wanglab/gogpt-training-data huggingface dataset:
Protein: SH3 and multiple ankyrin repeat domains protein 2 (Shank2) (Cortactin-binding protein 1) (CortBP1) (Q80Z38)
Organism: Mus musculus (Mouse)
Function: Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. May play a role in the structural and functional organization of the dendritic spine and synaptic junction (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:15207857}. Synapse {ECO:0000269|PubMed:15207857}. Postsynaptic density {ECO:0000269|PubMed:15207857}. Cell projection, dendritic spine {ECO:0000269|PubMed:15207857}. Cell projection, growth cone {ECO:0000250}. Note=Colocalizes with cortactin in growth cones in differentiating hippocampal neurons. Colocalized with PDE4D to the apical membrane of colonic crypt cells (By similarity). Present in the dendritic spines of cerebellar Purkinje cells. {ECO:0000250}.
Interaction partners:
- SH3 and multiple ankyrin repeat domains protein 3
- Disks large homolog 4
- SH3 and multiple ankyrin repeat domains protein 1
- Disks large-associated protein 1
- Disks large-associated protein 2
- Neurexin-1
- Neuroligin-3
- Ras/Rap GTPase-activating protein SynGAP
- Neuroligin-1
- Disks large homolog 2
Sequence:
MKSLLNAFTKKEVPFREAPAYSNRRRRPPNTLAAPRVLLRSNSDNNLNAGAPEWAVCSAATSHRSLSPQLLQQTPSKPDGATKSLGSYTPGPRSRSPSLNRLGGTAEDGKRTQPHWHVGSPFTPGANKDSLSTFEYPGPRRKLYSAVPGRLFVAVKPYQPQVDGEIPLHRGDRVKVLSIGEGGFWEGSARGHIGWFPAECVEEVQCKPRDSQAETRADRSKKLFRHYTVGSYDSFDAASDCIIEDKTVVLQKKDNEGFGFVLRGAKADTPIEEFTPTPAFPALQYLESVDEGGVAWQAGLRTGDFLIEVNNENVVKVGHRQVVNMIRQGGNHLILKVVTVTRNLDPDDTARKKAPPPPKRAPTTALTLRSKSMTAELEELGLSLVDKASVRKKKDKPEEIVPASKPSRTAENVAIESRVATIKQRPTSRCFPAASDVNSVYERQGIAVMTPTVPGSPKGPFLGLPRGTMRRQKSIDSRIFLSGITEEERQFLAPPMLKFTRSLSMPDTSEDIPPPPQSVPPSPPPPSPTTYNCPRSPTPRVYGTIKPAFNQNPVVAKVPPATRSDTVATMMREKGMFYRRELDRFSLDSEDVYSRSPAPQAAFRTKRGQMPENPYSEVGKIASKAVYVPAKPARRKGVLVKQSNVEDSPEKTCSIPIPTIIVKEPSTSSSGKSSQGSSMEIDPQATEPGQLRPDDSLTVSSPFAAAIAGAVRDREKRLEARRNSPAFLSTDLGDEDVGLGPPAPRMQASKFPEEGGFGDEDETEQPLLPTPGAAPRELENHFLGGGEAGAQGEAGGPLSSTSKAKGPESGPAAPLKSSSPAGPENYVHPLTGRLLDPSSPLALALSARDRAMQESQQGHKGEAPKADLNKPLYIDTKMRPSVESGFPPVTRQNTRGPLRRQETENKYETDLGKDRRADDKKNMLINIVDTAQQKSAGLLMVHTVDVPMAGPPLEEEEDREDGDTKPDHSPSTVPEGVPKTEGALQISAAPEPAVAPGRTIVAAGSVEEAVILPFRIPPPPLASVDLDEDFLFTEPLPPPLEFANSFDIPDDRAASVPALADLVKQKKNDTSQPPTLNSSQPANSTDSKKPAGISNCLPSSFLPPPESFDAVTDSGIEEVDSRSSSDHHLETTSTISTVSSISTLSSEGGESMDTCTVYADGQAFVVDKPPVPPKPKMKPIVHKSNALYQDTLPEEDTDGFVIPPPAPPPPPGSAQAGVAKVIQPRTSKLWGDVPEVKSPILSGPKANVISELNSILQQMNRGKSVKPGEGLELPVGAKSANLAPRSPEVMSTVSGTRSTTVTFTVRPGTSQPITLQSRPPDYESRTSGPRRAPSPVVSPTELSKEILPTPPPPSATAASPSPTLSDVFSLPSQSPAGDLFGLNPAGRSRSPSPSILQQPISNKPFTTKPVHLWTKPDVADWLESLNLGEHKETFMDNEIDGSHLPNLQKEDLIDLGVTRVGHRMNIERALKQLLDR
Protein: Carboxysome shell vertex protein CcmL (Carbon dioxide concentrating mechanism protein CcmL) (Q03512)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Probably forms vertices in the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Has been modeled to induce curvature upon insertion into an otherwise flat hexagonal molecular layer of CcmK subunits.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00858, ECO:0000269|PubMed:28616951, ECO:0000269|PubMed:31048338}. Note=This cyanobacterium makes beta-type carboxysomes (PubMed:24267892). Probably forms vertices in the polyhedral carboxysome (Probable). {ECO:0000269|PubMed:24267892, ECO:0000305|PubMed:24267892}.
