wanglab/gogpt-training-data huggingface dataset:
Protein: Regulator of G-protein signaling 5 (RGS5) (O15539)
Organism: Homo sapiens (Human)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha (By similarity).
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:15670159}. Membrane {ECO:0000269|PubMed:15670159}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:15670159}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Rho guanine nucleotide exchange factor 11
- Rho guanine nucleotide exchange factor 1
- Regulator of G-protein signaling protein-like
- Beta-adrenergic receptor kinase 1
Sequence:
MCKGLAALPHSCLERAKEIKIKLGILLQKPDSVGDLVIPYNEKPEKPAKTQKTSLDEALQWRDSLDKLLQNNYGLASFKSFLKSEFSEENLEFWIACEDYKKIKSPAKMAEKAKQIYEEFIQTEAPKEVNIDHFTKDITMKNLVEPSLSSFDMAQKRIHALMEKDSLPRFVRSEFYQELIK
Protein: ATP-dependent Clp protease proteolytic subunit (F4IAG5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAGLAISPPLGLSFSSRTRNPKPTSFLSHNQRNPIRRIVSALQSPYGDSLKAGLSSNVSGSPIKIDNKAPSSLPLPILNILKSSTVYFIFGVIEAKKGNPPVMPSVMTPGGPLDLSSVLFRNRIIFIGQPINAQVAQRVISQLVTLASIDDKSDILMYLNCPGGSTYSVLAIYDCMSWIKPKVGTVAFGVAASQGALLLAGGEKGMRYAMPNTRVMIHQPQTGCGGHVEDVRRQVNEAIEARQKIDRMYAAFTGQPLEKVQQYTERDRFLSASEALEFGLIDGLLETEY
Protein: D-alanine--D-alanine ligase (Q38FZ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Histone H3, putative
- Histone H3 variant
- Uncharacterized protein
- Histone H4
- Histone H4
- Polyubiquitin, putative
- Histone H2A
- Histone H2A
Sequence:
MKQIAHYFRIKTAKHAVLEAGDNIRELCSVLSFPLIIKHVSGYSSVGMDKSCKVYDMDSLHSRVTRFIEQYQIALVEEFVVGDEATILVCADSTQPDGIRVFPPVMVQFPEGEDFKHFHLKWETYEGMEWRLMPEDDPALSQVLSTARTSFMHMMGGVGYGRVDVRIDRSTHDVVFLEINPNCGVMYPPGQEGSADWILRLTPGFNQREFTLLQIKEALRRNERMQPLFRCVYNPAQGYRMCATRDISAGSPIFEAEGQSVRLYTKPHVKATRGKEEYDQFAQKAWPLGGDGHYYALWDNEPTNWRTFSHSCVPNMNFGPNRSLNLYATRDIARGEELTMDYRLFRDETTPPFQCCCGSECCEGWIAMNGGKLTKEENGNNY
Protein: Retinol-binding protein 4-A (Plasma retinol-binding protein 1) (PRBP-1) (Plasma retinol-binding protein II) (PRBP-I) (P24774)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: RBP delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.
Subcellular location: Secreted {ECO:0000269|PubMed:1740159}.
Interaction partners:
Sequence:
SDCQVSNIQVMQNFDRSRYTGRWYAVAKKDPVGLFLLDNVVAQFSVDESGKVTATAHGRVIILNNWEMCANMFGTFEDTPDPAKFKMRYWGAASYLQTGNDDHWVIDTDYDNYAIHYSCREVDLDGTCLDGYSFIFSRHPTGLRPEDQKIVTDKKKEICFLGKYRRVGHTGFCESS
Protein: RNA-editing complex protein MP63 (Q95W14)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MYRRFFRSAAVKHLGTTSAQCLMRATKYPCGAMCRNASSCHPQTLGYQQRFQSTTDKKFHCSVCKKPFRLEMAAKLHLQQAHGGDGSVEAGPGPGVEASSVNVVNTPVPSPISPVERTFVDEEERRPRRMRPTPKPLHQPDRDIPAAAMEEMLGVWDKIGLNRLEGNFVHSTMVMKVFAAPPDVSEIPLYEHVAPEGENPFDSLDHMTTGTVDATYVGHDAFAEVDLVDPFVAAPDQTLNPFRAGKVRNPFTRISPTQREVVKPLQPPQPKEEPLKAPVTPFGQLPMFGQTREPSASFAAAAVSVQAAANPNEVSSPFAAAVSSSPFVGQVASPFAPAQDVAGSPFEASPCAASSPFVTAGGQETSPFAAPSTPASFGQGSLFPPMGTGAPGFYLQLLRLSSANRSWSTGCPTCGKKFSTFEGAAMHSKSKHGIVLESKKVKDRLNRKGVPDLPAYVPSPVDLSSTSPFGTRSAIGASWAETELIPHAQCVSNITIVGRVLDVSQASENVSHVTVFVEGERSGEEETLTLCCFGEVSQKIRGTLKRNATIFASGTLRLHPVYEASNNKYYVSPVVHVSMPTGTLAVIT
Protein: Subtilisin-like protease 2 (EC 3.4.21.62) (Merozoite surface sheddase) (MESH) (PfSUB2) (Q8IHZ5)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Serine protease which plays an essential role in the shedding of AMA1, MSP1 and MSP7 from the surface of the invading merozoite; this step is essential for productive invasion and the release of the adhesion between the erythrocyte and the merozoite. May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23834729}; Single-pass type I membrane protein {ECO:0000305|PubMed:23834729}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:23834729}; Single-pass type I membrane protein {ECO:0000305|PubMed:23834729}. Note=In mature schizonts, localizes to micronemes at the merozoite apical region (PubMed:23834729). Immediately after schizont rupture, secreted from the micronemes to the merozoite surface where it redistributes in an actin-dependent manner to accumulate at the posterior end of newly released merozoites (PubMed:23834729). {ECO:0000269|PubMed:23834729}.
Interaction partners:
- Subtilisin-like protease 1
- Rh5-interacting protein
Sequence:
MLNIIYVVSLILIKFIFYKECNNNNNYYLSNIELYNYKLRKRNRILNNNINDRKSFLSDLEQNYKPLFDIYELSANFEKRRKELEKKTKGEENEIEKKKENDLEKKKENEIEKKKENDLEKEYNDVINLLELSLSSEYKELNADVSNNDNSGHEENNKHKLNKKNSSNYKNDKSLDELIKGAILKLKQNPNIKNKNMLDYDKIFKIIKEKLINKNLASNKIKGGDNEKLKEEKKQSDISTNVEVKKDIINDQLNKGIPTKKENKDDMINKESNKEDITNEGKSNSLNNLNTLNNDGNIITKVYDHYTIVTNSNDILNDISIDASDISKNSIGGINIPFNENDNSSFTHQRYIVLSNNGEKKYKIVLMTKNPKFMDMDGIYDEEEKKESLIELNQKVNKEENTNLYDGTGTLYYGKKSKKEKENTQQKGGNNPNVDINILNNNNNNNNNNNSNNNSNSMNDEEINYNNNNNNKESPSMFRRFINFLSFSGNENETEDTLIYHNKNDNSYKNKKEGTGKNNDNNDPNNNNNKKILLNVDKLVDQYLLNLKNNHTSKQELILVLKGELDLHSKNMKNVINNAKKNLEKYFKEHFKEFDKISYDISTPINFLCIFIPTLFDMNNMDLLKQALLILHNDLHEYVENWSFSSTYHTYEADYIKEQDSVYDRSPKKKYIKASKKLYNNKYSFLNKFLNIEPLILFAKKLNSKRSNIEKEILNFLPKELRDYSTWNLSIIRVFNAWFLAGYGNKNVKVCVVDSGADINHVDLNGNLYIPEYNEKYEMTQDFYNFMVKNPTDASGHGTHVTGIIGGVANDLGVVGVAPNITLISLRFIDGKKYGGSFHAIKALNVCILNKAPIINASWGSSHFDVNLHLAVERLKYTLNGKGSVLIAASGNKSNDNDISPLYPATFTFPHVYSVASISRNFEISPFSNYGHKSVHILAPGHHIYSTIPNNSYKIFTGTSMAAPHVCGVSALVYSVCYNQGFIPQAEEVLDILTRTSIKIISTKKRTINDSLVNAEGAVLTTLLGGLWMQMDCYFVKFNLEKGKKKHIPVVFSAYKKGVYETDIVIAIIPIDGKSKIYGEIHIPIKIVTDVNIPNFQESPRRGKNYTIDSNEAQHDEVLSYICENALYNLYEYDSHYLLASVILFFLALLSIFVGMIYMKSRKHSDKKCSKNLIKSNYIPEMDDGMEETQQLQQERRQYFRELFGENLEKNYDQHFVQDFGQDFRQDFKLGSTPDLKQYSDIDLQNKIQQPERKTVKIIINNFEDRKKETKRRLLKGLNYDGENAKKHDFTNESISNSRKNFKFSNNTEMKKNTIKSEDVKIASDDNVNKAMNQLDDMFMK
Protein: Large ribosomal subunit protein mL50 (39S ribosomal protein L50, mitochondrial) (L50mt) (MRP-L50) (Q8VDT9)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q8N5N7}.
Interaction partners:
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein mL53
- Large ribosomal subunit protein mL39
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL37
- Small ribosomal subunit protein bS18m
- Large ribosomal subunit protein mL51
- Large ribosomal subunit protein mL44
- Small ribosomal subunit protein mS22
Sequence:
MAALIVSRLARRGWLWKLPLATRREFWSRSRKEKEPVVAETVEEVKKEPVLVCPPLRSRAYTPPSDLQSRLESHIKEVLGSSLPNNWQDISLDDGHMKFRLLAGLADGLGHAVPNSRLHQMCRVRDVLDFYNVPVQDKSKFDELVASNLPPNLKISWSY
Protein: Peroxiredoxin-2 (EC 1.11.1.24) (Natural killer cell-enhancing factor B) (NKEF-B) (PRP) (Thiol-specific antioxidant protein) (TSA) (Thioredoxin peroxidase 1) (Thioredoxin-dependent peroxide reductase 1) (Thioredoxin-dependent peroxiredoxin 2) (P32119)
Organism: Homo sapiens (Human)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9497357}.
Interaction partners:
- Thioredoxin
- Peroxiredoxin-5, mitochondrial
- Sulfiredoxin-1
- Peroxiredoxin-1
- Parkinson disease protein 7
- Superoxide dismutase
- Cyclin-dependent kinase 5
- Peroxiredoxin-6
- Cyclin-dependent kinase 5 activator 1
- Glutathione peroxidase 7
Sequence:
MASGNARIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFSKHN
Protein: ABC transporter C family member 13 (ABC transporter ABCC.13) (Q54V86)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- ABC transporter G family member 19
Sequence:
MFERINKIKKKIKEKLSYSILKDEKIDYYNLPCPEESASFLSKLTFSWTQRMLMTGYFRGPIQMSDICDLPDDVKVQKTNPILDDIDFGNSKWPLLKFIYTNFVTKNKKSIFIVILCAIFSILSPLCLKYFIKYIQLSKNEKTFLTGLGYCVLLFVGTFSYTLSQQFLYWFGMRTSLHVRGALSQRIYEKMLKLSSSGGKKYSSGSIMNLISTDIGLFADFFWIGHLEIIIFPIQITALLALLCWIVGWSGLVGFGVMIISLPINTFFGSKMSKNLMLSLGYSDTRCNLTSEFINGIRFLKLYAWEKLFLDRIEEQRRLQLKYLYRRVIFAIFEKMLSQTTNAVVLVSTFSVYSINNEIELSVAFTAITIFVNLRQPIMRLPEAIHNLLGLIPSAKRVESFLQLSEIQTQPFINFNNKSINDDILIDNGTFNWNQDNDDYITNNGDNNNNNNKNEIKKRLIEKSEEEYETTTTTTDDNNNNNYESYLLNNINFKAPAGKLTIICGVVGSGKTSLVSGLIGEIYKVSGRVNTPNKISFTTQQSFLLSTSLRENILFGNEMNLERYKKVIEACCLAPDLLQLAAKDLTEIGERGINLSGGQKQRISLARALYANSDCYILDEPLSAVDPEVATHLFNHCIQGMMNDKTRILVTHQLQFIPSADHIVVVDNGKLVQGTYSELKSKGIDFESIMKTKKLNIDNQQQQQQQQQHDENEIIDENPMKKSNSLIESNKLINIDEIISDKHDSNLIEKAKLLVKEDKSEGAIGLHVYREYFKHGSSTFFFIATCVVYFFSQAIFQMTDFWLSTWSQHKLQGKSDSFYIFYYIIFIGLFIVTLVIRYFMLAHVTFSASKNLHTSLLNSVGFASCQFFDTNPSGRILNRFSKDIAEIDLLLYDLFSDVLYCGSTVVFAICVMIYISPLISLPFLVLIIVYNIIKNIYAVSSRDLKRYESITRSPIFSLLQETFNGLVTIRSYQQQNRFISMMQDHININLRLFYYSFSIHRWIGVRLEFISALVVFLTAFFSLFNSNAGFSVLSVTTAIGMCTYLNWAVRQFVELEVKMNSVERIESYINTPKEGNRFTIDNEEEGEENMINLNEKWPSKGEIEFRDVEIRYRPTSEPSLKNLSFKINSNDHIGIVGRTGAGKSTVGISLFRMVECSKGSILIDGIDISKIGLHDLRSSLGIVPQDPFIFSGTIRLNIDPFNKYTDSEIWVALEKVKLKSTISSMPLKLETMIEEGGDGLSFGQKQLLCLSRTILKNSKVVLMDEATSGIDYVTGDLIKQTLLENFNDCTMLTIAHRLDTIIDSTKIAVVDKGELIEYDTPINLINTKNSKFSKLVKYQTDFHKENEKNF
Protein: transketolase (EC 2.2.1.1) (Q95S19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPNTCVIYDNEEPFTIGRGKVVRQKSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCGGRVVVVEDHYQQGGLGEAVLSALAGERNFVVKHLYVPTVPRSGPPSVLIDMFGISARHVVNAVNEILKD
Protein: FACT complex subunit (Q580R3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367052}. Chromosome {ECO:0000256|RuleBase:RU367052}.
Interaction partners:
- Histone chaperone RTT106/FACT complex subunit SPT16-like middle domain-containing protein
- Cell division control protein 73 C-terminal domain-containing protein
- Transcription initiation protein, putative
- RNA polymerase-associated protein CTR9
- Histone H2A
- Spt4/RpoE2 zinc finger domain-containing protein
- Uncharacterized protein
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- Casein kinase II subunit beta
Sequence:
MEKIVNAWRKVPDAAEGCSVMCCVFGALTPETLENQRGQAMLQYLFTSLNTVCNAALFFSFDKLLVVHSNLNVELPPSSESFTYASATLDEKFGEILAAFVADAKVGVCQKELNIQEGDFAPKLISVVREIVPAERTVEVGPLLGEFLFVKDEAALSCVEKAAGLCNAIFRRSARGMIESEMQKSNPKTLSALREQLTKTLEAPNTVMGLETLDVSQFSIASGLTPCIMHRGTYNPQISVTEVSTQPLRSDVIVVRYGLKNCGYTAFIARTLIAERNAPSNVKDVYKFVYNVTEKLLEHLRVGTRLSAVHEEVMKYATTTDEALAKHLPKSLGFSTGLLVLEARGTISQKGTATVEDGMAFVTRVTLEGVPDGEGGTFDVELSDTVTVKGGAAQLNTKTSRKLEEVLYDDSAEEETAFETSARDLNKITRQGQSSVPLLSRESAREEKLKTLLRELHAELAAAGGKKAKTAVSEEFRTYEIARLSYGDVIPYANETSFPDVARGGGIYVDTEKEVAFFPVCGGVAAFHVSTISRVDVKFEGNQVAGIFSFHSLQEGNIAYRLNRTKIFVKELTYRARRDIFTDVKIAIQGIQQRIKNRDTERRRVSLNAGGAQLQTVPDAIRLPQVKIRPPATTGRYNKECIGNLEIHRNGLRFSYIGGAPIDMHFENIKHVIFQPAVNAVRVIYHITLKKGVEIARKSVDEVQFVAEVMESSETVMAARKGYEEEIAAEERELMRISDTNKQFLKFAQAVERVSMIKTQIPASNFSFEGVHAKGLTTFKANREVLWAIMDRPPFTQRVEDIEVVSLERVIPGGSTFDVNLIFKDYNKPPASITTIPRSSLESLKDWCLAARLYYMETSVNPNWKVVLKTIIEDEDWDPWRPGAGWAVLNDDFEGDEEASEDSDSDDSTYVEEEDETDETGSSFLDDEESEPESSDEEDSESVLSWDEMERRAEQHDRQRGYGSDDDDRPRKRPRTSSGASSNRRPHPPPQLPKKQSRLPPMGSAVPPPRRF
Protein: G-protein coupled receptors family 1 profile domain-containing protein (A0A060YTQ8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ig-like domain-containing protein
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Endothelin-3
- Neuropeptide Y
- Endothelin-1
- Endothelin-1
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MDITPTAFAASNSSEDTNGTSAQRPLPHSQSVAVFIVFLVTVIILVTIVGNVLVVVAVFTSRALRAPQNLFLVSLASADILVATLVIPFSLANEIMGYWYFGSTWCAFYLALDVLFCTSSIVHLCAISLDRYWSVTKAVSYNRKRTPRRIKCMITVVWVISAVISFPPLLMTKHDEHECLLNNETWYILSSCLVSFFAPGLIMILVYCKIYKVAKQRASTVRKFEVESPSSPSLGGHMRKGELDDIDLEESCVADSKPNNCLFSKRVKSCRVSWASNRNAKLSQEQKIRQMSLSKTKLAQMREKRFTFVLAVVMGVFVLCWFPFFFTYSLHAICRDCCPIPDALFNLFFWIGYCNSSVNPIIYTIFNRDFRRSFKKIICQTSHT
Protein: Adhesion G protein-coupled receptor D2 (G-protein coupled receptor 144) (G-protein coupled receptor PGR24) (Q7Z7M1)
Organism: Homo sapiens (Human)
Function: Orphan receptor.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDAPWGAGERWLHGAAVDRSGVSLGPPPTPQVNQGTLGPQVAPVAAGEVVKTAGGVCKFSGQRLSWWQAQESCEQQFGHLALQPPDGVLASRLRDPVWVGQREAPLRRPPQRRARTTAVLVFDERTADRAARLRSPLPELAALTACTHVQWDCASPDPAALFSVAAPALPNALQLRAFAEPGGVVRAALVVRGQHAPFLAAFRADGRWHHVCATWEQRGGRWALFSDGRRRAGARGLGAGHPVPSGGILVLGQDQDSLGGGFSVRHALSGNLTDFHLWARALSPAQLHRARACAPPSEGLLFRWDPGALDVTPSLLPTVWVRLLCPVPSEECPTWNPGPRSEGSELCLEPQPFLCCYRTEPYRRLQDAQSWPGQDVISRVNALANDIVLLPDPLSEVHGALSPAEASSFLGLLEHVLAMEMAPLGPAALLAVVRFLKRVVALGAGDPELLLTGPWEQLSQGVVSVASLVLEEQVADTWLSLREVIGGPMALVASVQRLAPLLSTSMTSERPRMRIQHRHAGLSGVTVIHSWFTSRVFQHTLEGPDLEPQAPASSEEANRVQRFLSTQVGSAIISSEVWDVTGEVNVAMTFHLQHRAQSPLFPPHPPSPYTGGAWATTGCSVAALYLDSTACFCNHSTSFAILLQIYEVQRGPEEESLLRTLSFVGCGVSFCALTTTFLLFLVAGVPKSERTTVHKNLTFSLASAEGFLMTSEWAKANEVACVAVTVAMHFLFLVAFSWMLVEGLLLWRKVVAVSMHPGPGMRLYHATGWGVPVGIVAVTLAMLPHDYVAPGHCWLNVHTNAIWAFVGPVLFVLTANTCILARVVMITVSSARRRARMLSPQPCLQQQIWTQIWATVKPVLVLLPVLGLTWLAGILVHLSPAWAYAAVGLNSIQGLYIFLVYAACNEEVRSALQRMAEKKVAEVLRALGVWGGAAKEHSLPFSVLPLFLPPKPSTPRHPLKAPA
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q385Z6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVHSAISSFIQQNPGDVSISILSCVVSCLSEPGVASNLVDQHRPICCKFMEHLINVINDGTKNPGVRLMAMECIYTLSAIPNDNFRRGDLFDAVQKLNESFEAFLESQAPNEAGDAGSLNEMLTIILFRCSGYNRLNAGDLLQQIFNGDDTRLVAALQSIIKNRSLEWDILHACIRCMYQLTTPASYFAAPEDNQPIETTKISAFQDKVSTLLIHLSQQNALHELFVEIGSRWEAAVQEFQLDSIIEGKTQLSKALLEGVTMNFVMVFRYLSVMLLNVADFCERMDLVHAYQNSFTERHQNFLVKTAIPFIRLAVRGWEATRDPAAPADSQENPYMNVAITALRLLRFVLYGASSPVPEEPLAAALASLTQQVHSMEELLRTEYVGMLVLVLTTEILCNVNAAAIPTLAPLFTKFVTTVVEDKSPLRPGAQFNTAQAFAYCIANETSTYCMNENESVIFLRDKLQDDDTVAVGQAAVAIRALEEQLTVLQSLMMELAIGQLLGDLCLLIPVGPGGEQARPRANWGAPPNLCDEADTEKRRKTGDKKKRKHPQEYVCMLTKKLMREPVLLSNGHRFELDVLQKVVDRVGHVDPLTGEAFTDEISVDAGLQQEIARYRVEMAARGDASAVA
Protein: PGR5-like protein 1B, chloroplastic (Ferredoxin-plastoquinone reductase 2) (Q8GYC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ferredoxin-plastoquinone reductase involved in cyclic electron flow (CEF) around photosystem I. The homodimer is probably not involved in CEF.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18243102}; Multi-pass membrane protein {ECO:0000269|PubMed:18243102}.
Interaction partners:
- Protein PROTON GRADIENT REGULATION 5
- Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic
- Dormancy-associated protein homolog 3
- NAD
- Protein CURVATURE THYLAKOID 1A
- Ferredoxin C 1, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
- Transport/golgi organization-like protein
- Ferredoxin C 2, chloroplastic
Sequence:
MAFTLTIPRFSAISRKPITCSSSRTQCPAPFTHGRSISLRRRLTLLPLKASTDQSGQVGGEEVDSKILPYCSINKNEKRTIGEMEQEFLQAMQSFYYEGKAIMSNEEFDNLKEELMWEGSSVVMLSSDEQRFLEASMAYVSGNPILSDEEYDKLKMKLKMDGSEIVCEGPRCSLRSKKVYSDLAIDYFKMFLLNVPATVVALGLFFFLDDITGFEITYLLELPEPFSFIFTWFAAVPAIVYLALSLTKLILKDFLILKGPCPNCGTENVSFFGTILSIPNDSNTNNVKCSGCGTEMVYDSGSRLITLPEGGKA
Protein: Testis-specific zinc finger protein topi (Protein matotopetli) (Q9VH70)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for male meiotic division and spermatid differentiation. Required for accumulation of aly and comr on chromatin. May function as a transcription factor.
Subcellular location: Nucleus {ECO:0000269|PubMed:15084455}. Note=Binds to chromatin.
Interaction partners:
- Cookie monster
- RT06796p1
- LD06557p
Sequence:
MKVKVSGEYTLAEIEVELDQQLTPDDLQPGATVLATNESTGGLERIVSHEELSRFFAVGPAGALPMPTDVVVERTLADPAFKQILQEADGKKGFDPQAEQMKIRDFLAGVTSSKMTTEQSVFHGSRSNSSASTVNRIKCPTCLVQFDAVAFQNHSCEAKPIEVAVPQQEKPHLVPTVSAPPAPLSKPASERVIRENQVRLRRYIKDEMKYDLATGIESSRKNAAKGPNECTMCDRKFVHASGLVRHMEKHALDLIPSQTSEQPHTIPAAGLHVVVKCNSCGRIFYDPQVAFRHGLIHDSEHSTMRQSPMTQVPSNRADFNELLLDGEMLIDNDPAFATSNQNTNPPKKEMFSSLILGSVLQCEFCEYIFADIAELLVHSASHVAERRFECTACDIQMNTAKEASIHFQTDCIFMREAIRSLNVTLSRYFVCNVCELKFANTDLLQEHRCTSFHYFPRLNENGKKLLLPCDFCDVNFEFAHDFLAHSEEKHLNKKKREKETRNTGAGRIRQYLCDICGKSYTQSSHLWQHLRFHQGVKPFVCQEENCDRKFTIRPDLNDHIRKCHTGERPYLCLVCGKRFLTGSVFYQHRLIHRGERRYECEECGKRFYRADALKNHQRIHTGEKPYSCLFCTKTFRQRGDRDKHIRARHSHLDANSRLMMQMQKFQLETAAAQKAQSHNPEQQDNDVAGGASTSDVPSGSGFMSTEPSVAEMQYSITPEQQEEMVCVPIDEVNNSFFMSHYMQAVPMEEDGSGQHIIVFEQPGQNMDMMSIYDQQQVGEPMHESGVPKRPAEENARVVVVKNNPTKPIFSDTYL
Protein: Protein TRANSPARENT TESTA 16 (Arabidopsis BSISTER MADS-box protein) (Q8RYD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in the developmental regulation of the endothelium and in the accumulation of proanthocyanidins (PAs) or condensed tannins which give the seed its brown pigmentation after oxidation. Necessary for the normal activation of the BANYULS promoter in the endothelium body. Is required, together with AGL11/STK for the maternal control of endothelium formation, which is essential for female gametophyte development and fertilization, and seed formation. Interacts genetically with AGL1/SHP1 and AGL5/SHP2 in a partially antagonistic manner and represses AGL1/SHP1, AGL5/SHP2, and AGL8/FUL during flower development. Is essential for the coordination of cell divisions in ovule, seed coat development and endosperm formation. Mediates the crosstalk between endothelium and nucellus to ensure proper seed formation. Functions redundantly with AGL63/GOA to repress nucellus growth and promote its degeneration. Represses the negative regulator of autophagy and programmed cell death HVA22D in the proximal nucellus. Binds specifically to the CArG box DNA sequence 5'-CC (A/T)6 GG-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Protein TRANSPARENT TESTA 1
- Transcription factor TT2
- WRKY transcription factor 44
- Transcription factor TT8
- Protein TRANSPARENT TESTA GLABRA 1
- Protein DETOXIFICATION 41
- Protein KOKOPELLI
- Biotin--protein ligase 1, chloroplastic
- Glutathione S-transferase F12
- MADS-box protein
Sequence:
MGRGKIEIKKIENQTARQVTFSKRRTGLIKKTRELSILCDAHIGLIVFSATGKLSEFCSEQNRMPQLIDRYLHTNGLRLPDHHDDQEQLHHEMELLRRETCNLELRLRPFHGHDLASIPPNELDGLERQLEHSVLKVRERKNELMQQQLENLSRKRRMLEEDNNNMYRWLHEHRAAMEFQQAGIDTKPGEYQQFIEQLQCYKPGEYQQFLEQQQQQPNSVLQLATLPSEIDPTYNLQLAQPNLQNDPTAQND
Protein: Calcium-activated potassium channel slo-1 (BK channel) (Maxi K channel) (MaxiK) (Slo homolog) (Slowpoke protein 1) (Q95V25)
Organism: Caenorhabditis elegans
Function: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Essential for the regulation of neurotransmitter release at synapses.
Subcellular location: Cell membrane {ECO:0000305|PubMed:28168949}; Multi-pass membrane protein {ECO:0000305}. Synapse {ECO:0000269|PubMed:28168949}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha
- Interactor with SLO-1
- Alpha-catulin
- Voltage-dependent calcium channel type A subunit alpha-1
- Dystrophin-1
- Dystrobrevin-1
- BK channel Interacting Protein
- AcetylCholine Receptor
- Potassium voltage-gated channel protein eag
- Syntrophin-1
Sequence:
MGEIYSPSQSKGFNQPYGYPMNCNLSRVFMEMTEEDRKCLEERKYWCFLLSSITTFCASMILVVIWRVVTHLCCQRREKEFVEPIPAPEAVQINMNGSKHAPSETDPFLKQQEEKHLGWMTEAKDWAGELISGQSLTGRFLVLLVFILSIGSLIIYFYDASFQNFQVETCIPWQDSPSQQIDLGFNIFFLVYFFIRFIAASDKVWFLLEMYSWIDFFTIPPSFVAIYLQRNWLGFRFLRALRLMTVPDILQYLNILKTSSSIRLTQLVTIFVAVCLTGAGLVHLLENSGDFFKGFINPHRITYADSVYFVLVTMSTVGYGDIYCTTLCGRLFMIFFILFGLAMFASYVPEIADLIGNRQKYGGEYKGEHGKKHIVVCGHITYDSVSHFLQDFLHEDRDDVDVEVVFLHRVVPDLELEGLFKRHFTKVEFFTGTVMDSLDLSRVKIGDADACLVLANKYSTNPDAEDAANIMRVISIKNYSSDIRVIVQLMQYHNKAYLLNIPSWDWKRGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSQTTPDWLNLYLCGAGMEMYTDTLSHSFVGMTFPEAVDLLFNRLGLLLLAIELKDEENKECNIAINPGPHIVIQPQTQGFFIAQSADEVKRAFFWCKQCHDDIKDVSLIKKCKCKNLALFRRNTKHSTAARARATDVLQQFQPQAPAGPMGHLGQQVQLRMINQQSSTSDTHLNTKSLRFAYEIKKLMPSSGGRRNSMSIPPDGRGVDFSKDFEQQFQDMKYDSTGMFHWCPSRNLEDCVLERHQAAMTVLNGHVVVCLFADQDSPLIGLRNFIMPLRSSNFHYHELKHVVIVGDLEYLRKEWKTLYNLPKISILNGSPLSRADLRAVNINLCDMCVIISARVPNTEDTTLADKEAILASLNIKAMQFDDTLGFFPMRHQTGDRSPLGSPISMQKKGAKFGTNVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAISVLDSLMSTTYFNDSALTLIRTLVTGGATPELELILAEGAGLRGGYSTPETLSNRDRCRIAQISLQDNPYDGVVHNTTYGAMFTIALRRYGQLCIGLYRLHDQDNPDSMKRYVITNPPAELRIKNTDYVYVLEQFDPGLEYEPGKRHF
Protein: Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calcineurin, testis-specific catalytic subunit) (Calmodulin-dependent calcineurin A subunit gamma isoform) (P48455)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:34446558}. Note=Localizes in the mitochondria in a SPATA33-dependent manner. {ECO:0000269|PubMed:34446558}.
Interaction partners:
- Calcineurin subunit B type 1
- Calcineurin subunit B type 2
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Protein phosphatase 3 catalytic subunit alpha
- Nuclear factor of activated T-cells, cytoplasmic 1
- Calmodulin-like protein 3
- Calmodulin-1
- Calmodulin-like protein 4
- Calmodulin 5
- Calmodulin-4
Sequence:
MSVRRPQFSTTERVIKAVPFPPTRRLTLKEVFENGKPKMDLLKNHLVKEGRVEEEVALKIINDGAAILKQEKTMIEVEAPITVCGDVHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTEYFTFKQECRIKYSEMVYDACMHTFDCLPLAALLNQQFLCVHGGMSPEITCLEDIRKLDRFSEPPAFGPVCDLLWSDPLEDYGSEKTLEHYTHNTVRGCSYFFSYPAVCEFLQNNSLLSIIRAHEAQDAGYRMYRKNQATGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNILNICSDEEMNVTDEEGATTGRKEVIKNKIRAIGKMARVFTVLREESENVLTLKGLTPTGTLPLGVLSGGKQTIETAKQEAAEEREAIRGFTIAHRIRSFEEARGLDRINERMPPRKEASYHHDAGRMHSHSHPPHPQASRRTDHGKKAL
Protein: DNA repair protein (A4FXZ3)
Organism: Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
Interaction partners:
- CRISPR-associated helicase, Cas3 family
- CRISPR-associated endoribonuclease Cas2
- CRISPR-associated endonuclease Cas1
- CRISPR-associated protein, Cas5h family
- CRISPR-associated protein, Csh2 family
- CRISPR-associated exonuclease Cas4
- CRISPR-associated protein, Csh1 family
Sequence:
MDLEYMHISYPNILLNMRDGSKLRGYFAKKYIDEEIVHNHRDNAFVYKYPQIQFKIIDRSPLIIGIGSLGINFLESKRIFFEKELIISNDTNDITEVNVHKDMDHFGTTDKILKYQFKTPWMALNAKNSEIYKNSDEIDREEFLKRVLIGNILSMSKSLGYTIEEKLKVKINLKEVPVKFKNQNMVGFRGEFYINFDIPQYLGIGRNVSRGFGTVVKV