wanglab/gogpt-training-data huggingface dataset:
Protein: Effector protein hopW1-1 (Type III effector hopPmaA) (Q8RP17)
Organism: Pseudomonas syringae pv. maculicola
Function: Induces hypersensitive response (HR).
Subcellular location: Secreted {ECO:0000269|PubMed:11872842}. Note=Secreted via type III secretion system (T3SS).
Interaction partners:
Sequence:
MSPAQIIRTPHSFPPSFTGTSSSAENSHAQSPQQVLTRAFVASGELNAAFGRTSTASEQDFTSLLGTLQRELERKTLSFPDIAELANQLAEAAKGDQGGHWLGRDEQQTLKGMIDRCKSQLAHTHASDASYDPLAQVCENLKTARLHQSISQMTGEAHAKVRGVPDLLALIQLDPDVLAEKPVGMTSYVNFGSFICMAKARTAELSEDLRSDPNEVALLLHPHADTILELERLPDALAALTENCPDTPTRDDLRSLAKETGELLQQLRANDLLPRSEEVSSYQGETSVRSREVVEPKLTLCQAGGNGQGQLEASSARPESLRYAPTRAASSGSEARVPGQAVGGKIADDAQKVAGLYAEKKRTNWTQANGVAGKISHKIQSLLGMRDAGSRVQAFVAFMADGKGRPGATMLDLGDGWMRATRVIKGEAALIDFQCDSDGKVVDARHPGRFPVLPQGNEREAFKTVLQELKFRGAETLSKVPVYYVNRNTRGYVIPTHGYVVAGHPNRGRKSGAVLYGVGGDPKRGPVALDEKLLGHLVGRSDSKTSSKLSAPVKAAISALAGASFATREDFYDAYCAVRGDAVDPLERHNEISSIYRLLPLSTMEMWPKKADDYRVARPAAPERDLRAFENLPKDIGRKAQLKKVSNVDSIDLLEAKRQFTLHQLYQDEMLGRNGTGVPSADFKPKVDAQRRDQLVASTPKFQRLPPHTTDKVGNCNTGASSLLQRAVDTYTEKNNLPPEKVTAASIFGIGSSHRLAIWDPLDGSSSNKSSKDR
Protein: Auxin response factor 3 (Protein ETTIN) (O23661)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression. Involved in the establishment or elaboration of tissue patterning during gynoecial development.
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor AS1
- Axial regulator YABBY 5
- Probable transcription factor KAN2
- Protein ASYMMETRIC LEAVES 2
- Axial regulator YABBY 1
- Auxin-responsive protein IAA9
- Probable transcription factor KAN4
- Transcription repressor KAN1
- RNA-dependent RNA polymerase 6
- Protein argonaute 7
Sequence:
MGGLIDLNVMETEEDETQTQTPSSASGSVSPTSSSSASVSVVSSNSAGGGVCLELWHACAGPLISLPKRGSLVLYFPQGHLEQAPDFSAAIYGLPPHVFCRILDVKLHAETTTDEVYAQVSLLPESEDIERKVREGIIDVDGGEEDYEVLKRSNTPHMFCKTLTASDTSTHGGFSVPRRAAEDCFPPLDYSQPRPSQELLARDLHGLEWRFRHIYRGQPRRHLLTTGWSAFVNKKKLVSGDAVLFLRGDDGKLRLGVRRASQIEGTAALSAQYNQNMNHNNFSEVAHAISTHSVFSISYNPKASWSNFIIPAPKFLKVVDYPFCIGMRFKARVESEDASERRSPGIISGISDLDPIRWPGSKWRCLLVRWDDIVANGHQQRVSPWEIEPSGSISNSGSFVTTGPKRSRIGFSSGKPDIPVSEGIRATDFEESLRFQRVLQGQEIFPGFINTCSDGGAGARRGRFKGTEFGDSYGFHKVLQGQETVPAYSITDHRQQHGLSQRNIWCGPFQNFSTRILPPSVSSSPSSVLLTNSNSPNGRLEDHHGGSGRCRLFGFPLTDETTAVASATAVPCVEGNSMKGASAVQSNHHHSQGRDIYAMRDMLLDIAL
Protein: Y+L amino acid transporter 2 (Solute carrier family 7 member 6) (y(+)L-type amino acid transporter 2) (Y+LAT2) (y+LAT-2) (D3ZMM8)
Organism: Rattus norvegicus (Rat)
Function: Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux routeby exporting cationic amino acids such as L-arginine from inside the cells in exchange with neutral amino acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and may participate in nitric oxide synthesis. Also exchanges L-arginine with L-lysine in a sodium-independent manner. The transport mechanism is electroneutral and operates with a stoichiometry of 1: 1 (By similarity). Contributes to ammonia-induced increase of L-arginine uptake in cerebral cortical astrocytes leading to ammonia-dependent increase of nitric oxide (NO) production via inducible nitric oxide synthase (iNOS) induction, and protein nitration. May mediate transport of ornithine in retinal pigment epithelial (RPE) cells (By similarity). May also transport glycine betaine in a sodium dependent manner from the cumulus granulosa into the enclosed oocyte (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q92536}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A2