Interaction partners:
- Carboxysome shell protein CcmK2
- Carboxysome assembly protein CcmO
- Carboxysome assembly protein CcmM
- Carboxysome shell protein CcmK4
- Carboxysome shell protein CcmK3
- Ribulose bisphosphate carboxylase large chain
- Carboxysome shell protein CcmP
- Carboxysome assembly protein CcmN
Sequence:
MRIAKVRGTVVSTYKEPSLQGVKFLVVQFLDEAGQALQEYEVAADMVGAGVDEWVLISRGSQARHVRDCQERPVDAAVIAIIDTVNVENRSVYDKREHS
Protein: RRM domain-containing protein (O45577)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Suppressor of forked domain-containing protein
- Cleavage stimulation factor 50 kDa subunit
- Probable cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 4
- DUF3453 domain-containing protein
- Cleavage and polyadenylation specificity factor subunit 3
- RNA polymerase II subunit A C-terminal domain phosphatase ssup-72
- Probable cleavage and polyadenylation specificity factor subunit 1
- Pre-mRNA polyadenylation factor Fip1 domain-containing protein
- Polyadenylation and cleavage factor homolog 11
Sequence:
MMSGGYKSSGVGNDRSQRSVFVGNISYDVSEDTIRSIFSKAGNVLSIKMVHDRETGKPKGYGFIEFPDIQTAEVAIRNLNGYELSGRILRVDSAAGGMNMEEFGSSSNAPAPVEENPYGPECDAGKAPERISQTVASLAPEKMFELMKQLQESLKNNPSELHKFLVEHPQIAYAVLQAAVVMRIVDPQTALGLLHRNKAATLTPFHNTPQGAPPMVQQQQMPMPPKPTFAHPGPSMGPPMGPPMGPPMGHPQAPQYGQNYGQPVAPQQYKPPPQQQPPVQMRPPVQQPQQNHQEEQQNAELLMQVMQLSEHDLQMLPAGDREKIIELRQQLKRNVK
Protein: Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Disrupter of telomere silencing protein 4) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10) (P53874)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Deubiquitinating enzyme involved in telomere and HM loci silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes. Targets histone H2B for deubiquitination, thus helping to localize SIR2 to the telomere. At silent chromatin, including telomeres and the rDNA locus, not only maintains low H2B 'Lys-123' ubiquitination (H2BK123Ub), but also low H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). Controls the proliferating-cell nuclear antigen PCNA/POL30 deubiquitination which is crucial for keeping TLS polymerases in check as well as for down-regulating the error-free bypass. Deubiquitinates and stabilizes RPA190, the largest subunit of RNA polymerase I, to achieve optimal levels of ribosomes and cell growth. Protects also nutrient transporters such as GAP1 from ubiquitin-dependent endocytosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10490600}. Chromosome, telomere {ECO:0000269|PubMed:15721261}. Nucleus, nucleolus {ECO:0000269|PubMed:22902402}. Note=Preferentially localizes to silent chromatin (PubMed:15988024). {ECO:0000269|PubMed:15988024}.
Interaction partners:
- Regulatory protein SIR4
- E3 ubiquitin-protein ligase BRE1
- Probable ATP-dependent RNA helicase DHR2
- Histone H2B.1
- Ubiquitin-conjugating enzyme E2 2
- Ubiquitin carboxyl-terminal hydrolase 8
- Small ribosomal subunit protein uS5m
- Ubiquitin carboxyl-terminal hydrolase 6
- Histone H2B.2
- Ubiquitin carboxyl-terminal hydrolase 14
Sequence:
MTTQESIKPLVDRILSNPLQFNAAMISNKSNNNDTSAAPENSSYIVIGKQHNNNSNSTAIAATAESKQIKENNLIDRPNGKKTNTVPKSMAEALLLYTSKNDKDAADATGAKKSAELSTELSTEPPSSSSEDDKVGKEEEEEGEIFHEARDYVEPRKASLKERDNADKGDGEDIGEDIGEDIGEDIGEDIGEDIGENLGSPLATIDDSSNENEKEKRKELSTSISSDDEIEDDEDEDDMDYDSSAMEKELPEEEENDSSSKISEGEKKSLYQDLMENSTVEVNRYEPVNNTKENGNRNPKGEEEEEEEEELKHKSRSITPPVTISNLSNFYQFNENINDRGSLNSTRIVKNWGDKFTNLKPRGLLNHGVTCYTNAAVQAMLHIPSIQHYLFDILMGKYDSTISKNSVSYTLAETSKKMWLPVSKNPRKNVSASYINPKHLISRLDDINCMMSEWQQEDSHEYFMSLMSRLQEDSVPKGHKLIESIIYDIFGGLLKQIVTCKSCGSISKTEQPFYDLSLHLKGKKKLDPNSDLSSDSINGTSATTSTTTSNAATKPSLSSSSSVNLNNGSPFAAASDLSSANRRFSIEKSIKDFFNPELIKVDKEQKGYVCEKCHKTTNAVKHSSILRAPETLLVHLKKFRFNGTSSSKMKQAVSYPMFLDLTEYCESKELPVKYQLLSVVVHEGRSLSSGHYIAHCKQPDGSWATYDDEYINIISERDVLKEPNAYYLLYTRLTPKSVPLPLAKSAMATGNVTSKSKQEQAVNEPNNRPLKINSKKNNRKKWKKNKKRKFTK
Protein: Purinergic receptor P2X 5 (H0YII8)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
XGYQDVDTSLQSAVITKVKGVAFTNTSDLGQRIWDVADYVIPAQGENVFFVVTNLIVTPNQRQNVCAENEGIPDGACSKDSDCHAGEAVTAGNGVKTGRCLRRENLARGTCEIFAWCPLETSSRPEEPFLKEAEDFTIFIKNHIRFPKFNFSNRLDNKLSKSVSSGYNFRFARYYRDAAGVEFRTLMKAYGIRFDVMVNGKGAFFCDLVLIYLIKKREFYRDKKYEEVRGLEDSSQEAEDEASGLGLSEQLTSGPGLLGMPEQQELQEPPEAKRGSSSQKGNGSVC
Protein: Mitogen-activated protein kinase kinase kinase 20 (MAPKK kinase 20) (EC 2.7.11.25) (Protein ABA-INSENSITIVE PROTEIN KINASE 1) (Q9SND6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitogen-activated protein kinase kinase (MAPKK) that phosphorylates both MKK3 and MPK18 and regulate two separate signaling pathways involved in root microtubule functions. MAPKK which regulates abscisic acid (ABA) responses in a MAPKKK20-MKK5-MPK6 cascade involved in root growth (e.g. root cell division and elongation) and stomatal response, probably via MKK5 activation by protein phosphorylation and subsequent activation of MAPK6 by MKK5. Involved in various abiotic stresses (e.g. osmotic stress, cold and hydrogen peroxide) responses by phosphorylating and thus regulating MPK6 activity, in an ABA-independent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:28848569}. Cytoplasm {ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569, ECO:0000269|PubMed:30081740}.
