wanglab/gogpt-training-data huggingface dataset:
Protein: Putative disease resistance protein At1g50180 (Q9SX38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential disease resistance protein.
Interaction partners:
- Disease resistance protein
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Protein C2-DOMAIN ABA-RELATED 1
- Bromodomain transcription factor
- Probable LRR receptor-like serine/threonine-protein kinase At1g63430
- Transcription initiation factor TFIID subunit 8
- At3g02160
- Disease resistance family protein / LRR family protein
- RNA polymerase I specific transcription initiation factor RRN3 protein
- RNA polymerase I specific transcription initiation factor RRN3 protein
Sequence:
MAEAIVSVTVQKLGQLLLEEPLFLFGIGDQVKQLQDELKRLNCFLKDADEKQHESERVRNWVAGIREASYDAEDILEAFFLKAESRKQKGMKRVLRRLACILNEAVSLHSVGSEIREITSRLSKIAASMLDFGIKESMGREGLSLSDSLREQRQSFPYVVEHNLVGLEQSLEKLVNDLVSGGEKLRVTSICGMGGLGKTTLAKQIFHHHKVRRHFDRFAWVYVSQDCRRRHVWQDIFLNLSYKDENQRILSLRDEQLGEELHRFLKRNKCLIVLDDIWGKDAWDCLKHVFPHETGSEIILTTRNKEVALYADPRGVLHEPQLLTCEESWELLEKISLSGRENIEPMLVKKMEEIGKQIVVRCGGLPLAITVLGGLLATKSTWNEWQRVCENIKSYVSNGGSSNGSKNMLVADVLCLSYEYLPPHVKQCFLYFAHYPEDYEVHVGTLVSYCIAEGMVMPVKHTEAGTTVEDVGQDYLEELVKRSMVMVGRRDIVTSEVMTCRMHDLMREVCLQKAKQESFVQVIDSRDQDEAEAFISLSTNTSRRISVQLHGGAEEHHIKSLSQVSFRKMKLLRVLDLEGAQIEGGKLPDDVGDLIHLRNLSVRLTNVKELTSSIGNLKLMITLDLFVKGQLYIPNQLWDFPVGKCNPRDLLAMTSLRRLSINLSSQNTDFVVVSSLSKVLKRLRGLTINVPCEPMLPPVDVTQLVSAFTNLCELELFLKLEKLPGEQSFSSDLGALRLWQCGLVDDPFMVLEKLPNLKILQLFEGSFVGSKLCCSKNLENLEEWTVEDGAMMRLVTVELKCCNKLKSVPEGTRFLKNLQEVEIGNRTKAFKDKLISGGEDFYKVQHVPCVVFENCEL
Protein: G-type lectin S-receptor-like serine/threonine-protein kinase CES101 (EC 2.7.11.1) (Protein CALLUS EXPRESSION OF RBCS 101) (Q9LW83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes the expression of genes involved in photosynthesis at least in dedifferentiated calli.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MWSNCIFLTLFTFYLFLGQSCCQTDTLLQGQYLKDGQELVSAFNIFKLKFFNFENSSNWYLGIWYNNFYLSGAVWIANRNNPVLGRSGSLTVDSLGRLRILRGASSLLELSSTETTGNTTLKLLDSGNLQLQEMDSDGSMKRTLWQSFDYPTDTLLPGMKLGFNVKTGKRWELTSWLGDTLPASGSFVFGMDDNITNRLTILWLGNVYWASGLWFKGGFSLEKLNTNGFIFSFVSTESEHYFMYSGDENYGGPLFPRIRIDQQGSLQKINLDGVKKHVHCSPSVFGEELEYGCYQQNFRNCVPARYKEVTGSWDCSPFGFGYTYTRKTYDLSYCSRFGYTFRETVSPSAENGFVFNEIGRRLSSYDCYVKCLQNCSCVAYASTNGDGTGCEIWNTDPTNENSASHHPRTIYIRIKGSKLAATWLVVVASLFLIIPVTWLIIYLVLRKFKIKGTNFVSESLKMISSQSCSLTNKRLSTLRVGSTIDQEMLLLELGIERRRRGKRSARNNNNELQIFSFESVAFATDYFSDANKLGEGGFGPVYKGRLIDGEEVAIKRLSLASGQGLVEFKNEAMLIAKLQHTNLVKLLGCCVEKDEKMLIYEYMPNKSLDYFLFDPLRKIVLDWKLRFRIMEGIIQGLLYLHKYSRLKVIHRDIKAGNILLDEDMNPKISDFGMARIFGAQESKANTKRVAGTFGYMSPEYFREGLFSAKSDVFSFGVLMLEIICGRKNNSFHHDSEGPLNLIVHVWNLFKENRVREVIDPSLGDSAVENPQVLRCVQVALLCVQQNADDRPSMLDVVSMIYGDGNNALSLPKEPAFYDGPPRSSPEMEVEPPEMENVSANRVTITVMEAR
Protein: Protein kinase (Eurofung) (Q5AVW7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Serine/threonine-protein kinase tel1
- non-specific serine/threonine protein kinase
- Protein kinase domain-containing protein
- non-specific serine/threonine protein kinase
- M-phase inducer phosphatase
- DNA damage checkpoint effector kinase
- DNA replication checkpoint mediator MRC1 domain-containing protein
- Polo-like kinase
- Histone chaperone asf1
- DNA replication licensing factor MCM4
Sequence:
MEATQESTQPYTDPRRGGLNASGLLEEDLSDVICILHPSSPQALEAVAATARVAPWHILQRDDLEYEVPSTAALDIALRLSSNVMDPSRGFSFGRTIGRSDILLCADNGSKRISNTHFRIYITTDSILMLEDVSTNGTIVDNCRLKKRDRENSRMLTNGSVISVVNGDYATNEVKFVVRLPNREGFTDLYAKNLQNYLGRVYGGAPGTVQPGRRHPSALSIPPWNSHGMHWSGGPTYNVTGQIGKGAFAVVYKLATKQHGAVFAAKELDKRHFMKNGVLNQKVDNELKIMKDLKHPNIVQYIDHHEHDRWIYIIMEYVPCGELSTYLQNMVNIPEDMVKTIARQILHALKYLHKRKITHRDIKPDNILIASHEPLKVKLSDFGLSKVVQEETFLKTFCGTLLYCAPEVYPEYDMYRRGEVRKRRRVGDPLPKTSPYDQSVDMYSLGAVLYHLLAGIPPYTGRGDDRGAQMLRTIMTTEPDYQILREAGVSEEGIDLVSKLLNRDPQLRPKELECLKHPWLVDIPDIDEYEDDDLLSNYSDGLSAIGEVAEDELDASQLSLEENPDFGDDLAENDSDLAQSKRPRINSPPPDVGYPSLPKLEVSQDHQQISHATPRRLFGEITSSALRSSHALGDNMDAFEDDHHSVQDFISSTGESMISYGGSLNSVLSLPENPVAGSALSLLGAEKLVRQLNMNSWHPGTSRNPLLSTEAASPQPSEDDGLADDKVQKEFPQAGSLMTPKAAKFKRRIELPLPDTASERSGSDDSNMRDADGQYRNLTREPEIFDIELANTIDAKTGQLIPDYAESRGFQPPADPSRAGGPVGVLRPLPTPGESRPLLGKLTTLPGSIFDLTLRLEDRMTSWGRGPQASICYPDPMDARIPAYALEITFWAPRLEERIASGQDWMTIPGTMAHLSTKTRKCIWVNDVELQKGPEGGFHFGKLYTGDIITVYRHRNKFLKFKCEFYHGDSARERPENEKGFVVRKVLTSKSTAVNQQPVRRNAISKE
Protein: ER degradation-enhancing alpha-mannosidase-like protein 1 (Q92611)
Organism: Homo sapiens (Human)
Function: Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It has low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19934218}; Single-pass type II membrane protein {ECO:0000269|PubMed:19934218}.