- Amino acid transporter heavy chain SLC3A1
- Large neutral amino acids transporter small subunit 4
Sequence:
MEARELGSPTPTYHLLPKANQHTVKEDASSPSQGSPETMQLKKEISLLNGVSLVVGNMIGSGIFVSPKGVLKYTASYGLSLVVWAIGGLFSVVGALCYAELGTTITKSGASYAYILEAFGGFIAFIRLWVSLLIVEPTSQAIIAITFANYIIKPSFPTCDPPYVACRLLAAACVCLLTFVNCAYVKWGTRVQDTFTYAKVLALIAIIIMGLVKLCQGHTEHFQDAFKGSSWNVGDLSLALYSALFSYSGWDTLNFVTEEIKNPERNLPLAIGISMPIVTLIYILTNVAYYTVLNIQDVHKSDAVAVTFADQTFGMFSWTIPIAVALSCFGGLNASIFASSRLFFVGSREGHLPNLLSMIHIERFTPVPALLFNCTMTLIYLVVKDVFLLINYFSFSYWFFVGLSVVGQLYLRWKEPDWPRPLKLSLFFPIVFCICSLFLVAVPLFSDTINSLIGIGIALSGVPVYFMGVYLPEARRPLFIRKVLATVTRVTQKLCFCVLTELDVAEEKNVERKTD
Protein: Melanocortin-2 receptor accessory protein 2B (zMRAP2b) (P0DM64)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Activator of melanocortin receptor 4 (mc4r), a receptor involved in energy homeostasis. Plays a role after larval development in the control of energy homeostasis and body weight regulation by increasing ligand-sensitivity of mc4r and mc4r-mediated generation of cAMP once the zebrafish begins feeding, increasing the capacity for regulated feeding and growth.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Melanocortin receptor 4
- Melanocortin receptor 5
- Melanocortin receptor 5
- Melanocortin 2 receptor.
- Melanocortin 3 receptor
Sequence:
MSEYSNRSQAGADYEWHYEYYEDEEPVSFEGLRANRYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHPEMCDASMKPHVLIGCELEVGGSLAFSLPPLPDQSRSLFHFYIHKEERVKTHKDAVIGRGMHCGRGNAERADEDEHFMSSFNIPNFVNSEQSSSLGHDDFLLSEPPIITDGQSDELKTAEPAHLCYDIIRH
Protein: V-type proton ATPase subunit d (V-ATPase subunit d) (DVA41) (V-ATPase 41 kDa accessory protein) (Vacuolar proton pump subunit d) (P54641)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system.
Interaction partners:
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- Vacuolar proton translocating ATPase 100 kDa subunit
- V-type proton ATPase subunit H
- V-type proton ATPase subunit C
- V-type proton ATPase subunit G
Sequence:
MGLFGGRKHGGLFTFNKDDGYLEAILRGFKKGILSRADYNNLCQCDNLEDMKMHFISTDYGDFLAGEPSPIHTTTIAEKATGKLVSEFNHIRNQAVEPLSTFMDFISYGYMIDNVVLLITGTLHERDISELVDKCHPLGLFKSMATLSVVHNVADLYNNVLIDTPLAPYIQGCLSEEDLDEMNIEIIRNTLYKAYLEDFYNYCKYLGGQTELIMSDILKFEADRRSINITINSFGATELSKDDREKLYPSLGLLYPEGTSKLGKAEDVDQVRGILEVYSTYRNFFSDGVNNEKSLEDSFFEHEVHLNRMAFEDQYGYGVFYAYIKLREQEIRNIVWIAECISQNMKQKMNQYIPIF
Protein: Signal peptidase complex subunit 1 (Microsomal signal peptidase 12 kDa subunit) (SPase 12 kDa subunit) (O44953)
Organism: Caenorhabditis elegans
Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Dispensable for SPC enzymatic activity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P83362}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P83362}.
