wanglab/gogpt-training-data huggingface dataset:
Protein: Mediator of RNA polymerase II transcription subunit 1 (Mediator complex subunit 1) (dTRAP220) (Q9VP05)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). Required for activated transcription of the MtnA, MtnB and MtnD genes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 15
Sequence:
MSGSNAKSSGTGFGSHIPSIEEKNKQIQQETMMEKLRAKYRNKPKSYEEIKKSVRMYFIEKHYPLDPLCKATLQSALDKLQHYIKVTSRHGLVERLESLSRQLGLKFMEDQQLLFISTDMFYVEILLDAAGSLSDVKVHHECKIEQQSSELVACLKSGDFADFTVQLEGLSSIYQLNAEPKVKKKAFVALQAMETDIQSLYQLHLQGHSGDSYSLMTSSSVGLVLPRRGGHPMRLTYFCPPLHLPEGDPKLASGDFTIDQVMRSSYGLSATINLEGSSANKLQTLPTVTLVRDAQTGLEVPTYAQLNQNNSLLMPATFVLRLNKPMPVCLESLKALGLPGLDSVATPPGPPTTVLNLIVQTASKQAIKNTQRGLYVNLPKETHCYFFTDNRKLQGTLVSSLPFTEPAQVPRIVAFLKKQALFYTLLASCVREQQKQYNDMDSTVILEVTAVSFNQITVELQHPYEESLATVDFLLEDGQPTCSVYCLTNEYELLSQKLTRTARKVVSIPMVIYKLLKCWDEEHEFKLHGAIGPGSGSGAIGGGGMSGGGPVSGVGNNFSQFSMDTPTPSDGSLPGGGFANINNLKMDAKSRSLADAFAASTSAAAAIAGLINLKRETDPQSGSSASGTTVSGSSSSSGSAKTSDHDIADKYKNIWKDKTPNLKHCVSITPIPGDGKSGSAGGVSGVEVQRTGGIEIIPLNAQAAIAGGGVTASSSATPTTITITPITGKDPSKDSTKKSTAASAGVGVAAKRPHESSTSSSSTSGCSGSGSSMSSSASSGSSDTQKEKKRKKKRDDSPMGPPEKIYSRQNSPAGGADASATGGVVRKFSSPSSSPKAGGGGQGLMAGVPTARPSPKHSPVYSSPKHNTASNSPKSPFGTHSPKHGSSGKPSMSTLKSAATAATILSPKGDKSSSAVGNTSSGPSASSGSSGATGLVRSFASVGAPPPPPPIPPLASSSGSISSSQSLKKEKTSSASGSSSTSSSATAGVASGGGISPASVAAAVAALKSSQQQMKSVASLSHLAAGGGLGSYAAPSGAGASGAAAVVVGAGAGAGAGASGLELSALRKGMAGGAVSLMTSTAALAPTIPAPTTTVAAGSAASLVSPVSAVVGQGQETAGAAAAATLATATILQQQPQPGAAPTSSCLTTSGGSSDSAGSINPAGASTEYMVKPSSQEGLKLTINKTGSSKSSGTGSGSSSSSGLQAKAKSSSSGATSFAGSTGSTKKQHTGLKPGVNSGPASKKATAAVSSATASSSKHFFQKANSSGNLSSKLSGSGSGGGIPLTKSNSTNSFQEHNAPRRRPSMGALASGSSGGGSGQRKLGSASGGGSGSSGSVSPALSGSMSQPPPRFDHHTDMMTILQYASPTMAASMEGFIKGLHNKFQIPKLSQRGSGGNTTSGRSTPSGSSEPALAGTSSSILGPIASSTGLTEPEAKPPVPPSQSGNEGLLNLSSTAGTPSADGIDEELLASLAGE
Protein: Bone marrow proteoglycan (BMPG) (Proteoglycan 2) [Cleaved into: Eosinophil granule major basic protein (EMBP) (MBP) (Pregnancy-associated major basic protein)] (P13727)
Organism: Homo sapiens (Human)
Function: Cytotoxin and helminthotoxin. Also induces non-cytolytic histamine release from human basophils. Involved in antiparasitic defense mechanisms and immune hypersensitivity reactions. The proform acts as a proteinase inhibitor, reducing the activity of PAPPA.