Interaction partners:
- DnaJ homolog subfamily C member 10
- Protein sel-1 homolog 1
- Calnexin
- X-box-binding protein 1
- Derlin-2
- Endoplasmic reticulum chaperone BiP
- Protein OS-9
- Alpha-mannosidase 2C1
- ER degradation-enhancing alpha-mannosidase-like protein 3
- Derlin-3
Sequence:
MQWRALVLGLVLLRLGLHGVLWLVFGLGPSMGFYQRFPLSFGFQRLRSPDGPASPTSGPVGRPGGVSGPSWLQPPGTGAAQSPRKAPRRPGPGMCGPANWGYVLGGRGRGPDEYEKRYSGAFPPQLRAQMRDLARGMFVFGYDNYMAHAFPQDELNPIHCRGRGPDRGDPSNLNINDVLGNYSLTLVDALDTLAIMGNSSEFQKAVKLVINTVSFDKDSTVQVFEATIRVLGSLLSAHRIITDSKQPFGDMTIKDYDNELLYMAHDLAVRLLPAFENTKTGIPYPRVNLKTGVPPDTNNETCTAGAGSLLVEFGILSRLLGDSTFEWVARRAVKALWNLRSNDTGLLGNVVNIQTGHWVGKQSGLGAGLDSFYEYLLKSYILFGEKEDLEMFNAAYQSIQNYLRRGREACNEGEGDPPLYVNVNMFSGQLMNTWIDSLQAFFPGLQVLIGDVEDAICLHAFYYAIWKRYGALPERYNWQLQAPDVLFYPLRPELVESTYLLYQATKNPFYLHVGMDILQSLEKYTKVKCGYATLHHVIDKSTEDRMESFFLSETCKYLYLLFDEDNPVHKSGTRYMFTTEGHIVSVDEHLRELPWKEFFSEEGGQDQGGKSVHRPKPHELKVINSSSNCNRVPDERRYSLPLKSIYMRQIDQMVGLI
Protein: Cuticle collagen 1 (Protein dumpy-15) (Protein squat-3) (P08124)
Organism: Caenorhabditis elegans
Function: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment.
Subcellular location: Secreted. Secreted, extracellular space {ECO:0000269|PubMed:37721936}.
Interaction partners:
- Zinc metalloproteinase dpy-31
Sequence:
METDGRLKAYKFVAYAAVGFSIAAVASVLLTLPMVYSYVSHVRQQMHHEINFCKGSAKDIFAEVNYMKANAGPVPPRNRTTRQAYGGPEVNPAPNLQCEGCCLPGPPGPAGAPGKPGKPGRPGAPGTPGTPGKPPVAPCEPTTPPPCKPCPQGPPGPPGPPGAPGDPGEAGTPGRPGTDAAPGSPGPRGPPGPAGEAGAPGPAGEPGTPAISEPLTPGAPGEPGDSGPPGPPGPPGAPGNDGPPGPPGPKGAPGPDGPPGVDGQSGPPGPPGPAGTPGEKGICPKYCALDGGVFFEDGTRR
Protein: Lysophosphatidic acid phosphatase type 6 (EC 3.1.3.2) (Acid phosphatase 6, lysophosphatidic) (Acid phosphatase-like protein 1) (PACPL1) (Q8BP40)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes lysophosphatidic acid (LPA) containing a medium length fatty acid chain to the corresponding monoacylglycerol. Has highest activity with lysophosphatidic acid containing myristate (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower activity with C18:0 and C6:0 lysophosphatidic acid.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12010880}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta-2
Sequence:
MRVWVPVGVLTSLAYCFHQRRVALAEQRAPNGQRPVDRNLLELKMVQVVFRHGARSPLKPLPLEEQVEWNPKLLEIPPQTRFDYTVTNLAGGPKPHSHYDTEYRKTTLRGGVLAGQLTKVGMQQMFALGEKLRKNYVEDIPFLSPVYNPQEVFIRSTNMFRNLESTRCLLAGLFQHQKGSAVIHTDEASSEVLYPNYQSCWVLKEKTRGRKKAAISQPGISEDLEKVKTGVGINNGDDVDFFVLLDNVAAEQVHSLLNCPALERFAQLIEQRAVDMALYVVEQEDRESIQMAVGPFLHILEGNLLKTVDPTTAPSKTRKMYLYATHDVTLLPMLLALGIFDQKWPPFAVDLTMELYQHQESKEWFVQLFYNGKEQVPRGCPDKLCPLDKFLNTMSVYSVSPEKYRTLCSKTRIVELGE
Protein: WD repeat-containing protein 44 (Rabphilin-11) (Rab11BP) (Q9R037)
Organism: Rattus norvegicus (Rat)
Function: Downstream effector for RAB11. May be involved in vesicle recycling.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10464283}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10464283}. Endosome membrane {ECO:0000269|PubMed:10464283}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10464283}. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia. {ECO:0000269|PubMed:10464283}.
Interaction partners:
- RNA helicase aquarius
- Mitochondrial glutathione transporter SLC25A40
- C-type lectin domain containing 16A
Sequence:
MMPLKMCTWGGSYPVGSPGKVGLLSFKETKNTGNKAGNESPVQELRQDVSKKIIECIIEESQKVLQLEDDSLDSKGKGLSDQATASHSVAGTEFSNIPGLLAIQHELQQGSRKADSQNAAEETELETQKCFPSDNNCEKSEKTEDETNNLTEVSSADQLDASKLETEILNKEAVEVKEGDVVNPASSDALSTKDFAAVEEVAPAKPPRHLTPEPDIVASTKKPVPARPPPPTNFPPPRPPPPSRPAPPPRKKKSDLEFEALKTPDLDVPKDNIASDSLLTTNMASESTVRDSLPSLDLASATSGDKIVTAQENGKAPDVQTVAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTPLTLHIMRRTKEYVSNDATQSDDEEKLQSQQTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAINKVKSVRDEVFHTDQDDPSSSDDEGMPYTRPVKFKAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNIVRIWALKNAFDYFNNMRMKYNTEGRVSPSPSQESLSSSKSDTDMGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRRECLCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIFYDTEHLKYHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDFTYLVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKLEGIDKYEDAEVLDNTSTGIVKTDNTEVLLSADFTGAQCFYVKNSFLYP
Protein: Fibronectin type-III domain-containing protein (Q385J1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFESLYELFSTSPGRTPSNVVCNNEMPPALIVVMLKADEQRSHTSQSEGEGRRLLNGLMAAYPSSNYMFVIDAAESTSEVFAAVTGEYNLLRELSPKFCYVVFAALRDPEVVVPCTSVFNPAWVGELRRMLDGLRNPRHMVAELLLRKELCMQLEGLLRFTAECRWIGDESLSAKLSRLVDSRVTDLSSSKNYSMPSCGGLQVSCISMLKEDEEAGSPPLVLQTGIRIRGVVPDLTRSLRLSDCNEQEYSPPLLLVVLHAGESIRENIVDGSVGRDSSVQELDCLLQQLSSSDEVFVSLGGYVVVPLCSAAAARKQWLDTKEVLTRRVTYDGADSHALIREMLTQALLPLRKWHRKHHTPAEDEKSSSPRSRVAILFYTPQEPCSVHQCVHSIVREQLAFLQVPLFCITTPVGVDTAYKLLDISSTSGERCICTLEASCTANVNHDSECGGKGQACYGVLGSSTGERVAQAALTAIRSVTHLGVSVTVHSIDNSKEDTRFEVGDLRQGLDTTVLISRPVQNPDRGASAKHQLTILAYSVDKSRYDIVRFMPSETVKEVPSSEHSWWSQLQIAGRLLKSMPSKAPPSVSQLGNTLMQHSEEVPSLGGLAEQQHKLVEWLLSNYGTQELEGTPYTLVIGWCPSPYMGNGSTEEEDGWPTSSGYLSASPCIADPLVELRWTNFPFCDGAPVTTISAIISRTFPFEALVESTASNSLALETLRNDSAEIRLASMKHIPELREARARIVAFLSVDTSTGAMSLQQLVPAKTEDDVKGGMLHTFRSLRLHQMYCVVHLALRCSLDSSFFMQNDVIIADGITFITPRASVHDVRVTTVTHCRADVEWKGTATSVRIECKPMKWISTQKNSERSPGGISDVTDSEVVGADGATTIVEYSCDGFQAAVAGLQPFTLYHLRVTPIGDSTHGAMIREKLEEGEAYFATCVDAGVIDTLSVESIVPDSETLKLTVAHPVLCKTAAISRTRSLVLTITPTMSMSNSLDKEKPLQMRRRKFSEGESVVTTFTLQKVERVQVCIEFNMKLCFGHVYLEETSSTCSHTCGSDDNDAQYIDDSGQVRGVCVWFARGVSPWTKEVALCGNSSPRSLSAPPMCSSPTQLLDGYRISRSDTPFAEMRSDFKASNDLKEHSTEENVVVTEGKEGCGEMEWSESSIVSVSHEKRLSKYVVDDSDPSTTGEATRSLYCVFSKDPTFRGVRFLTDMSSQVLLASFAVGGNSSGYISAVIMPLNVSVDNLDGDNTSLKVSYAHVDRERPVTVKLVQHLEQRYQRVGRKTMHLYAVTDVCCRSREEVLGVNGVKTKKMLLSWTCGAQQEGSSLFVLIGSKRYKPKPNNTLLIDCNDTLVAAPVCFCGSNIIKETCSIYLVPPPPPLSSQYCTVRAVKDEALHIFITEKYCVLLYRCLACVSDLIMVLLHVGGDNATELPCSQQKLSGGETGVHLQVPLDAVDPEKNTVELCVEVRVRNSACCIGDNPLVSDWRDRTGFGGSGSSSSLISTNILKGRRQQPILLIPWSTSESFDVPVASSTLIKNLQVTELHSTRAKLSWTTVPYKETADEKLGVFLTVQCAAAEGHVKKYKEYVVCSARSFLLRGLLPATPYHVELSLDGGCPPGRVVFVTPQDMEDNVLRKLIPSITAVWASRRGRNWQHVMRAACGGTDDAEQQRFVRLQLDIPNVESKHWTVSPSSAQIIKEEISGCGTLRLAVTAKVQVLLVAKSGKLLQMWSTVSGTQSQTVSFAFPICGGNPAASWPHIELRMDSFAQFSPAATEDETGDEVSPSVDQDSWSFSEKDKISDLRAGHLVSRKHLGDRTNCPFANSHVTVHLVGCPQLIKVDENCCVVEWSGSCSGYAIHWRVGPSGVVNTEHIEAERKQKPSITVDVSALDTVVLLFSLHGADCASNCVLFAVLVPPKVSKQIGCCCETTRGLSVPTSPRCSNKGLIKVDYTRGGQPGSTLTDGESLGQNGVSGVSSGLCCTASVVDTSSLEWREGFKGLLKDEVCCMLLPFPMEVVWLNPVVTAFYSRRT
Protein: FI10013p (Xrp1, isoform C) (Xrp1, isoform D) (Xrp1, isoform E) (Q8IN74)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFAEEDLIELEGKKTDPFSPAMDGMNNDNLDDDFLQLNDLLNEEETFDMSSMSGVGIDINQEQELDFINIFHNSQPTAMLTSSEDPYLATYSQATSTSSTTKFITEEPLLADMTSFDISYTSSQELGFGLVEDVSGSFASSCSDVAAAIPAPIQHPIITNIKRSAPAPVESQPTKRSRLMLQIKTELAPAFSPTTPEIINQLLNDDRFEAPTTSTSTSTSNTSISSSTHADIVEDLRSAEEETTTDFSAPNTPHSNYSASSSCAAPTCQTGYGGFLTAPTSPAYSTASTSVFSPSPASGISGKRKRGRPAKDHADGPDPVLMSSMKSEEERKAYQDRLKNNEASRVSRRKTKVREEEEKRAEDTLLAENLRLRARADEVASRERKFKKYLMERQRQKSTYVKQEQD
Protein: AT3g62110 (Pectin lyase-like superfamily protein) (Q9FPJ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- GDP-mannose transporter GONST2
Sequence:
MKRSFLLLYVLLVQAFYGAWCSVGESLHCEYSNLASLHRPHSVSITEFGAVGDGVTLNTKAFQNALFYLNSFSDKGGAKLFVPAGQWLTGSFDLISHLTLWLDKGATILGSTSSENWPVVDPLPSYGRGRELPGRRHRSLIYGQNLTDVVITGENGTIDGQGTVWWDWFRNGELNYTRPHLVELMNSTGLIISNLTFLNSPFWNIHPVYCRDVVVKNLTILAPLESPNTDGVDPDSSTNVCIEDCYIVTGDDLVSIKSGWDEYGISYARPSSKIKINRLTGQTTSSSGIAIGSEMSGGVSEIYIKDLHLFNSNTGIRIKTSAGRGGYVRNVHILNVKLDNVKKAIRFTGKYGEHPDEKYDPKALPAIEKITFENVNGDGIGVAGLLEGIEGDVFKNICFLNVTLRVKKNSKKSPWECSNVRGYSQWVSPEITCDSLKESIFPEHGSDCFGLSENNMEISSGLSRSPWLLSW
Protein: Synovial sarcoma translocation, chromosome 18 (Q4VAX2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSVAFAAPRQRGKGEITPAAIQKMLDDNNHLIQCIMDSQNKGKTSECSQYQQMLHTNLVYLATIADSNQNMQSLLPAPPIQNMPMGPGGMNQSGPPPPPRSHNMPSDGMVGGGPPAPHMQNQMNGQMPGPNHMPMQGPGPNQLNMTNSSMNMPSSSHGSMGGYNHSVPSSQSMPVQNQMTMSQGQPMGNYGPRPNMSMQPNQGPMMHQQPPSQQYNMPQGGGQHYQGQQPPMGMMGQVNQGNHMMGQRQIPPYRPPQQGPPQQYSGQEDYYGDQYSHGGQGPPEGMNQQYYPDGHNDYGYQQPSYPEQGYDRPYEDSSQHYYEGGNSQYGQQQDAYQGPPPQQGYPPQQQQYPGQQGYPGQQQGYGPSQGGPGPQYPNYPQGQGQQYGGYRPTQPGPPQPPQQRPYGYDQGQYGNYQQ
Protein: Nucleotide triphosphate diphosphatase NUDT15 (EC 3.6.1.9) (MutT homolog 2) (MTH2) (Nucleoside diphosphate-linked moiety X motif 15) (Nudix motif 15) (Nucleoside diphosphate-linked to another moiety X hydrolase 15) (Nudix hydrolase 15) (Q9NV35)
Organism: Homo sapiens (Human)
Function: May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives. Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides to prevent their incorporation into DNA, is unclear. Through the hydrolysis of thioguanosine triphosphates may participate in the catabolism of thiopurine drugs. May also have a role in DNA synthesis and cell cycle progression by stabilizing PCNA. Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
Interaction partners:
- Dihydropyrimidine dehydrogenase [NADP
- Glutamine-dependent NAD
- Thiopurine S-methyltransferase
- Folylpolyglutamate synthase, mitochondrial
- GTP cyclohydrolase 1
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Thymidylate synthase
- Nicotinate phosphoribosyltransferase
- Maestro heat-like repeat-containing protein family member 6
- Inosine triphosphate pyrophosphatase
Sequence:
MTASAQPRGRRPGVGVGVVVTSCKHPRCVLLGKRKGSVGAGSFQLPGGHLEFGETWEECAQRETWEEAALHLKNVHFASVVNSFIEKENYHYVTILMKGEVDVTHDSEPKNVEPEKNESWEWVPWEELPPLDQLFWGLRCLKEQGYDPFKEDLNHLVGYKGNHL
Protein: Cytosolic calcium-binding protein 1 (Cytosolic Ca(2+)-binding protein 1) (Q9SXE9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17145720}.
Interaction partners:
- Guanosine nucleotide diphosphate dissociation inhibitor 1
- H/ACA ribonucleoprotein complex subunit 3-like protein
Sequence:
MATIEVEQVTPVAAENIEVPPPKAVESEEVTTVSESLPAPVTESQAPVEVTTKDLVVEETEKPIEETEEAQVETPEVVEIKKDEEAPVETPVVVEDESKTEEVVEAKKEEEVEEKKTEEAPVVVEEEKKPEAEEEKPAVEASVTAPVEKADE
Protein: Transcription factor RFX4 (Regulatory factor X 4) (A2BGA0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May activate transcription by interacting directly with the X-box.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858}.
Interaction partners:
- Forkhead box protein J1-A
Sequence:
MHCGLLEEPDMDSTESWIERCLNESESKRFSSHSSIGNISNDENEEKENNRASKPHSTPATLQWLEENYEIAEGVCIPRSALYMHYLDFCEKLDSQPVNAASFGKIIRQQFPQLTTRRLGTRGQSKYHYYGIAVKESSQYYDVMYSKKGAAWVNETGKKEVTKQTVAYSPRSKLGTLLPDFPNVKDLNLPASLPEEKVSTFIMMYRTHCQRILDTVIRANFDEVQSFLLHFWQGMPPHMLPVLGSSTVVNIVGVCDSILYKAISGVLMPTVLQALPDSLTQVIRKFAKQLDEWLKVALHDLPENLRNIKFELSRRFSQILKRQTSLNHLCQASRTVIHSADITFQMLEDWRNVDLNSITKQTLYTMEDSREDQRRLIIQLYQEFDRLLEDQSPIEAYIEWLDSMVERCVVRVAGKRPGSLKRVAQQFLLMWSCFGTRVIRDMTLHSAPSFGSFHLIHLMFDDYVLYLLESLHCQERANELMRAMKGEGAPADTGEELMLMSSTPTSTSPAPYSPAKSVHSVGVPAVGSPNSAQSPEYTSISATTGAVQSYTWSLTYTVTTSGGSPTEPGSQLSCMRGGPALHGSSSAHRMPVYPHRDEHGYTGSYNYSSYANQHHHAIQSQYSSLTHEAGLPTPLHYSSYHRTSAQYPLNSQMSRMESCLMSGSPLLHSSPVTPRWPDVPSANSCYSSPTVHASRYSTGDMYSPLAPRRNSEYEHAQHFPGFAYINGEATTGWAK
Protein: BRCA1-associated RING domain protein 1 (BARD1) (Ce-BRD-1) (Cebrd-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BARD1) (Q21209)
Organism: Caenorhabditis elegans
Function: Constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity. When bound to chromatin, the brc-1-brd-1 heterodimer within the CeBCD complex is inactive during normal conditions, but in response to DNA damage, the brc-1-brd-1 heterodimer associates with other proteins such as the recombinase rad-51 or the E2-ubiquitin-conjugating enzyme let-70, which activate the CeBCD complex as an E3-ubiquitin ligase. Moreover, association between the brc-1-brd-1 heterodimer and rad-51 and let-70, probably requires DNA checkpoint proteins such as atl-1 and mre-11 in order to induce ubiquitination at DNA damage sites. To this end, the brc-1-brd-1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by ionizing radiation for example. In particular, protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16628214}. Nucleus {ECO:0000269|PubMed:16628214, ECO:0000269|PubMed:30383754}. Chromosome {ECO:0000269|PubMed:16628214, ECO:0000269|PubMed:30383754}. Note=Co-localizes with brc-1 in germline nuclei at meiotic prophase I (PubMed:30383754). At the transition between mid- and late- pachytene, localization together with brc-1 is less diffuse and becomes a linear pattern along the chromosomes (PubMed:30383754). In late pachytene nuclei, co-localizes with brc-1 at crossover sites and the short arm of homologous chromosomes (PubMed:30383754). {ECO:0000269|PubMed:30383754}.
Interaction partners:
- Breast cancer type 1 susceptibility protein homolog
- DNA repair protein RAD51 homolog
- Helicase ATP-binding domain-containing protein
- DNA repair protein brc-2
- Anaphase-promoting complex subunit 1
- MutS protein homolog 5
- FANCD2
- ATP-dependent DNA helicase II subunit 2
- RecQ-like DNA helicase blm-1
- Meiotic recombination protein spo-11
Sequence:
MFENTKKALETFRTAIECVKCKKPRGDLQYLGSSCKHAYCWECIATFQQKPSGKRSSVARHMCPSCAFPLDTSKITEAHMLKTCFDTLSELNDLLQKVGTTSLTQAEFACTQNIFNKEKTPADAVEKFLETQAHMPDEMGQLGEEDDDLMCKDENRENSNSPELDIFHDYSKEASPTRNSTKRPSTVSVHERKPKRSSILKTSVKNEPAAPVVDLFASQVPQRTHQNDLLTPFIERRSTAPAATGVATYAQAFGSSSNPVKAEIIEEDIFSKAIPLTKRQASMSASAKKQPKLEPEEPEEVPSTSRSRKNSIKSDKIERRSQSPMSFGEKSMSVKSEQRRSSYGTRRGEAVLVNSIRNNRIPQLRSAVEAGTCVNEKEDGKTPLYVAVENSSLEAVKILVEAGAVINASCGSTLETTLHEAVRRQNTQIVEYLLSKGASIKIRNIAGKTVEEMAKSDPKIRKIIEKFKTEQRVLQPVVAPPKSRLHFVQLIDEKMLTESEKRKLPGKINIVPADMDSPTHVVVTVDLKTRVLNINKEHIGEILKAIIKSGMIVSRDWLRACIIDPSKVDDDRSYMVQKVRWMEGEVFENTIEQWKKTITKMQPKLFAGCKFFIPKPKYNFLDRPALFEIIRSAGGQAAAREPIIDEKDPPPYHNANLKPNFVLYSLTHDIGDKFRDCTKYNLVSEQWLIEAILGCSITTPPH
Protein: tRNA (guanine(10)-N2)-dimethyltransferase (EC 2.1.1.213) ((Pab)Trm-G10) (tRNA:G10 dimethyltransferase) (Q9UY84)
Organism: Pyrococcus abyssi (strain GE5 / Orsay)
Function: Catalyzes the adenosylmethionine-dependent methylation of the exocyclic amino group (N(2)) of guanosine at position 10 of various tRNAs. Acts via a two-step process that leads to the formation of either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- CDP-archaeol synthase
- RecJ-like phosphoesterase, containing RNA binding S1 and OB-fold nucleic acid binding domain
- Methyltransferase
- tRNA
- tRNA
Sequence:
MFYVEILGLLPEMAEAEVKALAELRNGTIKERDYLLVVGNVENVEIFERLGLAHEYGILLGSGDDVRDILDLVRGLEWKEIIKGTFAVRKEVMVNCAHEVKNLEKIIGGIIHSQGLRVNLSKPDTIIKVYCGRKLWIGIRIREFRGKEFDERKADRRPFSRPIALPPRIARAMVNLTRATREILDPFMGTGGMLIEAGLMGLKVYGIDIREDMVEGAKINLEYYGVKDYVVKVGDATKIKEAFPGKTFEAIATDPPYGTSTTLPMDRDELYKRALESMYSVLEGRLAIAFPSDFDALDVAETIGFKVIGRFYQRVHSSLSRYFYIMEAR
Protein: Proteasome subunit beta type-3 (20S proteasome subunit beta-3) (Q9XYN7)
Organism: Drosophila melanogaster (Fruit fly)
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.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-1
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-3
- Proteasome subunit alpha type-4
- Proteasome subunit beta
- Proteasome subunit beta
- Proteasome subunit beta type-1
- Proteasome subunit beta
- Proteasome subunit beta type-4
Sequence:
MSILAYNGGCVVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPKPFSAMMSSFLYEHRFGPYFIEPVVAGLDPKTMEPFICNMDLIGCPNAPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFEVIAQSIVNAFDRDAMSGWGATVYIIEKDKITERTLKTRMD
Protein: Interleukin-1 (E9LHC8)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Lysosome {ECO:0000256|ARBA:ARBA00004371}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
Sequence:
MAFVPDLDVLESSSLSEETFYGPSCLCLQKKPRLDSEHTTVDEQVTVRKGRGARSFRRAAVLVVAMTKLLRRPRSRDFADSDLSALLEEVFEPVTFQRLESSYAGAPAFRYTRSQSFDIFDINQKCFVLESPTQLVALHLQGPSSSQKVRLNIALYRPRGPRGSAGTGQMPVALGIKGYKLYMSCVMSGTEPTLQLEEADVMRDIDSVELTRFIFYRLDSPTEGTTRFESAAFPGWFICTSLQPRQPVGITNQPDQVNIATYKLSGR
Protein: Small ribosomal subunit protein uS19B (40S ribosomal protein S15-B) (Q9UTQ6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q01855}. Nucleus {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS3
- Elongation factor 3
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS28A
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS28B
- mRNA export factor elf1
Sequence:
MAEENHDEAVRVAELRKKRTFRTFAYRGVELEQLLDLSAEQLVDLFHARARRRMLRGLGPNASRFIRKLRKAKSEAPLNEKPATVKTHLRNMIILPEMVGSVVGIYNGKLFNQVEIRPEMIGHYLGEFSITYKPTKHGRPGIGATHSSRFIPLK
Protein: Transcription factor SOX-1 (P53783)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator. May function as a switch in neuronal development. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Paired box protein Pax-6
- Nestin
- POU domain, class 5, transcription factor 1
- Tubulin beta-3 chain
- Homeobox protein NANOG
- Homeobox protein OTX2
- Hepatocyte nuclear factor 3-beta
Sequence:
MYSMMMETDLHSPGGAQAPTNLSGPAGAGGGGGGGGGGGGGGGTKANQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLAAGAGGGGAAVAMGVGVGVGAAAVGQRLESPGGAAGGGYAHVNGWANGAYPGSVAAAAAAAAMMQEAQLAYGQHPGAGGAHPHAHPAHPHPHHPHAHPHNPQPMHRYDMGALQYSPISNSQGYMSASPSGYGGIPYGAAAAAAAAAGGAHQNSAVAAAAAAAAASSGALGALGSLVKSEPSGSPPAPAHSRAPCPGDLREMISMYLPAGEGGDPAAAAAAAAQSRLHSLPQHYQGAGAGVNGTVPLTHI