protein SYD
- RuvB-like protein 1
- Protein FORGETTER 1
- AT-rich interactive domain-containing protein 5
Sequence:
MARASKREVSSDEAYSSEEEEQVNDQANVEEDDDELEAVARSAGSDEEDVAPDEAPVSDDEVVPVEDDAEEDEEDEEKAEISKREKARLKEMQKMKKQKIQQILDSQNASIDADMNNKGKGRIKYLLQQTELFAHFAKSDPSPSQKKGKGRGRHSSKLTEEEEDEECLKEEEGGIVGSGGTRLLTQPACIQGKLRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLGNPEERRHIREELLVAGKFDICVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLEVVNGGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGDHLVTNAGKMVLLDKLLPKLKDRDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGDERDASIEAYNKPGSEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTENAIEAKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIQFKMDDSADFYDFDDDNKDESKVDFKKIVSENWNDPPKRERKRNYSEVEYFKQTLRQGAPAKPKEPRIPRMPQLHDFQFFNIQRLTELYEKEVRYLMQAHQKTQMKDTIEVDEPEEVGDPLTAEEVEEKELLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAQVFQVRYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYRNPWLELKIQYGQNKGKLYNEECDRFMICMVHKLGYGNWDELKAAFRTSPLFRFDWFVKSRTTQELARRCDTLIRLIEKENQEFDERERQARKEKKLSKSATPSKRPSGRQANESPSSLLKKRKQLSMDDYGKRRK
Protein: Carbonic anhydrase 13 (EC 4.2.1.1) (Carbonate dehydratase XIII) (Carbonic anhydrase XIII) (CA-XIII) (Q8N1Q1)
Organism: Homo sapiens (Human)
Function: Reversible hydration of carbon dioxide.
Interaction partners:
- 1,25-dihydroxyvitamin D
Sequence:
MSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSVLRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQKITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAAAFLVSNHRPPQPLKGRKVRASFH
Protein: Calcium-activated potassium channel subunit beta-3 (BK channel subunit beta-3) (BKbeta3) (Hbeta3) (Calcium-activated potassium channel, subfamily M subunit beta-3) (Charybdotoxin receptor subunit beta-3) (K(VCA)beta-3) (Maxi K channel subunit beta-3) (Slo-beta-3) (Q9NPA1)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Alters the functional properties of the current expressed by the KCNMA1 channel. Isoform 2, isoform 3 and isoform 4 partially inactivate the current of KCNBMA. Isoform 4 induces a fast and incomplete inactivation of KCNMA1 channel that is detectable only at large depolarizations. In contrast, isoform 1 does not induce detectable inactivation of KCNMA1. Two or more subunits of KCNMB3 are required to block the KCNMA1 tetramer.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Calcium-activated potassium channel subunit alpha-1
- Small conductance calcium-activated potassium channel protein 1
- Intermediate conductance calcium-activated potassium channel protein 4
- Small conductance calcium-activated potassium channel protein 3
- Small conductance calcium-activated potassium channel protein 2
- Potassium channel subfamily U member 1
- Calcium-activated potassium channel subunit beta-1
- cGMP-dependent protein kinase 2
- Calcium-activated potassium channel subunit beta-4
- Calcium-activated potassium channel subunit beta-2
Sequence:
MDFSPSSELGFHFVAFILLTRHRTAFPASGKKRETDYSDGDPLDVHKRLPSSAGEDRAVMLGFAMMGFSVLMFFLLGTTILKPFMLSIQREESTCTAIHTDIMDDWLDCAFTCGVHCHGQGKYPCLQVFVNLSHPGQKALLHYNEEAVQINPKCFYTPKCHQDRNDLLNSALDIKEFFDHKNGTPFSCFYSPASQSEDVILIKKYDQMAIFHCLFWPSLTLLGGALIVGMVRLTQHLSLLCEKYSTVVRDEVGGKVPYIEQHQFKLCIMRRSKGRAEKS
Protein: Kinesin motor domain-containing protein (Q57ZI5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Kinesin-like protein
- Chromosomal passenger protein
- Chromosomal passenger protein
- Aurora kinase
Sequence:
MEQTSKPANLPPCSPRQAVKNILRGVDSHVRVMSHLDNVSTSSSYSAVRLKKPKTDSWTEPFNVTRVHRGTSTNSFYQEVIAPCVANCLAGQSYLFLVSGPCESGRSQTLYGSPHHKTKGVVELAAEDLLGYMTGGAENNDDNPSRGQPTVTHSAFVTRGSHINETKTGEPVPIVDFPPPLGRTALPRMQLLESAASVVQIPEHKYSDTSCIIQFQVYVPVDTLGRRSMATLTFVDAAAFHSQPCSEVRHLVSTVRRVAGLSNGDGPSFDQRKLTTLLEPALMGYVTLMSITTISGRDDLHEAACEALRFAETISRIHQVLMLVHINTPKWFLDTAEKVEVLRSQRNKMLSEQHARGVYDYYVTVTKWLSQHVAGAGCTFDKLLEEVEQIREDLACEMKERVKSVQASIQEAEKQHALQLERTRNAHAITTSQLDKVKRLDETIAALTQKVTQRDLFNDHKISEMRIEISAIESETETRRQELLRFENEERLYGTKCAEVMGVLEKYSADLANSQMHYVLTEEMSAIEEKKKRLEADLATASRIAHMESDNFRANREKNSRLSHLSVMQQKVDSLRGRILTNSVSHTMSRSASHLSPRSQPDASPSESPAQKRRRFASPRYSAV
Protein: Retinol binding protein (Q8JIZ4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MQNFDKTRYTGRWYAVAKKDPVGLFLLDNVVAQFSVDESGKMTATAHGRVIILNNWEMCANMFGTFEDTPDPAEFKMRYWGAASYLQTGNDDHWVIDTDYDNYAIHYSCREVDLDGTCLDGYSFIFSRHPTGLRPEDQKIVTDKKKEICFLGKYRRVG
Protein: Solute carrier family 9 (sodium/hydrogen exchanger), member 6 (A0A140LJ55)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
XYARQMMFSTTLLIVFFTVWVFGGGTTAMLSCLHIRYYARLWGYRDELTHGLYPQEAHSLFGETDRVGVDSDQEHLGVPDNERRTTKAESAWLFRMWYNFDHNYLKPLLTHSGPPLTTTLPACCGPIARCLTSPQAYENQEQLKDDDSDLILNDGDISLTYGDSTVNTESATASAPRRFMGNSSEDALDRELTFGDHELVIRGTRL
Protein: Pro-neuregulin-1, membrane-bound isoform (Pro-NRG1) [Cleaved into: Neuregulin-1 (Acetylcholine receptor-inducing activity) (ARIA) (Breast cancer cell differentiation factor p45) (Glial growth factor) (Heregulin) (HRG) (Neu differentiation factor) (Sensory and motor neuron-derived factor)] (Q02297)
Organism: Homo sapiens (Human)
Function: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development. Binds to ERBB4. Binds to ERBB3. Acts as a ligand for integrins and binds (via EGF domain) to integrins ITGAV:ITGB3 or ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and ERRB3 are essential for NRG1-ERBB signaling. Induces the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2 and AKT1. Ligand-dependent ERBB4 endocytosis is essential for the NRG1-mediated activation of these kinases in neurons (By similarity).
Subcellular location: [Pro-neuregulin-1, membrane-bound isoform]: Cell membrane; Single-pass type I membrane protein. Note=Does not seem to be active.; SUBCELLULAR LOCATION: [Neuregulin-1]: Secreted.; SUBCELLULAR LOCATION: [Isoform 8]: Nucleus. Note=May be nuclear.; SUBCELLULAR LOCATION: [Isoform 9]: Secreted. Note=Has a signal peptide.; SUBCELLULAR LOCATION: [Isoform 10]: Membrane; Single-pass type I membrane protein. Note=May possess an internal uncleaved signal sequence.
