wanglab/gogpt-training-data huggingface dataset:
Protein: FYVE-type domain-containing protein (Q5FC45)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLRRLKEQVSQVANDIDGRLNNSRPSISSQGSQSQSQKSENDQEIEGFLCPMCMVELGGPDELTVHFEKEHSDTSANRNHPDYTPPQQAPLAFATKDQEIEELRIRVNEEKRFAERIKEELDNIKSVMAIASEVTEDEIPYMAQQIQVLTADKGMVTRQFLELEKESGQQSRELQQVKQERGDLMAKLKQMSVTMREITDESESGKVEMEDLKRELKVVKSDVVRYEIEVSRLEKMLDQRPSEDDVNVLRTELVNAQKLMDAISQEKDIEIKEHLNSIRNLSMEREKQHIVNENLEKKIGEGEETVKQLQISYDAQSEELKQRNERVVQLEARIEENVFELSENKQNVKRLEDKVQESQDALQMLSNINGSNEEQMISLNSKFERNTAERKRIEAVFEEKVTVQGERLKTLEMANLDLTNELASMGSLLDKERSLLEEKNKEISERDSSINDLKEKLAESEKKATKYKNELKEHADLVENLTLQLNKLQENSKDLMEKISAGEGGAKMAIEQLEQEKVKLTNELQTSSEKTKKASGELEAKISELEKKLRDAEASRTDKEQKWKQEKESFERKLAEAEDEIKRKGERFVEMEKEMEEERQKATDRTLKLKDALVNSEKNLETIKKESEDREKIVREKDAHLEENKKRIEDAVQKLEEAEKRARELEASVSSRDTTVSTKESELSELKGKLTESNSFIEELKVQVEKVSNEISEKQQEVENLMAEMRDKEAHWKTKRDEFEAQMLRNQEDNEEASSTLKSVQEQLMKEKETSGEEKNQLISVKSQLEELKTEVERLIRSEEEKTQEIEKLKSAVTATTQERDELTATSESLRTECENLNSKIQSIEESRRHAEEKGSENLERMITEKSRLEKDIEERESTIQSIQEALETKDNEIESLKTTQRVVEDELVSKISHIESFNSRIEEFEKEMASGKRTIERLEAEKAEETEKLVVFTGTQSQKQEELEKLQKEIQEKETTIARMTSSKTQFEAMFADVQQTLSKEINDKTEEIERLMERIDSLEKVNHSRIEELESRLTQRERVVESLEADLAAVRNIEQEKLDELQKLKEEFDELKKAETMWQAEKDMLIERCLGSESDIEYEKERSQENKRRFDDALSAMHELGRANQSLQIDADRYSSRKWLDDAEAINCTECGKVFSLTVRKHHCRVCGKIYCNPCSSKSVRIASAKNPVRACNTCFTDSQK
Protein: Cell wall mannoprotein 1 (O42721)
Organism: Talaromyces marneffei (Penicillium marneffei)
Function: Constitutive protein of the cell wall. Binds fatty acids and may thus serve as a fatty acid transporter between P.marneffei and host cells during infection. Abundant antigen target of host humoral immune response.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:10074513, ECO:0000269|PubMed:9488383}. Note=Associated with the entire thickness of the cell walls of yeast and conidia found in mold form. Localizes on the outer layers of the hyphal cell walls. {ECO:0000269|PubMed:9488383}.
Interaction partners:
Sequence:
MKFLSSLVVLGLSAQALASPYVDHQATKDQRDVNVFKQVLQDINLDVQKFDQDITQYQGGDPTVLLADSDAIIKTTEEGIQRIGPQPPLSVTEALALVGPVQGVNKLIMKAVDHLIEKKGPLVGGGYGPQVKDSLERQAHAASKLSELVSSKVPSPLAPISKQLSDQVAQALQKGIQAFSISARQATKVKREATKVQRDISAFKKVIQNISLAVNKFNVDIERYVGGDASHLLADGNVLIKATLDGVQSLQNEPPLSSMEALALVGPVQDLSNQILLAIQNLIDKKEPLVQAGFGGKVENNLRQQEEAAQKLSELVSTKVPHELADISRQLSDGIAAGIKKGIDAFAGTGPAPTTSSTPEASTAPAPSTPPQTPEDTLVPATSTPAPGPAPTAPDSSMVWPTSTTASPDVQPTITSSGTSVPAAPTGGNSSPAVPAFTGAASANQVSGAVGLAAGLLAVLAF
Protein: Phosphate-specific transport system accessory protein PhoU homolog (Pst system accessory protein PhoU homolog) (P72686)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Plays a role in the regulation of phosphate uptake.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphate transport system permease protein PstA
- Phosphate transport system permease protein PstA
- Phosphate import ATP-binding protein PstB 1
- Phosphate import ATP-binding protein PstB 2
- Phosphate import ATP-binding protein PstB 3
- Sll0540 protein
- histidine kinase
- Phosphate transport system permease protein
- Phosphate transport system permease protein
- Protein SphX
Sequence:
MAASLSQQINNPERSYFEQALKRVEQDVLRMGALVEESFRMSHQALFENRLETPLKIAELEKEIDRLYRHIEQECASFLTLQAPVAQDLRLLSAIMQLVRDLERIGDYAQDLGEIAMKLTRYPPHPCMDEIAAMAWQAQHMLDQSLVCLTQLDPNAGEIVKKMDDVVDDAYDRLYKTLAFQRDIKGVVEPILLMALVIRHLERMADHATNIAQRVSYIVTGKRE
Protein: Thioesterase domain-containing protein (A0A0H2URF0)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKDFHFDAISAFENYEIEKMRDGHVVVTTKVVNSSLNYYGNAHGGYLFTLCDQISGLVVISLGLDGVTLQSSINYLKAGKLDDVLTIKGECVHQGRTTCVMDVDITNQEGRNVCKATFTMFVTGQRSEERRVRI
Protein: Membrane protein (M protein) (E1 glycoprotein) (Matrix glycoprotein) (Membrane glycoprotein) (P59596)
Organism: Severe acute respiratory syndrome coronavirus (SARS-CoV)
Function: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04202}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04202}. Note=Largely embedded in the lipid bilayer. {ECO:0000255|HAMAP-Rule:MF_04202}.
Interaction partners:
Sequence:
MADNGTITVEELKQLLEQWNLVIGFLFLAWIMLLQFAYSNRNRFLYIIKLVFLWLLWPVTLACFVLAAVYRINWVTGGIAIAMACIVGLMWLSYFVASFRLFARTRSMWSFNPETNILLNVPLRGTIVTRPLMESELVIGAVIIRGHLRMAGHSLGRCDIKDLPKEITVATSRTLSYYKLGASQRVGTDSGFAAYNRYRIGNYKLNTDHAGSNDNIALLVQ
Protein: Eukaryotic translation initiation factor 5 (eIF-5) (P59325)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 1
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic initiation factor 4A-I
- Eukaryotic translation initiation factor 3 subunit D
Sequence:
MSVNVNRSVSDQFYRYKMPRLIAKVEGKGNGIKTVIVNMVDVAKALNRPPTYPTKYFGCELGAQTQFDVKNDRYIVNGSHEANKLQDMLDGFIKKFVLCPECENPETDLHVNPKKQTIGNSCKACGYRGMLDTHHKLCTFILKNPPENSDIGTGKKEKEKKNRKGKDKENGSVSTSETPPPPPPNEISPPHAVEEEEDDDWGEDTTEEAQRRRMDEISDHAKGLTLSDDLERTVEERVNILFDFVKKKKEEGIIDSSDKEIVAEAERLDVKAMGPLVLTEVLFDEKIREQIKKYRRHFLRFCHNNKKAQRYLLHGLECVVAMHQAQLISKIPHILKEMYDADLLEEEVIISWSEKASKKYVSKELAKEIRVKAEPFIKWLKEAEEESSGGEEEDEDENIEVVYSKTASVPKVETVKSDNKDDDIDIDAI
Protein: L-threonine dehydratase catabolic TdcB (EC 4.3.1.19) (L-serine dehydratase) (EC 4.3.1.17) (Threonine deaminase) (P0AGF6)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. TdcB also dehydrates serine to yield pyruvate via analogous enamine/imine intermediates.
Interaction partners:
- Threonine/serine transporter TdcC
- Threonine synthase
- PFL-like enzyme TdcE
- L-serine dehydratase TdcG
- Propionate kinase
- Branched-chain-amino-acid aminotransferase
- Low specificity L-threonine aldolase
- HTH-type transcriptional regulator TdcA
- Acetolactate synthase isozyme 1 large subunit
- Acetolactate synthase isozyme 3 small subunit
Sequence:
MHITYDLPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRVSQITGFVDA
Protein: Pre-rRNA-processing protein rix1 (P87243)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA and the nucleoplasmic transit of the pre-60S ribosomal subunits. Regulates pre-60S association of the critical remodeling factor mdn1 (By similarity). Also required for heterochromatic gene silencing.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P38883}.
Interaction partners:
- Pre-rRNA-processing protein ipi1
- Pre-rRNA-processing protein crb3/ipi3
- Pescadillo homolog
- Nucleolar GTP-binding protein 2
- Nucleolar complex-associated protein 3
- Putative ribosomal RNA-processing protein 12
- Uncharacterized protein C1105.01
- Ribosome biogenesis protein ytm1
- Eukaryotic translation initiation factor 6
- Ribosome biogenesis protein erb1
Sequence:
MSDLLERGSLPLVKSWLAITFANEEDLPFQVPQIADILVHQKCIERLGTSENALSVRKNWCTSLTKMLQSKDFRIRWSAIILIHCTISQSWDCLVEHGATWAKLLIALLNRPETPKTLEIAMITVSKMFSSTVGRPAVTRELVTPNLPTFVNNCLRIAESGKCLCTVCSCLYQGIISHSPTFRPFVSSIRNICIKILDGEEVVPSSLQKKAAVLYASLYRCVGKGNFEDYWKQSIISILKEYHLTLDFLFQFVIEPQTYPTREENLMFPKLKGHYEETYQKALHRCRTLNLILISFLSTKTDKIVLLPINALKDLIQRVYTVQLSLPVKSVESSVQALLFMVLPHLHTLVNELTLKLFVVIPPAIILSFDSYLDSLNDCLLSESTHTGVLCSSLKLLSKFLDVTHMNVPLSKYENIVTLVLEYLANSSKGLASKSIEFSKNRGHSQKKRKTLSESQAGDTLMSSEESHQLYDSDVMDCCFSFLASILTHSIALPRLLRTKIDLCTLQISLSNPTSTVLISMHNLLLASILSPGDSQAVIVPHAIRIISGPLGLVHPDPLVASHARSSMQTIESLIHPRFPPLQKHLSPSEFENTFESRFEPVSLENQSHISPPQVDSQSEYKESSILAPSNPPFETESITDSTEIEGIKESFASTDTGLQNNSTATSENKRSESELTMSNVLSNEGDRNEEGSEINSSQPSTINHGTDHINIVSENKETTVSLLHGDVEVEETTNVALNNSQDTETKFTAIDVDFVDRPTSVVSSQIENINGDENGNTTSSVVETFEKTTDVVDEKTTSINVEGNGEDDEEEDNISLPSINLESDSDS
Protein: SR-related and CTD-associated factor 4 (CTD-binding SR-like protein RA4) (Splicing factor, arginine/serine-rich 15) (Q63627)
Organism: Rattus norvegicus (Rat)
Function: Anti-terminator protein required to prevent early mRNA termination during transcription. Together with SCAF8, acts by suppressing the use of early, alternative poly(A) sites, thereby preventing the accumulation of non-functional truncated proteins. Mechanistically, associates with the phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit (POLR2A), and subsequently binds nascent RNA upstream of early polyadenylation sites to prevent premature mRNA transcript cleavage and polyadenylation. Independently of SCAF8, also acts as a suppressor of transcriptional readthrough.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O95104}.
Interaction partners:
- Probable helicase senataxin
- DNA-directed RNA polymerase subunit
- Transcription elongation factor 1 homolog
- DNA-directed RNA polymerase subunit beta
Sequence:
MDAVNAFNQELFSLMDMKPPISRAKMILITKAAIKAIKLYKHVVQIVEKFIKKCKPEYKVPGLYVIDSIVRQSRHQFGTDKDVFGPRFSKNITATFQYLYLCPSEDKSKIVRVLNLWQKNGVFKIEIIQPLLDMAAGTSNAAPGAENVTNNEGSPPPPVKVSSELPQAPTNSMPAVPQLPSSDAFAAVAQLFQTTQGQQLQQILQTFQQPPKPQSPALDSAVMAQVQAITAQLKTAPTQPPEQKTAFDKKLLDRFDYDDEPEAVEDSKKEDAVAVATTALATAAPPVPAAATPAVAPAVPASSATSPPPPQAPFGYPGDGMQQPAYTQHQNVDQFQPRMMALQQDSMQHQVPLPPNGQMPGFGLLSAPPPFPPMPQPGMPQPGMPQPGMPQPGLSQPGLPQPGMPQPGMPQPGMPQPGMPQPGLPQPGLPQPGMPQPGMPQPGMPQPGMPQPGMPPTPPVQPTFQPTFQPQNEPHSQKPHQQEMEVEQPCVTEVKRHVPESRKSRSRSPKRRRSRSGSRSRRSRHRRSRSRSRDRRRHSPRSRSQERRDREKERERRQKGLPQIKSETASVCSTTLWVGQLDKRTTQQDVASLLEEFGPIESINMIPPRGCAYIVMVHRQDAYRALQKLSRGNYKVNQKSIKIAWALNKGIKADFKQYWDVELGVTYIPWDKVKAEELESFCEGGMLDSDTLNPDWKGIPKKPENEVAQNGGAEASHTEPVSPIPKPVPVPVPALPVPAPITVPPPQVPPHQPGPPVVGALQPPAFTPPLGIPPPGFGPGVPPPPPPPPPFLRPGFNPMHLPPGFLPPGPPPPITPPVSIPPPHTPPISIPNLVSGARGNAESADSAKMYGSAGPPAAPTSLPTPPVTQPVSLLGTQGVAPGPVIGLQAPSTGLLGARPGLIPLQRPPGMPPPHLQRFPMMPPRPMPPHMMHRGPPPGPGGFAMPPPHGMKGPFPPHGPFVRPGGMPGLGGPGPGPGGSEDRDGRQQQPQQQQQQQQQQQQQQQQQQQQPPPQQSQTQQQPAPSQQPAPAQQQPQQFRNDNRQQFNSGRDQERFGRRSFGSRVENDRERYGSRSDERDNSNRERREWGRRSPERDRHRDLEERSRRSSGHRDRDRDSRDRESRREKEESRGKEKHEVADRAGGNKAVEAPLSQVGNTDTVSELNKGEAMATVVKPEESPAEATSSVEPEKDSGSAAEAPR
Protein: Cell division control protein 15 (EC 2.7.11.1) (P27636)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein kinase of the mitotic exit network (MEN) essential for late nuclear division in the mitotic cycle. Promotes mitotic exit by phosphorylating DBF2 and directly switching on DBF2 kinase activity. Involved in the localization of DBF2 and DBF20 to the neck which is necessary to undergo cytokinesis. Plays a role in segregation of chromosomes during recovery from spindle checkpoint activation. Required for spindle pole localization of CDK1 and inactivation of CDC2 kinase activity at the end of mitosis. Required for spindle disassembly after meiosis II and plays a role in spore morphogenesis.
Subcellular location: Cytoplasm, cytoskeleton, spindle pole. Bud neck. Note=Localizes to the spindle pole bodies at late anaphase and translocates to the cytoplasm upon DNA replication stress. Localization to SPBs depends on CDC5 and TEM1 and is inhibited by BUB2. Accumulates at the daughter SPB after anaphase onset when the daughter SPB begins to penetrate the bud neck. Not found in the mother SPD during early anaphase. As anaphase proceeds, continues to accumulate on the daughter SPB and also localizes to the mother SPB. At the end of telophase, a portion of CDC15 localizes at the mother-bud neck.
Interaction partners:
- Tyrosine-protein phosphatase CDC14
- Nucleolar protein NET1
- Cell cycle protein kinase DBF2
- Protein TEM1
- DBF2 kinase activator protein MOB1
- Mitotic check point protein BUB2
- G2/mitotic-specific cyclin-2
- Sporulation-specific protein 12
- Kinetochore protein SLK19
- Protein SIC1
Sequence:
MNSMADTDRVNLTPIQRASEKSVQYHLKQVIGRGSYGVVYKAINKHTDQVVAIKEVVYENDEELNDIMAEISLLKNLNHNNIVKYHGFIRKSYELYILLEYCANGSLRRLISRSSTGLSENESKTYVTQTLLGLKYLHGEGVIHRDIKAANILLSADNTVKLADFGVSTIVNSSALTLAGTLNWMAPEILGNRGASTLSDIWSLGATVVEMLTKNPPYHNLTDANIYYAVENDTYYPPSSFSEPLKDFLSKCFVKNMYKRPTADQLLKHVWINSTENVKVDKLNKFKEDFTDADYHWDADFQEEKLNISPSKFSLAAAPAAWAENNQELDLMPPTESQLLSQLKSSSKPLTDLHVLFSVCSLENIADTIIECLSRTTVDKRLITAFGSIFVYDTQHNHSRLRLKFIAMGGIPLIIKFEHLAKEFVIDYPQTLIECGIMYPPNFASLKTPKYILELVYRFYDLTSTAFWCRWCFKHLDISLLLNNIHERRAQSILLKLSSYAPWSFEKILPSLIDSKLKKKILISPQITYVVFKSINYMITTNDDKIHKSAIPSSSSLPLSSSPTRNSPVNSVQSPSRSPVHSLMATRPSSPMRHKSISNFPHLTISSKSRLLIELPEGFFTWLTSFFVDMAQIKDLSVLKYFTKLCYLTVHINSTFLNDLLDNDAFFAFIRNIDTIIPFIDDAKTAAFIWKQITAICVEMSLDMDQMSASLFSTAMNFIRKKNNTSISGLEIILNCLHFTLRNVNDDVAPTVGSSESHSVFLIKVNNDAAIELPIDQLVDLFYALNDDDVNLSKLISIFTKICSLPGFENLTINIIFHPNFYEKIVSFFDTYFNSLLIQIDLLKFIKLIFSKSLLKLYDYTGQPDPIKQTEPNRRNKATVFKLRAILVQITEFLNNNWNKDVPKRNSNQVGGDSVLICQLCEDIRSLSKKGSLQKVSSVTAAIGSSPTKDERSNLRSSKDKSDGFSVPITTFQT
Protein: Uncharacterized serine/threonine-protein kinase SBK3 (EC 2.7.11.1) (SH3 domain-binding kinase family member 3) (Sugen kinase 110) (P0C264)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MERRASETPEDGDPEEDTATALQRLVELTTSRVTPVRSLRDQYHLIRKLGSGSYGRVLLAQPHQGGPAVALKLLRRDLVLRSTFLREFCVGRCVSAHPGLLQTLAGPLQTPRYFAFAQEYAPCGDLSGMLQERGLPELLVKRVVAQLAGALDFLHSRGLVHADVKPDNVLVFDPVCSRVALGDLGLTRPEGSPTPAPPVPLPTAPPELCLLLPPDTLPLRPAVDSWGLGVLLFCAATACFPWDVALAPNPEFEAFAGWVTTKPQPPQPPPPWDQFAPPALALLQGLLDLDPETRSPPLAVLDFLGDDWGLQGNREGPGVLGSAVSYEDREEGGSSLEEWTDEGDDSKSGGRTGTDGGAP
Protein: Calsequestrin (C0KTH7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004564}.
Interaction partners:
Sequence:
MLALWLLLLPCLSLSPLVQTEKGLEFPRYDGKDRVIDINNKNYQKAMKKYTMMCLLYHKPIPDGEELQKQHLMTEMVLELAAQVMEEKEIGFGMVDSHKDTKVAKKLGLVEEGSVYVFKADRVIEFDGMLSADTLVEFLLDLLEEPVEVIGNALELRAFDRMEEDVRLIGYFKNEDSEHYSAFKEAAEQFQPYIKFFATFEKAVAKELTLKMNEVDFYEPFMEEPVTLPDRPNSEEEIVAFVTEHRRPTLRKLRAEDMFETWEDVVEGSHIVAFAEEEDPDGYEFLELLKEVARDNTHHPGLSIIWIDPDDFPLLIPHWEKTFQVDLFKPQIGVVNVTDADSIWLEMEEQDLLTAQKLADWIENVLSGKVNTEDDDDDNDDDEEEDDDDDDDDDSDDDSDDDSDDDSDDSDDSDDEEDEDDDDE
Protein: PHD finger protein 7 (H7C4N0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XDPEKLGEFLQKDNISVHYFCLILSSKLPQRGQSNRGFHGFLPEDIKKEAARASRKICFVCKKKGAAINCQKDQCLRNFHLPCGQERGCLSQFFGEYKSFCDKHRPTQNIQHGHVGEESCILCCEDLSQQSVENIQSPCCSQAIYHRKCIQKYAHTSAKHFFKCPQCNNRKEFPQEMLRMGIHIPDRDAAWELEPGAFSDLYQRYQHCDAPICLYEQGRDSFEDEGRWCLILCATCGSHGTHRDCSSLRSNNYIPENSGDIPCCSSTFHPEEHFCRDNTLEENPGLSWTDWPEPSLLEKPESSRGRRSYSWRSKGVRITNSCKKSK
Protein: Guanine deaminase (Guanase) (Guanine aminase) (EC 3.5.4.3) (Guanine aminohydrolase) (GAH) (p51-nedasin) (Q9Y2T3)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Interaction partners:
- Purine nucleoside phosphorylase
- Xanthine dehydrogenase/oxidase
- Adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- Disks large homolog 4
- Disks large homolog 3
- Uracil phosphoribosyltransferase homolog
- Histidine ammonia-lyase
- 5'-nucleotidase
- Uridine phosphorylase 2
Sequence:
MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV
Protein: Serine/threonine-protein kinase gad8 (EC 2.7.11.1) (Q9P7J8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in a signaling module for sexual development and cell growth under stressed conditions. Required for G1 arrest under nitrogen starvation and for growth at high temperature and osmolarity.
Interaction partners:
- Serine/threonine-protein kinase tor1
- Target of rapamycin complex 2 subunit sin1
- Serine/threonine-protein kinase tor2
- cAMP-dependent protein kinase regulatory subunit
- Small ribosomal subunit protein eS6A
- Small ribosomal subunit protein eS6B
- GTP-binding protein ryh1
- Fork head protein homolog 2
- Tuberous sclerosis 2 protein homolog
- Tuberous sclerosis 1 protein homolog
Sequence:
MSWKLTKKLKETHLASAIGLNSGGSSFTRGLKNSTLSSTSSRKSSDEKSRKSSEDKRSPQSTVVQPGLLQVTIIEARNLKLPSGHVPANYGVSIDNSLLAPPLSNGSGHARSRSHAWWLPYIVVEFDKNEILVDALNTASLENPCWDYQATFDVSRYSKLSLNIYLRSSSSRSRNGMGNDAFLGGIKLSPSFIVNKLTDEWVPLHGGSGELRVQMLYKPNQSTPLTIDAFELLKVVGKGSFGKVMQVRKRDTSRIYALKTMKKAHIVSRSEVDHTLAERTVLAQVNNPFIVPLKFSFQSPGKLYLVLAFVNGGELFHHLQREGCFDTYRAKFYIAELLVALECLHEFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMAKTDRTNTFCGTPEYLAPELLLGHGYTKVVDWWTLGVLLYEMITGLPPFYDENINEMYRKILQDPLRFPDNIDEKAKDLLSGLLTRAPEKRLGSGGAQEIKNHPFFDDIDWKKLCAKKIQPPFKPSVESAIDTSNFDSEFTSEIPMDSVVADSHLSETVQQRFANWSYQRPTTIDTSDDINTIAPGSVIR
Protein: SUppressor of activated let-60 Ras (Q19096)
Organism: Caenorhabditis elegans
Interaction partners:
- Cation diffusion facilitator family protein 1
- Zinc transporter 2
- Histidine ammonia-lyase
- Zinc transporter ttm-1
- Protein MAK10 homolog
Sequence:
MSSNKNNITTNVISAAQRAHFEESPLMQNEQVIRTQGALHRLVVITVLFLALTQYGYGIAFHSSLMSIQFAASALAFISSIEVLWHSKSKNDIANRHSVFLLYRTAGTVFFIACLFLNLTHCLEDVSDLNSATHSEVGNETESVEEAHEHPIAYHTLYLSTADLVIKAIFSVIYNALSIHFVPNFIALVAPPVLTILIFFYNVNELDYFFGWLNHHLEPVTSILLTIVCISIAIYSLIRKKQFLLAEGPREFKIDDISSSVKAKNSRLEKVDHVHASCEWPQGFTVSLKAYIKVEKTNKDWVAQAASDFYELKALLHHEIKAQGAKEVVVEPVFVDQTELTTDFMDPICISRSCHNEDVGCCTIPKSTGDV
Protein: X11L, isoform B (X11L, isoform C) (E1JJN6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSNSCSDSSNESMVNPPHIQMNFGQQAQQQQSHQHQQQQQQQERYVWEMRTRSPNVTPASTVLNSPDLNGELSYVPLQGLSPSGGGVQGSGSYGSNAGRDSGSYYYQRPQLHQIRLGRSPGSQFETRDVLPQGLASPGSPTDVGKADGQCLRDGEIVVFDDIDTNWMNKASSGQRPGSNEDVLKVTKMIGQLPIAEYEGSPRRFGSQPNTNTITMGGPRKRPPGFPQRVSPTTSVANNATAAAKASVGNLIDLVDHEEERSGTLREKTPTFDYLYEFSETRKVLEEFFKANPEDEKRYTDYTTESGDDVASSQPQEYPATPMEQAYIGQRLARIPKDELYMVHRSPTKKPPSDQNPSTAYQEHNDIELYIDSNSRSSGDLADTELEANLRRHSRNFTLSPETTDYDSNCGDLDSLSNDINCPTDFGKLYTSMPVLEDGLSSGHASDTENNVSVVCDKQQSSQSQPVHEHNGNGERLENDYNVMSASLATLTTDASQSALISDFASLPMPPAPPPSSPPQIEIADASESMTMVPDADNPLDSHYGAVYAAALGGTHTEKSAGSGLGVTPVTAGGSLPSQAASEIQEAMKEIRSALQRAKTQPEKLKFCDEVLPTDPDSPVWVPRKGTTISTAQGAAADEEPDTDLETDRLLGQQRHDEQDFFADQSLADNNANEGTDIASNGHLNGTSDNNNPNPMNNSKPQTYSTATIRQGIGTSLTPNSPDICQIVGTTDISISSPEKLQFTKSPTGSIKSLKDSANSDKKAKSRNKEGLLEPKVLIEGVLFRARYLGSTQLVCEGQPTKSTRMMQAEEAVSRIKAPEGESQPSTEVDLFISTEKIMVLNTDLKEIMMDHALRTISYIADIGDLVVLMARRRFVPNSVVDPSITSPLGDVPTPGIGEEESPPKEPLSKHNRTPKMICHVFESDEAQFIAQSIGQAFQVAYMEFLKANGIENESLAKEMDYQEVLNSQEIFGDELEIFAKKELQKEVVVPKAKGEILGVVIVESGWGSMLPTVVIANLMSSGAAARCGQLNIGDQLIAINGMSLVGLPLSTCQSYIRNAKNQTAVKFTVVPCPPVVEVKILRPKALFQLGFSVQNGVICSLLRGGIAERGGVRVGHRIIEINNQSVVAVPHDTIVKLLSSSVGEILMKTMPTSMFRLLTGQETPIYI
Protein: Ferric uptake regulation protein (A2TEZ4)
Organism: Edwardsiella tarda
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364037}.
Interaction partners:
Sequence:
MTDNNTALKKAGLKVTLPRLKILEVLQDPTCHHVSAEDLYKKLIDMGEEIGLATVYRVLNQFDDAGIVTRHNFEGGKSVFELTQQHHHDHLICLDCGKVIEFSDESIEKRQREIAKKHGIQLTNHSLYLYGHCAEGDCRSDEALHDEKA
Protein: Centromere protein Cenp-F N-terminal domain-containing protein (Q8BV30)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSWALEEWKEGLPSRALQKIQELEGQLEKLKKEKQQRQFQLDSLEAALQKQKQKVEDGKTEGADLKRENQRLMEICEHLEKSRQKLSHELQVKESQVNLQESQLSSCKKQIEKLEQELKRCKSEFERSQQVAQSADVSLNPCSTPQKLFATPLTPSSTYEDLKEKYNKEVEERKRLEEEVKALHAKKVSLPVSQATMNHRDIARHQASSSVFPWQQENTPSRLSSDALKTPLRRDGSAAHFLGEEVSPNKSSMKTGRGDCSSLPGEPHSAQLLHQAKAQNQDLKSKMTELELRLQGQEKEMRSQVNKCQDLQLQLEKTKV
Protein: C-type lectin domain family 5 member A (C-type lectin superfamily member 5) (Myeloid DAP12-associating lectin 1) (MDL-1) (Q9NY25)
Organism: Homo sapiens (Human)
Function: Functions as a positive regulator of osteoclastogenesis (By similarity). Cell surface receptor that signals via TYROBP. Regulates inflammatory responses (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21566123}; Single-pass type II membrane protein {ECO:0000269|PubMed:21566123}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Hematopoietic cell signal transducer
- Tyrosine-protein kinase SYK
- High affinity immunoglobulin epsilon receptor subunit gamma
- Triggering receptor expressed on myeloid cells 1
- Maltase-glucoamylase
Sequence:
MNWHMIISGLIVVVLKVVGMTLFLLYFPQIFNKSNDGFTTTRSYGTVSQIFGSSSPSPNGFITTRSYGTVCPKDWEFYQARCFFLSTSESSWNESRDFCKGKGSTLAIVNTPEKLKFLQDITDAEKYFIGLIYHREEKRWRWINNSVFNGNVTNQNQNFNCATIGLTKTFDAASCDISYRRICEKNAK
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (EC 3.1.4.11) (Phosphoinositide phospholipase C-delta-1) (Phospholipase C-III) (PLC-III) (Phospholipase C-delta-1) (PLC-delta-1) (P51178)
Organism: Homo sapiens (Human)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development (By similarity). Binds phosphatidylinositol 4,5-bisphosphate.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Inositol polyphosphate-5-phosphatase A
- Protein kinase C alpha type
- Myotubularin
- Protein kinase C gamma type
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MDSGRDFLTLHGLQDDEDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRTPESQLFSIEDIQEVRMGHRTEGLEKFARDVPEDRCFSIVFKDQRNTLDLIAPSPADAQHWVLGLHKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMSFKELQNFLKELNIQVDDSYARKIFRECDHSQTDSLEDEEIEAFYKMLTQRVEIDRTFAEAAGSGETLSVDQLVTFLQHQQREEAAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGSAFSLAHRRVYQDMGQPLSHYLVSSSHNTYLLEDQLAGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCTLEQQRVMARHLHAILGPMLLNRPLDGVTNSLPSPEQLKGKILLKGKKLGGLLPPGGEGGPEATVVSDEDEAAEMEDEAVRSRVQHKPKEDKLRLAQELSDMVIYCKSVHFGGFSSPGTPGQAFYEMASFSENRALRLLQESGNGFVRHNVGHLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYQGRFQDNGACGYVLKPAFLRDPNGTFNPRALAQGPWWARKRLNIRVISGQQLPKVNKNKNSIVDPKVTVEIHGVSRDVASRQTAVITNNGFNPWWDTEFAFEVVVPDLALIRFLVEDYDASSKNDFIGQSTIPLNSLKQGYRHVHLMSKNGDQHPSATLFVKISLQD