wanglab/gogpt-training-data huggingface dataset:
Protein: Glutamate receptor 2 (GluR-2) (AMPA-selective glutamate receptor 2) (GluR-B) (GluR-K2) (Glutamate receptor ionotropic, AMPA 2) (P23819)
Organism: Mus musculus (Mouse)
Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity). Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P42262}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P42262}. Postsynaptic cell membrane {ECO:0000269|PubMed:20547133}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P42262}. Postsynaptic density membrane {ECO:0000269|PubMed:20547133}; Multi-pass membrane protein {ECO:0000255}. Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression (By similarity). Displays a somatodendritic localization and is excluded from axons in neurons (PubMed:18341993). {ECO:0000250|UniProtKB:P19491, ECO:0000269|PubMed:18341993}.
Interaction partners:
- Glutamate receptor 3
- Voltage-dependent calcium channel gamma-2 subunit
- Glutamate receptor 4
- Glutamate receptor-interacting protein 1
- PRKCA-binding protein
- Glutamate receptor 1
- Voltage-dependent calcium channel gamma-8 subunit
- Disks large homolog 4
- Protein cornichon homolog 3
- Protein cornichon homolog 2
Sequence:
MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI
Protein: Potassium channel, subfamily, member 5 (KCNK5), transcript variant 2 (A0A0B6VRS7)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVDRGPLLTSAIIFYLAIGAAIFEVLEEPHWKEAKKNYYTQKLHLLKEFPCLSQFLTRRGVSLRKAQITCTAIFIVWGVLVHLVIPPFVFMVTEEWNYIEGLYYSFITISTIGFGDFVAGVNPSANYHALYRYFVELWIYLGLAWLSLFVNWKVSMFVEVHKAIKKRRRRRKESFESSPHSRKALQMAGSTASKDVNIFSFLSKKEETYNDLIKQIGKKAMKTSGGGERVPGPGHGLGPQGDRLPTIPASLAPLVVYSKNRVPSLEEVSQTLKNKGHVSRPLGEEAGAQAPKDSYQTSEVFINQLDRISEEGEPWEALDYHPLIFQNANITFENEETGLSDEETSKSSVEDNLTSKEQPEQGPMAEAPLSSTGEFPSSDESTFTSTESELSVPYEQLMNEYNKADNPRGT
Protein: Zinc finger protein 124 (Zinc finger protein HZF-16) (Q15973)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSGHPGSWEMNSVAFEDVAVNFTQEEWALLDPSQKNLYRDVMQETFRNLASIGNKGEDQSIEDQYKNSSRNLRHIISHSGNNPYGCEECGKKPCTCKQCQKTSLSVTRVHRDTVMHTGNGHYGCTICEKVFNIPSSFQIHQRNHTGEKPYECMECGKALGFSRSLNRHKRIHTGEKRYECKQCGKAFSRSSHLRDHERTHTGEKPYECKHCGKAFRYSNCLHYHERTHTGEKPYVCMECGKAFSCLSSLQGHIKAHAGEEPYPCKQCGKAFRYASSLQKHEKTHIAQKPYVCNNCGKGFRCSSSLRDHERTHTGEKPYECQKCGKAFSRASTLWKHKKTHTGEKPYKCKKM
Protein: Ankyrin repeat domain-containing protein 1 (Cardiac ankyrin repeat protein) (Q9CR42)
Organism: Mus musculus (Mouse)
Function: May play an important role in endothelial cell activation. May act as a nuclear transcription factor that negatively regulates the expression of cardiac genes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Titin
- Myopalladin
- CCN family member 1
- Calpain-3
- CCN family member 2
- Transcriptional coactivator YAP1
- Four and a half LIM domains protein 2
- Telethonin
Sequence:
MMVLRVEELVTGKKNSNGAAGEFLPGEFRNGEYEAAVALEKQEDLKTLPANSVKQGEEQRKSEKLREAELKKKKLEQRSKLENLEDLEIIVQLKKRKKYKKTKVPVVKEPEPEIMTEPVDVPRFLKAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNADVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLKVKNCAGKTPMDLVLHWQSGTKAIFDSLKENAYKNSRIATF
Protein: Fgr42p (A0A1D8PNV0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MLVGMGVYLVGDLVYTLYYILLFVFFVHKLFNSVVVVVVIYRLHLLLCLKKNIQSLISSPFSTIITPPFFEVFLFFFFFVLFSSNHNCSFSNLPIFQSSNLPIF
Protein: Collagen type I alpha 2 chain (H0VHD0)
Organism: Cavia porcellus (Guinea pig)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Collagen type I alpha 1 chain
- Collagen type III alpha 1 chain
- Collagen type V alpha 2 chain
- Lumican
- Integrin beta
- Collagen alpha-2
- VWFA domain-containing protein
- Integrin alpha-2
- SPARC
- Integrin alpha-V
Sequence:
MLSFVDTRTVLLLAVTSCLATCQSKCLRCGGEDRGPRGERGPPGSPGLDGEDGPPGPPGPPGPPGPPGLGGGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGSRGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGPRGHNGMDGLKGQAGAPGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPTGARGSDGSVGPVGPAGPIGAAGPPGFPGAPGAKGEIGPVGNPGPSGPAGPRGEVGLPGLSGPVGPPGNPGANGLPGSKGATVNGPPCAPSQGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGSAGAQGPPGPSGEEGKRGPNGEVGSAGPPGPPGLRGSPGSRGLPGADGRSGVMGPPGSRGATGPAGVRGPNGDTGRPGEPGLMGPRGLPGSPGNAGPAGKEGPMGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPTGDPGKSGDKGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGPAGEVGKPGERGLPGEFGLPGPAGARGERGPPGESGAVGPAGPIGNRGPSGPPGPDGNKGEPGVVGAPGTAGASGPGGLPGERGAAGIPGGKGEKGETGHRGEPGNTGRDGARGAPGAIGAPGPAGATGDRGEAGPAGPAGPAGPRGSPVSKNLGHLDTKTLKLLDVHGLRVAKGERGEVGPAGPNGFAGPAVNQSENNATATVCSPQGAGITGPPGPPGPAGKEGIRGPRGDQGPVGRTGDTGAGGPPGFAGEKGPSGEPGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGIAGASGEPGPLGLAGPPGARGPPGNVGSPGVNGPPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPTGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEVGDKGPRGLPGIKGHNGLQGLPGLALISEMGSGKDGHAGQPGPVGPAGVRGSQGSQGPAGPPGPPGPPGPAGASGGGYDFGFDGDFYRADQPRSAPALRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGQTCIRAQPESIMPKSWYKNSKPKKHIWLGETINGGSQFEYNMEGVTSKEMATQLAFMRLLANHASQNITYHCRNSIAYMDEETGSLNKAVILQGSNDVELIPEGNSRFTYTVLVDGCSKKTNEWEKTIIEYKTNKPSRLPFLDIAPLDIGDADQEIRVDVGPVCFK
Protein: GM30371p (Q8MSE3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMKIVPGAVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVPIATPAPPTTVAPSMRFDLQSKNLLNSPPPLLNTPTLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRDLPVVNTRGDVLFNSWKGIFNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGGFASNLDGHKLLEQKRQSCDSKLIILCVEALSQDRKRKKREIGDGGSHGESESREFKTADEYAAHLENLLL
Protein: trypsin (EC 3.4.21.4) (Q9VXC8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
- Spaetzle-processing enzyme
- Serine protease grass
- Sphinx1
- trypsin
- trypsin
- Modular serine protease
- Retinoid-inducible serine carboxypeptidase
- trypsin
- RE65433p
- Sphinx2, isoform B
Sequence:
MMQPRLVILGLIGLTAVGMCHAQGRIMGGEDADATATTFTASLRVDNAHVCGGSILSQTKILTTAHCVHRDGKLIDASRLACRVGSTNQYAGGKIVNVESVAVHPDYYNLNNNLAVITLSSELTYTDRITAIPLVASGEALPAEGSEVIVAGWGRTSDGTNSYKIRQISLKVAPEATCLDAYSDHDEQSFCLAHELKEGTCHGDGGGGAIYGNTLIGLTNFVVGACGSRYPDVFVRLSSYADWIQEQIA
Protein: Drosomycin-like 3 (Drosomycin-like E) (Drosomycin-like G) (GEO11147p1) (Q8IRD7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Dorsal-related immunity factor Dif
- Embryonic polarity protein dorsal
- Splicing factor ESS-2 homolog
Sequence:
MVQMIFLFAILAVMTIVLMEANTVLARDCLSGTFGGPCWAWSGEKCRRLCIEEGHVSGHCSGAMKCWCEGC
Protein: LexA repressor (EC 3.4.21.88) (Q9ZFA4)
Organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Has been shown to bind to the direct repeat sequence 5'-GTT-N(7)-GTTC-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- DNA polymerase IV
- DNA repair protein RecN
- Methyltransferase
- Error-prone DNA polymerase
- Crossover junction endodeoxyribonuclease RuvC
- UvrABC system protein A
- Holliday junction branch migration complex subunit RuvA
- DNA repair enzyme
- Cyclic pyranopterin monophosphate synthase
Sequence:
MLTRKQMELLDFIKTRMDRDGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPEAMERAGFSARAAKAAAAPLPKGAVTVETAGALDLPLMGRIAAGLPIEAINGGPQSVTVPGMMLSGRGQHYALEVKGDSMIAAGINDGDIVVIREQQTADNGDIVVALVADHEATLKRYRRRGGMIALEPANDSYETQVYPEQMVKVQGRLVGLIRSY
Protein: Lectin-related NK cell receptor LY49L1 (Q9JIQ2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MSEQEVTFSAVRFHKSSGLQNRVRLEETGKPQKAGLRVCSVPWQLIVIALGILISLRLVIVSVLVTNIFQNSQQNHELQETLNCHDKCSTTTQSDINLKDELLSSTSIECRPGNDLLESLHKEQNRWYSETKTFSDSSQHTGVHKRPISKAEGKGRGFEKYWFCYGIKCYYFVMDRKTWSGCKQTCQISSLSLLKIDNEDELKFLKLLVPSDSCWIGLSYDNKKKDWAWINNGPSKLALNTMKYNIRDGGCMLLSKTRLDNDNCDKSFICICGKRLDKFPH
Protein: Thiosulfate sulfurtransferase (EC 2.8.1.1) (Rhodanese) (Q16762)
Organism: Homo sapiens (Human)
Function: Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity). Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Cystathionine gamma-lyase
- Adenylyltransferase and sulfurtransferase MOCS3
- Cysteine desulfurase
- Sulfite oxidase, mitochondrial
- Persulfide dioxygenase ETHE1, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Putative aspartate aminotransferase, cytoplasmic 2
- Aspartate aminotransferase, mitochondrial
- Sulfide:quinone oxidoreductase, mitochondrial
- Molybdopterin synthase catalytic subunit
Sequence:
MVHQVLYRALVSTKWLAESIRTGKLGPGLRVLDASWYSPGTREARKEYLERHVPGASFFDIEECRDTASPYEMMLPSEAGFAEYVGRLGISNHTHVVVYDGEHLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRSLLKTYEQVLENLESKRFQLVDSRSQGRFLGTEPEPDAVGLDSGHIRGAVNMPFMDFLTEDGFEKGPEELRALFQTKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRAPPESRVSQGKSEKA
Protein: Peptide chain release factor 1-like, mitochondrial (Mitochondrial translational release factor 1-like) (mtRF1a) (Q9UGC7)
Organism: Homo sapiens (Human)
Function: Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain termination codons UAA and UAG.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17803939}.