Interaction partners:
- Receptor tyrosine-protein kinase erbB-3
- Receptor tyrosine-protein kinase erbB-4
- Epidermal growth factor receptor
- Receptor tyrosine-protein kinase erbB-2
- Pro-neuregulin-4, membrane-bound isoform
- Pro-epidermal growth factor
- Pro-neuregulin-3, membrane-bound isoform
- Pro-neuregulin-2, membrane-bound isoform
- Probetacellulin
- Disks large homolog 4
Sequence:
MSERKEGRGKGKGKKKERGSGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEIITGMPASTEGAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCTENVPMKVQNQEKAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRKKLHDRLRQSLRSERNNMMNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREAETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESILSESHSVIVMSSVENSRHSSPTGGPRGRLNGTGGPRECNSFLRHARETPDSYRDSPHSERYVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVSMPSMAVSPFMEEERPLLLVTPPRLREKKFDHHPQQFSSFHHNPAHDSNSLPASPLRIVEDEEYETTQEYEPAQEPVKKLANSRRAKRTKPNGHIANRLEVDSNTSSQSSNSESETEDERVGEDTPFLGIQNPLAASLEATPAFRLADSRTNPAGRFSTQEEIQARLSSVIANQDPIAV
Protein: Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) (P78917)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent 6-phosphofructokinase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- Phosphoglucomutase
- Probable transketolase
- Hexokinase-2
- Enolase 1-1
- Hexokinase-1
- Phosphoglycerate mutase
- Enolase 1-2
Sequence:
MSFSLASTLPAWQAVQTHYESVGKHLVLKELFAKDSSRFEKFSFTFNGLKEEDGPILFDFSKNLITEETVELLVKLAKEANVEGLRDALFAGEHINFTEDRAVFHPALRNVSEKPMKVNGQDVMPGVRKVLRHMKEFSDAVRSGAWKGYTGKPIKSIVNVGIGGSDLGPVMVTEALKPYGQENLELHFVSNIDGTHLAEALKKCDPETTLFLIASKTFTTAETCTNAKSAKDWFLASAKDPSHVAKHFVALSTNEKEVTAFGISAQNMFEFSDWVGGRYSVWSAIGLSVALYIGYENFEAFLSGAHAMDEYFCSTPLEKNIPALAALISIWYSDFFGAQTHLVAPYDQYLHRFPAYLQQLSMESNGKAITRSGDMVNYTTGKILWGEPGTNSQHSFFQLIHQGTKLIPADFLIPIESHNPIDNNKHHRMLFSNFAAQTEALMLGKTPAEVKAEGTPDEIVPHKTFVGNRPSNSIIAKKITPASLGALIAFYEWVTFTEGAVWNINSFDQFGVELGKKLAKNVLAQLETKGDVENHDSSTNGLINLFKNGF
Protein: ER membrane protein complex subunit 3 (Protein pob) (Transmembrane protein 111) (Q7SXW4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P0I2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9P0I2}.
Interaction partners:
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 5
- Cox4 neighbor
- ER membrane protein complex subunit 10
- Endoplasmic reticulum membrane protein complex subunit 7
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 9
- Zgc:195050.
Sequence:
MAEPELLLDSNIRLWVVLPIVFITFLVGVIRHYVSILLQSDKKLTLEQVSDSQVLIRSRVLRENGKYIPKQSFLMRKFYFNNQEDGFFKKTKRKVVPPSPMTDPSMLTDMMKGNVTNVLPMILIGGWINWTFSGFVTTKVPFPLTLRFKPMLQQGIELLSLDASWVSSASWYFLNVFGLRSMYSLILGQDNGADQSRIMQEQMSGAAMAMPADTNKAFKAEWEALELTDHQWALENVEEDLMSKDLDLSGMFSKDLPTGIF
Protein: Transcriptional regulator STP2 (Q5AL16)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor involved in the regulation of gene expression in response to extracellular amino acid levels. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS amino acid sensor system (including CSY1 and CSH3), becomes proteolytically activated and relocates to the nucleus, where it induces the expression of SPS-sensor-regulated genes. Required for efficient alkalinization through the release of ammonia from the cells produced during the breakdown of amino acids, and subsequent switch to the hyphal form.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to the cytoplasm in its unprocessed form and is targeted to the nucleus after proteolytic processing upon induction by amino acids. {ECO:0000250}.
