wanglab/gogpt-training-data huggingface dataset:
Protein: Probable alkaline/neutral invertase A, chloroplastic (A/N-INVA) (EC 3.2.1.26) (Q84JL5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chloroplastic invertase that cleaves sucrose into glucose and fructose and may participate in the carbon flux between the cytosol and plastids in leaves.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- At5g49410
Sequence:
MNAITFLGNSTMIPSQCILRAFTRISPSKYIRDTSFRSYPSRFSSCINQYRNADSDRIIRPTNAVPFCTDRQSSVTAQVVSEARSHSASTTCANDTTLDQIYTKNGLNVKPLVVERLKRDEKDEEAVNEDEEGVKRDGFEGVKCNDVEEEAWRLLRDSIVTYCDSPVGTVAAKDPTDTTPSNYDQVFIRDFVPSALAFLLKGESEIVRNFLLHTLQLQSWEKTVDCYSPGQGLMPASFKVRTLPLEEDKFEEVLDPDFGEAAIGRVAPVDSGLWWIILLRAYGKITGDYSLQERIDVQTGIKMIANLCLADGFDMFPTLLVTDGSCMIDRRMGIHGHPLEIQALFYSALRSSREMITVNDSSKNIIKTISNRLSALSFHIRENYWVDKNKINEIYRYKTEEYSMDATNKFNIYPEQVSPWLMDWVPESPDSGFLIGNLQPAHMDFRFFTLGNLWSIISSLGTPKQNQAILNLVEEKWDDLVGHMPLKICYPALESSEWHIITGSDPKNTPWSYHNGGSWPTLLWQFTLACIKMGRPELAEKAVTLAEKRLQADRWPEYYDTRDGKFIGKQSRLYQTWTIAGFLTSKQLLQNPEIASSLFWEEDLELLESCVCVLTKSGRKKCSRAAAKSQILI
Protein: Desmocollin 2-like protein (F1QSQ0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. Involved in the formation and structural organization of desmosome cell-cell junctions during embryonic development. Required for embryogenesis, specifically for progression of epiboly and normal convergence-extension movements during gastrulation. Required for the development of desmosomal-rich midlines in the heart. Plays an important role in ventricular contraction and resulting heart stroke volume.
Subcellular location: Cell junction, desmosome {ECO:0000250|UniProtKB:Q02487}. Cell membrane {ECO:0000250|UniProtKB:Q02487}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Plakophilin-2
- Junction plakoglobin a.
- Wu:fi04e12.
- Desmoglein-2.1-like isoform X1
- Plakophilin 1b
- Desmoplakin a.
Sequence:
MRTPPRPEGLYPSPTVRYTQFMVETGHIQLLQITYPHTHSRFRMYERAHFAACLLALVLFQRAESCDPRPVLVQVPNTVPAGYFITQVTLNGCTAIPVSFTSSDPDFTVNTDGSIVTLRSLVISTKRFSVLVQDNSGLDWRVEIILSCKNEDSQKSGSVAQKRAKRRWRPLPFSVVENASPPFPKDVEMIASDSSVNYTVHYVISGQGVTEEPIGLFQLDQKTGMVRVTGPVDREKNPEFNFIARAFDQNNREVDQFLPITVMVEDVNDNAPEFTGNRFFTVEERCRAGTRVGQVNATDRDQPKTPHSLIKYILLNATDMFSIDQSTGIITAKSNTLDREAQDKVFVGVEIRDMGGAPNGLFNRGTAVISLTDVNDNPPTFKEKLYKGTIKENLANVLVTRIPVEDKDLVNTPNWKAVYEVTKGNENGNFRMETDPKTNEGLLYVVKGLDFEKTPVMNLEVTARNEAPLVGTDAKWQSVPLQLNVEDVDEGPEFNPNIMYLKVKENLPNGTVIGTYKALDPETKNSNGIKYYKLTDPGNWITVVESTGELKVANTIDRESSLVHNDTYNITIKAVDESKKTGNGVVILQIEDVNDNIPVIQRPDLNMCNRGDAVSSVLVEAVDQDKPPYSTPFIFELGAEQEGKWKLKDITDSSVVLQQVEPMPNGMYTVPITVKDLQGTGKEQIVNVRVCSCQREDSGVGICGARSASVSLGNYGILALVLSGLLLLLLCLFLIFFCTTKRDKLQITDDTGTGGILLKSNTEAPGEEVKDGTLLLIPTADVVDGSFQSAVTESKNVNTAPGRYGQQFFQSGGVYNTTTQEFGTDQYYTSGRYDNKIYGNGTLQKFSNTGTLDTWRTNGCYLDRKLAYFGEQEDGRYADDLLKNYGNEGVGSSAGSVGCCSILGEQESMEFLNTLGPKFRPLADICYTTNKTGK
Protein: Mycofactocin maturase MftC ([Mycofactocin precursor peptide]-pyrrolidinone derivative synthase) (EC 4.1.99.26) ([Mycofactocin precursor peptide]-tyrosine decarboxylase) (EC 1.3.98.7) (P9WJ79)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Radical S-adenosylmethionine (SAM) enzyme responsible for the first step of the biosynthesis of the enzyme cofactor mycofactocin (MFT). Catalyzes two reactions at the C-terminus of the mycofactocin precursor (the MftA peptide). The first one is the oxidative decarboxylation of the C-terminal L-tyrosine of MftA, forming an unsaturated tyramine moiety. The second reaction is the cross-linking of the tyramine with the penultimate L-valine residue, forming a five-membered lactam ring. Its activity requires the presence of the MftB chaperone.
Interaction partners:
- Peptide chaperone MftB
- Pre-mycofactocin synthase
- Mycofactocin precursor peptide peptidase
- Pre-mycofactocin glycosyltransferase
- Putative mycofactocin biosynthesis transcriptional regulator MftR
- Mycofactocin precursor peptide
- Uncharacterized oxidoreductase Rv2750
- Alcohol dehydrogenase B
- Uncharacterized NAD-dependent oxidoreductase Rv0687
- Probable dehydrogenase
Sequence:
MTSPVPRLIEQFERGLDAPICLTWELTYACNLACVHCLSSSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYATAHHVGVKFSTNGVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAGVKISVVITRRNVAQLDEFATLASRYGATLRITRLRPSGRGTDVWADLHPTADQQVQLYDWLVSKGERVLTGDSFFHLAPLGQSGALAGLNMCGAGRVVCLIDPVGDVYACPFAIHDHFLAGNVLSDGGFQNVWKNSSLFRELREPQSAGACGSCGHYDSCRGGCMAAKFFTGLPLDGPDPECVQGHSEPALARERHLPRPRADHSRGRRVSKPVPLTLSMRPPKRPCNESPV
Protein: Bridge-like lipid transfer protein family member 1 C-terminal domain-containing protein (Q8T620)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNVCVVSEGTFEVCSRTTAAKKGENAKWLLNVKWQMEGVDIHLDVNIGKQLSSLGHTLTMLTGFEEDETQMESPDSDEGDQSCRDTFVRRRGDFDNLPAFVFDPTIDSKKRSFMMEKEMAEQLKIINDLRTLGASHNTVAHEERRLQELQAICYKYFRRDMIQKWKRPSLRRSLKTYGRSHSYIGSGSSVSGVGVPQTLDNVSYTGRRLDTIASNDEISSLQSTPASCHSRSASLKHTTGGGVIGGGVNALGRVTFTEAMRQTSLPNADTDTETADNELDWRGDITPSEIDVDGTSVEMRRKHGHGQKQPEPNIDFELDIKVLVNSGKCVLHTKDTGEERGYAGGSGAATSGVPASSVKSHKREKSIGNDWGSPTPSRRQRDKSKLRYNANALLADLTIFHIPGLDVKLHYQSKTLAEQLTGDQLPTGRRMGSKRATLCAWMTLQSIPEETIISPHILEFLEQTLEPIPARQSSSVPPTPSHNTGVNLDILPANYVTYASFPVDVIVYFHMQPSTFRFSCLPVSRVECMLQLPSLDIVFSSKRSSEEENSAQPGGHTQPDQQLPTGGLSVTGCLADFNVFIFHPYGGKKTSKETQFSPLSDSERKDSLSINVEFVKFHITRCRKVYIEPLPSSKRSLDQSRAVIRFSTIVDIGSASFKYDMRRLTEILAFPKAWYRRRIVRRLFLGDLSVQQQQQQQQGNGAETPTGCPPATPTPNEDASRAKDNMRLDFDGQPSQQQQQLGHFGAVRHLKNLGKSSSAESSGTPPSEKNQITAWETLVIFAVNFTKLNVQMNIGNVCGNVVWLTKDFQSDGRLSIGSTGYKNMYAGIYLGGSALDAKGGIVGGSFEVNKINKRFHIKEEAGMEPYHTMGLSFMALELRLDYMGTSVLMTRISSFSAAMKDEWRTASQAAATPAHGKDQPRALIFIHGDLTWDQLQIMISKSTTADLLKMYFKLEEFFTQQFKSSKRVFSNLEPRLQDRTASIKRRQQHKKKPANGELVAPPQIHGMIGENTDARHHRHWQKPLAQAVGLVVPSLVTRLPRHGNVLGGTVELRGQNISLACFHGINFKSKSWALFSLRSPSINFATEARQSEDEVLVTQTLTSSLGQTTEVQQQQNHSMAIVSRITRNIIFPPQFKTLNEWFHYAFANSEIDGKLIRNNVETRLIDPPFSSHPQLWIDSPCWNASGRSHPIL
Protein: Dynein light chain roadblock (Q9SWQ6)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR009998}.
Interaction partners:
- Dynein light chain
- Uncharacterized protein
- Dynein light chain
- Uncharacterized protein
- Dynein light chain
- Mr19,000 outer arm dynein light chain
- Inner arm dynein light chain
- Dynein light chain 9
- Dynein light chain Tctex1
- Dynein light chain roadblock
Sequence:
MVDIAAVDETFKRLQSHKGVLGIIVINAEGIAIRTTFDNDLTVQYAALVSHFTVKARSAVRKLDGDNDLKFLRIRSKKHEIMIAPEFERSHEYYLVVVQDPSREA
Protein: Leukocyte immunoglobulin-like receptor subfamily B member 5 (CD85 antigen-like family member C) (Leukocyte immunoglobulin-like receptor 8) (LIR-8) (CD antigen CD85c) (O75023)
Organism: Homo sapiens (Human)
Function: May act as receptor for class I MHC antigens.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 6
- Tyrosine-protein kinase SYK
- CMRF35-like molecule 6
Sequence:
MTLTLSVLICLGLSVGPRTCVQAGTLPKPTLWAEPASVIARGKPVTLWCQGPLETEEYRLDKEGLPWARKRQNPLEPGAKAKFHIPSTVYDSAGRYRCYYETPAGWSEPSDPLELVATGFYAEPTLLALPSPVVASGGNVTLQCDTLDGLLTFVLVEEEQKLPRTLYSQKLPKGPSQALFPVGPVTPSCRWRFRCYYYYRKNPQVWSNPSDLLEILVPGVSRKPSLLIPQGSVVARGGSLTLQCRSDVGYDIFVLYKEGEHDLVQGSGQQPQAGLSQANFTLGPVSRSHGGQYRCYGAHNLSPRWSAPSDPLDILIAGLIPDIPALSVQPGPKVASGENVTLLCQSWHQIDTFFLTKEGAAHPPLCLKSKYQSYRHQAEFSMSPVTSAQGGTYRCYSAIRSYPYLLSSPSYPQELVVSGPSGDPSLSPTGSTPTPGPEDQPLTPTGLDPQSGLGRHLGVVTGVSVAFVLLLFLLLFLLLRHRHQSKHRTSAHFYRPAGAAGPEPKDQGLQKRASPVADIQEEILNAAVKDTQPKDGVEMDAPAAASEAPQDVTYAQLHSLTLRREATEPPPSQEREPPAEPSIYAPLAIH
Protein: Ras-related protein Rab-32A (Q54QR3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSNNPADDEGYNEYLYKILVVGDIGTGKTSIIKRFVHNIFSMHYKSTIGVDFALKVINWDPKTEVRLQLWDIAGQERFGSMTRVYYKEAVGAMITFDVTRMSTFEAVAKWKADIDSKVTYGADEKPIPVVLLANKCDLGKDAFIKTANDMDKYCKDNGFIGWFETSAKENMNIEKAARFLVDHILKNDVRRNQPIEGTIQPGDLNKQPQPTSTGPSCCK
Protein: Cathelicidin antimicrobial peptide (Cathelin-like protein) (CLP) [Cleaved into: Cathelin-related antimicrobial peptide (Cramp)] (P51437)
Organism: Mus musculus (Mouse)
Function: Antimicrobial protein that is an integral component of the innate immune system (By similarity). Binds to bacterial lipopolysaccharides (LPS) (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P54229}. Vesicle {ECO:0000250|UniProtKB:P54229}. Note=Stored as pro-peptide in granules and phagolysosomes of neutrophils. {ECO:0000250|UniProtKB:P54229}.
Interaction partners:
- Neutrophilic granule protein
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- Transcription factor Jun
- Cathepsin G
- Myeloblastin
- Myeloperoxidase
- Lactotransferrin
- Protein S100-A9
- H2-O alpha
Sequence:
MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPSYRDAVLRAVDDFNQQSLDTNLYRLLDLDPEPQGDEDPDTPKSVRFRVKETVCGKAERQLPEQCAFKEQGVVKQCMGAVTLNPAADSFDISCNEPGAQPFRFKKISRLAGLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE
Protein: Rho GTPase-activating protein 40 (Rho-type GTPase-activating protein 40) (Q5TG30)
Organism: Homo sapiens (Human)
Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
Interaction partners:
Sequence:
MAEPALLPAAQMERLAPGPLASPCPRIPRARIARRCAQRWADLGCSSGPSSGRMDQLPQKNLLRLHPAGSAGCSTGVESSSMDGFWMEVEQIQQRDELREEDSGGNEGQLPEEGEAESQWLQDTGLSGLLGGLGLDGDHQELLSTLTQTQVAAVCRRLDIYARSVRRQHKTPVRDVRDVFGVFNSGKMSSENGDSGMKGAQLSSGASKFPPAAEPGGLQEQAGREEAFNMDSAYSEQAAVLLQRSRPSRGGTSAWGKCSLPKFTVPKGRLGVTRIGDLSLQDMRKVPSLALIELTALCDILGLDLKRSKAGKWKAAETRLFGVPLDSLLEADHKVLPSTQVPLVLQALLSCLEKRGLDMEGILRVPGSQARVKGLEQKLERDFYAGLFSWDEVHHNDASDLLKRFIRKLPTPLLTAEYLPAFAVVPNIPNLKQRLQVLHLLILILPEPNRNALKALLEFLRKVVAREQHNKMTLRNVSTVMAPNLFLHQGRPPKLPKGKEKQLAEGAAEVVQIMVHYQDLLWTVASFLVAQVRKLNDSSSRRPQLCDAGLKTWLRRMHADRDKAGDGLEATPKVAKIQVVWPIKDPLKVPLTPSTKVAHVLRQFTEHLSPGSKGQEDSEDMDSLLLHHRSMESANILLYEVGGNINEHRLDPDAYLLDLYRANPHGEWVLKQNPT
Protein: Neuropeptide CCHamide-1 (Q4V4I9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ligand for the CCHamide-1 receptor CCHa1-R.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Neuropeptide CCHamide-1 receptor
- Allatostatin C, isoform A
- Neuropeptide CCHamide-2
- Neuropeptide F
- Short neuropeptide F
Sequence:
MWYSKCSWTLVVLVALFALVTGSCLEYGHSCWGAHGKRSGGKAVIDAKQHPLPNSYGLDSVVEQLYNNNNNNQNNQDDDNNDDDSNRNTNANSANNIPLAAPAIISRRESEDRRIGGLKWAQLMRQHRYQLRQLQDQQQQGRGRGGQGQYDAAAESWRKLQQALQAQIDADNENYSGYELTK
Protein: Toll-interacting protein (Q9QZ06)
Organism: Mus musculus (Mouse)
Function: Component of the signaling pathway of IL-1 and Toll-like receptors (By similarity). Inhibits cell activation by microbial products (By similarity). Recruits IRAK1 to the IL-1 receptor complex (By similarity). Inhibits IRAK1 phosphorylation and kinase activity. Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates (By similarity). The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates (By similarity). In a complex with TOM1, recruits ubiquitin-conjugated proteins onto early endosomes (By similarity). Binds to phosphatidylinositol 3-phosphate (PtdIns(3)P) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H0E2}. Endosome {ECO:0000250|UniProtKB:Q9H0E2}. Early endosome {ECO:0000250|UniProtKB:Q9H0E2}. Note=Localized to endo/exosomal vesicles. {ECO:0000250|UniProtKB:Q9H0E2}.
Interaction partners:
- Interleukin-1 receptor-associated kinase 1
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 2
- Target of Myb1 membrane trafficking protein
- Interleukin-1 receptor-associated kinase 4
- Toll-like receptor 4
- TNF receptor-associated factor 6
- Toll/interleukin-1 receptor domain-containing adapter protein
- Interleukin-1 receptor type 1
- Interleukin-1 receptor accessory protein
Sequence:
MATTVSTQRGPVYIGELPQDFLRITPTQQQQQIQLDAQAAQQLQYGGTVGTVGRLSITVVQAKLAKNYGMTRMDPYCRLRLGYAVYETPTAHNGAKNPRWNKVIQCTVPPGVDSFYLEIFDERAFSMDDRIAWTHITIPESLKQGQVEDEWYSLSGRQGDDKEGMINLVMSYTSLPAAMMMPPQPVVLMPTVYQQGVGYVPIAGMPAVCSPGMVPMAMPPPAVAPQPRCNEEDLKAIQDMFPNMDREVIRSVLEAQRGNKDAAINSLLQMGEES
Protein: Geranylfarnesyl diphosphate synthase (GFPS) (EC 2.5.1.81) (Farnesylgeranyl diphosphate synthase) (FGPP synthase) (Q8PYS1)
Organism: Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Function: Involved in biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis. Catalyzes the condensation of isopentenyl pyrophosphate with the allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFPP). It prefers geranylgeranyl diphosphate (GGPP) and farnesyl diphosphate (FPP) as allylic substrate.
Interaction partners:
Sequence:
MPVKVHGVILMNIEEWEEYRYVEAGIKESITLIEDPGLKKMVEHVCHSGGKRIRPIILLLVSEICSGSYSRSLNAALAVEMMHSASLIHDDLLDQGLVRRNLPSAPEKFGPSGALLCGDYLIAKSIAFISPYGEKVIQDFGKAGMDMAEGEVLDLKLEDESFGENDYFKCIYKKTASLFAISASIGAYTGGAEEELAERFSHFGNALGTAYQIVDDILEFLEVVEGKESKFTSETLPHIYMKSTSKEEALKKSIDCVKLHVAAAKETLETFRECPARDKLFQITDYITVDMLENL
Protein: Pectate lyase A (EC 4.2.2.2) (Q5AVN4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pectinesterase A
- Probable endopolygalacturonase D
Sequence:
MQNLKFLIAAVSCLGPALAAPTPTSNFINSNFNKRASVEDSAFGYASLNGGTTGGAGGTTTTVSSYAEFTAAVQGDDPKIVIVSGPIEETAEQVDVGSNTSILGADSSAVLTGFGLRLKEVENVIIRNLGIAKVLADNGDAIGAEYSNNIWIDHVDVSSDRDHDKDYYDGLLDFKRGSDYITVSNSFIHDHWKASLVGHSNSNEDEDSGKLHVTYANNYWYNLNSRAPSIRFGTGHIYNNYYETVSDGINTRIGAQVLVEGNVFVDSKKALYSTDEGYAVERNNDFGDAKNEALEGTLTSVEYEYDLLDTSEVKSAVVGTAGQTLTF
Protein: Sperm acrosome-associated protein 7 (Q9D2S4)
Organism: Mus musculus (Mouse)
Function: Involved in fertilization. Seems not to play a direct role in sperm-egg binding or gamete fusion.
Subcellular location: Secreted {ECO:0000269|PubMed:22495889}. Cytoplasmic vesicle, secretory vesicle, acrosome lumen {ECO:0000269|PubMed:22495889, ECO:0000269|PubMed:24307706}. Note=Localized in perinuclear pro-acrosomal granules in round spermatides (PubMed:24307706). Localized between the inner and outer acrosomal membranes (matrix or lumen) in spermatozoa (PubMed:24307706). Secreted during acrosome exocytosis (PubMed:24307706). {ECO:0000269|PubMed:24307706}.
Interaction partners:
Sequence:
MAANRGSRTFLSVFLLCCWQGAELQPIKTTSGPITEGSLNSTTENIPEALDEILAQEILEPKTSAVSETSPRPRSSILTTVQTKEINAGIDENYQEEAFENYHEVLENIEHLPTKEESGKNDRSTVANLHDHSSQTKHEPPSSPEGKGSSNDDVYGKLSVLDKILENIGQSEGSLELTESIF
Protein: Cell number regulator 2 (ZmCNR02) (B6TYV8)
Organism: Zea mays (Maize)
Function: May act as a negative regulator of cell number.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 4
- BHLH transcription factor
- Transcription factor bHLH51
- BHLH transcription factor
- DNA binding protein
- BHLH transcription factor
Sequence:
MYPKAADEGAQPLATGIPFSGGGGYYQAGGAMAAAFAVQAQAPVAAWSTGLCNCFDDCHNCCVTCVCPCITFGQTAEIIDRGSTSCGTSGALYALVMLLTGCQCVYSCFYRAKMRAQYGLQVSPCSDCCVHCCCQCCALCQEYRELKKRGFDMSIGWHANMERQGRAAAAVPPHMHPGMTR
Protein: Protein delta homolog 2 (DLK-2) (Endothelial cell-specific protein S-1) (Epidermal growth factor-like protein 9) (EGF-like protein 9) (Q8K1E3)
Organism: Mus musculus (Mouse)
Function: Regulates adipogenesis.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPSGCRCLNLVCLLCILGATSQPARADDCSSHCDLAHGCCAPDGSCRCDPGWEGLHCERCVRMPGCQHGTCHQPWQCICHSGWAGKFCDKDEHICTSQSPCQNGGQCVYDGGGEYHCVCLPGFHGRGCERKAGPCEQAGFPCRNGGQCQDNQGFALNFTCRCLAGFMGAHCEVNVDDCLMRPCANGATCIDGINRFSCLCPEGFAGRFCTINLDDCASRPCQRGARCRDRVHDFDCLCPSGYGGKTCELVLPAPEPASVGTPQMPTSAVVVPATGPAPHSAGAGLLRISVKEVVRRQESGLGESSLVALVVFGSLTAALVLATVLLTLRAWRRGICPTGPCCYPAPHYAPARQDQECQVSMLPAGFPLSPDLPPEPGKTTAL
Protein: Uncharacterized protein (Q583W8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRCVRAATTPPAAPWRAGSSFIPIWRFSAFYSSSKFIGRRSSGSKKLGAFPRMPHAVKKSSTDVPRAAESPVDTTAVQTSVIEEDKEEEQPHMCNNKRTKSKRSSQPCTEAKQCSNSREGKQAVAVTGTKSCNPSEGSTAQCLPCVTDDKNTQKKEREGENVCLVDRAVVLKLFVVSDALAFMFATSPKDQRCVNWHLKKVDQSVIMQPPTQAPRSQHKGQEGITDNDSNSKDKKDARRESRSRRREQRNAVTREYNIALRVLSEESADNVHYIHVREMERLVPPADVLPRNAMSTVLASKKGNENSKRRQSSEKRNSKVQKGRGTSPAEPSAAALEALGRVMALRQWQTAALRKAQESQRLHALPPACHAITHVYMNDPSLPDTTVVQGCNIKKSVTDILDLMKQSTVSGNLLGFVNLHKGRKSSSSGNKGTTPSATLSMPFELKPLLSVVASCIPRSDAALGVRFDEDGFLRSVLQRHSRKSGSNEPTTAVAQVVSEEERQTATDRELSARRVPPVPRYTTRVVLLIDYDSSESWDLHSDGVSSETKAKSAKGDSGEEVVNRRRRRKEPHIYCLIADGGEV
Protein: ADP-ribosyltransferase binding component (CdtB) (Protective antigen) (A8DS70)
Organism: Clostridioides difficile (Peptoclostridium difficile)
Interaction partners:
Sequence:
MKIQMRNKKVLSFLTLTAIVSQALVYPVYAQTSTSNHSNKKKEIVNEDILPNNGLMGYYFTDEHFKDLKLMAPIKDGNLKFEEKKVDKLLDKDKSDVKSIRWTGRIIPSKDGEYTLSTDRDDVLMQVNTESTISNTLKVNMKKGKEYKVRIELQDKNLGSIDNLSSPNLYWELDGMKKIIPEENLFLRDYSNIEKDDPFIPNNNFFDPKLMSDWEDEDLDTDNDNIPDSYERNGYTIKDLIAVKWEDSFAEQGYKKYVSNYLESNTAGDPYTDYEKASGSFDKAIKTEARDPLVAAYPIVGVGMEKLIISTNEHASTDQGKTVSRATTNSKTESNTAGVSVNVGYQNGFTANVTTNYSHTTDNSTAVQDSNGESWNTGLSINKGESAYINANVRYYNTGTAPMYKVTPTTNLVLDGDTLSTIKAQENQIGNNLSPGDTYPKKGLSPLALNTMDQFSSRLIPINYDQLKKLDAGKQIKLETTQVSGNFGTKNSSGQIVTEGNSWSDYISQIDSISASIILDTENESYERRVTAKNLQDPEDKTPELTIGEAIEKAFGATKKDGLLYFNDIPIDESCVELIFDDNTANKIKDSLKTLSDKKIYNVKLERGMNILIKTPTYFTNFDDYNNYPSTWSNVNTTNQDGLQGSANKLNGETKIKIPMSELKPYKRYVFSGYSKDPLTSNSIIVKIKAKEEKTDYLVPEQGYTKFSYEFETTEKDSSNIEITLIGSGTTYLDNLSITELNSTPEILDEPEVKIPTDQEIMDAHKIYFADLNFNPSTGNTYINGMYFAPTQTNKEALDYIQKYRVEATLQYSGFKDIGTKDKEMRNYLGDPNQPKTNYVNLRSYFTGGENIMTYKKLRIYAITPDDRELLVLSVD
Protein: Protein archease (O59205)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently.
Interaction partners:
- tRNA-splicing ligase RtcB
- 312aa long hypothetical nucleolar protein
- RNA 3'-terminal phosphate cyclase
Sequence:
MKKWEHYEHTADIGIRGYGDSLEEAFEAVAIALFDVMVNVNKVEKKEVREIEVEAEDLEALLYSFLEELLVIHDIEGLVFRDFEVKIERVNGKYRLRAKAYGEKLDLKKHEPKEEVKAITYHDMKIERLPNGKWMAQLVPDI
Protein: Homoserine kinase (HK) (HSK) (EC 2.7.1.39) (P00547)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. Is also able to phosphorylate the hydroxy group on gamma-carbon of L-homoserine analogs when the functional group at the alpha-position is a carboxyl, an ester, or even a hydroxymethyl group. Neither L-threonine nor L-serine are substrates of the enzyme.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Threonine synthase
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- Lysine-sensitive aspartokinase 3
- Aspartate-semialdehyde dehydrogenase
- Branched-chain-amino-acid aminotransferase
- Methionine synthase
- Cystathionine gamma-synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Ketol-acid reductoisomerase
Sequence:
MVKVYAPASSANMSVGFDVLGAAVTPVDGALLGDVVTVEAAETFSLNNLGRFADKLPSEPRENIVYQCWERFCQELGKQIPVAMTLEKNMPIGSGLGSSACSVVAALMAMNEHCGKPLNDTRLLALMGELEGRISGSIHYDNVAPCFLGGMQLMIEENDIISQQVPGFDEWLWVLAYPGIKVSTAEARAILPAQYRRQDCIAHGRHLAGFIHACYSRQPELAAKLMKDVIAEPYRERLLPGFRQARQAVAEIGAVASGISGSGPTLFALCDKPETAQRVADWLGKNYLQNQEGFVHICRLDTAGARVLEN
Protein: Serine repeat antigen 1 (EC 3.4.22.-) (O96167)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Uncharacterized protein
- Serine repeat antigen 3
- Cysteine proteinase falcipain 1
Sequence:
MKFFIPYVYIICVIFIINVIRTRGEEDDDNNNISGKSILGTSHNNISNIDLSSIPNLDSNIHASFSSDTKEWSPNNLTSKKKKKKKEIRPKDIMSNSDSSNTSSINKQNNNQIKSVLLKENKGVKITGPCNVNLSIFLVPHIYIDVETKYNNIELKYELDEFSDSIKFKDTTTELRTSDDTLMNTNFNVGVSRDTLDKDRLYNICAENKTFKFVVYIKDNILTLKWKVYETGVTNNKVDIRQYKMKELTRPITTIQIHSVSENKDTHLLESKNYVIKTDIPETCDVMATNCFLSGNINIEKCLECTLLVQNNDTSSECFTYVSNDVRENFNQIKAEAEDDENFRNYHLTDTINNILKRIYKINKNEGKKELITLEELDNFLKESITDYCKILREIDTNGTLVNHELGNNVDVFNNLIRLLKLHKNESISTLHNKLRNSAICMKYPDKWIEKKTGLILPNVVNNNIIYNNKYEKLNEEKKRKIYDNKDDSKISDIINIKKYIFTNNTLKYFNNDKQFCNSSFCNRLKDENNCISKIQIEDQGNCAISWIFASKYYLETLKCMKGYEPHAISALYIANCSKRKHKNRCNVGSNPLEFLQIIEENQFLPMDTNYLYSYTKVGNDCPDEEKNWVNLLKHTRMLNYNNKHRSTLSTKAYRAYESEHFKDKMDTFIKLIKDEIMNNGSVIAYVKAENVLGYELNGKNVQNLCGDKTPDHAVNIVGYGNYINDEDEKKSYWIVRNSWGKYWGDEGYFKVDMYGPSTCEDNFIHTVVVFNINMPKSKKSPVKITFPLYNYYLKYSPDFYHNLYYKNFNSKKSMKLVNASDEHKNIYSQEDKVNHKKGSKILNSEVTTSLLSQEISQRRGEDDDIDTLIGDSPDINEQEKNIKDEFNKSSITHNSVSSSNITKSNKNTNKVKIYHIIKHVKNTKIKIGFVKYDNYNTIGTNHTCSRSYSEDQEKHEGCIKFCELHWNECKDKTSPGYCLTKLKGSNECFFCYV
Protein: Dihydrolipoyl dehydrogenase 1, mitochondrial (AtmLPD1) (mtLPD1) (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase 1) (Glycine cleavage system L protein 1) (Pyruvate dehydrogenase complex E3 subunit 1) (E3-1) (PDC-E3 1) (Q9M5K3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lipoamide dehydrogenase is a component of the glycine decarboxylase (GDC) or glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. LPD1 is probably the protein most often associated with the glycine decarboxylase complex while LPD2 is probably incorporated into alpha-ketoacid dehydrogenase complexes.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537, ECO:0000305|PubMed:25862457}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 5 of pyruvate dehydrogenase complex, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 4 of pyruvate dehydrogenase complex, chloroplastic
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
- Aminomethyltransferase, mitochondrial
Sequence:
MAMASLARRKAYFLTRNLSNSPTDALRFSFSLSRGFASSGSDENDVVIIGGGPGGYVAAIKASQLGLKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHSFANHGIKVSSVEVDLPAMLAQKDNAVKNLTRGIEGLFKKNKVTYVKGYGKFISPNEVSVETIDGGNTIVKGKHIIVATGSDVKSLPGITIDEKKIVSSTGALSLSEVPKKLIVIGAGYIGLEMGSVWGRLGSEVTVVEFAGDIVPSMDGEIRKQFQRSLEKQKMKFMLKTKVVSVDSSSDGVKLTVEPAEGGEQSILEADVVLVSAGRTPFTSGLDLEKIGVETDKAGRILVNDRFLSNVPGVYAIGDVIPGPMLAHKAEEDGVACVEFIAGKHGHVDYDKVPGVVYTHPEVASVGKTEEQLKKEGVSYRVGKFPFMANSRAKAIDNAEGLVKILADKETDKILGVHIMAPNAGELIHEAVLAINYDASSEDIARVCHAHPTMSEALKEAAMATYDKPIHI
Protein: Cell adhesion molecule 2a (Q6PFK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MMVKQHMLFTLYSICGIVLKDILAVSVAATKNKVRGAQGQVPLVQNMTVTEGGTANLTCRVEHNDNTSLQWSNPAQQTLFFGDKKALRDNRIELVRATSQELTISISEVSLSDEGLYTCSLFTMPVKTAKAFLTVLGVPKKPEINGLTKPVLEGDHITLTCVTSGSKPAADVRWFKNEMEVKGAKEVNASGKTFTVKSSLRLHVNRDDDGVAYTCRVDHVALTATHEETTQVLEVHYAPYVEIRQSTNVPQEGQYLKLQCVPKGNPSPDPVLWTKDGGELPDMDRMIVDGRDLTFTSLNKTDNGTYRCGATNHLGTSHAEFKLVIYDPNELKRATDHALIGGIVAVVVFATLCLIIVLGRYLARHKGTYLTNEAKGADDAPDADTAIINADGNHAHAEEKKEYFI