wanglab/gogpt-training-data huggingface dataset:
Protein: Retinoic acid-induced protein 1 (Q61818)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator of the circadian clock components: CLOCK, BMAL1, BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation.
Subcellular location: Cytoplasm. Nucleus. Note=In neurons, localized to neurites.
Interaction partners:
Sequence:
MQSFRERCGFHGKQQNYPQTSQETSRLENYRQPGQAGLSCDRQRLLAKDYYSPQPYTGYEGGTGTPSGTVATAAADKYHRGSKSLQGRPAFPSYVQDSSPYPGRYSGEEGLQTWGGPQPPPPQPQPLPGAVSKYEENLMKKTVVPPPNRQYPEQGPQLPFRTHSLHVPPPQPQQPLAYPKLQRQKPQNDLASPLPFPQGSHFPQHSQSFPTSSTYAPTVQGGGQGAHSYKSCTAPSAQPHDRPMSANANLAPGQRVQNLHAYQPGRLGYEQQQQALQGRHHTQETLHYQNLAKYQHYGQQGQGYCPPDTAVRTPEQYYQTFSPSSSHSPARSVGRSPSYSSTPSPLMPNLENFPYSQQPLSTGAFPTGITDHSHFMPLLNPSPTDAASSVDPQAGNCKPLQKEKLPDNLLSDLSLQSLTALTSQVENISNTVQQLLLSKATMPQKKGVKNLVSRTPEQHKSQHCSPEGSGYSAEPAGTPLSEPPSSTPQSTHAEPQDTDYLSGSEDPLERSFLYCSQARGSPARVNSNSKAKPESVSTCSVTSPDDMSTKSDDSFQSLHSTLPLDSFSKFVAGERDCPRLLLSALAQEDLASEILGLQEAIVEKADKAWAEASSLPKDNGKPPFSLENHGACLDTVAKTSWSQPGEPETLPEPLQLDKGGSTKDFSPGLFEDPSVAFATTDPKKTSSPLSFGTKPLLGTATPDPTTAAFDCFPDTPTASSVDGANPFAWPEENLGDACPRWGLHPGELTKGLEQGAKASDGVGKADAHEASACMGFQEDHAIGKPAAALSGDFKQQEAEGVKEEVGGLLQCPEVAKANQWLEESRHCCSSTDFGDLPLLPPPGRKEDLEAEEEYSSLCELLGSPEQRPSLQDPLSPKAPLMCTKEEAEEALDTKAGWVSPCHLSGEPAVLLGPSVGAQSKVQSWFESSLSHMKPGEEGPEMERAPGSSGTSQGSLAPKPNKPAVPEGPIAKKEPVPRGKSLRSRRVHRGLPEAEDSPCRVPALPKDLLLPESCTGPPQGQAEGAGAPGRGLSEGLPRMCTRSLTALSEPQTPGPPGLTTTPTPPDKLGGKQRAAFKSGKRVGKPSPKAASSPSNPAALPVASDSSPMGSKTKEPDSPSMPGKDQRSMVLRSRTKPQQVFHAKRRRPSESRIPDCRATKKLPANNHLPTAYKVSSGPQKEGRMNQRVKVPKPGTGNKLSDRPLHTLKRKSAFMAPVPAKKRSLILRSNNGSGGDGREERAESSPGLLRRMASPQRARPRGSGEPPPPPPLEPPAACMGLSTQSSLPSAVRTKVLPPRKGRGLKLEAIVQKITSPGLKKLACRVAGAPPGTPRSPALPERRPGGSPAGAEEGLGGMGQMLPAASGADPLCRNPASRSLKGKLLNSKKLSSAADCPKAEAFMSPETLPSLGTARAPKKRSRKGRTGTLGPSKGPLEKRPCPGQPLLLAPHDRASSTQGGGEDNSSGGGKKPKTEELGPASQPPEGRPCQPQTRAQKQPGQASYSSYSKRKRLSRGRGKTAHASPCKGRATRRRQQQVLPLDPAEPEIRLKYISSCKRLRADSRTPAFSPFVRVEKRDAYTTICTVVNSPGDEPKPHWKPSSSAASSSTSSSSLEPAGASLTTFPGGSVLQQRPSLPLSSTMHLGPVVSKALSTSCLVCCLCQNPANFKDLGDLCGPYYPEHCLPKKKPKLKEKARLEGTLEEASLPLERTLKGLECSASTTAAAPTTATITTPTALGRLSRPDGPADPAKQGPLRTSARGLSRRLQSCYCCDGQGDGGEEVAQADKSRKHECSKEAPTEPGGDTQEHWVHEACAVWTSGVYLVAGKLFGLQEAMKVAVDMPCTSCHEPGATISCSYKGCIHTYHYPCANDTGCTFIEENFTLKCPKHKRLPL
Protein: Solute carrier family 12 member 6 (Electroneutral potassium-chloride cotransporter 3) (K-Cl cotransporter 3) (Q924N4)
Organism: Mus musculus (Mouse)
Function: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells (Probable).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9UHW9}. Basolateral cell membrane {ECO:0000269|PubMed:16048901}; Multi-pass membrane protein {ECO:0000269|PubMed:16048901}.
Interaction partners:
- STE20/SPS1-related proline-alanine-rich protein kinase
- Serine/threonine-protein kinase OSR1
Sequence:
MHPPEATTKMSSVRFMVTPTKIDDIPGLSDTSPDLSSRSSSRVRFSSRESVPETSRSEPMSELSGATTSLATVALDPSSDRTSNPQDVTEDPSQNSITGEHSQLLDDGHKKARNAYLNNSNYEEGDEYFDKNLALFEEEMDTRPKVSSLLNRMANYTNLTQGAKEHEEAENITEGKKKPTKSPQMGTFMGVYLPCLQNIFGVILFLRLTWVVGTAGILQAFAIVLICCCCTMLTAISMSAIATNGVVPAGGSYFMISRALGPEFGGAVGLCFYLGTTFAAAMYILGAIEIFLVYIVPRAAIFRSDDALKESAAMLNNMRVYGTAFLVLMVLVVFIGVRYVNKFASLFLACVIVSILAIYAGAIKSSFAPPHFPVCMLGNRTLSSRHLDICSKTKEVDNMTVPSKLWGFFCNSSQFFNATCDEYFVHNNVISIQGIPGLASGIITENLWSNYLPKGEIIEKPSAKSSDVLGNLNHEYVLADITTSFTLLVGIFFPSVTGIMAGSNRSGDLKDAQKSIPIGTILAILTTSFVYLSNVVLFGACIEGVVLRDKFGDAVKGNLVVGTLSWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIAKDNIIPFLRVFGHSKANGEPTWALLLTAAIAELGILIASLDLVAPILSMFFLMCYLFVNLACALQTLLRTPNWRPRFRYYHWALSFMGMSICLALMFISSWYYAIVAMVIAGMIYKYIEYQGAEKEWGDGIRGLSLSAARFALLRLEEGPPHTKNWRPQLLVLLKLDEDLHVKHPRLLTFASQLKAGKGLTIVGSVIVGNFLENYGDALAAEQTIKHLMEAEKVKGFCQLVVAAKLKEGISHLIQSCGLGGMKHNTVVMGWPNGWRQSEDARAWKTFIGTVRVTTAAHLALLVAKNVSFFPSNVEQFSEGNIDVWWIVHDGGMLMLLPFLLKQHKVWRKCSIRIFTVAQLEDNSIQMKKDLATFLYHLRIEAEVEVVEMHDSDISAYTYERTLMMEQRSQMLRHMRLSKTERDREAQLVKDRNSMLRLTSIGSDEDEETETYQEKVHMTWTKDKYMASRGQKVKSMEGFQDLLNMRPDQSNVRRMHTAVKLNEVIVNKSHEAKLVLLNMPGPPRNPEGDENYMEFLEVLTEGLERVLLVRGGGSEVITIYS
Protein: Innexin-10 (Protein opu-10) (Q22549)
Organism: Caenorhabditis elegans
Function: Structural component of the gap junctions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000250}.
Interaction partners:
Sequence:
MVLAAVLSMLRYVGGSDDRDFVDRLHSYFTCNLLIGLAVLVSFKQFGGKPVECLVPDIFSSSWEQYAENYCWASDTYYVPTNEPVAGLQSDEKRQRKISYYQWVPFFLLLEAACFRLPSLLWKYLAGHSGIKINEIVKLSSDPNNIKPDIKRANIKSLTVHLQGALRFHRRLQKKQIRPHRFLWLFNLPYSAFFVTAMYLCTKFFYLANVCLQLMFMNRFLETDKYKWYGMGALVDLLNGTTWEQSGMFPRVSLCDFDVRVMGNMQEHTIQCVLVINIFNEKIFILLWFWYLALLVFTFGSFFYWLLVSLWRHLNVRFIIRHLEMSDIAFDSSEDGAQEKVNRFISNYLKSDGVFVIRMMTLQSGVIFGTDLVQELWRNFHGSEPQLKRSNSAPKIEEREQWWPAYPSLVNPINPWRYRDENQANALRWRRALGANVDNSIATQDLMEKLLPQNAHMRPSDDELLNRQPIAVQASYIDDESDGKLKNEEKQNQQNATQPPYCYTNQNPTPYQNQNQIQNQNQYSNYYRTPSLSRGTDSRPVSTATDTDQTKKQSMSTFK
Protein: Uncharacterized Nudix hydrolase YfcD (EC 3.6.-.-) (P65556)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Phosphodiesterase YfcE
- Pantothenate synthetase
Sequence:
MEQRRLASTEWVDIVNEENEVIAQASREQMRAQCLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARREAEEELGIAGVPFAEHGQFYFEDKNCRVWGALFSCVSHGPFALQEDEVSEVCWLTPEEITARCDEFTPDSLKALALWMKRNAKNEAVETETAE
Protein: Bifunctional epoxide hydrolase 2 [Includes: Cytosolic epoxide hydrolase 2 (CEH) (EC 3.3.2.10) (Epoxide hydratase) (Soluble epoxide hydrolase) (SEH); Lipid-phosphate phosphatase (EC 3.1.3.76)] (P34913)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators.
Subcellular location: Cytoplasm. Peroxisome.
Interaction partners:
- Cytochrome P450 2J2))
- Cytochrome P450 2C8
- Cytochrome P450 2C9
- Cytochrome P450 2B6
- Purine nucleoside phosphorylase
- Inosine-5'-monophosphate dehydrogenase 2
- S-methyl-5'-thioadenosine phosphorylase
- NAD-capped RNA hydrolase NUDT12
- GMP reductase 2
- Inosine-5'-monophosphate dehydrogenase 1
Sequence:
MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM
Protein: Response regulator aspartate phosphatase H (EC 3.1.3.-) (PSP28) (Q59HN8)
Organism: Bacillus subtilis (strain 168)
Function: Dual specificity regulatory protein that can control both sporulation and competence by acting on two distinct response regulators: Spo0F and ComA, respectively. Is involved in the temporal separation of competence and sporulation. Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity. RapH can also antagonize sporulation by sterically blocking phosphoryl transfer to and from Spo0F. In addition, inhibits the activity of ComA, a transcriptional factor that regulates the development of genetic competence. Acts by binding to ComA, leading to the inhibition of its DNA-binding activity.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sporulation initiation phosphotransferase F
- Phosphatase RapH inhibitor
- Transcriptional regulatory protein ComA
- Transcriptional regulatory protein DegU
- RapF inhibitor
- HTH-type transcriptional repressor RghR
- Competence and sporulation stimulating factor
Sequence:
MSQAIPSSRVGVKINEWYKMIRQFSVPDAEILKAEVEQDIQQMEEDQDLLIYYSLMCFRHQLMLDYLEPGKTYGNRPTVTELLETIETPQKKLTGLLKYYSLFFRGMYEFDQKEYVEAIGYYREAEKELPFVSDDIEKAEFHFKVAEAYYHMKQTHVSMYHILQALDIYQNHPLYSIRTIQSLFVIAGNYDDFKHYDKALPHLEAALELAMDIQNDRFIAISLLNIANSYDRSGDDQMAVEHFQKAAKVSREKVPDLLPKVLFGLSWTLCKAGQTQKAFQFIEEGLDHITARSHKFYKELFLFLQAVYKETVDERKIHDLLSYFEKKNLHAYIEACARSAAAVFESSCHFEQAAAFYRKVLKAQEDILKGECLYAY
Protein: Putative eukaryotic translation initiation factor 4 gamma (Q4QEK5)
Organism: Leishmania major
Interaction partners:
- Probable eukaryotic initiation factor 4A
- Putative eukaryotic translation initiation factor eIF-4E
- Polyadenylate-binding protein
- Polyadenylate-binding protein
- Poly
- Putative eukaryotic translation initiation factor 4e
- Putative eukaryotic translation initiation factor
Sequence:
MQFTVEQIRSVRNNYLEPPYPGFSLDEVVRRRRLTQTKLVRGENAWVAKGTAQTTEEWVQRLLHGTLNKLTEENKDIMIDKLLTKELFATEDIMNMVVNIIFKKALDEPENSKLYAGVCHSLALYEAKVLRDGHKGERPQSQLRDAIISTAQHEFRTLSKELSKMEDKSEEELEYERSNVMRRKRSNMRFIGELYLCTALTHSTMFTVMDLTMRCSDKTGFPSSENIELLAALLNTIGDRLDKNHKKTLDPYFTSLENFNKKSDCPYPPRIRFKIMDLLDLRKRGWGLKPKPVKAALPPSHGKDKKYATAPPPKKGGRDQGSAAAASKSWRDAATTKTGTAAAPAPSADKGLNGRGTSSAAPAANTAALSSSAASTAAATAPAGASFRDEASPQVPLVKFELRVASMFQEWVADRTNDVILHWVDQFNTCDRFFESESELCVAVAQEVIHSACTTTRKDAQREAFSFLVVGLYMIDTEVFDGFASALASAIEDGLLEDVPKFGERFMSMLRLTSTEQETRADVYFDAANVLRLTYNRLESPDDSAVDTLMSFWDRVPLPSTDEENMIRMDLDVVYSLCNPEGVQDGLEKLLSRIIHSMLQMQLMDAEVLDEFLCLDVEDGLCAKVIADYKERFPK
Protein: Regulator of V-ATPase in vacuolar membrane protein 2 (Q03956)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the RAVE complex, which is required for stable assembly of the vacuolar ATPase complex V-ATPase under many conditions. May be required for transport between the early endosome and the late endosome/prevacuolar compartment (PVC).
Subcellular location: Cytoplasm {ECO:0000305}. Early endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=May be membrane-associated and localize to early endosomes via its interaction with RAV1.
Interaction partners:
- Regulator of V-ATPase in vacuolar membrane protein 1
- Suppressor of kinetochore protein 1
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit C
- Putative uncharacterized protein YDR203W
Sequence:
MSVDLFPNDRFGAEDKYDNFKDAVKECSWLIEEIVKPQLPNIIDNFSKCLEMLESDQIFKMPVSNGIPNESNKQNDSPTVKGVITRQGQYIVDFHIVVRFPQFQRGKQVMFRMNTGLNFLLIQFSKIMTHLKNILEILNQLQVATDVSEFVSKFGVAMELLNHSLILLQNPPRDLVFPEDNNFAMKEMFQDCYSVCESTAHILGLELTLCRNELCIELRNLIKVTKKPWCEIDSKTGRSFCDQIRNQVTNERNKTLSKILSENGVQVQDSTLLNHIISSFQSEAITLPEAQELLRRGVTFDNRVVMECEKLIVSTSDPTLISISAKLNSLKASMANHQANLVASKQLSTYK
Protein: Dynein, 78 kDa intermediate chain, flagellar outer arm (IC78) (Q39578)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Is essential for arm assembly or attachment to the outer doublet microtubule.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme.
Interaction partners:
Sequence:
MPALSPAKKGTDKGKTGKKTGKQEQNAQDYIPPPPPMPGDEAFAMPIREIVKPDNQLWLSEADLNEEVAKMLTANNPAAPKNIVRFNMKDKVFKLEPMVEQTVVHYATDGWLLHKSSDEAKRQMDMEKMEQEASARFQADIDRASHEHKDHGDVEPPDDSRQLRNQFNFSERAAQTLNYPLRDRETFTEPPPTATVSGACTQWEIYDEYIKDLERQRIDEAMKSKGGKKAAAAARAAGAAHRQRNEHVPTLQSPTLMHSLGTLDRMVNQNMYEEVAMDFKYWDDASDAFRPGEGSLLPLWRFVSDKSKRRQVTSVCWNPLYDDMFAVGYGSYEFLKQASGLINIYSLKNPSHPEYTFHTESGVMCVHFHPEFANLLAVGCYDGSVLVYDVRLKKDEPIYQASVRTGKLNDPVWQIYWQPDDAQKSLQFVSISSDGAVNLWTLTKSELIPECLMKLRVVRAGETREEEDPNASGAAGGCCMDFCKMPGQESIYLVGTEEGAIHRCSKAYSSQYLSTYVSHHLAVYAVHWNNIHPSMFLSASCRLDHQAVGLCHDPKRAVMNFDLNDSIGDVSWAALQPTVFAAVTDDGRVHVFDLAQNKLLPLCSQKVVKKAKLTKLVFNPKHPIVLVGDDKGCVTSLKLSPNLRITSKPEKGQKFEDLEVAKLDGVVEIARKSDADLAKNAAH
Protein: Chaotic nuclear migration protein 67 (P53865)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required for the proper formation of the spindle pole body (SPB) outer plaque. May connect the outer plaque to the central plaque embedded in the nuclear envelope.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:9571234}. Note=Localizes to the meiotic outer plaque of the SPB, at the end of the meiotic spindles.
Interaction partners:
- Spindle pole body component SPC42
- Spindle pole body component 110
- Spindle pole component 29
- Gamma tubulin complex adapter SPC72
- Protein NUD1
- Sporulation-specific protein 21
- Spindle pole component BBP1
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Spindle pole body component SPC97
- Meiotic plaque component protein 54
Sequence:
MTDFDLMNFPFHERLDSPVSENGEIKDGEPIPQNWLNENHVGKSILPLFVNPEDVINCNFSNARDSYEENKSPSMDQMNYARNTSYQESPGLQERPKNEKDKSPIGTDVHKKDVPNFIHSTPRENSSKHFTRANEQASAQPTDEHTSPDISIEDCNGAKIFLQNSLSKEDFRMLENVILGYQKKVIELGRDNLRQEERANSLQKELEAATKSNDKTLDNKKKIEEQTVLIENLTKDLSLNKEMLEKANDTIQTKHTALLSLTDSLRKAELFEIPIGILFFDLYDSEENSSKLDHILQEKYPNIKGFLCASQQEELSRISQRFKNAKAEAEDLRNELENKKIEIQTMREKNNTLIGTNKTLSKQNKILCDKFDKLTIDEKEILKGCNEEIKIKLERLNERLGSWEKSKEKYETSLKDKEKMLADAEKKTNTLSKELDNLRSRFGNLEGNTSERITIKNILQSRPDISAEECNFLMVEQIDSANLTTLQNTVKEIVLAVGIPYPKLRRKIPLLAIKLKYENIMLSNFAQRLHRQVYSQEMNLKKFTDQAYYDFMSTRRMDSIDHHLERCLDHLYDHILEKMVK
Protein: Protein phosphatase 1, regulatory subunit 13B (A0A0G2KB61)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cellular tumor antigen p53
- Cellular tumor antigen p53
- Tumor protein 63
- Tumor protein p73
- Protein phosphatase 1, regulatory subunit 26
- Hypoxia-inducible factor 1-alpha inhibitor
- Ras association domain family member 8
Sequence:
MMPMILTVFLSNNEQILTEVPITPETTCRDVVEFCKEPGEGGCHLAEVWRGSERPIPCDHMMYEHLQKWGPRREEVKFFLRHEDSPTESSEQGARQSQEQRTQRNVMNVPGEKHTENGVGNPRVELTLSELQDMAARQQQQIESQQQMLVAKEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLKKGKLNGFQSYNGRLTGPAAVELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRNMEVAMMDKRISELRERLYGKKIQLNRVNGTSSPQSPLSTSGRVAAVGPYIQVPSTGGFPLPGDPVKPQSLTIASSAAHGRSKSANDGNWPTLKQNSASVKSTQMAGGDWKDSGMEGTLKQGAISSQPLPLSALGATDKLGIEIGKGPPPIPGVGKPLPPSYGTYPSPGPLGPGSTSSLERRKEGSLPRPAAGPPSRQKPAPLPPAGSAPQPSSSQQIQQRISVPPSPTYPPAGPPAFPAGDGKPELPLTVAIRPFLADKGSRPQSPRKGPQTVNSSSIYSMYLQQATPPKNYQPPAHGTLNKSVKAVYGKPVLPSGSASPSPLPFLHGSLGTGTTQPQPPSECAEKEAEPEGPSVPGEGSTVESLPRPLSPTKLTPIVHSPLRYQSDADLEALRRKLANAPRPLKKRSSITEPEGPGGPNIQKLLYQRFNTLAGGMEGTPFYQPSPSQDFVGTLADVDNGNTNANGNLDESFPPRPTAPLPDELAPSSDANDNELPSPEPEELICPQTTHQTAEPTEDNNNNVATVPSTEQIPSPVAEAPSEEDQVPPAPLSPVVHPPTASASKRTNLKKPNSERTGHGLRVRFNPLALLLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWTPLHCAASCNSVHLCKQLVESGAAIFASTISDIETAADKCEEMEEGYIQCSQFLYGVQEKLGVMNKGIVYALWDYEAQNNDELSFHEGDAITILRRKDENETEWWWARLGDREGYVPKNLLGLYPRIKPRQRTLA
Protein: DNA relaxase MbeA (EC 5.6.2.1) (DNA nickase) (Mobilization protein MbeA) (P13658)
Organism: Escherichia coli
Function: Relaxase involved in plasmid ColE1 conjugative mobilization and is thus essential to promote the specific transfer of the plasmid during conjugation. First catalyzes the specific cleavage of one of the DNA strands at oriT, forming a covalent 5'-phosphotyrosine intermediate. The nic site corresponds to 5'-(1469)CTGG/CTTA(1462)-3' in the cleaved strand. The cleaved strand is then transferred through the dedicated type IV secretion apparatus. MbeA remains covalently linked at the 5' end of the strand, and once in the recipient cell, it probably catalyzes the rejoining of the two ends of the strand, re-forming the circular plasmid DNA. Is functional in vitro without a requirement for the conjugative accessory proteins.
Interaction partners:
Sequence:
MIVKFHARGKGGGSGPVDYLLGRERNREGATVLQGNPEEVRELIDATPFAKKYTSGVLSFAEKELPPGGREKVMASFERVLMPGLEKNQYSILWVEHQDKGRLELNFVIPNMELQTGKRLQPYYDRADRPRIDAWQTLVNHHYGLHDPNAPENRRTLTLPDNLPETKQALAEGVTRGIDALYHAGEIKGRQDVIQALTEAGLEVVRVTRTSISIADPNGGKNIRLKGAFYEQSFADGRGVREKAERESRIYRENAEQRVQEARRICKRGCDIKRDENQRRYSPVHSLDRGIAGKTPGRGERGDDAAQEGRVKAGREYGHDVTGDSLSPVYREWRDALVSWREDTGEPGRNQEAGRDIAETEREDMGRGVCAGREQEIPCPSVREISGGDSLSGERVGTSEGVTQSDRAGNTFAERLRAAATGLYAAAERMGERLRGIAEDVFAYATGQRDAERAGHAVESAGAALERADRTLEPVIQRELEIREERLIQEREHVLSLERERQPEIQERTLDGPSLGW
Protein: Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (F1M110)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Acyl-CoA-binding domain-containing protein 6
- G protein subunit alpha transducin 1
Sequence:
MRRRRNTPKEALEGIWEQKRKRRNRREKRRSQTLGVPSPTPHLTPRRLRFSSLLNTTPSGSRFQQEQPWNPTIPIQKLQDIQRAMELLSACQGPARNIDEATKRRYQFWDTQPVPKLNEVITSHGAIEPDKDNIRQEPYSLPQGFMWDTLDLSNAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKRMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPVATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIRAVRELINVYLKQFHLAPVMGDEEVAHWFLPREHIIDTFVVESPSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMNDALIIAKLKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ
Protein: GM18993p (Transcript 48, isoform A) (Transcript 48, isoform B) (Q9VBA5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Rho guanine nucleotide exchange factor 2, isoform D
Sequence:
MRSVEVAQSGPSAIFWLVQVLIVGAAQAATPFAKEYRNAGLYNGNTLVDLDGSTTLDMGQEKPTSSSSGLSGGFKSESSVVLPGMLQNSGCPLTTSSHCLRCNKVGCIKCPMYLVTDTRQCVDQCPAGYLDQWSAHTEFMGRVCVPTGYSGPLMAALAGLLGGFLVCLSLLAVAVMLVKRKRRRKSIKQKLINENTMDRADFMRQLNEMRPNAEYFLAMLNDTRRQIRKLYLSGEVAAANSYRPIVRDLAKLLILLNRPIELIPAPPPDWSRLYAWSEQALERYKPQVGQLIDFFQASHGHSAGHHEVLYAAPNKKKQLQQPSIFRQQVTPTATPQGVGELMAGDRSSSASAQQKLHLFGSLISLHEFEEPRASDPFGSSFNTLKSGNLISDLNASSLWLEDEFYKLGFRPQDEITTEL
Protein: Uncharacterized vacuolar membrane protein YNL115C (P53925)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized protein YNL108C
- Uncharacterized protein YIL067C
- Protein UIP5
- Vacuolar membrane protein YOR292C
Sequence:
MKANGLDNDPARTGMERTDIDSEHPEAQPLLNNNHRTLGAGSANGPAVNEGRDIESDGFIKDSLFQIRKGYRIFIHNSKWILNILILINTIWLVTTLISDFFFNINILFGFSNRYASFNDLTLIFISIIANSFNLWFNKLGLYSALDYSLNVTLCVLTLFNLALTYLIKYTRQRIGFVGTFTYLWTSFSFFIGAILDWYLLFYNNSINEPLEERRIDDANISTFNENHTNSTENRDRSQYGSGSPTPTHRSQLVQNKHTLTEWVSIGFRNTIKFLILIFFALFTLNTLLTTLDTYRLTHKLPITVQSPSYEAFHYVDAAKTYQLHITCYGDVFDQENNTDLSENKKQPIILFEHGGYDTGYLSATWIEELYHLDKIQRYCLYDRPGYGLSDSPPAPISIAMVAESLRYALIKDAKIKGPFTTVGYDLGGLFTRVFTAKNVDIVDSMMLVESWHEELLLKNYIQRLLPPGRGDGDDGDDGNGNDGDGRNHDKTWLPSEIERHNEFRLWWKGIWSSLGWRLQTSWLLAHHGSKERIYGRDMKYQGRFLRSKFLESVTSSILSYRDVTNNAESLQNVKTSIVSSKEMVKKSALWGDWQRDLTKISHKTQEWKIVEGGHEIYKYGLGKQQTQEVLLRLIGELGKLTED
Protein: Protein TIC 21, chloroplastic (Protein CHLOROPLAST IMPORT APPARATUS 5) (AtCIA5) (Protein PERMEASE IN CHLOROPLASTS 1) (AtPIC1) (Translocon at the inner envelope membrane of chloroplasts 21) (AtTIC21) (Q9SHU7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in chloroplast protein import across the inner envelope membrane. Acts also as a chloroplast permease regulating the iron transport and homeostasis. Involved in the uptake and sequestration of iron in plastids.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein TIC 22, chloroplastic
- Protein TIC110, chloroplastic
- Protein TIC 40, chloroplastic
- Protein TOC75-3, chloroplastic
- ABC transporter I family member 11, chloroplastic
- Protein TIC 55, chloroplastic
- Protein TIC 56, chloroplastic
- Protein TIC 100
- Ferric reduction oxidase 7, chloroplastic
- Solute carrier family 40 member 3, chloroplastic
Sequence:
MQSLLLPPASSSGVSAVALRPGFQHSFNHQSLSTRSLPLFNPLLLAPKKKTTISSYQSPPSLSVYGFQIGGSKPSFTPSTVAFSYPTSPSSVPGDNEVDKAKLAQVAKRLEKTSRYFKRLGSIGFWGQLVSTVVAAVILSFSIVVTGKPTSPATFYATASGIAAAFVSVFWSFGYIRLSERLRRTSIDPAKAPPRADVVKGLRSGIMVNILGMGSALLGMQATVGFLVAKALTTSANPFYQGVSQGYSPVLALDVFLVQASANTLLSHFLGLVCSLELLRSVTVPNSESVVVPKVA
Protein: RE63573p (TweedleH) (Q9VBD4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRVLIALCLVAAVSARSGYNYQPAASAPAVASFAPSGPSYSPSVAASQDAPAETYAPASAPEAAPSAVATNYAAPQAELQKEFFTYTADEQDFVEPAGSQQVSASLNKALRVIFIKGPENTGLENAAVALAKQAGQQETAIYVLNKQADIGDLSNKLNSIRNNNNNKPEVHFVKYRTNQDALNAQQAIQSQYDQLGGSSTILNGGVAPVLNFASQPAAQQVAAPSAPGSSYLPASVLRFRQ
Protein: Solute carrier family 41 member (D6RDB0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU369007}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU369007}.
Interaction partners:
Sequence:
MDGTETRQRRLDSCGKPGELGLPHPLSTGGLPVASEDGALRAPESQSVTPKPLETEPSRETTWSIGLQVTVPFMFAGLGLSWAGMLLDYFQGKKLRGFSCELTRSPHGVLPESFFTIMCQVVVPILLSGLCMMTAGLVMNTIQHWPVFVEVKDLLTLVPPLVGLKGNLEMTLASRLSTAANTGQIDDPQEQHRVISSNLALIQVQATVVGLLAAVAALLLGVVSREEVDVAKVELLCASSVLTAFLAAFALGVLMVCIVIGARKLGVNPDNIATPIAASLGDLITLSI
Protein: Forkhead box P2 (Forkhead box protein P2) (Q4JNX5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Contactin-associated protein 2b.
Sequence:
MMQESANETISNSSMSQNGMSSLSSQLDAGSRDGRSSGETSSEVSAVELLHLQQQQALQAARQLLLQQPGSGLKSPKNNDKQRPLQVPVSVAMMSPQVITPQQMQQILQQQVLSPQQLQALLQQQQAVMLQQQHLQEFYKKQQEQLHLQLLQQQHPGKQAKEQQQQQQQLAAQQLVFQQQLLQMQQLQQQQHLLNMQRQGLLSMPPGPGQPTLPGQTLPPAGLSPAELQQLWKDVTASHTMEDNGMKHSGLDLSTNNNTSTTSTSNPKASPPITHHSMSNGQSPALNNNRRESSLHEETAVSHSLYGHGVCKWPGCESICDDFGQFLKHLNNEHALDDRSTAQCRVQMQVVQQLEIQLSKERERLQAMMAHLHMRPSEPKPSPKPLNLVSSVTMSKNLPSISPPNLPQTPTTPTAPVTPLSQMPQVPNVLSPANVPSMGAMRRRHTDKYSMALSSEIAPNYEFYKNADVRPPFTYATLIRQAIMESSDMQLTLNEIYSWFTRTFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEMEYQKRRSQKITGSPTLVKNLPSSLGYGAALNASLQAALAETTLPLLGNPGLMNSASAMMGASPPVMMSGSPTGLLQGTTHEELNGTLDHLDTNGHSSPGYSPHTHLPPIHVKEEPLNMEDEDCPMSLVTTANHSPELDDDRELEEGNLSEDLE
Protein: Citrate synthase (A0A060WFK8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
- malate synthase
- Malate dehydrogenase
- Malate dehydrogenase
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- Cytoplasmic aconitate hydratase
Sequence:
MNHKNVSNLRYVLSNLVPKEQSRIKNFKTQYGKTNIGSISVDMIYGGIRGMKGLVYETSVLDADEGIRFCGYSIPEYQQLLPKAPGRAEPLPEGLFWLLVTGQVPTDEQVNWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFAQAYSEGVNKAKYWWEFVYEDSMDLIAKLPCVAAKIYRNLYREGSSIGAIDSSLDWSHNFTNMLGYRDATFTELMRLYLTIHSDHEGGNMSAHTSHLEVLVWLTALQKEMGGEVSDEAMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYTCQQEFAFKHLPDDPIFKLVHQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTNGLMTLVGANNSGKDEVSKEEGGEGKEEQKGQVEGRGMHKMQYTYEKKGLCWIYVNNYCSLEFFFFFIAVCLWRCGCCTFFT
Protein: Uncharacterized amino-acid permease PB24D3.02c (Q9C0Z0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Zinc-type alcohol dehydrogenase-like protein PB24D3.08c
Sequence:
MDETIGMKKEFHDISVGDIEVGESAPVTEDDKMLLNLGYKQEFKREFSLLAVFGQSFGSMGLCPSLVGSMAFSMNCGAGGMVWSWFVGATCLLPIAFALSELASSMPTSGSLYFWTAYLSPPKYRAFLSWFLGYVLALAYSTGFASTIYAAAGLVQATASVANPSYAPTKYEEYGIYVALSFACSALIVLPTKFLARFSSFNVVFQICTILIFIISLAASSTSETRNTGSYIFGNFENYSGWTNMGWSFILCFTTPVWVLSGFESCATIVEEAKNASKAAPIAIISSLTVSLFMGFCIMITIAGTMGHDFSSILNTPYGEPVSQVLYNNLGKRGAVGVSAVLIIALCFNCSALCLASSREIFAFARDKGLPGSWIFRKLTPGGIPLNAILLVNLYTIIVGLLMLVNVTAISSIFNLAIIAFFISYSLPLVCRLLFNRLNPGKFYCGKFSKPISIVAVAWLWFMALMLLFPSYQNPNKVEMNWAIVVLGFTVFFCVGYYYLPKYGGKTFFKGPVKTVDENVTEGVTVDFQADHVSKEDDGKSYN