wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger SWIM domain-containing protein sws1 (SWIM domain-containing and srs2-interacting protein 1) (O13600)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in early stages of the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents.
Subcellular location: Cytoplasm. Nucleus, nucleoplasm.
Interaction partners:
- DNA repair protein rdl1
- DNA repair protein rlp1
- Uncharacterized protein C22G7.03
- Uncharacterized protein C651.12c
- Phospholipid-transporting ATPase accessory subunit ivn1
- Swi5-dependent recombination DNA repair protein 1
- Small ribosomal subunit protein uS15m
- O-glycoside alpha-1,2-mannosyltransferase homolog 5
- DNA excision repair protein ckn1
- Spindle pole body-associated protein sad1
Sequence:
MQQGHFTSNSYHSKTLNSSSLPVSSKFSHTNDPDVEGVDNDSFSKALCNKDLDPSSTIRSVISSLLDSLQDKALQQSPNTSLSKLLLEDQDFGSLWLSLSFIFCNYWQPAMLILDSKSIHPLPLTDGEVLHRWECEVDSNNKTTIDLKYWYCSCSQFSYNAFNSSRSFDEPMPKNEQETWGGRCLSHHPTICSHILAASILRACHNLVI
Protein: Polymerase gamma 1 (F4JEQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGVSLRHLSPSSFWVSRRPRVSSSILSFLVPRRRILCTRSRLKMCVCSIALFRKKVAIIKGNAGYSTATDCGGSHGFHHSGHQRSSSVEFSGEWKLNLGSKTARMVPPTVKQAGAVSAWREEVNNKLRGRNREYANNQDDAFGNGSYILKGFVPKIDDVHSYGNGQNFDYNLKPGTDITTLGRELNGFMQTNSIRGSVVALPSKDIEVGETTDVTLKPLNSDTTLDNASYKKTATISKVEKCTNLSQVRANLKKIYNRVRVVDNVSSAKETVALLMNQYRNLVHACDTEVSRIDVKTETPVDHGEMICFSIYCGSEADFGDGKSCIWVDVLGENGRDILAEFKPFFEDSSIKKVWHNYSFDNHIIRNYGIKLSGFHGDTMHMARLWDSSRRISGGYSLEALTSDPKVLGGTETKEEAELFGKISMKKIFGKGKLKKDGSEGKLVIIPPVKELQMEDREAWISYSALDSISTLKLYESMKKQLQAKKWFLDGKLISKKNMFDFYQEYWQPFGELLAKMESEGMLVDRDYLAQIEIVAKAEQEIAVSRFRNWASKHCPDAKHMNVGSDTQLRQLFFGGISNSCNDEDLPYEKLFKVPNVDKVIEEGKKRATKFRNIKLHRISDRPLPTEKFTASGWPSVSGDTLKALAGKVSAEYDYMEGVLDTCLEENIGDDDCISLPDEVVETQHVNTSVESDTSAYGTAFDAFGGGESGKEACHAIAALCEVCSIDSLISNFILPLQGSNVSGKDGRVHCSLNINTETGRLSARRPNLQNQPALEKDRYKIRQAFIASPGNSLIVADYGQLELRILAHLASCESMKEAFIAGGDFHSRTAMNMYPHIREAVENGEVLLEWHPQPGQEKPPVPLLKDAFASERRKAKMLNFSIAYGKTAIGLSRDWKVSREEAQDTVNLWYNDRQEVRKWQELRKKEAIQKGYVLTLLGRARKFPEYRSRAQKNHIERAAINTPVQGSAADVAMCAMLEISNNQRLKELGWKLLLQVHDEVILEGPSESAENAKDIVVNCMSEPFNGKNILSVDLSVDAKCAQNWYAGK
Protein: Phosphomannomutase (EC 5.4.2.8) (Q38AW2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU361118}.
Interaction partners:
- mannose-1-phosphate guanylyltransferase
- mannose-6-phosphate isomerase
- Phosphotransferase
- Phosphotransferase
- fructose-bisphosphatase
- riboflavin kinase
- Sugar transporter, putative
Sequence:
MKRVLLLFDVDGTLTPPRLCQTDEMRALIKRARGAGFCVGTVGGSDFAKQVEQLGRDVLTQFDYVFAENGLLAYRNGLEIHRQSLLNALGNDRIVKFVKKTLRLIADLDIPVQRGTFVEYRNGMINVSPIGRNCSQAERDEFEVYDNEHRVRASLIAELENSFPDFGLKYSIGGQISFDVFPVGWDKTYCLQFVEDDFEEIHFFGDKTQEGGNDYEIYTDKRTIGHKVTSYKDTIAEVEKIIAMK
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (Q8IMG6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
Sequence:
MGGGSGACPPAHMYGAVAPQDIIVRDMVQMPPPPSNAPTSADACLSIVHSLMCHRQGGESEGFAKRAIESLVKKLKEKRDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARIWRWPDLHKNELKHVKYCAFAFDLKCDSVCVNPYHYERVVSPGIDLSGLSLQSGPSRLVKDEYSAGPLVGSMDIDGNDIGTIQHHPTQMVGPGGYGYPQGPSEYAVPHGMPGMPGPMNPGPVMAPPPPPQQAQNPQGNGVHHTQANSPTDPASALAMQQQQQQQQQQQQQQQQQQQQSGGVPNGSVNAGGGAAAGGQYYGQPPPVSQMQGAGGGGTSVAPSVHAQQNGYVSQPGSAGSAPVGGGGVFGTAQPTPQQPQQPPTGVQANTGSAGAQAGAGGGAAGTWTGPNTLTYTQSMQPPDPRSLPGGFWNSSLSGDLGSPQQTPPQQQQQQQQPRLLSRQPPPEYWCSIAYFELDTQVGETFKVPSAKPNVIIDGYVDPSGGNRFCLGALSNVHRTEQSERARLHIGKGVQLDLRGEGDVWLRCLSDNSVFVQSYYLDREAGRTPGDAVHKIYPAACIKVFDLRQCHQQMHSLATNAQAAAAAQAAAVAGVANQQMGGGGRSMTAAAGIGVDDLRRLCILRLSFVKGWGPDYPRQSIKETPCWIEVHLHRALQLLDEVLHAMPIDGPRAAA
Protein: Transmembrane protein (Q381C1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSARESESRDGVSCVSSVIEEETTSPWRHNEIERYLPYTIGRETAYVALASPDTVSPETSISGHCSTFARATSEADGRHGVISDVYCGDGGGGSGRTGGCDVDRISYVNDCDGAEYSRVKTSSVTPVADSVRSMEYGVGYGSPLLHDTQELRVSWCYQRDDRAAGGDFTPAFTVSPVITPWQHPGNGRKERDVVKSAPLPPNCCWLWPDIREEKDGSSSYDVGWRGLKVTEGVPRVNYTDGVPDYLEPLLFRDHLPKNSLKGTEGPAEGPTPRTPGKKVKRVRFSETVVGSVSFVETHNEIQVIVESHYPWLALAGLFIAVTLFVLHWGVIAVIAGPREGIERITAVSLVDFVSSGLASLIMLLFLALLWRPGREEVDVISSCSGISRVMCVAFCGALATLSLVCMFMFTNSAVGFVCFCCCPFVGTHLYEVLKLHNVPLLSTMASILIVWAFAALVIGCFVEGDDVTFRCLWPVAIAISGGAAMCVYLFQFRSVGREVSGLFLSFVTLVTVTLMLALASYASGGFSLPTQSTQSSLFVLVMTDFSSVLFSVFFLVLYHLIYHCSSPFFSRLCVPGSFVFGGAISLLISRLLLDSVVFWPLEATGSILMMAGSALIFVAEYHQWQSAGAIAGVE
Protein: Dynein arm light chain, axonemal, putative (Q57VS8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- HYDIN/VesB/CFA65-like Ig-like domain-containing protein
- Sperm-associated antigen 6
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MATLNAPPNVYDEEGTVLYRAVPSNLISDDEPITAAAVNAATAAAAGQEAPTIPTTNRQKFGQTQSGVAGTRDAIQSDGGPVRLTQESLTPVKALAKLFPPVPLNVPGHDKDRTNTRGQEQECAWMKAAAVDHTSRLDCVHLQEHLERRCQQEHARPSGVVCTIREGIYADGMREVIRQVTVLCPERGLLLAELAEEMQQTTNTYDILFDSASQYTVRKAIERDLRSYLFKEKEWMESEVRRLENRVNELRAKHNGMLKRFEEQKQSEQKIHEEEVKYLRKANQQIINEIKRFAAVEKSSTPTPGM
Protein: Endoglin (Cell surface MJ7/18 antigen) (CD antigen CD105) (Q63961)
Organism: Mus musculus (Mouse)
Function: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis. Required for normal structure and integrity of adult vasculature (By similarity). Regulates the migration of vascular endothelial cells. Required for normal extraembryonic angiogenesis and for embryonic heart development. May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis. May play a role in the binding of endothelial cells to integrins. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors. Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:8125301}; Single-pass type I membrane protein {ECO:0000305|PubMed:8125301}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-3 proprotein
- Activin receptor type-1-like
- TGF-beta receptor type-2
- Growth/differentiation factor 2
- 5'-nucleotidase
- Thy-1 membrane glycoprotein
- Hematopoietic progenitor cell antigen CD34
- Platelet endothelial cell adhesion molecule
- Bone morphogenetic protein receptor type-2
Sequence:
MDRGVLPLPITLLFVIYSFVPTTGLAERVGCDLQPVDPTRGEVTFTTSQVSEGCVAQAANAVREVHVLFLDFPGMLSHLELTLQASKQNGTETQEVFLVLVSNKNVFVKFQAPEIPLHLAYDSSLVIFQGQPRVNITVLPSLTSRKQILDWAATKGAITSIAALDDPQSIVLQLGQDPKAPFLCLPEAHKDMGATLEWQPRAQTPVQSCRLEGVSGHKEAYILRILPGSEAGPRTVTVMMELSCTSGDAILILHGPPYVSWFIDINHSMQILTTGEYSVKIFPGSKVKGVELPDTPQGLIAEARKLNASIVTSFVELPLVSNVSLRASSCGGVFQTTPAPVVTTPPKDTCSPVLLMSLIQPKCGNQVMTLALNKKHVQTLQCTITGLTFWDSSCQAEDTDDHLVLSSAYSSCGMKVTAHVVSNEVIISFPSGSPPLRKKVQCIDMDSLSFQLGLYLSPHFLQASNTIELGQQAFVQVSVSPLTSEVTVQLDSCHLDLGPEGDMVELIQSRTAKGSCVTLLSPSPEGDPRFSFLLRVYMVPTPTAGTLSCNLALRPSTLSQEVYKTVSMRLNIVSPDLSGKGLVLPSVLGITFGAFLIGALLTAALWYIYSHTRGPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA
Protein: Protein S100-A4 (Calvasculin) (Metastasin) (Placental calcium-binding protein) (Protein Mts1) (S100 calcium-binding protein A4) (P26447)
Organism: Homo sapiens (Human)
Function: Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy. Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9. Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (By similarity). Modulates also the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels. Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes (By similarity). In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors.
Subcellular location: Secreted {ECO:0000269|PubMed:26654597, ECO:0000269|PubMed:30713770}. Nucleus {ECO:0000269|PubMed:23752197}. Cytoplasm {ECO:0000250|UniProtKB:P07091}.
Interaction partners:
- Annexin A2
- Myosin-9
- Cellular tumor antigen p53
- Advanced glycosylation end product-specific receptor
- Fibroblast growth factor 2
- Pro-epidermal growth factor
- Epidermal growth factor receptor
- Annexin A1
- Amphiregulin
- Protein S100-A1
Sequence:
MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK
Protein: Transforming acidic coiled-coil containing protein 3 (A0A494BZT8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSLQVLNDKNVSNEKNTENCDFLFSPPEVTGRSSVLRVSQKENVPPKNLAKAMKVTFQTPLRDPQTHRILSPSMASKLEAPFTQDDTLGLENSHPVWTQKENQQLIKEVDAKTTHGILQKPVEADTDLLGDASPAFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRVTPASETLEDPCRTESQHKAETPHGAEEECKAETPHGAEEECRHGGVCAPAAVATSPPGAIPKEACGGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTNHLVAGRAMTLSPQEEVAAGQMASSSRSGPVKLEFDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGRSGAGEDPPMPASRGSYHLDWDKMDDPNFIPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGPCLSQQLHSASAEDTPVVQLAAETPTAESKERALNSASTSLPTSCPGSEPVPTHQQGQPALELKEESFRDPAEGTGAEVDYLEQFGTSSESALRKQSLYLKFDPLLRDSPGRPVPVATETSSMHGANETPSGRPREAKLVEFDFLGALDIPVPGPPPGVPAPGGPPLSTGPIVDLLQYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI
Protein: Zinc finger MYND domain-containing protein 12 (Q9H0C1)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:37934199}. Note=Found along the full length of the sperm flagellum. {ECO:0000269|PubMed:37934199}.
Interaction partners:
Sequence:
MNVIYPLAVPKGRRLCCEVCEAPAERVCAACTVTYYCGVVHQKADWDSIHEKICQLLIPLRTSMPFYNSEEERQHGLQQLQQRQKYLIEFCYTIAQKYLFEGKHEDAVPAALQSLRFRVKLYGLSSVELVPAYLLLAEASLGLGRIVQAEEYLFQAQWTVLKSTDCSNATHSLLHRNLGLLYIAKKNYEEARYHLANDIYFASCAFGTEDIRTSGGYFHLANIFYDLKKLDLADTLYTKVSEIWHAYLNNHYQVLSQAHIQQMDLLGKLFENDTGLDEAQEAEAIRILTSILNIRESTSDKAPQKTIFVLKILVMFYYLMMNSSKAQEYGMRALSLAKEQQLDVHEQSTIQELLSLISTEDHPIT
Protein: Cross-pathway control protein A (Q00096)
Organism: Aspergillus niger
Function: Master transcriptional regulator that mediates the response to amino acid starvation (By similarity). Binds variations of the DNA sequence 5'-ATGA[CG]TCAT-3' (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:14648200}.
Interaction partners:
Sequence:
MSTPNIAQDFPELFDLQSNRFGDDLSSPESNMLSPQINTSFFSPMGEVAPPGTVSPKDLFFDASAPPSTTFTDLSTPPLDTPGFFSQNTSPMINTEMDLNAVPEEWESLFPQDGFSLDLDSAALELAASLQQPKATGPPPTPVIRASASPAPSASPAPSRQGTKHSTVAGVNARQRKPLPPIKFDSADPAAMKRARNTEAARKSRARKLERQGEMERRIEELERMLEESKQREEYWRSMAKTGTN
Protein: Glutamine synthetase (EC 6.3.1.2) (A8WCU4)
Organism: Gossypium herbaceum (Levant cotton) (Arabian cotton)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSLLTDLVNLNLSDCTDKIIAEYIWIGGSGMDLRSKARTLSGPVSDPSKLPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRRGNNILVMCDAYTPAGEPIPTNKRCNAAKIFSHPDVAAEEPWYGIEQEYTLLQKDVKWPIGWPLGGYPGPQGPYYCGVGVDKAYGRDIVDSHYKACLYAGINISGINGEVMPGQWEFQVGPAVGISAGDELWVARYILERITEIAGVVLSFDPKPIQGDWNGAGAHTNYSTKSMRSDGGYEVIKKAIAKLGLRHKEHIAAYGEGNERRLTGRHETADINTFLWGVANRGASIRVGRDTEKAGKGYFEDRRPASNMDPYVVTSMIAETTILWKP
Protein: Zinc metalloproteinase nas-7 (EC 3.4.24.-) (Nematode astacin 7) (P55113)
Organism: Caenorhabditis elegans
Function: Metalloprotease.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Nematode cuticle collagen N-terminal domain-containing protein
Sequence:
MLLPWIITIVTVIPATLGHRNRVQDDEMLVISDSTDSLNLEDFEFADKLTREELFGKHIPVEVVNDFKSDIRLPRRHKRNGVSRAAKLWPNARIPYAISPHYSPHERALLAKAVKQYHEKTCIRFVPRQTGEPDYLFIGKVDGCFSEVGRTSGVQVLSLDNGCMEYATIIHEMMHVVGFYHEHERWDRDNFIDIIWQNIDRGALDQFGKVDLSKTSYYGQPYDYKSILHYDSLAFSKNGFPTMLPKVKSATIGNARDFSDVDISKINRMYNCPVEKSVTAPFARARHVPIYSPQYHKYEDRPKIPLRSFDMQQGPINPPMAQIPSQSLVVSSSSGRVNYNSNKPSSQCEDRITVCWWTADRCRSPAIYQVMSSLCPKTCKFC
Protein: START domain-containing protein (C7FZT8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEVTRAMTNPPPELMINLAPTLAPPSPMKRKRFPVFDEQEAGFQPIAPVPSPRRQQEDVVGPTFLRDLLTASCSRSPCSESNYSDRLATSDTATTQKASRASSFEWLENSGHGKYEQCSSDEADREVASIEMVKQTEVLQRKKTIEDLEESVNELQSLGNGSWFPHPPPPPAEARDQIYESLPASFRNRKSENRKNAVGSVYDNAAISSKPSSSETTSFSQQKPIIDRKPFSLENLPMVQRLTELSAAKKNADSKNEVAKRSNTFSLQLAERDAVDACSWLRKAGFSKYADQFEEGKLPIVASKDPTLLEADLRALNRRIDVLNRCHTMKVDSVPMRRRINNEFPRLDPMKIDDNSGYSSDSWRYGSVGGSHHSNTWSRPSGSDHHVYGGSLARMPNSTSSAWHHQMADPTRDSRKVLRTDWYDAQNTPPRGRNNDVLETASSAACVNELNSKLQRSQSERIKDRARAIMKKMDLRSTNKRPKETRGRPAPMNIGDPVLVSYDTPKNSIRSHHIDRPSILPERGRQLYPTSPYQAPSRSKSIAQNNRRGGLVFITPTSPNSLDTSFGYSDTNSSVVSSHRSNGESRRRELSMPPPSRHRVQMNGPSYPVMDGTLRRREIMPFDSYLYAGNPKMLERYDKTYESPRNLIPDRMYDDLDDLPLPKSTKTTNSNSTSNSNSLDNKKTDNISMFNDGYYTHEIKTALPRHHNILTTVKPENLKVNTEKIDIISSSDEPIGRTALTKRSDSGLGSSLSRSPSGPHTQRIRQSLLPYSNATSSSASAYSCCSWGSSTKLLDEQQPFFTDMVELARSIDSLNLIEMTRLRKTAFLRLSSILERNIEGKGVGLVDPDQEELPSKHVWSVQRLIKRMKINDGQKREKDVDGDGAVFGVGLDVIFNRTGYFLPRPILEVMKFLRNIAPETVGIFRKNGVKSRIAELRSIIESYSGNTDVFVGENLLDSTQVHDVADLLKQYFRDLPEPLMTVKMSEVFANICSVVPDVERITALQYAILLLPDENREALKTLLLFLKEVSRNSQVNNMTAQNLSVCFTPSLFQLGASRLDKVTPGNRRHKTVGATGLPSEKEMKEARACQLCLTMLIEYVQTVFMVPDGLDDSMDAEDDNPNLTELGLKGPRSFLVDRVIDLIRDHSDQWKNWTIEGSFRGIEISSKRPSDSHPLKTFRVWLNVPAGPKSVMMRLLKERYTWDSSVINWRHLEYVSAPDTDIHQYVVNETIGHPTKDCHVARFHSSGLTEIRGACAIAERSVKCTEDQLLGGVSATIFDQRFLIEPVSGGQSRVNYIARVDLKGRSLQWYNKSFGSIMCRHLDRLRESFHLGDKGGPETNV
Protein: Uridine diphosphate glucose pyrophosphatase NUDT14 (UDPG pyrophosphatase) (UGPPase) (EC 3.6.1.45) (Nucleoside diphosphate-linked moiety X motif 14) (Nudix motif 14) (O95848)
Organism: Homo sapiens (Human)
Function: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP-mannose.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12429023}.
Interaction partners:
- NAD-capped RNA hydrolase NUDT12
- Uridine diphosphate glucose pyrophosphatase NUDT22
- ADP-sugar pyrophosphatase
- Nucleotide triphosphate diphosphatase NUDT15
- 8-oxo-dGDP phosphatase NUDT18
- ADP-ribose pyrophosphatase, mitochondrial
- NAD
- m7GpppN-mRNA hydrolase NUDT17
Sequence:
MERIEGASVGRCAASPYLRPLTLHYRQNGAQKSWDFMKTHDSVTVLLFNSSRRSLVLVKQFRPAVYAGEVERRFPGSLAAVDQDGPRELQPALPGSAGVTVELCAGLVDQPGLSLEEVACKEAWEECGYHLAPSDLRRVATYWSGVGLTGSRQTMFYTEVTDAQRSGPGGGLVEEGELIEVVHLPLEGAQAFADDPDIPKTLGVIFGVSWFLSQVAPNLDLQ
Protein: GEO11122p1 (Q9VRW1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTSESKMVLLFLIGCLVMQTINALPFDRFSQEDDERNNEISGEWFKKPILRFDRLFATEESPSGSRKEVRRPSRSDKGETTESSKHAHSMITSMLGFVSSVINFGRTFIRDQ
Protein: GDSL esterase/lipase At1g29660 (EC 3.1.1.-) (Apoplastic EDS1-dependent protein 3) (Extracellular lipase At1g29660) (Q9C7N5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in EDS1-dependent systemic acquired resistance, maybe in phloem-mediated long-distance signaling.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:24755512}.
Interaction partners:
- Transport/golgi organization-like protein
- Uncharacterized protein At5g42530
- Protein rolling protein
- At2g17710/T17A5.17
- AT5g51950/MSG15_3
- Phosphatidylinositol N-acetyglucosaminlytransferase subunit P-like protein
- Glycerophosphodiester phosphodiesterase GDPDL5
- PLAT domain-containing protein 1
- MLP-like protein 328
- AGAMOUS-like 46
Sequence:
MESYLRKWCLVSVWVLLLGLGFKVKAEPQVPCYFIFGDSLVDNGNNNRLRSIARADYFPYGIDFGGPTGRFSNGRTTVDVLTELLGFDNYIPAYSTVSGQEILQGVNYASAAAGIREETGAQLGQRITFSGQVENYKNTVAQVVEILGDEYTAADYLKRCIYSVGMGSNDYLNNYFMPQFYSTSRQYTPEQYADDLISRYRDQLNALYNYGARKFALVGIGAIGCSPNALAQGSQDGTTCVERINSANRIFNNRLISMVQQLNNAHSDASFTYINAYGAFQDIIANPSAYGFTNTNTACCGIGRNGGQLTCLPGEPPCLNRDEYVFWDAFHPSAAANTAIAKRSYNAQRSSDVYPIDISQLAQL
Protein: Histone deacetylase HDA1 (EC 3.5.1.98) (Q5A960)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates the YNG2 subunit of NuA4 histone acetyltransferase (HAT) module, leading to the reduction of YNG2 and NuA4 HAT at the promoters of hypha-specific genes. Plays a key role in the regulation of filamentous growth and virulence. Involved in the switch between two heritable states, the white and opaque states. These two cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically at low frequency.
Subcellular location: Nucleus {ECO:0000269|PubMed:22536157}. Note=Recruited to promoters of hypha-specific genes by BRG1 in a rapamycin-dependent manner.
Interaction partners:
- Uncharacterized protein
- HDA1 complex subunit 2
- Transcription factor SKN7
- Nucleoporin NSP1
- Transcriptional regulator GZF3
- Histone deacetylase
- histone deacetylase
Sequence:
MSTGQEEHLDSKLENQISEEENQSQNQNFPTAIEDSIQASIEKLDEVDDEINPIEVKDEFPTTIGTTYDILHPREPFPKRIKLEETETEPDSNGIADNDQTMVVVPPKKPQLFYTPLKTGLVYDVRMRYHAKVFTSYSEYIDPHPEDPRRIYRIYKKLVEAGIVLDPSLAGINEIGPFMLKIPIREATSEEILQVHSEDHLKFIQSTEDMSRDQLLKETETGDSIYVNNDSYLSAKLSCGGTIEACKAVIEGRVKNSLAIVRPPGHHAEPNTPAGFCLFSNVAVAAKNMLKNYPESVRRIVIVDWDIHHGNGTQKAFYNDPRVLYISLHRFENGKFYPGTKYGDLNQVGEGPGEGFTINIPWRSSGMHDGDYVYAFNKIIQPVISEFDPDLIIVSSGFDAADGDVIGACHVTPAGYGYMTHTLKGIARGKLAVILEGGYNLDSISKSALAVAKVLVGEPPENTITLRPQAEAIEVVDEVIKIQSKYFKSLRNGIPNGIFEDVYDLADVEKSNYKLVNIADPIRSHQVEKLFNEKEFINIPIISSPSNGEKPPFTTDLPDQLEDLIVASPDIYNCTTIILTIHDPPEIWANINPTNGVIETNSTMVLEHPLVQIMDKIQKEKDPENQEKFGYLDINIPSFQLPIPGTTSESSTYNPIIFAQEVLLYIWDNYIAYFQQLKNLVMVGFGDSYQSIVNLYGKRPSNEIKDLIKGTVAFLNRTTLKPLIPVMDESMVDWYYQNSIIFTSNFNTCWTGGSGAGNGNGNGNGNNGNSSNGGGNKSADSNGHDDFSKRPRKKFGRVIKAKTDGLCDVIQEKFDEGVDFILDSIEDYSSSED
Protein: bZIP transcription factor 14 (B7FX91)
Organism: Phaeodactylum tricornutum (strain CCAP 1055/1)
Function: Transcriptional activator which binds to the C-box-like motif 5'-TGACGT-3' and A-box-like motif 5'-GTACGTA-3' of target promoters to positively regulate the expression of genes involved in the tricarboxylic acid (TCA) cycle in response to nitrogen starvation. May also regulate the TCA cycle during day-to-night transitions.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
Sequence:
MRFPAASVAVDSTPQLRLLQMKDSHETYSTVQLVHSPLPEKGPNSVLVDVPQQISRRKPTAEQSFVSGSDSSRSSTKSSSGSRPVMTTTADPNIVTAASTESVSSSPKWLPKKADTDDRVQRSRERNRIHARKTRQRKKEQMQSLEGRATDLKHEQIRLKQIINEKNTANILVGLFSKGQSQSPNEDPRVEALMYRSVEEIPDPSKIPELPALILPGQHASKKIKVAVPVVAASPQSMSDGGGEEVASTSDVSGDEQQVPDDGIDYDLLGKDRSKCTPEELDQIRRERNRMHAKRTRDRKRIFTEEMAEMCRILEEENHLLRVHLGGLDSDFKSESTTTSTHVVDRIDSVLSTPTLASCAPPQDMVSVSLSPSQLPSKPSTKEVAFNQLQTLLDVAGSFERQQREAERKVPQMCSISAASDTSTSDSSHHHRQRRCHKGDSDRPVKRQRYQVPRSITTTTSLAAPVGW
Protein: ATP binding cassette subfamily F member 1 (Q5STZ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPKAPKQQPPEPEWIGDGESTSPSDKVVKKGKKDKKIKKTFFEELAVEDKQAGEEEKVLKEKEQQQQQQQQQQQKKKRDTRKGRRKKDVDDDGEEKELMERLKKLSVPTSDEEDEVPAPKPRGGKKTKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNRINKAVSEEQQPALKGKKGKEEKSKGKAKPQNKFAALDNEEEDKEEEIIKEKEPPKQGKEKAKKAEQGSEEEGEGEEEEEEGGESKADDPYAHLSKKEKKKLKKQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQGDDTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFEDYKREVLEALGEVMVSRPRE
Protein: Fusion glycoprotein F0 (Protein F) [Cleaved into: Fusion glycoprotein F2; Fusion glycoprotein F1] (O89342)
Organism: Hendra virus (isolate Horse/Autralia/Hendra/1994)
Function: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with G at the virion surface. Upon G binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).
Subcellular location: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MATQEVRLKCLLCGIIVLVLSLEGLGILHYEKLSKIGLVKGITRKYKIKSNPLTKDIVIKMIPNVSNVSKCTGTVMENYKSRLTGILSPIKGAIELYNNNTHDLVGDVKLAGVVMAGIAIGIATAAQITAGVALYEAMKNADNINKLKSSIESTNEAVVKLQETAEKTVYVLTALQDYINTNLVPTIDQISCKQTELALDLALSKYLSDLLFVFGPNLQDPVSNSMTIQAISQAFGGNYETLLRTLGYATEDFDDLLESDSIAGQIVYVDLSSYYIIVRVYFPILTEIQQAYVQELLPVSFNNDNSEWISIVPNFVLIRNTLISNIEVKYCLITKKSVICNQDYATPMTASVRECLTGSTDKCPRELVVSSHVPRFALSGGVLFANCISVTCQCQTTGRAISQSGEQTLLMIDNTTCTTVVLGNIIISLGKYLGSINYNSESIAVGPPVYTDKVDISSQISSMNQSLQQSKDYIKEAQKILDTVNPSLISMLSMIILYVLSIAALCIGLITFISFVIVEKKRGNYSRLDDRQVRPVSNGDLYYIGT
Protein: Growth hormone (D8MIT8)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDGTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF