wanglab/gogpt-training-data huggingface dataset:
Protein: C2H2-type domain-containing protein (H2KYB3)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SUPpressor
- Regulator of microtubule dynamics protein 1
- Ubiquitin-conjugating enzyme E2 ubc-18
- Myb-like domain-containing protein
- Zinc finger CCCH-type with G patch domain-containing protein
- F-box domain-containing protein
- Retinoblastoma-like protein homolog lin-35
- Serpentine Receptor, class H
Sequence:
MSISGEDNEIILNASLSNSPDQLDVFEESRRNFLESINATVSMTSNGSKNGIEDIANRLKQNGNTTSTSLTSNSGLYPTDPTIISNHTPSMQLSCVECGVTKANSEEMEIHIKTEHLKWLPFQCPMCLVERASDAQMREHLHSSHQKNMSKFIYVDNVKAKRRLQILMDSAFSLNVSERVNAKNHPSSSTSASPYSPTSYHRGMNSSPSSGRNTSTSNGSATSAATASAQAAATAIVNHHKEKEKQTAQATADFLKLLDFTGINGEIGEHKAQSSSTRSSSGRKRPYVPTSATEAITTMELAAPSAESFLASLNSFSHAQTPENEENDHPTLFSVDDLNIDSTSTLATLFGGGARKTKYDDGEMPHDEDPLLDSLNPISVLDNVAALFGSTPDRSVETETKKTSSISKKRVLGECSKCQKPVTAGARQMHMFFHLAKDELIFRFRCKHEGCSVEHYRKDQMENHQSKAHGRIDPDMMEDRSLELFQKCQDLSMELLGTKNGTIPGPTAAKAEIAYAAQQAANAQRNSQKSKLPGLSSLCSSTAGTAGSTSNGFGPLKLVPDEDHPLQCRLCGKTMQNRIRGFHILWHMAKDKGINRYTCKYCNFGHDRSQSVQVHGKKEHGTDDCVEDRIGEYQDDVKEMSASCFGISSLFAQESKRKNKFPAAAPREHKDLVSMVSSSHEASPAVPVDEEASNDSAIKEEEKPLILNDEEMEELGEDDEVEHEQEHEDEDGEGDEDDDGEGEETTPITSSKSSKKKWRRAFNIRSKKSKKQKEDAVVARSVSILIGGAQFYKKKVNEFCYCEKCGKQTNSRLPEHAYTHMDGVELYSCSACSFGNQCKETVMKHMRESHPLCAERCVDNRLGHIKEIKKQLGQCFPAFFIDHPLPTRSDIEKLQILASGGDLKIGGIEKYLKEECEDGEPSEAPEDEEMEEDDDGVSSD
Protein: Uncharacterized protein (Q57XQ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Chromatin target of PRMT1 protein C-terminal domain-containing protein
Sequence:
MPVKKKVATAKNDEKEDLTTSPVMAAETTPTASSPTMQHLDTPQGTTSASELYAVLQAAVAEDPAKVNDFAEEIAQTFVEAEKAETPLLLRVRMLEFFAKYGQHMRDGNALKKVVTSLVKILSGPDNTQQLLVAAVQGIAALGPVSMLDKKWEYLSREGADVLMQVMIDENGFAEPVRSAASKALDTLVSTAFRPVVTKLLHWLSDDREAEEEDQLQKERRTAMARLRKVAQTASFRPQWTEEIQEHVLALIIRVLSAVTITEFAQLARIAASLPSVEEKKGLPLLTAFLASTKLNTDRALESLSLVAQHVGAVAYDLTPMLDEAGLLSAPVDGTTVRGMWHAKLLLLAARSATPENTDTLYKTLLEHVMNLIGDGNTLPEYLTTLEALLLALTSVGQKKPLDFVKQLKDKQFTAKCRNMLAAVEKVEPLLIYAVKRLVQKSSAGAKEAEMLGSCHNLRIILSSFSSSHIPMGAITESWAHKHKLPVLRQGREGLLPSAKGGRSGYDAQLPAVNKRPRTESNYRPQSNRGSSRDLQGRSRGWKY
Protein: PNO1 second type I KH domain-containing protein (Q38DL0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- AATF leucine zipper-containing domain-containing protein
- Serine/threonine-protein kinase RIO2
- RNA-binding protein NOB1
- Bystin, putative
- 40S ribosomal protein S14
- Bms1-type G domain-containing protein
- Protein LTV1 homolog
- Periodic tryptophan protein 2, putative
- Bms1-type G domain-containing protein
- Small ribosomal subunit protein uS4
Sequence:
MTGSNGNDEPFKREMRTVKVPHHRFPALKKVWMDVYTPIVEQCKLEIRMNLRGRSVELRTCPATVEAAGNEGSKALLQKAEDFVKAVVAGFDVKDAVALLRMDDVYIEGFEVKDVRANLQGDNLSRCIGRMSGSHGKTKHTIENVTRTRIVIADTHICIMGTTQNIRVARDALCDLIRGSPATKVYTRVRAVMNRVNDTF
Protein: Sperm acrosome membrane-associated protein 4 (Sperm acrosomal membrane-associated protein 14) (Q8TDM5)
Organism: Homo sapiens (Human)
Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12788941}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12788941}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:12788941}. Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:37377732}. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000269|PubMed:37377732}. Note=Expressed in acrosomal matrix and outer and inner acrosomal membranes. {ECO:0000269|PubMed:12788941, ECO:0000269|PubMed:37377732}.
Interaction partners:
- Urokinase plasminogen activator surface receptor
- Testis-expressed protein 101
Sequence:
MVLCWLLLLVMALPPGTTGVKDCVFCELTDSMQCPGTYMHCGDDEDCFTGHGVAPGTGPVINKGCLRATSCGLEEPVSYRGVTYSLTTNCCTGRLCNRAPSSQTVGATTSLALGLGMLLPPRLL
Protein: Sulfopyruvate decarboxylase subunit beta (EC 4.1.1.79) (P58416)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.
Interaction partners:
Sequence:
MYPKRIDIIKKIVENVGEKEIIVSNIGIPSKELYYVKDRERNFYMLGSMGLASSIGLGLALNCEDKVIVIDGDGSILMNLGSLSTIGYMNPKNYILVIIDNSAYGSTGNQKTHTGKNTNLEEIAKGCGLDTITTESLEEFEKEFKNALNEEKCKVIIAKTIPYNEKCSNIEIPPVVLKYRFMEAIKRS
Protein: Nitrate reductase (EC 1.7.5.1) (P39458)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Interaction partners:
- NADH dehydrogenase
- Ferredoxin--nitrite reductase
- Nitrate/nitrite binding protein NrtA
- Nitrate import ATP-binding protein NrtC
- Molybdopterin molybdenumtransferase
- Nitrate import ATP-binding protein NrtD
- Nitrate import permease protein NrtB
- ABC-type nitrate/sulfonate/bicarbonate transport systems periplasmic components-like
- Ferredoxin--nitrite reductase
- Integral membrane protein
Sequence:
MFDLSKFLPVITPLMIDTAKTLCPYCGVGCGLEAVPPAQPGRATVRDREGTPIWQIRGDRQHPSSQGMVCVKGATVAESVSKSRLKYPMFRASLDDPFTEISWDEALDRLCDRIQQTQADYGKDGICFYGSGQFQTEDYYIAQKLVKGCLGTNNFDTNSRLCMSSAVSAYSLCLGSDGPPACYEDLDLADCLLIVGSNTAECHPILFNRYRKRHKQGGTNLIVVDPRCTPTAEVADLHLALKPGSDVALLNGLGWLLYQMGYVKKDFIANQTEGFEDWLAIIEDYPPQRTAELTGLAVAELVRAADLIASAQRWLSLWSMGVNQSIQGTAKATSLINLHLLTRQIGLPGCGPFSLTGQPNAMGGRETGGLAHLLPGYRKVIDPQHRADVETIWGLPMGSISPQPGRTAWQMIEGLEQGAVGFLWVAATNPAVSLPDVKRAQAALKRSPFTVLQDAYHPTETTTYAHLLLPAAQWSEKTGTMTNSERRVTLCQAFRQPPGEARADWQIFAEVGRRLGFAFDYTDAAAVFAEYVQVTAGRLCDLSGLSHELLAQAGPQQWPFPAGAEPTTESKRLYTKHHFAYADGRARFQPFHHLGVAEPPDDRYPLVLTVGRLYGHWHTQTRTGRIDKINKLHPSAFVEIHPRDADRYNISEGQAVVIRSRRGEGCFPAKVTTAISPGVLFVPMHWGALWGDRTEANALTHPAACPISGEPELKACAVQIEAASSTFTI
Protein: Sphingosine 1-phosphate receptor 1 (S1P receptor 1) (S1P1) (Endothelial differentiation G-protein coupled receptor 1) (Lysophospholipid receptor B1) (Sphingosine 1-phosphate receptor Edg-1) (S1P receptor Edg-1) (CD antigen CD363) (O08530)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis. Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P21453}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21453}. Endosome {ECO:0000250|UniProtKB:P21453}. Membrane raft {ECO:0000250|UniProtKB:P21453}. Note=Recruited to caveolin-enriched plasma membrane microdomains in response to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine. Ligand binding leads to receptor internalization. {ECO:0000250|UniProtKB:P21453}.
