wanglab/gogpt-training-data huggingface dataset:
Protein: Caskin, isoform F (A0A0B4LF60)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVSCLLEIFAHLFEDGGFRLAYAAYRVAVLLLLLFCCDIHFDGVGSIEEWLQLLRLEEYIQPLLEQNYKTVRDVTQVTWEDLEDIGIVKLGHQKKILLAIKRVKDIISGKWNPGGANAYQQQEYQRKPWQFNVPIPSTPSYVPTTRVSWDDTKIYATSSVLNSTAPSGSSCLNSSLANGDAYYCTGSNHECCSGNDVVLIKVRQPRGKSLESLEDIHDNSTRSHLTFSHYTTTDYGHFGPPTTAAAAAAMAAAATLQQQHHHQQLLHQQQQQAAAARLLGNNAPGIGWRRSYDDGDITPTNDATRELLYEQEGGGTLPRQQRGILQRAVLNTMPPLEHHHYMNAAAAAEYGAASGVEGGANYMGGSPLTGKKIAPEPPRRHCSIRNSRTLSGEGVPSGAAAQAHQQAAQQQQGQHMFYGHTAQHWQQQQQQAGAGTGQQPIYANYATIQQTTAEIHCEKYHDSKSTSSIDSIDTIPFANENTGTIKQRLLNRQELQGGGAGNNNVPGGGHPAHLHSSSSSSSSSSTNTIANIAHSFHSLKSSSSLHDATLARSESMGSTASGGSALHLRSPTLDMSNAGGSTAEPASSPEAAVPTVAINNGVPPKVSVNVLNDIGNMLANLTDELDAMLEEEKRVGLNIDSE
Protein: ATP-dependent protease La (LON) domain protein (F6F9.20 protein) (Q9FXH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable membrane metalloprotease ARASP2, chloroplastic
- Membrane metalloprotease ARASP, chloroplastic
- ATP-dependent Clp protease ATP-binding subunit CLPT2
- Pentatricopeptide repeat-containing protein At1g01970
- Putative chloroplast RNA binding protein family protein)
- ATP-dependent Clp protease ATP-binding subunit CLPT1, chloroplastic
- Mitochondrial transcription termination factor family protein
- Peptidyl-prolyl cis-trans isomerase CYP26-2, chloroplastic
- At2g27680/F15K20.22
- Thylakoid lumenal protein TL20.3
Sequence:
MALPSTVSSPSFKSTPPYLSAFNPKPLHLPATYRSINRRSCKLLSFRCSSSSFSEKHHNNANPPKSDDLVELPLFPLPLVLFPGATIPLQIFEFRYRVMMQTLLQSDLRFGVVYSDAVSGSAAGIGCVGEIVKHERLVDDRFFLICKGQERFRVTDLVRTKPYLVAKVTWLEDRPSGEENLDELANEVEVLMKEVIRLSNRLNGKPDKESQDLRKNQFPTPFSFFVGSTFEGAPMEQQALLELEDTAARLKRERETLRNTLNYLTAASAVKDVFPSQP
Protein: Protein IQ-DOMAIN 14 (AtIQD14) (Q8LPG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking. Regulates cell and organ shapes (prevents twisting) in aerial parts probably by regulating transverse microtubules (MT) arrays alignment. Regulates the formation of oval xylem secondary cell-wall deposition pits through microtubule-dependent lateral inhibition of Rho GTPase domains, thus confining the area of active ROP domains within the lattice of the cortical microtubules. May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}.