Interaction partners:
- Mitogen-activated protein kinase 18
- Transcription factor DUO1
- Protein kinase ATN1-like protein
Sequence:
MEWVRGETIGFGTFSTVSTATKSRNSGDFPALIAVKSTDAYGAASLSNEKSVLDSLGDCPEIIRCYGEDSTVENGEEMHNLLLEYASRGSLASYMKKLGGEGLPESTVRRHTGSVLRGLRHIHAKGFAHCDIKLANILLFNDGSVKIADFGLAMRVDGDLTALRKSVEIRGTPLYMAPECVNDNEYGSAADVWALGCAVVEMFSGKTAWSVKEGSHFMSLLIRIGVGDELPKIPEMLSEEGKDFLSKCFVKDPAKRWTAEMLLNHSFVTIDLEDDHRENFVVKVKDEDKVLMSPKCPFEFDDWDSFTLDSNPSFDSPVERLGSLVSGSIPDWSVGGSWLTVR
Protein: GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase) (Q5APF2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9P772}.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- Adenine phosphoribosyltransferase
- CTP synthase
- Guanylate kinase
- Inosine triphosphate pyrophosphatase
- arginine--tRNA ligase
- Hypoxanthine phosphoribosyltransferase
- Ribosome biogenesis protein ERB1
- 3'\5'-cyclic-nucleotide phosphodiesterase PDE1
- ubiquitinyl hydrolase 1
Sequence:
MSANIDDVPIEVSKVFDTILVLDFGSQYSHLITRRLREFNVYAEMLPCTQKIAELSWKPKGIILSGGPYSVYAEDAPHVDHDIFKLGVPILGICYGMQELAWINGKGVARGDKREYGPATLNVEDPECALFKGVDHSQVWMSHGDKLHALPTGFKVVATSDNSPFCGISNESEHIYGIQFHPEVTHTVQGKKLLKNFAVDICQAKTNWSMENFIDTEIARIKKLVGPTAEVIGAVSGGVDSTVGAKIMKEAIGDRFHAIYVDNGVMRKNETESVKKTLDEGLGINLTVVDAGDLFLGRLKGVTDPEKKRKIIGNTFIHVFEEEAAKIKPRDGSEIEYLLQGTLYPDVIESISFKGPSQTIKTHHNVGGLLEDMKLKLIEPLRELFKDEVRHLGELLGVPEDLVWRHPFPGPGLAIRVLGEVTKEQVKIAREADAIFIEEIKKAGLYRQISQAFAALLPVKSVGVMGDQRTYEQVIALRAIETLDFMTADWFIFEAAFLKKVASRIVNEVDGVARVTYDITSKPPATVEWE
Protein: AP-4 complex subunit sigma-1 (AP-4 adaptor complex subunit sigma-1) (Adaptor-related protein complex 4 subunit sigma-1) (Sigma-1 subunit of AP-4) (Sigma-4-adaptin) (Sigma4-adaptin) (Q9WVL1)
Organism: Mus musculus (Mouse)
Function: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y587}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y587}.
Interaction partners:
- AP-4 complex subunit epsilon-1
- AP-4 complex subunit beta-1
- AP-4 complex subunit mu-1
- AP-4 complex accessory subunit Tepsin
- AP-5 complex subunit mu-1
- AP-2 complex subunit beta
- AP-2 complex subunit alpha-1
- AP-5 complex subunit zeta-1
- AP-5 complex subunit sigma-1
- AP-2 complex subunit mu
Sequence:
MIKFFLMVNKQGQTRLSKYYEHVDINKRALLETEVSKSCLSRSSEQCSFIEYKDFKLIYRQYAALFVVVGVNDTENEMAIYEFIHNFVEVLDGYFSRVSELDIMFNLDKVHIILDEMVLNGCIVETNRARILAPLLILDKLSES
Protein: DNA primase large subunit (DNA primase 58 kDa subunit) (p58) (P49643)
Organism: Homo sapiens (Human)
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 via direct interactions with MCM10 and WDHD1 (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. Binds RNA:DNA duplex and coordinates the catalytic activities of PRIM1 and POLA2 during primase-to-polymerase switch.
Interaction partners:
- DNA primase small subunit
- DNA polymerase alpha catalytic subunit
- DNA polymerase alpha subunit B
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit 2
- DNA polymerase zeta catalytic subunit
- DNA replication licensing factor MCM3
- CST complex subunit STN1
- Replication protein A 32 kDa subunit
Sequence:
MEFSGRKWRKLRLAGDQRNASYPHCLQFYLQPPSENISLIEFENLAIDRVKLLKSVENLGVSYVKGTEQYQSKLESELRKLKFSYRENLEDEYEPRRRDHISHFILRLAYCQSEELRRWFIQQEMDLLRFRFSILPKDKIQDFLKDSQLQFEAISDEEKTLREQEIVASSPSLSGLKLGFESIYKIPFADALDLFRGRKVYLEDGFAYVPLKDIVAIILNEFRAKLSKALALTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQGNVGKISLDQIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGLFLKGIGLTLEQALQFWKQEFIKGKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCLKIILSNPPSQGDYHGCPFRHSDPELLKQKLQSYKISPGGISQILDLVKGTHYQVACQKYFEMIHNVDDCGFSLNHPNQFFCESQRILNGGKDIKKEPIQPETPQPKPSVQKTKDASSALASLNSSLEMDMEGLEDYFSEDS
Protein: Alkaline phosphatase isozyme conversion protein (EC 3.4.11.-) (P10423)
Organism: Escherichia coli (strain K12)
Function: This protein, presumably an aminopeptidase, mediates the conversion of E.coli alkaline phosphatase isozyme 1, to isozymes 2 and 3 by removing, one by one, the two N-terminal arginine residues.
