wanglab/gogpt-training-data huggingface dataset:
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.-) (A0A8I5YBL7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGPTPASPTAGGLAPFASPRHGLALPEGDGSRDPPDRPRSPDPVDGAVCTVAATAAAPAASAAVGVAPSPAGGGGNNSASSTSSPTSSSSSSPSSPGSSIAESPEAAGVGSTATLGPGAAGLGPGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTEINLLPFYRSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVAELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDSLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPIRTSDVDYRLLEASKAGDLETVKQLCSPQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLRGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLERGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEALPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGAERKEGEVAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT
Protein: Nudix hydrolase 4 (AtNUDT4) (EC 3.6.1.-) (ADP-ribose pyrophosphatase) (EC 3.6.1.13) (NADH pyrophosphatase) (EC 3.6.1.22) (Q9LE73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose as substrates; however the relevance of such substrates in vivo is unclear.
Interaction partners:
- Nudix hydrolase 11
- Nudix hydrolase 25
- Nudix hydrolase 1
- Nudix hydrolase 10
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Late embryogenesis abundant protein At1g64065
- mRNA-decapping enzyme-like protein
- Nudix hydrolase 14, chloroplastic
- Nudix hydrolase 5
- Nudix hydrolase 6
Sequence:
MTGFSVSLFVSNLSNVASYLSPIFENIPSTKVVPAQIEKVVSLVSRTGRDLQRYDHAGYRQVVGCVPYRYKKQEVNGVETQVIQVLLVSAQKGKGMLFPKGGWETDESMEEAALRETIEEAGVTGELEEKLGKWQYKSKRHSIIHDGYMFALLVSQEFERWPEAEMRQRRWVSLDEAREVCQNWWMREALEAFINLKCLADDDESGN
Protein: Acyl-homoserine lactone acylase PvdQ (AHL acylase PvdQ) (Acyl-HSL acylase PvdQ) (EC 3.5.1.97) [Cleaved into: Acyl-homoserine lactone acylase PvdQ subunit alpha (Acyl-HSL acylase PvdQ subunit alpha); Acyl-homoserine lactone acylase PvdQ subunit beta (Acyl-HSL acylase PvdQ subunit beta)] (Q9I194)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the deacylation of acyl-homoserine lactone (AHL or acyl-HSL), releasing homoserine lactone (HSL) and the corresponding fatty acid. Possesses a specificity for the degradation of long-chain acyl-HSLs (side chains of 11 to 14 carbons in length). Degrades 3-oxo-C12-HSL, one of the two main AHL signal molecules of P.aeruginosa, and thereby functions as a quorum quencher, inhibiting the las quorum-sensing system. Therefore, may enable P.aeruginosa to modulate its own quorum-sensing-dependent pathogenic potential. Also appears to be required for pyoverdin biosynthesis.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- L-ornithine N
- PvdL
- PvdO
- PvdN
- PvdG
