wanglab/gogpt-training-data huggingface dataset:
Protein: NAD(P)-dependent benzaldehyde dehydrogenase (EC 1.2.1.28) (EC 1.2.1.7) (Q84DC3)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: NAD or NADP-dependent benzaldehyde dehydrogenase that catalyzes the conversion of benzaldehyde into benzoate in the (R)-mandelate degradation pathway.
Interaction partners:
Sequence:
MNYLSPAKIDSLFSAQKAYFATRATADVGFRKQSLERLKEAVINNKEALYSALAEDLGKPKDVVDLAEIGAVLHEIDFALAHLDEWVAPVSVPSPDIIAPSECYVVQEPYGVTYIIGPFNYPVNLTLTPLIGAIIGGNTCIIKPSETTPETSAVIEKIIAEAFAPEYVAVIQGGRDENSHLLSLPFDFIFFTGSPNVGKVVMQAAAKHLTPVVLELGGKCPLIVLPDADLDQTVNQLMFGKFINSGQTCIAPDYLYVHYSVKDALLERLVERVKTELPEINSTGKLVTERQVQRLVSLLEATQGQVLVGSQADVSKRALSATVVDGVEWNDPLMSEELFGPILPVLEFDSVRTAIDQVNKHHPKPLAVYVFGKDMDVAKGIINQIQSGDAQVNGVMLHAFSPYLPFGGIGASGMGEYHGHFSYLTFTHKKSVRIVP
Protein: Transcriptional adapter ADA2b (AtADA2b) (Protein PROPORZ 1) (Q9ATB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the function of some acidic activation domains, which activate transcription from a distant site. The exact mechanism of action is not yet known (By similarity). ADA2 stimulates the acetyltransferase activity of GCN5 on free histones or nucleosomes, probably by opening up the promoter region. Mediates auxin and cytokinin signals in the control of cell proliferation and might be involved in repression of a freezing tolerance pathway at warm temperature. Involved in the positive regulation of salt-induced gene expression by maintaining locus-specific acetylation of histones H4 and H3.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:12747832}.
Interaction partners:
- Histone acetyltransferase GCN5
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10
- Ubiquitin C-terminal hydrolase 22
- Transcription and mRNA export factor ENY2
- SAGA-associated factor 11
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Transcription initiation factor TFIID subunit 6b
- Transcription initiation factor TFIID subunit 5
Sequence:
MGRSRGNFQNFEDPTQRTRKKKNAANVENFESTSLVPGAEGGGKYNCDYCQKDITGKIRIKCAVCPDFDLCIECMSVGAEITPHKCDHPYRVMGNLTFPLICPDWSADDEMLLLEGLEIYGLGNWAEVAEHVGTKSKEQCLEHYRNIYLNSPFFPLPDMSHVAGKNRKELQAMAKGRIDDKKAEQNMKEEYPFSPPKVKVEDTQKESFVDRSFGGKKPVSTSVNNSLVELSNYNQKREEFDPEYDNDAEQLLAEMEFKENDTPEEHELKLRVLRIYSKRLDERKRRKEFIIERNLLYPNPFEKDLSQEEKVQCRRLDVFMRFHSKEEHDELLRNVVSEYRMVKRLKDLKEAQVAGCRSTAEAERYLGRKRKRENEEGMNRGKESGQFGQIAGEMGSRPPVQASSSYVNDLDLIGFTESQLLSESEKRLCSEVKLVPPVYLQMQQVMSHEIFKGNVTKKSDAYSLFKIDPTKVDRVYDMLVKKGIAQL
Protein: Guanine nucleotide-binding protein G(q) subunit alpha (EC 3.6.5.-) (Guanine nucleotide-binding protein alpha-q) (P82471)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Required for platelet activation. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity). Together with GNA11, required for heart development (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P50148}; Lipid-anchor {ECO:0000250|UniProtKB:P50148}. Golgi apparatus {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000250|UniProtKB:P21279}. Nucleus membrane {ECO:0000250|UniProtKB:P21279}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:P21279}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Sphingosine 1-phosphate receptor 2
- 5-hydroxytryptamine receptor 2C
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
- Histamine H1 receptor
- Regulator of G-protein signaling 2
- Beta-adrenergic receptor kinase 1
- 5-hydroxytryptamine receptor 2B
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
- Sphingosine-1-phosphate receptor 3
Sequence:
MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMVRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Protein: Tubulin tyrosine ligase-like 4A, isoform I (Tubulin tyrosine ligase-like 4A, isoform L) (Tubulin tyrosine ligase-like 4A, isoform N) (M9NEE5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRNNSGYHIPASNSLNNNGAPASRYCNADNTFCYYSYDNCNLIAPAWGNRQNQNQNSVPNQNHNLPTKRIPTKQSARSSYHQSAANSAPDSSLFTDAFGQQSLVNQRIAGNKSCEYVYQTVQRSEDQHSNRQYKQARSYAVDKEQQQQMLLQPSIVYFDAELKKRKDRGGRVSNDYVDNSPDRYRPLNSPSPEPTWDNILSERPVQYQTTNQHYQHYFSYFYNRGAEKLSKPTFAAANSRKVPMSKFQKAGASRRDSREVDGTVIIGRRDNSEDRTWQGQKYEKHVLKEKLPSNDLKADYLDNGWGGDPGSEDDYRDIKDSYDPVVVIDNGLEQVGVHRRYCRMTENTVLDGSGDTLINNNNNELKIMRKSTDQPMPRLPMTPKRAKGGTVSTKKPMPTVHRVLLYSTQSPRLGRKQQFSTQRLSVKQQSSKVLGAGDERQTVLLLEPEHKQEDHRSAIDFDRNDDFDEDDDLDNLSNFDESDTASVLSDTEDGYRAHAFKLTHSVDRFSSPQSTPSFLSSQSSEDDLKNPDSLLVPSLFPYVPPYLSFSSNTKRGPRVPPDLHRVLKWRITNIMPKVVRLILANSGMRMLKKTNDWMGVWGKHLKSPCFKAIRSYQKINHLPGSFRIGRKDSCWKNLQRQMGKHSNKEFGFMPRTYIIPNDLGALRRHWPKYAQRNTKWIIKPPASARGAGIRVINRWGQIPKRRPLIVQKYIERPLLINGSKFDLRLYVLVTSVNPLRVFMYHNGLARFASVKYSAKTDTLNDRCMHLTNYSINKFSSNYSKNEDVNACHGHKWTIKSLWTYLANRGVRTDCLWEALRSLVLRTILAGENGINSMIRANVESKYSCFELFGFDVILDSDLVPWLLEVNISPSLHSELPLDAHVKAPLVQGVLNTALYNVPPKLSLDKQKELAAEFSFPPGTQMCYDKRLYINYLSREEKIKHNTFTRKSMEDRNEYVDAILNNLTPDDVRCLIIAEDELARCAPLERIFPTDQTHKYLKYNDTPRYYNRLLDAWESRYANNRTEGIALLRDYCQNKYHLQVPTPPAKKVRSLFINSAEAFHKTHLNES
Protein: Chanoclavine-I dehydrogenase (ChaDH) (EC 1.1.1.332) (D3J0Z1)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Function: Oxidoreductase involved in the biosynthesis of ergot alkaloid biosynthesis. Catalyzes the oxidation of chanoclavine-I in the presence of NAD(+) resulting in the formation of chanoclavine-I aldehyde. Ergot alkaloids, which are produced by endophyte fungi, can enhance plant host fitness, but also cause livestock toxicosis to host plants.
Interaction partners:
Sequence:
MASVESRIIAITGGASGIGAATCRLLAERGAAVLCVCDISPKNFDDLKISIKKINPSTKVHCATVDVTSSVEVRQWIEGIISDFGDLHGAVNAAGIAQGAGMRNTPTIAEEVDEEWTRIMNTNLNGVFYCTREEVRAMKGLPATDRSIVNVGSIASVSHMPDVYAYGTSKGACAYFTTCVAADAFPLGIRINNVSPGVTNTPMLPQFAPMAKTFEEIEESYKKEGLSLIEAEDVARTIVWLLSEDSRPVFGANINVGACMP
Protein: Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1) (Q13136)
Organism: Homo sapiens (Human)
Function: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:24120883}. Cytoplasm {ECO:0000269|PubMed:7796809}. Note=Colocalizes with PTPRF near focal adhesions.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase F
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- ELKS/Rab6-interacting/CAST family member 1
- Receptor-type tyrosine-protein phosphatase S
- Receptor-type tyrosine-protein phosphatase delta
- ARF GTPase-activating protein GIT1
- Protein unc-13 homolog B
- Liprin-beta-1
- Glutamate receptor-interacting protein 1
Sequence:
MMCEVMPTISEAEGPPGGGGGHGSGSPSQPDADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDADVSDGEDDRDTLLSSVDLLSPSGQADAHTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESRVGSGSLDNLGRFRSMSSIPPYPASSLASSSPPGSGRSTPRRIPHSPAREVDRLGVMTLLPPSREEVRDDKTTIKCETSPPSSPRALRLDRLHKGALHTVSHEDIRDIRNSTGSQDGPVSNPSSSNSSQDSLHKAPKKKGIKSSIGRLFGKKEKGRPGQTGKEALGQAGVSETDNSSQDALGLSKLGGQAEKNRKLQKKHELLEEARRQGLPFAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLTSPSAPPTSRTTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRLNYDRKELERKREESQSEIKDVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLLVMGTDRRFDEDDDKSFRRAPSWRKKFRPKDIRGLAAGSAETLPANFRVTSSMSSPSMQPKKMQMDGNVSGTQRLDSATVRTYSC
Protein: ATP synthase subunit alpha (O96252)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- ATP synthase subunit C, putative
- ATP synthase subunit gamma
- ATP synthase subunit delta, mitochondrial, putative
- ATP synthase subunit beta
- ATP synthase subunit O, mitochondrial, putative
- ATP synthase subunit epsilon, mitochondrial, putative
- V-type proton ATPase proteolipid subunit
- JmjC domain-containing protein, putative
- V-type proton ATPase 21 kDa proteolipid subunit, putative
- Cytochrome c1, putative
Sequence:
MKASGLCQQLNKCMWNQLVVSRKCIKKFVCNYSTKISPIEISKILEKKFESFNFKTSSNEVGYVLSVGDGICRAYGLNNVKSSELVEIHNEDDKGSVTYGMATNLEYDNVGIVIFGNDRNIKEGDVIKRTNRIIDVNVGYELLGRVVDALGNCIDGEKNVVTKERRKIEIKAPGIIARKSVNESIITGIKCIDSLVPIGRGQRELIIGDRQTGKTAIAIDAIIHQKNINDNVLNNNEKVYCIYVAIGQKKSNIAKLVNLLKKYDALKYTIIVNSSASDASPLQFLAPYTGCAMAEFFRDNGKHALIIFDDLSKQAVAYRQLSLLLRRPPGREAYPGDIFYIHSKLLERSSKLNDNLKGGSLTALPIIETLNNDVSAYIPTNVISITDGQIFLESELFYKGIIPAINVGLSVSRIGSSAQYNCMKKLASSMKLELAQFREIVAFSQFGSDLDVSTKKLIEKGKILTEILKQKQYSPVNISYQICLIYAATKDYLLNLPIEKVQDFETKYFDYLDNNYLDVLKKIQSNCHLSEVEDQIKESIQKFLELYKNEA
Protein: V-set and immunoglobulin domain containing 4 (A0A8I6AIJ0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
PRNLLSLLLISSLWWTSCHPVLKTPERVTGTWKGDVKIQCIYNPLTGYREVLVKWLVQRGSDHVTIFLRDYSGDHVQQAKYRGRLKVSHKVPGDVSLQLNNLQMDDRNHYTCEVTWQTPDGDQVRRDKITELRVQKYPYKPPKITTEALTTMQSSLEATTITSSTSDWTTSVTQTPQGTTTVPGGKLPIFAIILIICFCCIVVVTIAFIMFRRRTFQVLVHRMYARQTSNSEETTRVTTIASAYFNNEPDSQALINDYSDDPCLSQEYQITTRSTMTIPAC
Protein: long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Q5BJL7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
DVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSVVKDPLFYLDARTGCYVALDQEAYTRIQAGEEKL
Protein: UV-stimulated scaffold protein A (Q2YD98)
Organism: Homo sapiens (Human)
Function: Factor involved in transcription-coupled nucleotide excision repair (TC-NER), a mechanism that rapidly removes RNA polymerase II-blocking lesions from the transcribed strand of active genes. Facilitates the ubiquitination of the elongating form of RNA polymerase II (RNA pol IIo) at DNA damage sites, thereby promoting RNA pol IIo backtracking and access by the TC-NER machinery to lesion sites. Acts by promoting stabilization of ERCC6 by recruiting deubiquitinating enzyme USP7 to TC-NER complexes, preventing UV-induced degradation of ERCC6 by the proteasome. Also facilitates transfer of TFIIH to RNA polymerase II. Not involved in processing oxidative damage.
Subcellular location: Chromosome {ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:22466612}. Note=Accumulates at UV DNA damage sites. {ECO:0000269|PubMed:22466611}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 7
- DNA excision repair protein ERCC-8
- DNA excision repair protein ERCC-6
- General transcription factor IIH subunit 1
- DNA damage-binding protein 1
- Cullin-4A
- DNA-directed RNA polymerase II subunit RPB1
- E3 ubiquitin-protein ligase RBX1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- Superkiller complex protein 8
Sequence:
MDQKLSKLVEELTTSGEPRLNPEKMKELKKICKSSEEQLSRAYRLLIAQLTQEHAEIRLSAFQIVEELFVRSHQFRMLVVSNFQEFLELTLGTDPAQPLPPPREAAQRLRQATTRAVEGWNEKFGEAYKKLALGYHFLRHNKKVDFQDTNARSLAERKREEEKQKHLDKIYQERASQAEREMQEMSGEIESCLTEVESCFRLLVPFDFDPNPETESLGMASGMSDALRSSCAGQVGPCRSGTPDPRDGEQPCCSRDLPASAGHPRAGGGAQPSQTATGDPSDEDEDSDLEEFVRSHGLGSHKYTLDVELCSEGLKVQENEDNLALIHAARDTLKLIRNKFLPAVCSWIQRFTRVGTHGGCLKRAIDLKAELELVLRKYKELDIEPEGGERRRTEALGDAEEDEDDEDFVEVPEKEGYEPHIPDHLRPEYGLEAAPEKDTVVRCLRTRTRMDEEVSDPTSAAAQLRQLRDHLPPPSSASPSRALPEPQEAQKLAAERARAPVVPYGVDLHYWGQELPTAGKIVKSDSQHRFWKPSEVEEEVVNADISEMLRSRHITFAGKFEPVQHWCRAPRPDGRLCERQDRLKCPFHGKIVPRDDEGRPLDPEDRAREQRRQLQKQERPEWQDPELMRDVEAATGQDLGSSRYSGKGRGKKRRYPSLTNLKAQADTARARIGRKVFAKAAVRRVVAAMNRMDQKKHEKFSNQFNYALN
Protein: Mating-type protein ALPHA2 (MATalpha2 protein) (Alpha-2 repressor) (P0CY08)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that binds cooperatively with MCM1 to a 31-basepair DNA sequence termed the a-specific gene (asg) operator, to repress the transcription of a-cell-specific genes. Additionally, in a/alpha diploid cells, binds cooperatively with the A1 protein to a 21-basepair DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MNKIPIKDLLNPQITDEFKSSILDINKKLFSICCNLPKLPESVTTEEEVELRDILGFLSRANKNRKISDEEKKLLQTTSQLTTTITVLLKEMRSIENDRSNYQLTQKNKSADGLVFNVVTQDMINKSTKPYRGHRFTKENVRILESWFAKNIENPYLDTKGLENLMKNTSLSRIQIKNWVSNRRRKEKTITIAPELADLLSGEPLAKKKE
Protein: 40S ribosomal protein S10, putative (Q38B66)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- 40S ribosomal protein S4
- 40S ribosomal protein S5, putative
- Small ribosomal subunit protein uS4
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S27, putative
- 40S ribosomal protein S33, putative
- 40S ribosomal proteins S11, putative
- 40S ribosomal protein S24
- 40S ribosomal protein S14
- 40S ribosomal protein S23, putative
Sequence:
MTTYVPKSSRDDVYRFFFTEGVVSCKKDPLGTWKGTLGGKTFKLPTLQVMQLMRSLKSRGLIKEQFAWRHFYWTLNDEGINYMRKYLYLGADAVPNTHKVDHKTFEREGGRGRGRGDGRGRGRGFGRGRGEGRGFGRGRGEGRGRGFHSERDQYRAGAAAQGEDAAPVAAVE
Protein: RIMS-binding protein 3A (RIM-BP3.A) (RIMS-binding protein 3.1) (RIM-BP3.1) (Q9UFD9)
Organism: Homo sapiens (Human)
Function: Probable component of the manchette, a microtubule-based structure which plays a key role in sperm head morphogenesis during late stages of sperm development.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q3V0F0}. Note=In elongating spermatids, localizes to the manchette. {ECO:0000250|UniProtKB:Q3V0F0}.
Interaction partners:
- Protein Hook homolog 1
- Regulating synaptic membrane exocytosis protein 2
- RIMS-binding protein 3C
- RIMS-binding protein 3B
- Kinesin-like protein KIF3B
Sequence:
MAKDSPSPLGASPKKPGCSSPAAAVLENQRRELEKLRAELEAERAGWRAERRRFAARERQLREEAERERRQLADRLRSKWEAQRSRELRQLQEEMQREREAEIRQLLRWKEAEQRQLQQLLHRERDGVVRQARELQRQLAEELVNRGHCSRPGASEVSAAQCRCRLQEVLAQLRWQTDGEQAARIRYLQAALEVERQLFLKYILAHFRGHPALSGSPDPQAVHSLEEPLPQTSSGSCHAPKPACQLGSLDSLSAEVGVRSRSLGLVSSACSSSPDGLLSTHASSLDCFAPACSRSLDSTRSLPKASKSEERPSSPDTSTPGSRRLSPPPSPLPPPPPPSAHRKLSNPRGGEGSESQPCEVLTPSPPGLGHHELIKLNWLLAKALWVLARRCYTLQAENKQLRRAGCPYQADEKVKRLKVKRAELTGLARRLADRARKLQETNLRAVSAPIPGESCAGLELCQVFARQRARDLSEQASAPLAKDKQIEELRQECHLLQARVASGPCSDLHTGRGGPCTQWLNVRDLDRLQRESQREVLRLQRQLMLQQGNGGAWPEAGGQSATCEEVRRQMLALERELDQRRRECQELGAQAAPARRRGEEAETQLQAALLKNAWLAEENGRLQAKTDWVRKVEAENSEVRGHLGRACQERDASGLIAEQLLQQAARGQDRQQQLQRDPQKALCDLHPSWKEIQALQCRPGHPPEQPWETSQMPESQVKGSRRPKFHARPEDYAVSQPNRDIQEKREASLEESPVALGESASVPQVSETVPASQPLSKKTSSQSNSSSEGSMWATVPSSPTLDRDTASEVDDLEPDSVSLALEMGGSAAPAAPKLKIFMAQYNYNPFEGPNDHPEGELPLTAGDYIYIFGDMDEDGFYEGELEDGRRGLVPSNFVEQIPDSYIPGCLPAKSPDLGPSQLPAGQDEALEEDSLLSGKAQGVVDRGLCQMVRVGSKTEVATEILDTKTEACQLGLLQSMGKQGLSRPLLGTKGVLRMAPMQLHLQNVTATSANITWVYSSHRHPHVVYLDDREHALTPAGVSCYTFQGLCPGTHYRARVEVRLPRDLLQVYWGTMSSTVTFDTLLAGPPYPPLDVLVERHASPGVLVVSWLPVTIDSAGSSNGVQVTGYAVYADGLKVCEVADATAGSTLLEFSQLQVPLTWQKVSVRTMSLCGESLDSVPAQIPEDFFMCHRWPETPPFSYTCGDPSTYRVTFPVCPQKLSLAPPSAKASPHNPGSCGEPQAKFLEAFFEEPPRRQSPVSNLGSEGECPSSGAGSQAQELAEAWEGCRKDLLFQKSPQNHRPPSVSDQPGEKENCSQHMGTSKSPAPGFIHLRTECGPRKEPCQEKAALERVLRQKQDAQGFTPPQLGASQQYASDFHNVLKEEQEALCLDLWGTERREERREPEPHSRQGQALGVKRGCQLHEPSSALCPAPSAKVIKMPRGGPQQLGTGANTPARVFVALSDYNPLVMSANLKAAEEELVFQKRQLLRVWGSQDTHDFYLSECNRQVGNIPGRLVAEMEVGTEQTDRRWRSPAQGNLPSVAHLEDFQGLTIPQGSSLVLQGNSKRLPLWTPKIMIAALDYDPGDGQMGGQGKGRLALRAGDVVMVYGPMDDQGFYYGELGGHRGLVPAHLLDHMSLHGH
Protein: ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (Q9BKU2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSGLAPDGLPKGNRVWADGCYDMVHFGHANQLRQAKQFGQKLIVGVHNDEEIRLHKGPPVFNEQERYRMVAGIKWVDEVVENAPYATTVETLDKYDCDFCVHGDDITLTADGKDTYQEVKDHQRYRECKRTCGVSTTDLVGRMLLLTKNHHTQDEHIEQHVERARSLSTDNVAMSPWTRVSRFIPTTTTILEFAEGRPPKPTDKVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGSNHPIMSIHERVLSVLAYKPVNEVVFGAPYEITSDILDQFNVQAVINGFRDNNSSVVNSSLASIDPFAEAKRRGIYHEVDSGSDMTTDLIIDRIIHHRLEYETRNKKKEKKEADVAKAMNLI
Protein: Tryptase beta-2 (Tryptase-2) (EC 3.4.21.59) (Mast cell protease 6) (mMCP-6) (P21845)
Organism: Mus musculus (Mouse)
Function: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Plays a role in innate immunity.
Subcellular location: Secreted {ECO:0000250}. Note=Released from the secretory granules upon mast cell activation. {ECO:0000250}.
Interaction partners:
- Tryptase
- Mast cell protease 4
- Mast cell carboxypeptidase A
- Chymase
- High affinity immunoglobulin epsilon receptor subunit alpha
Sequence:
MLKRRLLLLWALSLLASLVYSAPRPANQRVGIVGGHEASESKWPWQVSLRFKLNYWIHFCGGSLIHPQWVLTAAHCVGPHIKSPQLFRVQLREQYLYYGDQLLSLNRIVVHPHYYTAEGGADVALLELEVPVNVSTHIHPISLPPASETFPPGTSCWVTGWGDIDNDEPLPPPYPLKQVKVPIVENSLCDRKYHTGLYTGDDFPIVHDGMLCAGNTRRDSCQGDSGGPLVCKVKGTWLQAGVVSWGEGCAQPNKPGIYTRVTYYLDWIHRYVPEHS
Protein: Glutamate--cysteine ligase catalytic subunit (EC 6.3.2.2) (GCS heavy chain) (Gamma-ECS) (Gamma-glutamylcysteine synthetase) (P97494)
Organism: Mus musculus (Mouse)
Function: Catalyzes the ATP-dependent ligation of L-glutamate and L-cysteine and participates in the first and rate-limiting step in glutathione biosynthesis.
Interaction partners:
- Glutamate--cysteine ligase regulatory subunit
- Glutathione synthetase
- Glutathione hydrolase 6
- Glutathione hydrolase 1 proenzyme
- Glutathione hydrolase 7
- Gamma-glutamylcyclotransferase
- Glutathione hydrolase 5 proenzyme
- Aminopeptidase N
- 5-oxoprolinase
- Nuclear factor erythroid 2-related factor 2
Sequence:
MGLLSQGSPLSWEETQRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDHENRKVQLLLNGGDVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTVEANMRKRRKEATSVLGEHQALCTITSFPRLGCPGFTLPEHRPNPEEGGASKSLFFPDEAINKHPRFGTLTRNIRHRRGEKVVINVPIFKDKNTPSPFVETFPEDAEASKASQPDHIYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLEPLKNNRFRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLEEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDIGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVLQGMFYFRKDICKGGNAVVDGCSKAQSSSEPAAEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEINYSLIWKCNQIADELCECPELLGSGFRKAKYSGGKSDPSA
Protein: G1/S-specific cyclin CLN3 (Q5A1N6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: G1/S-specific cyclin essential for the control of the cell cycle at the G1/S (start) transition. CLN3 may be an upstream activator of the G1 cyclins which directly catalyze start. Required for budding and for cell cycle progression and morphogenesis in environment-induced hyphae. Degradation is mediated by GRR1. Through binding to CDC28, controls the phosphorylation of SLA1 which regulates cortical actin patch dynamics.
Interaction partners:
- Cyclin-dependent kinase 1
- Transcription factor MBP1
- Transcription factor MBP1
- Transcriptional regulator
- Nucleoporin NSP1
- Rme1p
- Negative regulator of the PHO system
- Hypha-specific G1 cyclin-related protein 1
- Ubiquitin-protein transferase activating protein
- mRNA-binding protein
Sequence:
MFPNSPDAFHQVRMMQSSIKASNFKLQSMEFRCHSNNVCEYQMEMLHHLLSVEAKTLPNLSLIEQQPEIKLGMRPLLLDFLMEVITILSLSRSTFPLTVNLIDRYCSTRIVKKQHYQLLGLTSLWISCKNLDSKFKVPTLNDLRKICVDSYYKELFVEMEKHILKSLEWVVNAPTFDAFIDLYSNLLISNSSNFEVANIIKKSSHKIKLFSNYIGELFQFYPNIYYDYTSSQIALIAILITVLTLKIPVDLISLLNFYNGLVKTEMFKSNVEQGAEDQFEEILSVDSFKSLFNKSFFKNLIKIIDNPPSSLKIKYFAENGKYSVLMKQLVTTASNTLKCILDPVPTTPKANSFVKHQQQQHHYHPRPPMSINTSMIPLTPVSNSTSPNRFSPDQIFSENESTPGIAFGTMTPDSQSTSPGEKRSYECIDELEIGTSTIAGYTLKNHDTLKRSKSANYGTLFYLQQ
Protein: NAD-specific glutamate dehydrogenase (EC 1.4.1.2) (A0A1D8PI00)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Glutamate synthase
- Glutamate dehydrogenase
- Multifunctional fusion protein
- Glutamine synthetase
- Transaminase A
- 2-oxoglutarate dehydrogenase, mitochondrial
- Aspartate aminotransferase
- Malate dehydrogenase, cytoplasmic
- Glutamate decarboxylase
- Citrate synthase
Sequence:
MTSASLENGVSRLNIYRTTSNTSSQVSLKHDYIDSPFSGKKDQFDQVLDVLDSTGFIPESLIESEAKWFYESLGIDDVFFARSSPEDIASHIHALYSCKVQAYSSFGEQPLISYKREAEDHAVFFDTVDAESYKRNQFEERIDDKYIDPSSTTTNSYRTEYFSAPLNYQSDPILSGVYQQNKELRDQYVRLFFVYKNNYTISEAAANETDLEKIGDKTFLKIASDNTKQLYTSIVKDVINTTGPVIKHFPLEDSEEYRVVIGYKQKTSARYNSALSDLANYYKLQVTRKYVEQFSNGVTIISMYVTSKSRKSPVDLSIYQVIKEASLLYCIPHNYFHDRFIQGELSLQESIYAQSGVIFVTHFLNRLGPEYNKLSSLLDPSKSIEHAEVLNSLKKRLRAETYTQDYIKEVFDNRRDIVRKLYRQFADVHYIRSSMEKTLSYQRLSQITPVGSEEEFEQLLSRECSQNEHHAIVLRALYTFNKSILKTNFYTSTKVALSFRLNPSFLPESEYPERPYGMFFVVGSDFRGFHIRFRDIARGGIRIVRSRSLDAYNVNARNLFDENYNLANTQQRKNKDIPEGGSKGVILLDPGAAQERPQACFEKYIDALIDLLLKQNIPGVKDNYVDLYAKPEILFLGPDEGTAGYVDWATLHARERGAPWWKSFLTGKSPELGGIPHDEYGMTTLSVRAYVNKIYEKLDIDDAKIRKFQTGGPDGDLGSNEILLSRKENYVGIVDGSGVICDPQGLDKQELIRLAKERKMIEHYDKTKLSPQGYVVLVDDMDVKLPSGEVVTSGVAFRNTFHLKLKQQFGVDGVDLFVPCGGRPAAIDTNNVHDLIDEKTGKSVVPYFVEGANLFITQSAKLILEKAGIVIFKDASTNKGGVTSSSLEVLASLSFDDKGFLENMCVDPETKAKPQFYQDYVKDVQKIIVGNADSEFEALWKLKAETGTPFTILSDKLSVAINKLGDELANSKELWNDDIEFRNAVLLDSLPPLLLEKVGIENVLSRVPEAYLKAIFATHLASKFVYSRGIDSNPAKFLEFISSIRKDFIQKGLLKY
Protein: GEO02306p1 (Q8MLV4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRSCTLLVFIVSTLLFAVTNAQQNYDGRNGPHEFGTPGNGIYIRGQNEGPYTVPEMGGTFQNSPSSGQHSYTDEHGNTYTHSSTATVTSLAYSTFGFSMGGVLIFLISLITI
Protein: Cytokinin dehydrogenase 2 (EC 1.5.99.12) (Cytokinin oxidase 2) (AtCKX2) (CKO 2) (Q9FUJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group. Modulates asymmetric cytokinin signaling in emerged lateral roots. Its activity determines cell elongation and number in emerged lateral roots and defines angular growth of lateral roots.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:14555694}. Secreted, extracellular space {ECO:0000269|PubMed:14555694}.
Interaction partners:
- Adenylate isopentenyltransferase 4
- Histidine kinase 3
- Histidine kinase 2
- Histidine kinase 4
- Adenylate isopentenyltransferase 8, chloroplastic
- Adenylate isopentenyltransferase 1, chloroplastic
- Adenylate isopentenyltransferase 5, chloroplastic
- Probable WRKY transcription factor 10
- Cytokinin hydroxylase
Sequence:
MANLRLMITLITVLMITKSSNGIKIDLPKSLNLTLSTDPSIISAASHDFGNITTVTPGGVICPSSTADISRLLQYAANGKSTFQVAARGQGHSLNGQASVSGGVIVNMTCITDVVVSKDKKYADVAAGTLWVDVLKKTAEKGVSPVSWTDYLHITVGGTLSNGGIGGQVFRNGPLVSNVLELDVITGKGEMLTCSRQLNPELFYGVLGGLGQFGIITRARIVLDHAPKRAKWFRMLYSDFTTFTKDQERLISMANDIGVDYLEGQIFLSNGVVDTSFFPPSDQSKVADLVKQHGIIYVLEVAKYYDDPNLPIISKVIDTLTKTLSYLPGFISMHDVAYFDFLNRVHVEENKLRSLGLWELPHPWLNLYVPKSRILDFHNGVVKDILLKQKSASGLALLYPTNRNKWDNRMSAMIPEIDEDVIYIIGLLQSATPKDLPEVESVNEKIIRFCKDSGIKIKQYLMHYTSKEDWIEHFGSKWDDFSKRKDLFDPKKLLSPGQDIF