Interaction partners:
- AT5g04550/T32M21_140)
- Putative pectinesterase/pectinesterase inhibitor 43
- Protein REDUCED CHLOROPLAST COVERAGE 2
- Rho GTPase-activating protein 1
- M phase phosphoprotein 10
- Putative pectinesterase/pectinesterase inhibitor 45
Sequence:
MVKKGSWFSAIKRVFTPHSKEKLANEPERKSGKEKKKKGFGKLRHGETNSFLPIFREPSSIEKILGEAERDHNLVFRPPTPDRPNPYSASPPPRPASPRVASPRPTSPRVASPRVPSPRAEVPRTLSPKPPSPRAEVPRSLSPKPPSPRADLPRSLSPKPFDRSKPSSASANAPPTLRPASTRVPSQRITPHSVPSPRPSSPRGASPQAISSKPPSPRAEPPTLDTPRPPSPRAASLRADPPRLDAARPTTPRPPSPLADAPRLDAPRPTTPKPPSPRSDPPRLDAPRPTTPKPPSPRSVSPRAVQRREIVYRPEPTLPVQHASATKIQGAFRGYMARKSFRALKGLVRLQGVVRGYSVKRQTINAMKYMQQVVRVQSQIQSRRIKMLENQAQVEKDEAKWAASEAGNDNWDDSVLTKEERDSRSQRKTDAIIKRERSMAYAYSRKLWKNSPKSTQDNRSFPQWWNWVDRQNPLASPAPSYSQPQRDFRLTPSRLCPSPLSQSSKQHHIRLDNHFDTSTPRSSRSTFHTPSRPIHTGTSRYSRGRLRGQDSPFKDDDSLTSCPPFPSYMAPTVSAKAKVRPNSNPKERVMGTPVSEKRRMSYPPTQDTFRWNKGSLVMSNSSSHRGPGSPGGVVLEKHKTLKSVGNLSIGSTASMATTVGRKEFNRFV
Protein: Signal transducer and activator of transcription 4 (P42228)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator mainly expressed in hematopoietic cells that plays a critical role in cellular growth, differentiation and immune response. Plays a key role in the differentiation of T-helper 1 cells and the production of interferon-gamma. Participates also in multiple neutrophil functions including chemotaxis and production of the neutrophil extracellular traps. After IL12 binding to its receptor IL12RB2, STAT4 interacts with the intracellular domain of IL12RB2 and becomes tyrosine phosphorylated. Phosphorylated STAT4 then homodimerizes and migrates to the nucleus where it can recognize STAT target sequences present in IL12 responsive genes. Although IL12 appears to be the predominant activating signal, STAT4 can also be phosphorylated and activated in response to IFN-gamma stimulation via JAK1 and TYK2 and in response to different interleukins including IL23, IL2 and IL35 (By similarity). Transcription activation of IFN-gamma gene is mediated by interaction with JUN that forms a complex that efficiently interacts with the AP-1-related sequence of the IFN-gamma promoter. In response to IFN-alpha/beta signaling, acts as a transcriptional repressor and suppresses IL5 and IL13 mRNA expression during response to T-cell receptor (TCR) activation (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250|UniProtKB:Q14765}. Note=Translocated into the nucleus in response to phosphorylation. {ECO:0000250|UniProtKB:Q14765}.
Interaction partners:
- Non-receptor tyrosine-protein kinase TYK2
- Tyrosine-protein kinase JAK2
- Signal transducer and activator of transcription 1
- Interleukin-12 receptor subunit beta-1
- Tyrosine-protein kinase JAK3
- Interleukin-12 receptor subunit beta-2
- Interferon regulatory factor 9
- Signal transducer and activator of transcription 3
- Tyrosine-protein phosphatase non-receptor type 2
- Cytokine-inducible SH2-containing protein
Sequence:
MSQWNQVQQLEIKFLEQVDQFYDDNFPMEIRHLLAQWIETQDWEVASNNETMATILLQNLLIQLDEQLGRVSKEKNLLLIHNLKRIRKVLQGKFHGNPMHVAVVISNCLREERRILAAANMPIQGPLEKSLQSSSVSERQRNVEHKVSAIKNSVQMTEQDTKYLEDLQDEFDYRYKTIQTMDQGDKNSILVNQEVLTLLQEMLNSLDFKRKEALSKMTQIVNETDLLMNSMLLEELQDWKKRQQIACIGGPLHNGLDQLQNCFTLLAESLFQLRQQLEKLQEQSTKMTYEGDPIPAQRAHLLERATFLIYNLFKNSFVVERQPCMPTHPQRPMVLKTLIQFTVKLRLLIKLPELNYQVKVKASIDKNVSTLSNRRFVLCGTHVKAMSSEESSNGSLSVEFRHLQPKEMKCSTGSKGNEGCHMVTEELHSITFETQICLYGLTINLETSSLPVVMISNVSQLPNAWASIIWYNVSTNDSQNLVFFNNPPSVTLGQLLEVMSWQFSSYVGRGLNSEQLNMLAEKLTVQSNYNDGHLTWAKFCKEHLPGKTFTFWTWLEAILDLIKKHILPLWIDGYIMGFVSKEKERLLLKDKMPGTFLLRFSESHLGGITFTWVDQSENGEVRFHSVEPYNKGRLSALAFADILRDYKVIMAENIPENPLKYLYPDIPKDKAFGKHYSSQPCEVSRPTERGDKGYVPSVFIPISTIRSDSTEPQSPSDLLPMSPSAYAVLRENLSPTTIETAMNSPYSAE
Protein: Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta) (P0A836)
Organism: Escherichia coli (strain K12)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. Can use either ATP or GTP, but prefers ATP. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed.
Interaction partners:
- Succinate--CoA ligase subunit alpha
- Succinate dehydrogenase flavoprotein subunit
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- 2-oxoglutarate dehydrogenase E1 component
- Succinate dehydrogenase cytochrome b556 subunit
- Succinate dehydrogenase iron-sulfur subunit
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- Citrate synthase
- Isocitrate dehydrogenase
- Aconitate hydratase B
Sequence:
MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKRLVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQGRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDPREAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEGK
Protein: Histone-arginine methyltransferase METTL23 (EC 2.1.1.319) (Methyltransferase-like protein 23) (A2AA28)
Organism: Mus musculus (Mouse)
Function: Histone methyltransferase that dimethylates histone H3 at 'Arg-17', forming asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. Maternal factor involved in epigenetic chromatin reprogramming of the paternal genome in the zygote: mediates H3R17me2a, promoting histone H3.3 incorporation in the male pronucleus, leading to TET3 recruitment and subsequent DNA demethylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:28930672}. Cytoplasm {ECO:0000269|PubMed:28930672}. Note=Localizes in male and female zygote pronucleus and cytoplasm. {ECO:0000269|PubMed:28930672}.
Interaction partners:
- GA-binding protein alpha chain
- Methyltransferase-like protein 22
Sequence:
MDSVRPRAPWAPPPDPASLDSPTCEPGLMAGTQLFRFREEPVPGGNRAVLEVRVPQVLHVQYGMYVWPCAVVLAQYLWFHRRSLPGKAVLEVGAGVSLPGILAAKCGAKVILSDSSEFPHCLDICRQSCQMNNLPQVEVVGLTWGHISKDILSLPPQDIILGSDVFFEPEDFESILATVYFLMQKNPKVQFWSTYQVRSADWSLEGLLYKWDMKCVHIPLESFDADKEDIAESTLPGRHTVEMLIISFAKDSF
Protein: Farnesyl diphosphate synthase (Dfps) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Geranyltranstransferase) (Q9NH03)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a sterol precursor. Involved in the inhibition of cell growth.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Isopentenyl-diphosphate Delta-isomerase
- Squalene synthase
- Diphosphomevalonate decarboxylase
- Alkyl transferase
- Geranylgeranyl pyrophosphate synthase
- ditrans,polycis-polyprenyl diphosphate synthase [
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
- Probable farnesyl diphosphate synthase DDB_G0268742
- Cycloartenol synthase
Sequence:
MNNQSLQRAAMISEHLAPTSELNMNQTSAPIKTAKEELADFVEIFPILTNEILKELPGMDMPPQTIAWVEKMINVNVSGGKMNRGLTVLHSLQLLVEGRQLSRSEIFLANVLGWCVEWLQAFFLVADDIMDQSITRRGQPCWYRQANPISNNGTIGSIAINDSFILESCIYILIKKYFRNEPYYADILDIFHETSYQTELGQLLDLTTQPNRGDFSLFTLNTYRRIVKYKTAYYSFYLPVALAMLMAGITSTPAFSTAKDILLPMGEFFQVQDDFLDCYGSPAVIGKIGRDIEENKCSWMICQAILNGTPEQINLLKKHYGLDNPTDVELVKKIYGEIGLKKIFKDYEDESYAFLISKIKSVRIMPQEVFIKLLSKIYKRDL
Protein: phosphorylase kinase (EC 2.7.11.19) (Q9I7D0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable phosphorylase b kinase regulatory subunit beta
- Probable phosphorylase b kinase regulatory subunit alpha
- LP02557p
Sequence:
MAKDEEDDLLPDKDAAKGFYAKYEPKEILGRGISSTVRRCIEKETGKEFAAKIIDLGATTESGETNPYHMLEATRQEISILRQVMGHPYIIDLQDVFESDAFVFLVFELCPKGELFDYLTSVVTLSEKKTRTIMRQIFEGVEYIHAKSIVHRDLKPENILLDENHNVKITDFGFAKQLQEGEKLTNLCGTPGYLAPETLKCNMFEGSPGYSQEVDIWACGVIMFTLLVGCPPFWHRKQMVMLRNIMEGKYSFTSPEWADISEDPKDLIRKCLVVDPSQRITVKEVLRHPFFNQMVLMGDRRHPAPPIAPAQTNSRHLLQPEASSYRFGQLNSSCAGAPNYLYCAPQSSYSSNRMRDGALDDAGASAASATCHVMSPSNASNSYATNTTANTSNSALASASSHKTLTAMVYYQQQPQQHQTQQQQQQYQQQQTTQLPVQLQLQHPLLQTGGDGKQSVYAPPTVQLRKQSRFNARKKFQFAILVIRAIIRIRRLRFTAEPLHVEEAIRDPYRVKVLRKVIDGCAFRVYGHWVKKGEGQNRAALFENTPRTELHALYINNLSR
Protein: Ycf3-interacting protein 1, chloroplastic (Protein CHLOROPLAST ENHANCING STRESS TOLERANCE) (AtCEST) (Q9LU01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nuclear genome-encoded factor that participates in photosystem I (PSI) biogenesis. Cooperates with the plastid genome-encoded protein PSI assembly Ycf3 in the assembly of stable PSI units in the thylakoid membrane. Involved in light-induced chloroplast development and growth. Involved in the plant response to abiotic and photooxidative stresses. May be involved in the suppression of photooxidative damage.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:20807881, ECO:0000305|PubMed:20876334}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosystem I assembly protein Ycf3
- Tetratricopeptide repeat domain-containing protein PYG7, chloroplastic
- Eukaryotic aspartyl protease family protein
- Photosystem I assembly factor PSA3, chloroplastic
- Photosystem I assembly protein Ycf4
- Photosystem I iron-sulfur center
Sequence:
MTTQIFQLPLKYCASSFSSTGQRNYGASSSPSPIVICKSNGISDGLWVKRRKNNRRFGSLIVKQEKGDVTEIRVPVPLTLEQQEKEKQNRDDEEDEIDEGDVDPEDLKYVNEIKRVIELLRRNRDMIFSEVKLTIMIEDPRELERRRLLGIEDADTPSRDDLAEALEQVNDGKIPKDRATLRMLHEEMIRWPNLEVEVSKKQRGKSMYAKSTDTGIDPKEAAKRLNVEWDSAAAIEEVDVDDEQGVVTKVAGYGALYFVSALPVIIGISVVLILFYNSLQ
Protein: Protein sda1 (Q10342)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for 60S pre-ribosomal subunits export to the cytoplasm. May also be required for 60S ribosomal subunit maturation and accumulation (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Ribosome biogenesis protein NOP53
- Nucleolar GTP-binding protein 2
- Probable nucleolar GTP-binding protein 1
- Ribosome assembly protein 4
- GTPase grn1
- Pescadillo homolog
- Ribosome biogenesis protein nsa2
- Pre-rRNA-processing protein crb3/ipi3
- Ribosome assembly factor mrt4
- Uncharacterized RNA-binding protein C1827.05c
Sequence:
MVKRRTAAVLPNNLPHLQHLVKKDPKSYREEFLQQWNHYETAREIFLVNPSSDISEFCSLIDFISQTCNYYHDVTADFPSELIELLQKNHTIFPFELCEKIVLCLVLLKNKTVISPITLLQCFFPLFRENPTRGVRELLYQQVSLTIRNANKQAKNDKLNKAVQSALFTLVDGSGSGSATHTDYSGQKREYSASELSGVWAVKMVRDLWKRNVWSGDARAVNIMKSAALSSNPKVMLAGIYFFLGADNQEEEEESDDEGPDVSKLLHQANVNKKTKSREAALLRARAVVKKKERGKQNVPTNVNFPALQLLHDPQGFAEELFEKHLASSKSRLSMDQKLVVLRLLTRLVGSHKLTVLGLYSFLMKYLTPHQRDVTQFLACLAQASHEFVPPDALEPLVRKIADEFVTSGVANEVVCAGINAIREVCARAPLAMTPDLLQDLTEYKSSKDKGVMMASRSLITLYREVAPDMLKRKDRGKLASIEMKDRTPLKYGEELNVTHGIQGLELLAQYKAEHGEEGENGDDWDNWEVSEDGQNSDDSGGWIDVDSDDNIELSDSDEEEEKATARKESDEKGSSSQKELVDRMTELASQSILTPNDLKKLEELREQAGVDRLVNGPKRSLKRPDDAVEADEIEGPRKKAKNDREARIASVMEGREGRDKFSSKKAGFNPTSLSNKRKQRNKNFMMIKHKLKGKAGRSLVQKQKVLREHVAREKRKIK
Protein: Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit (Dihydroorotate oxidase B, electron transfer subunit) (P56968)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrDB subunit to the ultimate electron acceptor NAD(+).
