wanglab/gogpt-training-data huggingface dataset:
Protein: Protein kintoun (Dynein assembly factor 2, axonemal) (B1H1W9)
Organism: Xenopus laevis (African clawed frog)
Function: Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069}. Dynein axonemal particle {ECO:0000269|PubMed:30561330, ECO:0000269|PubMed:33263282}. Note=Localizes in the apical cytoplasm around the gamma-tubulin-positive pericentriolar region, not in the cilia. {ECO:0000255|HAMAP-Rule:MF_03069}.
Interaction partners:
Sequence:
MAEKLQNLELSSEELDRFTKAFQDPKFREMFVQYAEEIRDPENRRKYEQEISQMESERGMDIKFIHPKPGYVLLTSVNGVQKCYLNICSNDLLQKPECKPGKDGEGKAGLHWSLPYSLSAGREDLGKDGSKHVIYDVVFHPDTLHIASKNEKFKMIVDSTSLEAVASQFDVKLDKANVRTLSMKYKGVPNPSVLRKPLLGTTPKHGDPEDPLSFPYPYDVPTAVGKEKKDQKRVIKEEHKQHVTTSEQDPDIQIATTPNYTVRHRSYVDLQDFRDSRDSTPSPVPKELVITVDLPLLNSAESVNLHIAGKNLSLESEKPAYKLNVKLPYVVEDNQGKAQFNKARRQLIITVPVIQHNILTLMQDHFEEARGEKDLRGAESSVLHEEYTDNGSRTSACGTENKLEPLISCLNEEENNSEGLTSESNLDTGAPYLPEISPNQNTLDREEVVYGLTEDVPSMPSDTLVCPTFSCSQDPTSLTLIAHVRDIDENSISTDVGSNHYHIRCSVKQSTSSYDLLVTFLPHDIINPNEVYVNISENNALIGLTKSPESVGFWKMLYFGVSGQPLQERRFVSEDNINEVLACSIPLSQVSPSTQEHQPLIEVLEMTDERTHIRINKPKTECVVSAEHKEHCTDHSEHERDVGVERSNIAVGDTTEHYSNQVSPCRENTELDRDHTSERYEEPESTSCTGESTSDQQQKDSNLVFPGDSSAENKMACLKSSEQTTQESDLAEDDMPDRSDHTQNFDSRPASSSVLKEIGKKDGSVQVISDHTTQCPFQFQNSLLFDLD
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8MSY6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSRQEGAASRPADGATGPVASSSSSTSSNHSVSAVLGSKISTSTPQKNDEHQEQEFINQSVASEIEAMSISDSASAESSSGATATATATMSGSPVPKRHLSTANLSRIRPQSSYSARVLIFDDSDQEAAAAAAALAAASSSCNSSVKSCSGLELLPTSPAKLSIGNDSTNGSSMMRNLNLTKSSSGGLSGSSSSLHSRGYTALLRKISYQQHTNSLRAVSGETSNLLRMRHSSLGKSAPCLTGNYFRHELTAPLPVQPPGFGASPLGGHNISRSGSCAGIGLAKHHHHHHLHGVVMRGSAGGGAGSGGGSSSGVAHHRLSLVTNSAAVAAAGGSRTHSPYSASPVDSPRLNSPMPFAFAPIKRIASCRGVVADGRRWSVASLPSSGYGTTPGSSNLSSQCSSQEGLNQLAHNIPPGVQEADAAAVAAGACCAEHLKQHCPKHCALLLAVSQKQLTPQPPKPTQLQPQKSMTAACVNCCAELSVTCGGQQAGGGAANGGSSANSSGSSAMQVGGRMSPYFRPRSRSLSSPSRSPIVDNEIAVMNTLYKERFPKATQQMEERLKLFINENKSAACNSFRDSQPIVRFVHHQVLEMARDCLHKSEAKLITSQYFYELSENLERLLVETKEKSPEAAAELNGVIKKLLLIISRPARLLECLEFDPQEFYELLEAAEGHAKAMPVIKADIPQYIIHKLGLNRDPIAELQQELRETQQMCSEQVTVDADPLHPGGSLLLNSPLTSAAKQLSSLALDAIAMDSGSGTATPQQPPQTPVATCDTAPSFALAISQMNEEKGGSSSAVGGGSSSKVAGAEGITGGSAATATGSGAQQPSPQENDFDIVKLISNGAYGAVYLVKHKTTRQRFAMKKKKKKK
Protein: Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (SBCAD) (EC 1.3.8.5) (2-methyl branched chain acyl-CoA dehydrogenase) (2-MEBCAD) (2-methylbutyryl-coenzyme A dehydrogenase) (2-methylbutyryl-CoA dehydrogenase) (P70584)
Organism: Rattus norvegicus (Rat)
Function: Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA. Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway (By similarity). Can also act on valproyl-CoA, a metabolite of the valproic acid drug.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:6874697}.
Interaction partners:
- Enoyl-CoA hydratase, mitochondrial
- Peroxisomal bifunctional enzyme
- Trifunctional enzyme subunit alpha, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Acetyl-CoA acetyltransferase, cytosolic
- Acetyl-CoA acetyltransferase, mitochondrial
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Peroxisomal acyl-coenzyme A oxidase 1
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAVSAFQLWRAGGLLRRNFLTHSSSWKIPPRVLKSSQPEALLSVTNNALCFAPLQTFTDEDIMMQKAVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGMMGIEVEAKYGGTEASFLCSVLVIEELAKVDASVALLCDIQNTVINKLFRKHGTEEQKATYLPKLVTEKLGSFCLSEAGAGSDSFALKTRADKSGNYYVINGSKMWISNAEHAELFLVFANVDPPSGYRGITCFLVDRDTEGFQIGRRENKMGIRASSTCQLTFENVKVPETSVLGKIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAHVATQLEAARLLTYNAARLVEAGRPFIKEASMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGTSNIQLNTIAKHIDAEY
Protein: Rifin (Q8IEU7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYINILLFALPLNILVRNQRNHRKSILSTTKSELTKTHRTLCECELYAPSKYENDPEMKEVMENFDRQTSERFRKYDERIQDKRKQFKEQCEKDIQKIILKDKIEKQLSQQFSKLQTNIETNDIPTCICEKSVAEKVEKTCLKCGEILGTVVPELGLIGGTVIYASAQSAAVKVGVSKAIELMKDIYFLGQVPFFDLVAKITPSNFNDKMSLIGIVHDASYTVCETTNAQDTLVFCLSKYSIGRRNPSMFLSVTANQAKDAAEAAGEAATGTFSEMTSVGAIFSDALVISAIVVVIIAVIILIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: SPRY domain-containing protein 4 (Q91WK1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MALPFARCWKLYRWGTKRWGVPAVESRRGISFKLEEKTAHSSLALFRGDTGVKYGLVGLEPTKVALNLERFREWAVVLGDTTVTSGRHYWEVTVKRSQQFRIGVADVDMSRDSCVGADDRSWVFSYAQRKWHSMLANEKAPIKGIGQPEKVGLLLDYEAKKLSLVDVSRISVIHTLQTDFRGPVAPAFALWDGELLTHSGLEVPKGL
Protein: Cyclopropyl isomerase (F4K8Y4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSGSSSPSLWLAPNPSKRWGELFFLFYTPFWLTLCLGIVVPYKLYETFTELEYLLLALVSAVPAFVIPMLLVGKADRSLCWKDRYWVKANLWIIVFSYVGNYFWTHYFFKVLGASYTFPSWKMNNVPHTTFFLTHVCFLFYHVASNITLRRLRHSTADLPDSLKWCFEAAWILALSYFIAYLETIAIANFPYYEFVDRSAMYRVGCLFYAIYFIVSFPMFFRMDEKSTDEWDLSRVAVDALGAAMLGIDMGLREKPAKEFPLTLYGIGKQLMQGMFLRLFFSNC
Protein: Lysine-specific histone demethylase (EC 1.14.99.66) (A0A0G2K736)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR038051}.
Interaction partners:
Sequence:
MLSGKKAAAAAAAAAAAAAGTEAGPGAAGGAENGSEVAAPPAGLAGPADIATGAAGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTAGPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGQAGGLQDDSSGGYGDGQASGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQADTVKVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
Protein: 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial (EC 1.3.1.124) (2,4-dienoyl-CoA reductase [NADPH]) (4-enoyl-CoA reductase [NADPH]) (Q64591)
Organism: Rattus norvegicus (Rat)
Function: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in mitochondria. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:2383590}.
Interaction partners:
- Enoyl-CoA delta isomerase 1, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Peroxisomal bifunctional enzyme
- Delta
- Enoyl-CoA delta isomerase 2
- Trifunctional enzyme subunit beta, mitochondrial
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-ketoacyl-CoA thiolase A, peroxisomal
Sequence:
MALLARAFFAGVSRLPCDPGPQRFFSFGTKTLYQSIDAPQSKFFPPILKPMLPPNAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRNIDVLKATAEEITSKTGNKVYAIRCDVRDPDMVHNTVLELIKVAGHPDVVINNAAGNFISPSERLSPNGWKTITDIVLNGTAYVTIEIGKQLIKAQKGAAFLAITTIYAESGSGFVMPSSSAKSGVEAMNKSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGGEEVFLSGEFNSLKKVTKEEWDVIEGLIRKTKGS
Protein: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 (Alpha 2,3-ST 4) (Beta-galactoside alpha-2,3-sialyltransferase 4) (EC 2.4.3.2) (EC 2.4.3.4) (Alpha 2,3-sialyltransferase IV) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (Gal-beta-1,4-GlcNAc-alpha-2,3-sialyltransferase) (N-acetyllactosaminide alpha-2,3-sialyltransferase) (EC 2.4.3.6) (ST3Gal IV) (ST3GalIV) (Sialyltransferase 4C) (SIAT4-C) (Q91Y74)
Organism: Mus musculus (Mouse)
Function: A beta-galactoside alpha2-3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids (By similarity). Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc- and Galbeta-(1->4)-GlcNAc-terminated glycoconjugates through an alpha2-3 linkage (By similarity). Plays a major role in hemostasis. Responsible for sialylation of plasma VWF/von Willebrand factor, preventing its recognition by asialoglycoprotein receptors (ASGPR) and subsequent clearance. Regulates ASGPR-mediated clearance of platelets. Participates in the biosynthesis of the sialyl Lewis X epitopes, both on O- and N-glycans, which are recognized by SELE/E-selectin, SELP/P-selectin and SELL/L-selectin. Essential for selectin-mediated rolling and adhesion of leukocytes during extravasation. Contributes to adhesion and transendothelial migration of neutrophils likely through terminal sialylation of CXCR2. In glycosphingolipid biosynthesis, sialylates GM1 and GA1 gangliosides to form GD1a and GM1b, respectively (By similarity). Metabolizes brain c-series ganglioside GT1c forming GQ1c (By similarity). Synthesizes ganglioside LM1 (IV3Neu5Ac-nLc4Cer), a major structural component of peripheral nerve myelin (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
Interaction partners:
- Galactoside alpha-
- Galactoside alpha-
- Beta-1,3-galactosyltransferase 1
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
- Beta-1,3-galactosyltransferase 5
- Galactoside 2-alpha-L-fucosyltransferase Sec1
- Beta-1,3-galactosyltransferase 2
- CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
- Alpha-
Sequence:
MTSKSHWKLLALALVLVVVMVWYSISREDRYIEFFYFPISEKKEPCFQGEAERQASKIFGNRSREQPIFLQLKDYFWVKTPSTYELPFGTKGSEDLLLRVLAITSYSIPESIKSLECRRCVVVGNGHRLRNSSLGGVINKYDVVIRLNNAPVAGYEGDVGSKTTIRLFYPESAHFDPKIENNPDTLLVLVAFKAMDFHWIETILSDKKRVRKGFWKQPPLIWDVNPKQVRILNPFFMEIAADKLLSLPIQQPRKIKQKPTTGLLAITLALHLCDLVHIAGFGYPDASNKKQTIHYYEQITLKSMAGSGHNVSQEAIAIKRMLEMGAVKNLTYF
Protein: AP-1 complex subunit gamma (B3KXW5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MEKNINLRNCQTLNTYVMLTHLRMPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPTEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPSSAGGELLDLLGDINLTGAPAAAPAPASVPQISQPPFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ
Protein: Solute carrier family 4, sodium bicarbonate cotransporter, member 9 (Q8BUG8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKLQEVTSLSRQSAALAEDKHHHGPHTPIPELQRTGSVSQLCSTFTWPQSQTPSLLGVFWEMPLKVPRDYSLDYLPFRLWVGIWVTAFCLALVATEASLLVRYFTRFTEEGFCALISLIFIYDAMGKMLNLIRAYPIQRPGSSAYGCFCQYPGTGGNTSEWTSAKLKDTEDILSVPGLVNASFLPPPECIRQGGHPLGPSCHTVPDIAFFSLLLFFTSFLCAIALKHIKNSRFFPSVVRKVLGDFSSVLAILLGCGLDTFLGLATPKLLVPTEFKPTLSGRGWLVSPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRAEYRLQKGAGFHLDLFCVAVLMLFTSALGLPWYVSATVISLAHIDSLRRESKACIPGEAPNFLGIREQRLTGLVVFVLTGVSIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFVKRVQLLLMPRKHQPDMLLLRHVPLSRVHLFTAIQLACLGLLWVVKSTPAAIVFPLMLLGLVAIRKALEWVFSPQELLWLDELMPEEEETIPENRSEPEHLFSGNDSEDSELMYQPKAPEINISVN
Protein: Evasin P1174 (V5I3C5)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1 and CXCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
LKTFCLFLQIAVFIALGIQIFLCGTDALNNENELFSVEYCGANCTQQDNGSWTKCKGNCTCYHEDGKRYGLCLSTEYTDFTQFPKPTSEEIADASPRPKETNSH
Protein: Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein) (Pyruvate dehydrogenase complex E3 subunit) (E3) (PDC-E3) (P31023)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. The pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix.
Interaction partners:
Sequence:
MAMANLARRKGYSLLSSETLRYSFSLRSRAFASGSDENDVVIIGGGPGGYVAAIKAAQLGFKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHSFANHGVKVSNVEIDLAAMMGQKDKAVSNLTRGIEGLFKKNKVTYVKGYGKFVSPSEISVDTIEGENTVVKGKHIIIATGSDVKSLPGVTIDEKKIVSSTGALALSEIPKKLVVIGAGYIGLEMGSVWGRIGSEVTVVEFASEIVPTMDAEIRKQFQRSLEKQGMKFKLKTKVVGVDTSGDGVKLTVEPSAGGEQTIIEADVVLVSAGRTPFTSGLNLDKIGVETDKLGRILVNERFSTNVSGVYAIGDVIPGPMLAHKAEEDGVACVEYLAGKVGHVDYDKVPGVVYTNPEVASVGKTEEQVKETGVEYRVGKFPFMANSRAKAIDNAEGLVKIIAEKETDKILGVHIMAPNAGELIHEAAIALQYDASSEDIARVCHAHPTMSEAIKEAAMATYDKPIHI
Protein: Tehao (Q58S71)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
VVCTNDEACQYKSAEWQCDPRCICWVQRSVGSLIVDCRGTSLEELPDLPRTTLLSTVLKVGNNSLTSLPTVSEHSGYANVSGLFLSDNNLTSLGSGDQLPDNLTHLDVRDNQIQSLSEEFLLFLQEPNNTMTLSLSGNPITCGCESLSLLFFVRTNPQRVRDIADIVCTKQKKSFQQMEAFELCPSYVLLISCVVGGLVIVICLLTVFYLMFQQELKIWLYNNNLCLWWVSEEELDKDKTYDAFISYSHKDEELISKLLPKLESGPHPFRLCLHDRDWLVGDCIPEQIVRTVDDSKRVIIVLSQHFIDSVWARMEFRIAYQATLQDKRKRIIIILYRELEHMNG
Protein: Protein LATERAL ROOT PRIMORDIUM 1 (Q94CK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influence vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM). Modulates root growth.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein uL5m
- Electron carrier/iron ion-binding protein
- Probable mediator of RNA polymerase II transcription subunit 19b
- Eukaryotic translation initiation factor 4B3
- Large ribosomal subunit protein P3y
- DUF4228 domain protein
Sequence:
MGMVGLRDVFLVAPAYHHQNAGVISGSDHMNSNAAAAAALGVGVIPLLTAGTPQQNVEDSDINFLGNNRRWQNNNNNHETQYLHFKSTNQTTVGTSSNNSGSGSGASGTATCQDCGNQAKKECKQRRCRTCCKSRGFDCSTHVKSTWVSAARRRERQVMPTGANPTAGSSLSTSSGTKKPRIVGSQQQQQQQATSHTSTSNTPPQSFETSSSRQDGGGSREAWPGQVRAAAVFKCVRVTAVEDGDDEYAYQAVVKIGGHVFKGFLYDQGLEPKEGFPSMSDLHLGGSANNHNGVSASAPILDPPNVVYGGGGGSGGGFYS
Protein: Probable conserved Mce associated protein (O07421)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Probable conserved Mce associated transmembrane protein
- Probable conserved Mce associated membrane protein
- Probable conserved Mce associated membrane protein
- Carboxyltransferase domain-containing protein
- Proline-rich antigen homolog
- Possible exported protein
- Possible conserved transmembrane protein
- Mce-family protein Mce1F
- Mce-family protein Mce1C
- Carboxyltransferase domain-containing protein
Sequence:
MSPRRKFEPGEGALLAPQSIEPSRRWGLPLALTASAVVMAAAISACALMRISHESHQRAAHKDIVMLSDVRSFMTMFTSPDPFHANEYAERVLSHATGDFAKQYHERANDILIRISGVEPTTGTVLDAGVQRWNEDGSANVLVVTQITSKSADGKRVVSNANRWLVTAKQEGNEWKISSLLPVI
Protein: Vezatin (F8W8C2)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLKEWAIKQGILLKVAETIKSWIFFSQCNKKDDLLHKLDIGFRLDSLHTILQQEVLLQEDVELIELLDPSILSAGQSQQQENGHLPTLCSLATPNIWDLSMLFAFISLLVMLPTWWIVSSWLVWGVILFVYLVIRALRLWRTAKLQVTLKKYSVHLEDMATNSRAFTNLVRKALRLIQETEVISRGFTLLLDRVSAACPFNKAGQHPSQHLIGLRKAVYRTLRANFQAARLATLYMLKNYPLNSESDNVTNYICVVPFKELGLGLSEEQISEEEAHNFTDGFSLPALKVLFQLWVAQSSEFFRRLALLLSTANSPPGPLLTPALLPHRILSDVTQGLPHAHSACLEELKRSYEFYRYFETQHQSVPQCLSKTQQKSRELNNVHTAVRSLQLHLKALLNEVIILEDELEKLVCTKETQELVSEAYPILEQKLKLIQPHVQASNNCWEEAISQVDKLLRRNTDKKGKPEIACENPHCTVVPLKQPTLHIADKDPIPEEQELEAYVDDIDIDSDFRKDDFYYLSQEDKERQKREHEESKRVLQELKSVLGFKASEAERQKWKQLLFSDHAVLKSLSPVDPVEPISNSEPSMNSDMGKVSKNDTEEESNKSATTDNEISRTEYLCENSLEGKNKDNSSNEVFPQGAEERMCYQCESEDEPQADGSGLTTAPPTPRDSLQPSIKQRLARLQLSPDFTFTAGLAAEVAARSLSFTTMQEQTFGGEEEEQ
Protein: Achintya, isoform A (RE30881p) (Q7JR08)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MISPEQEEVNMVLDRHVRQNIQDMMHEAHVQASLLENEGRGRFHSDSSLDQDSLHADVIVEEDQSTEHGANQVQNYHDMMVDSEHHIDINGSLRKRRGNLPKTSVKILKRWLYEHRYNAYPSDAEKFTLSQEANLTVLQVCNWFINARRRILPEMIRREGNDPLHFTISRRGKKVSPNCSRSSALGANLTGPNPAHGSPASEVVVGATEEVDGAGEIHEGIANVLTNFEQYVQGPNGQMVKMEPEYEDSVIYRSEGEESAQGYESCGPNSEEEVRFETSHDWQSVIKTVFGTEEVSTSAGNNPGTSGSKGSVQNTAIWNRNQTAKRDVNQQLTDFESELNRIQASEIQTIDPTNSNQQDIGDNLQADEVFTGAEAEAGQSQLSAMSQGTSPDERAKYKCLYYLVETAMAVRQNDDVQDDDFVYMGD
Protein: RNA helicase (EC 3.6.4.13) (Q6AYT6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLQLLLHKKATGPVMEQAVRGLVLVPTKELARQAQSMIQQLASYCARDVRVANVSAAEDSASQRAVLMEKPDVVVGTPSRILNHLQQKNLKLRDSLELLVVDEADLLFSFGFEDELKSLLCHLPRIYQAFLMSATFNEDVQTLKELVLHNPVTLKLQESQLPGPDQLQQFQVVCETEEDKFLLLYALLKLSLIRGKALLFVNTLERGYRLRLFLEQFSIPSCVLNGELPLRSRCHIISQFNQGLYDCVIATDAEILGPQVKAKRQGRGSKGDKASDPESGVARGIDFHHVSAVLNFDLPPTAEAYVHRAGRTARANNPGIVLTFVLPTEQSSLGKIEELLSGEGQAPILLPYQFQMEEIESFRYRCRDAMRSVTKQAIREARLKEIKEELLHSEKLKTYFEDNPRDLQLLRHDLPLHPAVVKPHLGNVPDYLVPAALRGLVHPRKKRRKMPFSRKAKKVKTQNPLRDFKHRGKKPKPTAKPS
Protein: Protein FAR1-RELATED SEQUENCE 1 (Q5UBY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription activator involved in regulating light control of development.
Subcellular location: Nucleus {ECO:0000269|PubMed:15591448}. Note=The nuclear localization is independent of the light treatment.
Interaction partners:
- Histone acetyltransferase subunit NuA4-domain protein
- Non-specific lipid transfer protein GPI-anchored 23
Sequence:
MSSGECSNVQLDDHRKNNLEIDEGREFESKEEAFEFYKEYANSVGFTTIIKASRRSRMTGKFIDAKFVCTRYGSKKEDIDTGLGTDGFNIPQARKRGRINRSSSKTDCKAFLHVKRRQDGRWVVRSLVKEHNHEIFTGQADSLRELSGRRKLEKLNGAIVKEVKSRKLEDGDVERLLNFFTDMQVENPFFFYSIDLSEEQSLRNIFWVDAKAMHGCRPRVILTKHDQMLKEAVLEVFPSSRHCFYMWDTLGQMPEKLGHVIRLEKKLVDEINDAIYGSCQSEDFEKNWWEVVDRFHMRDNVWLQSLYEDREYWVPVYMKDVSLAGMCTAQRSDSVNSGLDKYIQRKTTFKAFLEQYKKMIQERYEEEEKSEIETLYKQPGLKSPSPFGKQMAEVYTREMFKKFQVEVLGGVACHPKKESEEDGVNKRTFRVQDYEQNRSFVVVWNSESSEVVCSCRLFELKGFLCRHAMIVLQMSGELSIPSQYVLKRWTKDAKSREVMESDQTDVESTKAQRYKDLCLRSLKLSEEASLSEESYNAVVNVLNEALRKWENKSNLIQNLEESESVTAQDLPIHEEQNNTYDMNKDDNVADTGQEYSLQEVWKVTALQEQRNRYSILDDYLSAQHMSHEMGQINSMASNRNGYCSVHQNIHSLQGQSITHPRLYETEQSSFRPEAMYERLQDMVKDLN
Protein: Ketol-acid reductoisomerase (NADP(+)) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 2) (Ketol-acid reductoisomerase type II) (P05989)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Interaction partners:
- Dihydroxy-acid dehydratase
- Dihydroxyacid dehydratase
- Acetolactate synthase
- 3-isopropylmalate dehydrogenase
- Acetolactate synthase isozyme 3 small subunit
- Acetolactate synthase isozyme 3 large subunit
- 2-isopropylmalate synthase
- Acetolactate synthase isozyme 1 small subunit
- Acetolactate synthase
- Acetolactate synthase isozyme 2 small subunit
Sequence:
MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVVNLTPDKQHSDVVRSVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPQGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSYACVPLLKPFMAELQPGDLGSAIPEGAVDNAQLRDVNDAIRSHAIEQVGKKLRGYMTDMKRIAVAG
Protein: RNA helicase (EC 3.6.4.13) (Q9VY54)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Pre-mRNA-splicing factor Slu7
- Pre-mRNA-processing factor 17
- Cwc25
- Pre-mRNA-splicing factor 18
- Pre-mRNA-splicing factor CWC22 homolog
- RNA helicase
- FI23980p1
- Pre-mRNA-splicing factor Syf2
- 116 kDa U5 small nuclear ribonucleoprotein component
- Cell division cycle 5, isoform A
Sequence:
MSDDDESGVHRLEGTAGQETRGGLVIRKPKDAGAGGGGGFKVPQGSMLGLDKLAAKRRAEKERSERLISFKDSEFDDTGGGSSTPQANASGASSEFAFKKPDTKSFEKLRGQLREHKDDTPSHTGGVSEKARERLREHIQRDRKRGPVSSTAAEGRDRDRDWDRDRRRDRDRDRDRDRDRRQHRERERDRHRSWDRDRGRDRDRDRSMSERSVHTPREPGTPGGSSGGISNSSWDDEDGEFGQRKSDWDMPTPRRHGNKSGDWSVRSGGSRRNHGRQDDTVRPTPAHRYNQWAHGRKRSGATPWGEDPESLDLWEEEQRRLDREWYNIDEGYDDENNPFGGPNSEYFRKREEQLEQKRTKRISAQQRQNNRDNELWERNRMLTSGVVTLISVNDDFDEEALERVHLLVHHIIPPFLDGRIVFTKQPEPVVPVKDPTSDMALLARKGSALVRNYREQKERRKAQKKHWELSGTKLGNIMGVQRPQDEDDMRFDKEKDKADYRKDQKFADHMRDQDTGGKSDFSRKKTISEQRRFLPVFASRQELLNVIRENSVIIIVGETGSGKTTQLTQYLHEDGYSKRGMIGCTQPRRVAAMSVAKRVSDEMDTQLGEDVGYAIRFEDCTSERTVIKYMTDGILLRESLRDPELDSYSAIIMDEAHERSLSTDVLFGLLREIVARRHDLKLIVTSATMDSSKFATFFGNVPTFTIPGRTFPVDVMFSKNTCEDYVESAVKQALQVHLTPNEGDMLIFMPGQEDIEVTCEVLEERLAEIDNAPALSILPIYSQLPSDLQAKIFQKSSDGLRKCVVATNIAETSLTVDGIIYVIDSGYCKLKVYNPRIGMDALQIYPISQANANQRSGRAGRTGPGQAYRLYTQRQYKDELLALTVPEIQRTNLANTVLLLKSLGVVDLLQFHFMDPPPQDNILNSLYQLWILGALDHTGALTTLGRQMAEFPLDPPQCQMLIVACRMGCSAEVLIIVSMLSVPSIFYRPKGREDEADGVREKFQRPESDHLTYLNVYQQWRQNNYSSTWCNEHFIHIKAMRKVREVRQQLKDIMTQQNLSVISCGIDWDIVRKCICSAYFYQAARLKGIGEYVNLRTGMPCHLHPTSALYGLGTTPDYVVYHELIMTAKEYMQCATAVDGYWLAELGPMFFSVKESGRSGREKKKQAAEHLKEMEEQMLKAQHEMEERKQQAAEREEQLATKQEIATPGNATPRRTPARIGL