Interaction partners:
- Early activation antigen CD69
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Sphingosine 1-phosphate receptor 4
- Beta-arrestin-2
- Sphingosine kinase 2
- Sphingosine kinase 1
- Apolipoprotein M
- Vascular endothelial growth factor receptor 2
Sequence:
MVSTSIPEVKALRSSVSDYGNYDIIVRHYNYTGKLNIGAEKDHGIKLTSVVFILICCFIILENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPAQWFLREGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNSSRSFLLISACWVISLILGGLPIMGWNCISSLSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKNISKASRSSEKSLALLKTVIIVLSVFIACWAPLFILLLLDVGCKAKTCDILYKAEYFLVLAVLNSGTNPIIYTLTNKEMRRAFIRIVSCCKCPNGDSAGKFKRPIIPGMEFSRSKSDNSSHPQKDDGDNPETIMSSGNVNSSS
Protein: Small ribosomal subunit protein uS10 (C3SQT7)
Organism: Escherichia coli
Interaction partners:
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS12
- 30S ribosomal protein S5
- Small ribosomal subunit protein uS3
Sequence:
MQNQRIRIRLKAFDHRLIDQATAEIVETAKRTGAQVRGPIPLPTRKERFTVLISPHVNKDARDQYEIRTHLRLVDIVEPTEKTVDALMRLDLAAGVDVQISLG
Protein: Large ribosomal subunit protein P2 (60S acidic ribosomal protein P2) (Renal carcinoma antigen NY-REN-44) (P05387)
Organism: Homo sapiens (Human)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL36
Sequence:
MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD
Protein: Synaptic vesicular amine transporter (Monoamine transporter) (Solute carrier family 18 member 2) (Vesicular amine transporter 2) (VAT2) (Vesicular monoamine transporter 2) (Q8BRU6)
Organism: Mus musculus (Mouse)
Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior to their release via exocytosis. Transports a variety of catecholamines such as dopamine, adrenaline and noradrenaline, histamine, and indolamines such as serotonin (By similarity). Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates somatodendritic dopamine release in hippocampal neurons, likely as part of a regulated secretory pathway that integrates retrograde synaptic signals (By similarity). Acts as a primary transporter for striatal dopamine loading ensuring impulse-dependent release of dopamine at the synaptic cleft. Responsible for histamine and serotonin storage and subsequent corelease from mast cell granules (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:9427251}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q01827}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:Q01827}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q01827}. Note=Sorted to large dense core granules in neuroendocrine cells, presumably at the level of the trans-Golgi network. In neurons it is predominantly detected in somatodendritic tubulovesicular membranes, a distinct population of secretory vesicles that undergo calcium-dependent exocytosis in axons and dendrites upon depolarization. Localized at synaptic vesicles in axons. {ECO:0000250|UniProtKB:Q01827}.
Interaction partners:
- Alpha-synuclein
- Vesicular inhibitory amino acid transporter
- Vesicular glutamate transporter 2
- Vesicular glutamate transporter 3
- Vesicular glutamate transporter 1
- Tyrosine 3-monooxygenase
- Aromatic-L-amino-acid decarboxylase
- Sodium-dependent dopamine transporter
- Vesicular acetylcholine transporter
- Chromaffin granule amine transporter
Sequence:
MALSDLVLLRWLRDSRHSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNTTEIQTARPALTASTSESFHSIFSYYNNSTVFTGNATGGLPGGESPKATTTQHTVTNTTVPPDCPSEDKDLLNENVQVGLLFASKATVQLLTNPFIGLLTNRIGYPIPMFAGFCIMFISTVMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGNAMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWMMETMCSRKWQLGVAFLPASISYLIGTNIFGILAHKMGRWLCALLGMIVVGISILCIPFAKNIYGLIAPNFGVGFAIGMVDSSMMPIMGYLVDLRHVSVYGSVYAIADVAFCMGYAIGPSAGGAIAKAIGFPWLMTIIGIIDIVFAPLCFFLRSPPAKEEKMAILMDHNCPIKTKMYTQNNVQPYPVGDDEESESD
Protein: Actin-related protein 2/3 complex subunit 2 (Arp2/3 complex 34 kDa subunit) (p34-ARC) (Q3MHR7)
Organism: Bos taurus (Bovine)
Function: Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the mother actin filament. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15144}. Cell projection {ECO:0000250|UniProtKB:O15144}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9CVB6}. Nucleus {ECO:0000250|UniProtKB:O15144}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 5-like protein
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 1A
- Actin nucleation-promoting factor WASL
Sequence:
MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSISLKFYKELQAHGADELLKRVYGSYLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNCFASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKVFMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNASARDNTINLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITGKTFSSR
Protein: GTP-binding nuclear protein Ran (EC 3.6.5.-) (Androgen receptor-associated protein 24) (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein) (P62826)
Organism: Homo sapiens (Human)
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.
Subcellular location: Nucleus {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:1961752, ECO:0000269|PubMed:19753112, ECO:0000269|PubMed:31075303, ECO:0000269|PubMed:8421051, ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9822603}. Nucleus envelope {ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9822603}. Cytoplasm, cytosol {ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:8276887}. Cytoplasm {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:9822603}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Predominantly nuclear during interphase (PubMed:10679025, PubMed:12194828, PubMed:8421051). Becomes dispersed throughout the cytoplasm during mitosis (PubMed:12194828, PubMed:8421051). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:8421051}.
Interaction partners:
- E3 SUMO-protein ligase RanBP2
- Exportin-T
- Exportin-1
- Exportin-5
- Importin subunit beta-1
- Ran-specific GTPase-activating protein
- Nuclear transport factor 2
- Ran GTPase-activating protein 1
- Regulator of chromosome condensation
- Nuclear pore complex protein Nup153
Sequence:
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Protein: rRNA N(6)-adenosine-methyltransferase METTL5 (EC 2.1.1.-) (Methyltransferase-like protein 5) (Q8K1A0)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of a heterodimer with TRMT112, which specifically methylates the 6th position of adenine in position 1832 of 18S rRNA. N6-methylation of adenine(1832) in 18S rRNA resides in the decoding center of 18S rRNA and is required for translation and embryonic stem cells (ESCs) pluripotency and differentiation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NRN9}. Presynapse {ECO:0000250|UniProtKB:Q9NRN9}. Postsynapse {ECO:0000250|UniProtKB:Q9NRN9}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- rRNA N
- RNA N
- Zinc finger CCCH domain-containing protein 13
- Protein virilizer homolog
- Pre-mRNA-splicing regulator WTAP
- N
- RNA-binding protein 15
- N
- Probable methyltransferase-like protein 25
Sequence:
MKKLKLKELESRLQEVDGFEKPKLLLEQYPTRPHIAACMLYTIHNTYDDIENKAVADLGCGCGVLSIGAAMLGAGLCVGFDIDEDALEIFNKNVEEFELTNVDMIQCDVYSLSNRMSKLFDTVIMNPPFGTKNNKGTDMAFLKTALGMARTAVYSLHKSSTREHIQKKAAEWKVKIEIIAELRYDLPALYNFHKKKSVDIEVDLIRFSF
Protein: Proteasome subunit beta type-2 (20S proteasome subunit beta-4) (Q9NHC6)
Organism: Trypanosoma brucei brucei
Function: Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MAETTIGFRCQDFVLVAAAGLNAFYYIKITDTEDKITELDSHKVVACAGENGPRTHFVEYVKCNMALKKMREHGRMISTHATASFMRNTLAGALRSRDGLYPVNCLLAGFDVPASAEDDVATGAHLYYLDYLGTLQEVPYGCHGYGAPFVTAMLDRMWRPNLTAQEGVELMQKCCDEVNKRVVVSNNTFICKAVPKDGVERVQSVS
Protein: OSJNBb0013O03.11 protein (Os04g0300600 protein) (Q7XKP5)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEAAADMGVLLDLYWHTPHIFDLAVADSLLMDGFGGGMYGPAAAPATPAMVEKEYDESLSELYAYTSQSRYADSSSPDVVNLCSTAVASAAAAASSKNIAMERDRRKRLNEKLFALRAVVPKITKMDKASIVRDAIAHIEKLQEEERQLLDEISVLQSAAAVAATAVEDVDDSGVTMPSMKKLRSTPPLDGGGGALRVASSPPLQILEVETKETEDFYGLILQTSQSWPSDPQLQVSKVGEKTVAVSIRCAKTRGAMAKVCHAVESLYLKVVSASVAAVDGTIVHTMFVEVTN
Protein: Stage IV sporulation protein A (EC 3.6.1.-) (Coat morphogenetic protein SpoIVA) (P35149)
Organism: Bacillus subtilis (strain 168)
Function: ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.
Subcellular location: Cytoplasm {ECO:0000305}. Note=Uniformly distributed on the membrane around the forespore, lying close to or on its outer surface. Expression only necessary in the mother cell chamber of the sporangium for the formation of a mature spore. According to PubMed:8299942, not a coat protein of the mature spore, is only transiently associated with the assembling coat. According to PubMed:9922240, present as a component of the fully mature spore. Proper localization requires the expression of a gene spoVM which is under the control of the mother cell transcription factor sigma E. {ECO:0000269|PubMed:1729247, ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:19775244, ECO:0000269|PubMed:23267091, ECO:0000269|PubMed:8299942, ECO:0000269|PubMed:8936302, ECO:0000269|PubMed:9922240}.
Interaction partners:
- Stage VI sporulation protein D
- Spore coat protein E
- Stage V sporulation protein M
- Stage III sporulation protein D
- SpoIVD-associated factor A
- Stage III sporulation protein AA
- Stage 0 sporulation protein A
- Stage II sporulation protein D
- Stage II sporulation protein P
- Stage III sporulation protein AH
Sequence:
MEKVDIFKDIAERTGGDIYLGVVGAVRTGKSTFIKKFMELVVLPNISNEADRARAQDELPQSAAGKTIMTTEPKFVPNQAMSVHVSDGLDVNIRLVDCVGYTVPGAKGYEDENGPRMINTPWYEEPIPFHEAAEIGTRKVIQEHSTIGVVITTDGTIGDIARSDYIEAEERVIEELKEVGKPFIMVINSVRPYHPETEAMRQDLSEKYDIPVLAMSVESMRESDVLSVLREALYEFPVLEVNVNLPSWVMVLKENHWLRESYQESVKETVKDIKRLRDVDRVVGQFSEFEFIESAGLAGIELGQGVAEIDLYAPDHLYDQILKEVVGVEIRGRDHLLELMQDFAHAKTEYDQVSDALKMVKQTGYGIAAPALADMSLDEPEIIRQGSRFGVRLKAVAPSIHMIKVDVESEFAPIIGTEKQSEELVRYLMQDFEDDPLSIWNSDIFGRSLSSIVREGIQAKLSLMPENARYKLKETLERIINEGSGGLIAIIL