wanglab/gogpt-training-data huggingface dataset:
Protein: Putative diacyglycerol O-acyltransferase Rv3480c (EC 2.3.1.20) (Putative triacylglycerol synthase Rv3480c) (P9WKA7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Upon expression in E.coli has a weak triacylglycerol synthase function, making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA. Also functions weakly as a wax synthase, as it incorporates palmityl alcohol into wax esters in the presence of palmitoyl-CoA.
Interaction partners:
- Possible multi-functional enzyme with acyl-CoA-reductase activity AcrA1
- Triacylglycerol lipase
- Diacylglycerol kinase
- Uncharacterized oxidoreductase Rv1543
- Possible ketoacyl reductase
- Polyketide synthase Pks13
- Phenyloxazoline synthase MbtB
Sequence:
MSQTARRLGPQDMFFLYSESSTTMMHVGALMPFTPPSGAPPDLLRQLVDESKASEVVEPWSLRLSHPELLYHPTQSWVVDDNFDLDYHVRRSALASPGDERELGIPVSRLHSHALDLRRPPWEVHFIEGLEGGRFAIYIKMHHSLIDGYTGQKMLARSLSTDPHDTTHPLFFNIPTPGRSPADTQDSVGGGLIAGAGNVLDGLGDVVRGLGGLVSGVGSVLGSVAGAGRSTFELTKALVNAQLRSDHEYRNLVGSVQAPHCILNTRISRNRRFATQQYPLDRLKAIGAQYDATINDVALAIIGGGLRRFLDELGELPNKSLIVVLPVNVRPKDDEGGGNAVATILATLGTDVADPVQRLAAVTASTRAAKAQLRSMDKDAILAYSAALMAPYGVQLASTLSGVKPPWPYTFNLCVSNVPGPEDVLYLRGSRMEASYPVSLVAHSQALNVTLQSYAGTLNFGFIGCRDTLPHLQRLAVYTGEALDQLAAADGAAGLGS
Protein: Tubulin beta chain (K7ES63)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDSVRSGPFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDRIMNTFSVMPSPKVSDTVVEPYNATLS
Protein: Serpentine receptor class beta-6 (Protein srb-6) (P54141)
Organism: Caenorhabditis elegans
Function: Mediates recognition and avoidance of Streptomyces species by detecting dodecanoic acid secreted by the bacteria. Also mediates avoidance of decanoic acid which is not secreted by Streptomyces species but this may represent an additional important avoidance response in the environment.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Serpentine receptor class alpha-7
Sequence:
MNDCDEVNNISYDPLYRYSQFYTLLTSIFSVFPLLYLIIFKLRVCTFNDNIKFLYIVYFTQILISVLNNCVVFAHHVVIPFLAVSKCDLLVNPVKNRIFQNIGVFGISCPMLTILGITAERLLALIFARCYENVKLHIGVFIGVFAMLCDMALVYFFFLDEKFDQPSISYFMVPDTSGYKMNWLCYSLLAINSVNLVFNYFLVKINTILKEKWRNSLSTRYQMEENIITTKFSTFISFIHVFFFSLYLIFTLIIRLLGPGFLKTQADLMSVRGVYITIPTYNLIIGIASCVILRHLQRQKVAKVYAEVTLKYSGIDGAQIHQEAILNVWKTKSSGRK
Protein: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase 1) (Glutamine:fructose-6-phosphate amidotransferase 1) (GFAT 1) (GFAT1) (Hexosephosphate aminotransferase 1) (P47856)
Organism: Mus musculus (Mouse)
Function: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes BMAL1 and CRY1. Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and its effects on hyaluronan synthesis that occur during tissue remodeling (By similarity).
Interaction partners:
- Glucosamine 6-phosphate N-acetyltransferase
- Glucose-6-phosphate isomerase
- Hexokinase-1
- N-acetylglucosamine-6-phosphate deacetylase
- Glucosamine-6-phosphate deaminase 1
- Glutamine synthetase
- Hexokinase-2
- Hexokinase-3
- Hexokinase HKDC1
- Mannose-6-phosphate isomerase
Sequence:
MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGLDGGNDKDWEANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPNPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNWESQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTARTQIGSTWWGSQAERGKDKKGSCGLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE
Protein: Iroquois homeobox protein 5a (Q1LXU5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MAYPQGYLYQPSASLALYSCPAYSTSVISGPRTEELGRSSSGSAFAPYAGSTAFTSASPGYNSHLPYSADAAAAATFTSYVSSPYDHTTGMAGSIGYHPYAAPLGSYPYGDPAYRKNATRDATATLKAWLNEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWTPRNRSEDEEEDENIDLEKNDDDEPNKPTDKGDSTDTEADHKLINPGEIPCDRFKDETHSKDLDPPLTDSELKEAEERTDLLAEQAKPTTSSPSVLQRGSDLITQEKPSEPGHAASTGNSNVTSVIHSPPSAPKPKLWSLAEIATSSDRCKGSSEASQAAGLSQSTVIASAASPTRSSPQCPLPNNTVLSRPIYYTSPFYPGYTNYSTFGHLHSSHGTNTSSTAHFNGLSQTVLNRAEALVRESKVRSQTQVDLCKDSPYELKKGMSNI
Protein: Eukaryotic peptide chain release factor subunit 1 (Eukaryotic release factor 1) (eRF1) (P79063)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
Subcellular location: Cytoplasm.
Interaction partners:
- Eukaryotic peptide chain release factor GTP-binding subunit
- Translation initiation factor rli1
- eRF1 methyltransferase catalytic subunit mtq2
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL31
- Elongation factor 1-alpha-A
- Elongation factor 1-alpha-B/C
- Small ribosomal subunit protein uS2A
- Elongation factor 1-alpha-B
- Small ribosomal subunit protein uS3
Sequence:
MSETAEKAIEIWKIRRLVKQLINCHGNGTSMITLIIPPGEQISRYSNMLAEEYGTASNIKSRVNRLSVLSAITSTRERLKLYNKVPDNGLVIYCGEVIMEGNKTRKLNIDFEPFKPINTSQYLCDNKFHTEALAELLESDQRFGFIVMDGHQTLYGVVSGSAREVLQRFTVDLPKKHGRGGQSALRFARLRDEKRHNYVRKVAEGAVQHFITDDKPNVAGIVLAGSADFKTELGQSDLFDQRLQSRIIKTVDVSYGGDAGFNQAIELAADTLSNVKYVQEKKLIQRFFDEISLDSGKYCFGVVDTMNALQEGAVETLLCFADLDMIRYEFKNSEGNPVITYMTKEQEEKDSTNSFLLDKDTGAEMELVSSMLLSEWLAEHYKDYGANLEFVSDRSQEGMQFVKGFGGIGAVMRYQLDLSMLDPESDEFYSDSD
Protein: Temporin-1Tf (TF) (Temporin-F) (P56921)
Organism: Rana temporaria (European common frog)
Function: Amphipathic alpha-helical antimicrobial peptide with potent activity against Gram-positive bacteria, weak activity against Gram-negative bacteria, and moderate activity against fungi (By similarity). Also displays anti-leishmania activity by damaging parasite membrane. Stimulates insulin release from pancreatic beta-cells in a dose-dependent manner, without increasing intracellular calcium. Protects beta-cells against cytokine-induced apoptosis and augments beta-cells proliferation. In vivo, intraperitoneal injection together with a glucose load into mice does not have effect on plasma glucose levels.
Subcellular location: Secreted {ECO:0000269|PubMed:34235566, ECO:0000269|PubMed:9022710}.
Interaction partners:
Sequence:
FLPLIGKVLSGIL
Protein: 15-cis-phytoene desaturase, chloroplastic/chromoplastic (EC 1.3.5.5) (Phytoene dehydrogenase) (Phytoene desaturase) (P28554)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis.
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:Q40406}. Plastid, chromoplast {ECO:0000250|UniProtKB:Q40406}. Membrane {ECO:0000250|UniProtKB:A2XDA1}; Peripheral membrane protein {ECO:0000250|UniProtKB:A2XDA1}.
Interaction partners:
- 15-cis-phytoene synthase
- Phytoene synthase 1, chloroplastic
- Prolycopene isomerase, chloroplastic
- 15-cis-phytoene synthase
- Zeta-carotene desaturase
- Neoxanthin synthase, chloroplastic
- Zeaxanthin epoxidase, chloroplastic
- 1-deoxy-D-xylulose-5-phosphate synthase
- Violaxanthin de-epoxidase
- beta-carotene 3-hydroxylase
Sequence:
MPQIGLVSAVNLRVQGSSAYLWSSRSSSLGTESRDGCLQRNSLCFAGSESMGHKLKIRTPHATTRRLVKDLGPLKVVCIDYPRPELDNTVNYLEAAFLSSTFRASPRPTKPLEIVIAGAGLGGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDDDGDWYETGLHIFFGAYPNIQNLFGELGINDRLQWKEHSMIFAMPSKPGEFSRFDFSEALPAPLNGILAILKNNEMLTWPEKVKFAIGLLPAMLGGQSYVEAQDGISVKDWMRKQGVPDRVTDEVFIAMSKALNFINPDELSMQCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVEHIESKGGQVRLNSRIKKIELNEDGSVKSFILSDGSAIEGDAFVFAAPVDIFKLLLPEDWKEIPYFQKLEKLVGVPVINVHIWFDRKLKNTYDHLLFSRSSLLSVYADMSVTCKEYYNPNQSMLELVFAPAEEWISRSDSEIIDATMKELATLFPDEISADQSKAKILKYHVVKTPRSVYKTVPGCEPCRPLQRSPIEGFYLAGDYTKQKYLASMEGAVLSGKLCAQAIVQDYELLVGRSQKKLSEASVV
Protein: Sodium/calcium exchanger 2 (Na(+)/Ca(2+)-exchange protein 2) (Solute carrier family 8 member 2) (Q9UPR5)
Organism: Homo sapiens (Human)
Function: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells. Contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory. Plays a role in regulating urinary Ca(2+) and Na(+) excretion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P48768}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48768}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8K596}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8K596}. Perikaryon {ECO:0000250|UniProtKB:P48768}. Cell projection, dendrite {ECO:0000250|UniProtKB:P48768}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P48768}.
Interaction partners:
- Sodium/calcium exchanger 3
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- cGMP-dependent protein kinase 1
- cAMP-dependent protein kinase catalytic subunit gamma
- Sodium/calcium exchanger 1
- cGMP-dependent protein kinase 2
Sequence:
MAPLALVGVTLLLAAPPCSGAATPTPSLPPPPANDSDTSTGGCQGSYRCQPGVLLPVWEPDDPSLGDKAARAVVYFVAMVYMFLGVSIIADRFMAAIEVITSKEKEITITKANGETSVGTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFQAGELGPGTIVGSAAFNMFVVIAVCIYVIPAGESRKIKHLRVFFVTASWSIFAYVWLYLILAVFSPGVVQVWEALLTLVFFPVCVVFAWMADKRLLFYKYVYKRYRTDPRSGIIIGAEGDPPKSIELDGTFVGAEAPGELGGLGPGPAEARELDASRREVIQILKDLKQKHPDKDLEQLVGIANYYALLHQQKSRAFYRIQATRLMTGAGNVLRRHAADASRRAAPAEGAGEDEDDGASRIFFEPSLYHCLENCGSVLLSVTCQGGEGNSTFYVDYRTEDGSAKAGSDYEYSEGTLVFKPGETQKELRIGIIDDDIFEEDEHFFVRLLNLRVGDAQGMFEPDGGGRPKGRLVAPLLATVTILDDDHAGIFSFQDRLLHVSECMGTVDVRVVRSSGARGTVRLPYRTVDGTARGGGVHYEDACGELEFGDDETMKTLQVKIVDDEEYEKKDNFFIELGQPQWLKRGISALLLNQGDGDRKLTAEEEEARRIAEMGKPVLGENCRLEVIIEESYDFKNTVDKLIKKTNLALVIGTHSWREQFLEAITVSAGDEEEEEDGSREERLPSCFDYVMHFLTVFWKVLFACVPPTEYCHGWACFGVSILVIGLLTALIGDLASHFGCTVGLKDSVNAVVFVALGTSIPDTFASKVAALQDQCADASIGNVTGSNAVNVFLGLGVAWSVAAVYWAVQGRPFEVRTGTLAFSVTLFTVFAFVGIAVLLYRRRPHIGGELGGPRGPKLATTALFLGLWLLYILFASLEAYCHIRGF
Protein: Immunoglobulin kappa variable 1D-33 (Ig kappa chain V-I region AG) (Ig kappa chain V-I region Bi) (Ig kappa chain V-I region Lay) (Ig kappa chain V-I region Ni) (Ig kappa chain V-I region Rei) (Ig kappa chain V-I region Roy) (Ig kappa chain V-I region Scw) (Ig kappa chain V-I region WAT) (P01593)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDMRVPAQLLGLLLLWLSGARCDIQMTQSPSSLSASVGDRVTITCQASQDISNYLNWYQQKPGKAPKLLIYDASNLETGVPSRFSGSGSGTDFTFTISSLQPEDIATYYCQQYDNLP
Protein: Neurobeachin/beige protein, putative (Q384U3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MALVGGEHRVTEDIVAVKYLESVRRLYFNPHAKDLERRTVQLLAQLLACPPHSLLVWDSLRRTRLLTTVARVLGSEKKLQGLLSVGGRPEDYLRVVELASNSSPCECMNHLTKGEDSHTELEPFFAVLGRLGKLDCDAATYRACYDSFARAVSNLLSDARNCARLVRADISPIKILFNTLKGSPSSRIDVSLCVLRVILQILLHTAAFTCIWIKEFSDLDGPSTCLSVVLTWCGTCEDPSLPLSTESTVVFDLLCLLLSFPGNGRGPSSALYMYLRGCHWEAENLEVGPLDDTATIGMFGLNVLVEACSIAMNFRPAIFTHLARLLVRALKLGGDDVVSAGLVSAALVAVLRQYAKFCDDCDKTILAIVRLCVTVCSCHGAYDAQTEGATQLCTLVVELVCDMRGHISKGTVRAVMCLTSRVNAESTFTRLFSVHLLERLEGRLAISQDPAEVYLFLQMMNEICGNVPVLRREFMLTLNTLFQLLGTEAKNGRETLMLCVDLLSTMCRDDEETTFNIYAGLREFITRSDFCSVDSIRLGCWGLQALIDLLAHASSSLTHFADSVDFLVTCVEKLCVAMCRAFDSQMTVTECFGVPSQILGPQPLEVGGFDVNPGSVVPNVYYFYCQFLVLGLHALCYVQATSTGTFFRDLPAKLERVLARGPFLRCRVYTSAVVRALIAMASSTSSVVFDEVFFANRGDCAQWFAGWGAVHRRSWRFNTSFGDVSFFHERQRIVHIGYFWCLQRLLLQLSDTSQKSMLGASVLELWFNVFSNSSENIYILMDSKMTLTLASLCAVSAADDCEYSFERYEILLKTMHEMGVYGMDCASVLYLLRLCLCDRDSSSVLYNDEATVKVLSTLKTLLRQSLPSNGPVLFYGVSSGCTPRSHFCNNTAALQVRGPRIGGGVDIPVLLGRVKSDRCFSFVLWFLLEPKSPHTVEEVDIILMSIAFNRNSAFIQLVYTVQGTLHLRVILRSPEDRNQQQQRLHSEYVLFSNDEIPTKRWCMVSMLVSQKRTKSFGRNPKYLLNVQLSLYTGSQADAQPSVVMKLSDIRCHGTCKGGQLLREVNMVSLVMTDGPPTNYPRRFLLGSLGAFGGVLSRVEVEMLFAMGSDSLFSLHFMDKKFVNNLFPALAYMSERNRGKHGAQLMRLAVPWLAQGYANAENAILASTFPFAVYQKRERQVVVAGVRNGDLCVESNAEYLQPTNDRPKVQGSGAEETLPPASARSVKSGTRIPVPIFLGVRSVSDLQNSGVAGEDMLALLNAPQFICSTPLYSILDALGGPPFFLCFSSLQLPHSGAFEEAWECACAAVKWHTTNNLLCPKAQRGDAHLLALVKALLYHRIHVSETTASSLCDVVGDRLITRMDILPLLLEFTVWARDTGAFRFVVGKLRQYILDDVYGRFNRQILGAGRHIASTEGECNALEEFLLHLHIHFSEGIVGSWDTSLIPFATEFLTALCQTATHARRVVKAATALLALDKPLTSAAIEWVIGLLEAVFYLMNENVILCGDESASLAEDITAIFKSSHEAVRRKALSLFSRTPMSRTQLDAVISQYMVRGVLSSVDDLLSEEEFLTIVGIIERSAASGDTTRARGLLYFLVTLLSHVPNEIRLGILSLLEEITCERGAFEGGLLSPLDTGGFPVSLLYGRLLHVLHMVEGNCSSLVESFVRLVIRMCVGMVSVSCERNDMNCGHLLGEVGLASLTCVASILKRSGREGSLDACISSALIRAYRYSSEVLRAYSMHLEKGTATGAFLMSYVSFLKSTAIVVILLSWCERDYRLSSEVKVEDESCVCHAAAEAYLAQFSKPIHFGDHHLSARLCMSFFEGGQRLFFQLQQAGTTGLHAKEVKQISQELLTLQWRVAVTLLNDADTSGEDLMKELALLYVASSGSASYGFKFSTWKERERLVEPPLGSDWKHLQFAPGALITELLKVDYERAVRESAPWLIVSRGASSLLSESRLENSSRYNMAVSICRLVRYNSGIWSNVKGGFTPLSVAELDSNIKTNAMSIGGAALKPLPEGGDGISVHWEVEFSRSGVASLERYINDIHSTALSSLNQCSERFALLLLSVSAEQALQHREKSGLAVEQYCRSVLRQVASHRKCIEGESKAVLAAYAAYRFSLTPWWGQSVNLYVASPVPMNQWELDRFTGPEWQRIRFRRFAHAMRVKHVKSKGDMLPYVYRGDISYPDDTQLLEIYSVTAVPQLIGVHCDGPQPFVAKCVLVLPMDRVPITLYVSPHTISYVHDESEPSPDATERGVTATQATKGNGGSCFSGLPCISASADQESDTVACNGDVRRYQRVFAVSSLRAVWPRRNLLQPSALELLFSTGESIFLVFHSQDTMKLVSDIVTTVACPYLDRALVLTEANLKMWCNWWREGRITNFHYLMYLNFAAGRSYGDMRQYPVFPHVVADFSSLTLDLTSPSTYRCLKRPIGAQTPEGIQRAAKTYAETSTDVGMAVEASCCGSPYHYGSHYSPLGGALHYLVRVQPFSDFFMKMNSKLDDAGRVFDSVGAAYAIATCGKDVKELLPEFYCLPELFVNANRIPFGTKQDGEVVNDVQLPPWASTPRKLSQTLRRALEGCYVSENLHSWIDLIFGFRQRGKEAVAALNTFHPLTYEGSVNLPNISDDVLRSSHETQIDCFGQTPLQLFSQPHKSRRKIADITFRQSPCPTLRCDASNLALCVLLNPGRLIPAGVCKRSCGTTVVFPRTKLNGIGSSIDEGTERKAQDGQVRPLVLPKGVFPFTVVHEQVRDCLRYKGSCIVLVDGKDASHQTRSFHVGYGEITALTVDSPNVYVGMESGAIHMLTMTYDTFLEVELTFRDGKGVRLGGEEVFQRFLQGKLNFTESRQTACRTLCVLYGHTARVTALCLSSEWGILVSSSEDCNVALWDTERRVLIRTIPNHLMSPAYSKFPMKSVMNHRLQGSSGSWYFDLITVNAKHGDIILAGGSLAGLHEVRRYSINGEFLGFYSLGETPATAILSVGDIVFVGRGSVVHMLKGNSLEWSCDLIHPGIEDCIESLALSPNGQSLVACDRRENLVTWKVAPQ
Protein: Forkhead box protein L2 (P58012)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator. Critical factor essential for ovary differentiation and maintenance, and repression of the genetic program for somatic testis determination. Prevents trans-differentiation of ovary to testis through transcriptional repression of the Sertoli cell-promoting gene SOX9 (By similarity). Has apoptotic activity in ovarian cells. Suppresses ESR1-mediated transcription of PTGS2/COX2 stimulated by tamoxifen (By similarity). Is a regulator of CYP19 expression (By similarity). Participates in SMAD3-dependent transcription of FST via the intronic SMAD-binding element (By similarity). Is a transcriptional repressor of STAR. Activates SIRT1 transcription under cellular stress conditions. Activates transcription of OSR2.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:19744555}.
Interaction partners:
- Mothers against decapentaplegic homolog 3
- Steroidogenic factor 1
- Homeobox protein NOBOX
- Factor in the germline alpha
- Bone morphogenetic protein 15
- Transcription factor SOX-9
- Probable ATP-dependent RNA helicase DDX20
- Doublesex- and mab-3-related transcription factor 1
- Small ribosomal subunit protein mS22
- Protein odd-skipped-related 2
Sequence:
MMASYPEPEDAAGALLAPETGRTVKEPEGPPPSPGKGGGGGGGTAPEKPDPAQKPPYSYVALIAMAIRESAEKRLTLSGIYQYIIAKFPFYEKNKKGWQNSIRHNLSLNECFIKVPREGGGERKGNYWTLDPACEDMFEKGNYRRRRRMKRPFRPPPAHFQPGKGLFGAGGAAGGCGVAGAGADGYGYLAPPKYLQSGFLNNSWPLPQPPSPMPYASCQMAAAAAAAAAAAAAAGPGSPGAAAVVKGLAGPAASYGPYTRVQSMALPPGVVNSYNGLGGPPAAPPPPPHPHPHPHAHHLHAAAAPPPAPPHHGAAAPPPGQLSPASPATAAPPAPAPTSAPGLQFACARQPELAMMHCSYWDHDSKTGALHSRLDL
Protein: Transglutaminase-like domain-containing protein (Q57VW3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
Sequence:
MLPPIRRIGGKTASVPGTSPGRGGAVANTAKVGLGTATPTDAEEGGEEKVPGPATLSPAPYEATRAERLTHWLRKEGFPPSYTEISPAEESIFKATRRFQSHFHEYFPKRAPQLLAPLNECRTRKMICTFIRPTIFPFDELFDVGSCARFLAGYMRYEILEDTERLPEVVVSPATTLQWQIGNCFELSILLTSLLVGVGYNAYVVVGYAERAVCENDSSQREWTDEYGELSTSGKSKSKRRTSNKDSTYCSNVVGTTGGREENANTKAPVTDDYCCYVDSDADDDGSDMVDAEYAALVKDRLVLRPADEIDMYSQYHHQQDDDKDTRSNTSFAGSRVQGASESYANSVSLCSPLANNVVGATSPLCGPNTSFNAFNNPARCGNADAASVIGGDDAVKGPAKGESVNFPPVRRLHSWVLVLPGGRKSVREPVFVEPSRGDLIAPGDADSFYTGVEGVFNGDNYFVNLTPDAAVSSLVPDLQDASQWEAVLFELDVEDERNISHNFVGTPLSTLGGQVHLGATPGSGGGVLSASPSAVYGSRGLGNSAGMRRRYNDEGSPAQHPGSTFSGGFSTLAGGLTHLMQTTRDRAVHFCCASWVEELTLNRAQYESRYPGGMKFTRYVNADVFRYAAYLMPDHRVLEVYLPDTQYPSQAQIHLLFEHRADKLRRRSVYPTASAFMRRTNSVSDFRSGAAAASGGEGLVALPAAEGEGKEPYDTDYDYSSGAQQRAGLRRNIVTSALDDEFRETNVGKRRSFVRHRSFSSGAFMRERTVSNSNSQLIPLVDVVVQSGNFRLMQEWFERGRMLQTSVGGLRLLTYEPGVQRTMTFYWDARNDGLWRRQEFFYESRALRKVKEFYRGRDDRLWYRSATFDNVAALNMGYNLSHTNSQQVGSSPSTKGSVRGADDTQRAEPIRMSEKYHRNETIPPDDDVAKYVFVRPAAVAAARAATGTMHPQLVASAALSPVCAGPSTGSVGSLSEGGEMWVYFHYRPGSIIRPYRMYPKTDPGEECLLSAVAGPKGSISGTLPSIIVMMPNATPPSDMEQCNERNRLRWWVTMCQGRVRASLAECNAIVESTREPSGPVAGPDEAEAAKRSSVELGGLAGAQLTPVAEQKSQAQNQEYLLPGLCPSKRVALANEKQRRVPAVVSVFDTLRNRPRETEAERRRRLAEEALREEARCDYLAPYIAKLDLPTTFSGDYMNVALTMDQARRVRDEALRELKERLIHRGRIIQKQMDEEREELTRRQANYQSNVDAAVAGVESTVKASGVETCSIQGVLGAAEQKDMSDSVALAATGGGALGEAVTGIPSVMGASCTITANALASTSAAVAVTTSGEVARDAKEFAQYCKEATWRMKTLDELLVKHIDRASERYAKLAQKLADDPRLSALYKNNPTPQTDKYSVQL
Protein: Cyclic di-GMP phosphodiesterase PdeH (EC 3.1.4.52) (P37646)
Organism: Escherichia coli (strain K12)
Function: Involved in the control of the switch from cell motility to adhesion via regulation of cellular levels of cyclic-di-GMP (c-di-GMP). Part of a signaling cascade that regulates curli biosynthesis. The cascade is composed of two c-di-GMP control modules, in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates the activity of the DgcM/PdeR pair (module II), which in turn regulates activity of the transcription factor MlrA and expression of the master biofilm regulator csgD. Effect on flagella is controlled via the c-di-GMP-binding flagellar brake protein YcgR.
Interaction partners:
- Flagellar brake protein YcgR
- Cyclic di-GMP phosphodiesterase PdeR
- Probable diguanylate cyclase DgcE
- Diguanylate cyclase DgcM
- Probable diguanylate cyclase DgcC
- Probable diguanylate cyclase DgcQ
- Oxygen sensor protein DosP
- Probable cyclic di-GMP phosphodiesterase PdeK
- Cyclic di-GMP phosphodiesterase PdeF
- Diguanylate cyclase DgcZ
Sequence:
MIRQVIQRISNPEASIESLQERRFWLQCERAYTWQPIYQTCGRLMAVELLTVVTHPLNPSQRLPPDRYFTEITVSHRMEVVKEQIDLLAQKADFFIEHGLLASVNIDGPTLIALRQQPKILRQIERLPWLRFELVEHIRLPKDSTFASMCEFGPLWLDDFGTGMANFSALSEVRYDYIKIARELFVMLRQSPEGRTLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQNSPAFAAQGWFLSRPAPIETLNTAVLAL
Protein: Integrin subunit alpha 3 (A0A8I6GLI8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MGPGPRRVPRDPGWMLRALALMVAASGRVAFAFNLDTKFLVVKEAVNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLAVDDDYTNRTGAVYLCPLTALKNDCERMDISEKSDPDHHIIEDMWLGVTVASQGPAGRVLVCAHRYTKVLWSGLEDQRRMVGKCYVRGNDLQLDPGDDWQTYHNEMCNSNTDYLQTGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLSEYSYRGSEDQGNLYIGYTMQVGSAILHPSEITLVTGAPRHQHMGAVFLLKQESGGDLQRRQVLKGTQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAVYVFMNQAGTSFPDQPSLLLHGPSRSAFGISVASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSGGLLKQPQQIIHGETLGLPGLATFGYSLSGKMDVDENLYPDLLVGSLRPGRVMARPVINILHRTLVARPAVLDPSLCTVTSCVQVELCFAYNQSAGNPNYRRNITLAYTVEADRDRRPPRLRFARSQSSVFHGFFSMPETHCQTLELLLMDNVRDKLRPIVITMNYSLPLRMPDRLKLGLRSLDAYPVLNQAQAMENHTEVHFQKECGPDNKCDSNLQMRAAFVSEQLQPLSRLQYSRDTKKLFLSINVTNSPSRQRAGEDAHEALLTLEVSSALLLSSVRPAGTCQANETNTVCELGNPFKRNQRMELLIAFEVTGVTLHTRDLRAHLQLSTSSHQDNLQPMFLTLQVDYTLQASLSLMNHRLQSFFSGTVMGEAAMKTVKDVGSPLKYEFQVSPVGDGLAALGTLVLGLEWPYEVTNGKWLLYPTEITIHSNGSWPCQPVSSLATLVVFRNLTIPFKPLSPQRRRRQLDPGGDQGPPPVTLAAAKKAKSETVLTCSNGRARCVWLECPLPDASNITNVTVKARVWNSTFIEDYKDFDRVRVDGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIELWLVLVAVGAGLLLLGLIIILLWKCGFFKRARTRALYEAKRQKAEMRSQPSETERLTDDY
Protein: Variant surface glycoprotein (VSG)-related, putative (Q4GY64)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MWKFKVLVAAAVVIIAAQINSVKIVNQEEFEILCGFVRLTLAPAPLIQLSQRIKNEAVGAAVDAIYSEPNQEHLWKKLSPNCEAHQISDRESVCDAYARFKHEAEERLKTSRLTEPELTDYSPDVLDHLEKAFKLYQASELEGKQTSIVTLQEGINSIMYGENDSGGNSLWGDHFRNEDCGTVLGQRPKYAGGALVTDLLCLCAQHVNGSDTKHLCCEGCSWRSNTTVWSEEGGLKLQWEILREKCIGYNMDLANPKDRLKRLREEMECRTVPRGIGSRKGLFVYTYGELEKRELVSCGGEDRQDSGACVLYEWGGTQIQTARIPWMQRLEKLVDMLPNVSEESDRMEKRRRQIENIVYRVNETSKKQPKLEKKEALSQQDTPHPPLGDVLQTFTDNPNTEGEAREKQQVKNDSSDKSVEIKPAEGRTPGIGIRPLKSASKIGTPLTMFLLLL