wanglab/gogpt-training-data huggingface dataset:
Protein: Mirror, isoform C (M9PI45)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Lysyl oxidase-like
Sequence:
MTVHSNETGICLVMNAVSTHLATSSPNTPPTNAPQSPPSTLPTLACPAAQPLSAPGIAGPGHSGMVTSTVPPGARSTSPCGPSAGLPALSLVGAPPPGPHSSAPGGAPAPGAGNPPNRCCDTGRTIYTDPVSGQTICSCQYDMLNYQRLAAAGGVPLGVYPEGMSAYLSGIAADQPPFYANPAGIDLKENLVAGASPWPYPSMYHPYDAAFAGYPFNSYGMDLNGARRKNATRETTSTLKAWLNEHKKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWEPRNRVDDDDANIDDDDDKNTEDNDLLDAKDSGVGSTDDKDRSGRLGDMMTDRPGESNNSEWSESRPGSPNGSPDLYDRPGSMPPGAHPLFHPAALHHHFRPPAGSPPDIAAYHHHQQQLLQQHQQAQQNSLQTAVGGTAKPRIWSLADMASKDSKDSSSGAKDNHPELPPAHPGFYGHPGQQPSPGKILSPLAARIPNYSPYVRPDLYRGFYGPAAAHLGAPTQEFLEHQRTFGASLAAHNGPLGMNPLLWKAAVSGAANGHHFAPLSLTTSGGSSGGQQVAPPPVASPSASSSSSSMGCDVVHIPTSSGQSAAQHMMGPISSNSTASSSSSHSGKISPGVNVTSLSAKPXHPSAASPDPELGAAPIASPISAFRSLIAFREQQKLTLLRP
Protein: Fer-related kinase 1 (EC 2.7.10.2) (Fer oncogene-related kinase 1) (Q22146)
Organism: Caenorhabditis elegans
Function: Non-receptor tyrosine-protein kinase which plays a role in morphogenesis by regulating the epidermal enclosure of the embryo, independently of its kinase activity. Prevents hyperactivation of the Wnt signaling pathway during endoderm development, probably by preventing hmp-2 nuclear translocation.
Subcellular location: Nucleus {ECO:0000269|PubMed:15958510}. Cytoplasm {ECO:0000269|PubMed:15958510}. Cell junction {ECO:0000269|PubMed:15958510}. Cell membrane {ECO:0000269|PubMed:15958510}; Peripheral membrane protein {ECO:0000269|PubMed:15958510}. Note=Localizes to the nucleus during cell division in the early embryo and in seam cells and in the developing germline at the larval stage. Localizes in the cytoplasm and at the cell-cell contacts during embryo enclosure and elongation. Nuclear exclusion during elongation is regulated by integrin alpha subunit pat-3 and beta-catenin hmp-2. {ECO:0000269|PubMed:15958510}.
Interaction partners:
- Armadillo repeat-containing protein wrm-1
- Juxtamembrane domain-associated catenin
- Protein ver-2
Sequence:
MGTVEKSSNNDASVTDDIRSAEYYHGMVPRQDAEGFLKREGDFLVRKTEQMPGKVVLAMSVRVTDELCRHFMLNMDPTSNKFYFEHTHQESTISELINWHMTTKTPISAASGAKIRRPMERSPWLINHDSIVANKKLGEGAFGDVFIAELDQGGKQEVAVKTMRAEATREARLRFMKEARLMRKYQHKHVVKLIGVAIHEHPLMIVMEYCPNGSLLSHLKKNKVSLIEKLRFTTEAADGIAYLERSKCIHRDIAARNCLLSAKNELKISDFGMSDNKDEIKDETLEKVPIKWLAPETMQEKVYTHKTDIWTFGVLVWEIYSDGAEPYPGLTKIQTRAKIVVNDYRMKMPDGTHPTVADVVTGTCWQKNPEKRSTMDSIHKKLREFYESKK
Protein: holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) (Q59N08)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Dephospho-CoA kinase
- Holo-[acyl-carrier-protein] synthase
- Saccharopine dehydrogenase [NAD
- Alpha-aminoadipate reductase
- [acyl-carrier-protein] S-malonyltransferase
- Acyl carrier protein
- Homoaconitase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase
Sequence:
MTLQDHLNDKSNIILLFTTRLTNELIEFWNDDYNFECSLRLLNDLSLQQKISSITKNPNHQQQRFKYKQLLSNLFIRYAINSIIQSNDLFKKIEFDYNEFGKPILPYNFQFNISSSNDIIALIVEFPSSSSLSSSSLSSSLSGDRAYDPIGIDLSHSIQNSISNTEYLEQFKPIFDDVYELPQIDNYFKFNHFWTLKESFTKLIGSGLNIELSDFYFIVDYNDNEFSSDNEKFQTSIVGNNIGDSWMYYSLNWFDKILINIDKLELAKNQFITALNKKEFYCRSSILDNGNVDESKLPVIITIINQNKNKSIQPIELRFEKLLSEHLNQ
Protein: Neurosecretory protein VGF [Cleaved into: Neuroendocrine regulatory peptide-1 (NERP-1); Neuroendocrine regulatory peptide-2 (NERP-2); VGF-derived peptide TLQP-21; VGF-derived peptide TLQP-62] (Q0VGU4)
Organism: Mus musculus (Mouse)
Function: Secreted polyprotein that is packaged and proteolytically processed by prohormone convertases PCSK1 and PCSK2 in a cell-type-specific manner (By similarity). VGF and peptides derived from its processing play many roles in neurogenesis and neuroplasticity associated with learning, memory, depression and chronic pain.
Subcellular location: [Neurosecretory protein VGF]: Secreted {ECO:0000250|UniProtKB:O15240}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:O15240}. Note=Stored in secretory vesicles and then secreted, NERP peptides colocalize with vasopressin in the storage granules of hypothalamus. {ECO:0000250|UniProtKB:O15240}.
Interaction partners:
- Secretogranin-2
Sequence:
MKTFTLPASVLFCFLLLIQGLGAAPPGRPDVFPPPLSSEHNGQVAEDAVSRPKDDGVPEVRAARNPEPQDQGELFQGVDPRALASVLLQALDRPASPPSVPGGSQQGTPEEAAEALLTESVRSQTHSLPAPEIQAPAVAPPRPQTQDRDPEEDDRSEELEALASLLQELRDFSPSNAKRQQETAAAETETRTHTLTRVNLESPGPERVWRASWGEFQARVPERAPLPPPVPSQFQARMSESAPLPETHQFGEGVSSPKTHLGETLTPLSKAYQSLGGPFPKVRRLEGSFLGGSEAGERLLQQGLAQVEAGRRQAEATRQAAAQEERLADLASDLLLQYLLQGGARQRDLGGRELQETQQERENEREEEAEQERRGGGEDDVGEEDEEAAEAEAEAEEAERARQNALLFAEEEDGEAGAEDKRSQEEAPGHRRKDAEGAEEGGEEDDDDEEMDPQTIDSLIELSTKLHLPADDVVSIIEEVEEKRKRKKNAPPEPVPPPRAAPAPTHVRSPQPPPPAPARDELPDWNEVLPPWDREEDEVFPPGPYHPFPNYIRPRTLQPPASSRRRHFHHALPPARHHPDLEAQARRAQEEADAEERRLQEQEELENYIEHVLLHRP
Protein: Protein SYS1 (P41544)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Necessary for the targeting of ARL3 to the Golgi. Involved in protein trafficking. May serve as a receptor for acetylated ARL3.
Subcellular location: Golgi apparatus membrane; Multi-pass membrane protein.
Interaction partners:
- ADP-ribosylation factor-like protein 3
- GTP-binding protein YPT6
- Protein transport protein SEC24
- Conserved oligomeric Golgi complex subunit 6
- Golgin IMH1
- ADP-ribosylation factor-like protein 1
- Conserved oligomeric Golgi complex subunit 5
- GRIP domain-containing protein RUD3
- Conserved oligomeric Golgi complex subunit 8
- GTPase-activating protein GYP1
Sequence:
MVSIRRYLRVPNELKPSQIFKQDSLSPSKIGLQIVLLQIFYYTTAIVLFYCWAKLAGYDLNIKEWLFSWENIDFTNAYGLSISLLWLLDSLICVFFLTVIVGRSKLAWDFAITIHAINFIVVFLYTRKFPSFSWFFLQILSSLILIFLGTWTTRWRELRDTFFEGLVDPNEGEVGLVTPSQQHSNHSELEQSPIQLKDLESQI
Protein: Myosin binding subunit, isoform L (M9NDA1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSLDARNNSAMMKRAEQLKRWEESDTNRAAPTPRHEHGRRIKFSSGCVFLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAIDVQHMAMIDYMEKMVQELNINVDEARKAEELAMLNDAKKWLRSDAAEVDRPHPKTGATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVADRKIVKFLEELRANKRNKRRPSSQIRISDAMENHVEKTPTKLVRVEVRTDATKDAENVKPNQQIHAVEHPVEEEAPWRRKLPRTPSDSPTNNQVPDRELGTNSSETANDVILRRTQSFENDQKFYQKYNELRARIKANSCPILPANANANAAAANKSNNNNNLSSNNYHNNNNNNNKSDLLLGYAAGTTTTTSTPTTTTTTTSSTFNNTHSNTNNTSTTQQQPAAAAAASAANQLYSVQRSASLKDNSMYYRKPTVTIATSTAATAINSPSTTVQTPPIRRSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEELVKKKNMGMANNNNNNNISTTTTNTISNSGNETSSASSTSAPTPSILGSNEQQDELQPPPPPTTPPPAVIPTTTTATDETEIEEVVSSPPAGQSQNDTTASFTLSAPVRRSLSTEGEADANSDPEGDQDQTVVSASYTIMPRRERLPESSENVESIRSPQKTEPVAKSSSEDKSEEPPHARPTDLPLIPAPAAPSTEAIKSSSAATTPAALESPVRLRDKRGLSGSQESETKSDTASPVSSHPDFNARDSLLSLYARRTTDSSAGGGGVGGGAGVGAGGASGAATSSSTSAAERRPSWRLKFDAGSKFKLEDITSGGTYPPNNSTIIPSAPAVMAAANLSTTTGVQRRISSGPIALNASNQSLNSVGRPVSAPSEGTNNSAYVTPSARKFETNATSTGATTAATTTSNSTSNSVSATSANHTTATAPNATSNHDDKDNDKENDNRTQTVIQRRRKPKRRSTGVVHIDMDELDPERQNESSNNDNEEKEKESGSERTSRSRLGSTASTATTSESKSSSSNDKTENGDGIDYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFANATTKNSLSELEKRERRAMERKLSELEEELKQLDAYKSDNHRLKEENAALIRVISKLSK
Protein: tRNA pseudouridine synthase 1 (EC 5.4.99.-) (tRNA pseudouridylate synthase 1) (tRNA-uridine isomerase 1) (O94396)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr). Catalyzes pseudouridylation at position 44 in U2 snRNA (By similarity). Also catalyzes pseudouridylation of mRNAs (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11095668}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit cbf5
- Multisubstrate pseudouridine synthase 7
- tRNA
Sequence:
MGRGGKRTWYNGDRREAKRNRPNSIYNGEGRPENLVVGEKKPKRKVACLVGYCGSGYHGMQLNPPSKTIEGDLFDAFVKAGAVSSYNADDPKKVALARAARTDKGVHAAGNVISLKLIMEDEKLIEKVNEHLPPSIRLWDVIRTINSFNPRTYCESRIYEYMVPTYAFVPPKPSSILGNCIMKNSPMPAEPINKENINQLSRSLFYEEGKEFWDDYDIAAKEILSLYEQDPEGFVNPYSKRGAAALANSENNKGSEAGVSAKTNPDMDSDSSAIVNEFLKPDSVEDESAGSKIDPSYRLERALKHIEVLKLKNYRISADRLSVIRETLNQYVGVHNFHNFTVGQAFHQKNSNRVIRSFTASDPFMIGDTEWISCKVHGQSFMLHQIRKMIALAILVVRTGCPVERIQDAFKKTKINIPKGPGFGLLLESPFFKGYNEHKAPENNRDPIDFTKYEQKITAFKHAHIYDKIFLEEARKQVFHCFLSFIDSYNEEDFSYLSDIGITEKTQEVSSKLPDVLSSDEEEDSAENKDDLEG
Protein: Isocitrate lyase (ICL) (EC 4.1.3.1) (Isocitrase) (Isocitratase) (D4GTL3)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.
Interaction partners:
- Malate synthase
- Citrate synthase
- Aconitate hydratase
- Pyridoxal phosphate-dependent aminotransferase
- Aconitate hydratase
- 2-dehydro-3-deoxy-phosphogluconate aldolase, bacterial-type
- Uncharacterized protein
- acetate--CoA ligase
- Acyl-CoA synthetase
- Acetate--CoA ligase
Sequence:
MNPTELDSDVFAQDVDNQKARELREMLNTQDFVFAPGMYHALDARLAEMTGHDAAYMSGYSTVLGQFGFPDLEMVTMTEMVENAKRMVEATNLPVIADCDTGYGGIHNVRRAVREYEKAGVAAVHIEDQTTPKRCGHIAGKQIVSREKAKARFEAAVDAKQSEDTVVIARTDAYGSSNGDWDEHVERGRIYADAGVDIVWPEMPNPSREDAVAYAEEIHETHPDLKLAFNYSSSFAWSEEEDPLTFQELGDLGYKYIFITLFGLHSGAHAVYEDFKKLAEQDEEGQFDLEQRYLDHPTESHHELSFVSRYQDIETEFDPEARRRIEESEGFSEEQADPITSNDDD
Protein: Stretchin-MLCK (Q9NBC1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GLPLDSYSDTSYFRDPPGCISTEPLVVDSGPTHISLSWGKPVSANSAPVMAYKVEAWVVGHEGGAYWRELGLTPINSFDAFNLKPNVEYHFRVTPKNRYGWGPTVQTSSPLQVGGVECLPEFVKILPGQAKALLGSSFTLQCNMRGAPRPQVTWFKDGIQLSSSSERVKIRQIGSTCALTIATVSELDSGRYTCEATNSKGR
Protein: Eukaryotic peptide chain release factor subunit 1 (Eukaryotic release factor 1) (eRF1) (Q9NAX8)
Organism: Trypanosoma brucei brucei
Function: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MTDHELSESEKAIERYKVKKLIQMLESARGMGTSVISIYMTPKEQISGMVTKLNNEYGTASNIKSHTNKLSVQSAITASLGRLKQYNRLPPNGLLLYCGTVLTAENKEKKLTLDIEPFKPVSRSLYLCDNKFHTEELHRMLESDEKFGFIVVDGSGTTYATLCGSVKEKLSSFTVELPKKHGRGGQSKNRFARIRMERRHNYLRKVAEGATQLFITNDRPNIVGLVLAGSAEFKEVLYQSDLFDPRLKAIVVKVVDVAHPGDVGLNQAIDLAADALSGVKLVQEKKLLQGFFDQIACDTQLYCFGVQDTLKCLEAGAVETLIVYEDLNIYRYTVVKNRGADDEETFVHVMSEEEAKRSNIHMQESGKTRNEIEQEDFVDWLATNYRKFGCALELITNRSQEGTQFVRGFGGIGGVLRYKLDIIALRDVEKKEDDEERIAANNEEFDFDDDFM
Protein: Histone-lysine N-methyltransferase ATXR2 (EC 2.1.1.-) (Protein SET DOMAIN GROUP 36) (Trithorax-related protein 2) (TRX-related protein 2) (Q5PP37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase that methylates 'Lys-36' (H3K36me) of histone H3 to produce H3K36me3. Promotes early stages of cellular dedifferentiation through H3K36me3-dependent, and to a lesser degree H3K4me3-dependent, activation of Lateral organ Boundaries-Domain (LBD) (e.g. LBD16 and LBD29) genes. Positive regulator of root organogenesis including lateral root formation as well as adventitious root formation from wounded leaf tissues. Recruited by JMJ30/ARF (e.g. ARF7 and ARF19) complexes to promote the deposition of H3K36me3 and, to a lower extent, H3K4me3 at LBD genes promoters, thus ensuring their stable activation during callus formation on callus-inducing medium (CIM).
Subcellular location: Nucleus {ECO:0000269|PubMed:29184030}.
Interaction partners:
- Auxin response factor 19
- Auxin response factor 7
- Enhancer of polycomb-like protein
- Histone-lysine N-methyltransferase ASHR2
- Enhancer of polycomb-like protein
- Enhancer of polycomb-like protein
- Lysine-specific demethylase JMJ30
- LOB domain-containing protein 29
- LOB domain-containing protein 16
- Histone acetyltransferase GCN5
Sequence:
MDSVYKTDENFAADVAALLAPLPTPQLQEYFNKLITSRRCNGIEVKNNGTIGKGVYANSEFDEDELILKDEILVGIQHSSNKVDCLVCSFCFRFIGSIEKQIGRKLYFKNLGVSGCCDDDSSEEDECVKYNGNEEQCGGSSSSHNTLPEGVVSSLMNGEMALPHTDKFPLPSPLSCPGGCQEAFYCSESCAAADWESSHSLLCTGERSESISREALGEFIKHANDTNDIFLLAAKAIAFTILRYRKLKAEHVDKKAKQSEPKQSLLLEAWKPVSIGYKRRWWDCIALPDDVDPTDEGAFRMQIKNLACTSLELLKIAIFDKECEALFSLEIYGNIIGMFELNNLDLVVASPVEDYFLYIDDLPDAEKEETEEITRPFLDALGDEYSDCCQGTAFFPLQSCMNHSCCPNAKAFKREEDRDGQAVIIALRRISKNEEVTISYIDEELPYKERQALLADYGFSCKCSKCLEDSSSI
Protein: MAGUK p55 subfamily member 5 (Q17549)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEYIAATSGPPSVAPRGSVHTNGFGIERGSLRRPPEQFEMQEKKRKEQENTFLRSSLRKSKKLQALARNVDPLTNEPMKVTSFANPLAEVEETPSRKTENGATRITVGEEVLESSEVLIDEENKDSRQLDEVIISVERIASKLSSMQGRESDVAMLRDFFAAPPIQAAIEQTVKQNGKCGTTSSGIGTDSGGDSSSCTSSPIPPVIMNGNGKSERCPSTSSSSSVSPRNAPNVKVVEVVKDEDSYLGATVRNENNKIIVGRVVKGGIVEKMNLFQEGDELLELNGSSLKGKQVNEICDILRNLSGPITFVVAPKEEQDTEQPTDTATNTVTAKKSQQHVQHLRALFDYDPEDDVYVPCKELAMKFQRGDILHVLNTKDDNWWQAYRDGEDIQHSLAGLIPSSSFRQQVVLYADEVEREQEQKRKECKGKKKKKLEVKKGADEENLPAIGVYSDFLTYEEVVLELPKATHRRPIVLCGAEGVGCLKLRDRLLESDRITLACPVPYTSRTPKEGEFNGVHYHFVSKQKFHEDAKSGKFVEFGEYQKFWYGTAKKDVVNVIERGKTCVMTLKAESLGAIRSPDIQPYIIFIAAPSLYILRRQREVEGTFGVKDDELKAILTQSKSIEQKYGHLFDGIIVNIDFEKSFRELKQILMKVNTEPMWVPATWTAC
Protein: Integrin alpha-1 (CD49 antigen-like family member A) (Laminin and collagen receptor) (VLA-1) (CD antigen CD49a) (P56199)
Organism: Homo sapiens (Human)
Function: Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin beta-1
- Integrin beta-3
- Integrin beta-5
- Integrin beta-2
- Integrin beta-6
- Integrin alpha-2
- Integrin beta-8
- Integrin alpha-3
- Integrin alpha-10
- Integrin beta-7
Sequence:
MAPRPRARPGVAVACCWLLTVVLRCCVSFNVDVKNSMTFSGPVEDMFGYTVQQYENEEGKWVLIGSPLVGQPKNRTGDVYKCPVGRGESLPCVKLDLPVNTSIPNVTEVKENMTFGSTLVTNPNGGFLACGPLYAYRCGHLHYTTGICSDVSPTFQVVNSIAPVQECSTQLDIVIVLDGSNSIYPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTMTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRGNLSTEKFVEEIKSIASEPTEKHFFNVSDELALVTIVKTLGERIFALEATADQSAASFEMEMSQTGFSAHYSQDWVMLGAVGAYDWNGTVVMQKASQIIIPRNTTFNVESTKKNEPLASYLGYTVNSATASSGDVLYIAGQPRYNHTGQVIIYRMEDGNIKILQTLSGEQIGSYFGSILTTTDIDKDSNTDILLVGAPMYMGTEKEEQGKVYVYALNQTRFEYQMSLEPIKQTCCSSRQHNSCTTENKNEPCGARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHGGAVYIYHGSGKTIRKEYAQRIPSGGDGKTLKFFGQSIHGEMDLNGDGLTDVTIGGLGGAALFWSRDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSKEDTIYEADLQYRVTLDSLRQISRSFFSGTQERKVQRNITVRKSECTKHSFYMLDKHDFQDSVRITLDFNLTDPENGPVLDDSLPNSVHEYIPFAKDCGNKEKCISDLSLHVATTEKDLLIVRSQNDKFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKDSCESNHNITCKVGYPFLRRGEMVTFKILFQFNTSYLMENVTIYLSATSDSEEPPETLSDNVVNISIPVKYEVGLQFYSSASEYHISIAANETVPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSENANCRPHIFEDPFSINSGKKMTTSTDHLKRGTILDCNTCKFATITCNLTSSDISQVNVSLILWKPTFIKSYFSSLNLTIRGELRSENASLVLSSSNQKRELAIQISKDGLPGRVPLWVILLSAFAGLLLLMLLILALWKIGFFKRPLKKKMEK
Protein: G domain-containing protein (Q57XB3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSKHVVGNVFAATAVLRCGRFVSGTRLGCSSGKIIIPTLPTSGVVERNLGSFSSTSALGRGSSEYYENKRMDPAVGQFLGGDASATLRRQQQLEHFRNATEDAAVRIWRDSKSHIRRQEKLVQDIGVEGAVRELLQPTQISFRQELRQRPLDRGILEEIYKGLHGRRIERQLKRGVSWEHWITKGDGTAPVFTASRKAQQTFAFGGNIKLVAKATHPKQFPVMAMGGGYESSNGVFAMGESQRLVPEVAFVGRTSSGKSSLVNAIVNAMVAPYGHLQGTTSSVNFYNIADKIVLVDCPGYGYYNPMETPHLDAENAVASMRAYLTSCSRCVDEKQAVAGTGRINIAERAAKDKAAKHGNRSRIRAPGVPRPIKRVFVCVSARGMQHSDLAYLDHLETLSLPFSVVLTKTDAAPIRFLARLADHTRCQLVHYKNCKELLLTSSLRLAGIDKMQSLIGSMALGEDKLHGATTDFSAIV
Protein: Synaptotagmin-13 (Synaptotagmin XIII) (SytXIII) (Q7L8C5)
Organism: Homo sapiens (Human)
Function: May be involved in transport vesicle docking to the plasma membrane.
Subcellular location: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Neurexin-1
Sequence:
MVLSVPVIALGATLGTATSILALCGVTCLCRHMHPKKGLLPRDQDPDLEKAKPSLLGSAQQFNVKKSTEPVQPRALLKFPDIYGPRPAVTAPEVINYADYSLRSTEEPTAPASPQPPNDSRLKRQVTEELFILPQNGVVEDVCVMETWNPEKAASWNQAPKLHYCLDYDCQKAELFVTRLEAVTSNHDGGCDCYVQGSVANRTGSVEAQTALKKRQLHTTWEEGLVLPLAEEELPTATLTLTLRTCDRFSRHSVAGELRLGLDGTSVPLGAAQWGELKTSAKEPSAGAGEVLLSISYLPAANRLLVVLIKAKNLHSNQSKELLGKDVSVKVTLKHQARKLKKKQTKRAKHKINPVWNEMIMFELPDDLLQASSVELEVLGQDDSGQSCALGHCSLGLHTSGSERSHWEEMLKNPRRQIAMWHQLHL
Protein: 12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase (EC 2.5.1.110) (Fumitremorgin biosynthesis protein H) (Q4WAX1)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: 12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Interaction partners:
- Fumitremorgin C monooxygenase
- Verruculogen synthase
Sequence:
MTIPTEISCPEEDAFQLLDKFSWFPSDDQRRWWEYTGPYLLKLLRDAKYPQKDQVPCLYLLQQLLVPYLGTFPVVGQAPLPWWSNVTTYGVPFELSWNLLHNIVRIGFEPLSHLAESGVDAFNKTAPEECVSRLACLDNTIDLARFRHFQHHLLVTPEEETWLLKEKAPLAKSGRGQQTLAVEFQNGGISAKAYFFPGMKSLATGLSPGKLILDSIERLALPGLKEPVHHLRSTLGLQDDGHPTDTAIAPFLLGVDLCTPERSRLKFYVTDQVVSWDRVADMWTLRGKRLEDPQCADGLALLRKLWDLLAIPEGYRSNIRPDFAFGTPPPEDYRPVMMANWTLSPKKKFPDPQIYLLTVGMNDAVVMDALVAFYEVLGWTDLASTYKDKVASYFPGPDFTKTNYIHSGVSFSYRHSKPYLSVYYSPF
Protein: Thioredoxin-like protein CXXS1 (AtCXXS1) (Mono-cysteine thioredoxin 1) (Q8LDI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses low disulfide reductase activity, but efficient protein disulfide isomerase activity. Does not possess deglutathionylation activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18384502}.
Interaction partners:
- Thioredoxin-like 1-2, chloroplastic
- Chaperone protein dnaJ 13
- Glutaredoxin-C11
Sequence:
MARVVKIDSAESWNFYVSQAKNQNCPIVAHFTALWCIPSVFMNSFFEELAFNYKDALFLIVDVDEVKEVASQLEVKAMPTFLFLKDGNAMDKLVGANPDEIKKRVDGFVQSSRVVHIA
Protein: Reticulon (Q4G5V9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU210713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU210713}.
Interaction partners:
Sequence:
MHANSDNTTSMTTSGMEIKHWKEQVVELLYWRDLQRTGVVFGAGLFLLLSLSMCSIISVLSYVALALLSVTVSFRIYKGILQAVQKSEDGHPFKMYLDKDTALPAEMVHKYSDSTLVHINTVIKELRRLFLVEDLVDSLKFAVLMWILTYVGALFNGLTLIILGFIGAFSCPVIYEKHQAQIDHYYGLVNKQFKDVVGKIQAKIPGAKPKTE
Protein: Nucleoside diphosphate kinase homolog 5 (NDK-H 5) (NDP kinase homolog 5) (3'-5' exonuclease NME5) (EC 3.1.-.-) (Inhibitor of p53-induced apoptosis-beta) (IPIA-beta) (Testis-specific nm23 homolog) (nm23-H5) (P56597)
Organism: Homo sapiens (Human)
Function: Does not seem to have NDK kinase activity. Confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. May play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q99MH5}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q99MH5}.
Interaction partners:
- DPY30 domain-containing protein 2
- DPY30 domain-containing protein 1
- UMP-CMP kinase
- Adenylate kinase isoenzyme 1
Sequence:
MEISMPPPQIYVEKTLAIIKPDIVDKEEEIQDIILRSGFTIVQRRKLRLSPEQCSNFYVEKYGKMFFPNLTAYMSSGPLVAMILARHKAISYWLELLGPNNSLVAKETHPDSLRAIYGTDDLRNALHGSNDFAAAEREIRFMFPEVIVEPIPIGQAAKDYLNLHIMPTLLEGLTELCKQKPADPLIWLADWLLKNNPNKPKLCHHPIVEEPY
Protein: Bifunctional protein Rv2228c [Includes: Ribonuclease H (EC 3.1.26.4); Adenosylcobalamin/alpha-ribazole phosphatase (EC 3.1.3.73)] (P9WLH5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Endonuclease that displays both RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. As the only authenticated RNase HI in M.tuberculosis, probably plays an important role in the physiology of this organism, being likely involved in bacterial replication.
Interaction partners:
- Uncharacterized protein Rv2229c
- GTP cyclohydrolase 1 type 2 homolog
- Adenosylcobinamide-GDP ribazoletransferase
- Histidinol-phosphate aminotransferase Rv2231c
- Ribonuclease HII
- Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase
- DNA polymerase I
- Single-stranded DNA-binding protein
- Single-stranded DNA-binding protein
- Low molecular weight protein-tyrosine phosphatase A
Sequence:
MKVVIEADGGSRGNPGPAGYGAVVWTADHSTVLAESKQAIGRATNNVAEYRGLIAGLDDAVKLGATEAAVLMDSKLVVEQMSGRWKVKHPDLLKLYVQAQALASQFRRINYEWVPRARNTYADRLANDAMDAAAQSAAADADPAKIVATESPTSPGWTGARGTPTRLLLLRHGQTELSEQRRYSGRGNPGLNEVGWRQVGAAAGYLARRGGIAAVVSSPLQRAYDTAVTAARALALDVVVDDDLVETDFGAWEGLTFAEAAERDPELHRRWLQDTSITPPGGESFDDVLRRVRRGRDRIIVGYEGATVLVVSHVTPIKMLLRLALDAGSGVLYRLHLDLASLSIAEFYADGASSVRLVNQTGYL
Protein: Uncharacterized protein (Q72EI3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Chaperone protein HtpG
- Probable membrane transporter protein
- Fructose-1,6-bisphosphatase
- Glutamine synthetase, type III
Sequence:
MHYDLLVHVDSDDAAVLGLALANIVNYRAALPQDQFHVVLVANGPAVKQFVLQEQTHAPVIADLHAAGVSFRMCNNALTKFGIAPETLQTACEVVPAGVVEVVDLQRKGYAYIKP
Protein: C2H2-type domain-containing protein (O18067)
Organism: Caenorhabditis elegans
Interaction partners:
- Sun domain-containing protein 1
- HORMA domain-containing protein
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Protein MRVI1
- Meiotic recombination protein spo-11
- HORMA domain-containing protein
- PH domain-containing protein
- HORMA domain-containing protein
- DNA endonuclease activator Ctp1 C-terminal domain-containing protein
- Serine/threonine-protein kinase chk-2
Sequence:
MTCDDWNSFIQVNIYGKTIEGLQQQGVVLETLLNNVGCSKLWIVEGSVCTSSTPESSTYSEKRTIEPVVSLSTTLATNKLPRFSTPAVGHSKYNSAKNFTLNLAEKLSEILSDDDKTDKCLENSYQSETSREDVIQDLLEEMVQTVADVDQAPILLSTTLANIGVPRFSTPIKPQNGLDRKFTMNMTERISEIDSNYLGYEVLDDSNKILTANCEEVEMSLCENIPGVNNARTFSNTPYDDFLNIYSTPKNPKSNSSVPYQEGKRRSSRRLSTLSSLKETVKIEPAVSKSTKRSRLAPIQILSQTVRPNIEHTFPVSTSAIQSDGFSYEHPINEYGDNESFSSAKSHCDEPSFCNAVDLKPVLKVLNSGRTVLTGSIISDQPPVIELSRDHNIEGVFQNNFVDVEDTMLIENYEEVGAEIVEVDDQDQYEVISEDDEKEKSPIPSKNRVSFAFPLVQSPNKQKEEMNKVHNIKCHFDNCNRKIHWKIRYGKLRLVDHALSHQEEKSIDCQKCEYSCQTTRQMRYHYKKIHANLKMEGFGILNIPLQNTKFSDVWNKCFGDQLKTIGPVRKAERTPRRKLKSIRL