Subcellular location: Cytoplasm.
Interaction partners:
- Dihydroorotate dehydrogenase B
- Dihydroorotate dehydrogenase A
- Orotate phosphoribosyltransferase
- Dihydroorotase
- Orotidine 5'-phosphate decarboxylase
- Carbamoyl phosphate synthase large chain
- Glutamate synthase, small subunit 1
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase small chain
- TFIIB-type zinc ribbon-containing protein
Sequence:
MSQLQEMMTVVSQREVAYNIFEMVLKGTLVDEMDLPGQFLHLAVPNGAMLLRRPISISSWDKRAKTCTILYRIGDETTGTYKLSKLESGAKVDVMGPLGNGFPVAEVTSTDKILIIGGGIGVPPLYELAKQLEKTGCQMTILLGFASENVKILENEFSNLKNVTLKIATDDGSYGTKGHVGMLMNEIDFEVDALYTCGAPAMLKAVAKKYDQLERLYISMESRMACGIGACYACVEHDKEDESHALKVCEDGPVFLGKQLSL
Protein: Spindle assembly checkpoint component MAD1 (Mitotic arrest deficient protein 1) (P40957)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Central component of the spindle assembly checkpoint. Thought to recruit MAD2 to unattached kinetochores. During checkpoint activity, MAD2 is relayed from the MAD1-MAD2 complex to the mitotic checkpoint complex (MCC). The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism.
Subcellular location: Nucleus.
Interaction partners:
- Mitotic spindle checkpoint component MAD2
- Spindle assembly checkpoint serine/threonine-protein kinase BUB1
- Serine/threonine-protein kinase MPS1
- APC/C activator protein CDH1
- Spindle assembly checkpoint component MAD3
- Origin recognition complex subunit 2
- Spindle assembly checkpoint protein BUB3
- APC/C activator protein CDC20
- Mitotic check point protein BUB2
- Mitotic check point protein BFA1
Sequence:
MDVRAALQCFFSALSGRFTGKKLGLEIYSIQYKMSNSGGSSPFLESPGGSPDVGSTNGQSNRQIQALQFKLNTLQNEYEIEKLQLQKQTNILEKKYKATIDELEKALNDTKYLYESNDKLEQELKSLKERSANSMNDKDKCIEELRTTLQNKDLEMETLRQQYDSKLSKVTNQCDHFKLEAESSHSLLMKYEKEIKRQSVDIKDLQHQVMEKDDELSSVKASKMINSHPNYSTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQSQDTSTFWKLENEKLQNKLSQLHVLESQYENLQLENIDLKSKLTKWEIYNDSDDDDDNNVNNNDNNNNNKNDNNNDNNNDTSNNNNINNNNRTKNNIRNNPEEIIRDWKLTKKECLILTDMNDKLRLDNNNLKLLNDEMALERNQILDLNKNYENNIVNLKRLNHELEQQKSLSFEECRLLREQLDGLYSAQNNALLEVENSETHASNKNVNEDMNNLIDTYKNKTEDLTNELKKLNDQLLSNSNDVETQRKKRKLTSDQIGLNYSQRLNELQLENVSVSRELSKAQTTIQLLQEKLEKLTKLKEKKIRILQLRDGPFIKDQFIKKNKLLLLEKENADLLNELKKNNPAVETVPISVYDSLNFELKQFEQEVFKSNKRFSRLKQVFNNKSLEFIDVVNSLLGFKLEFQQDSRVKIFSCFKPEKYLIADLNENTLKSNLDADIEGWDDLMNLWVEDRGQLPCFLATITLRLWEQRQAK
Protein: Vitamin K epoxide reductase domain-containing protein (E9PLN8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGSTWGSPGWVRLALCLTGLVLSLYALHVKAARARDRDYRALCDVGTAISCSRVFSSRWGRGFGLVEHVLGQDSILNQSNSIFGCIFYTLQLLLGLQAAQRACGQRGPGPPKPQEGNTVPGEWPWQASVRRQGAHICSGSLVADTWVLTAAHCFEKAAATELNSWS