Interaction partners:
- MTRF1L release factor glutamine methyltransferase
- Large ribosomal subunit protein mL62
- Ribosome-recycling factor, mitochondrial
- Translation initiation factor IF-2, mitochondrial
- Large ribosomal subunit protein bL20m
- Ribosome-releasing factor 2, mitochondrial
- Small ribosomal subunit protein uS7m
- Methyltransferase HEMK2
- Large ribosomal subunit protein mL49
- Small ribosomal subunit protein bS16m
Sequence:
MRSRVLWGAARWLWPRRAVGPARRPLSSGSPPLEELFTRGGPLRTFLERQAGSEAHLKVRRPELLAVIKLLNEKERELRETEHLLHDENEDLRKLAENEITLCQKEITQLKHQIILLLVPSEETDENDLILEVTAGVGGQEAMLFTSEIFDMYQQYAAFKRWHFETLEYFPSELGGLRHASASIGGSEAYRHMKFEGGVHRVQRVPKTEKQGRVHTSTMTVAILPQPTEINLVINPKDLRIDTKRASGAGGQHVNTTDSAVRIVHLPTGVVSECQQERSQLKNKELAMTKLRAKLYSMHLEEEINKRQNARKIQIGSKGRSEKIRTYNFPQNRVTDHRINKTLHDLETFMQGDYLLDELVQSLKEYADYESLVEIISQKV
Protein: Interferon gamma inducible protein 47 (Irgd) (Olfr56 protein) (Q99M59)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDQFISAFLKSASENNFQQLAKEFLPQYSALISKAGGMLSPETLTGIHKALQEGNLSDVMSQIQKAISAAENAILEVAVIGQSGTGKSSFINALRGLGHEADESADVGTVETTMCKTPYQHPKYPKVIFWDLPGTGTPNFHTDTYLDQVGFANYDFFIIISSSRFSLNDALLAQKIKDAGKKFYFVRTKVDSDLYNEQKAKPIAFKKEKVLQQIRDYCVTNLIKTGVTEPRIFLISNLDLGTFDFPELEETLLKELPGHKRHMFALLLPNISDASIELKKHFLREKIWLEALKSAAVSFIPFMTFFKGFDLPEQEQCLKDYRSYFGLDDQSIKEIAEKLGAPLADIKGELKCLDFWSLVKDNSIIAQATSAAEAFCAVKGGPESSAFQALKVYYRRTQFLNIVVDDAKHLLRKIETVNVA
Protein: Saccharopine dehydrogenase-like oxidoreductase (EC 1.-.-.-) (Q8NBX0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATEQRPFHLVVFGASGFTGQFVTEEVAREQVDPERSSRLPWAVAGRSREKLQRVLEKAALKLGRPTLSSEVGIIICDIANPASLDEMAKQATVVLNCVGPYRFYGEPVIKACIENGASCIDISGEPQFLELMQLKYHEKAADKGVYIIGSSGFDSIPADLGVIYTRNKMNGTLTAVESFLTIHSGPEGLSIHDGTWKSAIYGFGDQSNLRKLRNVSNLKPVPLIGPKLKRRWPISYCRELKGYSIPFMGSDVSVVRRTQRYLYENLEESPVQYAAYVTVGGITSVIKLMFAGLFFLFFVRFGIGRQLLIKFPWFFSFGYFSKQGPTQKQIDAASFTLTFFGQGYSQGTGTDKNKPNIKICTQVKGPEAGYVATPIAMVQAAMTLLSDASHLPKAGGVFTPGAAFSKTKLIDRLNKHGIEFSVISSSEV
Protein: CG10206 protein (CG10206-PA) (DNop5 protein) (Q9U5W4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MFVLYETPAGYAIFKLLDEKKLEQVDNLYQEFETPEKANKLLKLKHFEKFNDTTEALAAATAAVEGKVAKPLKKTLKKLLVDDVQSSLLVADAKLGTAIKDKLSVQCVCNTGVQELMRCIRQQADSLLGGLPKREMTAMALGLAHSLSRYKLKFSPDKIDTMIVQAQCLLDDLDKELNNYMMRAREWYGWHFPELGKIITDNIAFVKTIKLVGTRDNMATSDLSDILPEDVEEKVKEAAEISMGTEISEEDVLNIQCLCDEIISINDYRTHLYDYLKARMMAMAPNLTVLVGDTVGARLIAHAGSLINLAKHPSSTVQILGAEKALFRALKTKKDTPKYGLIYHAQLVGQASQKNKGKMSRSLAAKASLATRVDAFGEEATFELGAAHKVKLESRLRLLEEGNLRKLSGTGKAKAKFEKYQAKSEVFTYQPEADNTLNVKKRKHSESEQQTPVKKEEPAEEEAEVKSEKKKKKKKKQKDEEVEAVEEAAAPEPEDQPTPAKKKKKSKHQE
