wanglab/gogpt-training-data huggingface dataset:
Protein: Sugar ABC transporter, ATP binding protein (Q5LKX4)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
Sequence:
MSDQPLVRMRGITKRFGGVTALQDVDLEAYSGEVLAIVGDNGAGKSTLIKILTGVYQATEGEIFLDGKRLEMSSHSDAIKVGIDAVYQTLALADHLTPANNMFLGNELTKRVLGIPMLDNRRMKSEATRILDERLGVRLRSMDVQTDSLSGGQRQAVAIARAVYHEDLRLLVMDEPTAALGPQETARTLKLIKSLRDQGLAVILISHSLDDVFEVADRVHVQRRGRAVGVVNTAQSSVQEVLGLIVGAQDAAA
Protein: Nuclear receptor binding SET domain protein 2 (D6R9V2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEGVMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNGSPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLEQGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMVSADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQAPTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVAKEAGIAAESLGEMAESSGVSEEAAENPKSVRE
Protein: Probable autophagy-related protein 17 (B0G140)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Autophagy-related protein 13 N-terminal domain-containing protein
- Serine/threonine-protein kinase atg1
- Probable serine/threonine-protein kinase DDB_G0291918
- Autophagy-related protein 9
- Uncharacterized Golgi apparatus membrane protein-like protein 2
- Uncharacterized Golgi apparatus membrane protein-like protein 1
Sequence:
MDFSSKSLELCKSHSNQTDQLLKISKQTYEKYDNSLSKLHLIIRELNKQLIILKETSTQFNDRYNTFINDFTSLSNQKQSLFTSIENKLEILKKKYLDKGLVFKNNNNNNNNNNNNNNNNNNNSNKSTEDDNNENNNNNDVNKNNNNNNNNNLNTLYDFIDIESLELIKNQFLSELSGLNEICDKSKQIYKSTNESNLEMENRFLEIQKQYNKQIEESNSLSDLLTQQNNLYKTIQNQLINVASQCDFITFYKPSPSPLSPSPSPSSSSSSSSPSPSSPQQQHDFNINNKKEQIQLLLTSSLENIQLMSKNVKDIENQFKESCSIYTLVYLLNEKLSFGNDFSENWETFERFNCIFEQRLAGANYFIGELYSLGKWYDLFDESYDNLLEEVKRRQKEYLRQKTIAEQFNEELKHNYNQEIQNRLKFYDSYGKYLPVSLFSTISDQPISFQVKQIIEESVIDYSFNPLNLKRSSPINQQQQQQQPPPNS
Protein: Tyrosine--tRNA ligase, cytoplasmic (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) (O14055)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular location: Cytoplasm.
Interaction partners:
- Putative leucine--tRNA ligase, cytoplasmic
- tRNA-aminoacylation cofactor arc1
- Putative leucine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, mitochondrial
- Probable cysteine--tRNA ligase
- Tryptophan--tRNA ligase, cytoplasmic
- Putative glycine--tRNA ligase
- Tryptophan--tRNA ligase, mitochondrial
Sequence:
MSLTPDEKYELITRNLQEVLGAKMIREILNERDISLYWGSAPTGRPHCGYFVPMMKLADFLKAGVHVTVLLADVHAFLDNMKAPMELVQHRVRYYEIIVKSILKSLNIPIEKLRFVIGSSYQLKEDYTLDNFRLAASTTEHTARRAGAEVVKQVASPLLSSLIYPGMQALDEQYLGVDVQFGGVDQRKIFVMAEEVLPVLGYKKRGHLMNPMVPSLAGGKMSSSAAANAKIDILDDPKTVNKKIRSAFCEPGVVEENGCLAFLKYVSFPAMELRGETEFVIDRPEQFGGRMVFKTYEEVEKAYKDLTLSPQDLKLGLESSVNTLLAGVQEQLKQYPDLDSILKAAYPDPKDLKKAMKQKKQDKKNAKKAGTTNASIAAESGAAPATESQTAESFKKLNLDD
Protein: Actophorin (EhActo) (C4LVG4)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Actin-binding protein that severs actin filaments.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:35281106}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:35281106}. Cell membrane {ECO:0000269|PubMed:35281106}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:35281106}. Cell projection, phagocytic cup {ECO:0000269|PubMed:35281106}. Cell projection, pseudopodium {ECO:0000269|PubMed:35281106}. Note=During phagocytosis, localizes to the tip of the actin-rich phagocytic cup until the closure of the phagocytic cup. {ECO:0000269|PubMed:35281106}.
Interaction partners:
- Adenylylcyclase-associated protein, putative
- Adenylyl cyclase-associated protein
- Profilin
- Actin, putative
- Actin, putative
- Actin, putative
- Actin, putative
- Actin
- Actin, putative
- Actin, putative
Sequence:
MAGIQLADEVTSVYNDFKLSHKYRYIVFKMNDGMTEVVVEKTAEKNATYDDFLKDLPEKSARYAVYDLEYDTPEGLRQKIIFYLWTPEGCKIREKMLYSATKATIKQALVGLSAEIQATDAGELNLDEVIAKVKTISK
Protein: Heat shock protein 42 (42 kDa heat shock protein) (Q12329)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Heat shock protein 104
- Protein BTN2
- Protein SIS1
- Heat shock protein 78
- Heat shock protein 26
- Hsp70 nucleotide exchange factor FES1
- Heat shock protein SSA4
- ATP-dependent molecular chaperone HSP82
- Curing of [URE3] protein 1
- Heat shock protein homolog SSE2
Sequence:
MSFYQPSLSLYDVLNALSNQTGQRGQQGYPRQPQRPQRYHPHYGQVHVGGHHPRHHPLYSRYNGVPNTYYYQFPGQAYYYSPEYGYDDEDGEEEDQDEDMVGDSGTTRQEDGGEDSNSRRYPSYYHCNTARNNRTNQQANSLNDLLTALIGVPPYEGTEPEIEANTEQEGEKGEEKDKKDKSEAPKEEAGETNKEKPLNQLEESSRPPLAKKSSSFAHLQAPSPIPDPLQVSKPETRMDLPFSPEVNVYDTEDTYVVVLALPGANSRAFHIDYHPSSHEMLIKGKIEDRVGIDEKFLKITELKYGAFERTVKFPVLPRIKDEEIKATYNNGLLQIKVPKIVNDTEKPKPKKRIAIEEIPDEELEFEENPNPTVEN
Protein: No circadian temperature entrainment, isoform D (M9PE74)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTLGGSRGERNAKPKFTALDINRMYKNSRGESSEPSAQKNQVPRKHGMQILGKVPSARRPPANLPSLKAETHTSSNNNLLVSVEGATSGGAGAGGAAGSGAAGTNTSHNNTTAHSGSSGTSGGAGSGGGGTASSSAGGHLSQQLTHSQHQHNNNVALGPNAGKFVNSNNGSSNNNAGSSGSGNKNFKLINNSVGSSGGGGQGGSGGGGSSGVGGGSGSGSGGHSVNSPKTWSAITTGHERGSGGQNYGRQQQQVVPHYQSPQFQYEFPTLDGTVGSGAGGGSGAGVGSGSGAGKSHYQNQVHHAGHQNHHQHQQHHQQHQQHHHQQQQHHRDYHHGHGRQYGHHSHRDYRDGSDDVGGGSADLGELSLRPQNDTAAWLQQQEKAAKVAAAAAADQGLNLQGPGHHQMGGNGGAGGGSGGAVPLPILSLMPSFMRSGAPMPASGATAASILAGGSLDTSALPNAPYQNGILGARSASPAVVGSGSFRAATAIPKRPPTSSSPPQSGLGIGGSPTPPQSQQQANGGAGGAGRKDKDYVVEPEVAQMQRPIIREEDLERLNAIAKDDSWTKQDDIDFTKKLAFSDDESTPEEHQGQGKQHSSAQLQAQGSSSSTDQRKLSASTTSWQRGKESTDRDQPSEGIQDQQQQLQQQQQQQEVRQQNGHRGSSGNVGAPVAGGIALDASVYERVKQRKEEEERREMERKQAAAKKLQELEMKMNSKKAAAAALAGAEGGVSSASVPLSNEVPPTSAPLGNASEDEGGGQGGGGGLNRRPRGSISSLGSGVTPTGGAGGGGGGVSSSSSAGGDYGQKNFLTHFQSNLPPRFQRQQQQQQQQLPRLEKSASASSAFDSNSRYLQKGGVSGGGGGVSGGAQANAGQGRSISGGYVQRGASVGGSSGYGRNRHDSSSAREDQDLDQQRFTRGQDYRQAQALPRSISENSHRKTSVSSAGDDVLGGSCSSWAEQTDAEQKVHHRHREESFSSSHSHDSAVQIKILQRPARQPSLSEESSTQQKQLPASPQQQKTLTTDPMPTQILRRSVDIDKSGDERAEDKSALESDDKAKSAGKVEEDKSGNKRVSPRSGAACGGRGGRGYAGSSGGSSVGSGSSYRGQRNASDWGSSRGSGGAGGRRYYGSGGEQSEHSEDVDEECYSSGGGGAARRSPKESGNGAPNSGASANKAGFSPRGEPSRRGRGGLSSGGGASASCYRRQPVGTGSAGGSGSGGSGRSYGRLGYEEYGKQQRTSESETDLDKTKQNQLALSAGLHKPSKDDKDLPALGGEEKDKTAALAPAHNTALLAKDELQKDAAGRLPLPPGLAAPGSAVGSVTATSSSVVVPGAADKKKIESCAVVGGEKVTGSKLPAIGEKTSLGAVGSGPSTSLLLDAGAPVNTIIFENSTYKQQAAAASVVTKPGTLSVSSSGATMTVDSLSSALSQMSFGGKATAAGSGDDSQDMKLGFSFGDDPTTPLKVVDNIDKTASQQQQQQQQQHSQQQQQQQQQQNNSTADLNMKIASVKKVWESATPMSDGPSPAQVQQQQQQQPQQQQQSQVQVAAQQQQQQVVGPQQAGDDGSGHMSAASFVAAVAASQHQQQHQQMPHYAVSAVHMQSHHHQQQQQQQQAAVAAAQAQHHQQQQAQAHHQHHALSSPGPVPGSHGHGYSHGSPFDAGSLEQQFQQEDYPSPQQQQQAHQKTKQLQQQQHLGMSPPPSQQQQQQHSQQQQQAQHQQQQQQAHQQQQQQQQPSFYQASPQFGVGGIPTIPSPPAVVYNSSQMPPPSQGGNLYAPFHSLDHSSRSPAYSAAAAAHSYPNPYAAAAAAAAAAAAGGGPFNVNVNAYAMQTPHGGSLPPTAPTPDMYSNLSSQFRLGGGPGPGPGPFGQPSSQQLSNPSNHAAVAIISSSSNSMMSSGAAKPPQSQQTIGAIGSKSAGSGGGPGPGPGPYATTQTYMNLYAAPPPQHPGQGGPPPGAHQLQSNSFYSNSAPGGPSGPQFYGGPPPQGNGGAQSYGLATAAGMYGGHQGGPPGSNGPPGPPQSQHTMGTFNTPFMNSQLLTAASINQYRGGPTPGAAYLKGNQGQTHMQDSMGRQLKSPLSADMSLGLAKQVQSQPSPPHHKNYGANQVLQQQQQQSQQQQQQQQRQVGGGNGPSMNALGGRGSGAVGSGSGNGGGGGGGAGGSQVGGNGGGNGVGSVGQSGGGGQGRYPTPIQRPNNYPQHPQQQQQQQQQQQQQREQAAAAAVAAQRAQNMRQVTGAGGGVAGSAGGGGSQTPVGPAGGNGGPGGAGGGGGAGGAAGSGPGKPYYANNASGAAVAANRGEWHAN
Protein: TFIIS central domain-containing protein (Q38BD5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAASEAMREKATSQLSALLQKMEEFRSEPVSAMTFARGIVDKMCSTCRDKEAFRDQLMGLLANLKGLDGELLSLGPDTIATMKPKEMLSVEERRKRDRFLRKRIREHMLHDSTKMLCSTCKLVRRDRLNVNQLALDSEENGTHFEYNFDNQCQCSSRSGSEAASSTSSSSSSSDYGGGEGSSEKSLKG
Protein: Hyphally-regulated cell wall protein N-terminal domain-containing protein (G8B4T8)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- SPX domain-containing protein
- Ubiquitin-like domain-containing protein
- Glycerophosphodiester phosphodiesterase
- 60S ribosomal protein L21-A
- Large ribosomal subunit protein eL40 domain-containing protein
- Uncharacterized protein
- Large ribosomal subunit protein uL2 C-terminal domain-containing protein
- MPN domain-containing protein
- 60S ribosomal protein L16
- Complex 1 LYR protein domain-containing protein
Sequence:
MQSLFRAQLVLWLFIATAWARNFQGGKTIDWGTQNVGYGDVHIFPGAIWSIINNAASDFHGNIQVDENGGLYVSAVSPSITLSATLYDSIYGFVNNGVVSFNAIKGASGYIFKIMGNKFENNGDLFFAASGQGSMESWIKAPDFHNNGLMHFYQSMKSDSYTYLGYDGKTMVNNGQICFTNQNWKQLTGMLGSGCVTAQGKSSFYFMNTNLQISEGEIFYLSNGETSIMAVGSINNPQTFHVRGFGTDKNGVANKLGLTATLSTPTPGKNPWAYNARDGILTLYVGLYTQNFEIGTGYDFTKFQIVSDTSRGLPGIYNGAVQYNGPPPNPGMPSECKPCKSVPGIPGVDPDERAETSLLSTNQETETSSTPTSTQPSVETLDNTSTSPEYYSTTTVTDIFTTTETTVLTTTWLVTKSDGSVETETGVVTQSGDSSSTITTFETPSDTLSYDSTTTVTDTFTTTETTVFTTTWIVTKSDGSVETETGIITQSGSSSSTITTFEPSETGASSSATDTGLLPNSSETGAGSVSPPESSDTLSYDSTTTVTDTFTTTETTVFTTTWIVTKTDGSVETETGIITQSGSSSSTITTFEPSETEISSTVTGFSSETGLGSGSATSTEPLTNSDETKISSGSTSEVSSNAASESSGEPTGEPTGEPSGSGSESTGEPTGEPTGEPSGSGSESTGEPTGEPSGSGSASTGEPTGEPSGSGSESTGEPTGEPTGEPSGSGSESTGEPTGEPTGEPTGEPSGSGSESTGVPTGEPSGSGSESTGEPTGEPTGESTGEPTGEPTGEPTGEPTGEPTGEPTGSASESTGGASGSGQPTGEPTGEPSGSGSASTGEPTGEPSGSGSESTGEPTGQPTGSASESTGGASEPTGEPTGEPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGEPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGQPTGSKGLSSSGNESTSSGVESATTGSDSGLGSTTESPGSHESGSGNTGAGDNGSGNTGAGDNGSGNTGAGNTGAGDNGAGSGNTGAGDNGAGSGNTGAGGNGSGNTGAGDNGSGSGNTGAGDNGSGSGNTGAGDNGAGSGNTGAGGNGSGNTGAGDNGAGSGNTGAGDNGSGNTGAGNTGAGDNGAGSGNTGAGDNGAGSGNTGAGGNGSGNTGAGDNGSGSGNTGAGDNGSGSGNTGAGDNGSGNTGAGNTGAGDNGAGSGNTGAGDNGAGDNGAGNTGAGDNGTGSGNTGAGDNGAGGNGSGNTGAGNTGAGSGNTGAGGNGSGNTGAGNTGAGNTGAGGNGSGNTGAGNTGAGDNGAGSNGSASNGGPSAHESLSASQPKESSPSNVTTYEGSGAVTKVSSVTSIIVCLVMLIAF
Protein: Protein ECM3 (Extracellular mutant protein 3) (Q99252)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cell wall organization and biogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTHITLGQAIWASVRPIIKIYLIIGVGFGLCKMNILTVQATRSISDIVLTILLPCLSFNKIVANIEDNDIKDVGIICLTSVILFATGLGFAFIVRSVLPVPKRWRGGILAGGMFPNISDLPIAYLQSMDQGFIFTEAEGEKGVANVIIFLAMFLICVFNLGGFRLIENDFHYKGDDDEENTLTNDDSAQQPTQPIEGNSSSSSNQDILKEPNESTVPNSSQASYISEKNKKEKTELSVPKPTHTAPPAIDDRSSNSSAVVSIDSITHSLRTNHVDAQSVSELNDPTYRTRSQPIAYTTESRTSHVHNNRRNSITGSLRSIDMRELPAEGMSDLIREYSNVDQYGRRRKSSISSQGAPSVLQADGTISPNLTRTSTLQRVKTSNLTRIITSDATVSKKDIETSGSSLPKWLQKFPLTKFFVFFLKNCLRPCSMAVILALIIAFIPWVKALFVTTSNTPKIKQAPDNAPALTFIMDFTSYVGAASVPFGLILLGATLGRLKIGKLYPGFWKSAVVLVFLRQCIMPIFGVLWCDRLVKAGWLNWENDKMLLFVTAITWNLPTMTTLIYFTASYTPEDETEPVQMECTSFFLMLQYPLMVVSLPFLVSYFIKVQMKL
Protein: Cysteine proteinase, putative (A0A8U0WQ39)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Interaction partners:
Sequence:
MFTVLLLVVVAYATNFNTWVANNNKHFTIVESLRRRAIFNNNARFIAKFNKNNSFQLSVEGPFAAMTEAEYNSMLKPFVIDKQHEEIVYDSRGDVPESVDWRAKGKVPAIRDQASCGSCYSFASVAAIEGRLLVAGSKKFTVDDLDLSEQQLVDCSVSVGNKGCNGGSLLLSFRYVKLNGIMQEKDYPYVAAEETCTYDKKKVAVKITGQKLVRPGSEKALMRAAAEGPVAAAIDASGVKFQLYKSGIYNSKECSSTQLNHGVAVVGYGTQNGTEYWIVRNSWGTIWGDQGYVLMSRNKNNQCGIASGAAYPVGVADA
Protein: Polycomb protein esc (Protein extra sex combs) (Q24338)
Organism: Drosophila melanogaster (Fruit fly)
Function: Polycomb group (PcG) protein. While PcG proteins are generally required to maintain the transcriptionally repressive state of homeotic genes throughout development, this protein is specifically required during the first 6 hours of embryogenesis to establish the repressed state. Component of the Esc/E(z) complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3, leading to transcriptional repression of the affected target gene. The Esc/E(z) complex is necessary but not sufficient for the repression of homeotic target genes, suggesting that the recruitment of the distinct PRC1 complex is also required.
Subcellular location: Nucleus {ECO:0000269|PubMed:12533794, ECO:0000269|PubMed:7556071}.
Interaction partners:
- Polycomb protein Su
- Histone-lysine N-methyltransferase E
- Chromatin assembly factor 1 p55 subunit
- E3 ubiquitin-protein ligase RING1
- Polycomb group protein Pc
- Histone deacetylase HDAC1
- Polycomb group protein Asx
- Polycomb protein PHO
- Polycomb group protein Psc
- Zinc finger protein jing
Sequence:
MSSDKVKNGNEPEESEESCGDESASYTTNSTTSRSKSPSSSTRSKRRGRRSTKSKPKSRAAYKYDTHVKENHGANIFGVAFNTLLGKDEPQVFATAGSNRVTVYECPRQGGMQLLHCYADPDPDEVFYTCAWSYDLKTSSPLLAAAGYRGVIRVIDVEQNEAVGNYIGHGQAINELKFHPHKLQLLLSGSKDHAIRLWNIQSHVCIAILGGVEGHRDEVLSIDFNMRGDRIVSSGMDHSLKLWCLNTPEFHHKIELSNTFSQEKSTLPFPTVTKHFPDFSTRDIHRNYVDCVQWFGNFVLSKSCENAIVCWKPGQLHQSFEQVKPSDSSCTIIAEFEYDECEIWFVRFGFNPWQKVIALGNQQGKVYVWELDPSDPEGAHMTTLHNSRSVATVRQIAFSRDASVLVYVCDDATVWRWNRRQTTSI
Protein: TSC complex subunit 1a (Tuberous sclerosis 1a) (Q7SXZ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAKEQPSVFDLIPLLGSTDLHELEQVKTLLQETLSADKGTMLLNSLVDYFLQTNSSQAVDILSSVREPHDKYLLDKMNECMGKQSCRLSTITLLGHVVRKQPPWIHKIARFPLLVSLLKCLKTDSDVVVLITGVLVLITLMPMIPQTNKQLLCDYFDIFGRLAAWNQRHPGHAQGVFAVHLHASVYSLFHRLYGMYPCNFVSYLRAYYSMKENVDTFEEVVKPMLEHVRIHPELITGTKDYEVDPIRWKRFEPHDIVIECAKISLDSKEASSEEGYSSLADHIQRRAVHHSQSCSELSFHEISSVTPIGAICQSLSKSQPYLTVTQDSGSSAQTPNNQSDEVKSSGMKEELWSPSSICGMSTPPSSRGMSPTTVSDISLSASHLSGRIPSTPGDGKWTLSPSTPSGSSPLPSLSEEIGQAAQNTSSTQAKTCEEVKKVTSRSINNSSENGGDAKTPVSLAQLSDIVKRTEGEREDDTINEEILSLTHGKLDFGSRPGLESSFSGSLDTLLSSHPNHEQNLVSTPDRVECSAKAGEHQLPRSLWPFTPIENGKHSKCSLSDLTKESMPYEPLFDLALPKVASLFLERKTAEAFRRVEGERDHQDEMEGEDLSVTSPLEVLDRVIQQGHDTHGKVLKRTFSSPSQSSDPHLKGLVPAVSDELDMLRSQLLLLHNQLLYERHKREQHALRNRRLFGRIVNTTALEEQNNSMKTQLKLQEVEIQAVKVSLKEEQRRSVHIQEDREAVVNQLQTQIQQLQKERNDYYSKMQVLKSELQENQTKAGKMEAELQKANNKVCNMGHMLSQLSIKLNNSENMEQQMAFLNKQLLLLGEANKLYMEEIDRLGPEAHKELNMLQASSVREGERLRQSSLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDNVKRQATEQLQASENRYLAQKNITQALQTELLELYSKIELKNLKTNAPAEPISDPSSPTNQRPNGNSAGPSAPSLPADLMKREEGAHVCVNGEISAASPQTPTALINGSQEEDLSALTHSFPSLPCQPFAVGSYPSTRSFLGKKAREMFRNKSESHYDGDSPTLTCLSKDLKVEPITDPTESLESEEAADQFDLQPMDRPRAYNVQSRRHQDLRIMDYNETHHVH
Protein: SPARC (Basement-membrane protein 40) (BM-40) (Osteonectin) (ON) (Secreted protein acidic and rich in cysteine) (P34714)
Organism: Caenorhabditis elegans
Function: Has a high affinity for collagen. Affects nematode body morphology and mobility. Essential for C.elegans development and muscle function. The cysteine-rich region could have protease inhibitory activity or may provide the framework for a protein binding module. Probable role in skeletal morphogenesis.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}. Note=In or around the basement membrane. {ECO:0000250}.
Interaction partners:
- Collagen alpha-1
- Nidogen
- Collagen alpha-2
Sequence:
MRYALAACLLLLAASSFVDAKKKKIADDELGELLDNIDADEEKKSVEPAKNPCEDHQCGWGKECVVGKKGEPTCECISKCPELDGDPMDKVCANNNQTFTSLCDLYRERCLCKRKSKECSKAFNAKVHLEYLGECKKLDECTEEHMAQFPERMADWLFQVMKELKKRRELHKLEWEELLSEAENDDEKKHVYPVIWKFCELDTKPHDKSVSHHELIPITAPVIPMESCIKPFLEGCDANNDGNISIKEWGKCLGLKEGEIQERC
Protein: Xylulose kinase (Xylulokinase) (EC 2.7.1.17) (Q9C0U6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribulose-phosphate 3-epimerase
- Sorbitol dehydrogenase
- Probable transketolase
- Ribose-5-phosphate isomerase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Transaldolase
- Hexokinase-2
- 6-phosphogluconate dehydrogenase, decarboxylating
- Zinc-type alcohol dehydrogenase-like protein C1198.01
- Probable phosphoketolase
Sequence:
MFLGLDLSTQQLKGVVIDESLNVHQEVAVDFDRDLSDYNTIKGVYRNGYEVFAPVCMWLDAIDLLFERLKASVDVSKIQAISGAGQQHASVFLLKGSKKALNSLDAKSSLKQQLESLIHPTSPNWQDASTTKECEELESCIGGAKALADLTGSKAHLRFTGPQIKRFRRLHPETYENTERIALVSNFLASVLLQTEAPLDISDVCGMNLWDIQNEKFDIRLLEEVAGNSKGPDLANKLGTVEINGAKHLGPIGKYFVKKYGFSPNCQIIPLTGDNPATILSLPLRPGKDVLLSLGTSTTALMATQNYVCSPEYHMFAHPVTQNHYMVMLCYKNGSLAREQVRNTINEKYNVSDNTSWDRFNESILNPNIKGAGEKKQLGLFYPQREILPAVGPGTWRFAIQGTELYQVDKDEESWDYPDEDASAIVESQNLDIRMRITPLLTGIPQPDRVYVVGGASRNEAIVFKISQVLGCDVYRLKHGGSNACAVGGAIKAAYAMNGKGFTFEEYVNKSWDESKKIELIMNKPSAQTYEEYGKLLPFLKKAEDIAIQQSDIRH
Protein: Cell division cycle 20.1, cofactor of APC complex (AtCDC20.1) (Q9SZA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Subcellular location: Nucleus {ECO:0000269|PubMed:21687678}.
Interaction partners:
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Cell division cycle protein 27 homolog B
- Anaphase-promoting complex subunit 7
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 2
- Mitotic spindle checkpoint protein MAD2
Sequence:
MDAGMNNTSSHYKTQARCPLQEHFLPRKPSKENLDRFIPNRSAMNFDYAHFALTEGRKGKDQTAAVSSPSKEAYRKQLAETMNLNHTRILAFRNKPQAPVELLPSNHSASLHQQPKSVKPRRYIPQTSERTLDAPDIVDDFYLNLLDWGSANVLAIALDHTVYLWDASTGSTSELVTIDEEKGPVTSINWAPDGRHVAVGLNNSEVQLWDSASNRQLRTLKGGHQSRVGSLAWNNHILTTGGMDGLIINNDVRIRSPIVETYRGHTQEVCGLKWSGSGQQLASGGNDNVVHIWDRSVASSNSTTQWLHRLEEHTSAVKALAWCPFQANLLATGGGGGDRTIKFWNTHTGACLNSVDTGSQVCSLLWSKNERELLSSHGFTQNQLTLWKYPSMVKMAELTGHTSRVLYMAQSPDGCTVASAAGDETLRFWNVFGVPETAKKAAPKAVSEPFSHVNRIR
Protein: High mobility group protein HMG-I/HMG-Y (High mobility group AT-hook protein 1) (Q6NV11)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDSGKDTVATKEKDGAEKRGRGRPRKHPQQEASGSPTPKRPRGRPKGSKNKPSSTVSRGKKAAAASAPAGTKRRGRPKKAEKEEQPSKSSEEEEEEEEEQ
Protein: Interleukin-33 (IL-33) (Q66H70)
Organism: Rattus norvegicus (Rat)
Function: Cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines. Also involved in activation of mast cells, basophils, eosinophils and natural killer cells. Acts as a chemoattractant for Th2 cells, and may function as an 'alarmin', that amplifies immune responses during tissue injury (By similarity). Induces rapid UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O95760}. Chromosome {ECO:0000250|UniProtKB:O95760}. Cytoplasm {ECO:0000250|UniProtKB:O95760}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:O95760}. Secreted {ECO:0000250|UniProtKB:O95760}. Note=Associates with heterochromatin and mitotic chromosomes. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000250|UniProtKB:O95760}.
Interaction partners:
- Interleukin-1 receptor accessory protein
- Interleukin-1 receptor-like 1
- Caspase-1
- Interleukin-1 receptor type 1
- Interleukin-13
- Cytokine receptor-like factor 2
- Thymic stromal lymphopoietin
- Myeloid differentiation primary response protein MyD88
- Interleukin-5
- T-cell surface glycoprotein CD4
Sequence:
MRPRMKYSNSKISPAKCDSTSGRALVPPCKITRSQQKTKDICHVYCMRLRSGLTIRKETCYFGKEPAKRYSLKSGSKHEGRLSTCLPDSRKRSLLGSIQAFAASVDTLSIQGTSLLTESCALSTYNDQSVSFVLENGCYVINVEDCGKNQEKDKVLLRYYESSFPAQSGDGVDGKKLMVNMSPIKDTDIWLNANDKDYSVELQKGDVSPPDQAFFVLHKKSSDFVSFECKNLPGTYIGVKDNQLALVEENDESCNNIMFKLSKM
Protein: Innexin-8 (Protein opu-8) (Q23593)
Organism: Caenorhabditis elegans
Function: Structural component of the gap junctions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000250}.
Interaction partners:
- Peptidase S1 domain-containing protein
- Innexin-14
Sequence:
MFSVPFLTSLTSHLGITAIDDASDTLSCLITAFLFITAAILTSAKTYVGSAMECWLPQTYSGDWGEFAENYCFLKDTYFYPRQQSMTDIPMYHKERHRLTYYQWSSMYLAVAGIAFMIPKFLWRLSQSTTDMPVVYFCDTANEIKNETEDKRSAKIKEMARFMRTKITSVHTPSLFSFIRMYMVYSVIKILYLVNAIAQFVIIAIFLGQKRNLFWGWTLFMNLLNGITWETTGLFPRVTFCDFQVREMAGNNRDETVECVIGINEFNEKIFLFFWFWLVFLVFSTLIAHFYNAAQIVKPYFIHSLLFAIRDHDIVDQKELFREFGEKYLTMDGKLILSFVKSQSDLVASEVAVEMYSDFLEARDRANIAEDKYNNILKNGKQ
Protein: HTH myb-type domain-containing protein (A0A178VYP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIPSMEGGGKTNREEEEEEEEEEEEGEESKVSSNSTVEESDKKTKVRPYVRSKVPRLRWTPDLHLRFVRAVERLGGQERATPKLVRQMMNIKGLSIAHVKSHLQMYRSKKIDDQGQAIAGHKHLFETSTDRNIYKLSQLPMFRGYNHNHDSPFRYGSKISNASLWNSSSQGTERSLIDQIRPGLIRNASVSNNIRGSDYWTNNKSFQNIYSSSISNHFPKLRHDHHERTNSVTFNSIQGHSRTFQKFHNGVEENTNHSYCSKTNGKRDASRSIDLDLSLKLRQPEKTILEETETAATTTDQTLSLSLCPGSSSWKKSRLMKDEEDRTVKIGQESTLDLTL
Protein: Bowman-birk type proteinase inhibitor 2 (TcTI2) (P83283)
Organism: Amburana cearensis (Cerejeira) (Torresea cearensis)
Function: Inhibits trypsin, chymotrypsin, plasmin and factor XIIa. Does not inhibit factor Xa, thrombin, human plasma kallikrein, porcine pancreatic kallikrein and human urinary kallikrein.
Interaction partners:
Sequence:
SSKWEACCDRCACTKSIPPQCHCADIRLNSCHSACESCACTHSIPAQCRCFDITDFCYKPCSG