wanglab/gogpt-training-data huggingface dataset:
Protein: RE28239p (Q7YU38)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVSRRKILSRSRDDLNLDQTFTQQEEEEDIWFQKDKLYKEHIQEVLDKWTQIDDEIWAKVIVFERNRRVAKAYARAPVLTINGSDDGFDGMRIGLCGFDNPMRDQKTDEMKRVIGQGVKIKMDDAGNILIRRYAKSNVYVKSTASSPNEETSIGAEILKLPNQALESEKIVKLFDMKKFQSNVNRELRRAYPDRRRLETQCLSAVAFVKSENDILECPIWVLIVNVVAMDMLKSKLPPVQRPIVDIKNRPRIPIPDEDPYSVAGNGSGGSSGSSGFGSGHQAQLHPQQQLGKHLNGNGGGHVAATREQLLLQTQQLAHKRSEKPPKLPPRDNIYSHDLIPKPDYDDIDLETRIKLSRGKSDKGKDNKKYDDPYYCGLRARVPNFVKSGKPIPAQVAKDQRDGNGNNIGNGGISTLSQKKTSMIHNHLGGMHPHHIQQQQLMAAAAAAHAAQNHHAGHQREQQQHHQIWQTRSYESGIDSELVESPYNHIYGRHLPLPTRGYVPTPRMFIGEWD
Protein: Bni4p (A0A1D8PD43)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Serine/threonine-protein phosphatase
- Chs4p
- Cell division control protein 10
- chitin synthase
- chitin synthase
- TATA-box-binding protein
- chitin synthase
- Myosin 2
- Septin
- Actin-related protein 2
Sequence:
MADSTFDEFFDNDFYSAPTSINNSKNHVKNVRNSIQIKHSMSSRSLNEFTKDIPPSATTGSITTKSNTQTNPSSSKAGNTSGSTRTSIIKASPSLKALESILNEKNKQYNTANTNIIEEVEEETEETEKVGKAKNHSQGLHSLSPPILFNYNNSNNRESVQTFETAIESLNEDDTLAVLSTNTSNSIGNNSNNNNNSNGYPLTTKTSKSSSVNSHKYNKSSISTISESGYSTDDTPIISQPLTFQSFTPHSFESPQLKMVDITEESNFENENSNSTITTNTIMAKNESKNNLFCGVSDGGVDVGSAGGGAQYNKNKFNANFSNKQIKENFHSSSQQSFQQQEHHHQPSFHQSPLNSTDQQMSPKSSEPLHPPRHVKHPTDTTTNTTTNNNNPFYNTTSHSNQNNLFNKNVSIPLNQPAYPGNNTTTTTNTNNHHHNKSNSYNNNYNIIRTVSNNSNSNMSLDSNFSSHSPSNNNSSRPKIVCKSKSMLTVLTNDNDSMSSSHTPPPRSPLPPQPTNDSVSLGSPHKRPSQPRSNSSYSIMKGKFNRKNSNTTTSTDFHPENKTLSHKRSNTLNDFSKLNKEQQPSSGVLPSTASTNSKSSNGKKKFSFKSLFKSKSKSHSLNESNSSISSEPKKMTSKSYSTPNMQMLSEQPKSIDDVEDTTNNEQSTKSESKAPLPTKTNTSFMNRFKKNKSSDSLNKLGSSHQQSGLKKGVSNSNPSLSSLNGNKPVVNSTNNNNLIQPNEEHSKFGLSAPPVNRNSFNFIREVSEDSVYIGDQNDDIEDEHSGEEDIKPSKKRQGYKDVGNIHNNSDDEEDDDNVDRLSNFKSIERGQERGASDDDDDDDDQEKEKDFDYYDAQNLTEDPPKKLSSGNKYGEEISLIPPLIDSNQFGSPFKVNYQSSPKSIDLKREAQHTNTNDDDDNSSPLQRTIKRFSGPPTSSSLIPIKPPSPIRYPQQQTNNNVHVTEDKPNTQLLGEALFPKSLNAHEVESIVSLERSRSMKSVKSNKRSSFVNYDGSDDNIVHYVGPISKPTTGNNGNNGITRSNSILKNSTSRKSNLNEELKMNSIDGTVSGTTNNNINNIDTSGNFKVINDTTTTNNDTFTTITDIGPSGGAIGQNILGSNNGFGDNSGIDTGDDDLMEFSEFIDVENMNFLDSPIRGSPINNNGKFMQSSTTPSSPLANYHFDNDSINKLQQQEEESQSQGKIVDQSTPEPPVIVINKDNLDDKPTTMESKLNSIPVITIPDKETIDISNKDSIDSKTPTSSPLSMKHDDSPKTSVEEKDDDQHQTSNEKANNNDIIDDQVIIASPILESAYRIKSQRSENGKFTKQNRPISMSFKGMNAPSFTGKLKKEALRSSDSHQSFNINFNDDDDGDDDSSLSVGGGFGSSSEDEDDDAYSFEQGNEISSASRFYNTNDDYIENKENRVPGSAHTNNSNSTANDKVSPLIPPPPTNSQPNIIAQPQSPAPSTKSSVFSPKQSNDINKKPLNQPPPPPSSSPPQTQQHFSLQPLKKFTHNKIPSISDQSSINSESSPRSFTSMISKKWGNRKNNNYNPSNSPNSNSSPKFNSIPPRPAPPPPPPPPPQVGKLQITNGVRFSSRIILYDTYNEDEYDRHPDTATCNQLTPLLAQQIKDELNSFKSEMEIHVESKCYTHFF
Protein: Coronatine-insensitive protein homolog 1a (OsCOI1a) (Q6Y9P5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in jasmonate (JA) signaling. Required for jasmonate signaling in plant defense responses. Can complement Arabidopsis coi1-1 mutant and restore jasmonate signaling. Required for JA-regulated defense responses to infestation by the leaffolder Cnaphalocrocis medinalis. May act on an initial response of jasmonate-regulated gene expression toward drought tolerance as part of a BHLH148-TIFY11D/JAZ12-COI1A complex. Component of SCF(COI1) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including TIFY/JAZ family (By similarity).
Interaction partners:
- Protein TIFY 3
- Protein TIFY 10a
- Protein TIFY 6a
- Protein TIFY 8
- Protein TIFY 10b
- Cullin-1
- Protein TIFY 6b
- Protein TIFY 11a
- Protein TIFY 11e
- SKP1-like protein 1
Sequence:
MGGEVPEPRRLNRALSFDDWVPDEALHLVMGHVEDPRDREAASRVCRRWHRIDALTRKHVTVAFCYAARPARLRERFPRLESLSLKGKPRAAMYGLIPDDWGAYAAPWIDELAAPLECLKALHLRRMTVTDADIAALVRARGHMLQELKLDKCIGFSTDALRLVARSCRSLRTLFLEECHITDKGGEWLHELAVNNSVLVTLNFYMTELKVAPADLELLAKNCKSLISLKMSECDLSDLISFFQTANALQDFAGGAFYEVGELTKYEKVKFPPRLCFLGLTYMGTNEMPVIFPFSMKLKKLDLQYTFLTTEDHCQIIAKCPNLLILEVRNVIGDRGLEVVGDTCKKLRRLRIERGDDDPGLQEEQGGVSQLGLTAVAVGCRELEYIAAYVSDITNGALESIGTFCKNLYDFRLVLLDRERQVTDLPLDNGVCALLRNCTKLRRFALYLRPGGLSDDGLSYIGQYSGNIQYMLLGNVGESDHGLIRFAVGCTNLQKLELRSCCFSERALSLAVLQMPSLRYIWVQGYRASQTGLDLLLMARPFWNIEFTPPSPESFNHMTEDGEPCVDSHAQVLAYYSLAGRRSDCPQWVIPLHPA
Protein: LD24318p (Uncharacterized protein, isoform A) (Q9VAF2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MOB kinase activator-like 4
- RRP15-like protein
- GH23506p
- Homeobox protein goosecoid
- Transcription elongation factor SPT6
- Dorsal interacting protein 4
- IP10578p
- Zinc finger protein 330 homolog
- RE31520p
- LD29420p
Sequence:
MVGKNFKALAHFHRLTEYIVQCKHCEKTLSSKHTSSNLTRHLIRNHKLLARSIFAGEEGKMLAELKDELEASASEDLSMELGEGETKSAVRGIMNAKLEQEQMERHSQEEMRNKVIGKNNKLWAHFIRISEFMAKCMHCGKTLSSKHSSSNLMRHIVRRHTSLAKTLNHSHQHLMTPKKDSYASLERRQAADPLEKVNFDDVDSIIEKVADHLEEEVTSISLQEPFYEYVVDNSDSVVVDRCDEPEPAEMQNMIPQDSASLAESTTQLDEKLKAETIYYNEMAELARAKRRLIDLQTKKLLLDMNVVDN
Protein: Nucleoside diphosphate kinase (EC 2.7.4.6) (Q7SXL4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Guanosine-3',5'-bis
- Ribonucleoside-diphosphate reductase large subunit
- Nucleoside-triphosphatase, cancer-related.
- Thymidylate kinase
- Adenylate kinase 9
- CTP synthase 1
- Cytidine monophosphate
- CTP synthase
- Deoxyuridine triphosphatase.
Sequence:
MAGKTERTFIAVKPDGVQRGLMGEIIKRFEQKGFRLVAAKFVQASEDLAKQHYIDLKDQPFYAGLVKYTSSGPLLAMVWEGLNVIKTGRVMLGETDPFASKPGTIRGDFCIEVGRNLIHGSDSEKSAATEVSLWFKPEELVSYRSCAQEWIYE
Protein: Phosphoribosylformylglycinamidine synthase subunit PurL (FGAM synthase) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase subunit II) (FGAR amidotransferase II) (FGAR-AT II) (Glutamine amidotransferase PurL) (Phosphoribosylformylglycinamidine synthase subunit II) (P12042)
Organism: Bacillus subtilis (strain 168)
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.
Interaction partners:
- N5-carboxyaminoimidazole ribonucleotide synthase
- Phosphoribosylamine--glycine ligase
- Phosphoribosylformylglycinamidine synthase subunit PurQ
- Phosphoribosylglycinamide formyltransferase
- Phosphoribosylformylglycinamidine cyclo-ligase
- Phosphoribosylformylglycinamidine synthase subunit PurS
- Bifunctional purine biosynthesis protein PurH
- Amidophosphoribosyltransferase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Adenylosuccinate lyase
Sequence:
MSLLLEPSKEQIKEEKLYQQMGVSDDEFALIESILGRLPNYTEIGIFSVMWSEHCSYKNSKPILRKFPTSGERVLQGPGEGAGIVDIGDNQAVVFKIESHNHPSALEPYQGAATGVGGIIRDVFSMGARPIAVLNSLRFGELTSPRVKYLFEEVVAGIAGYGNCIGIPTVGGEVQFDSSYEGNPLVNAMCVGLINHEDIKKGQAKGVGNTVMYVGAKTGRDGIHGATFASEEMSDSSEEKRSAVQVGDPFMEKLLLEACLEVIQCDALVGIQDMGAAGLTSSSAEMASKAGSGIEMNLDLIPQRETGMTAYEMMLSESQERMLLVIERGREQEIIDIFDKYDLEAVSVGHVTDDKMLRLTHKGEVVCELPVDALAEEAPVYHKPSQEPAYYREFLETDVPAPQIEDANEMLKALLQQPTIASKEWVYDQYDYMVRTNTVVAPGSDAGVLRIRGTKKALAMTTDCNARYLYLDPEVGGKIAVAEAARNIICSGAEPLAVTDNLNFGNPEKPEIFWQIEKAADGISEACNVLSTPVIGGNVSLYNESNGTAIYPTPVIGMVGLIEDTAHITTQHFKQAGDLVYVIGETKPEFAGSELQKMTEGRIYGKAPQIDLDVELSRQKALLDAIKKGFVQSAHDVSEGGLGVAIAESVMTTENLGANVTVEGEAALLFSESQSRFVVSVKKEHQAAFEATVKDAVHIGEVTADGILAIQNQDGQQMIHAQTKELERVWKGAIPCLLKSKA
Protein: Integrin alpha-7 (H36-alpha7) [Cleaved into: Integrin alpha-7 heavy chain; Integrin alpha-7 light chain; Integrin alpha-7 70 kDa form] (Q63258)
Organism: Rattus norvegicus (Rat)
Function: Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. Involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells (By similarity). Acts as Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin beta-1
- Integrin beta-3
- Integrin beta-4
- Paxillin
- Integrin subunit alpha 5
- Integrin alpha-9
- Myelin proteolipid protein
- Integrin subunit alpha 3
- Integrin alpha-6
- Vasodilator-stimulated phosphoprotein
Sequence:
MARIPRCDFLGLPGICYLLSFLLAGLLLPRASAFNLDVMGAIRKEGEPGSLFGFSVALHRQLQPRPQSWLLVGAPQALALPGQQANRTGGLFACPLSLEETDCYRVDIDRGANVQKESKENQWLGVSVRSQGAGGKVVTCAHRYESRQRVDQVLETRDVIGRCFVLSQDLAIRDELDGGEWKFCEGRPQGHEQFGFCQQGTAATFSPDSHYLIFGAPGTYNWKGLLFVTNIDSSDPDQLVYKTLDPADRLTGPAGDLTLNSYLGFSIDSGKGLMRSEELSFVAGAPRANHKGAVVILRKDSASRLIPEVVLSGERLTSGFGYSLAVTDLNSDGWADLIVGAPYFFERQEELGGAVYVYMNQGGHWADISPLRLCGSPDSMFGISLAVLGDLNQDGFPDIAVGAPFDGDGKVFIYHGSSLGVVTKPSQVLEGEAVGIKSFGYSLSGGLDVDGNHYPDLLVGSLADTAALFRARPVLHVSQEIFIDPRAIDLEQPNCADGRLVCVHVKVCFSYVAVPSSYSPIVVLDYVLDGDTDRRLRGQAPRVTFPGRGPDDLKHQSSGTVSLKHQHDRVCGDTVFQLQENVKDKLRAIVVTLSYGLQTPRLRRQAPDQGLPLVAPILNAHQPSTQRTEIHFLKQGCGDDKICQSNLQLAQAQFCSRISDTEFQALPMDLDGTALFALSGQPFIGLELTVTNLPSDPARPQADGDDAHEAQLLATLPASLRYSGVRTLDSVEKPLCLSNENASHVECELGNPMKRGTQVTFYLILSTSGITIETTELKVELLLATISEQDLHPVSVRAHVFIELPLSISGVATPQQLFFSGKVKGESAMRSERDVGSKVKYEVTVSNQGQSLNTLGSAFLNIMWPHEIANGKWLLYPMRVELEGGQGPEKKGICSPRPNILHLDVDSRDRRRRELGQPEPQEPPEKVEPSTSWWPVSSAEKRNVTLDCAQGTAKCVVFSCPLYSFDRAAVLHVWGRLWNSTFLEEYMSVKSLEVIVRANITVKSSIKNLLLRDASTVIPVMVYLDPVAVVAEGVPWWVILLAVLAGLLVLALLVLLLWKLGFFKRAKHPEATVPQYHAVKILREDRQQFKEEKTGTIQRSNWGNSQWEGSDAHPILAADWHPELGPDGHPVSVTA
Protein: TBC1 domain family member 23 (HCV non-structural protein 4A-transactivated protein 1) (Q9NUY8)
Organism: Homo sapiens (Human)
Function: Putative Rab GTPase-activating protein which plays a role in vesicular trafficking. Involved in endosome-to-Golgi trafficking. Acts as a bridging protein by binding simultaneously to golgins, including GOLGA1 and GOLGA4, located at the trans-Golgi, and to the WASH complex, located on endosome-derived vesicles. Together with WDR11 complex facilitates the golgin-mediated capture of vesicles generated using AP-1. Plays a role in brain development, including in cortical neuron positioning (By similarity). May also be important for neurite outgrowth, possibly through its involvement in membrane trafficking and cargo delivery, 2 processes that are essential for axonal and dendritic growth (By similarity). May act as a general inhibitor of innate immunity signaling, strongly inhibiting multiple TLR and dectin/CLEC7A-signaling pathways. Does not alter initial activation events, but instead affects maintenance of inflammatory gene expression several hours after bacterial lipopolysaccharide (LPS) challenge (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:28823706, ECO:0000269|PubMed:29084197, ECO:0000269|PubMed:29426865}. Cytoplasmic vesicle {ECO:0000269|PubMed:29426865}. Note=Localization to the trans-Golgi is regulated by ARL1 and ARL5B/ARL8. ARL1 increases Golgi localization, while ARL5B decreases it. Recruitment to the trans-Golgi network requires the presence of GOLGA1 and GOLGA4, but not that of FAM91A1 (PubMed:28823706, PubMed:29084197). Recruited on AP-1-derived vesicles by WDR11 complex (PubMed:29426865). {ECO:0000269|PubMed:28823706, ECO:0000269|PubMed:29084197, ECO:0000269|PubMed:29426865}.
Interaction partners:
- Protein Njmu-R1
- Protein FAM91A1
- Glutaredoxin-3
- tRNA N6-adenosine threonylcarbamoyltransferase
- Golgin subfamily A member 1
- Apoptosis inhibitor 5
- Golgin subfamily A member 4
- TBC1 domain family member 20
Sequence:
MAEGEDVPPLPTSSGDGWEKDLEEALEAGGCDLETLRNIIQGRPLPADLRAKVWKIALNVAGKGDSLASWDGILDLPEQNTIHKDCLQFIDQLSVPEEKAAELLLDIESVITFYCKSRNIKYSTSLSWIHLLKPLVHLQLPRSDLYNCFYAIMNKYIPRDCSQKGRPFHLFRLLIQYHEPELCSYLDTKKITPDSYALNWLGSLFACYCSTEVTQAIWDGYLQQADPFFIYFLMLIILVNAKEVILTQESDSKEEVIKFLENTPSSLNIEDIEDLFSLAQYYCSKTPASFRKDNHHLFGSTLLGIKDDDADLSQALCLAISVSEILQANQLQGEGVRFFVVDCRPAEQYNAGHLSTAFHLDSDLMLQNPSEFAQSVKSLLEAQKQSIESGSIAGGEHLCFMGSGREEEDMYMNMVLAHFLQKNKEYVSIASGGFMALQQHLADINVDGPENGYGHWIASTSGSRSSINSVDGESPNGSSDRGMKSLVNKMTVALKTKSVNVREKVISFIENTSTPVDRMSFNLPWPDRSCTERHVSSSDRVGKPYRGVKPVFSIGDEEEYDTDEIDSSSMSDDDRKEVVNIQTWINKPDVKHHFPCKEVKESGHMFPSHLLVTATHMYCLREIVSRKGLAYIQSRQALNSVVKITSKKKHPELITFKYGNSSASGIEILAIERYLIPNAGDATKAIKQQIMKVLDALES
Protein: L-2-aminoadipate reductase (EC 1.2.1.31) (EC 1.2.1.95) (Alpha-aminoadipate reductase) (Alpha-AR) (L-aminoadipate-semialdehyde dehydrogenase) (P07702)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Interaction partners:
- Histidine biosynthesis trifunctional protein
- Acyl carrier protein, mitochondrial
- Saccharopine dehydrogenase [NADP
- 3-isopropylmalate dehydrogenase
- Orotidine 5'-phosphate decarboxylase
- Imidazoleglycerol-phosphate dehydratase
- N-
- Phosphoribosylaminoimidazole carboxylase
- L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
- Aromatic/aminoadipate aminotransferase 1
Sequence:
MTNEKVWIEKLDNPTLSVLPHDFLRPQQEPYTKQATYSLQLPQLDVPHDSFSNKYAVALSVWAALIYRVTGDDDIVLYIANNKILRFNIQPTWSFNELYSTINNELNKLNSIEANFSFDELAEKIQSCQDLERTPQLFRLAFLENQDFKLDEFKHHLVDFALNLDTSNNAHVLNLIYNSLLYSNERVTIVADQFTQYLTAALSDPSNCITKISLITASSKDSLPDPTKNLGWCDFVGCIHDIFQDNAEAFPERTCVVETPTLNSDKSRSFTYRDINRTSNIVAHYLIKTGIKRGDVVMIYSSRGVDLMVCVMGVLKAGATFSVIDPAYPPARQTIYLGVAKPRGLIVIRAAGQLDQLVEDYINDELEIVSRINSIAIQENGTIEGGKLDNGEDVLAPYDHYKDTRTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFNWMSKRFNLTENDKFTMLSGIAHDPIQRDMFTPLFLGAQLYVPTQDDIGTPGRLAEWMSKYGCTVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENCRIVNMYGTTETQRAVSYFEVKSKNDDPNFLKKLKDVMPAGKGMLNVQLLVVNRNDRTQICGIGEIGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEKDHWNYLDKDNGEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRKNADNEPTLITFMVPRFDKPDDLSKFQSDVPKEVETDPIVKGLIGYHLLSKDIRTFLKKRLASYAMPSLIVVMDKLPLNPNGKVDKPKLQFPTPKQLNLVAENTVSETDDSQFTNVEREVRDLWLSILPTKPASVSPDDSFFDLGGHSILATKMIFTLKKKLQVDLPLGTIFKYPTIKAFAAEIDRIKSSGGSSQGEVVENVTANYAEDAKKLVETLPSSYPSREYFVEPNSAEGKTTINVFVTGVTGFLGSYILADLLGRSPKNYSFKVFAHVRAKDEEAAFARLQKAGITYGTWNEKFASNIKVVLGDLSKSQFGLSDEKWMDLANTVDIIIHNGALVHWVYPYAKLRDPNVISTINVMSLAAVGKPKFFDFVSSTSTLDTEYYFNLSDKLVSEGKPGILESDDLMNSASGLTGGYGQSKWAAEYIIRRAGERGLRGCIVRPGYVTGASANGSSNTDDFLLRFLKGSVQLGKIPDIENSVNMVPVDHVARVVVATSLNPPKENELAVAQVTGHPRILFKDYLYTLHDYGYDVEIESYSKWKKSLEASVIDRNEENALYPLLHMVLDNLPESTKAPELDDRNAVASLKKDTAWTGVDWSNGIGVTPEEVGIYIAFLNKVGFLPPPTHNDKLPLPSIELTQAQISLVASGAGARGSSAAA
Protein: UvrABC system protein A (UvrA protein) (Excinuclease ABC subunit A) (P0A698)
Organism: Escherichia coli (strain K12)
Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}.
Interaction partners:
- Transcription-repair-coupling factor
- UvrABC system protein C
- UvrABC system protein B
- DNA helicase II
- Holliday junction branch migration complex subunit RuvA
- Holliday junction branch migration complex subunit RuvB
- Protein RecA
- Crossover junction endodeoxyribonuclease RuvC
- DNA polymerase I
- DNA mismatch repair protein MutL
Sequence:
MDKIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKGEHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDPKAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDRRNFYYFQMLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYMNDRGDTSIRRHPFEGVLHNMERRYKETESSAVREELAKFISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVIDIGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRVPANPEKVLKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLNGATIAEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVPESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPML
Protein: RE57120p (Q7JZ62)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- BcDNA.GH12326
- Protein yippee-like
- GM09977p
- UBX domain-containing protein 7
- Caspar, isoform A
- Cullin 3, isoform F
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Sequence:
MSESMSGDHKILLKGHSSQYLKLNVGGHLYYTTIGTLTKNNDTMLSAMFSGRMEVLTDSEGWILIDRCGNHFGIILNYLRDGTVPLPETNKEIAELLAEAKYYCITELAISCERALYAHQEPKPICRIPLITSQKEEQLLLSVSLKPAVILVVQRQNNKYSYTSTSDDNLLKNIELFDKLSLRFNERILFIKDVIGPSEICCWSFYGHGKKVAEVCCTSIVYATDRKHTKVEFPEARIYEETLQVLLYENRNAPDQELMQATSSARVGSASGTSINQYTSDEEEERTGLARLRSNKRNNPS
Protein: Endonuclease/exonuclease/phosphatase family protein (F4IRT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDSVIIEPDEREALASLVPAHPLPPRKTHSYVEQCEQKPHHPIRKYSLDEGSRSVTSDSEAVYFDSSDGEFSTEGVAIVDGRTSGERGNGEECGFVTPPSKPASQGGGNDGGREDDIESLPEFIGAGGGLDVFKVPVRAAVNPGRPPCLELRPHPLRETQTGKFLRNIACTESQLWAGQENGVRFWNLEEAYEVGCGLGGQVRRGDEDTAPFHESVPTSPALCLLVDHGNRLVWTGHKDGKIRAWKMNQPNTTTADDSKPFKERLSWQAHRGPVNYIVISSYGDMWSCSDGGVIKIWTLDSLEKSLVLKLEEKHMAALLVERSGIDLRSQVTVNGTCSISSSDVKFLLVDTVKAKVWAVQHLSFSLWDAQNKELLKVFNIDGQVENRVDMPPTQGQQVEDTKAKFFSAPKKEKSQGFLQRSRHAIMGAAGAVRRAATRSAGAFAEDTRKVEAIAIAADGSIWTGSMNGVIAQWDGNGSRLREVNHHQQAVLCFCTFGDRIYVGYSSGYIQVLDLGGKLIASWVSHNEPVIKLAAGGGFIFSLATHGGVRGWYVTSPGPLDSLIRTELSQKEMAYARQDSVKILIGTWNVGEGRASRGALVSWLGSAVSDVGIVAIGLQEVDMGAGFLAMSTAKETVGVEGSAVGQWWLDAIGNALDERNTFERMGSRQLAGLLISLWVRKSIRTHVGDLDVAAVPCGFGRAIGNKGGVGLRIRVYDRIMCFVNCHLAAHLEAVTRRNADFNHIYRSMVFSKGQSVYTAAAAGASTSAQALKNNPNTNNSTEEEKSHLASADLVAFFGDFNYRLFGITYDEARDFISHRSFDWLREKDQLRQEMNEGKVFQGMREALITFPPTYKFEKNKPGLGGYDSGEKKRIPAWCDRVIYRDNQSISYTECSLKCPVVSSTIMYEACMDVTESDHKPVRCKLHANIAHTDKSVRRQELGKIVKSNEKLRAMFEELKSVPETSVSTNNILLHSQDTFIFTIRNTSNSSRAIFNIVCKGQTLVREDGEEPDNHSRGTFGLPRWLEVSPGAGIIKPDASLQVKVHHEDSHNSEEFIDGIQQNSLSEESSDKEVTLIIIVQGSCSTRTISHSIKVRHCSSAAKSLSLVHSKTTTMTKNLEGSTRYQTDANRDRRSSRTVKPSKEMHPVIVSSFSFLNSSDIRKGQIALRLFFRVQ
Protein: Legumin-like protein Mac i 2 (11S globulin seed storage protein Mac i 2) (allergen Mac i 2) (C0HLR7)
Organism: Macadamia integrifolia (Macadamia nut)
Function: Seed storage protein.
Interaction partners:
Sequence:
LSTLNTHNLPLLRLVYLEREDLVAVHVDDLNNQANQLDQKLDGGLLPQGHAPHWLMNAHSLFYLTRLLVAQCRAPKGMLVVLPAGVAHWCLNDGKHYLDNPR
Protein: EF-hand domain-containing family member C2 (A0A3Q1N1R0)
Organism: Bos taurus (Bovine)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37327785}.
Interaction partners:
- Tektin-2
- EF-hand calcium binding domain 6
- Calaxin
- Tektin bundle-interacting protein 1
- Parkin coregulated gene protein
- Outer dynein arm-docking complex subunit 4
- Outer dynein arm-docking complex subunit 1
- Outer dynein arm-docking complex subunit 3
- Tektin-3
- Outer dynein arm-docking complex subunit 2
Sequence:
MGKEKFHKSQHWGFCNNVRMLVGEDKPGIGGELLFGQKIKPKYSVFPKGMGTDSPSWVAFDKQVLSFDAYLEDEVPDKSQENYRIRRYKIYFYLEDDTVEVNEPVLQNSGLPQGIFIRRHRISLPPPNEDQFYTVHHFNVNTDIVFYGRTFKVYDCDAFTKNFLTKIGVKLNPPGQCPEDPYMKTRREKLDCMEPICPYESFDTLKQFLEYDRKVLRFFCVWDDSGSVFGDRRELILHYFLSDDTIEIKEVLPHNSGRDAMSLFLQRRKLPKYGPPGVYQPGQLTDQTVLNVYGGYSETRVYGFLLDKYQLGKLDQEFYKDTDLSIGTTINVWGRKVLLCDCDDFTKTYYRTKYGIENFTSIPCKAPSPPKIERKFPPYTGFGSEEDSLRSCIGLMPTPHQRNFKKFIEFDSYGNISNTLRFFAKLITHKCADVERMFVISYFLSDDTISVFEPIERNSGYTGGMFLKRVRVKKPGQEVFKSEFSEYIKAEELYVGAKVNVNGYLFFLVNADEYTLNYMERNSDKFPLSSIELVIQKLKEEECKSRELKQVFTAADCMHTKMVDFNTFREIMMNLTVGKLTDQEVITIARRYRVPEDPCPHRNVLVAQAHEQLKKNAFENFERLIAMCVYEDREKKKVLPSKDIKRLCKSSRLPLNEDLLGSLLSGFEDSEKQINYESFFCALNWRVNPVPVLEVASYIKERCEDEWLGMPSPIPVKYIYYLNLLKDVFGVDE
Protein: NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (HIRA-interacting protein 5) (mHIRIP5) (Q9QZ23)
Organism: Mus musculus (Mouse)
Function: Iron-sulfur cluster scaffold protein which can assemble [4Fe-4S] clusters and deliver them to target proteins.
