wanglab/gogpt-training-data huggingface dataset:
Protein: Deuterosome assembly protein 1 (Coiled-coil domain-containing protein 67) (F7DP49)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Key structural component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells and can generate more than 100 centrioles. Probably sufficient for the specification and formation of the deuterosome inner core.
Subcellular location: Cytoplasm {ECO:0000250}. Note=Localizes to the deuterosome. {ECO:0000250}.
Interaction partners:
Sequence:
MFTNIHSIARNSSCENELEELMHQIDIMVSHRKVEWEKHVKVLEQKLEAQDRELTEARNLVDEKNHEIGILCKKLEGVDTAQHEMAQNYERQLQALKFQLCKLKKSYEKLHFHQEKHQKNENAAQERSRCELQWLTQKIEEFKARSREWEKQRVFYQDQLKSLDEQRKTLAEKCQLFQKESLSYQEQLSSQKQLQSEAITNNQSEMRRLRCLLDTSQETIRSDGVIIENLKSTVKEITLSRDSLKDENQQLLQELRRCQKQSQNMEAQLYKAKLELQSCNDLLRVPALEERQAQKETANLANQKTAQGEEASFQVTDPRMNYMTSEPEHKSFNLSKSEKYQAENDLHGTEAKNSDLERLRKDIGDLTAKLNQKDVTIATVSRKVSRLERELELKGAQNRQTSMPLSQKDVIAELESEMPQIHAVNKAPQTDSGEVDPWISIKCGEHDKPQKHRSFHGENNSLKPTNYADTRNHSVGSEWESEKSLCPWNTPTLGSATDDDCDLVDNENEWLSLYNSTLYPGLDLPPISYACDQLKDSTNSSLAGSSLISAAEKFLLEETRRASDFEKILNSHIEEMKRNSESTVSRYQSHGQSRHI
Protein: Homoisocitrate dehydrogenase (HICDH) (EC 1.1.1.87) (O14104)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Homoaconitase, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Aromatic amino acid aminotransferase C569.07
- Aromatic amino acid aminotransferase C56E4.03
- Aromatic amino acid aminotransferase C1773.13
- Saccharopine dehydrogenase [NADP
- Homocitrate synthase, mitochondrial
- Probable acetolactate synthase small subunit
- Tryptophan synthase
- 2-oxoglutarate dehydrogenase, mitochondrial
Sequence:
MSATRRIVLGLIPADGIGKEVVPAARRLMENLPAKHKLKFDFIDLDAGWGTFERTGKALPERTVERLKTECNAALFGAVQSPTHKVAGYSSPIVALRKKMGLYANVRPVKSLDGAKGKPVDLVIVRENTECLYVKEERMVQNTPGKRVAEAIRRISEEASTKIGKMAFEIAKSRQKIRESGTYSIHKKPLVTIIHKSNVMSVTDGLFRESCRHAQSLDPSYASINVDEQIVDSMVYRLFREPECFDVVVAPNLYGDILSDGAASLIGSLGLVPSANVGDNFVMSEPVHGSAPDIAGRGIANPVATFRSVALMLEFMGHQDAAADIYTAVDKVLTEGKVLTPDLGGKSGTNEITDAVLANIHN
Protein: Creatine kinase B-type (EC 2.7.3.2) (Creatine kinase B chain) (H0YJG0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
FLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISMQKGGNMKEIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQAIDDLMPAQK
Protein: Ubiquitin-like modifier-activating enzyme 1 (EC 6.2.1.45) (Ubiquitin-activating enzyme E1) (A0A024R1A3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDKCLQRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEVQGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR
Protein: Lactoyl-CoA dehydratase subunit beta (EC 4.2.1.54) ((R)-lactyl-CoA dehydratase component E II) (2-hydroxybutyroyl-CoA dehydratase) (G3KIM3)
Organism: Anaerotignum propionicum (Clostridium propionicum)
Function: Involved in the acrylate pathway for the conversion of D-lactic acid to propionic acid. Catalyzes the reversible dehydration of Lactoyl-CoA and 2-hydroxybutyroyl-CoA to acryloyl-CoA and crotonyl-CoA, respectively.