Protein: Nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1) (EC 2.7.7.18) (A0A8I5ZV91)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAARRSSSEMLDDNNIGIRGLHLDQQLQLLPMDSSKKTEVVLLACGSFNPITNMHLRLFELAKDYLNATGEYKVIKGIISPVGDAYKKKGLIPAHHRIIMAELATKNSHWVEVDTWESLQKEWVETVKVLRHHQEKLATGSRSHPQSSPVLERPGRKRKWADQKQDSSPQKPQEPKPTGVPRVKLLCGADLLESFSVPNLWKMEDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQSNIHLVTEWITNDISSTKIRRALRRGQSIRYLVPDLVQEYIEEHDLYNSESEDRNAGVTLAPLQRNTSEAKHNHSTR
Protein: Protein arginine N-methyltransferase 5 (prmt5) (EC 2.1.1.320) (Histone synthetic lethal 7 protein) (Hsl7) (Histone-arginine N-methyltransferase PRMT5) (Q6NUA1)
Organism: Xenopus laevis (African clawed frog)
Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins; such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates the arginine in the motif G-R-G-X-G in its substrates histone H2A, H2AX and H4, producing both monomethylated and symmetrically dimethylated 'Arg-3'. Methylates nucleoplasmin at 'Arg-192', producing both monomethylated and symmetrically dimethylated 'Arg-192'. Involved in the DNA replication checkpoint. Promotes entry into mitosis by promoting the proteasomal degradation of wee2-a. May act as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1. Involved in spliceosome maturation and mRNA splicing (By similarity).
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytosol. Note=Enriched on chromatin.
Interaction partners:
Sequence:
MAAGDGGRVSSGRDVACVTEVADTLGAMANQGFDFLCMPIFHPRFKREFYKEPAKSRPGPQTRSDLLLSGRDWNTLIVGKLSDWIKTDSEVSRIRKTSEAAMQQELNFSAYLGLPAFLIPLKQEDNSNLSRLLINHIHVGHHSTMFWMRVPLMAPNDLRDDLIENEPISLSEEDNSGEERTWIWWHNFRSLCDYNKKIALAIEIGADLPSGHVIDRWLGEPIKAAFLPTSIFLTNKKGFPVLTKVHQRLIFKLFKLEVQFVISGSHHHSEKDLCSYLQYLEYLSQNSPPPNAYEMFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPVKYSQYQQAVYKCLLDRVPEEEKETNIQILMVLGAGRGPLVNASLRAAKQAERKIKVYAVEKNPNAVITLEGWRYEEWGSQVTVVSGDMREWKAPEKADIIVSELLGSFGDNELSPECLDGAQHFLKDDGVSIPGEYTSYLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSDPLPCFTFHHPNKDDVIDNNRYCCLQYRVDLNTVLHGFAGYFNTVLYKDVTLSICPESHSPGMFSWFPILFPIKQPIPMREGDTVCVRFWRCNNGKKVWYEWAVTSPVCSAIHNPTGRSYTIGL
Protein: Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 3, chloroplastic (Q6F6B5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with MIND1 and MCD1, regulates FtsZ ring positioning in chloroplasts in an ARC6-dependent manner. Z-ring accessory protein involved in the initiation of plastid division and division site placement (might functionally replace bacterial MinC). Acts as a disassembly factor that accelerates fragmentation and depolymerization of existing FtsZ2 