Interaction partners:
- Uncharacterized sugar kinase YgcE
- 7-carboxy-7-deazaguanine synthase
- O-acetyltransferase WecH
- Uncharacterized protein YbaE
- Protein SseB
Sequence:
MFSALRHRTAALALGVCFILPVHASSPKPGDFANTQARHIATFFPGRMTGTPAEMLSADYIRQQFQQMGYRSDIRTFNSRYIYTARDNRKSWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPLSDADADANLGGLTLQGMDDNAAGLGVMLELAERLKNTPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGDKLYFNSGVKTPEAVRKLTRDRALAIARSHGIAATTNPGLNKNYPKGTGCCNDAEIFDKAGIAVLSVEATNWNLGNKDGYQQRAKTPAFPAGNSWHDVRLDNHQHIDKALPGRIERRCRDVMRIMLPLVKELAKAS
Protein: Segregation/condensation protein A (Q8TZY3)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Interaction partners:
- SMC-Scp complex subunit ScpB
- Chromosome partition protein Smc
Sequence:
MEIEVTPVDILLQLVKMGKVDPWNIDIVDLTEKYIKMLREMQELDLRISARAILAAAILVRMKSEALLNEDSREQEEKEEERIRVEVDPLVPPLRRVERYYTLDDLIDALMEALEEAERRKPKKKKKVEIDEEIFVIDDFRVDIEKYVEELYKVVKKIYEKTGTPIKFWDLVPDVEPKIIARTFLYLLFLENMGRVEIIQEEPFGEILVVPM
Protein: Tetratricopeptide repeat (TPR)-like superfamily protein (F4JX83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASLPVQFTRNQISSPFFSVNLRREPRSLVTVHCSAKVVYVILICIMFSAGENRENGEGVKKSLFPLKELGSIACAALCACTLTIASPVIAANQRLPPLSTEPDRCEKAFVGNTIGQANGVYDKPLDLRFCDYTNDQTNLKGKTLSAALMVGAKFDGADMTEVVMSKAYAVEASFKGVNFTNAVIDRVNFGKSNLKGAVFRNTVLSGSTFEEANLEDVVFEDTIIGYIDLQKICRNESINEEGRLVLGCR
Protein: Isoflavone 4'-O-methyltransferase (LjHI4'OMT) (EC 2.1.1.46) (2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase) (EC 2.1.1.212) (S-adenosyl-L-methionine: 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase) (Q84KK4)
Organism: Lotus japonicus (Lotus corniculatus var. japonicus)
Function: 2-hydroxyisoflavanone 4'-O-methyltransferase involved in the biosynthesis of formononetin. Can use 2,7,4'-trihydroxyisoflavanone as substrate, but not daidzein.
