wanglab/gogpt-training-data huggingface dataset:
Protein: Runt related A, isoform C (R9PY33)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHLTTTSSNSTASNANNNNNNTANNNNTSSNNNTTNTNGSSNNNTSGNNNNSSGNNSNTEQNTPPTPAQLLNEAYTKMTSDILAERTLGDFLTEHPGELIRTSSPLFVCTVLPPHWRSNKTLPVAFKVVSLGDIMDGTMVTVRAGNDENYCAELRNCTAVMKNQVAKFNDLRFVGRSGRGKSFTLTITVSTNPPHIATYNKAIKVTVDGPREPRSKTMLSLLGQQQQFHFAFGQRPFHFSTDPLSGFRMPPIGNCQSASNTHWGYGSAASAYSPYLASSGLSSCTTPTSAQFNNPALGFTCSSNDQSNNQDFGGATNRDCVPMLPDSTASDLDQHLSSLVGSTSGQMTHHSLLGAGGQTSISSTVNGASGGGSAGAGTAGGGAGSGGGAGGGAGGNSILVPRYHTNASNEYNVHSSQNGPRSLSDSSQAESPVQEDLLTTNTPNLGSTAGGGAANGGAGSNAGSGAAGSGAGGAGGASSAVGNPAMLGANQNFPGIVNQAQHSAASAYGGGTGVVGGGHGSAAAAAAGCNGSLYPVLPASLLYSQLYTAANQSAHGFHSHTLPAHASPNSSVHGELQSVMDHISNVGVRQQHNIMAGGGVTHPGDLTLIGNCGASVRNIEDGNSNRQVAALAAHRGHHNPTDNGGSVWRPY
Protein: At1g62305 (Core-2/I-branching beta-1,6-N-acetylglucosaminyltransferase family protein) (Glycosyltransferase) (Q6DST3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Leucine-rich repeat receptor-like serine/threonine-protein kinase BAM1
- Succinate--CoA ligase subunit alpha-2, mitochondrial
- E3 ubiquitin-protein ligase ORTHRUS 1
Sequence:
MPRLPSSRRGVVWFRWKILITISTALCILALFCINRQSNSTATTTTLSSSLSVARSRIPLVKYSGDRPKLAFLFLARRDLPLDFLWDRFFKSADQRNFSIYVHSIPGFVFDESSTRSHFFYNRQLKNSIEVVWGESSMIAAERLLLASALEDPSNQRFVLLSDSCVPLYDFGYIYRYLVSSPKSFVDSFLDKDNRYTMKMFPVIRKEKWRKGSQWISLIRSHAEVIVNDDTVFPVFQKFCKRSLPLDPRKNWLYLKKRRHNCIPDEHYVQTLLTMRGLENEMERRTVTYTTWNLSAKKAEAKSWHPLTFTSDNCGPEEIEGIKKINHVYYESEYRTEWCRANSKPVPCFLFARKFTRGAAMRLLSEGLIESSIDTTTF
Protein: IST1 homolog (hIST1) (Charged multivesicular body protein 8) (CHMP8) (Putative MAPK-activating protein PM28) (P53990)
Organism: Homo sapiens (Human)
Function: ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation. Is required for efficient abscission during cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing. Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2. Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20719964}. Midbody {ECO:0000269|PubMed:20719964}. Nucleus envelope {ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}. Note=Localizes to centrosome and midbody of dividing cells (PubMed:19129479, PubMed:19129480, PubMed:20719964). Colocalized with SPART to the ends of Flemming bodies during cytokinesis (PubMed:20719964). Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:20719964, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}.
Interaction partners:
- Spastin
- Charged multivesicular body protein 1b
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 5
- Vacuolar protein sorting-associated protein VTA1 homolog
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 6
- Charged multivesicular body protein 3
- Vacuolar protein sorting-associated protein 4A
- Charged multivesicular body protein 2a
Sequence:
MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMAEAPPGVETDLIDVGFTDDVKKGGPGRGGSGGFTAPVGGPDGTVPMPMPMPMPSANTPFSYPLPKGPSDFNGLPMGTYQAFPNIHPPQIPATPPSYESVDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDNFVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
Protein: PTPRF interacting protein alpha 2 (F1M8A4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Peripheral plasma membrane protein CASK
- Receptor-type tyrosine-protein phosphatase F
- Peripheral-type benzodiazepine receptor-associated protein 1
- Protein lin-7 homolog B
- Protein lin-7 homolog A
- PPFIA binding protein 1
- PPFIA binding protein 2
- Regulating synaptic membrane exocytosis protein 2
- Peripheral plasma membrane protein CASK
- Regulating synaptic membrane exocytosis protein 1
Sequence:
EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLDGMEPGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKDRLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLGSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNLARVHPGTSITASVTASSLASSSPPSGHSTPKLTPRSPAREMDRMGVMTLIAVVEEDGREDKATIKCETSPPPTPRAIRMTHTLPSSYHNEARSSLSASLEPDRLGLGSANSSQDSLHKAPKKKGIKSSIGRLFGKKEKARLGQLRGFMETEAAAQESLGLGKLGTQAEKDRRLKKKHELLEEARRKGLPFAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPPTSRTPSGNVWVTHEEMENLAAPAKTCPVFLQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELERRREASQHEIKDVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLLALGTERRLDESDDKNFRRGSTWRRQFPPREVHGISMMPGSSETLPAGFRLTTTSGQSRKMTTDGTVVLHFCL
Protein: U-box domain-containing protein 48 (EC 2.3.2.27) (Plant U-box protein 48) (RING-type E3 ubiquitin transferase PUB48) (Q3E9F5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as an E3 ubiquitin ligase.
Interaction partners:
- DBH-like monooxygenase
- SWAP
- RING/U-box superfamily protein
- Arabidopsis thaliana genomic DNA, chromosome 5, P1 clone:MOK16
- FK506-binding-like protein
- Sulfate/thiosulfate import ATP-binding protein, putative
- RING-H2 finger protein ATL79
- RING-type E3 ubiquitin transferase
- CCT motif family protein
- Ethylene-responsive transcription factor ERF091
Sequence:
MADSTADATETNADTLTLRRELKKVLTENLNDGGVKDRVETVKSIDEAIRILNRLKIVESKKRKRESDSSSVEVPKEFKCTLSKTIMIDPVIIFSGQTYEKRYITEWLNHDLTCPTAKQVLYRVCLTPNHLINELITRWCLANKYDRPAPKPSDIDYVTELFTDGIESLLQRISSPSSSVADQTEAAKELALQTEKFVNVRDFFIKELPDSITRLLTPLSVLGDEVDSNPELQENIVTALFNMSTFEKNKTVLAENHQVIPLLAKSMKQGSVVTRRNATLTLASLSDIDSNKIIIGNSVALKALIDLIGELDDLSATHDALCAVIDLCCDERENWKKAISLGLAPAAIKNIKARRNLFESLAALALISPHERVIQEVANLGVIYDLLSILRKTSCMVTCENAVVIVGNMYAKSRERSIKKILAEEENQHKTFTKIATQGSVVAVMKAQGILQCINY
Protein: DNA repair enzyme (Q8MWS6)
Organism: Toxoplasma gondii
Interaction partners:
Sequence:
MLDSLYGDLPPPSKDEGCPPKPTSLLGSLYDDLDDTPDTSSSSSASSSSSSSSALFASSSWTAERLQMLTPAVVRKQTLKSASGLGAASSQTAGQASSSKPPLDVAAVAAAASAAAAAVAAQLKAVKSEAFGDRARSLFGRGEREKAEALGASDEAASAPGVAGGVKRDESEKGESLRALGRLGVETAEGRRGHQGGDKETESSGFVSIGQMKDEYDPGTPNDYSAIYREKIRKQQREELERLRQQELDKQRRDRELPGSGSSLSGVAFGDSPSTPSPPAAPPAPPVLPSYIDPAKKSFAARMMEKMGWKHGEGLGVNKQGITAPLVAKKTAMSSGVIVQGAEVVQAAAQVWAQFNRPPTRVLLLLNMVGRGEVDEDLKEETEEEAAKFGNLLQVKIVEAAEAPDDEAVRIFCEYERKEEATRAFMTMNGRVFGGRTVKGRFYCEERWGKDDLMPNPEEEADKPLD
Protein: PDF receptor (Pigment-dispersing factor receptor) (Protein groom-of-PDF) (Q9W4Y2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for PDF, a neuropeptide controlling circadian behavioral rhythms. Probably regulates circadian behavioral rhythms through coordination of activities of clock neurons. PDF-binding results in the elevation of cAMP synthesis. Plays a role in sleep regulation and regulates the state transition from sleep to wake.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Protein PDF
- G protein alpha s subunit subunit alpha)
- EG:152A3.5 protein
- Diuretic hormone 44, isoform A
Sequence:
MTLLSNILDCGGCISAQRFTRLLRQSGSSGPSPSAPTAGTFESKSMLEPTSSHSLATGRVPLLHDFDASTTESPGTYVLDGVARVAQLALEPTVMDALPDSDTEQVLGNLNSSAPWNLTLASAAATNFENCSALFVNYTLPQTGLYCNWTWDTLLCWPPTPAGVLARMNCPGGFHGVDTRKFAIRKCELDGRWGSRPNATEVNPPGWTDYGPCYKPEIIRLMQQMGSKDFDAYIDIARRTRTLEIVGLCLSLFALIVSLLIFCTFRSLRNNRTKIHKNLFVAMVLQVIIRLTLYLDQFRRGNKEAATNTSLSVIENTPYLCEASYVLLEYARTAMFMWMFIEGLYLHNMVTVAVFQGSFPLKFFSRLGWCVPILMTTVWARCTVMYMDTSLGECLWNYNLTPYYWILEGPRLAVILLNFCFLVNIIRVLVMKLRQSQASDIEQTRKAVRAAIVLLPLLGITNLLHQLAPLKTATNFAVWSYGTHFLTSFQGFFIALIYCFLNGEVRAVLLKSLATQLSVRGHPEWAPKRASMYSGAYNTAPDTDAVQPAGDPSATGKRISPPNKRLNGRKPSSASIVMIHEPQQRQRLMPRLQNKAREKGKDRVEKTDAEAEPDPTISHIHSKEAGSARSRTRGSKWIMGICFRGQKVLRVPSASSVPPESVVFELSEQ
Protein: Type I restriction enzyme EcoKI methylase subunit (M protein) (EC 2.1.1.72) (Type I methyltransferase M.EcoKI) (M.EcoKI) (P08957)
Organism: Escherichia coli (strain K12)
Function: The subtype gamma methyltransferase (M) subunit of a type I restriction enzyme. The M and S subunits together form a methyltransferase (MTase) that methylates A-2 on the top and A-3 on the bottom strand of the sequence 5'-AACN(6)GTGC-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage.
Interaction partners:
- Type I restriction enzyme EcoKI specificity subunit
- Type I restriction enzyme EcoKI endonuclease subunit
- Type IV methyl-directed restriction enzyme EcoKMrr
- UvrABC system protein B
- Type IV methyl-directed restriction enzyme EcoKMcrB subunit
- DNA adenine methyltransferase YhdJ
Sequence:
MNNNDLVAKLWKLCDNLRDGGVSYQNYVNELASLLFLKMCKETGQEAEYLPEGYRWDDLKSRIGQEQLQFYRKMLVHLGEDDKKLVQAVFHNVSTTITEPKQITALVSNMDSLDWYNGAHGKSRDDFGDMYEGLLQKNANETKSGAGQYFTPRPLIKTIIHLLKPQPREVVQDPAAGTAGFLIEADRYVKSQTNDLDDLDGDTQDFQIHRAFIGLELVPGTRRLALMNCLLHDIEGNLDHGGAIRLGNTLGSDGENLPKAHIVATNPPFGSAAGTNITRTFVHPTSNKQLCFMQHIIETLHPGGRAAVVVPDNVLFEGGKGTDIRRDLMDKCHLHTILRLPTGIFYAQGVKTNVLFFTKGTVANPNQDKNCTDDVWVYDLRTNMPSFGKRTPFTDEHLQPFERVYGEDPHGLSPRTEGEWSFNAEETEVADSEENKNTDQHLATSRWRKFSREWIRTAKSDSLDISWLKDKDSIDADSLPEPDVLAAEAMGELVQALSELDALMRELGASDEADLQRQLLEEAFGGVKE
Protein: Perilipin-1 (Lipid droplet-associated protein) (O60240)
Organism: Homo sapiens (Human)
Function: Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:23399566}. Lipid droplet {ECO:0000269|PubMed:23399566, ECO:0000305|PubMed:26357594}. Note=Lipid droplet surface-associated. {ECO:0000269|PubMed:23399566}.