Interaction partners:
- Ssy5p
- Ptr3p
- Ssy1p
- RuvB-like helicase 1
- Ato5p
Sequence:
MSVAITSNNNKQPQPQPQPHLKVVNNNSTFNLYTWLRSVFQYCISLIISYTSNWLLVNNDNNNNNININYKSNNNDNNNASTSLQPKISNVKAESMKIFPDLQKSNFTTYYTTEKPLHQDVLKPVICSTGITSRILPYTNEKGELEWKFTEVQGKELDEFKMHPQQQQQQQEVKQELSPAESNESNESLAKDSSTTPASISDSPSHSETESTVSSTIIANSNQIFKCPSCDAEFRVRGYLTRHMKKHSTKKAYTCPFHDKSIYVDENNITHKCHSSGGFSRRDTYKTHLKSRHFNYAKPIKSAERSKVPGQCAMCGEHFNSAEIWCEIHVEGGECKFLPMGFKGKSRIKNRLKKQIQKNKMIDPELVPFASKVLEEVEQERQKKKNYRTTGTGSESSIQSQESESSINSTPLSMQISAPVPMPVSIQQQHQHQHQHHHHVQNQHQQHVNQQQSIATPASIYSSSASSTSSYESTHSPYTPQSSRSPLSHMYNPQQPPYFNQIAQAHQQDGQKNQVKDDYDDEYCLDVDQLNTTFVNETVANYLQIHDFHSMNQYQPGQQQQQQQQQQQQQQQRQHQQQQPSMYF
Protein: Cell adhesion protein trophinin (Q99PM6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDIQAAAVAVAEAKARAEARAQMGIGEEAVAGPWNWDDMDINCLTREELGDDAQAWSRFSFEIEPRAQENADPTTNVLFNQGATTRNSFSDGAGISFGGITNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGISNPSGGFGGRNSITFGSVPNTSANFSSAPSISFGDTPNTSTSFSGGANSSFSGTPSTSAPFCNAASISFGGAPSTSTSFSTASISFGGAPSTSTSLSTASISFGGAPSTSTSFSTASISFGGAPSTSTSLSTASISFGGAPSINSSSGGSSVSFGGAPTTSTSFSGGPCISFGGAPCTTASISGGASSGFGSTLCSTNPGFSALSTNTSFGSAPTTSTVFSGAVSTTTGFGGTLSTSVCFGSSPYSGAGFGGTLSTSISFGGSPSTNTGFGGTLSTSVSFGASSSTSSDFGGTLSTSVSFGGSSGANAGFGGTLNSSTSFGGAISTSTGFGSALNNSANFGGAISTSFSGVLNSSASFGGAINTSAGFGSTLNSSASFGSALSTSASFGGVLNGRAGFGGALNTNATFGGVLNGSAGFGGAMNTNATFGGALNSNAGFGGAISTSTNFGGALNNSAGFGGAMNTSASFGGVLNNSAGFGGAINTSANFGGALTNSAGFGGAISTSASFGGALNNSAGFGGAISTSASFGGALNNSAGFGGAISTNASFGGAISNSPDFGGAFSTSVGFGGTLNTTDFGSNHSNSISFGSAPTTSVSFGGSHSTNLCFGGAPSTSLCFGSASNTNLCFGGSNSTNCFSGATSANFNEGHSISFGNGLSTSAGFGNGLGTSAGFDSSLGTSTGFGGSLGPSASFNGGLGTSTGFGGGLGTSTDFSGGLNHNADFNGGLGNSAGFNGGLNTNTDFGGELGTSAGFGDGLGSSTSFGAGLVTSDGFAGNLGTNTGFGGTLGTGAGFSVSLNNGNGFGNGPNASFNRGLNTIIGFGSGSNTSNGFTGEPNTGSSFSNGPSSIVGFSGGPSTGAGFCSGPSTGGFGGGPSTGPGFGGPSTGPGFGGPSTGGGFGGPNTGGGFGGPSTGGGFGGPSTGGGFGGPSTGGGFGGPSTAAGFGSGLSTSTGFGGGLNTSAGFSGGPPSTGTGFGGGASSHGGCGFPYG
Protein: Putative Polycomb group protein ASXL2 (Additional sex combs-like protein 2) (Q76L83)
Organism: Homo sapiens (Human)
Function: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility (By similarity). Involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator for PPARG and enhances its adipocyte differentiation-inducing activity; the function seems to involve differential recruitment of acetylated and methylated histone H3.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase BAP1
- Forkhead box protein K2
- Forkhead box protein K1
- AOF1 protein
- Host cell factor 1
- Methyl-CpG-binding domain protein 6
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Zinc finger protein 462
- Methyl-CpG-binding domain protein 5
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
Sequence:
MREKGRRKKGRTWAEAAKTVLEKYPNTPMSHKEILQVIQREGLKEIRSGTSPLACLNAMLHTNSRGEEGIFYKVPGRMGVYTLKKDVPDGVKELSEGSEESSDGQSDSQSSENSSSSSDGGSNKEGKKSRWKRKVSSSSPQSGCPSPTIPAGKVISPSQKHSKKALKQALKQQQQKKQQQQCRPSISISSNQHLSLKTVKAASDSVPAKPATWEGKQSDGQTGSPQNSNSSFSSSVKVENTLLGLGKKSFQRSERLHTRQMKRTKCADIDVETPDSILVNTNLRALINKHTFSVLPGDCQQRLLLLLPEVDRQVGPDGLMKLNGSALNNEFFTSAAQGWKERLSEGEFTPEMQVRIRQEIEKEKKVEPWKEQFFESYYGQSSGLSLEDSKKLTASPSDPKVKKTPAEQPKSMPVSEASLIRIVPVVSQSECKEEALQMSSPGRKEECESQGEVQPNFSTSSEPLLSSALNTHELSSILPIKCPKDEDLLEQKPVTSAEQESEKNHLTTASNYNKSESQESLVTSPSKPKSPGVEKPIVKPTAGAGPQETNMKEPLATLVDQSPESLKRKSSLTQEEAPVSWEKRPRVTENRQHQQPFQVSPQPFLNRGDRIQVRKVPPLKIPVSRISPMPFHPSQVSPRARFPVSITSPNRTGARTLADIKAKAQLVKAQRAAAAAAAAAAAAASVGGTIPGPGPGGGQGPGEGGEGQTARGGSPGSDRVSETGKGPTLELAGTGSRGGTRELLPCGPETQPQSETKTTPSQAQPHSVSGAQLQQTPPVPPTPAVSGACTSVPSPAHIEKLDNEKLNPTRATATVASVSHPQGPSSCRQEKAPSPTGPALISGASPVHCAADGTVELKAGPSKNIPNPSASSKTDASVPVAVTPSPLTSLLTTATLEKLPVPQVSATTAPAGSAPPSSTLPAASSLKTPGTSLNMNGPTLRPTSSIPANNPLVTQLLQGKDVPMEQILPKPLTKVEMKTVPLTAKEERGMGALIATNTTENSTREEVNERQSHPATQQQLGKTLQSKQLPQVPRPLQLFSAKELRDSSIDTHQYHEGLSKATQDQILQTLIQRVRRQNLLSVVPPSQFNFAHSGFQLEDISTSQRFMLGFAGRRTSKPAMAGHYLLNISTYGRGSESFRRTHSVNPEDRFCLSSPTEALKMGYTDCKNATGESSSSKEDDTDEESTGDEQESVTVKEEPQVSQSAGKGDTSSGPHSRETLSTSDCLASKNVKAEIPLNEQTTLSKENYLFTRGQTFDEKTLARDLIQAAQKQMAHAVRGKAIRSSPELFSSTVLPLPADSPTHQPLLLPPLQTPKLYGSPTQIGPSYRGMINVSTSSDMDHNSAVPGSQVSSNVGDVMSFSVTVTTIPASQAMNPSSHGQTIPVQAFSEENSIEGTPSKCYCRLKAMIMCKGCGAFCHDDCIGPSKLCVSCLVVR
Protein: Elongin-B (EloB) (Elongin 18 kDa subunit) (RNA polymerase II transcription factor SIII subunit B) (SIII p18) (Transcription elongation factor B polypeptide 2) (Q15370)
Organism: Homo sapiens (Human)
Function: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity).
Subcellular location: Nucleus {ECO:0000305|PubMed:34700328}.
Interaction partners:
- Elongin-A
- Cullin-2
- RING-box protein 2
- Elongin-C
- von Hippel-Lindau disease tumor suppressor
- Hypoxia-inducible factor 1-alpha
- Core-binding factor subunit beta
- Cullin-5
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-like protein NEDD8
Sequence:
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGECGFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ
Protein: Pentatricopeptide repeat-containing protein At2g15820, chloroplastic (Protein ORGANELLE TRANSCRIPT PROCESSING 51) (AtOTP51) (Q9XIL5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes the splicing of group II introns in chloroplasts. Required for the splicing of intron 2 of plastid ycf3 transcripts, a factor required for the assembly of photosystem I (PSI). Involved in the splicing of several other group-IIa introns. May be involved in the splicing of precursor forms of trnL, trnG, trnI, and trnA. Required for the assembly of PSI and PSII.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At4g25270
- Protein THYLAKOID ASSEMBLY 8, chloroplastic
- AT5g10910/T30N20_180