Interaction partners:
Sequence:
MDFSSSNGSEDTELSQAQIHLYKHVYNFVSSMALKSAMELGIADVIHSHGKPITLPELATALNLRPSKIGVLHRFLRLLTHNGFFAKTTVSRGEGAEEETAYGLTPPSKLLVKSNSTCLAPIVKGALHPSSLDMWRSSKKWFLEDNEELTLFESATGESFWEFLNKETESDTLSMFQEAMAADSHMFKLALKECKHVFEGLGSLVDVAGGRGGVTKLIREAFPHVKCTVFDQPQVVANLTGDENLNFVGGDMFKSVPPADAVLLKWVLHDWNDELSLKILKNCKEAISGRGKEGKVIIIDISIDETSDDRELTELKLDYDLVMLTMFNGKEREKKEWEKLIYDAGFSSYKITPICGFKSLIEVFP
Protein: Transcription factor GTE11 (BROMODOMAIN AND EXTRATERMINAL DOMAIN PROTEIN 10) (AtBET10) (Bromodomain-containing protein GTE11) (Protein GLOBAL TRANSCRIPTION FACTOR GROUP E11) (Q93ZB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- BTB/POZ and TAZ domain-containing protein 2
- U-box domain-containing protein 3
- Phosphoinositide phosphatase SAC2
- Protein SHOOT GRAVITROPISM 6
- At1g61215
Sequence:
MTVRNGGFPGDYNRNSFDSPGGCDDSPNASKDDETFGVPRIVLPLSDLSSSERRKWIHTLRQELEQLRSFQKSVGDLLPISKIVTSTPASNVSRPKSFGMSRCSTGPGKRVLPFTATKPEPVTTSTMLRMKQCESLLKRLMSQQHCWLFNTPVDVVKLNIPDYFTIIKHPMDLGTVKSKLTSGTYSSPSEFSADVRLTFRNAMTYNPSDNNVYRFADTLSKFFEVRWKTIEKKSSGTKSEPSNLATLAHKDIAIPEPVAKKRKMNAVKRNSLLEPAKRVMTDEDRVKLGRDLGSLTEFPVQIINFLRDHSSKEERSGDDEIEIDINDLSHDALFQLRDLFDEFLRENQKKDSNGEPCVLELLHGSGPGNSLTQHCDGSELEDEDVDIGNYEHPISHISTVRTEKDSVGGLNQMEDASRGKLSLIEGADGHQDGNSAPKEKELPPEKRYRAALLKNRFADIILKAQEITLNQNEKRDPETLQREKEELELQKKKEKARLQAEAKEAEEARRKAEAQEAKRKLELEREAARQALLEMEKSVEINENTRFLKDLELLKTVNTDQLRNLRDVGSESDGLAVFGFGGSNPLEQLGLFMKHEEDEDESDMLAFPDPGNEVEEGEID
Protein: Bifocal (O16125)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}. Rough endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004269}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004269}.
Interaction partners:
Sequence:
MESQKRPSLDLHTDVPAGLAAGGSGLGAAAEMSPTSGFLPDMPQWKKDLIQRRKTNVPAPRRVHHLAHRWQLWGFGRSNAAPGAIADFTEPATISSTSQKRNMIGSEEKSEKSSISNTNSDSTGGHHSVVAVSLSPDAAATTNVTVTPIPKQRSSLLNTRSQEREMVRYILSESGERDGELESGEQPAGVVSNSRCGEVETGTIGSPSSSANQNPNPNHLKTKCKPGQSVAEGKPSAKETIVDNSKSCSKTKSISDKLQSNKFIIQQQQQQQQQQQQQQQLSPTKVTVKPTMVAMQEMKKTTKQNGQHRHLAGKIGSVAGGDVDPQHPPTNPIPDSLDTGEDLSYGPGIVSKLRCRYLSLALRESRQQSSKQRLQRSTSLNTLLDRDDDEVEVEEPEMTNSQVRAKSTPPPILGAKPTPKPSSQHQRPVSLGANGAGSAVNPPSNSDQAQTGAVANGGAGSGQRSRHFKRGNEVMKRARSVEALLCEKSPWNSQRISTAGAAAAAAPSPPAPKATATAPSPVTSPTCVTIEDKIHNARERLHSGTDTAPPKRLTSIIDDTERPPPDLVKQTLKMFEASANRRPRAAHRSNGVGGVASKVANYKSIIKDQKQPSSAAATPPPTGMGFASSTPLRHVHPDIIPRQVDSPVSALSVMIARMELQEPETPERETRDAEATPQTEALSETERNDRDEGDGEVDDDNHNNNDDDHDDGDDGSDNNEQRDKMGAAAAGDKPKPPAESAAGGAQRSFAASTENAHVASGSSSSTSASVRKLSNNNDSSSGPAVTKQIGVIRPLFNSQGAGSTPLTSREIEKNRINEMKKSTATDAGGSVSGSGTVAGAGSGTSPTTSLDSVINTKEAASSETDASASPLWTLRNVRNQSQTAGGGSGPSSSLHSTENTSMVFNFSKSTKEVPDYIESDVVIYRRKRELPNGNEPGFVLLGDLSVETSTDTDYDDYSMCPPSPCDVEFENANIVIDGKSSIRQKPKESSFRVQFNDTLTSTFEYPSEASMTIEDPPYADPFGHVSKHHQMLLAEQMHLLQHQEQLELEQMHQLGLRPEQHHHVTVDEIIELPTSTAGHGHGIGLGHRSGAAGGGGTMLGNLPLDII
Protein: Glutathione S-transferase D5 (EC 2.5.1.18) (Q9VG95)
Organism: Drosophila melanogaster (Fruit fly)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May be involved in detoxification.
Interaction partners:
- Glutathione S-transferase D2
- Glutathione S-transferase D7
- Glutathione S-transferase D4
- Glutathione S-transferase D1
- Bifunctional glutamate/proline--tRNA ligase
- Glutathione S transferase D9, isoform A
- Uncharacterized protein, isoform C
- GH16740p
- GM20958p
- Putative gustatory receptor 22d
Sequence:
MDFYYSPRGSGCRTVIMVAKALGVKLNMKLLNTLEKDQLKPEFVKLNPQHTIPTLVDNGFSIWESRAIAVYLVEKYGKDDTLFPKDPKKQALVNQRLYFDMGTLYDSFAKYYYPLFHTGKPGSDEDFKKIESSFEYLNIFLEGQNYVAGDHLTVADIAILSTVSTFEIFDFDLNKYPNVARWYANAKKVTPGWEENWKGAVELKGVFDARQAAAKQ
Protein: Transcription activation suppressor family member 2 (A0A2R8YH03)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSIYDINREQDYVKNSEGILGENELRPPSQLHSLLEKIETGSLSEKIFETVSLSSDSLFQRAVSLLHTSYLDSSSEHGFQYSQVTLVKNDIFLNEYKTFYQQKKASSYTQEELQDTYGFLLFDTEKQAKLVCQCGLRVGSSAVTTLGDPAKGVYISKYSDCLHSRPWYHGKSGYVVIFNIIKYYFYELSGNTVIERPRQICPYVIVAFRYRESKTMAPPAHKSILERSENVLMSPWKGKLIVQDRMLCDIALWSTYGAMIPTQLPQELDFKYVMKVSSLKKRLPEAAFRKQNYLEEKVCFQDLCFNLYEVELSNRQGENIDKLTECIKNKQLAIIKCLEDRGFFILLTSSALLSEPDFGGKQMGLHGLHLFRSPLSTGVKDLKVEDDISMKVIPILSTLNCALLETKKSLPEERIHPNTLVKRHFQELYKADRSPSLSVAPQDRMKDPTFLGKLPSGFDLIPPAEKCPSESLTQLNSYFSDPSAYILEVSTALDLLAEHPQSPCVSDGICDAGFSLVMTPDPEFLVSEAEVRKETETKKDSEEMLKAKKRVFPLSPASNLRVQPKRKASMPHMVQSKKVNLCRPFPKRTASRADNSSDSPTTLKLVKGQFPQKRKRGAEVLTAQFVQKTKLDRKNQEAPISKDVPVPTNAKRARKQEKSPVKTVPRAKPPVKKSPQKQRVNIVKGNENPRNRKQLQPVKGETASKLQSEISRGCQEDGISINSVQPENTTAAHNDLPENSIVNYDSQALNMLADLALSSATSSTPVSEARNLHCSSELPQNDVLLSKENSLRGTSDHEYHRGVKTQKGELLPNPSSDRKSNSGSDLTVSQDEESLVPCSQAPAKAQSALTEEMLESSDASQSSSVSVEHSYALLLTEHSKKHLQEREILSPLFPRNGTKSPEAATPVGKVMPFRHQPGLLLQQKPPDDPVVKPKDRPPSARVKKSSCSRIVLSCDDSVKITFKCETEYAFSLDSKYTNNPLEKTVVRALHGPWNTDLPDNVEEVKLLLHMWVALFYSNQNKIIRSSRKVVEHSNPAKYVSINSTLESCELREIEESLGLEKCSADSLLETNEISRAHAAEVSFRDPNCLLPFIKTPLTQGLELCVQNEQKKTFARECDPDTQEDQNFICSYNNEVTGEEAKQESLETSNLVLSGIGSTQTNGPSVPSEEEIVQPLDSTRVASYSGTVTQATFTRTYDGPGSQPVICQSSVYGTLENKVDILDAAVQTKTGTLQDLIQHGSPINNECHPSLERKDDNMGCAVINPEPITLTFEKNAHVPIQTEGVNTADERTTFKKELIKQVSPAASLRHPVSTSENARTQGLRDIPSLVVAGQKGTKYLCASSVGGETLDKAVCSLQKETPLPVSLPSDKTMVMEALSLAKSSSHLSPSEEVRCTQDFLSQTQSLLGLSSEGLLELTQVEVDSSSASTTLGRQCSLNCISSGCHTSGDSLELRKNHKNGPNTENMNLEAFDSVFIKQTSLSVSREVSLELSEEDSDIDLALTISPPTSPREEMPAGEIEQFEEAPFSNLELQDVAEEIGEPEEVALTESREVSSADNVSVYPSVSEEPVENKERKGDNLQPVTLILSKENCTLEIAEEINVTSDFPFDSVIEEVSPASSPEPPVPVKETRPYQAVTPCILKLHGTQCEKSNQISQCESEDLGITEKENVFVGPTHPVGQDNFTQVQQMQVSAEMPLILTDHPGRTGRPTLPGKVTEEIVSSEHDEGLSFSGKVQCYGRELNQPASAAKCTGDFSPSPEKLVKSGNPLQPVSIENRNLDLKHLVLESSEPPFGPRNVIENKSLSDTLVSTTAPSGIVNVSVKQQTSPKSSQNHLFPGDLKTDEGIYLQVKSLTAASVDGAYSTQGCMCSVVPTLCSSSDNATLTHYVRPINAEPVFQAQEIPAGRMASLLKNGEPEAELHKETTGPGTAGPQSNTTSSLKGERKAIHTLQDVSTCETKELLNVGVSSLCAGPYQNTADTKENLSKEPLASFVSESFDTSVCGIATEHVEIENSGEGLRAEAGSETLGRDGEVGVNSDMHYELSGDSDLDLLGDCRNPRLDLEDSYTLRGSYTRKKDVPTDGYESSLNFHNNNQEDWGCSSWVPGMETSLPPGHWTAAVKKEEKCVPPYVQIRDLHGILRTYANFSITKELKDTMRTSHGLRRHPSFSANCGLPSSWTSTWQVADDLTQNTLDLEYLRFAHKLKQTIKNGDSQHSASSANVFPKESPTQISIGAFPSTKISEAPFLHPAPRSRSPLLVTVVESDPRPQGQPRRGYTASSLDSSSSWRERCSHNRDLRNSQRNHTVSFHLNKLKYNSTVKESRNDISLILNEYAEFNKVMKNSNQFIFQDKELNDVSGEATAQEMYLPFPGRSASYEDIIIDVCTNLHVKLRSVVKEACKSTFLFYLVETEDKSFFVRTKNLLRKGGHTEIEPQHFCQAFHRENDTLIIIIRNEDISSHLHQIPSLLKLKHFPSVIFAGVDSPGDVLDHTYQELFRAGGFVISDDKILEAVTLVQLKEIIKILEKLNGNGRWKWLLHYRENKKLKEDERVDSTAHKKNIMLKSFQSANIIELLHYHQCDSRSSTKAEILKCLLNLQIQHIDARFAVLLTDKPTIPREVFENSGILVTDVNNFIENIEKIAAPFRSSYW
Protein: FAS1 domain-containing protein YDR262W (Q12331)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcriptional regulatory protein RCO1
- Transcriptional regulatory protein SDS3
- Uncharacterized WD repeat-containing protein YNL035C
- Regulator of rDNA transcription protein 5
- UPF0659 protein YMR090W
- Uncharacterized membrane protein TOS7
- Chromatin modification-related protein EAF3
- Probable histone deacetylase HOS2
- Histone deacetylase HOS1
- Histone deacetylase RPD3
Sequence:
MIFNLPVSVLLYFSLIWAMEPSFVRGKNVVNLITFKDSNGKLHKRLAPEEIPPRLHNSQVNSYPLGYKGMRDFSRPAVNLDDILGTQQRKQQEFLAELSPLSLESKLSLVNEVQIFASYVRNDVETYNKVSDPNEDLIIIAPTNRAVSQLTLKPWQFPNNIDKLESDGATEKELDTAIQENISKFVRSHIVVYNDDKNSYKKVSPGCTLLQSIDFTESKKSDSETGGDILLKKEGEVYYVASSRDEKFHAVESIENGSNGVILMVDFTLVGP