Protein: Histone-lysine N-methyltransferase SUV39H2 (EC 2.1.1.355) (Histone H3-K9 methyltransferase 2) (H3-K9-HMTase 2) (Suppressor of variegation 3-9 homolog 2) (Su(var)3-9 homolog 2) (Q9EQQ0)
Organism: Mus musculus (Mouse)
Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H5I1}. Chromosome. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin during most stages of spermato- and spermiogenesis. Predominantly accumulates at the sex chromosomes present at the XY body.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 3, X-linked
- Eukaryotic translation initiation factor 2 subunit 3, Y-linked
- Chromobox protein homolog 3
- Histone H3.1
- Histone H3.2
- Histone H3.3
- DNA
- Histone-lysine N-methyltransferase KMT5C
- Histone-lysine N-methyltransferase KMT5B
- DNA damage-binding protein 1
Sequence:
MATARAKARGSEAGARCHRAPGPPPRPKARRTARRRRAETLTARRSRPSAGERRAGSQRAWSGAPRAAVFGDECARGALFKAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVAKGVEYYLVKWKGWPDSTNTWEPLRNLRCPQLLRQFSDDKKTYLAQERKCKAVNSKSLQPAIAEYIVQKAKQRIALQRWQDYLNRRKNHKGMIFVENTVDLEGPPLDFYYINEYRPAPGISINSEATFGCSCTDCFFDKCCPAEAGVVLAYNKKQQIKIQPGTPIYECNSRCRCGPECPNRIVQKGTQYSLCIFKTSNGCGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNKGITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFSVFIDNLDTRLPRIALFSTRTINAGEELTFDYQMKGSGEASSDSIDHSPAKKRVRTQCKCGAETCRGYLN
Protein: Zinc finger protein 555 (Q8NEP9)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription intermediary factor 1-beta
Sequence:
MDSVVFEDVAVDFTLEEWALLDSAQRDLYRDVMLETFQNLASVDDETQFKASGSVSQQDIYGEKIPKESKIATFTRNVSWASVLGKIWDSLSIEDQTTNQGRNLSRNHGLERLCESNDQCGEALSQIPHLNLYKKIPPGVKQYEYNTYGKVFMHRRTSLKSPITVHTGHKPYQCQECGQAYSCRSHLRMHVRTHNGERPYVCKLCGKTFPRTSSLNRHVRIHTAEKTYECKQCGKAFIDFSSLTSHLRSHTGEKPYKCKECGKAFSYSSTFRRHTITHTGEKPYKCKECAEAFSYSSTFRRHMISHTGEKPHKCKECGEAFSYSSAFRRHMITHTGEKPYECKQCGKTFIYLQSFRRHERIHTGEKPYECKQCGKTFIYPQSFRRHERTHGGEKPYECNQCGKAFSHPSSFRGHMRVHTGEKPYECKQCGKTFNWPISLRKHMRTHTREKPYECKQCGKAFSLSACFREHVRMHPEDKSYECKLCGKAFYCHISLQKHMRRHTAEKLYKCKQCGKAFSWPELLQQHVRTHTVEKPYECKECGKVFKWPSSLPIHMRLHTGEKPYQCKHCGKAFNCSSSLRRHVRIHTTEKQYKCNVGHPPANEFMCSASEKSHQERDLIKVVNMVLPL
Protein: Histone-lysine N-methyltransferase SETD1B-A (EC 2.1.1.354) (SET domain-containing protein 1B-A) (Q1LY77)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q9UPS6}. Chromosome {ECO:0000250|UniProtKB:Q9UPS6}.
Interaction partners:
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Retinoblastoma-binding protein 5.
- WD repeat-containing protein 82
- Protein dpy-30 homolog
- WD repeat domain 5
- CXXC finger protein 1b.
- CXXC finger protein 1a.