Subcellular location: Mitochondrion {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- Iron-sulfur cluster assembly enzyme ISCU
- Cysteine desulfurase
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- Lipoyl synthase, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Ferredoxin-2, mitochondrial
- LYR motif-containing protein 4
Sequence:
MAAAERAWGAAVGVVRLCRRFCHVATPHTFKKQPLHQYVRRPLFPLRAPLCNTVRFMFIQTQDTPNPNSLKFIPGKPVLETRTMDFPTPAAAFRSPLARQLFRIEGVKSVFFGPDFITVTKENEELDWNLLKPDIYATIMDFFASGLPLVTEETPPPPGEAGSEEDDEVVAMIKELLDTRIRPTVQEDGGDVIYRGFEDGIVRLKLQGSCTSCPSSIITLKSGIQNMLQFYIPEVEGVEQVMDDDESDEKEANSS
Protein: Probable two-component response regulator (Q9HYP9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- STAS domain-containing protein
- HPt domain-containing protein
- histidine kinase
- Sensory/regulatory protein RpfC
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
Sequence:
MNPPAARIESLTILIAEDNAADRLLLSTIVSRQGHRVLTAGNGLEAVALFETERPQLVLMDVMMPVMDGFEAARRIKQQAGEELVPIIFLTSLSETEALVQSLEAGGDDFLSKPYNRVILEAKINAMGRLHLLQRTVLEQRDLIVRHNEHLLNEQRVAKAVFDKVAHSGCLNASNVRYLQSPLALFNGDLLLAAYKPSGGMHVLLGDFTGHGLPAAIGAMPLAEVFYGMTAKGYPMADILREMNAKLKRILPVGVFCCATLLNLSFQRELVEVWNGGLPDGYLLRAASGERVALVSRHLPLGILEPAAFSDRCETYPLDIEDRIFLFSDGVLEASNKAGEMFGEARLLQLFERNRQPSALFDEIQRSLAQFRGAVQDDVSMLEVRLQPDSGLQCPPLAFSDSGVSSPLDWSVSFEFRAETLKHFNPLPHVLQLLLEVHDLRARGGALYTVLAELYSNALEHGVIGLDSTMKSDAAGFARYYQERVSRLQALRDGYVRLHLDLAPHGAGGRLLVRVEDSGEGFDVERALNAVERQERLCGRGLRLIRELSDRCQWSADGKVVSVEFFWSPQA
Protein: Vesicle-associated membrane protein 2 (Q7SZZ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046280}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00046280}.
Interaction partners:
- Synaptosomal-associated protein 25-A
- Syntaxin 1A
- Synaptosomal-associated protein 25-B
- Synaptotagmin
- Synaptosomal-associated protein
- Syntaxin 4
- Syntaxin 1B
- Ras-related protein Rab-3
- Vesicular glutamate transporter 1
- Syntaxin-binding protein 1a
Sequence:
MSAPAGAPAPEGGNQAPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKNKYWWKNAKMMIILGVICVIVLIIIIVYFST
Protein: Thioredoxin-3 (Trx-3) (P29447)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Interaction partners:
- Thioredoxin domain-containing protein
- Glutaredoxin
Sequence:
MSKVIHVTSNEELDKYLQHQRVVVDFSAEWCGPCRAIAPVFDKLSNEFTTFTFVHVDIDKVNTHPIVKEIRSVPTFYFYVNGAKVSEFSGANEATLRSTLEANI