- L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, PvdH
- Pyoverdine export membrane fusion protein PvdR
- Pyoverdine biosynthesis protein PvdE
- PvdP
- PvdJ
Sequence:
MGMRTVLTGLAGMLLGSMMPVQADMPRPTGLAADIRWTAYGVPHIRAKDERGLGYGIGYAYARDNACLLAEEIVTARGERARYFGSEGKSSAELDNLPSDIFYAWLNQPEALQAFWQAQTPAVRQLLEGYAAGFNRFLREADGKTTSCLGQPWLRAIATDDLLRLTRRLLVEGGVGQFADALVAAAPPGAEKVALSGEQAFQVAEQRRQRFRLERGSNAIAVGSERSADGKGMLLANPHFPWNGAMRFYQMHLTIPGRLDVMGASLPGLPVVNIGFSRHLAWTHTVDTSSHFTLYRLALDPKDPRRYLVDGRSLPLEEKSVAIEVRGADGKLSRVEHKVYQSIYGPLVVWPGKLDWNRSEAYALRDANLENTRVLQQWYSINQASDVADLRRRVEALQGIPWVNTLAADEQGNALYMNQSVVPYLKPELIPACAIPQLVAEGLPALQGQDSRCAWSRDPAAAQAGITPAAQLPVLLRRDFVQNSNDSAWLTNPASPLQGFSPLVSQEKPIGPRARYALSRLQGKQPLEAKTLEEMVTANHVFSADQVLPDLLRLCRDNQGEKSLARACAALAQWDRGANLDSGSGFVYFQRFMQRFAELDGAWKEPFDAQRPLDTPQGIALDRPQVATQVRQALADAAAEVEKSGIPDGARWGDLQVSTRGQERIAIPGGDGHFGVYNAIQSVRKGDHLEVVGGTSYIQLVTFPEEGPKARGLLAFSQSSDPRSPHYRDQTELFSRQQWQTLPFSDRQIDADPQLQRLSIRE
Protein: Mapk8IP3 (L7RKJ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MELDEVVYQDDYGAVSVMSERVTGLASSIYQEFERLIKTYDEEVVKELMPLVVNVLENLDSVLTENQEHEVELELLKEDNEQLITQYEREKALRKQAEEKFIEFEDALEADKKDLQTTVETLELQAKQLELKSKNYADQISRLEERESDMKKEYNALHQRHTEMIQTYVEHIERSKLQQSGSNQSESTGCGRSQRHNWRKSKTERPPSLSLYPGGDGMEDGSDSDSVAATPSSTGSKSNTPTSSVPSATVTPLNDGLVSVGEYDTSRGRARDRRTGKRLSRNMEVQVSQETRNVSIGMGSSDEWSEFQEIIDSTPELDMCLDPRIFGGGNSPSQGIVNEAFGINTDSLYHEIKDAKSDIIGDVDAGAELLGEFSVRDDFFGMGKEVENLLTENKQLLETKNALNIVKNDLIAKVDELSSEQEVLREELESVKQSKTKVDQRVKELEEELKRLRAEALGASQDSKDEGGEDYSSPLQDDVTMTQRRRFTQVEMARVLMERNQYKERLMELQEAVRWTEMIRASRESPPLPEKKKSIIWQFFARLFSSSASPPPVKRPYTSVNIHYKSPSPAGYNQRRSQTMCQISTSTCIREFLPEDDSALCTRREQRREQYRQVREHMRRKDGPMQTCGWSVPSRLKQNGCQADSAPDATAKRNQATEKEDNRMKNVPVPVYCRPLVEKDPNRKLWCAAGVDLTGWKTSSQEAASVKPSNGSDPLTAENEGGDGKSEQSSPEKKKPKELHETDPVSSRVWILTSTHSASKVVIIDANLPCSLVDQFNVCNAHVLCISSVPAASESDYPAGEIFLEQQAGDGASEEKGGVEGMLAGITIVGCATNCSVVRSNCSSRTDTPVQDRSNAPTAPVCRSLAVSQSAEEATEAIEVTEEAGPSENADSTLGSFTEHVFTDNTHSEPGVAKEKVSSAPADSEEAADERAGTSAAPTMWLGAQNGWLYVHSAVSNWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRSEDGQWDLSNYHLMDLGRPHHSIRCMAVVHDKVWCGNKNKIHVIQPKSMQIEKSFDAHPRKESQVRQLAWIGDGVWVSIRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGTGKLGFSFVRITALLIGGNRLWVGTGNGVIISIPLTETVVLHRGQLLGLRANKVSPTSSGGVIHVYADDSTSEKSSFIPYCSMAQAQLCFHGHRDAVKFFVSVPGNVLATLNGSVLDSPSESQGSSAPAETEAQSLQNVLVLSGGEGYIDFRIGDGEDDETEEADDDEAPQMKPALSKAERSHIIVWQVSYVPE
Protein: Glutamine synthetase cytosolic isozyme 1-4 (EC 6.3.1.2) (Glutamate--ammonia ligase GLN1;4) (GLN1;4) (Q9FMD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-affinity glutamine synthetase. May contribute to the homeostatic control of glutamine synthesis in roots.
Subcellular location: Cytoplasm.