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 3, chloroplastic
- CRM-domain containing factor CFM2, chloroplastic
- Pentatricopeptide repeat-containing protein At3g48250
- Nuclear protein-like
- Photosystem I assembly protein Ycf3
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic
- Transcription termination factor MTERF2, chloroplastic
Sequence:
MTKSNGHNATMIVTGACDFSSSFSLASSSSSTVSVTTFNISSLSSNPNIINSSSTLFRSLSFSLIRHRSSYSRRSLRRLSIHTVHGNKTQFFSHSSTRTPPLFTANSTAQRSGTFVEHLTGITESEEGISEANGFGDVESARNDIRNVATRRIETEFEVRELEELPEEWRRSKLAWLCKEVPTHKAVTLVRLLNAQKKWVRQEDATYISVHCMRIRENETGFRVYRWMTQQNWYRFDFGLTTKLAEYLGKERKFTKCREVFDDVLNQGRVPSESTFHILVVAYLSSLSVEGCLEEACSVYNRMIQLGGYKPRLSLHNSLFRALVSKQGGILNDQLKQAEFIFHNVVTTGLEVQKDIYSGLIWLHSCQDEVDIGRINSLREEMKKAGFQESKEVVVSLLRAYAKEGGVEEVERTWLELLDLDCGIPSQAFVYKIEAYSKVGDFAKAMEIFREMEKHIGGATMSGYHKIIEVLCKVQQVELVETLMKEFEESGKKPLLPSFIEIAKMYFDLGLHEKLEMAFVQCLEKCQPSQPIYNIYLDSLTKIGNLEKAGDVFNEMKNNGTINVSARSCNSLLKGYLDCGKQVQAERIYDLMRMKKYEIEPPLMEKLDYILSLKKKEVKKRPFSMKLSKDQREVLVGLLLGGLQIESDKEKKSHMIKFEFRENSQAHLVLKQNIHDQFREWLHPLSNFQEDIIPFEFYSVPHSYFGFYAEHYWPKGQPEIPKLIHRWLSPHSLAYWYMYSGVKTSSGDIILRLKGSLEGVEKVVKALQAKSMECRVKKKGKVFWIGLQGTNSALFWKLIEPHVLENLKEHLKPASESLDNVKEAEEQSINFKSNSDHSDDCVNSEAHFY
Protein: Uncharacterized protein (Q4GZ77)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGAFPSHDAPELIYSMLVLRPSTNSQVEVCLVPLLPRFFNDGHKKAKKKLNELLASKGAHQSSLAASLAPRAPATIAPGKVPDQGIGHALVDYFISSTEGSFFVTTKDAVVSKVAIQAEQGQRERSDISTTGGRSAPGTASTGETQPSNAPSHTAHHSSSHQAMSNSVRPVPFAVCIVDSDVSTGTPGTTGGSAQAAAAKHHHVHANNVVLIKGRRLQLVGFIACCMDRPVRHMTTANPVKPHGASGGAGATSGEGKKQGIPVCLDVIFDDTEAHGFLTESVVLLASFAFRKQFLNCCALHFRAGDPDVESSFGRHMDPLQLRLVMRHDNYRILRLFHSRYPLLDMVKELRVSGGSSAPQFSLYENDGNEVGLEVTFGMNFLTRWMRFVEKMMHVETVVGNHIRCGTTAIMSERDKLIQERRDSGAFLEEEEDDERIFGGAVYAVSLRRWTAAEKQAVQQQQQVPLSGASPMYVYPTTAAPGQYWPQMSVMMGQPPGWPTSVVPLSAAAAAPTAVAPVIGQQQPFVIQASGTRPQLYYASPQPTVSGNATFVTQSGIPIVQQAATASPFGVAATQPASGQQIVYVMQGAQATSASVAAPTVSAMAPGMTPQAFYYPQTTAYAVPYSPYGFQQQPQQQLVTQATHIGTQQQQQQVTSAGQVAQQ
Protein: Uricase (EC 1.7.3.3) (Urate oxidase) (P09118)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Subcellular location: Peroxisome {ECO:0000269|PubMed:3194410}.
Interaction partners:
- 5-hydroxyisourate hydrolase
- Xanthine dehydrogenase/oxidase
- Transthyretin
- Solute carrier family 22 member 12
- Albumin
- Probable inactive allantoicase
- Purine nucleoside phosphorylase
- Adenosine deaminase
- 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
- Tryptophan 2,3-dioxygenase
Sequence:
MAHYHDDYGKNDEVEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLRSKKDYLHGDNSDIIPTDTIKNTVHVLAKFKGIKSIETFAMNICEHFLSSFSHVTRAHVYVEEVPWKRFEKNGVKHVHAFIHTPTGTHFCDVEQVRNGPPIIHSGIKDLKVLKTTQSGFEGFIKDQFTTLPEVKDRCFATQVYCKWRYQNRDVDFEATWGAVRDIVLKKFAGPYDRGEYSPSVQKTLYDIQVLTLSQLPEIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKITGTVRRKLPSRL