wanglab/gogpt-training-data huggingface dataset:
Protein: Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (Lung surfactant protein D) (P50404)
Organism: Mus musculus (Mouse)
Function: Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
Subcellular location: Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.
Interaction partners:
- Surfactant protein C
- Pulmonary surfactant-associated protein A
- Pulmonary surfactant-associated protein B
- Uteroglobin
- Secretoglobin family 3A member 2
- Advanced glycosylation end product-specific receptor
- C-X-C motif chemokine 15
- Deleted in malignant brain tumors 1 protein
- Sodium-dependent phosphate transport protein 2B
- Claudin-18
Sequence:
MLPFLSMLVLLVQPLGNLGAEMKSLSQRSVPNTCTLVMCSPTENGLPGRDGRDGREGPRGEKGDPGLPGPMGLSGLQGPTGPVGPKGENGSAGEPGPKGERGLSGPPGLPGIPGPAGKEGPSGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSTGAKGSTGPKGERGAPGVQGAPGNAGAAGPAGPAGPQGAPGSRGPPGLKGDRGVPGDRGIKGESGLPDSAALRQQMEALKGKLQRLEVAFSHYQKAALFPDGRSVGDKIFRTADSEKPFEDAQEMCKQAGGQLASPRSATENAAIQQLITAHNKAAFLSMTDVGTEGKFTYPTGEPLVYSNWAPGEPNNNGGAENCVEIFTNGQWNDKACGEQRLVICEF
Protein: Probable T-complex protein 1 subunit beta (TCP-1-beta) (CCT-beta) (Q10147)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta
- Probable T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- Probable T-complex protein 1 subunit theta
- T-complex protein 1 subunit alpha
- Phosducin-like protein C2A9.09
- Elongation factor 1-gamma
- Eukaryotic translation initiation factor 2 subunit alpha
Sequence:
MSLNPHQIFNESGIQERGENARLSSFVGAIAVGDLVKSTLGPKGMDKILQSNSSGDIVVTNDGATILKSIALDNAAAKVLVNISKVQDDEVGDGTTSVCVFAAELLRQAEIMVNAKIHPQVIIDGYRIATKTAIDALRASSIDNSSDPAKFRSDLENIARTTLSSKILSQNKNHFAQLAVDAVLRLKGSTNLDNIQIIKILGGKLDDSFLDEGFILNKTIGVNCPKVMENANILIANTAMDTDKVKVFGARVRVDTTGKLAELERAEREKMKAKVEKIKSHNINCFINRQLIYNWPEQLFADAGIMSIEHADFDGIERLSLVTGGEIASTFDHPELVKLGHCKKIEEIIIGEDKMIKFSGVEAGEACTIVLRGATHQLLDESERAIHDALAVLSQTVAESRVTLGGGCAEMLMAKAVEEAATHEPGKKAVAVSAFAKALSQLPTILADNAGFDSSELVAQLKAAHYDGNDTMGLDMDEGEIADMRAKGILEALKLKQAVVSSGSEGAQLLLRVDTILKAAPRPRERM
Protein: Branched-chain-amino-acid aminotransferase, cytosolic (BCAT(c)) (EC 2.6.1.42) (P54687)
Organism: Homo sapiens (Human)
Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P54690}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Cystathionine gamma-lyase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- L-amino-acid oxidase
- Glutamate--cysteine ligase regulatory subunit
- L-serine dehydratase/L-threonine deaminase
- Glutamate--cysteine ligase catalytic subunit
- Serine dehydratase-like
- Branched-chain-amino-acid aminotransferase, mitochondrial
Sequence:
MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS
Protein: Transcription factor SOX-8 (Q04886)
Organism: Mus musculus (Mouse)
Function: Transcription factor that may play a role in central nervous system, limb and facial development. May be involved in male sex determination. Binds the consensus motif 5'-[AT][AT]CAA[AT]G-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- Oligodendrocyte transcription factor 2
- Oligodendrocyte transcription factor 1
Sequence:
MLDMSEARAQPPCSPSGTASSMSHVEDSDSDAPPSPAGSEGLGRAGGGGRGDTAEAADERFPACIRDAVSQVLKGYDWSLVPMPVRGGGGGTLKAKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLSESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKTGRSDSDSGTELGHHPGGPMYKADAVLGEAHHHSDHHTGQTHGPPTPPTTPKTDLHQASNGSKQELRLEGRRLVDSGRQNIDFSNVDISELSSEVISNMDTFDVHEFDQYLPLNGHSALPTEPSQATASGSYGGASYSHSGATGIGASPVWAHKGAPSASASPTEAGPLRPQIKTEQLSPSHYNDQSHGSPGRADYGSYSAQASVTTAASATAASSFASAQCDYTDLQASNYYSPYPGYPPSLYQYPYFHSSRRPYASPLLNGLSMPPAHSPSSNWDQPVYTTLTRP
Protein: Dally-like, isoform A (LD47466p) (Q9VUG1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}.
Interaction partners:
- Syndecan
- Protein hedgehog
- Tyrosine-protein phosphatase Lar
- Protein wingless
- Frizzled-2
- Protein patched
- Protein dispatched
- Frizzled
- Frizzled-3
- Interference hedgehog
Sequence:
MLHQQQQQQHLHCRRKATATTTARLVIFSSPLLLLLLTTHLPPTLQADNGPAPQVAALAAPNPAGGVAGSSIIDQFSPNCSAVTHIFQARGIDAIEIPQKPSNERVLRYCESPSVGTCCTYNMETRMAMQSRQQLEGHTKDQISRMSGILGSKATKFKDIFTALLKESRTQFNSMFIRTYGVIYERNSYVFSDLFKELETYFANGRVDLLEVMDKFFNTLYQKMFTVLNTQYTFDENYMRCVSEHMKELKPFGDVPDKLSVQIKRSFVATRTYGQALTTASEVAKKVLNVRLNADCTGALTKMQHCGACKGYTEKPCTNYCVNVIKGCLHYQHEFDSEWENFAMAMDKVAERLLGSFNIVMVVEPLNIKISEAIMNFQDSGQDITNRVFQGCGRPKLKKMKRSISPKLQGVQILNARSPVEADTLDIDETLDEAIVLRERRAAEPGSQETSAQQSQEQGVGKSGNGGGGGGGNNRRQQQRRKQQQQRRKQQNNRDDNDDDDNESGGGREPILDRIVRDIRQRVKDYKKFWSNLPHSVCSNEDIASSSDVDGMCWNGHTIDRYMHSITTEHGSNPEFTGNPASTKQTAQMASQLSHLKNAIVHLRNAYNGQDVEWSEQEELPYAGSGAGSGSGSEDDEDDDEGSGLGPFEPSHKPDVERPSVDADNDDDEDAGGRGHMPTHTSRPTSGVDDKNPLIHTTHFDQDHNDLDEDHRQLDEDEDTDAGHDGANDNRSSDAPEKMTLRRALVVYLLPLYMAWFGGVCADLL
Protein: Cobalamin reductase PduS (Propanediol utilization protein PduS) (Q9XDM9)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: A protein that aids in conversion of cob(III)alamin to cob(II)alamin and then to cob(I)alamin in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The latter step requires PduO. No free cob(I)alamin is released, suggesting a complex is formed with PduO that finishes conversion to adenosylcobalamin. PduS and PduO allow regeneration of the adenosylcobalamin cofactor within the BMC. Another study showed reduction of cob(II)alamin to cob(I)alamin in the absence of PduO. Both reactions require NADH. Cyanocobalamin (CN-Cbl) is not a substrate for the first reaction. Cobalamin reduction probably occurs spontaneously in the presence of free reduced flavin nucleotides, this protein may be involved in electron transfer for this reduction (Probable).
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:20656910}.
Interaction partners:
- Bacterial microcompartment shell protein PduT
- Corrinoid adenosyltransferase PduO
- Bacterial microcompartment shell vertex protein PduN
- 1-propanol dehydrogenase PduQ
- Propanal dehydrogenase
- Ion-translocating oxidoreductase complex subunit D
- Ion-translocating oxidoreductase complex subunit B
- Bacterial microcompartment shell protein PduK
- Bacterial microcompartment shell protein PduU
- Ion-translocating oxidoreductase complex subunit G
Sequence:
MSTAINSVEMSLSADEIRERVRAAGVVGAGGAGFPAHVKLQAQVEIFLVNAAECEPMLKVDQQLMWQQAARLVRGVQYAMTATGAREGVIALKEKYRRAIDALTPLLPDGIRLHILPDVYPAGDEVLTIWMATGRRVAPAALPASVGVVVNNVQTVLNIARAVEQRFPVTRRTLTVNGAVARPLTVTVPIGMSLREVLALAGGATVDDPGFINGGPMMGGLITSLDNPVTKTTGGLLVLPKSHPLIQRRMQDERTVLSVARTVCEQCRLCTDLCPRHLIGHELSPHLLVRAVNFHQAATPQLLLSALTCSECNVCESVACPVGISPMRINRMLKRELRAQNQRYEGPLNPADEMAKYRLVPVKRLIAKLGLSPWYQEAPLVEEEPSVEKVTLQLRQHIGASAVANVAVGERVTRGQCVADVPPGALGAPIHASIDGVVSAISEQAITVVRG
Protein: Salivary thrombin inhibitor anophelin (Q9NJS1)
Organism: Anopheles albimanus (New world malaria mosquito)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MANKLVLISLLCVVLVAKITQAAPQYAPGDEPSYDEDTDDSDKLVENDTSITDEDYAAIEASLSETFNTAADPGRRLGEGSKP
Protein: Septin-interacting protein 1 (Septin and tuftelin-interacting protein 1) (STIP-1) (Q9Y103)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- ATP-dependent RNA helicase DHX15 homolog
- Protein crooked neck
- Protein BUD31 homolog
- Pre-mRNA-splicing factor syf1 homolog
- 116 kDa U5 small nuclear ribonucleoprotein component
- DnaJ homolog subfamily C member 5 homolog
- Pre-mRNA-processing-splicing factor 8
- Probable U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor Syf2
- Puff-specific protein Bx42
Sequence:
MSDNDYERFEITDYDLDNEFNINRPRGRQSRHQQIYGIWADDSEEESGGEGGTKRRGRAARKPKDYTMPVNFVAGGIQQAGKKKKKALQADDEKGSQKEGAEADQGEESDDSAASGRPAFGQNDPGSSNSSSEEERPTLSRKQPSTTFQHRSHIASERNVGAWEQHTRGIGAKLLLQMGYEPGKGLGKDLQGISHPVQAHVRKGRGAIGAYGPETAASIGGKTNKSIKVDEDVREAKEFKDQLNKWRKGSAGGAEPMERQGKRYYYKSVEEVIAKGHTSGHLLSEKLSKKLGNVRVIDMTGPEKRVLSGYHALGQAKITPEETLYDTEATEKGSAPACVFAMPELTHNLQLLVSQCEQQIIAIDNQERECSSQQAALESEHRKLEEIVQLERNHIRTLEESLERVERLIDNPDLSLPQAERLFRELLVDYAAEFHEFGLADLAAGVIAPLLKRELVQWQPLENPTEPLPLIKKWRGMLQQGDAAEQQPRNVFDPYSSLIWAGVMPSFRSSAAAWQPKEHPPMASLLDAWAPLLPSWVLDSVLEQLVLPRLVAGVQEWDPLTDTVPIDSWVLPWHAILGSKLEEAVYPQIRSKLGIALRAWSPHDRSARAMLTPWQKAFPEEEMQEFLQRYIVPKLQATLGELIINPMHQDLELWQQVWEWHELIDPMYMAQLLDRHFFPRWMQVLVVWLNQSPDYAEISRWYTGWKSMLSEPLLREPSVKEHLRRALEIMHRASDTLLQPTVTPTPPPPVPPAPVIMMDLIHPPAQLEFKELVSQQCADLGIIFAPLPGRREMGKQIYRVGKLFCYIDRHVCMVSDGSFSNWKPVSLNHLLERSQTGIL
Protein: Spermidine synthase (EC 2.5.1.16) (Q8II73)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Arginase
- S-adenosylmethionine decarboxylase/ornithine decarboxylase
- S-adenosylmethionine synthase
- Eukaryotic translation initiation factor 5A
- Pyrroline-5-carboxylate reductase, putative
Sequence:
MDKLISNNKLKLSVVLLGGLCSLAYYHLKNKFHLSQFCFSKKWFSEFSIMWPGQAFSLKIKKILYETKSKYQNVLVFESTTYGKVLVLDGVIQLTEKDEFAYHEMMTHVPMTVSKEPKNVLVVGGGDGGIIRELCKYKSVENIDICEIDETVIEVSKIYFKNISCGYEDKRVNVFIEDASKFLENVTNTYDVIIVDSSDPIGPAETLFNQNFYEKIYNALKPNGYCVAQCESLWIHVGTIKNMIGYAKKLFKKVEYANISIPTYPCGCIGILCCSKTDTGLTKPNKKLESKEFADLKYYNYENHSAAFKLPAFLLKEIENI
Protein: Protocadherin beta-3 (PCDH-beta-3) (Q9Y5E6)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MEAGGERFLRQRQVLLLFVFLGGSLAGSESRRYSVAEEKEKGFLIANLAKDLGLRVEELAARGAQVVSKGNKQHFQLSHQTGDLLLNEKLDREELCGPTEPCILHFQILLQNPLQFVTNELRIIDVNDHSPVFFENEMHLKILESTLPGTVIPLGNAEDLDVGRNSLQNYTITPNSHFHVLTRSRRDGRKYPELVLDKALDPEEQPELSLTLTALDGGSPPRSGTAQINIQVLDINDNAPEFAQPLYEVAVLENTPVNSVIVTVSASDLDTGSFGTISYAFFHASEEIRKTFQLNPITGDMQLVKYLNFEAINSYEVDIEAKDGGGLSGKSTVIVQVVDVNDNPPELTLSSVNSPIPENSGETVLAVFSVSDLDSGDNGRVMCSIENNLPFFLKPSVENFYTLVSEGALDRETRSEYNITITITDLGTPRLKTKYNITVLVSDVNDNAPAFTQISYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLSSLVSINADNGHLFALRSLDYEALQAFEFRVGATDRGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADLLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCSVPEGPFPGQMVDVSGTGTLSQSYQYEVCLTGGSGTNEFKFLKPIIPNFVAQGAERVSEANPSFRKSFEFS
Protein: Chromosome stability protein 9 (Molecular zipper protein 3) (Q06032)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the synapsis initiation complex (SIC) necessary for the synaptonemal complex assembly. Stabilizes the ZIP2 component to the chromosomes. The SIC complex loads onto chromosomes and nucleates ZIP1 polymerization, a molecular zipper that acts to bring homologous chromosomes in close apposition, which is required for meiotic crossover. May also be involved in double strand break repair.
Subcellular location: Nucleus. Chromosome. Note=Synapsed meiotic chromosomes.
Interaction partners:
- Protein ZIP2
- Synaptonemal complex protein ZIP1
- Sporulation-specific protein 22
- Sporulation-specific protein 16
- E3 SUMO-protein ligase MMS21
- MutS protein homolog 4
- Meiosis-specific protein SPO11
- E3 SUMO-protein ligase SIZ2
- E3 SUMO-protein ligase SIZ1
- MutS protein homolog 5
Sequence:
MGGYLAIVFIPQTNTKSMREKKQKCLKQVRRLSLISPKKYIMPDSIFEQPFVYCGVCHRRTSHGDPLRLTSCAHILCSQHSPLTSKVCPICRSSDISIINLVESKQLPTDIRIFFEPLPPLLESLYNVSQFQLNGLSKQCQYYQNHCLKLREKCARQQQLLYQAKIELDSMAILKKRIQELESVLNHNNVSSMSVGVLPTRNSHQNHYQPPPTVDLTVDDNSLEEFEAKSFIKKLKKNSSLRNSSKNNNGTVTPSTSGRVNKNQPLFMETLNNPNRNSIPPPGMNPNANSNLPNISTIAESTNLNRFSFSPVRVAKGFDGKLPNLDILTNNGSVSSKNISRLSSASLQPSSPLSSSSNRLILPNSNLKELHHSNTPLTSTSTQFPSALEKLKITRKRNNTISGSNRITHNLSSHVRSSGLAFSSSSNSLQQSKLPKSNILKRSNSTQQLTNTHLKSDNHLPPRSSNTVLGSSKKNNKFRRIR
Protein: Regulatory protein SIR3 (Silent information regulator 3) (P06701)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form.
Subcellular location: Nucleus.
Interaction partners:
- NAD-dependent histone deacetylase SIR2
- Regulatory protein SIR4
- Histone H3
- DNA-binding protein RAP1
- Regulatory protein SIR1
- Histone H4
- Cell division control protein 6
- Histone H2B.1
- Cell division cycle protein CDT1
- Histone H2A.2
Sequence:
MAKTLKDLDGWQVIITDDQGRVIDDNNRRRSRKRGGENVFLKRISDGLSFGKGESVIFNDNVTETYSVYLIHEIRLNTLNNVVEIWVFSYLRWFELKPKLYYEQFRPDLIKEDHPLEFYKDKFFNEVNKSELYLTAELSEIWLKDFIAVGQILPESQWNDSSIDKIEDRDFLVRYACEPTAEKFVPIDIFQIIRRVKEMEPKQSDEYLKRVSVPVSGQKTNRQVMHKMGVERSSKRLAKKPSMKKIKIEPSADDDVNNGNIPSQRGTSTTHGSISPQEESVSPNISSASPSALTSPTDSSKILQKRSISKELIVSEEIPINSSEQESDYEPNNETSVLSSKPGSKPEKTSTELVDGRENFVYANNPEVSDDGGLEEETDEVSSESSDEAIIPVNKRRGAHGSELSSKIRKIHIQETQEFSKNYTTETDNEMNGNGKPGIPRGNTKIHSMNENPTPEKGNAKMIDFATLSKLKKKYQIILDRFAPDNQVTDSSQLNKLTDEQSSLDVAGLEDKFRKACSSSGRETILSNFNADINLEESIRESLQKRELLKSQVEDFTRIFLPIYDSLMSSQNKLFYITNADDSTKFQLVNDVMDELITSSARKELPIFDYIHIDALELAGMDALYEKIWFAISKENLCGDISLEALNFYITNVPKAKKRKTLILIQNPENLLSEKILQYFEKWISSKNSKLSIICVGGHNVTIREQINIMPSLKAHFTEIKLNKVDKNELQQMIITRLKSLLKPFHVKVNDKKEMTIYNNIREGQNQKIPDNVIVINHKINNKITQLIAKNVANVSGSTEKAFKICEAAVEISKKDFVRKGGLQKGKLVVSQEMVPRYFSEAINGFKDETISKKIIGMSLLMRTFLYTLAQETEGTNRHTLALETVLIKMVKMLRDNPGYKASKEIKKVICGAWEPAITIEKLKQFSWISVVNDLVGEKLVVVVLEEPSASIMVELKLPLEINYAFSMDEEFKNMDCI
Protein: Receptor activity-modifying protein 1 (Q9JJ74)
Organism: Rattus norvegicus (Rat)
Function: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O60894}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60894}.
Interaction partners:
- Calcitonin receptor
- Calcitonin gene-related peptide type 1 receptor
- Pro-adrenomedullin
- Calcitonin gene-related peptide 2
- Islet amyloid polypeptide
- Receptor activity-modifying protein 2
- Receptor activity-modifying protein 3
- DNA-directed RNA polymerase III subunit RPC9
- Calcitonin
- Neuroendocrine secretory protein 55
Sequence:
MAPGLRGLPRRGLWLLLAHHLFMVTACRDPDYGTLIQELCLSRFKEDMETIGKTLWCDWGKTIGSYGELTHCTKLVANKIGCFWPNPEVDKFFIAVHHRYFSKCPVSGRALRDPPNSILCPFIVLPITVTLLMTALVVWRSKRTEGIV
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (Q8II92)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Thymidylate kinase
- Nucleoside diphosphate kinase
- nucleoside-diphosphate kinase
- Inosine triphosphate pyrophosphatase
- Ribonucleoside-diphosphate reductase
- Calponin homology domain-containing protein, putative
- Proliferating cell nuclear antigen 2
- Proliferating cell nuclear antigen 1
- Replication factor C subunit 5, putative
Sequence:
MHLKIVCLSDEVREMYKNHKTHHEGDSGLDLFIVKDEVLKPKSTTFVKLGIKAIALQYKSNYYYKCEKSENKKKDDDKSNIVNTSFLLFPRSSISKTPLRLANSIGLIDAGYRGEIIAALDNTSDQEYHIKKNDKLVQLVSFTGEPLSFELVEELDETSRGEGGFGSTSNNKY
Protein: Xyloglucan endotransglucosylase/hydrolase (EC 2.4.1.207) (B2KL34)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Secreted, cell wall {ECO:0000256|RuleBase:RU361120}. Secreted, extracellular space, apoplast {ECO:0000256|RuleBase:RU361120}.
Interaction partners:
Sequence:
MGMGLRNGFLLILSCVVTLSLSVLGRPATFLEDFRITWSDSHIRQIDGGRAIQLVLDQNSGCGFASKRQYLFGRVSMKIKLIPGDSAGTVTAFYMNSVTDAVRDELDFEFLGNRTGQPYTVQTNIYAHGKGDREQRVNLWFDPAADFHTYSIMWNHHQIVFYIDEVPIRVYKNNEARNIPYPKLQPMGVYSTLWEADDWATRGGLEKIDWTKAPFLAYYKDFDIEGCPVPGPVNCATNSRNWWEGTAYQALNAMEAKRYRWVRMNHVIYDYCTDKSRYPVTPPECMSII
Protein: Probable ketoamine kinase HMPREF0351_12196 (EC 2.7.1.-) (Q3XZZ9)
Organism: Enterococcus faecium (strain ATCC BAA-472 / TX0016 / DO)
Function: Ketoamine kinase that phosphorylates ketoamines, such as erythruloselysine, erythrulosecadaverine, ribuloselysine and ribulosecadaverine, on the third carbon of the sugar moiety to generate ketoamine 3-phosphate. Has higher activity on free lysine (erythruloselysine and ribuloselysine), than on ribuloselysine and erythruloselysine residues on glycated proteins.
Interaction partners:
Sequence:
MDIQTVLSDLKLNGKVIPVVGGDVNQTYRIKTEHRAYFLKIHPNVKKGFFEAEVDGLKELSAFVRVPDTYMLGETSEGAYLLMEWIEPGKGDQRDLAAALANLHQQTAPQFGFRKDNYLGTLVQKNSFEEDWWTFFFKDRLESQISLAEETNRWNVQRQEKYLRFKERVLKSVEPKKITPRLLHGDLWSGNVFFDQQGHPVFVDPAVSYGNREQDIAMSQLFGGFRPEFLDAYQTIFPLEKGWKDRLPIYQLYYLLAHLNMFGESYGSQVDQLLENF
Protein: Dynein light chain (Q38DF9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU365010}.
Interaction partners:
- Cytoplasmic dynein 2 light intermediate chain 1
- Dynein light chain, putative
- Dynein light chain, putative
- Uncharacterized protein
- Dynein light chain 2B, cytoplasmic, putative
- Dynein light chain roadblock
- Dynein light chain roadblock
- Dynein light chain roadblock
- Dynein light chain 2B, cytoplasmic, putative
- Dynein heavy chain, cytosolic, putative
Sequence:
MSSGSHRSPSAMRPSTRISSIGATSNRSSTHNTETELDPFVASLSRVTVYTDIPDKTLQRIMSITVDAYNRFVLVPTRNTWRKEEGSRKELEREVERTALRDIAQAVKVNVEAALGGTWHVIYGRSFATYVTHQQRCFCHFQLDGANVVVWRHGG
Protein: Choline O-acetyltransferase (EC 2.3.1.6) (A0A060WZI4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Ribonuclease P/MRP 14 subunit
- SCP2 domain-containing protein
- Thiolase N-terminal domain-containing protein
- Podocan
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Hydroxysteroid dehydrogenase-like protein 2
- malate synthase
- Glycerophosphocholine phosphodiesterase GPCPD1
- Glycerophosphocholine phosphodiesterase GPCPD1
- Mitochondrial carnitine/acylcarnitine carrier protein
Sequence:
MPILEREPPKGRRESYVLPKVPVPPLKQTLDMYLNCMKHLVKEEQYQKTKAIVVKFGEPGGTGELLQKKLLERSEKTYNWVYDYWLEDMYLNQRLALPVNSNPAMVFPKQNFKDRKDSLRFAAHLITGVLEYKERIDTRVLPVDFARGQLAGTPLCMKQYYRLFNTYRLPGHKRDTLIIHKPGSTEQEHIIVACKNQFFVLDLVVNKKKLKEMDILTQLEKIVKMAENSEERQPPFGLLTSDGRTEWAQAREVLIKDSVNRESLAVIEKCLCVLCLDNPSGMEVGDTSRALLMLHGGGHEKMGANRWYDKPMQFIVGEDGVCGTVCEHSPFEGIVLVACTEYLMKFMTGSPSKMGRATSVSELPTPARLLWKTTPHIQDLLKASAERLQR
Protein: Beta-1,3-galactosyltransferase sqv-2 (EC 2.4.1.134) (Squashed vulva protein 2) (Q9N491)
Organism: Caenorhabditis elegans
Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-linked galactose residue. Required for vulval morphogenesis and zygotic cytokinesis, suggesting that glycosaminoglycans play a central role in vulval morphogenesis.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Xylosylprotein 4-beta-galactosyltransferase
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase sqv-8
- Xylosyltransferase sqv-6
- B3GNT1, Beta-1,3-N-acetylGucosamiNylTransferase 1, homolog
- UDP-glucuronate decarboxylase
- Uncharacterized protein T07A5.1
- Glycosyltransferase-like protein LARGE
- Phosphatidylinositol-glycan biosynthesis class W protein
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
Sequence:
MRFYRTYLLVAGAFCSLCTLAVIFNCGWDDSPPATPSAINGGGSNAPLISSPTNLPETFLYISILTSPNETERRQNVRDTWFRLSTKGPSVFIAKFAVGTMGLAAEDRRLLAEENEKFGDLALLDRHEESYERLAKKTLACFVHAFANFKFKFFLKTDIDSFVRITPLIINLKQIQDPMLYWGFLDGRAKPFRKGKWKEPEWNLCDRYLPYQLGGGYVLSYELIRFLAINAQLFRHYRNEDVSVGAWIGGLDVKYVHDPRFDTEWRSRGCNNEYLITHKHTEQEMQEMFENLKKTGKLCAKEFQKHPSYVYDFSKAPSECCTRVNGSNIP
Protein: WD repeat-containing and planar cell polarity effector protein fritz (Q9VQ36)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Functions cell autonomously to regulate wing cell hair polarity and number.
Subcellular location: Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}.
Interaction partners:
- Protein inturned
- Protein fuzzy
Sequence:
MLLSETHFWTTLREDVVRIKSQDLGAFRYLRQRDKEQEQQDLACLAKRDYTERRNGLAVLKNSGRKSTGRLKDNLKKLEDLLRQHRIIHSEWQDAAQVLLLFSHGLIAHICVDIYTGDILRMVFEKYLVGKLASEVITDAFFTRSHIVLAYNTNQLTVVHLQRPNARSQGPEKIANMDPRIFHVIIPGATERKLSRHLTVNASFDLFVVWTQSSQNEVYPWRPTIRDQDRANIHVFKIKGLQLESIAYCWSENDPLCVDFLRSSESQIITLEQKVSRKGDISAEICSYELAAGKMQRTAITSIPMGAQICSFAFSPDQEKLFLGSVDRNICLHDLVQQSTKYANQIEIVPNQCAWHCDSAMLCVANERSVLQCFDLALATIGHQLVSENVTPSSLLDLSHYFVAQPTLLSVAFSRKPDLSTFKHTYAQTDCLLLLVYEQGPLACMRIFGGTGMRGDIHNSGLTADVIADKYLRLQQPDRAVNVLAALNWETYGAMCLITLHKIANYVFFGGDQRRPRIELMARALKTFAHTLSEETKDEFSDQVYDLKRRFCFYLLRKNLFAEAFEIAQDVADYDIFMDLYNLTKCISSLSEFAQVAFSQAAAIIHEEDRANGNLSLTCDLRSESACSLSTCSDMLRGQGAGTAPETGLGASQPQSQQVLKNYVPPLPSFKSKVFNAEMIKINIPKPELRPPLPKVSIAPPTSSLASLTLKSNSSLQQAPAKSLHPNGNLWSQDVPDQTVGLPMASSPLPRLPPSNIPDQSAQLGQFSTMPASPPPTGSYQPKFYQHPLVSGNIPAMLPSLTSEDYQKRLLQKKPTASILSNPANPAPTNGEAPATPAKSQTAEKNKVKFSDTIQVAVVPEIPRKEKPMPPKRNGYSRPAARHLTNPKKELADSLPLCHPNDEYLKDFNPITTNVTKPPIRRREEEPKSSSKGGNSSSSSSSIKVVHFGVV
Protein: BcDNA.GH07188 (Q7KML7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MVAAAPTSEEDLKQDTPYMKELLRQAKTAEIESFMDQKADPCNDFYAFSCGNYKRINSALSMQVVTTGVFETLTKGLNRKILKMLNTPHDSHDTPEDIKVKHFYESCLQIKELNSTYSEKLKRLIAEFGTMPLLEGSSWQEDDFDWLNTTARMAYRYGITPIFGIEVNKDLASNTRNRIYLGQQDFPLEARSMYVDDATAVYRQKYRNNIQRILQRYLGVKMDLAKKTAKELIDFEVDLAQGLVDESEGLDVGELTQLLTVDEIQRRYSPTLDIDRLLFVSMGERISDQIYEYNNRYQQNLVEVIKRTPKRTVANYIFFRLIWEFVETPSDSPEKQMKACVDLTKKYFAKNLDNMFYRRYNNEKSSREIDNMWRQLKSTFNETLRSSPALNWIERPTRNLAMAKLQAMTLEVNNYADDNFTEEFAELNLQSDDYVENVRYTSLLGAKQMREMLHKPAKPFEAGSQLSYTPANILIENTIKVPVALLQPFYIWSDVYPNAIMFGTLASLIGHELIHGFDDSGRKFDEKGNSKDWWDEKSSSNFLKRRDCFTKQYGRYVYDGIQLKESTAQSENIADNGGMRLAYTAYRKWYENQLTLPNGAQDMTKETLPNLRYTAKQLFFISFAQSWCNDAHPSVKALQVSTDQHMPGRFRVIGSLSNFEEFSKEFNCPAGSAMNPSEKCILY