Interaction partners:
- Signal peptidase complex subunit 2
- Signal peptidase complex subunit 3
- Signal peptidase complex catalytic subunit SEC11
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit dad-1
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit gamma
- Mitochondrial inner membrane protease subunit 2
- Peptidase S26 domain-containing protein
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
- Signal recognition particle 9 kDa protein
Sequence:
MDGMIAMLPAPLQKLSSHIDFQGQKVAERTYQVILTIAGIIGFLVGFWTQQLSYAMFTVLGASAFTALIILPPWPFLFRKNPIVWHTPAEPQESGDKKKETKKTK
Protein: PH and SEC7 domain-containing protein 2 (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 C) (Exchange factor for ARF6 C) (Pleckstrin homology and SEC7 domain-containing protein 2) (Q6P1I6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000269|PubMed:23603394}; Single-pass membrane protein {ECO:0000305}. Cell projection, ruffle membrane {ECO:0000269|PubMed:23603394}. Cleavage furrow {ECO:0000269|PubMed:23603394}. Note=In interphase associated with the plasma membrane, in particular with membrane ruffling regions. In cells undergoing cytokinesis, transiently found around the ingressing cleavage furrow. Not detected at the midbody ring/Flemming body. {ECO:0000269|PubMed:23603394}.
Interaction partners:
Sequence:
MDEEKLPCELHKEGSATQEDHGLEPEEEPGLQNGTAASEGLSSHISGPGGEKTLEGTMEPVRGPDVALPGLNLSLTNGLALGQDGNILEDSIEFKTWRSGPAEEEDVPGSPCPDAGDPQLGLDCPGEPDVRDGFSATFEKILESELLRGTQYSSLDSLDVLSLTDESDSCVSFEAPLTPLIQQRARDSPEAGAGLGNGDMGPEGDLGATGGCDGELGSPLRRSISSSRSENVLSHLSLTSVPNGFHEDGPGGSGGDDEDDEDTDKLLNSASDTSLKDGLSDSDSELSSSEGLEPGSTDPLANGCQGVSEAARRLARRLYHLEGFQRCDVARQLGKNNEFSRLVAGEYLSFFDFSGLTLDRALRTFLKAFPLMGETQERERVLTHFSRRYCQCNPDDSTSEDGIHTLTCALMLLNTDLHGHNIGKKMSCQQFIANLDQLNDGQDFAKDLLKTLYNSIKNEKLEWAIDEDELRKSLSELVDDKFGTGTKKVTRILDGGNPFLDVPQALNATTYKHGVLTRKTHADMDGKRTPRGRRGWKKFYAVLKGTILYLQKDEYRLDKALSEGDLKNAIRVHHALATRASDYSKKSNVLKLKTADWRVFLFQAPSKEEMLSWILRINLVAAIFSAPAFPAAVSSMKKFCRPLLPSCTTRLCQEEQLRSHENKLRQVTAELAEHRCHPLERGLKSKEAEEYRLKEHYLTFEKSRYETYIHLLAVKIKVGSDDLERIEARLATIEGDDPALRKTHSSPALSLGHGPVTGSKATKDTSASDT
Protein: Acryloyl-CoA reductase electron transfer subunit beta (Electron transfer flavoprotein large subunit) (ETFLS) (Electron transfer flavoprotein subunit beta) (Beta-ETF) (G3KIM6)
Organism: Anaerotignum propionicum (Clostridium propionicum)
Function: Part of the ETF-acryloyl-CoA reductase complex involved in the pathway of L-alanine fermentation. The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for acryloyl-CoA reductase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12603323}.