filaments by enhancing FTSZ2 GTPase activity, thus leading to the conversion of FTSZ2 bound GTP into GDP, a process which triggers FtsZ2 filaments destabilization. Prevents misplaced Z-ring formation at chloroplast stroma nondivision sites. May control the rate of chloroplast expansion. Seems to influence stromule (stroma-filled tubular extensions of the plastid envelope membrane) length and frequency.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:15356321}; Peripheral membrane protein {ECO:0000269|PubMed:15356321}; Cytoplasmic side {ECO:0000269|PubMed:15356321}. Plastid, chloroplast stroma {ECO:0000269|PubMed:17304239}. Note=Distributed in two pools, a first one throughout the stroma, probably to inhibit Z-ring assembly at nondivision sites, and a second one localized to a midplastid ring-like structure (PubMed:30824505). Located at the site of chloroplast division on the outer surface in a ring-shaped structure at the early and middle stages of the process according to PubMed:15356321. Forms ring-like structures, short filaments and discrete foci in the chloroplast stroma according to PubMed:17304239 (PubMed:15356321, PubMed:17304239). {ECO:0000269|PubMed:15356321, ECO:0000269|PubMed:17304239, ECO:0000269|PubMed:30824505}.
Interaction partners:
- Plastid division protein CDP1, chloroplastic
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Dynamin-like protein ARC5
- Cell division protein FtsZ homolog 1, chloroplastic
- Cell division topological specificity factor homolog, chloroplastic
- Septum site-determining protein minD homolog, chloroplastic
- Plastid division protein PDV1
- Plastid division protein PDV2
- Protein MULTIPLE CHLOROPLAST DIVISION SITE 1
- Cell division protein FtsZ homolog 2-1, chloroplastic
Sequence:
MPISMELPVFSTLRVPLFSRLALLPTFGVPFSSLGATTRLNCTSRKARRICVMCLVRDSAPIETCERAGEDGSDEFIEVLVIGSRKESIMDSCLDSPFPSLPLRFWSISKDSSGGLVLQQRLNHQDNALKTMNPIELLQSRPRAFILVASAGYGSDQVEAINILSAVRSGGNLAVAVLLKPFSFEGRKRLEEVNELARKLQQHTNFCIDIDIEVLLQKDLVTLDEALRNANNAVSMAINAASALISGMHGNFIDVMHKDLKELEGSEVKTILESYKEAKVGFGVGHNLKTSILRAIYDCPFFRPGLKDLNAIICIVASSVPLQKKDVKTILRTFRQTMEYTGDIIVSTVHEPDLEPKVRVTTFFILSSSEVETSNKGNIFSGLVPFVLNIFTRYRSQLQKETNIGLGETPVSIKDSADSTDVKTSNQNIEEFEIDSEDLLEVSENGDDSEYPLKEGEPSRNSRLDLKDENVEDFGAIQREPIANWSMDQGYQIEQKWQADSGDTAVLSLGIVNLPVGVRPSKKLNSNLSVASQLSRKADSREESFFNPNGSTKDSSDTASTLLSEKYADFTKQRNLSARASSMLEAERDSSKRWSPILEMQYRGGLFKGRCQGGLPEGKGRLVLGDGSIYDGMWHNGKRSGLGTFYFKNGDVFQGTWREDLIHGKGWFYFHKGDRWFANFWKGKASGEGRFYSKSGEIFFGHFKDGWRHGQFLCIDLDGTRYSETWDDGVLIDRKQVDAGD
