wanglab/gogpt-training-data huggingface dataset:
Protein: 28 kDa heat/acid-stable phosphoprotein-like protein (Q9FNM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transmembrane protein
- Plasma membrane fusion protein
- Large ribosomal subunit protein P2z
- Prefoldin subunit 6
- Ureide permease 5
- High mobility group B protein 5
- Probable serine/threonine-protein kinase PIX13
- Myosin-1
- COX assembly mitochondrial protein
- Ribosomal protein L18e/L15 superfamily protein
Sequence:
MGRGKFKGKPTGQRRFSSAADILAGTSAARPRSFKQKEAEYEEDVEEESEEESEEESEDEADVKKKGAEAVIEVDNPNRVRQKTLKAKDLDASKTTELSRREREELEKQRAHERYMRLQEQGKTEQARKDLDRLALIRQQREEAAKKREEEKAARDAKKVEGRK
Protein: GAF domain-containing protein (Q57VD8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTESVGASTPTGGRSDKVTFYSRLVKEVQGIVEFPSKRLAPAANAIINLSNVAASLFYGLNRHANPEAVLQSPPVNWLGFYLMHGPELLALGPFQGRPACTEIKMGRGVCGTAAQQAKTLVVSDVHEFPGHIACDSASNSEIVVPIKSAAGEVVGIIDVDSTQLNFFDDVDAQGLQEVAEIVARHVDFSVFHQFCTQMPLAGTGPSAPEKPTANVGAGSETQPSVLPSNDGTDKNIKDKVCLTGSAVAALCASGLAAKAVTLPPSCKLSAATIMPLSNHAVQGQREASLEEGRPLVQASPRRWSVDISGWEFEGTDFTRILTQEELKQYEEELGIGSIPELQFPFNTLHITPVARHGKVPLLSFSLKDLLRAAAAYYKTESYRETTVPQLVIPVSETWKRTPYAVFDAKVDWAWRNDFFGFDKSSCTLKPLEPTMPGLNWDLLRDRTLPILFFHNFDMLEDDLHDHGVVKSSVRIRAMPTAFFILHRHFIRIDHYRIWIRDVRIFHQYEVRRENGEPHIVVREEVRLLDINNDVQWSEKDSDECAQLAKLESEQEYYVSFDRDSAGRGWWNTINTS
Protein: NFKB inhibitor epsilon (Q6P780)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Transcription factor p65
- Nuclear factor NF-kappa-B p105 subunit
- NF-kappa-B inhibitor beta
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- NF-kappa-B inhibitor alpha
- REL proto-oncogene, NF-kB subunit
- NF-kappa-B essential modulator
- Transcription factor RelB
- 26S proteasome non-ATPase regulatory subunit 10
Sequence:
MSDARKGPDEADDSQCDSGIESLRSLRSLPDPAAAPVSGSSHSGCPQPWSHAPKTDKEPEGKEDADGERADSTYASSSLTESLPLLERPEAKDPNPPTPSSPVSPAGVLSPQQLEALTYISEDGDTLLHLAVIHEAPSVLFCCLAFLPQEVLDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACQRQNLACACCLLEEQPEPGRQPSHPLDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDAQEGTSGKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGADSLLLNVEDETPQDLAEDLLSYLPFDDLKISGKPLLCTD
Protein: Cyclic nucleotide-gated channel beta-1 (CNG channel beta-1) (Cyclic nucleotide-gated cation channel 4) (CNG channel 4) (CNG-4) (CNG4) (Cyclic nucleotide-gated cation channel gamma) (Cyclic nucleotide-gated cation channel modulatory subunit) (Glutamic acid-rich protein) (GARP) (Q14028)
Organism: Homo sapiens (Human)
Function: Subunit of cyclic nucleotide-gated (CNG) channels, nonselective cation channels, which play important roles in both visual and olfactory signal transduction. When associated with CNGA1, it is involved in the regulation of ion flow into the rod photoreceptor outer segment (ROS), in response to light-induced alteration of the levels of intracellular cGMP.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:A0A8I5ZN27}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:A0A8I5ZN27, ECO:0000250|UniProtKB:E1AZ71}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic nucleotide-gated channel alpha-4
- Cyclic nucleotide-gated channel alpha-1
- Cyclic nucleotide-gated channel alpha-2
- Calmodulin-1
- Calmodulin-like protein 4
- Calmodulin-like protein 6
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
Sequence:
MLGWVQRVLPQPPGTPRKTKMQEEEEVEPEPEMEAEVEPEPNPEEAETESESMPPEESFKEEEVAVADPSPQETKEAALTSTISLRAQGAEISEMNSPSRRVLTWLMKGVEKVIPQPVHSITEDPAQILGHGSTGDTGCTDEPNEALEAQDTRPGLRLLLWLEQNLERVLPQPPKSSEVWRDEPAVATGAASDPAPPGRPQEMGPKLQARETPSLPTPIPLQPKEEPKEAPAPEPQPGSQAQTSSLPPTRDPARLVAWVLHRLEMALPQPVLHGKIGEQEPDSPGICDVQTISILPGGQVEPDLVLEEVEPPWEDAHQDVSTSPQGTEVVPAYEEENKAVEKMPRELSRIEEEKEDEEEEEEEEEEEEEEEVTEVLLDSCVVSQVGVGQSEEDGTRPQSTSDQKLWEEVGEEAKKEAEEKAKEEAEEVAEEEAEKEPQDWAETKEEPEAEAEAASSGVPATKQHPEVQVEDTDADSCPLMAEENPPSTVLPPPSPAKSDTLIVPSSASGTHRKKLPSEDDEAEELKALSPAESPVVAWSDPTTPKDTDGQDRAASTASTNSAIINDRLQELVKLFKERTEKVKEKLIDPDVTSDEESPKPSPAKKAPEPAPDTKPAEAEPVEEEHYCDMLCCKFKHRPWKKYQFPQSIDPLTNLMYVLWLFFVVMAWNWNCWLIPVRWAFPYQTPDNIHHWLLMDYLCDLIYFLDITVFQTRLQFVRGGDIITDKKDMRNNYLKSRRFKMDLLSLLPLDFLYLKVGVNPLLRLPRCLKYMAFFEFNSRLESILSKAYVYRVIRTTAYLLYSLHLNSCLYYWASAYQGLGSTHWVYDGVGNSYIRCYYFAVKTLITIGGLPDPKTLFEIVFQLLNYFTGVFAFSVMIGQMRDVVGAATAGQTYYRSCMDSTVKYMNFYKIPKSVQNRVKTWYEYTWHSQGMLDESELMVQLPDKMRLDLAIDVNYNIVSKVALFQGCDRQMIFDMLKRLRSVVYLPNDYVCKKGEIGREMYIIQAGQVQVLGGPDGKSVLVTLKAGSVFGEISLLAVGGGNRRTANVVAHGFTNLFILDKKDLNEILVHYPESQKLLRKKARRMLRSNNKPKEEKSVLILPPRAGTPKLFNAALAMTGKMGGKGAKGGKLAHLRARLKELAALEAAAKQQELVEQAKSSQDVKGEEGSAAPDQHTHPKEAATDPPAPRTPPEPPGSPPSSPPPASLGRPEGEEEGPAEPEEHSVRICMSPGPEPGEQILSVKMPEEREEKAE
Protein: Peptidoglycan amidase Tse1 (EC 3.4.19.11) (Type VI secretion exported 1) (Q9I2Q1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Toxin secreted by the H1 type VI (H1-T6SS) secretion system into the periplasm of recipient cells. Degrades peptidoglycan via amidase activity thereby helping itself to compete with other bacteria. To protect itself, the bacterium synthesizes immunity protein Tsi1 that specifically interacts with and inactivates cognate toxin.
Subcellular location: Host membrane {ECO:0000269|PubMed:21776080}. Secreted {ECO:0000269|PubMed:21776080}. Note=Delivered to the target cell periplasm by the H1 type VI (H1-T6SS) secretion system. {ECO:0000269|PubMed:21776080}.
Interaction partners:
- Immune protein Tsi1
- Type VI secretion system spike protein VgrG1a
- Toxin Tse2
- Immune protein Tsi2
- Protein hcp1
- Toxin protein Tse5
- AAA+ ATPase ClpV1
- Immune protein Tsi3
- NAD
- Peptidoglycan muramidase Tse3
Sequence:
MDSLDQCIVNACKNSWDKSYLAGTPNKDNCSGFVQSVAAELGVPMPRGNANAMVDGLEQSWTKLASGAEAAQKAAQGFLVIAGLKGRTYGHVAVVISGPLYRQKYPMCWCGSIAGAVGQSQGLKSVGQVWNRTDRDRLNYYVYSLASCSLPRAS
Protein: Surfeit locus protein 4 (O15260)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum cargo receptor that mediates the export of lipoproteins by recruiting cargos into COPII vesicles to facilitate their secretion. Acts as a cargo receptor for lipoproteins bearing both APOB and APOA1, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis. Synergizes with the GTPase SAR1B to mediate transport of circulating lipoproteins. Promotes the secretion of PCSK9. Also mediates the efficient secretion of erythropoietin (EPO). May also play a role in the maintenance of the architecture of the endoplasmic reticulum-Golgi intermediate compartment and of the Golgi.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15308636, ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:30251625, ECO:0000269|PubMed:33186557}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:18287528}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:30251625, ECO:0000269|PubMed:33186557}; Multi-pass membrane protein {ECO:0000255}. Note=Active at endoplasmic reticulum exit sites (ERES) where it is incorporated together with its lipoprotein cargos into COPII-coated vesicles. From the Golgi it is recycled back to the endoplasmic reticulum. {ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:33186557}.
Interaction partners:
- Surfeit locus protein 2
- Golgi SNAP receptor complex member 1
- Protein ERGIC-53
- Endoplasmic reticulum-Golgi intermediate compartment protein 1
- Surfeit locus protein 1
- ER lumen protein-retaining receptor 1
- Transmembrane emp24 domain-containing protein 2
- Transmembrane emp24 domain-containing protein 10
- Transmembrane emp24 domain-containing protein 9
- Coatomer subunit alpha
Sequence:
MGQNDLMGTAEDFADQFLRVTKQYLPHVARLCLISTFLEDGIRMWFQWSEQRDYIDTTWNCGYLLASSFVFLNLLGQLTGCVLVLSRNFVQYACFGLFGIIALQTIAYSILWDLKFLMRNLALGGGLLLLLAESRSEGKSMFAGVPTMRESSPKQYMQLGGRVLLVLMFMTLLHFDASFFSIVQNIVGTALMILVAIGFKTKLAALTLVVWLFAINVYFNAFWTIPVYKPMHDFLKYDFFQTMSVIGGLLLVVALGPGGVSMDEKKKEW
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8I639)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MDKSSIANKIEAYLGAKSDDSKIDQSLKADPSEVQYYGSGGDGYYLRKNICKITVNHSDSGTNDPCDRIPPPYGDNDQWKCAIILSKVSEKPENVFVPPRRQRMCINNLEKLNVDKIRDKHAFLADVLLTARNEGERIVQNHPDTNSSNVCNALERSFADIADIIRGTDLWKGTNSNLEQNLKQMFAKIRENDKVLQDKYPKDQNYRKLREDWWNANRQKVWEVITCGARSNDLLIKRGWRTSGKSNGDNKLELCRKCGHYEEKVPTKLDYVPQFLRWLTEWIEDFYREKQNLIDDMERHREECTSEDHKSKEGTSYCSTCKDKCKKYCECVKKWKSEWENQKNKYTELYQQNKNETSQKNTSRYDDYVKDFFKKLEANYSSLENYIKGDPYFAEYATKLSFILNSSDANNPSEKIQKNNDEVCNCNESGIASVEQEQISDPSSNKTCITHSSIKANKKKVCKHVKLGVRENDKDLRVCVIEHTSLSGVENCCCQDFLRILQENCSDNKSGSSSNGSCNNKNQEACEKNLEKVLASLTNCYKCDKCKSEQSKKNNKNWIWKKSSGKEGGLQKEYANTIGLPPRTQSLCLVVCLDEKGKKTQELKNIRTNSELLKEWIIAAFHEGKNLKPSHEKKNDDNGKKLCKALEYSFADYGDLIKGTSIWDNEYTKDLELNLQKIFGKLFRKYIKKNNTAEQDTSYSSLDELRESWWNTNKKYIWLAMKHGAGMNSTTCCGDGSVTGSGSSCDDIPTIDLIPQYLRFLQEWVEHFCKQRQEKVKPVIENCKSCKESGGTCNGECKTECKNKCEVYKKFIEDCKGGDGTAGSSWVKRWDQIYKRYSKYIEDAKRNRKAGTKNCGPSSTTNAAENKCVQSDIDSFFKHLIDIGLTTPSSYLSIVLDDNICGADKAPWTTYTTYTTTEKCNKETDKSKLQQCNTAVVVNVPSPLGNTPHGYKYACQCKIPTNEETCDDRKEYMNQWSCGSARTMKRGYKNDNYELCKYNGVDVKPTTVRSNSSKLDDKDVTFFNLFEQWNKEIQYQIEQYMTNTKISCNNEKNVLSRVSDEAAQPKFSDNERDRNSITHEDKNCKEKCKCYSLWIEKINDQWDKQKDNYNKFQRKQIYDANKGSQNKKVVSLSNFLFFSCWEEYIQKYFNGDWSKIKNIGSDTFEFLIKKCGNDSGDGETIFSEKLNNAEKKCKENESTNNKMKSSETSCDCSEPIYIRGCQPKIYDGKIFPGKGGEKQWICKDTIIHGDTNGACIPPRTQNLCVGELWDKRYGGRSNIKNDTKESLKQKIKNAIQKETELLYEYHDKGTAIISRNPMKGQKEKEEKNNDSNGLPKGFCHAVQRSFIDYKNMILGTSVNIYEYIGKLQEDIKKIIEKGTTKQNGKTVGSGAENVNAWWKGIEGEMWDAVRCAITKINKKQKKNGTFSIDECGIFPPTGNDEDQSVSWFKEWSEQFCIERLQYEKNIRDACTNNGQGDKIQGDCKRKCEEYKKYISEKKQEWDKQKTKYENKYVGKSASDLLKENYPECISANFDFIFNDNIEYKTYYPYGDYSSICSCEQVKYYEYNNAEKKNNKSLCHEKGNDRTWSKKYIKKLENGRTLEGVYVPPRRQQLCLYELFPIIIKNKNDITNAKKELLETLQIVAEREAYYLWKQYHAHNDTTYLAHKKACCAIRGSFYDLEDIIKGNDLVHDEYTKYIDSKLNEIFDSSNKNDIETKRARTDWWENEAIAVPNITGANKSDPKTIRQLVWDAMQSGVRKAIDEEKEKKKPNENFPPCMGVQHIGIAKPQFIRWLEEWTNEFCEKYTKYFEDMKSNCNLRKGADDCDDNSNIECKKACANYTNWLNPKRIEWNGMSNYYNKIYRKSNKESEDGKDYSMIMEPTVIDYLNKRCNGEINGNYICCSCKNIGENSTSGTVNKKLQKKETQCEDNKGPLDLMNKVLNKMDPKYSEHKMKCTEVYLEHVEEQLKEIDNAIKDYKLYPLDRCFDDKSKMKVCDLIGDAIGCKHKTKLDELDEWNDVDMRDPYNKYKGVLIPPRRRQLCFSRIVRGPANLRNLKEFKEEILKGAQSEGKFLGNYYNEDKDKEKALEAMKNSFYDYEYIIKGSDMLTNIQFKDIKRKLDRLLEKETNNTEKVDDWWETNKKSIWNAMLCGYKKSGNKIIDPSWCTIPTTETPPQFLRWIKEWGTNVCIQKEEHKEYVKSKCSNVTNLGAQESESKNCTSEIKKYQEWSRKRSIQWEAISEGYKKYKGMDEFKNTFKNIKEPDANEPNANEYLKKHCSKCPCGFNDMQEITKYTNIGNEAFKQIKEQVDIPAELEDVIYRLKHHEYDKGNDYICNKYKNINVNMKKNNDDTWTDLVKNSSDINKGVLLPPRRKNLFLKIDESDICKYKRDPKLFKDFIYSSAISEVERLKKVYGEAKTKVVHAMKYSFADIGSIIKGDDMMENNSSDKIGKILGDGVGQNEKRKKWWDMNKYHIWESMLCGYKHAYGNISENDRKMLDIPNNDDEHQFLRWFQEWTENFCTKRNELYENMVTACNSAKCNTSNGSVDKKECTEACKNYSNFILIKKKEYQSLNSQYDMNYKETKAEKKESPEYFKDKCNGECSCLSEYFKDETRWKNPYETLDDTEVKNNCMCKPPPPASNNTSDILQKTIPFGIALALGSIAFLFMKKKPKTPVDLLRVLDIPKGDYGIPTPKSSNRYIPYASDRYKGKTYIYMEGDTSGDDDKYIWDLSSSDITSSESEYEEVDINDIYVPSFPKYKTFIELVLEPSKRDTFNTSSGDTFTNKLTDDEWNQLKQDFIEQYLQNIQKDFILHDSMDEKPFITQIQDRFLDSSHEEVTYNIDWNVPENINRITNNMDDPKYCSNNMYTGTDLINDSLNGNQYIDIYDEMLKRKENELFGTYHTKYTTFNSVSKQTPSDPIINQLDLYHKWIDKHRDICEQWKTKEDMLYKLNEVWNMERKEYLLDIQPSTLDDIHKINDETYNIISTNNIYDHPSQETPLQLLGSTNIIPSYITTEQNNGLRTNISMDTYIDETNNNNVVATSIIGDDQMENSYNC
Protein: Acyl-coenzyme A thioesterase MBLAC2 (Acyl-CoA thioesterase MBLAC2) (EC 3.1.2.2) (Beta-lactamase MBLAC2) (EC 3.5.2.6) (Metallo-beta-lactamase domain-containing protein 2) (Palmitoyl-coenzyme A thioesterase MBLAC2) (Q68D91)
Organism: Homo sapiens (Human)
Function: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Has an acyl-CoA thioesterase activity towards the long chain fatty acyl-CoA thioester palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA). Displays a substrate preference for fatty acyl-CoAs with chain-lengths C12-C18. Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin. Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:33219126}; Lipid-anchor {ECO:0000269|PubMed:33219126}. Cell membrane {ECO:0000269|PubMed:33219126}; Lipid-anchor {ECO:0000269|PubMed:33219126}.
Interaction partners:
Sequence:
MSALEWYAHKSLGDGIFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLQDREAKEDAARRPLLAVATHVHFDHSGGLYQFDRVAVHHAEAEALARGDNFETVTWLSDSEVVRTPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDRGLVEKVLPGHFNTFGAERLFRLASNYISKAGICHKVSTFAMRSLASLALRVTNSRTSP
Protein: Queuine tRNA-ribosyltransferase catalytic subunit 1 (EC 2.4.2.64) (Guanine insertion enzyme) (tRNA-guanine transglycosylase) (Q4QR99)
Organism: Rattus norvegicus (Rat)
Function: Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03218}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03218}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03218}. Note=Weakly associates with mitochondria, possibly via QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218}.
Interaction partners:
- Queuine tRNA-ribosyltransferase accessory subunit 2
- Protein N-terminal glutamine amidohydrolase
- Glutaryl-CoA dehydrogenase, mitochondrial
- tRNA
Sequence:
MAAVGSPGSLESAPRIMRLVAECSRSRARAGELRLPHGTVATPVFMPVGTQATMKGITAEQLDSLGCRICLGNTYHLGLRPGPELIQKAHGLHGFMNWPHNLLTDSGGFQMVSLISLSEVTEEGVRFRSPYDGEETLLSPERSVEIQNALGSDIIMQLDDVVSSTVTGPRVEEAMHRSVRWLDRCIAAHKRQDKQNLFAIIQGGLNADLRTTCLKEMTKRDVPGFAIGGLSGGESKEQFWKMVALSTSMLPKDKPRYLMGVGYATDLVVCVALGCDMFDCVYPTRTARFGSALVPTGNLQLKKQQYAKDFSPINPECPCATCQTHSRAFLHTLLHSDNTAALHHLTVHNIAYQLQLLSAARSSILEQRFPDFVRNFMRTMYGDHSLCPAWAIEALASVGITLT
Protein: Succinate dehydrogenase assembly factor 4, mitochondrial (Q8LCR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Succinate dehydrogenase assembly factor 2, mitochondrial
- AT1G25275 protein
- Transmembrane protein
- At4g33960
- At3g13845
- AT4g21620/F17L22_80
- AT4g05070 protein
- Protein RALF-like 33
- Protein RALF-like 24
- Protein RALF-like 32
Sequence:
MATNNIVRLIAPSRSVSSRFLEPVSRFLSSGTPPPPQAPSPNQDLNRDVKPDQNLQQNLQMQKEEEEEGEGGGGGEFVNEDTGEIGGPRGPEPTRYGDWEQRGRCSDF
Protein: Centromeric protein-C, isoform A (FI18815p1) (Q9VHP9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Chromosome alignment defect 1
- Spc105-related, isoform B
- Histone H3-like centromeric protein cid
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Centrocortin, isoform A
- CG1558-RA protein
- Nuf2
- Nnf1a
- Mis12
- Kinetochore protein NDC80
Sequence:
MSKPQNNDTLELDDILSQPVKDKERFAAFMMRKLAENKPAQNDNLFGNFKLDFDLDFEVPLIKKSQAKPKSKLPEVQPLGELVSKNSAATEKVNEPPVDQAPNENVPPRRSPTLSPNNRRSMRRSGNVPGSDKLRRHAIRRRSRSCGRQLLPEFEETVNLTRSISSPVNFLPEISSTPCTEKQKEEVAKNTTRVETDKPAEKPMELSQEPEPENPLQTKVTSPARNPILAAEIEQICKERQSSFHKNVLQLDYSGRAPYSRPPTPSSPSVAGLRRTYTMEKGPAPGQLLLSPSHRYDTPSKMPVVKAKRFNQELMVPDTPERQSHDPAWQSEPQPEFVVPETQPQDLGELVQTLSRSAISPIVVINTSNSNRSVRRDAVAMKSVPTSPVTALSSPPIAPSPRRSAAASPQKSIAQLPRVEENMDAIMTDDESDEHPSTVPLNLAPSGGNTTRQRRLRSSNRARATIESQESSMRLLNLHKSVNAKKSKPRKTAIPLNKAPSAPINGEQFARELTRMSNYEILDLRKRNSLNEIYPLNGHRNHRSEKLILEEEIQRELLRRNLMDEAEGLPKQQSSDDSNEDYIPVPPKTQSLRTKSNDRSQGRGRPRSTRRDLPMTTELVNYLGLSQTLETRRKSSKDGKRCLYTKGSSDHEDNDSLSPVKLPRLSKSIQIVPPPPVSLRYSQSLQNLPCSGKFDFDNVVMAAPPDFHDSVNSDAIEIAPPPPEYVVNTRGRSTSGRKSNKNDLVLPPPGYEGGQEEEHDERPSQPRCTAKELQQSTQNGRRAMENELVPPPIEYVEEENRNNEQSRRSTKNGNLVDRNTHNAVEYCEPPEPPEYDDSDHGQASILRRSGKKLQHSKQSVQKSNKEQIIAPSYENNEDYDSDEEPIYNEEYGKEESQNKNVTRRKSDKDEMASHTLECIEGPDPNWNSSCNKQNRNHQNASKSKENDKLANRSSKSQKLSNPRQNAVGTEKSVALSNRGEECTEKSSDVMESLRVNTPTPPIDQNSDDVPSRNPSPSRTLLSDDVPSTSRAALEFLQRSQNMSKSRPPDESSADVVFKKPLAPAPRAKSKKGKSEVDKLKLAKMPVEAEELNTTGIRRSKRGQVPLQMSWCHTMDPSKFNFMSGFIEPRSKNSKTKKGNLSKAKKASATKPKPTVEKNLPDNRGPLCSSTPRISEKLPGAIPHSESLGLSTLTWEETEVQAEAEKVPKKRGRPKKAVGGVQTDTEAEPEPEPEPMISSVAPLTSDQEEPDVPDEQAPYTEAALGPVVFSTPLRDEQEEASTKLMQWLRGVGDAPPSASMSDENASVSSANELIFCQVDGIDYAFYNTKEKAMLGYMRFKPYQKRSMKQAKVHPLKLLVQFGEFNVETLAVGEEKEVHSVLRVGDMIEIDRGTRYSIQNAIDKVSVLMCIRS
Protein: Ankyrin repeat domain-containing protein 20A1 (Q5TYW2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKLFGFGSRRGQTAQGSIDHVYTGSGYRIRDSELQKIHRAAVKGDAAEVERCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAVDRLRRSALMLAVYYDSPGIVNILLKQNIDVFAQDMCGRDAEDYAISHHLTKIQQQILEHKKKILKKEKSDVGSSDESAVSIFHELRVDSLPASDDKDLNVATKQCVPEKVSEPLPGSSHEKGNRIVNGQGEGPPAKHPSLKPSTEVEDPAVKGAVQRKNVQTLRAEQALPVASEEEQERHERSEKKQPQVKEGNNTNKSEKIQLSENICDSTSSAAAGRLTQQRKIGKTYPQQFPKKLKEEHDRCTLKQENEEKTNVNMLYKKNREELERKEKQYKKEVEAKQLEPTVQSLEMKSKTARNTPNWDFHNHEEMKGLMDENCILKADIAILRQEICTMKNDNLEKENKYLKDIKIVKETNAALEKYIKLNEEMITETAFRYQQELNDLKAENTRLNAELLKEKESKKRLEADIESYQSRLAAAISKHSESVKTERNLKLALERTRDVSVQVEMSSAISKVKAENEFLTEQLSETQIKFNALKDKFRKTRDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVNNSTGKWNCVEERICHLQRENAWLVQQLDDVHQKEDHKEIVTNIQRGFIESGKKDLVLEEKSKKLMNECDHLKESLFQYEREKTEGVVSIKEDKYFQTSRKTI
Protein: Ubiquitin-conjugating enzyme E2 C (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme C) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme C) (Ubiquitin carrier protein C) (Ubiquitin carrier protein vihar) (Ubiquitin-protein ligase C) (Q9VTY6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15458643}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15458643}. Note=Localizes in the cytoplasm of mitotic cells but also associates with centrosomes, and its own degradation is initiated at the metaphase-anaphase transition.
Interaction partners:
- Cell division cycle protein 27 homolog
- Cell division cycle 16
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 2
- G2/mitotic-specific cyclin-A
- Anaphase-promoting complex subunit 10
- Cyclosome subunit 8
- E1 ubiquitin-activating enzyme
Sequence:
MAQNISPEQSGGAGGGGSKHSDDSMPVKDNHAVSKRLHKELMNLMMANERGISAFPDGENIFKWVGTIAGPRNTVYSGQTYRLSLDFPNSYPYAAPVVKFLTSCFHPNVDLQGAICLDILKDKWSALYDVRTILLSIQSLLGEPNNESPLNAQAAMMWNDQKEYKKYLDAFYEKHKDT
Protein: Polymerase nucleotidyl transferase domain-containing protein (Q38EI4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSFDSKPGCNELEGELHDSPIDPQDSSGACVSLHERQIQHWSPLETPSSPSDHLEGAESVRAHGDLFFPLDEYLSSEVVLVPSRHVSQCGSSSADVVASAAACVSVVHEDFSESTEHINIAQTDNACENSSGSDVCTQLKDEEMAQANSPPQLCATVLPVACVLDEISADSPCTLNSVPITRGGFIEDNTTAGVGTGVSEDTESSNTVERRDLDHGIEEPTAKSAKRSVGPAKDSESSLNGIRPPRKVARGRAAETTKTQQVPQRARTAAPPTSSTLPHERILDDPQHGRWPSASGISSIDHAVTSETSCRTNKGKSNDGSRKQSSRVGPKSNNNNNGSASELGKGSNSLDGGVSGDKSGPARPATPHRSRRHKARQQQQVEETFGPFGFPFQRNMMLDSMPDGAQRVAEHTAMMLAQKQQLLYPVPLQGDASKMIDVSGGTPHWSMLPSYYFVSSLQIYVDTCLGLRGGDRQERHEFVSRIQRITTKVLGPRARLRMHGSITTDLALASSDIDILVVDYEPLAPLQAIQQLSKAIQSISGEELEGLSLEPAEGCSLETEVMHQPGNNSSLRESTGVVSVDNNVVDTTGSGVEENLLAMAVEPPESDCILRVEEEEAEYRLQIERDYALSTRVGPNAAAVALHSCIPSFTSAPLPPLPPLGRRRLYVPTVDGPLYQVQTIISTRVPVIKVTEKMTGLRCDISFAGGEHWRSMQLTNRLLKRYPTSRGLILFLKHCVRQMGIGDSQPGDMTSFAIYLLVHHFFNEISKHLEETLREQIRRQQQVGDGAQPCVQNPCELDPRNPTGGRSSPCVPSLRVQVSPSAHHGSGTTSPADQKPSSPDDRFPVVTGMLLGQFLSRQQQHSNQQGGNSRLSTEGILKSFILSMESEEVRGGARGVDEAQLPTKSGSPPNQVAEALDEWQQQQQQHTDVTEAPVVTVPGSVVSQSLDESAVDTAAVDDFDGRDIVCCDDVVDESAAGGPTCPNPMVECGSFSASGAVEDGDVNAKHPSEEVEDGESVGEGERNAETPDEDAERKVGTESQAESVEEDDLVRCTVHRLLTTSPLGHLFNDFCYYYGFVFNYDTQGLRFGPDGSSLVVPKPQQCQQRGQHLYMTSPFDVQYDITAHMMHTRAFQELCCMFVPLTNPLPLLTGDGSNVCTLRQVLEWISPDTAHKELIEVHNAVQMQQLHHGEVQQVPQVNPQLALENDRCTLFPSSRGRLSSGIEERSTSPSQLNFPDDGNELSSGGRSLRPRDQSHGRKGGKNANASSGLRDVNDGSAGSTGSSRGGKGLPANGTYVSDATKGRSGQPVGWRQGKRSEGDSEDVGAETRTAAVSATSPASEVSSAMDAEVSVVSPSPFPNAPLASGSKMVKGAPAMGDVNAGNCDPTYVPTNPTHANVLPGQQPMNFVADPSLSMFMFPPGGVNSPYPGMPQYYHPMPYTTEAQLHFRPDAYQQHPMAPFVYQGYDMNQMFPHRVMGDTTNDSVVNATSTVVTGKRQSSAYGSSTHSNTQSSARSGVSGNFLSRGRGRSSHRGSGSNNNGGEKASQYKAGHSDALEEQAPTPVVSSPSLTAEPLGTATFGGLTSSGINRDSMTTIAVGTVPGKEHQQQPLQSYVGDPKEWLKPETPTQGIEFHHYSHQTHRQASYPHHQQSSAPQHYHHHIQSSPKMRSNTQQQAQGHWRHQRCTMMMVPSPMYSIMSGMEGTATTSLCSPAQAGSPFQKQAAGGGSVFSSASQGATSPSGFSMSSALGMPDCGKVGNVVTDNHQQHSYHHHHHHFIHHNVHIQQRWPQPLGQQQRAEGTTTNTNTAAATVTSVGSGNGGKGAGGAPRPVATQSLDGRPEEISLEKIHQQGAGDTNSM
Protein: Autophagy-related protein 9 (H2L0M4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRINALFLRGLHDESIIHSSSRNYGGTTSSFNMHPTAMQSVFAMPDGFGQPAPAVESSLIDIETPTYHRESVQRSAAEHKMEHETPEPLAELPDLPGPSSSEHQQRSRLVPNTQHRQINEEEEEEEEEDNTPPLSFSS
Protein: Tryptophan synthase alpha chain, chloroplastic (EC 4.2.1.20) (Indole-3-glycerol-phosphate lyase, chloroplastic) (EC 4.1.2.8) (Protein TRYPTOPHAN-REQUIRING 3) (Q42529)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Required for tryptophan biosynthesis. Contributes to the tryptophan-independent indole biosynthesis, and possibly to auxin production.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18844775, ECO:0000269|PubMed:7890741}.
Interaction partners:
- Tryptophan synthase beta chain 2, chloroplastic
- Indole-3-glycerol phosphate synthase, chloroplastic
- Tryptophan synthase
- Tryptophan synthase beta chain 1, chloroplastic
- tryptophan synthase
- indole-3-glycerol-phosphate synthase
- Anthranilate phosphoribosyltransferase, chloroplastic
- N-
- N-
- Anthranilate phosphoribosyltransferase
Sequence:
MAIAFKSGVFFLQSPKSQIGFRHSSPPDSSLSFKRFTPMASLSTSSPTLGLADTFTQLKKQGKVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDKVVPQISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIVDASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVKLLGDAKSPTEGLKELEKLTKSLKSALL