- Actin-histidine N-methyltransferase
- Histone H3
- Histone H3.2
Sequence:
MCWKVEIVVYCKRQKPQTRGTQYVPGERNKLNEDHGRRQSSSLANGMDNSHPICSSGEKRSHHWRSYKLIIDPALKKGSHKVYRYDGHQFSTPSFGMSPVDIVRDPRIGRLWTKYKETDLPVPKFKIDECYVGRVPPKEVTFAKLNDNVREGFLTDMCKKFGDIEEVEILYNPKNKKHLGIAKVVFETVKAAKDAVQNLHNTSVMGNIIHVELDPKGENRQRYFQRLINGSYTPLTLPVGGEEACDVSPRSLAEALMACEPSRRLFEGGSSVVAGTTPSGTNTPMSLDTAYSSLRQDTPQSQGTPHTPRPSGTPFSQDSSYSSRQGTPAFQANRAESSGGYKSRRHETKFQDAYNRRPERRYVHGPTQRGNTEQPPSFKQHQPPEPPSPAFTHTPPPPTSANFKTAYSQYQPPIPQEYTVASYHQPVQRELDYRRPPQAPPPPSTDFLPVRDRPTTPPIPEPPPAPETQPTTPPSSTPEPCPSPTQESERNSLDSRIEMLLKPFLNERGDSDAEVRMDGSPISSSSSQLSPIPPQRPSRPSSTGLEDISPTPLPDSEDDEPIRGTASLLANSRGMSPTNMHSKSCVGEPRTAIDKMDTGHQSSGEDMEISDDEMPGTPIASGDCDKNIVVNSALSLIQTIPMPPPGFPPLPHAAGFPLPPHHLPHHSTVSHLPSHHPMLHPLHSYGMMHFLPVDLLSSLPQLLQMPFQMQTQMLSRMAQSQHPYAYPYPAPSANPAAMPFGGPYPPLSVVSAPADTLHGQPWPLPSMPQFNPAVPPPGYEPQKEDPHKATIDGVLMAIVKELKAIMKKDLNRKMVEVVAFRKFDEWWDKQELSAKATLTPVKTGEGKDEEKERAKPKETMSSHLPWNKGEGLGFEGMGLGIGLRGIRLPSFKVKRKQPPEPTSTSDNKRVRPSTPVDDELEDEESERMGRTDGSRVDPAGSSSKRRPARPLELDSEGEEEEETSGKEESSLSDHEEEPVDDASERLSSGKDLEEEDEKKSESHSSESESSDSSDDEASSSSSSKSGSDSSGSESSSDYESSSEEEEEEEEEEERIVGMDDEEDVDARTSTSSSTTSTSSSDEEEVVEVKAPSTPTGPPPEEEPNELGRLEAVDEAEIDHKPSMVSLIKTKVEEVRPPSPKGLPADELDVDLEVKIPVPKTEASLEEVGNLRPPTPTGSFADSDQDTRPKIPTEDFPRTPGHEGPVPLESETTVPRSLPTPSMHLPLPPSHVPDPQSLLPPPETLPDMPVRGRLPTEEDIPRTPGRDLMDRARGLGKLQSTDTVPVTPGSDTPLTGNSLSSPHILGSPFSYPAQSPVLSAGIPRTPGRDLTFAPAFPDSAGLSAGLPIHRKASSEILEEKPLFKEPLLSASPQASLPNNAASSPFPGPPLPTASLPEPALPPQGSPPASIENSFPASPKELPVPMIDVPVPLDDTPSKKKLVRSKNKKGIQDSEEPQVTLIEASSLPELPVNNQYPDLPSESIKEEDGEPAFSEKEESQVPTIIPKVEETSFYVEEPIQKTRRQRRGWQELLLSMHSPVASPRRPSFMPRSDFEEMTILYDIWNDGIDEEDIRYLKITYDKMLQQDNAHDWLNDTLWVHHPPTNMGSATGVKKKRKEDGIRDHVTGCARSEGYYKIDKKDKMKYLNSSRLQSEEPDVDTQGKSIPAQPQVSTRAGSERRSEQRRLLSSFSCDSDLLKFNQLKFRKKKIRFCRSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSYMFRVDHDTIIDATKCGNFARFINHSCNPNCYAKVITVESQKKIVIYSRQPINVNEEITYDYKFPIEDEKIPCLCGAENCRGTLN