Protein: PMS1 homolog 1, mismatch repair system component (E9Q8A5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKQLPAATVRLLSSSQTITSVVSVVKELIENSLDAGATSIEVKLENYGFDKIEIRDNGEGIKAVDVPVMAVKYYTSKISSHEDLGNLTTYGFRGEALGSICNVAEVVVTTRTSADDFSTQYVLDGSGHILSQKPSHLGQGTTVTALKLFKNLPVRKQFYSTAKKCKDELKNVQDLLISYGVLKPDVRITFVHNKAVIWQKSRVPDHRMALMSVLGTAVMGNMESVEQHCEQSQIYLSGFFPKHDADHNSTSLSTPERSFIFINSRPVHQKDILKLIRRYYNLKCLKESTRLYPIFFLKIDVPSAEVDINLTPDKSQVLLQNKESVLIALENLMMTCYGPLPTTESSENNRVDISSANMVVSQTAETDVLFNKMESFGNNYPNADTSAIHFQKDESRKNIDHHLNEQINIGNYFDGHFSGDINKDTFQNIPMNNLSSETNQSNHSETHSVGSMEHIQGENGRNGTGGSGGDGRETLPEKALEICADDWSKGNLCNSMGENIEPVKILVPQKSLSCKVTSSHPRLEPETLSDGPCSRTSDVIHNRSGRLTAYDLISSRAVKKPMSASALFIQDHRTQFLTENPKTGLEDATEQIKARWETLSEEEKHKYEEKAKKDLERYNNQMKKAIEQETQVSLKDGRKKRATSSWGWTQKHKVKDSSNQPKLDELFQS
Protein: Histone-lysine N-methyltransferase KMT5B (Lysine-specific methyltransferase 5B) (Suppressor of variegation 4-20 homolog 1) (Su(var)4-20 homolog 1) (Suv4-20h1) ([histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B) (EC 2.1.1.362) ([histone H4]-lysine20 N-methyltransferase KMT5B) (EC 2.1.1.361) (Q5U3H2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity. In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (By similarity). H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3. Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity). May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity).
Subcellular location: Nucleus. Chromosome {ECO:0000250}. Note=Associated with pericentric heterochromatin. {ECO:0000250}.
Interaction partners:
- [histone H3]-lysine
- Histone-lysine N-methyltransferase SUV39H1-A
- Ash1
- Round spermatid basic protein 1.
- N-lysine methyltransferase KMT5A-A
- Euchromatic histone-lysine N-methyltransferase 2.
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
Sequence:
MGESKNMVLNGRRHGRKFSSNQPVSKSRLQNTQRSHLRQNKGSPSVRRCSRRCGGAPPEAERRHVPSSGMTAKELCEYDDLSTSLILDPYLGFQTHKMNTRFRPIKGRQRELREIIELFKKHDNLEKAFQALTSGDWTRHHFLNKTKSQEKLFKAHVFVYLRMFASDSGFEILSCNRYSSEQNGAKIVATKDWKRNDKIEHLVGCIAELSPSEERMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKVLRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFKSKPGLPVEAPVINSKYGLRETDKRLNRLKKLGESCRNSDSQSVSSNAEADSQEPTTVQTSLRKRTSQSCVKKHGEAKAVTRQTLSSTPSSTSSSKRSQANISSLPKRLKSKPTQTLSKGRRRCRGLWTKGSSRVSASGNLKESSRRDTDRRRSASKGSVARSSENNRSSSKGASPCKDSTLCPYRTRRSTRTSLGAQGAEGTEASNHPASPSIVLKSEPGEFIPVTLGHQMSTPSLDSSCPKKGTCPRRRRTVKQEDSYGESFVQEGVPDLRHAVRAADVADCGKVVLGLPDRHQHYNGSSKSSKALRRGKGKKKRQITRYDAQLILQNNSGIPKITLRRRRDSSSSKNEPRETSSSSSSKISIKFSKEHEKDRSSSYVAKLNNGFSHGPHSSSTKLKIQLKREEDPASLHRTYPEDVTLGIVQRDAADVLDHKAAAQVGQDMEVESMSSEDDDDDYFDNEDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA