wanglab/gogpt-training-data huggingface dataset:
Protein: JNK-interacting protein 3 (Protein sunday driver) (Q9GQF1)
Organism: Drosophila melanogaster (Fruit fly)
Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK-signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Syd is required for efficient kinesin-I mediated axonal transport.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Kinesin light chain
- ADP-ribosylation factor 6
- JNK-interacting protein 1
- Uncharacterized protein, isoform A
- Dynein light intermediate chain
Sequence:
MMDNDDALLNNGGPQSGAETVYGTEDNNMVMSEKNEQVVSIVQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHASRLEEREADLKKEYNKLHERYTELFKNHVDYMERTKMLMGSTHSQMSTASERMDVSRARLNPVARSSGPVSYGFASLENSVMLDTETICSVGSQSDDSGPPSLQNELDNLSGTLERGAATDALQQQHHATSPQSPDSSPVVPNVPTNVGRSTTKKEQRSDNNLYQELSFQDNEESEENEIVTGSWVHPGEYASSANDNYFGMGKEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRFTRVEMAMVLMERNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQSIWKYFSNLFTPSNRPTERVADGLGGGPMFRHTGGGSPAHSHGSPSRGSGGGDNRLALTSGQPPVHPASAGLANALIMPKDYAEEGSSERISARRREQYRQLRAHVQKEDGRLHAYGWSLPINKASQEANPNRHSGGVPVPVYCNPLAEASPHMKVFCAAGVNLHGGFTKNGQSLIPANSPYAPKSTLKIAEITSPTADQSMEALDRQMARVSLETLEPETQLSSFVWICTSTHAASTVSVVDANQSATVLDAFPICASHLLCIASVQGAMESDYALLEQSEVVKAGEMLQRPGEGTELLGKVEFVRVKPKSDDEQNSNEKQQQEEEEAKEATEKSNEQLPAVSAEEPLGNVEAIKIRQPLPGAPQRLSTDGNQTNNNNNSSSSSNLLFATKSLNPILETKDRDEPAMSSVGPTMWLGAQDGWLYVHSSVGRWHECLHRVLLPDAVLAIVHVEARVVVALANAQLAVFRRQTDGQWDLNSYHLVTLGDRNHSIRCLCVAGERIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAGVWVSIRLDSTLRLYNTHTFEHKQDVDIEPYVSKMLGTGKLGFSFVRITALMVSCNRLWIGTSNGVIISVPLAEVQPKSSSDPHGQMPLCCMANAQLSFHGHRDAVKFFVSVPMLQQPNLNGGLTFTNKRPDMLVMCGGEGYIDFRINDNDMENSIQLEPNQTIENRGDKSYLIVWHVSQR
Protein: Sorbin and SH3 domain containing 1 (S4R303)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XEWRLSSSADANGNAQPSSLAAKGYRSVHPNLPSDKSQVLSPPRPPLPQKDRFAWQSPTIHNTYKDSLYLSSPKPYVPLGTPRQQNPSQPQPISVLLAAGSAPKGVVCPGSLLPDSTFPSASSQPQQRYAATRTVYHKNVSSNPCHEAVGIKKVSSLYVPCLSNNICLAASENSSRVARDPAEGTPLEAAGTRAPAPGLVSRTAGTGKPPPAPPPDPPKLFFDIRKDAVNRGESPSLGTQASFPDVRPPVLGPRVTSDPENRKSKESYLLQPSYPAKDSSPLLNEVSSSLIGTDSQAFPSVSKPSSAYPSTTIVNPTIVLLQHNREQQKRLSSLSDPVSERRVGEQDSAPTQEKPTSPGKAIEKRAKDDSRRVVKSTQDLSDVSMDEVGIPLR
Protein: ATP synthase subunit a (Q2F976)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU004450}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU004450}.
Interaction partners:
Sequence:
MNFDHNHVVIMGLNQRDSIWKLLNDYNVNSLKRRRQAEIDAFFEPFERAQRIRFNNWQNGIELLDGAEWRNGDIVIPGGGGPVISSPLDQFFIDPLFGLDMGNFYLSFTNESLSMAVTVVLVPSLFGVVTKKGGGKSVPNAWQSLVELIYDFVLNLVNEQIGGNVKQKFFPRISVTFTFSLFRNPQGMIPFSFTVTSHFLITLALSFSIFIGITIVGFQRHGLHFFSFLLPAGVPLPLAPFLVLLELISHCFRALSSGIRLFANMMAGHSSVKILSGFAWTMLFLNNIFYFIGDLGPLFIVLALTGLELGVAILQAHVSTISICIYLNDAINLHQNE
Protein: NAC domain-containing protein 22 (ONAC022) (Q10S65)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription activator that binds sequence-specific DNA motifs. Involved in stress response. Plays a positive role in drought and salt stress tolerance through the modulation of abscisic acid-mediated signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:26834774}.
Interaction partners:
- Small ribosomal subunit protein eS19
- Os10g0411700 protein
- Small ribosomal subunit protein uS9
- 40S ribosomal protein S29, putative, expressed
- 40S ribosomal protein S30
- Small ribosomal subunit protein uS19
- 40S ribosomal protein S15, putative, expressed
- 40S ribosomal protein S21
- Small ribosomal subunit protein eS21
- 60S ribosomal protein L29
Sequence:
MAAAVAVAGPSMEVEQDLPGFRFHPTEEELLDFYLSRVVLGKKLHFNIIGTLNIYRHDPWDLPGMAKIGEREWYFFVPRDRKAGNGGRPNRTTERGFWKATGSDRAIRSSGDPKRVIGLKKTLVFYQGRAPRGTKTDWVMNEYRLPDYGAARAAAPPPKEDMVLCKIYRKATPLKELEQRASAMEEMQRGSSHGDYTATRASLVHDASASTGDDYFSSDDVHDSGFLIQSSSSSAAPSGSSSKNGGAGAPREAKKEEADVTVTVASATSLQLPAVSQLPSLQLPAMDWLQDPFLTQLRSPWQDQHCLSPYAHLLYY
Protein: Spectrin, alpha, erythrocytic 1 (A0A8J8Y4Y9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
METPKETAVESSGPKVLETAEEIQHRRQEVLDQYQRFKERVAERGQKLEESYHYQVFRRDADDLEKWIMEKLEITKDKTYEPTNIQGKYQKHESFVSEVQAKSRVLPELEEIREARFAEDHFAHEATKTHLKELRHLWDLLLELTQEKSDILLRALKFYQYCQECEDILEWVKEKEAIVTLVELGDDWERTEVLHKKFEEFQEELTARKGKVDRVNQYANECAQEQHPKLPEIKAKQDEVNAAWDRLWSLALKRRESLSNAADLQRFKRDVNEAIQWMEEKEPLLTSEDYGKDLVSSEALFHSHKRLERNLAVMDDKVKELCAKADKLMVSHSADAPQIQQMKMDLVSNWELIRALATNRYAKLKASYGYHRFLSDYDELTGWMEEKTALINADELPTDVASGEALLARHQQHKHEIDSYDDRFQTAEATGQDLLDGNHEASDEIREKMTILAHDWAALRELWNKCQHQYRQSLDFHLFYRDSEQVDSWMSRQEAFLENEDLGNSVGSVEALLQKHDDFEEAFTAQEEKIITLDETATKLIDNDHYDSENIAAIRDGLLARRDALRERAATRRKLLVDSQLLQQLYQDSDDLKTWINKKKKLADDEDYKDVQNLKSRVQKQQDFEEELAANEIMLNNLERTGQDMIENDHYASDAVAARMSEVANLWKELLEATAQKGTQLYEANQLLQFENNAEDLKRWLEEVERQVASEDYGKGLADVQNLLRKHGLLESAVLARQDQVDTLTDMAAHFEEIGHPDSENICARQESLLSRFEALKEPLATRKKKLIDLLKLQQICRDSEDEEAWIQETEPSAASTHLGKDLVAAKNLLNRHEVILADIASHEPRIQTITERGNKMVEEGHFASEDIASRVESLNKNMESLRARAIRRENDLKANVQLQQYLADLHEAEAWIKEKEPIVDNKNYGADEEAAGALLKKHEAFLVDLNAFGNSIKALGDQAEACQQQQAAPVDEAGREARVIALYDFEARSRREVSMKKNDVLTLLSSINKDWWKVEADDHQGFVPAVYVRKLAHDELPGFPQQRREEPVNIPQLQEQIETLYHSLLDRAEERRRRLLQRYNEFLLAYEAGDMLEWIQEKKTENTGVELDDVWELQKKFDEFQRDLKSNEPRLKDINKVADELLFEDLLTPEGSHIRQELNTRWSSLKRLADEQYQLLSSAHAVEMFLREADDVKEQIDKKCQALNAADPGSDLLSVQALQRQHEVFERDIIPLGEKVTTLGETAERLCESHPDATEDLQKQRTELNEAWDTLQGLTSDRKESLNEAHKFFLFLSKASDLENWIKAIGGVISSPELAEDLTGTEILLERHQEHYDDIKREDPTFQALEDFGRELIDRGHRNSHEIETTLQDIKLKRDDLEKNWENRKKMLDQCLELQLFRGKCEQVESWMVARENSLRSDDRDHLNSLQALMKKRDDLDKAIAAQEGKIADLENHATRLMDNDHYAKEEIAARLQRVLDRWKDLKTQLLAELGKLGDYADLKQFYRDLEDLEEWISEMLPVACDESYKDPTNIQRKYLKHQAFENEVNGRAEQVEGVINLGKSLIERRVCDGDEENMQEQLDKLKENWDYLLERTTDKGQKLNEASRQQRFNTSIRDFEFWLSEVIVPGKMGAYNLVNNQLSDLNLYHLSTLFLCPQKLLRVSSQDCGRDLQSVQNLLKKHRRLEGELVAHEPAVQNVLDTAESLKDKAAVGKEEIQERLAQFVQHWEKLKELAKTRGVNLEESLQYLQFMENAEEEEAWLGEKDALVSRGDSGDTLAATQSLLKKHEALENDFAVHKNRVQDVCAQGEDILSKEETQNKDKISTKIEVLNEKTASLTKALAAWKSQLDEVHAFQQFNWKADVVESWIGEKEASLKTKSNGADLTAFLTLLAKQDTLDASLQSFQQERLSEITDLKDELLAAEHSQSKAIEERHAALLRRWEQLLEACRVHRQKLLEKQLPLQKAEELFMEFAHKASAFNNWCENAEEDLSEPVHCVSLNEIRQLQKEHEAFLASMVGAQEDFNYLLALDQQIKALNVSSSPYTWLTVDVLGRIWKHLPEIIKEREQELQKEEARQIKNFEMCQEFEQNASAFLQWIQETRYAVSLLKETGTLESQLEANKRKQKEIQAMKRHLTKIEDLGDSMEEALILDIKYSTIGLAQQWDQLHQLGMRMQHNLEQQIQAKDTIGVSEETLKEFSTTYKHFDENLTGRLTHKEFRSCLRGLNYYLPMVEEGEPEPKFEKFLNAVDPGRKGYVSLEDYTSFLIDKESENIKTSDDIESGFQALAEGKAYITKEDMKQALTPEQVSFCTIHMQQYMDPRGRSQPAGYDYVGFTNSFFGN
Protein: S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase TYW1B (EC 4.1.3.44) (Radical S-adenosyl methionine and flavodoxin domain-containing protein 2) (tRNA wybutosine-synthesizing protein 1 homolog B) (Q6NUM6)
Organism: Homo sapiens (Human)
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Interaction partners:
Sequence:
MDPSADTWDLSSPLISLWINRFYIYLGFAVSISLWICVQIVIEMQGFATVLAEAVTSLDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRDAVFGLGNSAYASHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDVVKSKHGSIEANFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSQEQDELHHRDTKEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGRNEDGERRAMITPALREALTKQVDAPRERSLLQTHILWNESHRCMETTPSLACANKCVFCWWHHNNPVGTEWLWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHCALSLVGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDSLKKIDRPLFKDFWQQFLDSLKALAVKQQRTVYRLMLVKAWNVDELQAYAQLVSLGNPDFIEVKGVTYCRESSASSLTMAHVPWHEEVVQFVRELVDLIPEYEIACEHEHSNCLLIAHRKFKIGGEWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGANERSFDPKDTRHQRKNKSKAISGC
Protein: Transposon Ty1-LR1 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q12088)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISDIESTGSGGMHRLDVPLLAPMSQSNTHESSHASKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRSPSIDTSSSESNSLHHVVPIKTSDTCPKENTEESIIADLPLPDLPPEPPTELSDSFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIQAYHKEVNQLLKMKTWDTDRYYDRKEIDPKRVINSMFIFNRKRGGTHKARFVARGDIQHPDTYDPGMQSNTVHHYALMTSLSLASDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: SidF, inhibitor of growth family, member 3 (Q5ZSD5)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Interaction partners:
Sequence:
MPRITENIETYVTHLLSDLEPVPSQNQHLAYGYPGERQVFKDPMLDGKQVVVVNSQYDKHGRPVTGQPDVIQEANNYIDNLVAAAKSLIDKDKKGEKDLRKNAIDEMAKTFKKSISETIPSDKAKADLFSSKKSSANKDFLEQLAKVEGSLQQFTQAVAKASGHKLKALDKEGHNIRSHNRDTLIHRFKAPNSKEGEEQFIMYIPCGRYTKRQQRLMGKDESEVNRDHDTTSHKRSDLVLGNSSMARMIAGTRHSDGTVTIHHDSFSGPGARMPYSDFKGADDYKKLAIKAVTLINQEEVIQTLAQRQIDRMTNEDLWNKIPEEYRPDELPPDAEKARAQLIKLYVEHNPLSVTECYTQVVTAGQRVAAENQKEQFEYVRQMMDAFDGSKAKITIQTGSNTEVETAVGYQARMSSWGVNWFRQVGALNPLSDNSVTKNQNARFVNQMTDDVIRNLDKVAQNLGDYDKAGALHTLLKGPDVSDLNQQITEKENALKEVKGAYREALFSYFEEYQKGEGKWDQAKLDQLKNQVDGYEKSIKKQESAIYELHNQIDALRKAYYTEHKGQINKALQELKEQISPVIQNKETDPETKSRLQHFYNSCAYLTQAQELYYENTWHHGKNNFKLQTLMASLSCELDYANTKGCKSNNDRGQRLAQKIVGNALWTAMSEDGLYTGEFLDHRRTHGKEVSNVEQLDRELTTIQALHHTANTGVSGGKFEIQDKANFADNGLFGKVANFAKIKEMGPENAFTKNMGTKIKAGLGLGLLAAGGFVALTLLFPPAGLAVAALGIGVAAGAAIVAGVTFAATYLFGTAIDAINNKIEEGKIKSIVREGMKAASENSPQHKTEQKDHLTVNAKLHQQLGVTRESVLERQSTPKQEFEKPKDMTSKVDLTAAMEDDNRSESTPTPVNF
Protein: Testis-specific serine/threonine-protein kinase 3 (TSK-3) (TSSK-3) (Testis-specific kinase 3) (EC 2.7.11.1) (Serine/threonine-protein kinase 22C) (Q9D2E1)
Organism: Mus musculus (Mouse)
Function: May be involved in a signaling pathway during male germ cell development or mature sperm function.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:34623009}. Note=Localizes to the sperm flagellum in mature sperm. {ECO:0000269|PubMed:34623009}.
Interaction partners:
Sequence:
MEDFLLSNGYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKMGGPEEFIQRFLPRELQIVRTLDHKNIIQVYEMLESADGKIYLVMELAEGGDVFDCVLNGGPLPESRAKALFRQMVEAIRYCHGCGVAHRDLKCENALLQGFNLKLTDFGFAKVLPKSRRELSQTFCGSTAYAAPEVLQGIPHDSKKGDVWSMGVVLYVMLCASLPFDDTDIPKMLWQQQKGVSFPTHLGISTECQDLLKRLLEPDMILRPSIEEVSWHPWLAST
Protein: T. brucei spp.-specific protein (Q57V76)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPQTVQKRQTHGRSRRGYDFVLEGVPMYDSPDISSDSSDIERTRTMAPPHGQNWGPAAYPKPSAAGAVAPPYRHQKQQQQQQQQQQEHARQQLLLQQKWLEQQQAAFHQRQQELSRAEYQRSHKTQQQSQQSSHNHTETRDARRTIMGDSTGRGSRERCPPVDDIDYVKYFPERGPRVMEYTSPGFNTNPSTTVAQHIQSGHNAQFTTMRPSARSQQHLECPGNHNNTVVGAYGTGETADTRNTGARETAIVGGGVHYGAQSLQATGKCAARYASTLYLENDHPSAQVPNGYTVEMGNSGLFTLANYPDADKGAVTNENRFSGGAVKPRWTSVSTTPMECRTPPSVATAPQYRNTAACDSTGGDIFSGDYEFMPVELGQCDFRTLHAVTLSTEPTPPFTPSHASVESRGGKRNALLPPVGHRDLSYFESLPQKQQKQQRRTSKQGDVQDVSEASLPFAVPQEYQYLNNDLTDPNSSLPAPAMSVETTHKSEKAQTRKVIDSSNPRRWIVL
Protein: Alpha pinene synthase, chloroplastic (Cf-Pin) (EC 4.2.3.-) (C3RSF5)
Organism: Chamaecyparis formosensis (Formosan cypress) (Cupressus formosensis)
Function: Monoterpene synthase involved in the biosynthesis of volatile compounds (Ref.1). Mediates the conversion of (2E)-geranyl diphosphate (GPP) into alpha-pinene (Ref.1).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSLGCITPLASAMVGPKLVRPLIHHNPLFHHKPLNRPYLQTKIPLRSRVAQNPINMALITTDEGITRRIGNHHPNLWDDDFIQSLSKAYEAPSYGERAEKLIKDVRDMFNALPLHSSSADDLIQHLSLVDSVERLGIDRHFQNEIKTALDYVYRYWSDAGIGCGRESTHADLNTTALGFRILRLHRYSVSSDVLQQFVLRDGPFLDSNNQPNEDDIKNILNLFRGSLIAFPGENVLDDAKSFTMTYLKQVLPKISNLNLSREIKFNLEYGWHTNVPRLEARTYIDIYGEDSSWASKSINNIFYTKLLELAKLDFNIIQSLQQQELQILSRWWMESDLGKLDFARHRHVEYYLWAATGCIEPKYSAFRIGFAKLSALVTYLDDMYDTYDFDEIKIFTKAIKRWDASIIKGLPEFMKVAFKAFDEAVKDMAQEAKKTQGRDTLDYARKAWEVYIDAYMKEAEWLATGYMPSLEEYLENGKVSAGSRVVTLQPILSLDVPLSDDILKEIDYPSRFDELLCLTLRLRGDTRTFKAEADRGEVVSCITCYMKDHPGSNEEDALNYLNSLIDERLKELNWEYLKTDNVPIISKGNAYNLSKGLQLLYKERDGFTVFSIETKNFIYRMMIGSIPI
Protein: Transcriptional regulatory protein AlgP (Alginate regulatory protein AlgR3) (P15276)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: The promoter for a critical alginate biosynthetic gene, AlgD, encoding GDP-mannose dehydrogenase, is activated only under conditions reminiscent of the cystic fibrosis lung (i.e. under high osmolarity), and at least two regulatory genes, AlgP and AlgQ, have been implicated in this activation process.
Interaction partners:
- Transcriptional regulatory protein AlgQ
- GDP-mannose 6-dehydrogenase
- Positive alginate biosynthesis regulatory protein
- Peptidase S8/S53 domain-containing protein
- Nucleotide-diphospho-sugar transferase
- Alginate biosynthesis transcriptional regulatory protein AlgB
- Clp protease
- Probable transcriptional regulator
- Flagellar hook-length control protein-like C-terminal domain-containing protein
- Uncharacterized protein
Sequence:
MSANKKPVTTPLHLLQQLSHSLVEHLEGACKQALVDSEKLLAKLEKQRGKAQEKLHKARTKLQDAAKAGKTKAQAKARETISDLEEALDTLKARQADTRTYIVGLKRDVQESLKLAQGVGKVKEAAGKALESRKAKPATKPAAKAAAKPAVKTVAAKPAAKPAAKPAAKPAAKPAAKTAAAKPAAKPTAKPAAKPAAKPAAKTAAAKPAAKPAAKPVAKPAAKPAAKTAAAKPAAKPAAKPVAKPTAKPAAKTAAAKPAAKPAAKPAAKPAAKPVAKSAAAKPAAKPAAKPAAKPAAKPAAKPVAAKPAATKPATAPAAKPAATPSAPAAASSAASATPAAGSNGAAPTSAS
Protein: NADH-ubiquinone oxidoreductase chain 3 (EC 7.1.1.2) (NADH dehydrogenase subunit 3) (P03898)
Organism: Bos taurus (Bovine)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH-ubiquinone oxidoreductase chain 6
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 3
Sequence:
MNLMLALLTNFTLATLLVIIAFWLPQLNVYSEKTSPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIALLLPLPWASQTANLNTMLTMALFLIILLAVSLAYEWTQKGLEWTE
Protein: Interferon gamma receptor 1 (A0A2R8Y7R1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCGSIVQSLVPTPTNVTIESYNMNPIVYWEYQIMPQVPVFTVEVKNYGVKNSEWIDACINISHHYCNISDHVGDPSNSLWVRVKARVGQKESAYAKSEEFAVCRDGKIGPPKLDIRKEEKQIMIDIFHPSVFVNGDEQEVDYDPETTCYIRVYNVYVRMNGSEIQYKILTQKEDDCDEIQCQLAIPVSSLNSQYCVSAEGVLHVWGVTTEKSKEVCITIFNSSIKGSLWIPVVAALLLFLVLSLVFICFYIKKINPLKEKSIILPKSLISVVRSATLETKPESKYVSLITSYQPFSLEKEVVCEEPLSPATVPGMHTEDNPGKVEHTEELSSITEVVTTEENIPDVVPGSHLTPIERESSSPLSSNQSEPGSIALNSYHSRNCSESDHSRNGFDTDSSCLESHSSLSDSEFPPNNKGEIKTEGQELITVIKAPTSFGYDKPHVLVDLLVDDSGKESLIGYRPTEDSKEFS
Protein: EF-hand domain-containing protein (Q384N8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MATEQHQQQRQKMLNSKDLENALDYIATFGRPHKQDETLPLFNYIFDLKDKLIGRMSSHEDVRMFVESDAGRRMSEGLVKALDADGDGHVTPRDLQTIYESKLKGAIRNNSDTLDTVIPWAGQWLVGIGSGYLTGRVIRRVYARKYFITLAGATVYTGLQFLAQRNFIEQQLLEAAFKRKVKELADANGDGVVNADDLSYLVENRMRHVSTKLGFGGVAPGVLGYLALAVGMRRGLRRV
Protein: histidine kinase (EC 2.7.13.3) (Q1DDJ8)
Organism: Myxococcus xanthus (strain DK1622)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- histidine kinase
- Sensory/regulatory protein RpfC
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- Response regulator
- Response regulator/GGDEF domain protein
- DNA-binding response regulator
- DNA-binding reponse regulator
Sequence:
MAHNGSIGGHADMSSGRGINRCQGTEGDEPLSEAVVVLRSVRSAVGGIVDFECVSANVQAERWLGGEEGSLVHNRLLEEAPWAWDGGLFSACVRVVTRRAPEIARVSRQSPMGTVWLLARVSPCDDGVVLFLEDLTERMAAEEALRRDHDLLHAVIESATDAIYVKDVSGRYILINPATASAFHRAPREILGRTDAELLGADRAAPTLAHDREVMSSGHTATYEGAEGGPGTDRIWHTTKGVLRRGDGTVYGLFAICRDVTARRRQELEREEEARFQERFIGVLGHDLGNPLAAVRLSSAALLARDTLPPEVRRVVARIDGSAERMARLVKQLLDFTRARMAGGIPLRPHEVCMEDVCRRIISELEPAHPECCVRLEVDGESRGIWDEERLGQVLSNLLGNALQHSPEGSSVRVRLAAKDSLFQRVEVHNGGPPIPESLRPRLFSPFHGVPPEPGQPKPKHQGLGLGLYIVSQIVTAHGGWLDVASSADTGTCFSVTLPRVTRPLGGPPGKTA
Protein: Peroxisomal coenzyme A diphosphatase 1, peroxisomal (Pcd1p) (EC 3.6.1.-) (EC 3.6.1.77) (8-oxo-dGTP/2-hydroxy-dATP diphosphatase) (EC 3.6.1.56) (Q12524)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Coenzyme A diphosphatase which mediates the cleavage of CoA into 3',5'-ADP and 4'-phosphopantetheine. Has a strong preference for oxidized CoA disulfide (CoASSCoA) as substrate. May be required to remove potentially toxic oxidized CoA disulfide to maintain the capacity for beta-oxidation of fatty acids. Can degrade 8-oxo-dGTP in vitro; however, such activity may not be relevant in vivo.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10922370}.
Interaction partners:
- Mitochondrial-processing peptidase subunit alpha
- NAD-capped RNA hydrolase NPY1
- mRNA-decapping enzyme subunit 1
Sequence:
MILSQRRMLSSKQLIENLIRYKFHKTPYTRSSIWPFKRNSAVIILLFIGMKGELRVLLTKRSRTLRSFSGDVSFPGGKADYFQETFESVARREAEEEIGLPHDPEVLHKEFGMKLDNLVMDMPCYLSRTFLSVKPMVCFLYKDKLEKHEDKYKVPLDIRKFFGKLNPGETSSLFSVPLNDLVIHLLPEADEDVKSYQAEYFERKEYKLNWGGIKWLIMHYHFHVANNNEMPWLQTIEDLSSSDEDGVDGGIFRFRDLWGLTCKILFDVSCIANGLMDEKLKGELGHEDLIVGLHDYGNQMQPNGRSEWEIGMINGDRNLKYSDVIPEYYMKHLLECRSLW
Protein: Protein kinase domain-containing protein ppk9 (O13945)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit gamma
- 5'-AMP-activated protein kinase subunit beta
- Probable Rho-GTPase-activating protein 6
- Uncharacterized protein C227.15
- Tuberous sclerosis 2 protein homolog
Sequence:
MQTPSSASAESEKDSGNTYVGPWLLGRTLGQGNLAKVKLGKHFQTNEKVALKMVYNDELEDKDTWKRLQREVTILRQLHHPNIITLYQVFRVPKYTVLALEYMDTDLHSMVVKHNRLDECTTRKIFRQIVHAIDYCHLHRVAHRDLKLENILLNKDLVVKLTDFGLSNFMLDGSFLSTSCGTPHYAAPEVIQGRYYDGCDVDVWGCGILLYLMLVGEFPFEDVTISNVLSRVCKGIYTIPSFVSSSASDLIRQMLMVLPTSRIKVAEIMQHPWFIADLPTHSRLPSRTSSFSSKHRSVTFSPPDLAILFDPSITSPSSSVGQIPQPTDHSALSPSKPMSISGTESPNPDPASLCYSSYEDLYSATSWHSDMAESSGFLDPTDIPPIPSNVETLRSSLPQRHASFMNKVYNHPLSRPPAPNRLRSLRWHYGIQTAKNPIEVLRKLCEALLELGARFRPCDEESFLKENKYKVFSCITCHNSPVYLVIELFSIGPSASVIDIRFSSSDDSIKYTSSYSPMPFLEVVKQLILKIA
Protein: Suprabasin (Q8CIT9)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000269|PubMed:15256262}.
Interaction partners:
- Keratinocyte differentiation-associated protein
- Dermokine
Sequence:
MYLVSLLSSCCLLVLLGTLPARAAHEDPVEKVIEGFSRGLSNAEREVGKALEGINNGITQAGREVEKIFGELSNMGSQAGKNVEHGLDKVAHDINNGIGHAGKEAEKFAHGVNHAAGQVGKETNKIIHHGVSQGGSEAGKFGQGSHHAFGQGGNVANKLGHETHHAFGQGGNVAHKLGHETHHAFGQGGNVADKLGHGGNVADKLGHGTHHAFGQGGNVADKLGHETHHAFGQGGNVADKLGHGTHHAFGQGGNVADKLGHETHHAFGQGGNVAEKLGHETHHAFGQGGNMADKFGQGAHHAFGQGGNMADKFGQGAHHAFGQGGNMADKFGQGAHHAFGQGGNMADKFGQGAHHAFGQGGNMADKFGQGAHHAFGQGGNMADKFGQGAHHAFGQGRDMAETFDQGAHHAFGQGGREGGRLVQGAGQGLSHAAKEAQQFGHGHGHGYYAAGQTWQEGDKVIHPGVSQAGEEMEQFGQGVRHTIKQAEKEAEKVAHGVQNGVNQAQKEAEKVAHGVQNGVNQAQKEAEKVAHGVQNGVNQAQKEAEKVAHGVQTGVNQAGKETQRVGQGVQTGFNQGQKEAEKVAHGVQTGVNQAGKETQKAGQGVNYAAGQAEKEAEKLGQGVHHAAGQEMNRLQQDVHNGVNQPSKEANQLLNGSHQGQGGYGGQHGGAATTTVVSGASVNKPFINFPALWRSIAATMP
Protein: Fe(3+) dicitrate-binding periplasmic protein FecB (Iron(III) dicitrate-binding periplasmic protein) (P15028)
Organism: Escherichia coli (strain K12)
Function: Binds citrate-dependent Fe(3+); part of the binding-protein-dependent transport system for uptake of citrate-dependent Fe(3+).
Subcellular location: Periplasm {ECO:0000269|PubMed:2651410, ECO:0000269|PubMed:2836368}.
Interaction partners:
- Fe
- Fe
- Fe
- Fe
- Ferric citrate uptake sigma factor regulator FecR
- Iron
- Ferric citrate uptake sigma factor FecI
- Ferric enterobactin transport ATP-binding protein FepC
- Ferric enterobactin transport system permease protein FepD
- Iron
Sequence:
MLAFIRFLFAGLLLVISHAFAATVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVIPIGIADDNDAKRILPEVRAHLKPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQLPKGTRVAFGTSREQQFNLHTQETWTGSVLASLGLNVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQKQQVASVDSNTWARMRGIFAAERIAADTVKIFHHQPLTVVK
Protein: CCHC zinc finger protein (Q9GRG8)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MADNMQMSNARTCYNCGHAGHMSRECPNARSGGNMGGGRSCYNCGQPDHISRDCPNARTGGNMGGGRSCYNCGRPGHISRDCPNARSGGNMGGGRACYHCQQEGHIARECPNAPLDAAAGGRACFNCGQPGHLSRACPVK