wanglab/gogpt-training-data huggingface dataset:
Protein: Stardust, isoform O (EC 2.7.4.8) (X2JCZ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQANSSRSNLSAQSSGTPSASTISSSQGKQQVVELSGYVIILVENVEGKIKLYGSPPDRDNLEVGDEILEVNGLTLENISRTEVIRHIHDCIKSCTICLRVRKKNDSRLAWDIGNSVQDAFVIAVEEHARERLQRLAALNRVTPVDITQLSKKLLEDVIVHQASDVHSYSTSASAAAIASSSNRSQQQQQQQQQHQLLSAAYELQQQQQLQLQQQQQQQNSPTSSISIGRTELLLGDQSLRQDPRGNRRRSGSSIVVLDGDDLKPCLPDDYISGQHHLNHQQQLQLQQQLQQQHPLQQQHYRTHSGDIREIDQEMLTMLSVNQDNGPHREMAVDCPDTFIARNKTPPRYPPPRPPQKHKKSTNTTTTTTITALTNNDHANKMLIVAYHSSHQHEQLQQQHPSKTSTTTTTIALDVATQNLYNQKQQNKLEQIENYENCLQSERNEQHEQQFEQQKQHQATTAMAATQVAQQQTPSHKLQATLSSDPNGNSNSNNNSHIVGISSSSSSNNSSITDDFLCVVDGLYQGRKDTASPSSSAFDEVMSKHTLDSFGSIAYRHLHQQHQATSNGNSSSNTSNTNSNTNSNTNSNSNTNGNTSNNTAVSTKTATVTKTGVSSSNSNSNSLNSSNSSMHTSSSSSGHSSNIASATSSSSATSSSTVPDDLSLAPPGYEVSQQQQQQHLVATPVTMLLPPMAKHRELPVDVPDSFIEMVKTTPRYPPPAHLSSRGSLLSNGSASTAHTTLSSMGVAPSPVTATAAAAASASAACATTAVAAAAVSGVADGDARRVADELNGNAKPVPPPRDHLRVEKDGRLVNCSPAPQLPDRRAPGNASSGSSGATTHPLQHQQIAQIVEPTLEQLDSIKKYQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPHTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: CBS domain-containing protein (Q38BM9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Association with the SNF1 complex
- Protein kinase, putative
- Cystathionine beta-synthase, putative
- phosphatidylinositol 3-kinase
- Atg6 BARA domain-containing protein
- Protein kinase, putative
- GMP synthase
- Protein kinase, putative
- non-specific serine/threonine protein kinase
- Nitrate reductase, putative
Sequence:
MSQYDHLFDTPAAYIAASSESRRNSVAVAASSITSNNFGPESHGHRTSQQVGYFPTDDECKQLANPVRELLSRCRCYEVLGTSTQVVLLDVDVELTTAFIAAQERGLAACVLWDREECAVCGVLSSTDYIEILLYCSDHPDEAERVPQYTIRYWREKVRNYKPSGTVNAGATEAETLANSFDRLCSLSPVPPLITCTSETSVSECLAQIMNNKAKRIVVLVEKESEDFNVKALLDLQQILSYLGALFLSVESQGSGPRGVSADTAMSSSITSREASDYAEGTGGPSALEAVSGYRPFIDSVVASNSEFSRGGVTLPLHVRNLHDLVLNEGRENPVDFGSYASVGPYKAITDVPFRFVPQLGQHRKTPISVTLETPFLDALRLLLLHNIDCIAVVSENDVVVDAIGRSDIVRIEDNGVYNTQLTVRGALGDRPPKKIRVFYENDTLREIFIFFVRQRVRELFLVDPNTKKLRGQLNISEVVFFLVFGTTNTNNPSKSQCGCGT
Protein: 3-phosphoinositide-dependent protein kinase 1 (AtPDK1) (EC 2.7.11.1) (Q9XF67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May couple lipid signals to the activation-loop phosphorylation of several protein kinases of the so-called AGC kinase family. Interacts via its pleckstrin homology domain with phosphatidic acid, PtdIns3P and PtdIns(3,4)P2 and to a lesser extent with PtdIns(4,5)P2 and PtdIns4P. May play a general role in signaling processes controlling the pathogen/stress response, polar auxin transport and development. Transphosphorylates the AGC protein kinases OXI1/AGC2-1, PK1/S6K1, PK19/S6K2 and PID resulting in their activation.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Membrane-associated after cell stimulation. {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase AtPK2/AtPK19
- Serine/threonine-protein kinase AtPK1/AtPK6
- Cytochrome b561 and DOMON domain-containing protein At5g35735
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein eS6z
- Serine/threonine-protein kinase TOR
- BSD domain-containing protein
- Glycine-rich protein family
- At4g28210
- Phospholipase D alpha 4
Sequence:
MLAMEKEFDSKLVLQGNSSNGANVSRSKSFSFKAPQENFTSHDFEFGKIYGVGSYSKVVRAKKKETGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQDTSSLYMALESCEGGELFDQITRKGRLSEDEARFYTAEVVDALEYIHSMGLIHRDIKPENLLLTSDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTEPSRRPGAGSEGYVALKRHPFFNGVDWKNLRSQTPPKLAPDPASQTASPERDDTHGSPWNLTHIGDSLATQNEGHSAPPTSSESSGSITRLASIDSFDSRWQQFLEPGESVLMISAVKKLQKITSKKVQLILTNKPKLIYVDPSKLVVKGNIIWSDNSNDLNVVVTSPSHFKICTPKKVLSFEDAKQRASVWKKAIETLQNR
Protein: Cis-retinol/androgen dehydrogenase type 3 (Q76LB8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MWLFLVALVGMWTLLCFFRERQVVSYLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKERVGSRGLWGLVNNAGISIPSGPNEWMKKQDFAHVLDVNLLGLIEVTLSMLPLVRKARGRVINVASVLGRVSLCGGAYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLWDQTSSEIREIYGEKYLASYLKRLNELDKRCNKDLSGVTDCMEHALTACHPHTRYSAGWDAKLFYLPLSYLPTFLVDALLFWTSLKPEKAL
Protein: PFTAIRE-interacting factor 2 (Q8WTI6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCSPCCGSCCGPCCSPCCSPCCPPCCNDCCGSCCSPCCGPCCSPCCGPCCSPCCSPCCTPCCTPCCTPCCKCCTPCCVPCCTPCCTPCCTPCCTPCCSPCCGPCCSPCCSPCGGSKCK
Protein: Basic helix-loop-helix transcription factor scleraxis (Class A basic helix-loop-helix protein 41) (bHLHa41) (Class A basic helix-loop-helix protein 48) (bHLHa48) (Q7RTU7)
Organism: Homo sapiens (Human)
Function: Plays an early essential role in mesoderm formation, as well as a later role in formation of somite-derived chondrogenic lineages.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Tenomodulin
- Homeobox protein Mohawk
- Paired box protein Pax-1
Sequence:
MSFATLRPAPPGRYLYPEVSPLSEDEDRGSDSSGSDEKPCRVHAARCGLQGARRRAGGRRAGGGGPGGRPGREPRQRHTANARERDRTNSVNTAFTALRTLIPTEPADRKLSKIETLRLASSYISHLGNVLLAGEACGDGQPCHSGPAFFHAARAGSPPPPPPPPPARDGENTQPKQICTFCLSNQRKLSKDRDRKTAIRS
Protein: Agglutinin-1 (Agglutinin I) [Cleaved into: Agglutinin-1 chain A (EC 3.2.2.22) (AAG-A); Agglutinin-1 chain B (AAG-B)] (Q9M6E9)
Organism: Abrus precatorius (Indian licorice) (Glycine abrus)
Function: The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA (By similarity). Less toxic than abrin-a.
Interaction partners:
Sequence:
MKFETTKNKLHGNAYYQAQFQDPIKFTTGSATPASYNQFIDALRERLTGGLIYGIPVLRDPSTVEKPNQYVTVELSYSDTVSIQLGIDLTNAYVVAYRAGSESFFFRNAPASASTYLFTGTQQYSLPFDGNYDDLEKWAHQSRQRISLGLEALRQGIKFLRSGASDDEEIARTLIVIIQMVAEAARFRYVSKLVVISLSNRAAFQPDPSMLSLENTWEPLSRAVQHTVQDTFPQNVTLINVRQERVVVSSLSHPSVSALALMLFVCNPLNATQSPLLIRSVVEQSKICSSHYEPTVRIGGRDGLCVDVSDNAYNNGNPIILWKCKDQLEVNQLWTLKSDKTIRSKGKCLTTYGYAPGNYVMIYDCSSAVAEATYWDIWDNGTIINPKSGLVLSAESSSMGGTLTVQKNDYRMRQGWRTGNDTSPFVTSIAGFFKLCMEAHGNSMWLDVCDITKEEQQWAVYPDGSIRPVQNTNNCLTCEEHKQGATIVMMGCSNAWASQRWVFKSDGTIYNLYDDMVMDVKSSDPSLKQIILWPYTGNANQMWATLF
Protein: Vesicular glutamate transporter 3 (VGluT3) (Solute carrier family 17 member 8) (Q8BFU8)
Organism: Mus musculus (Mouse)
Function: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter that mediates the uptake of L-glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification (By similarity). At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation (By similarity). The symporter activity is electrogenic (By similarity). Moreover, operates synergistically with SLC18A3/VACHT under a constant H(+) gradient, thereby allowing striatal vesicular acetylcholine uptake.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q7TSF2}. Cell membrane {ECO:0000250|UniProtKB:Q8NDX2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NDX2}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q7TSF2}.
Interaction partners:
- Vesicular acetylcholine transporter
- Vesicular inhibitory amino acid transporter
- Synaptic vesicular amine transporter
- Otoferlin
- Chromaffin granule amine transporter
- Vesicular glutamate transporter 2
- Vesicular glutamate transporter 1
- Synaptophysin
- Synapsin-1
- Vesicle-associated membrane protein 2
Sequence:
MPFKAFDTFKEKILKPGKEGVKNAVGDSLGILQRKIDGTNEEEDAIELNEEGRPVQTSRAHRPVCDCSCCGIPKRYICDCSCCGIPKRYIIAVMSGLGFCISFGIRCNLGVAIVEMVNNSTVYVDGKPEIQTAQFNWDPETVGLIHGSFFWGYIVTQIPGGFISNKFAASRVFGAAIFLTSTLNMFIPSAARVHYGCVMGVRILQGLVEGVTYPACHGMWSKWAPPLERSRLATTSFCGSYAGAVVAMPLAGVLVQYIGWASVFYIYGMFGIIWYMFWLLQAYECPAAHPTISNAERTYIETSIGEGANLASLSKFNTPWRRFFTSLPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFAISKVGLLSAVPHMVMTIVVPIGGQLADYLRSRKILTTTAVRKIMNCGGFGMEATLLLVVGFSHTKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPLIVGAMTKHKTREEWQNVFLIAALVHYSGVIFYGVFASGEKQDWADPENLSEDKCGIIDQDELAEETELNHETFVSPRKKMSYGATTQNCEVQKTEWRQQRESAFDGEEPLSYQAEGDFSETS
Protein: Histidine-rich glycoprotein (Histidine-proline-rich glycoprotein) (HPRG) (P04196)
Organism: Homo sapiens (Human)
Function: Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis.
Subcellular location: Secreted {ECO:0000269|PubMed:21215706}.
Interaction partners:
- Plasminogen
- Kininogen-1
- Fibrinogen alpha chain
- Alpha-2-HS-glycoprotein
- Antithrombin-III
- Alanine--glyoxylate aminotransferase
- Fibrinogen gamma chain
- Heparin cofactor 2
- Beta-2-glycoprotein 1
- Apolipoprotein A-V
Sequence:
MKALIAALLLITLQYSCAVSPTDCSAVEPEAEKALDLINKRRRDGYLFQLLRIADAHLDRVENTTVYYLVLDVQESDCSVLSRKYWNDCEPPDSRRPSEIVIGQCKVIATRHSHESQDLRVIDFNCTTSSVSSALANTKDSPVLIDFFEDTERYRKQANKALEKYKEENDDFASFRVDRIERVARVRGGEGTGYFVDFSVRNCPRHHFPRHPNVFGFCRADLFYDVEALDLESPKNLVINCEVFDPQEHENINGVPPHLGHPFHWGGHERSSTTKPPFKPHGSRDHHHPHKPHEHGPPPPPDERDHSHGPPLPQGPPPLLPMSCSSCQHATFGTNGAQRHSHNNNSSDLHPHKHHSHEQHPHGHHPHAHHPHEHDTHRQHPHGHHPHGHHPHGHHPHGHHPHGHHPHCHDFQDYGPCDPPPHNQGHCCHGHGPPPGHLRRRGPGKGPRPFHCRQIGSVYRLPPLRKGEVLPLPEANFPSFPLPHHKHPLKPDNQPFPQSVSESCPGKFKSGFPQVSMFFTHTFPK
Protein: RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1) (RNA binding motif protein, X chromosome retrogene) (Q91VM5)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein which may be involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Heterogeneous nuclear ribonucleoprotein U
- Heterogeneous nuclear ribonucleoprotein A3
- Poly
- RNA-binding motif protein, X chromosome
- RNA binding motif protein, X-linked-like 2
- DNA topoisomerase 1
Sequence:
MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEILLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGSGGTRGPPSRGGYMDDGGYSMNFNMSSSRGPLPVKRGPPPRSGGPPPKRSTPSGPVRSSSGMGGRTPVSRGRDSYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSRDYPSSRDTRDYAPPPRDYTYRDYSHSSSRDDYPSRGYGDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGYGGSRDSYSSSRSDLYSSGRDRVGRQERGLPPSMERGYPPPRDSYSSSSRGAPRGGGRGGSRSDRGGGRSRY
Protein: Ankyrin repeat domain 27 (A0A0G2K7U7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MALYDEDLLRNPFYLALQKWRPDLCSKVAQIHGIVLVPCRGSLPSNVQASCQFESYVLVPMEGHFQTLDGKAVLIEGNRVKLGAGFACLLSVPILFEETFYNEKEESFSILCIAHPLEKRETSEEPSAPSDPFSLKTIKDVREFLGRHSERFDKHIASFHRTFRECERKSLRHLIDSVNALYTKCLQQLLRDSHLKVLAKQEAQMNLMKQAVEMYVHHDIYDLIFKYVGTMEASEDAAFNKITRSLQDLQQKDIGVKPEFSFNIPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETVCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSSPKDELGYCLTSVEAAIEYIRQGSLSAQPPDAEGFGDRLFLKQRMNLLSQMSSTPIDCLFKHIASGNQKEVERLLSQDDQDKDAMQKMCHPLCSCEDCEKLVSGRLNDPSVVTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSKILSAMEAYHLSSDRRPKPSEVPAPSPTRSADSISQGSSTSSFSSVSVSFRPEEVKKDYREVEKLLRAVADGDLEMVRYLLEWTEDDLDDMDEAISTVDLEFCHPLCQCPKCAPAQKKLARIPANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCAEQDSKIMELLQVVPSCVAASPNNVVVVQETEHEDYVTVEIRKKCVLLFYSQGTPKCTTCQRNLFGDSFASLTQGGGSSEERTKSWETMGRDRSVPDLTGGLQEPEKQRVTGKQNDLSDQSRCQTSEEGNKGLPGRPVPRQAVPGHRPMVRRHTVNDAAILQVPEVTGHLTTQEAGVSRS
Protein: Sodium/hydrogen exchanger (B7YZY4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSIRTEQDYDSATPALAQQMNLARRACWRIKSYSSESLFKTYASVITDTSANEIDAEAPPPPRDKTKTRIEPQIAPAKRNSSCTSSDWRGMFSKRTLLICALALILGSAQARPNTSAVGVAPRKVSQDIVDAVTQLNLGQSAPIDAVDVGLDPTPSARVPRPEPLKSGDENAKGDEGHKMERYPLSSVDFARVKTPFIIGIWILSASIAKIGFHMTPKLHLIFPESCLLIVVGVVIGVVLYFCTDVAVSPLTPNTFFFYMLPPIILDAGYFMPNRLFFDNLGTILLMAVVGTIFNIATIGGSLYACGKMGIYGESETPGLMDVFLFASLISAVDPVAVLAVFEEIHVNEILYIVVFGESLLNDAVTVVMYHMMESYNEIGLDKIIAQDIASGVGSFFVVALGGTAIGIIWGFLTGLVTRFTDHVRVIEPIFIFVMAYLAYLNAEIFHMSGILAITFCGITMKNYVESNISQKSHTTVKYALKMLSSSAETIIFMFLGVATVNNMHVWNTWFVVLTIAFCSVFRVIGVILLSALANRFRLHKLSRVDQFVMSYGGLRGAVAFALVLLVDENVVKQKNMFVTTTIAVIYFTVFLQGITIKPLVKILNVKRANKRKPTMNERIHERFMDHLMAGIEDIVGKTGNYNVRDKFKRFDNRFIRPLLIRDLKEINELHLLDHIPMQSYERALNTNRGPSASNADGKSRRQRRYSRISSRMNPFRNMNDKI
Protein: Anthranilate synthase component 2, pyocyanine specific (AS) (ASII) (EC 4.1.3.27) (Anthranilate synthase beta subunit, pyocyanine specific) (Anthranilate synthase, GATase component) (Anthranilate synthase, glutamine amidotransferase component) (P09786)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, a precursor for Pseudomonas quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which is required to induce the genes for the biosynthesis of the virulence factor pyocyanine (PCN), a characteristic blue-green phenazine pigment produced by P.aeruginosa. In the first step, the glutamine-binding beta subunit (PhnB) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (PhnA) to produce anthranilate (By similarity).
Interaction partners:
- Anthranilate phosphoribosyltransferase
- Anthranilate synthase component 1, pyocyanine specific
- Anthranilate synthase component 1
- aminodeoxychorismate synthase
- Anthranilate--CoA ligase
- Indole-3-glycerol phosphate synthase
- N-
- anthranilate synthase
- Anthraniloyl-CoA anthraniloyltransferase
- 2-aminobenzoylacetyl-CoA thioesterase
Sequence:
MRITLLDNFDSFTYNLVEQFCLLGAEVRVMRNDTPLPTIQAALLADGCELLVLSPGPGRPEDAGCMLELLAWARGRLPVLGVCLGHQALALAAGGAVGEARKPLHGKSTSLRFDQRHPLFDGIADLRVARYHSLVVSRLPEGFDCLADADGEIMAMADPRNRQLGLQFHPESILTTHGQRLLENALLWCGALAVRERLRA
Protein: Acetyl-CoA acyltransferase 2 (A0A0B4J2A4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
Protein: Lysophosphatidic acid receptor 4 (LPA receptor 4) (LPA-4) (G-protein coupled receptor 23) (P2Y purinoceptor 9) (P2Y9) (Purinergic receptor 9) (Q8BLG2)
Organism: Mus musculus (Mouse)
Function: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Transduces a signal by increasing the intracellular calcium ions and by stimulating adenylyl cyclase activity. The rank order of potency for agonists of this receptor is 1-oleoyl- > 1-stearoyl- > 1-palmitoyl- > 1-myristoyl- > 1-alkyl- > 1-alkenyl-LPA (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Lysophosphatidic acid receptor 1
- Lysophosphatidic acid receptor 2
- Lysophosphatidic acid receptor 3
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Lysophosphatidic acid receptor 5
- Prothrombin
- Angiotensinogen
- Lysophosphatidic acid receptor 6
Sequence:
MGDRRFIDFQFQDLNSSLRPRLGNATANNTCIVDDSFKYNLNGAVYSVVFILGLITNSASLFVFCFRMKMRSETAIFITNLALSDLLFVCTLPFKIFYNFNRHWPFGDTLCKISGTAFLTNIYGSMLFLTCISVDRFLAIVYPFRSRTIRTRRNSAIVCAGVWILVLSGGISASLFSTTNVNNATTTCFEGFSKRVWKTYLSKITIFIEVVGFIIPLILNVSCSSVVLRTLRKPATLSQIGTNKKKVLKMITVHMAVFVVCFVPYNSVLFLYALVRSQAITNCLLERFAKIMYPITLCLATLNCCFDPFIYYFTLESFQKSFYINTHIRMESLFKTETPLTPKPSLPAIQEEVSDQTTNNGGELMLESTF
Protein: Farnesyltranstransferase (EC 2.5.1.29) (A7IAG2)
Organism: Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)
Interaction partners:
- Isopentenyl-diphosphate delta-isomerase
- Isopentenyl phosphate kinase
- Di-trans-poly-cis-decaprenylcistransferase
- Tritrans,polycis-undecaprenyl-diphosphate synthase
- Ribonuclease J
- Glutamate--tRNA ligase
- Mevalonate kinase
- Enolase
- Shikimate dehydrogenase
- Exonuclease VII, small subunit
Sequence:
MEADMSDLSAYLKSVAQQIDGMIEKNFTHAGGELDRASAHLLSAGGKRLRPAVVMLSADAIRHGSSKDVMPAALALEVTHTFTLIHDDIMDGDSLRRGVPTVHTKWDMPTGILAGDVLYARAFEFICQSKADEGPKVQAVALLARACADICEGQHQDMSFEHRADVTEEEYMAMVAKKTGVLYAAAAAIGGTLAGGNPEQIRALYQFGLNTGIAFQIQDDLIDLLTPTEKSGKDQGSDLREGKQTLVMIIARQKGVDLLKYRHELSPADIKAAIQELTDAGVIDAVKKKAADLVADSNRLLMVLPPTKERQLIMDVGEFFVTRSF
Protein: Protein Wnt-5 (dWnt-3) (dWnt-5) (P28466)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds as a ligand to a family of frizzled seven-transmembrane receptors and acts through a cascade of genes on the nucleus. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. May have a role in limb and CNS development; may be a downstream target of Dll that acts in the specification of these primordia.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Frizzled
- Frizzled-3
- Low-density lipoprotein receptor-related protein
- Frizzled-2
- Segment polarity protein dishevelled
- Tyrosine-protein kinase Drl
- Frizzled-4
- Protein-serine O-palmitoleoyltransferase porcupine
- Protein wntless
- Palmitoleoyl-protein carboxylesterase NOTUM
Sequence:
MSCYRKRHFLLWLLRAVCMLHLTARGAYATVGLQGVPTWIYLGLKSPFIEFGNQVEQLANSSIPLNMTKDEQANMHQEGLRKLGTFIKPVDLRDSETGFVKADLTKRLVFDRPNNITSRPIHPIQEEMDQKQIILLDEDTDENGLPASLTDEDRKFIVPMALKNISPDPRWAATTPSPSALQPNAKAISTIVPSPLAQVEGDPTSNIDDLKKHILFLHNMTKTNSNFESKFVKFPSLQKDKAKTSGAGGSPPNPKRPQRPIHQYSAPIAPPTPKVPAPDGGGVGGAAYNPGEQPIGGYYQNEELANNQSLLKPTDTDSHPAAGGSSHGQKNPSEPQVILLNETLSTETSIEADRSPSINQPKAGSPARTTKRPPCLRNPESPKCIRQRRREEQQRQRERDEWFRGQSQYMQPRFEPIIQTINNTKRFAVSIEIPDSFKVSSEGSDGELLSRVERSQPSISSSSSSSSSSSRKIMPDYIKVSMENNTSVTDYFKHDVVMTSADVASDREFLIKNMEEHGGAGSANSHHNDTTPTADAYSETIDLNPNNCYSAIGLSNSQKKQCVKHTSVMPAISRGARAAIQECQFQFKNRRWNCSTTNDETVFGPMTSLAAPEMAFIHALAAATVTSFIARACRDGQLASCSCSRGSRPKQLHDDWKWGGCGDNLEFAYKFATDFIDSREKETNRETRGVKRKREEINKNRMHSDDTNAFNIGIKRNKNVDAKNDTSLVVRNVRKSTEAENSHILNENFDQHLLELEQRITKEILTSKIDEEEMIKLQEKIKQEIVNTKFFKGEQQPRKKKRKNQRAAADAPAYPRNGIKESYKDGGILPRSTATVKARSLMNLHNNEAGRRAVIKKARITCKCHGVSGSCSLITCWQQLSSIREIGDYLREKYEGATKVKINKRGRLQIKDLQFKVPTAHDLIYLDESPDWCRNSYALHWPGTHGRVCHKNSSGLESCAILCCGRGYNTKNIIVNERCNCKFHWCCQVKCEVCTKVLEEHTCK
Protein: Lactaldehyde dehydrogenase (EC 1.2.1.22) (Aldehyde dehydrogenase A) (Glycolaldehyde dehydrogenase) (EC 1.2.1.21) (P25553)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the irreversible oxidation of L-lactaldehyde to L-lactate. Also shows high activity with glycolaldehyde and L-glyceraldehyde. Has weaker activity with various aldehydes such as methylglyoxal, propionaldehyde or benzaldehyde. Involved in the degradation of lactaldehyde produced during metabolism of L-fucose and L-rhamnose. It may be involved in several other metabolic pathways.
Interaction partners:
- Lactaldehyde reductase
- L-lactate dehydrogenase
- Glyoxylate/hydroxypyruvate reductase A
- Glycolate oxidase subunit GlcD
- NADP-dependent malic enzyme
- Probable pyruvate-flavodoxin oxidoreductase
- Glyoxylate/hydroxypyruvate reductase B
- Lactoylglutathione lyase
- D-lactate dehydrogenase
- Formate acetyltransferase 1
Sequence:
MSVPVQHPMYIDGQFVTWRGDAWIDVVNPATEAVISRIPDGQAEDARKAIDAAERAQPEWEALPAIERASWLRKISAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPRGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMATAAKNITKVCLELGGKAPAIVMDDADLELAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVAFGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEDAISMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQS
Protein: Probable thiol methyltransferase 2 (EC 2.1.1.9) (Protein HARMLESS TO OZONE LAYER 3) (AtHOL3) (Q6AWU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: S-adenosyl-L-methionine-dependent methyltransferase.
Interaction partners:
- RING-type E3 ubiquitin transferase
- At4g24340
- Phosphorylase superfamily protein
- ATP-dependent protease La
- At5g01015
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Fanconi anemia group F protein
- Small ribosomal subunit protein mL103
- Pentatricopeptide repeat-containing protein At2g18520
- ARM repeat superfamily protein
Sequence:
MENAGKATSLQSSRDLFHRLMSENSSGGWEKSWEAGATPWDLGKPTPVIAHLVETGSLPNGRALVPGCGTGYDVVAMASPDRHVVGLDISKTAVERSTKKFSTLPNAKYFSFLSEDFFTWEPAEKFDLIFDYTFFCAFEPGVRPLWAQRMEKLLKPGGELITLMFPIDERSGGPPYEVSVSEYEKVLIPLGFEAISIVDNELAVGPRKGMEKLGRWKKSSTFHSTL