wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein (Q383T4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDPLLLSREELEEAQRAIKRRRDTIRTATTERIQTELQPTGSGSLAKRTVPNSIPDKEKAESNSGVVKKLKEELRRRTEELENSVNEQRRAREEYKRLKSVFESFVVEVCEREEAYKIVFSKAYEEVEKHKKHCEGLQRQLEERSSTTTVAATVQVPVADTTTPPVAVGSRTLHEIIDQFRTMIDELECRVGCHGSDDNQSRVAATDISNPDKHRRSAATGTRNRAEQKQKQQVSEGKHQLQPHGQNDQPKEEVVGVVSGSVVPARGAAVLSRPQAPVARSAVSAPKKRRAAKSESAAAVKRAAAEKCNQASTSSLFTSFSTLSERPKKSEVNFGSEPIEDYLALLKKTDLSKVDVLRRELMNFCNSDVNVVATYVVEHFLRKALLTPPMTALWNETVEAMHIDVDVFPAFVRLVVRKLVHLLGPDTAVSAGNTLDHSPQLQRLSLVLRLACVVRLRETESGGDALFFAFYESTISALRSWRLSSTAEGQRDVLKLWMIAVRHLYGFVEDFHMLTRYYANTDGVMEALTLPKLLTCYAVRAVMGNCYFIPSAQPSLVEVEADVQLWTTFCDAMDWSGSELPIDGIGAAAVNILSHSTDERSRGEALLSLRLLVLQKGFGFLQSLTERLRVASGDVDVDEAFAELFSLAVVDLQLEDPLDDQWDRAMSFFMDYLYNCSVEQVNSVEELLTGCKEAHLLVLRAVFQLCSGTGALAEQRVEHATRALRWLKALRVGLDRSARGVASSPLTSVSKGHLLDRTSLGKDLVYLCRHDL
Protein: Aspartyl aminopeptidase (EC 3.4.11.21) (B9ZVU2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGHSPTRGAMQVAMNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLCALLAIPPQPTSPHRVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMELCLADT
Protein: Peroxisomal membrane protein 11E (Peroxin-11E) (AtPEX11e) (Q84JW1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in peroxisomal proliferation. Promotes peroxisomal duplication, aggregation or elongation without fission.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:17220199, ECO:0000269|PubMed:20179140}; Multi-pass membrane protein {ECO:0000269|PubMed:17220199, ECO:0000269|PubMed:20179140}.
Interaction partners:
- Mitochondrial fission 1 protein B
- Peroxisome biogenesis protein 19-1
- Mitochondrial fission 1 protein A
- Peroxisome biogenesis protein 16
- Peroxisomal membrane protein 11B
- Peroxisome biogenesis protein 3-2
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis factor 10
- Peroxisome biogenesis protein 19-2
- Peroxisomal ATPase PEX6
Sequence:
MTTLDLTRAELALIVLYLNKAEARDKICRAIQYGSKFLSGGQPGTAQTVDKNTSLARKVFRLFKFVNDFHGLISPVPKGTPLPLVLLGKSKNALLSTFLFLDQIVWLGRSGIYKNKERTELLGRISLFCWLGSSVCTSAVEIGELGRLSSSMKKMEKELKADDELYRAKLQKSNDRTLALIKSSMDIIVAIGLLQLAPKTISPRVTGAFGFTTSLISCYQLLPSRPKLKTP
Protein: Hemogen (Hemopoietic gene protein) (Negative differentiation regulator protein) (mNDR) (Q9ERZ0)
Organism: Mus musculus (Mouse)
Function: Regulates the proliferation and differentiation of hematopoietic cells. Overexpression block the TPA-induced megakaryocytic differentiation in the K562 cell model. May also prevent cell apoptosis through the activation of the nuclear factor-kappa B (NF-kB) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11404085}.