Interaction partners:
- Ferredoxin--nitrite reductase, chloroplastic
- Ferredoxin-dependent glutamate synthase 2, chloroplastic
- Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial
- Glutamate synthase 1, chloroplastic
- Glutamate dehydrogenase 2
- Glutamate dehydrogenase 1
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Carbamoyl phosphate synthase small chain, chloroplastic
- Glutamate--glyoxylate aminotransferase 1
- glutamate dehydrogenase
Sequence:
MSSLADLINLDLSDSTDQIIAEYIWIGGSGLDMRSKARTLPGPVTDPSQLPKWNYDGSSTGQAPGDDSEVIIYPQAIFKDPFRRGNNILVMCDAYTPAGEPIPTNKRHAAAKIFEDPSVVAEETWYGIEQEYTLLQKDIKWPVGWPVGGFPGPQGPYYCGVGADKAFGRDIVDSHYKACLYAGINVSGTNGEVMPGQWEFQVGPTVGIAAADQVWVARYILERITELAGVVLSLDPKPIPGDWNGAGAHTNYSTKSMREDGGYEVIKKAIEKLGLRHKEHIAAYGEGNERRLTGKHETADINTFLWGVANRGASIRVGRDTEQAGKGYFEDRRPASNMDPYTVTSMIAESTILWKP
Protein: Galacturonokinase (EC 2.7.1.44) (D-galacturonic acid-1-P kinase) (Q8VYG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sugar-1-kinase with a strict substrate specificity for the alpha-anomeric configuration of D-galacturonic acid (D-GalA) and ATP. Involved in the biosynthesis of UDP-galacturonic acid (UDP-GalA) from the salvaged GalA that is released during growth-dependent cell wall restructuring.
Interaction partners:
- Glucuronokinase 1
- Probable glucuronokinase 2
- Thylakoid lumenal P17.1 protein
- ADP-glucose phosphorylase
- UDP-sugar pyrophosphorylase
- Ethanolamine-phosphate cytidylyltransferase
- UDP-arabinose 4-epimerase 1
- Aldo-keto reductase family 4 member C10
- Exopolygalacturonase clone GBGA483
- Exopolygalacturonase clone GBGE184
Sequence:
MSWPTDSELNSIKEAVAQMSGRDKGEVRVVVAPYRICPLGAHIDHQGGTVSAMTINKGILLGFVPSGDTQVQLRSAQFEGEVCFRVDEIQHPIGLANKNGASTPSPSKEKSIWGTYARGAVYALQSSKKNLKQGIIGYLSGSNGLDSSGLSSSAAVGVAYLLALENANELTVSPTENIEYDRLIENGYLGLRNGILDQSAILLSNYGCLTYMDCKTLDHELVQAPELEKPFRILLAFSGLRQALTTNPGYNLRVSECQEAAKVLLTASGNSELEPTLCNVEHAVYEAHKHELKPVLAKRAEHYFSENMRVIKGREAWASGNLEEFGKLISASGLSSIENYECGAEPLIQLYKILLKAPGVYGARFSGAGFRGCCLAFVDAEKAEAAASYVKDEYEKAQPEFANNLNGGKPVLICEAGDAARVLL
Protein: Neuromusculin, isoform E (M9NE05)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Ninjurin C, isoform D
Sequence:
MGNMALRQSAKDVAKSNCVAVRSSISLSLVLVLCLALVDSSTAQVDTTISQQESQSVVLPCPVDAEKCGKLHSLNWFKGDDRIAAMLLGDSNVTSVNKEFDERVTVEQNPYRLVIKDLKIADEDIYLCDTTFFIPEETCDNFNGYRIELRVLVPPTEVVILDAKGDRIKNGSVVGPMQERQSLKATCTVRNTRPQPEVSWFRGTKRLTTYSPTHDLVDGLYTSTLELDWTLSREDLAQDIECRVKSAAIQNVTVTKFSVDLQVRPTSIDINGVKHHTVQGSKVVLTCDIHGARPAVNLTWYNTTTIISSGENEITEVRSKSLEKSDGTFHTQSELIFNATRFENDRVFRCEAENIVLQINREKPISSALTLEVLYPPVVKVSPSAITANTSEIVLLNCEYFANPASLTQVEWYRNDILVNVNDTTHYKGGNSENVALVIKSTEKEDIGNYSCQLSNNIGKGTSDQKINLDVQYAPTVEILMIPEGPVKESDESNVTLFCNVLDANPSVLTKVRWYANSTLLKELPDCEETREDLCHIDPSKLLLESIGRGFFYNYSCEGFNAAGWGPRSEDKELLVHYEPGPAALSHFPLVAVKKKSVTFSCSVDDPGFPESNRFRWLRGGRGPLQDIVTKDWTVEPVGLDSRTNYSCYAYNEGGKGVMATVNLEVHAPPFFIKNLPPYTGILHSSPNATLTCRIECVPRCDISWQKDGVPIERNDSRYFIKEKYMDASPATGDFESMLSVLHFNMPNWPDSKFNIEADNANYSCVSTGNIVGGSIRSRTYFGIEYAPENTTVSENIVYVQEDTIPGRVICKSRANPEPSYKWIFKNETIANGNALIINTAMNRNDDGTYTCLAYNKHGSSIAKTVIKVQFKPRCEIERQEIDDQDTLICTAYGNPIEADFSWSIKTENETDENLGSGKKENSVEKSFYILQTDYAISRTYRCVANNTVGYGPFCEIEVAEQLAWWQLWEKNTLIILVAAILGLLLTVIVICCIIICICRRRRRQDKYLTEVPINSIQSALSDQLDMSRAGRNLSTQDKCTAILPNPSSSRFIGSAPKSPPRWPIRPGVMLHVSSNTKENLTVNRMTVKPNVSGNRGDMSQLSAQLSAALNGSRDNSDGTILTEISAVSGENEASNLSILEVTNRKKATVPSTIRNVSTAEGEIISSKTHSAGHIALDHVWSLIFKKSDDRTRDSQRSHVGLLQTFWRGLGAKESTSGFESQHRLKGIRCSGSVTYKKAKETVHSTSDAASNGESSLTKRPNNCQPSVSIQLQSNMEEKTSKFVLKDERNNSSTEVENIPCNMVPSITRGSSIESPQRPAPSSLPLKNFLNVTSWGCSGNSTMVPSHILANEQIHDKSSSLREPLTEPGEYENLPFHGLQTAPNKFSTTPTNFNNNTNAVRVAQRPKELIGNINQPSVGLYQDCQATHDPLLYHQKYFCDQDALNDQRSQYTTMHRPPNNVQYNQSLFKPDSNLQDQHNLSNCISKSYTEYYQQHQRSEKLQMIFPQGASKELNSNSLCNTDHTPHSALVNINLRKYDRTEEELLGNMPRARHRKGTLNVENKFYSLKHLGGIEVRNQDLDKDYPIGGTTSSTPSATDDSSLSKCKIHNSLGCNRLCNVGTNVQPMRVYDPPGYQNMVLERADDQITLSKKDECNLATVQTHTHPGKDKIKNHHHWIHQHREKKDEGLGSDFHQLEPERISIYRSDSGISNSSYESQFSKPKMATLNSSSGPLVRKYAHRNIKVHNNVFNTSNVTESEAQLDDSSTLHQSCTVQSFAPSHCNRPQPRNRYSEETTKNECEQHQLGHQSLRPASTPSECISLDTSSRSEYIMSTVPAQSDSVETPNEKIQMLAINPLLVKNWNNESYTGNKINKKQRRQTINNPYEHIQSHPYARPGDVCEVSRKAQSNSSEAFKTYNYGSKSNSSAPQTAAPEHSKVKNATKICKKNGIGANREHYEGMLASKHIQGSRLGSLADIDDFPSQGPLNALVGNPADCLVARRPIRLPLRKHHTFHFQSTQTANGKLQQLRERLQLQLHESRKVDQEKFPLVFDALELSEKHAFKPISPIPSLNNSAVQSTGEQKQVDFPKHGSVRHLKGAEDDEDLGYSFCEEECVVENDINPTSDNLKTAPTNSSCSSTAVESANPINAQIFDDEFIYADLESQHYGPINYKAASLYSQVKKNKESGALDDLK
Protein: Ribose-phosphate pyrophosphokinase 2 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase 2) (O94413)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: 5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 1
- Probable transketolase
- Amidophosphoribosyltransferase
- Ribokinase
- Probable phosphoribomutase
- Ribose-5-phosphate isomerase
- Ribose-phosphate pyrophosphokinase 5
- Phosphoglucomutase
- Uncharacterized Nudix hydrolase P35G2.12
- ATP phosphoribosyltransferase
Sequence:
MASNSIKIFAGNSHPELAEKVARRIGLSLGKVAVVQYSNRETSVTIGESVRDEDVFILQTGCGSINDHLMELLIMINACRSASARRITAIIPCFPYARQDKKDKSRAPITARLVANMLQTAGCNHIITMDLHASQIQGFFNVPVDNLYAEPSVLRYIRENIDTTVNPTVIVSPDAGGAKRATALADRLDLDFALIHKERQKANEVSRMVLVGDVRDKLAILVDDMADTCGTLGLAAKTLKDNGAKAVYAIVTHGILSGKAIKVINESALEKVIVTNTIPHDDKRSLCSKIETIDISGVLAECIRRIHHGESVSVLFSVAPA
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (A0A8I6GLU2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLGTFKYLKLCFLFLAVPFPPTRRLTLKEVFENGKPKMDVLKNHLVKEGRVEEDVALKIINDGAAILKQEKTMLEVEAPITVCGDVHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTEYFTFKQECRIKYSELVYEACMHTFDCLPLAALLNQQFLCVHGGMSPEITCLDDIRKLDRFAEPPAFGPVCDLLWSDPLEDYGSEKTLEHYTHNTVRGCSYFFSYPAVCEFLQNNSLLSIIRAHEAQDAGYRMYRKNQATGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNILNICSDEEMSLVEEEGATSVRKEVIRNKIRAIGKMARVFTVLREESENVLILKGLTPTGTLPLGVLSGGKQTIETAKLQAAEEREAIRGFTIAHRIRSFEEARGLDRINERMPPRKEASYHHDAGKTHPHPSKRSDHGKKAL
Protein: Histone deacetylase HOS3 (EC 3.5.1.98) (Q02959)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10535926}.
Interaction partners:
- Histone deacetylase HOS1
- Probable histone deacetylase HOS2
- Histone deacetylase RPD3
- Protein AFG1
- Transcriptional regulatory protein SIN3
- G1-specific transcriptional repressor WHI5
- HDA1 complex subunit 3
- ISWI chromatin-remodeling complex ATPase ISW1
Sequence:
MSSKHSDPLERFYKQFQAFVQNNPNVISAARAAAQIPESAKAVVVLSPYSLQHVFPREWVTKSYRKTIVERPERLLASSMGISAAITMYPSLFTLKSSHQRKGSLMAPHVLKVHGSSWPAELIELCQMADAKLLKGEIEVPDTWNSGDIYLSSKTIKALQGTIGAIETGVDSIFKGPSAEHISNRAFVAIRPPGHHCHYGTPSGFCLLNNAHVAIEYAYDTYNVTHVVVLDFDLHHGDGTQDICWKRAGFKPEEEPEDSSYDDFGKKFAEFPKVGYFSMHDINSFPTESGFATKENIKNASTCIMNSHDLNIWNIHLSKWTTEEEFNVLYRTKYRTLFAKADEFFRSAKLEMNQQGRPFKGLVVISAGFDASEFEQTSMQRHSVNVPTSFYTTFTKDALKLAQMHCHGKVLSLMEGGYSDKAICSGVFAHLIGLQNQDWVKEWGSEQVVKEIVRGCKPAWKPYKTKRAKDVIRIWAEEVIRLGRAMIPEFDDIIFKDAVNSAPSNSLLKATVEPASTSTIAQRIIRSHRSNASPEKELHENKPRSTEKQEQREIRSDTKVKQLSSNNRAAETQIPFLQQEFSSEDEDEEYVYDEELNKTFNRTVEDITIDDISRHLETLEIEKKGDEDSDHELKEKNWKNSHQRRLQGNGMYKIPSNTKPHRIRQPQNANTPTYDDSDISMISHVSRKHTTRSGGRW
Protein: Mitogen-activated protein kinase kinase kinase 8 (Q5T853)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEYMSTGSDNKEEIDLLIKHLNVSDVIDIMENLYASEEPAVYEPSLMTMCQDSNQNDERSKSLLLSGQEVPWLSSVRYGTVEDLLAFANHISNTAKHFYGQRPQESGILLNMVITPQNGRYQIDSDVLLIPWKLTYRNIGSDFIPRGAFGKVYLAQDIKTKKRMACKLIPVDQFKPSDVEIQACFRHENIAELYGAVLWGETVHLFMEAGEGGSVLEKLESCG
Protein: Type II secretion system protein E (T2SS protein E) (EC 7.4.2.8) (General secretion pathway protein E) (Pectic enzymes secretion protein OutE) (Type II traffic warden ATPase) (Q01566)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Function: ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Acts as a molecular motor to provide the energy that is required for assembly of the pseudopilus and the extrusion of substrates generated in the cytoplasm.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:Q00512}. Note=Membrane association is not an intrinsic property but requires the OutL/GspL gene product. {ECO:0000250|UniProtKB:Q00512}.
Interaction partners:
- Type II secretion system protein F
- Type II secretion system protein L
- Type II secretion system core protein G
- Secretin OutD
- Type II secretion system protein F
- Type II secretion system protein F
- Prepilin leader peptidase/N-methyltransferase
- Type II secretion system protein C
- Type II secretion system protein E
- Type II secretion system protein J
Sequence:
MSDQPVNTPELRPVLPFSFARAQQILLLQDESVTVAEVVCVPDTPALALLEARRVAGVPLAVSQVSPEEFERQLVMRYQRDSEEARRLMEDIGNDIDFYTLAEELPDSDDLLDGEDDAPIIRLINAMLTEAIKHKASDIHIETFERHLLIRFRIDGVLREILRPQRQLASLLVSRIKVMAKLDIAEKRVPQDGRMALRIGGRAIDVRVSTLPSNYGERVVLRLLDKNSVRLDLEALGMAEHNRRQLDTLIHRPHGIILVTGPTGSGKSTTLYAALSRLNSAERNIMTVEDPIEYELEGIGQTQVNPKVDMTFARGLRAILRQDPDVVLVGEIRDGETAQIAVQASLTGHLVLSTLHTNSALGALSRLQDMGIEPFLLSTSLLGVLAQRLVRTLCPSCRQPYVINDEQAQQTGLAAGTTLYHPGGCEKCNYSGYRGRTGIHELLLIDDTVRTAIHHGESELGIARMLGDKRITIRQDGLDKVLAGVTTWEEVVRVTKEE
Protein: Reduction of Rh1, isoform A (Reduction of Rh1, isoform B) (Q0E8X7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADKAAAEKPAGRPMRYPYTFSAKIAQFPIKHYIKNQWIWRYYFIAAVACVPVFYKISKLANSPENKKAWAESQAKEHAEHH
Protein: Formimidoyltransferase-cyclodeaminase (58 kDa microtubule-binding protein) (Formiminotransferase-cyclodeaminase) (FTCD) [Includes: Glutamate formimidoyltransferase (EC 2.1.2.5) (Glutamate formiminotransferase) (Glutamate formyltransferase); Formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) (Formiminotetrahydrofolate cyclodeaminase)] (O88618)
Organism: Rattus norvegicus (Rat)
Function: Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9YH58}. Golgi apparatus {ECO:0000269|PubMed:12160147, ECO:0000269|PubMed:9677387}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O95954}. Note=More abundantly located around the mother centriole. {ECO:0000250|UniProtKB:O95954}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Probable imidazolonepropionase
- 5-formyltetrahydrofolate cyclo-ligase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Methylenetetrahydrofolate dehydrogenase
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Uncharacterized protein.
- Serine hydroxymethyltransferase
- Methionyl-tRNA formyltransferase, mitochondrial
Sequence:
MSQLVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKGEHPRMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVPDFGPSSFVPSWGATVTGARKFLIAFNINLLSTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLEEKNLAQVSTNLLDFEVTALHTVYEEARREAQELNLPVVGSQLVGLVPLKALLDAAAFYCDKEKLFVLEEEHRIRLVVNRLGLDSLAPFDPKERIIEYLVPDSGPEQSLLDASLRAFVREVGARSAAPGGGSVAAAVAALGAALASMVGQMTYGRRQFDHLDSTMRRLIPPFHAASAQLTSLVDADARAFAACLGAIKLPKNTPEERDRRTCALQEGLRQAVAVPLKLAETVSQLWPALQELAQCGNLSCLSDLQVAAKALETGVFGAYFNVLINLKDMTDDVFKEKTRHRISSLLQEAKTQAALVLGSLEARKE
Protein: Amine oxidase (EC 1.4.3.-) (Q8VEN4)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSFRTMAKKSGILVWGILLCVSSCLALYENLVKCFQDPDYEAFLLIAQNGLHTSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGWYLELGPMRIPESHKLIHTYVQKLGLKLNKFNQYDSNTWYLLNGQRYRASEVMANPGILGYPLRPSEKNKTVTDLFYQAITKIKPHRKTSNCSQLLSLYDSYSTKAYLMKEGTLSKGAIEMIGDIMNENAGYYKSLLESLRIASIFSKSDQFSEITGGFDQLPNGLSASLKPGTIRLGSKVERVVRDGPKVKVMYRTDGPTSALHKLTADYAIITASAKATRLITFQPPLSREKTHALRSVHYTSATKVVLVCNERFWEQDGIRGGYSITDRPSRFIYYPSHSLPGGKGVLLASFTVGDDSSFFAALKPNQVVDVVLDDLAAVHRIPKEELKRMCPKSAIKHWSLDPLTIGAFTEFTPYQFVDYSKQLSQPEGRIYFAGEHTCLPHSWIDTAIKSGIRASCNIQAAVDKEATRGHTAL
Protein: ORF8b protein (Accessory protein 8b) (Non-structural protein 8b) (ns8b) (Q80H93)
Organism: Severe acute respiratory syndrome coronavirus (SARS-CoV)
Function: Non-structural protein which is dispensable for virus replication in cell culture.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:16753150}. Host nucleus {ECO:0000269|PubMed:16753150}.
Interaction partners:
Sequence:
MCLKILVRYNTRGNTYSTAWLCALGKVLPFHRWHTMVQTCTPNVTINCQDPAGGALIARCWYLHEGHQTAAFRDVLVVLNKRTN
Protein: Vacuolar protein sorting-associated protein 18 homolog (Protein deep orange) (Q24314)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes probably as part of the class C core vacuole/endosome tethering (CORVET) complex. In larval neuromuscular junctions, essential for endosomal sorting which traffics old or dysfunctional synaptic vesicle proteins through a degradative endolysosomal route. Required for the biogenesis of eye pigment granules. Required to maintain normal levels of rush, which functions in endosome formation and trafficking.
Subcellular location: Early endosome {ECO:0000305|PubMed:27253064}. Late endosome membrane {ECO:0000269|PubMed:10549280}; Peripheral membrane protein {ECO:0000269|PubMed:10549280}; Cytoplasmic side {ECO:0000269|PubMed:10549280}. Lysosome membrane {ECO:0000269|PubMed:10549280}; Peripheral membrane protein {ECO:0000269|PubMed:10549280}; Cytoplasmic side {ECO:0000269|PubMed:10549280}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:28063257}. Note=Recruitment to autophagosomes enchanced by Rab2. {ECO:0000269|PubMed:28063257}.
Interaction partners:
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 39 homolog
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 8 homolog
- Vacuolar protein sorting 33B
- Vacuolar protein sorting-associated protein 33A
- Ras-related protein Rab7
- LD27967p
- Vacuolar fusion protein CCZ1 homolog
Sequence:
MDTSMPNQPKFLPRIEHNSSGATANSYVATASGNPFETDEEDEIFSRHKMVLRVPSNCTGDLMHLAVSRNWLVCLLGTPERTTLLRFFLPRAIPPGEAVLEKYLSGSGYKITRMFLDPTGHHIIIALVPKSATAGVSPDFLYIHCLESPQAQQLKVRRIEKFKDHEITAVAFNPYHGNESSTGPILLGTSRGLIFETELNPAADGHVQRKQLYDLGLGRPKYPITGLKLLRVPNSSRYIIVVTSPECIYTFQETLKAEERSLQAIFAGYVSGVQEPHCEERKTDLTFSQLRFFAPPNSKYPKQWAWLCGEGIRVGELSIEANSAATLIGNTLINLDFEKTMHLSYGERRLNTPKAFVLTEYHAVLLYADHVRAICLLNQEQVYQEAFDEARVGKPLSIERDELTGSIYVYTVKTVFNLRVTREERNVWRIYLDKGQYELATAHAAEDPEHLQLVLCQRADAAFADGSYQVAADYYAETDKSFEEVCLKFMVLPDKRPIINYVKKRLSRVTTKPMETDELDEDKMNIIKALVIWLIDLYLIQINMPDKDEEWRSSWQTEYDEFMMEAHVLSCTRQNRETVRQLIAEHADPRNMAQFAIAIGDYDEVVAQQLKAECYAEALQTLINQRNPELFYKYAPELITRLPKPTVDALMAQGSRLEVEKLVPTLIIMENREQREQTQRYLEFAIYKLNTTNDAIHNFLLHLYAEHEPKLLMKYLEIQGRDESLVHYDIYYAHKVCTDLDVKEARVFLECMLRKWISAVDLALTFDMKLAKETASRPSDSKIRRKLWLRIAYHDIKGTNDVKKALNLLKECDLLRIEDLLPFFADFEKIDNFKEAICDALRDYNQRIQELQREMAETTEQTDRVTAELQQLRQHSLTVESQDTCEICEMMLLVKPFFIFICGHKFHSDCLEKHVVPLLTKEQCRRLGTLKQQLEAEVQTQAQPQSGALSKQQAMELQRKRAALKTEIEDILAADCLFCGLLISTIDQPFVDDWEQVNVEWE
Protein: Prickle-like protein 1 (Q3U5C7)
Organism: Mus musculus (Mouse)
Function: Involved in the planar cell polarity pathway that controls convergent extension during gastrulation and neural tube closure (By similarity). Convergent extension is a complex morphogenetic process during which cells elongate, move mediolaterally, and intercalate between neighboring cells, leading to convergence toward the mediolateral axis and extension along the anteroposterior axis. Necessary for nuclear localization of REST. May serve as nuclear receptor (By similarity).
Subcellular location: Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=A smaller amount is detected in the cytosol. {ECO:0000250}.
Interaction partners:
- Vang-like protein 2
- Segment polarity protein dishevelled homolog DVL-1
- Vang-like protein 1
- Segment polarity protein dishevelled homolog DVL-2
- Segment polarity protein dishevelled homolog DVL-3
- Ankyrin repeat domain-containing protein 6
- Cadherin EGF LAG seven-pass G-type receptor 1
- Rho GTPase-activating protein 21
- Frizzled-6
- Frizzled-3
Sequence:
MPLEMEPKMSKLVFGCQRSSTSDDDSGCALEEYAWVPPGLRPEQIQLYFACLPEEKVPYVNSPGEKHRIKQLLYQLPPHDNEVRYCQSLSEEEKKELQVFSAQRKKEALGRGTIKLLSRAVMHAVCEQCGLQMNGGEVAVFASRAGPGVCWHPSCFVCFTCNELLVDLIYFYQDGKIHCGRHHAELLKPRCSACDEIIFADECTEAEGRHWHMKHFCCLECETVLGGQRYIMKDGRPFCCGCFESLYAEYCETCGEHIGVDHAQMTYDGQHWHATEACFSCAQCKASLLGCPFLPKQGQIYCSKTCSLGEDIHASDSSDSAFQSARSRDSRRSVRMGRSSRSADQCRQSLLLSPALNYKFPGLSGNADDTLSRKLDDVSLASRQGAGFANEEFWKARVEQEASEDPEEWAEHEDYMTQLLLKFGDKNLFQQQSSEVDPRASEHWIPDNMVTNKPEVKPNHQGLASKKYQSDMYWAQSQDGLGDSAYGSHPGPASSRRLQELDLDHGAAGYTHDQSQWYEDSLECLSDLKPEQSIRDSMDSLALSNITGASVDGESKPRPSLYSLQNFEEIEAEDCEKMSNMGTLNSSMLHRSAESLQSLNSGLCPEKILPEEKPAHLPVLRRSKSQSRPQQVKFSDDVIDNGSYDIEIRQPPMSERTRRRAYHFEERGSRPHHHRHRRSRKSRSDNALNLVTERKYSAKDRLRLYTPDNYEKFIQNKSARELQAYMQNANLYSQYAHATSDYALQNPGMNRFLGLCGEDDDSWCSSSTSSSDSEEEGYFLGQPIPQPRPQRFTYYTDDLSSPASALPTPQFTQRTTKSKKKKGHKGKNCIIS