Interaction partners:
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Hormone-sensitive lipase
- Lipid transferase CIDEC
- Perilipin-4
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit beta
- Lipid transferase CIDEA
- Adiponectin
- Patatin-like phospholipase domain-containing protein 2
Sequence:
MAVNKGLTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYTSTKEAHPLVASVCNAYEKGVQSASSLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKDTISTRLRSARNSISVPIASTSDKVLGAALAGCELAWGVARDTAEFAANTRAGRLASGGADLALGSIEKVVEYLLPPDKEESAPAPGHQQAQKSPKAKPSLLSRVGALTNTLSRYTVQTMARALEQGHTVAMWIPGVVPLSSLAQWGASVAMQAVSRRRSEVRVPWLHSLAAAQEEDHEDQTDTEGEDTEEEEELETEENKFSEVAALPGPRGLLGGVAHTLQKTLQTTISAVTWAPAAVLGMAGRVLHLTPAPAVSSTKGRAMSLSDALKGVTDNVVDTVVHYVPLPRLSLMEPESEFRDIDNPPAEVERREAERRASGAPSAGPEPAPRLAQPRRSLRSAQSPGAPPGPGLEDEVATPAAPRPGFPAVPREKPKRRVSDSFFRPSVMEPILGRTHYSQLRKKS
Protein: FACT complex subunit SPT16 (DNA unwinding factor 140 kDa subunit) (DUF140) (Facilitates chromatin transcription complex subunit spt16) (Q9W603)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
Sequence:
MAVTLDKEAYYRRIKRFFGSWKKGDDEFANVDAIVVSVGVDEEIVYAKSTALQTWLFGYELTDTIMVFCEEKILFMASKKKVEFLKQIANTKGNENANGTPAITLLVREKQNESNKGNFDKMIEAIKVSKKGKRIGVFIKDKFPGDFMKSWYDILNKESFEKVDISASVAYTIAVKEEGELNLMKKAASITSDVFSKFFKDRVMEIVDADEKVRHGKLAESVEKAIEDKKYLGGTDPSTIEMCYPPIIQSGGNYNLKFSVVSDKNHMHFGAITCALGIRYKSYCSNLVRTLMVDPTQEMQENYNFLLQLQEELLKELKHGAKICDAYQVIMDQVKKQKPDLMSKITKTLGFAMGIEFREGSLVINNKNQYKLKKGMVFSVHLGLAELNNKMGKKPEEKTYALFVGDTVLVNEEGAATVLTNVKKKVKNVGIFLKKEDEEEEEEEKDEAEDLLGRGSRAAALLTERTRNEMTAEEKRRTHQKELATQLNDEAKRRLTEQKGGQQTMKARKSNVSYKNASQVPKEPELREMKLYIDKKYETVIMPVFGISTPFHIATIKNISMSVEGDYTYLRINFFCPGSALGRNEGNIFPNPEATFVKEITYRASNVKTPGDPSVPSLNLQNAFRIIKEVQKRYKTREAEEKEKEGIVKQDSLVINLNRSNPKLKDLYIRPNIAQKRMQGSLEAHVNGFRFTSVRGDKVDILYNNIKHALFQPCDGEMIIVLHFHLKNAIMFGKKRHTDVQFYTEVGEITTDLGKHQHMHDRDDLYAEQLEREMRHKLKTAFKNFIEKVESLTKEDLEFEIPFRDLGFNGAPYRSTCLLQPTSSSLVNTTEWPPFVVTLDEVELVHFERVQFHLKNFDMVIVYKEYGKKVTMINAIPMASLDPIKEWLNSCDIKYTEGVQSLNWTKIMKTIVDDPEGFFEQGGWSFLEPDGEGSDAAEGDSESELDDETFNPSEDEEEEEEDSDEDYSDETEDSVDSEESADSEEESGKDWDELEEEARKADRESLYEEVEEQKSGNRKRKGHAPLPNPSKKRKK
Protein: RNA helicase (EC 3.6.4.13) (Q9UB20)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEPIGDLQVPSFKVVSGGTTFTYASPKSGAASLDFLAHTLRKREANTEKTILICQQNFEAERLKFELAERDVNTILLPPHGAMVGQVLLLWSKGYINQALILCDGMLEHLGVVEANLVIHTTLPELNKFEERLKWLSISARNAEMLVITPCDEENEKEGKGETEPEIVQQRMPLKVDALNSMQLYEIKENTPPTSSEDYKAEADVLLSAATPATIPNDNKEQEINLSVEDATVKLLASFELGSTDSAAVDESSPAAAKFNAPVYSPFVTENPTKSLDAEFQELVKSFKVQNVFKNMNLPPPPSVSIEEPVSSASASDYRHQIDTTSLDSIRTVKDSPASLAVVPFSAVGITYNNYGVLGWSRHAVVPCYGLTEAPDISTIIRRAMQQMGVARSRARAVQRFAWPHVSLGKSVLVVGNLQIGKTWSYLPTVCQRSHEDLQRRPDVGRGPTCIFVCPNQGQGKQIERWMSTLLCLLGSASGFEDVVTHWDKTQLVDIVRRLKKPVGILLTSVDLLLQLLNHNPVGSIFDAQAVKCIALDNLNDMVRVLPNDTMKLLQRLPEMFQLTQNKCQLLVSGRIWHTDLMVQHILPLMPDVLVLFDDALEASVYGGVQLDVRVVADEPEKIEHLKALIAERRNFANEPAVMVCSNSTEVLLLRRSLQAIGVNAHICVSEACYSNVAEWLRQSPSGLLLVTDDVVPRLKCGKIPLLIHYSFASMWARFKNRFSLFYANLKSPTTRPVGQSVVFAKPTDLENIWKLCDFYMKHKLPRPGHLLGILSQRRLEEQPTSRSLCHQMAAFGDCLRHKCMYRHVMWRDEVLPPDHYPKNGLIRFLVLVCYSPAALAVRLSDQFPTAIRFLNFPMSDLGERVQRHYELEANRHMHPNPVPGEMAVVKNINRYERVHIVSVESNAMVLVQLLDTSTECFSYKTSQLYSCDKIFKDSPREAMDLRILGLQPESLDRIWPDDARNLVRKDFFRRTHNKRNRQFHAVVQSAIHRTIFVRNIYDDEGNDLLSFVINRFRSHQDECCQLKLDAMVMSSKDCPYM
Protein: Rho guanine nucleotide exchange factor 38 (Q9NXL2)
Organism: Homo sapiens (Human)
Function: May act as a guanine-nucleotide releasing factor.
Interaction partners:
Sequence:
MEPKEATGKENMVTKKKNLAFLRSRLYMLERRKTDTVVESSVSGDHSGTLRRSQSDRTEYNQKLQEKMTPQGECSVAETLTPEEEHHMKRMMAKREKIIKELIQTEKDYLNDLELCVREVVQPLRNKKTDRLDVDSLFSNIESVHQISAKLLSLLEEATTDVEPAMQVIGEVFLQIKGPLEDIYKIYCYHHDEAHSILESYEKEEELKEHLSHCIQSLKKIYMQEGKPNLLDMGSLMIKPIQRVMKYPLLLCELRNSTPPSHPDYRALDDAFAAVKDINVNINELKRRKDLVLKYKKNDEDESLKDKLSKLNIHSISKKSKRVTNHLKILTRGESQVKDNTFNREEKLFRALEKTVRLCVKNISLCLQHIQDAMPLALQSVMDLQEISYNKDDEMDYSETLSNALNSCHDFASHLQRLILTPLSALLSLFPGPHKLIQKRYDKLLDCNSYLQRSTGEESDLAKKEYEALNAQLVEELQAFNQAARKILLNCLCSFITLLRDLMLVAQQAYSTLVPMPLLVSSISEIQNQVLEEIQNLNCVKENSATFIERKLSFEKKKPVQILPEMPHQTDIHRSKLLSTYSAEELYQAKRKCNATQEYDINLLEGDLVAVIEQKDPLGSTSRWLVDTGNVKGYVYSSFLKPYNPAKMQKVDAENRFCDDDFENISLFVSSRPASDSVTGTSESSIGDSSSSLSGTCGKFETNGTDVDSFQEVDEQIFYAVHAFQARSDHELSLQEYQRVHILRFCDLSGNKEWWLAEAQGQKGYVPANYLGKMTYA
Protein: COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis), isoform CRA_a (Testis secretory sperm-binding protein Li 231m) (A0A024R7W9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q583L8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MTAVLLAMQTVVLLPAMFGGAAETSIEAVTSPYHEVMYLEKLISNFKGKLSTARSRATALSNDYSLLTLAAVCTEDTQKAAAYIALSAETKEAELKQEAAIAAGEAQITELVKTLKARVSQTKALIHAERDAVDTQVATPATTTQTFLSAGTGEHCTIPTSRGPSTTDSCTEAAGSGTHIDKAVVELQEIENIKLLKDERFLTPEYELIVAAQGNAGTGGPHRSYKKGACATSGDSGASLRSLTVALGVKSITRKKGEDEDPAKQSLFKGQGAGSGCVDADTDSKSHLTTQKKVANAICRHRGADIKLYERPLLKSKTTLANEGNLRALAQLLATGKVNTKEEATSQTEAVKALLPAGESTLTADLVDPLATEEITYDNDNNPVKTTIKDTNKPGKFATTLAFSYSRRQRKKSAITAQKEVSDTKKEKCKEDTEKSKYIADTDCEHKDGKCKLKEGVNMENDGKTTNTTGNNSFVISKVPTFLAFLLL
Protein: SET and MYND domain containing, arthropod-specific, member 4, isoform C (M9PHK0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIVRILLLRQHDPEQFALIARMESHTEERRQNAVLWRHYEEKVVQRLRVTWQLEDLEAEQVHEVCGILDVNCFEIGQNGAKARTLYPSAFLLAHDCTPNTAHTDDPSSFEILLRTSRRVREREALTLSYAYTLQGTLKRRAFMHEGKLFWCCCRRCSDPRELGTDCSALVCATCRTGSVRAVDPLQQTGDWACDRCAHKMGATEVERQLDRINNDLEDIDVHDIPGLENFLLRYRDVLRPNHYLLLSAKYSLCQIYGRTEGYLLPQMSPEDIARKESYCREFLEIVDVLDPGLTRLRGLIMYELHAPVMVLAQSAFQSGQISRQEFQRRLKEVVKLLQVSRDILLMEPEGSTENAMGQAAADALSKMGC
Protein: Protein NRT1/ PTR FAMILY 6.4 (AtNPF6.4) (Nitrate transporter 1.3) (Q9LVE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low-affinity nitrate transporter.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- High affinity nitrate transporter 2.7
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
Sequence:
MVHVSSSHGAKDGSEEAYDYRGNPPDKSKTGGWLGAGLILGSELSERICVMGISMNLVTYLVGDLHISSAKSATIVTNFMGTLNLLGLLGGFLADAKLGRYKMVAISASVTALGVLLLTVATTISSMRPPICDDFRRLHHQCIEANGHQLALLYVALYTIALGGGGIKSNVSGFGSDQFDTSDPKEEKQMIFFFNRFYFSISVGSLFAVIALVYVQDNVGRGWGYGISAATMVVAAIVLLCGTKRYRFKKPKGSPFTTIWRVGFLAWKKRKESYPAHPSLLNGYDNTTVPHTEMLKCLDKAAISKNESSPSSKDFEEKDPWIVSTVTQVEEVKLVMKLVPIWATNILFWTIYSQMTTFTVEQATFMDRKLGSFTVPAGSYSAFLILTILLFTSLNERVFVPLTRRLTKKPQGITSLQRIGVGLVFSMAAMAVAAVIENARREAAVNNDKKISAFWLVPQYFLVGAGEAFAYVGQLEFFIREAPERMKSMSTGLFLSTISMGFFVSSLLVSLVDRVTDKSWLRSNLNKARLNYFYWLLVVLGALNFLIFIVFAMKHQYKADVITVVVTDDDSVEKEVTKKESSEFELKDIP
Protein: S100 calcium-binding protein, ventral prostate (Q80VT8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Prostatic steroid-binding protein C1
Sequence:
MAQNLTSTEQEIMELLMILQEFSVKKIDKLDVQEVKRLFREELPNFLKAMDEATKNKILNDKGKEMPFDEIWDMIGRMALEYRKKNSNALKD
Protein: Thymocyte nuclear protein 1 (Thymocyte protein Thy28) (mThy28) (Q91YJ3)
Organism: Mus musculus (Mouse)
Function: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.
Subcellular location: Nucleus {ECO:0000269|PubMed:14580360, ECO:0000269|PubMed:14601557}.
Interaction partners:
- WD repeat-containing protein 76
Sequence:
MPRPRKRQTGTAGPDRKKLSGKRTKTENSESTSVKLENSSLEMTTTFKNGGKNLSNYWLMKSEPESRLEKGIDMKFSIEDLKAQPKQTACWDGVRNYQARNFLRAMKLEDEAFFYHSNCKQPGIVGLMKIVKEAYPDHTQFEKSNPHYDPSSKEDDPKWSMVDVQFVRMMKRFIPLEELKTYHQAHKATGGPLKSMTLFTRQRLSVQPLTQEEFDFILSLEETEPS
Protein: Protein Tat (Transactivating regulatory protein) (P20879)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate JRCSF) (HIV-1)
Function: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.
Subcellular location: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
Interaction partners:
Sequence:
MEPVDPSLEPWKHPGSQPKTACTNCYCKKCCLHCQVCFTTKGLGISYGRKKRRQRRRPPQDSQTHQVSLPKQPSSQQRGDPTGPKESKKKVERETETDPDN
Protein: Toll-9, isoform A (Toll-9, isoform C) (Q9VPH1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Protein spaetzle 5
- MstProx
- Toll-4
- Neurotrophin 1
- LD20892p
- Protein spaetzle
Sequence:
MCPKYIWDVIVLVCLFLGNVREAYTEFSIQDGLIIEPDSATTSSEEAEEVSKERTDLKSLMLKYESDDGNSCLLDLIKDEVIWWQFPNGTLRDSTKKYAHKLYLDLSHGNLKDDSDLFREAKLSRKVTIWRTEVFSAAFNTLTAAPFRTLYSMRESLKLLSLRGNNFAELIPDAEDFARFVNESRLEASNSVPHHCELLLLHNTTDLYDRECYLYFNNNTNMGQSITTGRNYTNFIKVLKDRFDQHGSSSQSIAWATFPKMPRLVELDISNCSIEYVSKEAFRNVSNLRRLFMSDNKIMTISHDTFYYVQGVQYLDLSFTNFLTYSYQLQLPTLEMALSLIYGLKIQQNVFKYLPELIYLDLSHSKMTRNSAVAFAHLGDKLKFLSLCYTAIPMVSSTIFKNTVLEGLDLSGNPYLSYNIIDDAFDGIANTLKYLYFERSNIKDLEWSKSLKNLQVLGLAGNNINALTPAMFQSLESLEILDLSSNHVGNWYRSAFHNNSALRVLNLRSNTINMLSNEMLKDFERLDYLSLGDNDFICDCHLRAVVEVAAANNKDADCSYRLLNYSQNAVGEEVISLAESLIIDRKLWQSRYIPWLQRSYSNIREFNRANHIIKLRFSSEDYMVAKCSAAQPYHLGDLDGDLTLKFQLLDYEASQYYCFNNTDQLQVDELNCQIRSMSDLAEELHHVTNTVIAVMGSLVGACILGFIIYLKRWHIHYYYSSLKSAALLSSASKESVNKFTNISQRDPSAVYDIFISYCQNDRTWVLNELLPNVEETGDVSICLHERDFQIGVTILDNIISCMDRSYSLMLIISSKFLLSHWCQFEMYLAQHRIFEVSKEHLILVFLEDIPRRKRPKTLQYLMDVKTYIKWPTAKEDRKLFWKRLKRSLEVIGINSREISV