Interaction partners:
- Ammonium transporter Rh type A
Sequence:
MDMGKGRPRLKLPQMPEAHPQKSCAPDIIGSWSLRNREQLRKRKAEAQGRQTSQWLLGEQKKRKYQRTGKGNKRGRKRQGNVEQKAEPWSQTERERVQEVLVSAEEETEHPGNSATEALPLVPSPTKAVPADQCSEAHQESIQCQERAIQNHSQTHLSPTTCQGIAVLQHSPKMCQDMAEPEVFSPNMCQETAVPQTYPPKALEEMAAAEPLSPKMCQETTVSPNHSSKVPQDMAGPEALSPNMCQEPTVPQEHTLKMCHDVARPEVLSPKTHQEMAVPKAFPCVTPGDAAGLEGCAPKALPQSDVAEGCPLDTTPTSVTPEQTTSDPDLGMAVTEGFFSEARECTVSEGVSTKTHQEAVEPEFISHETYKEFTVPIVSSQKTIQESPEPEQYSPETCQPIPGPENYSLETCHEMSGPEDLSIKTCQDREEPKHSLPEGAQKVGGAQGQDADAQDSENAGAFSQDFTEMEEENKADQDPEAPASPQGSQETCPENGIYSSALF
Protein: L-type lectin-domain containing receptor kinase I.3 (AtLecRK2) (LecRK-I.3) (EC 2.7.11.1) (Salt-responsive receptor protein kinase 1) (Q9M3D8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in resistance response to the pathogenic fungus Alternaria brassicicola.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15067507}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- DEAD-box ATP-dependent RNA helicase 28
Sequence:
MACRLYLALIFSCVYLICLSSQQETGFVYNGFEQADLFIDGIAKILPDGLLQLTNTTELQMGHAFFKKPFDFDPSSSLSFYTHFVCALVPPKLGADGGHGIVFVVSPSIDLSHAYATQYLGVFSNLTNGTSSSHLLAIELDTVKTVEFNELEKPHVGIDLNSPISVESALPSYFSNALGKNISINLLSGEPIQVWVDYDGSFLNVTLAPIEIKKPNQPLISRAINLSEIFQEKMYVGFSSSTGNLLSNHYILGWSFSRRKEQLQSLNLSTLPRVPLPKEEKKKLSPLLIGLVILLVIPVVMVLGGVYWYRRKKYAEVKEWWEKEYGPHRFSYKSLYKATNGFRKDCRVGKGGFGEVYKGTLPGGRHIAVKRLSHDAEQGMKQFVAEVVTMGNLQHRNLVPLLGYCRRKCELLLVSEYMPNGSLDQYLFHEGNPSPSWYQRISILKDIASALSYLHTGTKQVVLHRDIKASNVMLDSEFNGRLGDFGMAKFHDRGTNLSATAAVGTIGYMAPELITMGTSMKTDVYAFGAFLLEVICGRRPVEPELPVGKQYLVKWVYECWKEACLFKTRDPRLGVEFLPEEVEMVLKLGLLCTNAMPESRPAMEQVVQYLNQDLPLPIFSPSTPGIGAFMPVSMEALSAIGVSSVRNSSVSMFVTHTILDGHGR
Protein: Paired box 6 (A0A1W2PP27)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGL
Protein: ATP-dependent lipid A-core flippase (EC 7.5.2.6) (Lipid A export ATP-binding/permease protein MsbA) (Q9KQW9)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity). Shows ATPase activity.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01703}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01703}.
Interaction partners:
- Toxin secretion transporter, putative
- RTX toxin transporter
- Tetraacyldisaccharide 4'-kinase
- Toxin secretion ATP-binding protein
- 3-deoxy-manno-octulosonate cytidylyltransferase
- UPF0434 protein VC_1876
- Intermembrane phospholipid transport system permease protein MlaE
- Rec2-related protein
- Translation initiation factor IF-2
- ABC transporter, ATP-binding protein
Sequence:
MSLHSDESNWQTFKRLWTYIRLYKAGLVVSTIALVINAAADTYMISLLKPLLDEGFGNAESNFLRILPFMILGLMFVRGLSGFASSYCLSWVSGNVVMQMRRRLFNHFMHMPVRFFDQESTGGLLSRITYDSEQVAGATSRALVSIVREGASIIGLLTLMFWNSWQLSLVLIVVAPVVAFAISFVSKRFRKISRNMQTAMGHVTSSAEQMLKGHKVVLSYGGQEVERKRFDKVSNSMRQQTMKLVSAQSIADPVIQMIASLALFAVLFLASVDSIRAELTPGTFTVVFSAMFGLMRPLKALTSVTSEFQRGMAACQTLFGLMDLETERDNGKYEAERVNGEVDVKDVTFTYQGKEKPALSHVSFSIPQGKTVALVGRSGSGKSTIANLFTRFYDVDSGSICLDGHDVRDYKLTNLRRHFALVSQNVHLFNDTIANNIAYAAEGEYTREQIEQAARQAHAMEFIENMPQGLDTVIGENGTSLSGGQRQRVAIARALLRDAPVLILDEATSALDTESERAIQAALDELQKNKTVLVIAHRLSTIEQADEILVVDEGEIIERGRHADLLAQDGAYAQLHRIQFGE
Protein: Kinesin-like protein bimC (P17120)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Important role in mitotic dividing cells. Microtubule motor required for spindle body separation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin-like protein klpA
- Calmodulin-binding protein Sha1, putative
- Kinesin-like protein
- Kinesin-like protein
- MAP65/ase1 homolog
- Mitotic spindle checkpoint protein
- Chromosome segregation protein sudA
- Uncharacterized protein
- Aurora kinase
- CorA family metal ion transporter
Sequence:
MAGPQRATSGLPTRRTTTRQPTRRAGSAIPERQTSTASPAVSTKTAAISRTRTLKSPGEPASVLAKRKERDIEREINEDTSIHVVVRCRGRNEREVKENSGVVLQTEGVKGKTVELSMGPNAVSNKTYTFDKVFSAAADQITVYEDVVLPIVTEMLAGYNCTIFAYGQTGTGKTYTMSGDMTDTLGILSDNAGIIPRVLYSLFAKLADTESTVKCSFIELYNEELRDLLSAEENPKLKIYDNEQKKGHMSTLVQGMEETYIDSATAGIKLLQQGSHKRQVAATKCNDLSSRSHTVFTITVNIKRTTESGEEYVCPGKLNLVDLAGSENIGRSGAENKRATEAGLINKSLLTLGRVINALVDKSQHIPYRESKLTRLLQDSLGGRTKTCIIATISPARSNLEETISTLDYAFRAKNIRNKPQINSTMPKMTLLREFTAEIEKLKAELIATRHRNGVYMSVESYEEMKMENESRRIISEEQRAKIESMESSLRHKVQELLTLTSKFNDLKKDNDDTLAALCSTNDVLQQTDIVLQNTRAQLEEEEMLRCAHEETEHQLQDVGKGLISTLGQTVEDINSLQSKLDRKAELDATNAELWRASSTEVSDVTKRIDQRVEAFQTRHAKLLETTSVKVNEFIATEISNIERTRSDLSEYNRSLDAACNNAKAETSSAHEDMNNVLEEIKDLREEVKSKVGEGLNGLSAAAARISEEVIGEFTQLHSQLHTSFNNLGKDLKSIFETMATHLSEQKNEINRLRAELQSSNRQNIETTHKASAHLAQAIEEEHVAAEAEREILMSQIKALVEESRQKQFARLRAKIDGVRTEISASGDMLEQATTQHDRQIDEWVFKSEQFAKDVNASKDEIRTKLQNDWEAFDQRNSTIRKATESVHKETVRIVDVQVDDMGRQMEALDDFVAKARSQNGRYRDAHIATLDTIATGVRDSYSSIEGRVENLTGRMNQFQQEATHHHATLEESIAPLSNDVRKPLTDLSSSFQNRSLEEYVATGVTPKKRKYDYISVLPSTESHEVLKSRLRTTKEMEVLPFNSDDQLSGPSSSPGGSPSKGFVYNDVEDEVGTHAPTVTNVNPSNTGLREVDANVAARPLVYSTGEKSTDQDGSPVVSPDSATEAEGMNGPPSKRRRSNSVVADTKLPNKMLARRMAGMMEGRENVPPPGISNGRRLRGRPSP
Protein: Large ribosomal subunit protein uL24 (60S ribosomal protein L26) (Silica-induced gene 20 protein) (SIG-20) (P61255)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS11
Sequence:
MKFNPFVTSDRSKNRKRHFNAPSHIRRKIMSSPLSKELRQKYNVRSMPIRKDDEVQVVRGHYKGQQIGKVVQVYRKKYVIYIERVQREKANGTTVHVGIHPSKVVITRLKLDKDRKKILERKAKSRQVGKEKGKYKEETIEKMQE
Protein: Putative gamma-secretase subunit APH-1C (Q9DCZ9)
Organism: Mus musculus (Mouse)
Function: Potential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (amyloid-beta precursor protein).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Gamma-secretase subunit PEN-2
- Presenilin-1
- Presenilin-2
- Nicastrin
- Transmembrane emp24 domain-containing protein 10
- Gamma-secretase subunit APH-1B
- Gamma-secretase subunit APH-1A
- Neurogenic locus notch homolog protein 1
- Amyloid-beta precursor protein
- Neurogenic locus notch homolog protein 3
Sequence:
MTLPVFFGCAFIAFGPAFALYLFTIATDPLRVIFLIAGAFFWLVSLLLSSMFWFLVRVITNNRDESVQNYLLIFGALLSVCIQELFRLAYYKLLKKASEGLKSINPEEDIAPSMRLLAYVSGLGFGIMSGVFSFVNTLSNSLGPGTVGIHGDSPQFFLNSAFMTLVVIMLHVFWGVVFFDGCEKNKWYTLLTVLLTHLVVSTQTFLSPYYEVNLVTAYIIMVLMGIWAFYVAGGSCRSLKFCLLCQDKDFLLYNQRSR
Protein: Transcription elongation factor SPT5 (DRB sensitivity-inducing factor large subunit) (DSIF large subunit) (Q21338)
Organism: Caenorhabditis elegans
Function: May function as a component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates transcription elongation by RNA polymerase II. DSIF may enhance transcriptional pausing at sites proximal to the promoter, which may in turn facilitate the assembly of an elongation competent RNA polymerase II complex.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB2
- Transcription elongation factor SPT4
- RNA polymerase Rpb4/RPC9 core domain-containing protein
- DNA-directed RNA polymerase II subunit RPB7
- Suppressor of Ty 6 homolog
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase RpoA/D/Rpb3-type domain-containing protein
- Putative transcription elongation factor S-II
- RNA polymerase-associated protein CTR9
Sequence:
MSSDESDAASNKEEDTTLSDDDGSDVEIKNSKKDRKRKLASESEKSGSDDDDDDDDDEDENVTSKKSKKQKRKNKAPSGRDFLAWDVEVDDEDEDDDNDYDDEDDPSMNAMNEREEAERAMKEMELSQRNRDRYKFQNMTEDEVQKYFENKYKGDKNDSQYDDEDSAMDDISKNSHLPSTKDPNLWIVKCRMGEEKLVAMHLMRKCLAVEHTNEPFQIKSVVVKEGLKGMIYIEAFKQSHVMSAIEGFSALNQFTITMVPIKDMVDVLRVVKDIPQLKLGSYVRLKRTMYKDDLAVVDLVDIAQNRVNLKLIPRVDYQKRRGAMRTDADKNYKLKRRPMPKLFDQDTIKEVGGEIVTDGDFLVFEGNHFRRGFLYKYFPINAIQADGVKPTLGELEKFQESSDDLKRELETASLKDTENPFVPGDIVEVKAGELVNLRGKVMTVDGTKVVMMPDQEDLKEAITLNAHELRKYFKEGDHAKVISGRYEGHTGLIVRVKDSTAIVLSDLGMEELKVRVRDLQLCADVTTGVDSLGQFQYHDLVQLDHTGNVGVIVRLEKEHLEVLNMHGVVNRIKPQAIIAKKDVRFAKVLDSQNNSIEAKDLVKVIGGPNAKERETDEDPVGEVLYAFRGTVFVYSRKVTKNGGVLVCKPKQLILQGAKKTTSTPMVSRMASPNPMASPRHSSGGMTPRSPQDGMSSRGSSGGQTPRQGGGGGRGGHFGTANQQKVRRDLTLIGKNVRIIKGPMKGHFGIVRDATEDTVRVELHTQCRTISVDRARVMVVGDTGITAGSGGGSSFYSSSKTPMRDSGKTPMYGSKTPMYGAQTPMYGSMTPAYDGGRTPAYGEGGRTPAYGSKTPAYGDLDEHSSSRTPAYGNDSSRTPAYGSADGARTPAYGSTEGGRTPAYGSMDNSRTPAYDDSGRTPGYESMPSRTPNYDSSSKTPAYPESEHSARTPAYNNDYDIPLSPAYEPDAPEAYDNAPARTPAFVSRTPGYDTYENSSPTYEPDAATKVEEDIGDTSSPTYDSPPHSYVVPTPGAMLNPATPGAYHVDTPGFAAPMTPGSGGAYDQYVAPSPFAGYDSNNYNNADGAIEQIPDHFLAQGVWIVQNLCVQIKDHEGRFNGREAIIKDVTDGKVDVYMPDHKCNLEVDFDQLTPMKPQPGDDARVIFGQDAGHSGQLVSMDGFEAVIRSQEDMSDMRVINIGLCCKMHSET
Protein: Vacuolar aspartyl aminopeptidase Lap4, putative (AFU_orthologue AFUA_5G03990) (C8V7I0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Autophagy-related protein 8
Sequence:
MAKKILSDIHHHESNLAYRQYAQLPETLHLNYQPPTATATPAAHTSPIPEAINPDDYSQAYCDFMTEHPTIFHAVDGFSKQLESKGYKYLSERELWTPQLKRGGKYYTTRNGSSLIAFSVGPEYKSGNGLAIIAGHIDALTAKLKPVSKLPNKAGYIQMGVAPYAGGLGKTWWDRDLSIGGKVLVRNASTGKVESKLVKLNWPIARIPTLAEHFGAPSQGPFNKETQMVPIIGVDNSDLFQSTTPAADEGIEPGTFASTQPPKLIKVISKELGITNYSSILSWELELYDSQPARIGGIDKDFIFAGRIDDKLCCYAAQEALMATSDHTSPSSIKMVGYFDDEEIGSLLRQGARSNFMSSVIERIAQSFATSYGPDLLAQTVAKSFLISSDVIHAVNPNFLNVYLENHAPRLNVGVSVSADSNGHMTTDSVSYGFIKRVAEKCGSQLQVFQIRNDSRSGGTIGPMTSSRIGMRAIDVGIPQLSMHSIRATTGSRDPGLGVKLFKGFFDYFEEVDREFSDF
Protein: Myosin phosphatase Rho interacting protein (H0Y7E2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XRFSTIQCQRYIHPEGSEKTWTSSTSSDTSQDRSPSEESMSSEPAPSVLPATGDSDTYLSIIHSLETKLYVTEEKLKDVTVRLESQQGQSREALLALHHQWAGTEAQLREQLRASLLQVGALASQLEQERQERARRVEGHVGELGDFQVKNSQALMCLENCREQLRSLPRASQEDEQDARAASLASVESALVSAIQALQHWPAPAHGGARAQLETGGTEENGKPASLQQCSQSELTEQEQVRLLSDQIALEASLISQIADSLKNTTSDVSRMLHEISWSGQPPMESAGAPVDTWARKVLVDGEFWSQVESLRKHLGTLGGEAVGASGDGQQSIPQGLAPILANATWVRAELSFATQSVRESFHRRLQSIQETLRGTQTALRQHKCLLREILGAYQTPDFERVMQQVLEALRLPAGHEDGVQLSWDLSPLGEVLGRDSDSSQEPFDVSDQSPGAFVAIQEELAQQLKEKASLLEEIAAALPSLPPVESLRDCQKLLQVSQSLSYNTCLGGLGQYSSLLVQDAIIQAQVCYASCRIRLEYEKELQLCKESWQTREPSCSEQAQAARALREEYEELLRKQKSEYLDVIAIVERENAELKAKAAQLDHQQQCLEDAESKHSMSMFTLRGRYEEEIRCVVEQLTRTESTLQAERSRVLSQLDASVRDRQDMERHHGEQIQTLEDRFQLKVRELQTIHEEELRTLQEHYSQSLRCLQDTLCLHQGPHPKALPAPAPNWQATQGEADSMTGLRERIQELEAQMDVMREELGHKDLEGDAATLREKYQRDLESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSVNSDVEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGEATGSPLAQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPDSATVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSVIEQVSWDT
Protein: JmjC domain-containing histone demethylation protein 1 (EC 1.14.11.27) (Jumonji/ARID domain-containing protein 1) (ScJHDM1) ([Histone-H3]-lysine-36 demethylase 1) (P40034)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Does not demethylate H3 'Lys-4' nor 'Lys-79'.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA damage-responsive transcriptional repressor RPH1
- Suppressor of kinetochore protein 1
- Histone H3
- Histone demethylase JHD2 demethylase JHD2)
- Transcriptional activator/repressor GIS1
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Protein ECM5
- Histone H4
- Histone H3-like centromeric protein CSE4
Sequence:
MQDPNICQHCQLKDNPGALIWVKCDSCPQWVHVKCVPLKRIHYSNLTSSEVLSYPNSAKQIKSYRCPNHKEGEYLTAYALITQKGKRQRNKENPEDSHINKRYNFRKKKLLDYIALNEGESKRDKMNHPHKESFMKSFEKWKNGSNIINAADFAEKFDNIDVPYKIIDPLNSGVYVPNVGTDNGCLTVNYITEMIGEDYHVDVMDVQSQMNENWNLGSWNEYFTNTEPDRRDRIRNVISLEVSNIEGLELERPTAVRQNDLVDKIWSFNGHLEKVNGEKAEENDPKPKVTKYILMSVKDAYTDFHLDFAGTSVYYNVISGQKKFLLFPPTQSNIDKYIEWSLKEDQNSVFLGDILEDGIAMELDAGDLFMIPAGYIHAVYTPVDSLVFGGNFLTIRDLETHLKIVEIEKLTKVPRRFTFPKFDQVMGKLCEYLALDKNKITSDVSDGDLLSRTTNCAIQSLHAYVIKPEVKYKPLNFTSKKHLAKALADLIS
Protein: Glutamate receptor ionotropic, kainate 2 (GluK2) (Excitatory amino acid receptor 4) (EAA4) (Glutamate receptor 6) (GluR-6) (GluR6) (Q13002)
Organism: Homo sapiens (Human)
Function: Ionotropic glutamate receptor. 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. Modulates cell surface expression of NETO2 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:14511640, ECO:0000269|PubMed:34375587}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P42260}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutamate receptor ionotropic, kainate 5
- Glutamate receptor ionotropic, kainate 1
- Disks large homolog 4
- Glutamate receptor ionotropic, kainate 4
- Glutamate receptor ionotropic, kainate 3
- Disks large homolog 1
- Neuropilin and tolloid-like protein 1
- Neuropilin and tolloid-like protein 2
- PRKCA-binding protein
- Disks large homolog 3
Sequence:
MKIIFPILSNPVFRRTVKLLLCLLWIGYSQGTTHVLRFGGIFEYVESGPMGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMSLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTESQKGKPANITDSLSNRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDANGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA
Protein: Small ribosomal subunit protein uS5m (37S ribosomal protein S5, mitochondrial) (P33759)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Ribosome assembly protein RSM22
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS33
- Large ribosomal subunit protein uL3m
- Small ribosomal subunit protein mS42
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS1m
Sequence:
MFKRQLSTSVRYLQHYDESLLSRYYPESLLKSIKLAQQTIPEDTKFRVSRNVEFAPPYLDDFTKIHPFWDYKPGMPHLHAQEENNNFSIFRWDQVQQPLPGEGNILPPGVSLPNDGGRKSKSADVAAGLHKQTGVDPDYITRKLTMKPLVMKRVSNQTGKGKIASFYALVVVGDKNGMVGLGEGKSREEMSKAIFKAHWDAVRNLKEIPRYENRTIYGDIDFRYHGVKLHLRSAKPGFGLRVNHVIFEICECAGIKDLSGKVYKSRNDMNIAKGTIEAFTKAQKTLDEVALGRGKKLVDVRKVYYSS
Protein: Rho GTPase-activating protein 26 (Rho-type GTPase-activating protein 26) (Q6ZQ82)
Organism: Mus musculus (Mouse)
Function: GTPase-activating protein for RHOA and CDC42.
Subcellular location: Cell junction, focal adhesion {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Endosome membrane {ECO:0000250|UniProtKB:Q9UNA1}. Note=Colocalizes with actin stress fibers and cortical actin structures. {ECO:0000250}.
Interaction partners:
Sequence:
MGLPALEFSDCCLDSPHFRETLKSHEAELDKTNKFIKELIKDGKSLISALKNLSSAKRKFADSLNEFKFQCIGDAETDDEMCIARSLQEFAAVLRNLEDERSRMIENASEVLITPLEKFRKEQIGAAREAKKKYDKETEKYCGTLEKHLNLSSKKKESQLQEADSQVDLVRQHFYEVSLEYVFKVQEVQERKMFEFVEPLLAFLQGLFTFYHHGYELAKDFGDFKTQLTISIQNTRNRFEGTRSEVESLMKKMKENPLEHKTISPYTMEGYLYVQEKRHFGTSWVKHYCTYQRDSKQITMVPFDQKSGGKGGEDESVTLKSCTRRKTDSIEKRFCFDVEAVDRPGVITMQALSEEDRRLWMEAMDGREPVYNSNRDSQSEGTAQLDSIGFSIIRKCIHAVETRGINEQGLYRIVGVNSRVQKLLSVLMDPKAASETETDICAEWEIKTVTSALKTYLRMLPGPLMMYQFQRSFIKAAKLENQETRVSEIHSLVHRLPEKNRQMLQLLMNHLANVANNHKQNLMTVANLGVVFGPTLLRPQEETVAAIMDIKFQNIVIEILIENHEKIFNTVPDVPLTNAQLHLSRKKSSDSKPPSCSKRPLTLFHAVPSTEKQEQRNSIINSSLESVSSSANSILNSSSSLQPNLNSSDSNLDVVKPSRPSSLPPNPSPTSPLSPSWPMFSAPSSPMPTSSTSSDSSPIRSVAGFVWFSVAAVVLSLAWSSLHAVFSLLVNFVPCHPNLHLLFDRPEEAVREDSSTPFRKAKALYACQAEHDSELSFTAGTVFDNVHPSQEPGWLEGTLNGKTGLIPENYVEFL
Protein: L-serine/homoserine O-acetyltransferase (EC 2.3.1.30) (EC 2.3.1.31) (Homoserine O-trans-acetylase) (D2Z028)
Organism: Streptomyces lavendulae
Function: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-serine to yield the activated serine, O-acetyl-L-serine. It prefers L-serine over L-homoserine.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
Interaction partners:
Sequence:
MREFIPPASRFIELPDGFAMRRGGALYGARIAYETFGSLNAARDNAVLVLTGLSPDAHAASRPDDPTPGWWEAMVGPGKPVDTDLWHVICVNSLGSCKGSTGPASTDPRTGEPYRLSFPELSIEDIADAAAHTVRALGISRLACVVGASMGGMSALALLARHPELARTHISLSGAVHALPFSIAVRSLQREAIRSDPGWLQGHYDEGEGPRRGMLTARKLGMMTYRSAQEWDCRFGRTRIGERRRADQGRFGPEFEVESYLDFHAQRFADRFDPNSYLYLSHAMDQFDLGDGGGGGGGAPGALSRMRVERALVMGARTDILFPLSQQQEIADGLSAGGADVSFLPVDTPAGHDAFLVDIERFGPPVAKFLAIVA
Protein: Homoserine kinase (EC 2.7.1.39) (Protein DOWNY MILDEW RESISTANT 1) (Q8L7R2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. Is specific for L-homoserine and cannot use other substrates such D-serine, L-serine, D-threonine and L-threonine, galactose or D-homoserine in vitro. Required for susceptibility to the downy mildew pathogen Hyaloperonospora parasitica.
Subcellular location: Plastid, chloroplast stroma {ECO:0000305}.
Interaction partners:
- Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic
- Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic
- Homoserine dehydrogenase
- Cystathionine gamma-synthase 1, chloroplastic
- Aspartokinase 2, chloroplastic
- Probable cystathionine gamma-synthase 2
- Threonine synthase 2, chloroplastic
- Threonine synthase 1, chloroplastic
- Cystathionine beta-lyase, chloroplastic
- Aspartokinase 1, chloroplastic
Sequence:
MASLCFQSPSKPISYFQPKSNPSPPLFAKVSVFRCRASVQTLVAVEPEPVFVSVKTFAPATVANLGPGFDFLGCAVDGLGDHVTLRVDPSVRAGEVSISEITGTTTKLSTNPLRNCAGIAAIATMKMLGIRSVGLSLDLHKGLPLGSGLGSSAASAAAAAVAVNEIFGRKLGSDQLVLAGLESEAKVSGYHADNIAPAIMGGFVLIRNYEPLDLKPLRFPSDKDLFFVLVSPDFEAPTKKMRAALPTEIPMVHHVWNSSQAAALVAAVLEGDAVMLGKALSSDKIVEPTRAPLIPGMEAVKKAALEAGAFGCTISGAGPTAVAVIDSEEKGQVIGEKMVEAFWKVGHLKSVASVKKLDNVGARLVNSVSR