Interaction partners:
Sequence:
MAFNSADINSFRDIWVFCEQREGKLINTDFELISEGRKLADERGSKLVGILLGHEVEEIAKELGGYGADKVIVCDHPELKFYTTDAYAKVLCDVVMEEKPEVILIGATNIGRDLGPRCAARLHTGLTADCTHLDIDMNKYVDFLSTSSTLDISSMTFPMEDTNLKMTRPAFGGHLMATIICPRFRPCMSTVRPGVMKKAEFSQEMAQACQVVTRHVNLSDEDLKTKVINIVKETKKIVDLIGAEIIVSVGRGISKDVQGGIALAEKLADAFGNGVVGGSRAVIDSGWLPADHQVGQTGKTVHPKVYVALGISGAIQHKAGMQDSELIIAVNKDETAPIFDCADYGITGDLFKIVPMMIDAIKEGKNA
Protein: Nudix hydrolase 26, chloroplastic (AtNUDT26) (EC 3.6.1.-) (Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)) (Q9CAF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use diadenosine 5',5'''-P(1)P(5) pentaphosphate (Ap(5)A), diadenosine 5',5'''-P(1)P(4) tetraphosphate (Ap(4)A) and diadenosine 5',5'''-P(1)P(3) triphosphate (Ap(3)A) as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18815383}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 48
- Nudix hydrolase
- Nudix hydrolase 1
- Nudix hydrolase 20, chloroplastic
- mRNA-decapping enzyme subunit 2
- Nudix hydrolase 9
- Nudix hydrolase 5
Sequence:
MALYRPLLLHHPTSPSVTTFLRNYPSKPIKFSSLPFLHRCRKSRVSSSSARCCSSMESPPEGYRRNVGVCLMNSSKKIFTASRLDIPSAWQMPQGGIDEGEDPRVAVMRELKEETGVHSAEILAEAPHWITYDFPPDVREKLKVRWGSDWKGQAQKWFLLKFTGKDEEINLLGDGTEKPEFGEWSWTSPDQVVENAVEFKKPVYKEVMSAFASHLQ
Protein: LIM domain 7 (A0A8I5ZR48)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSNMPLPNGTAQPISTRLLPGRIAWSLCLSRAGSATKPRFQDNINVFLKACEQIGLKEAQLFHPGDLQDLSNRVTVKQEETDRRLKNVLITLYWLGRKAQNNPYYHGPYLNLKAFETLLGQALTKALEDSSCLKRSGRDSGYGDIWCPDRGDFPAPPGSHRREDSFESLDSLGSRSLTSCSSDLTLRGGREGCESDNDWEFTFKMQDYNKDDMSYRRISAIEPKSALPFNRFLPNKSKQPSYVPAPLRKKRPDKNEDNRRSWASPVYTETEGTFSRSKSLSDVSAEDVQSLRQLRYEEMQKIKSQLKEQDQKWQDDLAKWKDRRKSYTSDLQKKKEEREEIEKQALEKSDRSSKTFREMLQDRESQSSTTTSRRRIYSSDDILDDGVLPPTVTLSETSYQSERLEDKARAHPAEMPKEDSTTFASREDGIAAEIPLASHIPEERRQAPWPSAETRQASSSSAESHQASLPSTESDQARLPSAEPHQASFSSAEPRQVPLVSAEPHQASSFSSTEPHQASLSSALQRPSSLSSSQQSWSTRGESTRISASLPRSYQRSDTARLTSVVTARPFGTSSRGISSLPRSYTMDDGWKYNGDVEVVKREQHDSGRAAGMKPDSSHFILGSSSEKEVATGEDVASLSSFVLPSSSSLSHDQAASSKATFSSTSGLDSVSDSGEGRSSSLREVSRSPDQFSDMRISINQTPGTKHDFGFTIKWDVSGISVASVEKGSPAEFSQLQVDDEILAINNTKFSYKDTKKWEEAMANAQETGNLVMDVRRYGKSGSPETKWIDTTSGIYSTEKSSSLSVTTDFSESLQSPYSESKEINGIHEESNAFDSKASESISLKNLKRRSQFFEQGSSDSVAPDLPVPTLSAPSRWAWDQEEERRRQERWQKEQDRLLQEKYQREQEKLREEWQRAQQEAERENSKYLDEELMVLNSNSISLTSRESVTASWEPSWSEGSKSLDREGTRAGDEDRGQLEDDAVYEDQSQKLQERLMLEHEKKRKEQEAQEEELRKQREAEAQARAEAEAQARAEAQARAEAQAQAEAEARKRAEAQKLQAERERETSVKIYQYRRPIDSYDLPKREEESSGLLPIDRSKSRSTTELNDPLIEKSGSSKYSDRIGTTSFSQRSSKKDQGPSEAELERQQILQEMRKKTSLHNDNSWIRQRSASVNKEPICLTGIMRRGESLDNLDSQRPGSWRQSSWHSQPAGVYASSSVQDFSRLPPQLLSTSNRAYMRNPSSAVPPLAGSVKTSPGSPSPRSHSPSMSQSGSQLRNRSVSGKRVCSYCNSILGKGAAMIIETLGLCYHLHCFKCVSCERDLGGSSSGAEVRIRNHQLYCNDCYLRFKSGRPTAM
Protein: Rho GTPase-activating protein 26 (GTPase regulator associated with focal adhesion kinase) (GRAF1) (Oligophrenin-1-like protein) (Rho-type GTPase-activating protein 26) (Q9UNA1)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein for RHOA and CDC42.
Subcellular location: [Isoform 2]: Endosome membrane {ECO:0000269|PubMed:32344433}. Note=Colocalized with RAB8A, RAB8B and RAB10 on endosomal tubules. {ECO:0000269|PubMed:32344433}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27512058, ECO:0000269|PubMed:38081847}. Cell junction, focal adhesion {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with actin stress fibers and cortical actin structures. {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase N3
- Transforming protein RhoA
- Rho GTPase-activating protein 10
- Cell division control protein 42 homolog
- Delta and Notch-like epidermal growth factor-related receptor
- Cdc42 effector protein 2
- Amphiphysin
- C2 domain-containing protein 2
- Claudin-18
Sequence:
MGLPALEFSDCCLDSPHFRETLKSHEAELDKTNKFIKELIKDGKSLISALKNLSSAKRKFADSLNEFKFQCIGDAETDDEMCIARSLQEFATVLRNLEDERIRMIENASEVLITPLEKFRKEQIGAAKEAKKKYDKETEKYCGILEKHLNLSSKKKESQLQEADSQVDLVRQHFYEVSLEYVFKVQEVQERKMFEFVEPLLAFLQGLFTFYHHGYELAKDFGDFKTQLTISIQNTRNRFEGTRSEVESLMKKMKENPLEHKTISPYTMEGYLYVQEKRHFGTSWVKHYCTYQRDSKQITMVPFDQKSGGKGGEDESVILKSCTRRKTDSIEKRFCFDVEAVDRPGVITMQALSEEDRRLWMEAMDGREPVYNSNKDSQSEGTAQLDSIGFSIIRKCIHAVETRGINEQGLYRIVGVNSRVQKLLSVLMDPKTASETETDICAEWEIKTITSALKTYLRMLPGPLMMYQFQRSFIKAAKLENQESRVSEIHSLVHRLPEKNRQMLQLLMNHLANVANNHKQNLMTVANLGVVFGPTLLRPQEETVAAIMDIKFQNIVIEILIENHEKIFNTVPDMPLTNAQLHLSRKKSSDSKPPSCSERPLTLFHTVQSTEKQEQRNSIINSSLESVSSNPNSILNSSSSLQPNMNSSDPDLAVVKPTRPNSLPPNPSPTSPLSPSWPMFSAPSSPMPTSSTSSDSSPVRSVAGFVWFSVAAVVLSLARSSLHAVFSLLVNFVPCHPNLHLLFDRPEEAVHEDSSTPFRKAKALYACKAEHDSELSFTAGTVFDNVHPSQEPGWLEGTLNGKTGLIPENYVEFL
Protein: Dimethylglycine dehydrogenase, mitochondrial (EC 1.5.8.4) (ME2GLYDH) (Q63342)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the demethylation of N,N-dimethylglycine to sarcosine. Also has activity with sarcosine in vitro.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:2417560}.
Interaction partners:
- Betaine--homocysteine S-methyltransferase 1
- Glycine N-methyltransferase
- Pipecolic acid and sarcosine oxidase
- Glycine cleavage system P protein
- Glycine N-methyltransferase
- Sarcosine dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- Serine hydroxymethyltransferase
- Glycine cleavage system H protein, mitochondrial
Sequence:
MLRLGALRLRGLALRSSQGRPSSAGLREGQESPPSPPEWKDRAETVIIGGGCVGVSLAYHLAKAGMRDVVLLEKSELTAGSTWHAAGLTTYFHPGINLKKIHYDSIKLYERLEEETGQVVGFHQPGSIRLATTPERVDEFKYQMTRTNWHATEQYIIEPEKIHELFPLLNMDKILAGLYNPGDGHIDPYSLTMALATGARKYGVLLKYPAPVTSLKPRPDGTWDVETPQGSVRANRIVNAAGFWAREVGKMIGLDHPLIPVQHQYVVTSTIPEVKALKRELPVLRDLEGSYYLRQERDGLLFGPYESQEKMKLQASWVAHGVPPGFGKELFESDLDRITEHVEAAMEMVPVLKKADIINIVNGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGVGKYLSDWILHGEPPFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYKILESKCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFRPVGSEYKQVMQRVGVIDLSPFGKFNIKGQDSTQLLDHLCANVIPKVGFTNISHMLTPRGRVYAELTVSHQSPGEFLLITGSGSELHDLRWIEEAAVRGGYDVEIRNITDELGVLGVAGPYARRVLQKLTSEDLSDDVFKFLQTKSLKISDIPVTAIRISYTGELGWELYHRREDSAALYERIMNAGQEEGIDNFGTYALNALRLEKAFRAWGSEMNCDTNPLEAGLDYFIKLNKPADFTGKQALKQIKAKGLKRRLVCLTLATDDVDPEGNESVWYKGKVIGNTTSGSYSYSIQKSLAFAYVPVELSEVGQQVEVELLGKNYPATIIQEPLVLTEPTRTRLQKDGRKS
Protein: Microtubule actin crosslinking factor 1 (A0A0A6YYJ5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKPLSRPDCLRRNPSCLGKGEEEDGYIEDCYVPQRSIYDTMRINEQIDQGSKLNQTSKSTMEKMEGSTISSNGTLGAASNVFESRAPEGKKLDERIIFDALKLSSDVQKSAPVPPRRRPNAERKDNVNRRSWKSFMPPNFPEFAERIEASLSEVSEAGASNPSLQEKKESSSALTESSGHLDHREPQSESVTLEHVSKSIGIPEVQDFKNLSGDCQDFRFQQHSANPPHEFQPVESEAVATSGNTDVMQESRFSSATWPRATKSLAKGGFSEKQHPLGDTACTVEMPPLSPCLSEELLDPELHVLITPSLREKTESELKFEEDERWIMMEAEGEWEEEKLSDREKTFLMADEKNSLADIFEEREQANTAVVEDGSDCLAAVLRTFGHLSLGQICCPDDPQPAKDQLATVPKDIPLDCDCVLTGEDILGEVANRTAQGLEGLVSDSACTVGTIDAEQLSDTDSVQMFLELEKECLCEEGVTPLVELQNQISSEGLAASQDAENLLVISHFSGAALEKEQHLGLLHVRAKDYDTRLDCGYFNTLDSSQVPNAVELIAHVDIMRDTSTVSKEECEKVPFSPRTAEFKSRQPADLDSLEKLDPGGLLNSDHRVSHEEKLSGFIASELAKDNGSLSQGDCSQTEGNGEECIERVTFSFAFNHELTDVTSGPEVEVLYESNLLTDEIHLESGNVTVNQENNSLTSMGNVVTCELSVEKVCDEDGEAKELDYQATLLEDQAPAHFHRNFPEQVFQDLQRKSPESEILSLHLLVEELRLNPDGVETVNDTKPELNVASSEGGEMERRDSDSFLNIFPEKQVTKAGNTEPVLEEWIPVLQRPSRTAAVPTVKDALDAALPSPEEGTSIAAVPAPEGTAVVAALVPFPHEDILVASIVSLEEEDVTAAAVSAPERATVPAVTVSVPEGTAAVAAVSSPEETAPAVAAAITQEGMSAVAGFSPEWAALAITVPITEEDGTPEGPVTPATTVHAPEEPDTAAVRVSTPEEPASPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPPPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPASPAAAVPTPEEPASPAAAVPTPEEPAFPAPAVPTPEESASAAVAVPTPEESASPAAAVPTPAESASFAAVVATLEEPTSPAASVPTPAAMVATLEEFTSPAASVPTSEEPASLAAAVSNPEEPTSPAAAVPTLEEPTSSAAAVLTPEELSSPAASVPTPEEPASPAAAVSNLEEPASPAAAVPTPEVAAIPAASVPTPEVPAIPAAAVPPMEEVSPIGVPFLGVSAHTDSVPISEEGTPVLEEASSTGMWIKEDLDSLVFGIKEVTSTVLHGKVPLAATAGLNSDEMFQKEQVDPLQMKLQQVNGLGQGLIQSAGKDCDVQGLEHDMEEINARWNTLNKKVAQRIAQLQEALLHCGKFQDALEPLLSWLADTEELIANQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAELADREKITGQLESLESRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIQQQIIRHKALEEDIENHATDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQA
Protein: Phosphoenolpyruvate carboxylase kinase 1 (AtPPCK1) (EC 2.7.11.1) (Q9SPK4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-independent kinase involved in light-dependent phosphoenolpyruvate carboxylase phosphorylation.
Interaction partners:
- Tonoplast dicarboxylate transporter
- Phosphoenolpyruvate carboxylase 1
- Phosphoenolpyruvate carboxylase 3
- Pyruvate, phosphate dikinase 1, chloroplastic
- Phosphoenolpyruvate carboxylase 2
- Pyruvate, phosphate dikinase regulatory protein 1, chloroplastic
- Aluminum-activated malate transporter 6
Sequence:
MTCSQTLGNNNTNKYQICEEIGRGRFGTVSRVYAPATGDFFACKTIDKASLSDDLDRACLDNEPKLMALLSYHPNIVQIHDLIDTDSTLSIFMELVHPSVSIYDRLVSSGTFFEPQTASFAKQILQALSHCHRYGVVHRDIKPENILVDLRNDTVKICDFGSGIWLGEGETTEGVVGTPYYVAPEVLMGYSYGEKVDLWSAGVVLYTMLAGTPPFYGETAEEIFEAVLRGNLRFPTKIFRGVSSMAKDFLRKLICKDASRRFSAEQALRHPWIQRAGETEERFI
Protein: Enoyl-CoA hydratase/isomerase family protein (O86369)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTHAIRPVDFDNLKTMTYEVTGRIARITFNRPEKGNAIIADTPLELSALVERADLDPGVHVILVSGRGEGFCAGFDLSAYAEGSSSTGGGGAYQGTVLDGKTQAVNHLPNQPWDPMIDYQMMSRFVRGFASLMHADKPTVVKIHGYCVAGGTDIALHADQVIAAADAKIGYPPTRVWGVPAAGLWAHRLGDQRAKRLLFTGDCITGAQAAEWGLAVEAPEPADLDERTERLVARIAALPVNQLIMVKLALNSALLQQGVATSRMVSTVFDGAARHTPEGHAFVADAVEHGFRDAVRRRDEPFGDYGRQASRV
Protein: Hydroxymethylglutaryl-CoA synthase (HMG-CoA synthase) (EC 2.3.3.10) (3-hydroxy-3-methylglutaryl coenzyme A synthase) (A0A1D8PTW6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG13 condenses acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase HMG1 finally reduces HMG-CoA to produce mevalonate (Probable).
Interaction partners:
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
- Acetyl-CoA acetyltransferase
- Squalene epoxidase ERG1
- acetyl-CoA C-acyltransferase
- Pot1-2p
- acetyl-CoA C-acyltransferase
- Lanosterol 14-alpha demethylase
- Isopentenyl-diphosphate delta-isomerase
- Squalene synthase ERG9
- Delta
Sequence:
MVMTNSPQNIGIKGIEVYIPGQAVNQSDLEKFDGIPQGKYTIGLGQTNMAFVNDREDIYSISLTVLSRLIKNYSIDTNKIGRLEVGTETLLDKSKSVKSVLMQLFPGNNDIEGIDTVNACYGGTSSVINAINWIESSSWDGRDAIVVAGDIAIYDKGAARPTGGVGAIALLIGPDAPIVFDSIRGSFMEHAYDFYKPDFTSEYPVVDGHFSLSCYVKAVDNCYKNYSKKITGDANKTVGVYDHFDFSAFHVPTCKLVTKSYARLLYNDYVSNPSKFADLIDETTRKHIDGLTYDESLTDKILEKTFVGLAKDETKKRVQPALQVPTNTGNMYTASAWVSLASLLYYVGSDNLKNKRISIFSYGSGLASTLLSVTVKGDVSAITKVLDFDYKLGDGRKIQSPEDYLAAIELREKAHLQKSFKPQGSTDNLSQGTYYLTEIDDKFRRAYAIKE
Protein: holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) (F9X6V3)
Organism: Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch fungus) (Septoria tritici)
Interaction partners:
- Dephospho-CoA kinase
- [acyl-carrier-protein] S-malonyltransferase
- Acyl carrier protein
- 3-oxoacyl-[acyl-carrier-protein] synthase
Sequence:
MAQQLQSLSDSLPSVSTLVNGITNAFHNATSLVSGAPHAGEITCWLIDTRKLWPGTKIWDAPGAAEAMGLISVAEQNAISTKMFIQDARMSLASALIKRLYISRTLDIPWKDVILARKGDAQHGKPCAVDVAGKPIEGIDFNVSHQAGLVTLIGWNGKLRHSYSSEGIIEGSVNTPAAEDFDTNVMVGTDIVCVHERNDDRTIEEEGLESWVDTFDFVFSDEERWSMKFDVDYVTLADGKILSKEELGRHDRCVQRNRNLAVTTKEGEAITLNSNRIIEAKLRRFYTYFCYKEAYIKLAGEALLAPWLKELEFFNVRSPKPADPPQKDGSSQWGEEVNDVEVHLSSEEVSDVRMNITAFDENHMVSTAIQGKIKGIKVPPFSSIDLQKDILDYAYQHLKIAPTTHT
Protein: Ovoinhibitor (OI) (OvoI) (Serine protease inhibitor Kazal-type 5) (allergen Gal d OIH) (P10184)
Organism: Gallus gallus (Chicken)
Function: Serine protease inhibitor involved in antimicrobial egg defense preventing contamination of table eggs (non-fertilized eggs) and protecting the chick embryo (fertilized eggs) (Probable). Inhibits trypsin, chymotrypsin, elastase, subtilisin and a proteinase of fungus Aspergillus oryzae. Inhibits calcium-activated potassium channels KCNMA1 (bovine) and slo (Drosophila). Has antibacterial activity against B.thuringiensis LMSA 3.06.004, but not against S.aureus CIP 103 811, P.aeruginosa PAO1, B.cereus ATCC6464 or B.subtilis ATCC 6633.
Subcellular location: Secreted {ECO:0000269|PubMed:22010862}.
Interaction partners:
- Ovotransferrin
- Ovotransferrin
- Ovotransferrin
- chymotrypsin
- Ovostatin
- Uncharacterized protein.
- Gallinacin-9
- Ovalbumin
- Gallinacin-10
- Cystatin
Sequence:
MTDWVLHHKVGPLDMTTRYIFPLLPLPFLPHSESKRAVCAPRCSAMRTARQFVQVALALCCFADIAFGIEVNCSLYASGIGKDGTSWVACPRNLKPVCGTDGSTYSNECGICLYNREHGANVEKEYDGECRPKHVTIDCSPYLQVVRDGNTMVACPRILKPVCGSDSFTYDNECGICAYNAEHHTNISKLHDGECKLEIGSVDCSKYPSTVSKDGRTLVACPRILSPVCGTDGFTYDNECGICAHNAEQRTHVSKKHDGKCRQEIPEIDCDQYPTRKTTGGKLLVRCPRILLPVCGTDGFTYDNECGICAHNAQHGTEVKKSHDGRCKERSTPLDCTQYLSNTQNGEAITACPFILQEVCGTDGVTYSNDCSLCAHNIELGTSVAKKHDGRCREEVPELDCSKYKTSTLKDGRQVVACTMIYDPVCATNGVTYASECTLCAHNLEQRTNLGKRKNGRCEEDITKEHCREFQKVSPICTMEYVPHCGSDGVTYSNRCFFCNAYVQSNRTLNLVSMAAC