Subcellular location: [Bone marrow proteoglycan]: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. Note=The proform is secreted.; SUBCELLULAR LOCATION: [Eosinophil granule major basic protein]: Cytoplasmic vesicle, secretory vesicle. Note=The proform is secreted. The mature protein is found in the matrix of the eosinophil's large specific granule (crystalloid core).
Interaction partners:
- Pappalysin-1
- Non-secretory ribonuclease
- Eosinophil cationic protein
- Eosinophil peroxidase
- Insulin-like growth factor-binding protein 4
- CMRF35-like molecule 8
Sequence:
MKLPLLLALLFGAVSALHLRSETSTFETPLGAKTLPEDEETPEQEMEETPCRELEEEEEWGSGSEDASKKDGAVESISVPDMVDKNLTCPEEEDTVKVVGIPGCQTCRYLLVRSLQTFSQAWFTCRRCYRGNLVSIHNFNINYRIQCSVSALNQGQVWIGGRITGSGRCRRFQWVDGSRWNFAYWAAHQPWSRGGHCVALCTRGGHWRRAHCLRRLPFICSY
Protein: Endophilin-B1 (Bax-interacting factor 1) (Bif-1) (SH3 domain-containing GRB2-like protein B1) (Q9Y371)
Organism: Homo sapiens (Human)
Function: May be required for normal outer mitochondrial membrane dynamics. Required for coatomer-mediated retrograde transport in certain cells (By similarity). May recruit other proteins to membranes with high curvature. May promote membrane fusion. Involved in activation of caspase-dependent apoptosis by promoting BAX/BAK1 activation. Isoform 1 acts proapoptotic in fibroblasts (By similarity). Involved in caspase-independent apoptosis during nutrition starvation and involved in the regulation of autophagy. Activates lipid kinase activity of PIK3C3 during autophagy probably by associating with the PI3K complex II (PI3KC3-C2). Associated with PI3KC3-C2 during autophagy may regulate the trafficking of ATG9A from the Golgi complex to the peripheral cytoplasm for the formation of autophagosomes by inducing Golgi membrane tubulation and fragmentation. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2. Isoform 2 acts antiapoptotic in neuronal cells; involved in maintenance of mitochondrial morphology and promotes neuronal viability (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15452144}. Golgi apparatus membrane {ECO:0000269|PubMed:21068542}; Peripheral membrane protein {ECO:0000250}. Mitochondrion outer membrane {ECO:0000269|PubMed:15452144}; Peripheral membrane protein {ECO:0000269|PubMed:15452144}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:17891140}. Midbody {ECO:0000269|PubMed:20643123}. Note=Association with the Golgi apparatus depends on the cell type (By similarity). Following starvation colocalizes with ATG5 and LC3 autophagy-related protein(s)on autophagosomal membranes (PubMed:17891140). {ECO:0000250, ECO:0000269|PubMed:17891140}.
Interaction partners:
- UV radiation resistance-associated gene protein
- Beclin-1
- Activating molecule in BECN1-regulated autophagy protein 1
- Beclin 1-associated autophagy-related key regulator
- Phosphoinositide 3-kinase regulatory subunit 4
- Endophilin-B2
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Immunity-related GTPase family M protein
- Vacuolar protein sorting-associated protein 26C
- Ubiquitin carboxyl-terminal hydrolase 14
Sequence:
MNIMDFNVKKLAADAGTFLSRAVQFTEEKLGQAEKTELDAHLENLLSKAECTKIWTEKIMKQTEVLLQPNPNARIEEFVYEKLDRKAPSRINNPELLGQYMIDAGTEFGPGTAYGNALIKCGETQKRIGTADRELIQTSALNFLTPLRNFIEGDYKTIAKERKLLQNKRLDLDAAKTRLKKAKAAETRNSSEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDFVEAQMTYYAQCYQYMLDLQKQLGSFPSNYLSNNNQTSVTPVPSVLPNAIGSSAMASTSGLVITSPSNLSDLKECSGSRKARVLYDYDAANSTELSLLADEVITVFSVVGMDSDWLMGERGNQKGKVPITYLELLN
Protein: Peroxiredoxin AHP1 (Prx) (EC 1.11.1.24) (Alkyl hydroperoxide reductase) (AHPC1) (Cytoplasmic thiol peroxidase 3) (cTPx 3) (Thiol-specific antioxidant II) (TSA II) (Thioredoxin peroxidase type II) (TPx type II) (Thioredoxin-dependent peroxiredoxin AHP1) (P38013)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation. Involved in cellular Mn(2+) homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10681558}.
Interaction partners:
- Thioredoxin-2
- Ubiquitin-related modifier 1
- Peroxiredoxin TSA1
- Peroxiredoxin PRX1, mitochondrial
- Glutathione peroxidase-like peroxiredoxin HYR1
- Peroxiredoxin DOT5
- Peroxiredoxin TSA2
- Thioredoxin-1
- Superoxide dismutase
- Glutathione reductase
Sequence:
MSDLVNKKFPAGDYKFQYIAISQSDADSESCKMPQTVEWSKLISENKKVIITGAPAAFSPTCTVSHIPGYINYLDELVKEKEVDQVIVVTVDNPFANQAWAKSLGVKDTTHIKFASDPGCAFTKSIGFELAVGDGVYWSGRWAMVVENGIVTYAAKETNPGTDVTVSSVESVLAHL
Protein: Chlorophyll a-b binding protein 4, chloroplastic (LHCI type III CAB-4) (P27521)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:10818090, ECO:0000269|PubMed:12766230}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosystem I reaction center subunit XI, chloroplastic
- Chlorophyll a-b binding protein 6, chloroplastic
- Photosystem I reaction center subunit VIII
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 3-1, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I reaction center subunit III, chloroplastic
- Photosystem I reaction center subunit IX
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I chlorophyll a/b-binding protein 5, chloroplastic
Sequence:
MATVTTHASASIFRPCTSKPRFLTGSSGRLNRDLSFTSIGSSAKTSSFKVEAKKGEWLPGLASPDYLTGSLAGDNGFDPLGLAEDPENLKWFVQAELVNGRWAMLGVAGMLLPEVFTKIGIINVPEWYDAGKEQYFASSSTLFVIEFILFHYVEIRRWQDIKNPGSVNQDPIFKQYSLPKGEVGYPGGIFNPLNFAPTQEAKEKELANGRLAMLAFLGFVVQHNVTGKGPFENLLQHLSDPWHNTIVQTFN
Protein: Probable arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) (Arginyl-tRNA synthetase) (Q9VXN4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P54136}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
Interaction partners:
- Lysine--tRNA ligase
- leucine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase
- leucine--tRNA ligase
- AaRS-interacting multifunctional protein 1
Sequence:
MSELNMELKKLRELELKTQGLAARIQTAKSGEQLDVDLVQLQIENKKLKNRLFILKKSIAEESTAAGGDVSKPKESSSITEHLESVFRQAIASAFPEFRDTPVIIAPVNSTSAKFGDYQCNNAMGLSKKLKEKGINKAPRDIATELKGHCPASPIIEKLEIAGAGFVNVFLSKDYASLALSNLLRNGVKPPEVIKKRVLVDFSSPNIAKQMHVGHLRSTIIGESLCRLLEFLQHDVIRINHLGDWGTQFGMLIAHLEDRFPNYLNESPPISDLQLFYKESKKRFDEDEEFKKRAYSRVVSLQKGVPNSIKAWELICNVSRKEFQTIYERLDISVKERGESFYQSRMLSVVEYLRGKGLLEVDEGREIMWPDDTKTGIPLTIVKSDGGFTYDTSDMAAIRHRLEEELCDWIIYVVDSGQSTHFNTIFKAAERSAILNPLSHRVDHVQFGVVLGEDGKKFKTRSGDTVKLSDLLDEGMKRSLQQLESRGRDKVLTPQELKDAQESLAYGCIKYSDLCHNRISDYIFSFDKMLEDRGNTAVYLLYTYTRICSIARNSGEDFTNLPEILKKTNIVLDHEKEWKLAKTLLKLHDILIKCSKELFLHFLCEFCFEVCTVFTEFYDSCYCIEKNKQGDIIGVNHSRILLCEATAAVLRQCFYILGLKPVSKM
Protein: Chromodomain-helicase-DNA-binding protein 4 (CHD-4) (EC 3.6.4.12) (Q6PDQ2)
Organism: Mus musculus (Mouse)
Function: ATP-dependent helicase that binds and distorts nucleosomal DNA (By similarity). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Localizes to acetylated damaged chromatin in a ZMYND8-dependent manner, to promote transcriptional repression and double-strand break repair by homologous recombination (By similarity). Involved in neurogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q14839}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14839}. Note=Associates with centrosomes in interphase. Localizes to sites of DNA damage in a manner dependent on ZMYND8 and ZNF687. {ECO:0000250|UniProtKB:Q14839}.
Interaction partners:
- Histone deacetylase 1
- Histone deacetylase 2
- Histone-binding protein RBBP4
- DNA helicase
- Histone-binding protein RBBP7
- Transcriptional repressor p66 alpha
- Metastasis-associated protein MTA2
- Transcriptional repressor p66-beta
- Activity-dependent neuroprotector homeobox protein
- Lysine-specific histone demethylase 1A
Sequence:
MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPDEDLSEAETPKLKKKKKPKKPRDPKIPKSKRQKKELGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDEDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVESMVTATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTAKKKKKGEEEVTAVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKEGIQWEAKEDNSEGEEILEEVGGDPEEEDDHHMEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCPALKGKVQKILIWKWGQPPSPTPVPRPPDADPNTPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSGDFGGDEEKSRKRKNKDPKFAEMEERFYRYGIKPEWMMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESEDVEIQDYDLFKQSYWNHRELMRGEEGRPGKKLKKVKLRKLERPPETPTVDPTVKYERQPEYLDATGGTLHPYQMEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRRLKADVFKNMPSKTELIVRVELSPMQKKYYKYILTRNFEALNARGGGNQVSLLNVVMDLKKCCNHPYLFPVAAMEAPKMPNGMYDGSALIRASGKLLLLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGLGSKTGSMSKQELDDILKFGTEELFKDEATDGGGDNKEGEDSSVIHYDDKAIERLLDRNQDETEDTELQGMNEYLSSFKVAQYVVREEEMGEEEEVEREIIKQEESVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRYGMPPQDAFTTQWLVRDLRGKSEKEFKAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHVNGRWSMPELAEVEENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAEDGIKIEENSLKEEESTEGEKEVKSTAPEATVECAQPPAPAPATAPATATAPEDDKAPAEPPEGEEKVEKAEVKERTEEPMETEAKGTTEVEKVEEKSAVDLTPIVVEDKEEKKEEEEKKDVMLQNGETPKDLSDEKQKKNSKQRFMFNIADGGFTELHSLWQNEERAATVTKKTYEIWHRRHDYWLLAGIINHGYARWQDIQNDPRYAILNEPFKGEMNRGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNMSEDPSHPSMALNTRFAEVECLAESHQHLSKESMAGNKPANAVLHKVLKQLEELLSDMKADVTRLPATIARIPPVAVRLQMSERNILSRLANRAPEPPPQQVAQQQ
Protein: Lipid droplet phospholipase 1 (EC 3.1.-.-) (EC 3.1.1.4) (Q08448)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phospholipase involved in maintaining the lipid droplet morphology. Has phospholipase activity with broad substrate specificity, acting on glycerophospholipids phosphatidylethanolamine (PE), phosphatidic acid (PA), phosphatidycholine (PC) and phosphatidylserine (PS), primarily at sn-2 position. It can later remove fatty acids from the sn-1 position of the produced lysophospholipids such as lysophosphatidylethanolamine (LPE). Shows also activity toward phosphatidylglycerol, but, in contrast to what was observed with the other phospholipids tested, prefers the sn-1 position.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:25014274}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein YOR376W-A
- Lipid droplet-associated triacylglycerol lipase
- Lipid droplet hydrolase 1
Sequence:
MTSDKHLFVLIHGLWGNYTHMESMRTILSTTLKKEDVNDDMIYFLPKQNAMFKTFDGIEIIGYRTLIEVCEFIRDYKDGKITKLSVMGYSQGGLVARFMIGKMLTEFKELFEDIEPQLFITMATPHLGVEFYNPTGIAYKSALYSALRTLGSTILGKSGREMFIANSSNNILVKLSQGEYLEALSLFKWRIAFANVKNDRTVAFYTAFITDCDPFIDFDNKLKYTFEEKIPGSGYKGILPKIVDLNALNVNSHAPTKPTKTYKKWGRTILIILVATFLILPIALVMNGLGTAYSYIVTCKYRKMLSNGILHNEVRGKLGLTEQLKGYVTDAYGSIINSALDMDANYEASNSNLVNEEELPWKEFIQKYTTINDGVWKSKFKKLPFDENRKVILRNLNKLKWIRVPIYIKAVNAHGVIVARRGMDENTAATGIACIEFTAQLLAYLMHKSN
Protein: AP-2 complex subunit alpha (A0A8I6A4J2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane, coated pit {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004277}.
Interaction partners:
Sequence:
MRDRPLGSHGRQTAPKPAPALCSSWATGKRRGGRKLITLPLVAGGCLWPCVPCSLSTGKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCVSLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHYDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIDTVINALKTERDVSVRQRAADLLYAMCDRSNAKQIVSEMLRYLETADYAIREEIVLKVAILAEKYAVDYSWYVDTILNLIRIAGDYVSEEVWYRVLQIVTNRDDVQGYAAKTVFEALQAPACHENMVKVGGYILGEFGNLIAGDPRSSPPVQFSLLHSKFHLCSVATRALLLSTYIKFINLFPETKATIQGVLRAGSQLRNADVELQQRAVEYLTLSSVASTDVLATVLEEMPPFPERESSILAKLKRKKGPGAASALDDSRRDTSSNDINGGVEPTPSNVSTPSPSADLLGLRAAPPPAAPPAPVGGNLLVDVFSDGPTAQPSLGPTPEEAFLSELEPPAPESPMTLLADPAPAADPGPEDIGPPIPEADELLNKFVCKNSGVLFENQLLQIGVKSEFRQNLGRMYLFYGNKTSVQFQSFLPTVVHPGDLQTHILCSCLAVQTKRVAAQVDGGAQVQQVLNIECLRDFLTPPLLSVRFRYGGTAQSLTLKLPVTINKFFQPTEMAAQDFFQRWKQLSLPLQEAQKIFKANHPMDAEVTKAKLLGFGSALLDNVDPNPENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEPVSRHLCELLAQQF
Protein: tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRM61 (EC 2.1.1.220) (General control non-derepressible protein 14) (Protein GCD14) (tRNA(m1A58)-methyltransferase subunit TRM61) (tRNA(m1A58)MTase subunit TRM61) (P46959)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. GCD14 is also required for repression of GCN4 mRNA translation by the upstream open reading frames (uORFs) under conditions of amino acid sufficiency.
Subcellular location: Nucleus {ECO:0000269|PubMed:9851972}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- Multifunctional methyltransferase subunit TRM112
- tRNA
- tRNA
- tRNA
- Multisite-specific tRNA:
- Periodic tryptophan protein 2
Sequence:
MSTNCFSGYKDLIKEGDLTLIWVSRDNIKPVRMHSEEVFNTRYGSFPHKDIIGKPYGSQIAIRTKGSNKFAFVHVLQPTPELWTLSLPHRTQIVYTPDSSYIMQRLNCSPHSRVIEAGTGSGSFSHAFARSVGHLFSFEFHHIRYEQALEEFKEHGLIDDNVTITHRDVCQGGFLIKKGDTTSYEFGNNETAASLNANVVFLDLPAPWDAIPHLDSVISVDEKVGLCCFSPCIEQVDKTLDVLEKYGWTDVEMVEIQGRQYESRRQMVRSLNDALERLRDIKRHKLQGVERRKRMFNNTIDSNDEKVGKRNEDGVPLTEKAKFNPFGKGSRIKEGDSNYKWKEVTKMEAEIKSHTSYLTFAFKVVNRSRDDEKVNEILRSTEK
Protein: Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8) (Q07010)
Organism: Trypanosoma brucei brucei
Function: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MEPACKYDFATSVLFTEAELHTRMRGVAQRIADDYSNCNLKPLENPLVIVSVLKGSFVFTADMVRILGDFGVPTRVEFLRASSYGHDTKSCGRVDVKADGLCDIRGKHVLVLEDILDTALTLREVVDSLKKSEPASIKTLVAIDKPGGRKIPFTAEYVVADVPNVFVVGYGLDYDQSYREVRDVVILKPSVYETWGKELERRKAAGEAKR
Protein: Oocyte-expressed protein homolog (KH homology domain-containing protein 2) (Oocyte- and embryo-specific protein 19) (hOEP19) (A6NGQ2)
Organism: Homo sapiens (Human)
Function: As part of the OOEP-KHDC3L scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart (By similarity). Positively regulates the homologous recombination-mediated DNA double-strand break (DSB) repair pathway by regulating ATM activation and RAD51 recruitment to DSBs in oocytes (By similarity). Thereby contributes to oocyte survival and the resumption and completion of meiosis (By similarity). As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for the formation of F-actin cytoplasmic lattices in oocytes which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25542835}. Nucleus {ECO:0000269|PubMed:25542835}.
Interaction partners:
- Transducin-like enhancer protein 6
- NACHT, LRR and PYD domains-containing protein 5
- KH domain-containing protein 3
- KH homology domain-containing protein 1
- Inactive protein-arginine deiminase type-6
- NACHT, LRR and PYD domains-containing protein 2
- Zinc finger BED domain-containing protein 3
Sequence:
MVDDAGAAESQRGKQTPAHSLEQLRRLPLPPPQIRIRPWWFPVQELRDPLVFYLEAWLADELFGPDRAIIPEMEWTSQALLTVDIVDSGNLVEITVFGRPRVQNRVKSMLLCLAWFHREHRARAEKMKHLEKNLKAHASDPHSPQDPVA
Protein: Small nuclear ribonucleoprotein polypeptide C (Q5TAL2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEQAQSLIDKTTAAFQQGKIPPTPFSAPPPAGAMIPPPPSLPGPPRPGMMPAPHMGGPPMMPMMGPPPPGMMPVGPAPGMRPPMGGHMPMMPGPPMMRPPARPMMVPTRPGMTRPDR
Protein: L-amino-acid oxidase (LAO) (Oh-LAAO) (EC 1.4.3.2) (P81383)
Organism: Ophiophagus hannah (King cobra) (Naja hannah)
Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Is very active against L-Lys, L-Phe, L-Leu, L-Tyr, L-Trp, L-Arg, and L-Met, moderately active against L-His, L-cystine, and L-Ile, and slightly active against L-Gln, L-Asn, L-Ala, and L-Val. L-Glu, L-Ser, L-Pro and Gly are oxidized very slowly. Its activity on platelet aggregation is controversial. It has potent inhibitory activity on platelet aggregation induced by ADP and the thromboxane analog U46619, but not by thrombin, mucetin, ristocetin and stejnulxin, but it has also been shown to induce platelet aggregation through the formation of hydrogen peroxide. It binds to bacteria and shows antibacterial activities by generating hydrogen peroxide. Binding and antibacterial activities are higher against Gram-positive than against Gram-negative bacteria. May also have an ability to induce hemorrhage, hemolysis, edema, apoptosis.
Subcellular location: Secreted {ECO:0000269|PubMed:2044840}.
Interaction partners:
Sequence:
MNDFLLLLLVLFLGVPRSENHVINLEECFQEPEYENWLATASHGLTKTLNPKKIVIVGAGISGLTAAKLFREAGHEVVILEASDRVGGRIKTHREDGWYVDVGPMRVPQTHRIVREYIKKFNISLNPFRQTDENAWYLIKHVRQKMSANNPENFGYQLNPNERGKSASQLFDETLDKVTDDCTLQKEKYDSFSTKEYLIKEGKLSTGAVEMIGDFLNEEAGFHNSFLISVMDHFLFLNNSFDEITGGFDQLPERFFKDMDSIVHLNSTVEKIVHINNKVTVFYEGLSTNMRLVADYVLITATARATRLIKFVPPLSIPKTRALRSLIYASATKIILVCTDKFWEKDGIHGGRSITDLPSRVIYYPNHDFTNGIGVLLASYTWYSDSEFYTTLSDEKCVDVVMDDLVEIHNVSKDYLKSVCGKHVVQKWALDQYSMGAFSTYTPYQITHYSQMLAQNEGRIYFAGEYTAHPHGWIETSMKSAIREAINIHNA
Protein: Uncharacterized protein (Q3TGB0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIRIAALNASSTIEDDHEGSFKSHKIQTKEAQEAEAFALYHKALDLQKHDRFEESAKAYHELLEARLLREAVSSGDEKEGLKHPGLILKYSTYKNLAQLAAQREDLETAMEFYLEAVMLDSTDVNLWYKIGHVALRLIRLPLARHAFEEGLRCNPDHWPCLDNLITVLYTLSDYTTCLYFICKALEKDCRYSKGLVLKEKIFEEQPCLRKDSLRMFLKCDMSIHDVSVSAAETQAIVDEALGLRKKRQALIVREKEPDLKLVQPIPFFTWKCLGESLLAMYSHLTTCEPPRPSLGKRIDLSDYQDPSQLLASSVVVTPVSVVQPSPICTNPTVAVAEPVLSYTSVTAASFPLHSPSLLDTGTPMGDVSGGDKSKKGVKRKKTVEESGETAKRRSARVRNTKC