Interaction partners:
Sequence:
MSRVEAILSQLKDVAANPKKAMDDYKAETGKGAVGIMPIYSPEEMVHAAGYLPMGIWGAQGKTISKARTYLPAFACSVMQQVMELQCEGAYDDLSAVIFSVPCDTLKCLSQKWKGTSPVIVFTHPQNRGLEAANQFLVTEYELVKAQLESVLGVKISNAALENSIAIYNENRAVMREFVKVAADYPQVIDAVSRHAVFKARQFMLKEKHTALVKELIAEIKATPVQPWDGKKVVVTGILLEPNELLDIFNEFKIAIVDDDLAQESRQIRVDVLDGEGGPLYRMAKAWQQMYGCSLATDTKKGRGRMLINKTIQTGADAIVVAMMKFCDPEEWDYPVMYREFEEKGVKSLMIEVDQEVSSFEQIKTRLQSFVEML
Protein: Homeobox expressed in ES cells 1 (Anterior-restricted homeobox protein) (Homeobox protein ANF) (Rathke pouch homeo box) (Q61658)
Organism: Mus musculus (Mouse)
Function: Required for the normal development of the forebrain, eyes and other anterior structures such as the olfactory placodes and pituitary gland. Possible transcriptional repressor. Binds to the palindromic PIII sequence, 5'-AGCTTGAGTCTAATTGAATTAACTGTAC-3'. HESX1 and PROP1 bind as heterodimers on this palindromic site, and, in vitro, HESX1 can antagonize PROP1 activation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pituitary-specific positive transcription factor 1
Sequence:
MSPSLREGAQLRESKPAPCSFSIESILGLDQKKDCTTSVRPHRPWTDTCGDSEKGGNPPLHAPDLPSETSFPCPVDHPRPEERAPKYENYFSASETRSLKRELSWYRGRRPRTAFTQNQVEVLENVFRVNCYPGIDIREDLAQKLNLEEDRIQIWFQNRRAKMKRSRRESQFLMAKKPFNPDLLK
Protein: Uncharacterized protein (Q38E88)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAQGGVVEIPPDFVPLEHVQRGMKNADCRTPVILFGEDGDPYLSLCKIARETDSAVWYFDFATTQDVEHTLGYIEIGSNNGDWVLIMNCGGVGQQAFRDIALMVFCLKPEPKKYPRREFFRLIFCVEKAFDIDQNVDIPFPPLILKNSIAVRRADGSGKWSLRLPSEARFREAQEAKRQRRRAEGRDSDSETDLDEDEALSGKWFHRSVELNRAIDEAPLALAAQKMKEALLNEDVDTIKHLIVSGEYDIARAIVPGMTPLQYACSVEKPKAAISLLECGADPNQPRESDGRPPLFMAIEDVSLARALIKHGADLHLRFEGYRVDNHPDTSPEVARLTKKMRQEM
Protein: MYB transcription factor (Myb domain protein 112) (Putative transcription factor MYB112) (Q94CJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNISRTEFANCKTLINHKEEVEEVEKKMEIEIRRGPWTVEEDMKLVSYISLHGEGRWNSLSRSAGLNRTGKSCRLRWLNYLRPDIRRGDISLQEQFIILELHSRWGNRWSKIAQHLPGRTDNEIKNYWRTRVQKHAKLLKCDVNSKQFKDTIKHLWMPRLIERIAATQSVQFTSNHYSPENSSVATATSSTSSSEAVRSSFYGGDQVEFGTLDHMTNGGYWFNGGDTFETLCSFDELNKWLIQ
Protein: Protein Bride of doubletime (Q9VDE4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24210908, ECO:0000269|PubMed:32750048, ECO:0000269|PubMed:36994075}. Cell membrane {ECO:0000269|PubMed:32750048}; Peripheral membrane protein {ECO:0000269|PubMed:32750048}; Cytoplasmic side {ECO:0000269|PubMed:32750048}. Note=During the dark period, forms discrete cytosolic foci in photoreceptor cells (PubMed:24210908, PubMed:36994075). During the day (ZT1 and ZT7), detection is limited to the outer part of the retina and does not occur in all photoreceptors (PubMed:36994075). At early night (ZT13), the foci increase in number and are broadly localized in the retina, and by ZT19 most photoreceptors express high levels of the foci in both the inner and outer parts of the retina (PubMed:36994075). Under conditions of constant darkness, foci accumulation is high and broad in photoreceptor cells (PubMed:36994075). Under conditions of constant light, foci accumulation is low and are restricted to 'finger-like' projections in the retina, appearing to be mostly localized to the Rh3 cell cytosol adjacent to the rhabdomeres (PubMed:36994075). {ECO:0000269|PubMed:24210908, ECO:0000269|PubMed:36994075}.
Interaction partners:
- Discs overgrown protein kinase
- HDC05827
- NHP2-like protein 1 homolog
- V-type proton ATPase subunit
- tRNA
- U3 small nucleolar RNA-associated protein 15 homolog
- Histone chaperone asf1
- Protein NipSnap
- rRNA methyltransferase 2, mitochondrial
- Nucleolar protein 56
Sequence:
MDWYVGTEWEDKNRGLAKKVIGLQFTEMDKPTIISTVEFSVNKKATNLGGRPSKYLVSDESATYPQKHSLEMGTSLTAVDCYLELLLQQFVPGETAACSITTKTGERIEFELKLEKIVKNTQVEKLSAAEIYEVALRLKESGVATFKTFPKFAFDYFVRAAKLLITYKPFDKLTKKTNGINGQAVEELFIQIQTNLAACLLQEKRYEHVIYHTQFVETEESPSEKSIYRRALAYYHLKEFAKAQATIERMPNYEEKREFSKLRDNIAVSWKDSKAHYKEVVQRMFS
Protein: Zinc finger MYM-type protein 6 (Transposon-derived Buster2 transposase-like protein) (Zinc finger protein 258) (O95789)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of cell morphology and cytoskeletal organization.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone-lysine N-methyltransferase SETDB2
Sequence:
MKEPLDGECGKAVVPQQELLDKIKEEPDNAQEYGCVQQPKTQESKLKIGGVSSVNERPIAQQLNPGFQLSFASSGPSVLLPSVPAVAIKVFCSGCKKMLYKGQTAYHKTGSTQLFCSTRCITRHSSPACLPPPPKKTCTNCSKDILNPKDVITTRFENSYPSKDFCSQSCLSSYELKKKPVVTIYTKSISTKCSMCQKNADTRFEVKYQNVVHGLCSDACFSKFHSTNNLTMNCCENCGSYCYSSSGPCQSQKVFSSTSVTAYKQNSAQIPPYALGKSLRPSAEMIETTNDSGKTELFCSINCLSAYRVKTVTSSGVQVSCHSCKTSAIPQYHLAMSNGTIYSFCSSSCVVAFQNVFSKPKGTNSSAVPLSQGQVVVSPPSSRSAVSIGGGNTSAVSPSSIRGSAAASLQPLAEQSQQVALTHTVVKLKCQHCNHLFATKPELLFYKGKMFLFCGKNCSDEYKKKNKVVAMCDYCKLQKIIKETVRFSGVDKPFCSEVCKFLSARDFGERWGNYCKMCSYCSQTSPNLVENRLEGKLEEFCCEDCMSKFTVLFYQMAKCDGCKRQGKLSESIKWRGNIKHFCNLFCVLEFCHQQIMNDCLPQNKVNISKAKTAVTELPSARTDTTPVITSVMSLAKIPATLSTGNTNSVLKGAVTKEAAKIIQDESTQEDAMKFPSSQSSQPSRLLKNKGISCKPVTQTKATSCKPHTQHKECQTDLPMPNEKNDAELDSPPSKKKRLGFFQTYDTEYLKVGFIICPGSKESSPRPQCVICGEILSSENMKPANLSHHLKTKHSELENKPVDFFEQKSLEMECQNSSLKKCLLVEKSLVKASYLIAFQTAASKKPFSIAEELIKPYLVEMCSEVLGSSAGDKMKTIPLSNVTIQHRIDELSADIEDQLIQKVRESKWFALQIDESSEISNITLLLCYIRFIDYDCRDVKEELLFCIEMPTQITGFEIFELINKYIDSKSLNWKHCVGLCTDGAASMTGRYSGLKAKIQEVAMNTAAFTHCFIHRERLVAEKLSPCLHKILLQSAQILSFIKSNALNSRMLTILCEEMGSEHVSLPLHAEVRWISRGRMLKRLFELRHEIEIFLSQKHSDLAKYFHDEEWVGKLAYLSDIFSLINELNLSLQGTLTTFFNLCNKIDVFKRKLKMWLKRTQENDYDMFPSFSEFSNSSGLNMTDITRIIFEHLEGLSQVFSDCFPPEQDLRSGNLWIIHPFMNHQNNNLTDFEEEKLTELSSDLGLQALFKSVSVTQFWINAKTSYPELHERAMKFLLPFSTVYLCDAAFSALTESKQKNLLGSGPALRLAVTSLIPRIEKLVKEKE
Protein: Enhancer of split mdelta protein (E(spl)mdelta) (HLH-mdelta) (Split locus enhancer protein mC) (Q01071)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional repressor of genes that require a bHLH protein for their transcription (By similarity). May serve as a transcriptional regulator of the Achaete-scute complex (AS-C) genes. Contributes to the neural-epidermal lineage decision during early neurogenesis. As part of the Notch signaling pathway, required to maintain the self-renewal and identity of type II neuroblasts by regulating the expression of the transcriptional repressor erm.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Enhancer of split m7 protein
- Enhancer of split mgamma protein
- Enhancer of split M2 protein
- Enhancer of split malpha protein
- Bearded
- BARBU
- Enhancer of split m3 protein
- Protein groucho
- Sphingosine-1-phosphate lyase
- Enhancer of split m5 protein
Sequence:
MAVQGQRFMTKTQHYRKVTKPLLERKRRARMNLYLDELKDLIVDTMDAQGEQVSKLEKADILELTVNYLKAQQQQRVANPQSPPPDQVNLDKFRAGYTQAAYEVSHIFSTVPGLDLKFGTHLMKQLGHQLKDMKQEEEIIDMAEEPVNLADQKRSKSPREEDIHHGEEVWRPW
Protein: Trophoblast glycoprotein (5T4 oncofetal antigen) (5T4 oncofetal trophoblast glycoprotein) (5T4 oncotrophoblast glycoprotein) (M6P1) (Wnt-activated inhibitory factor 1) (WAIF1) (Q13641)
Organism: Homo sapiens (Human)
Function: May function as an inhibitor of Wnt/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24582434}; Single-pass type I membrane protein {ECO:0000269|PubMed:24582434}.
Interaction partners:
- HLA class II histocompatibility antigen, DRB1 beta chain
- HLA class II histocompatibility antigen, DR alpha chain
Sequence:
MPGGCSRGPAAGDGRLRLARLALVLLGWVSSSSPTSSASSFSSSAPFLASAVSAQPPLPDQCPALCECSEAARTVKCVNRNLTEVPTDLPAYVRNLFLTGNQLAVLPAGAFARRPPLAELAALNLSGSRLDEVRAGAFEHLPSLRQLDLSHNPLADLSPFAFSGSNASVSAPSPLVELILNHIVPPEDERQNRSFEGMVVAALLAGRALQGLRRLELASNHFLYLPRDVLAQLPSLRHLDLSNNSLVSLTYVSFRNLTHLESLHLEDNALKVLHNGTLAELQGLPHIRVFLDNNPWVCDCHMADMVTWLKETEVVQGKDRLTCAYPEKMRNRVLLELNSADLDCDPILPPSLQTSYVFLGIVLALIGAIFLLVLYLNRKGIKKWMHNIRDACRDHMEGYHYRYEINADPRLTNLSSNSDV
Protein: Erythrocyte membrane protein band 4.1 like 2 (E9PQD2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTEVGSVSEVKKDSSQLGTDATKEKPKEVAENQQNQSSDPEEEKGSQPPPAAESQSSLRRQKREKETSESRGISRFIPPWLKKQKSYTLVVAKDGGDKKEPTQAVVEEQVLDKEEPLPEEQRQAKGDAEEMAQKKQEIKVEVKEEKPSVSKEEKPSVSKVEMQPTELVSKEREEKVKE
Protein: Zinc finger and SCAN domain-containing protein 20 (Zinc finger protein 31) (Zinc finger protein 360) (Zinc finger protein KOX29) (P17040)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Zinc finger protein with KRAB and SCAN domains 4
- Zinc finger protein with KRAB and SCAN domains 3
- SCAN domain-containing protein 1
- Zinc finger protein 396
- Zinc finger protein 174
- Zinc finger and SCAN domain-containing protein 32
- SCAN domain-containing protein 3
- Zinc finger and SCAN domain-containing protein 22
- Zinc finger and SCAN domain-containing protein 30
- Zinc finger protein 394
Sequence:
MAMALELQAQASPQPEPEELLIVKLEEDSWGSESKLWEKDRGSVSGPEASRQRFRQFQYRDAAGPHEAFSQLWALCCRWLRPEIRLKEQILELLVLEQFLTILPREVQTWVQARHPESGEEAVALVEDWHRETRTAGQSGLELHTEETRPLKTGEEAQSFQLQPVDPWPEGQSQKKGVKNTCPDLPNHLNAEVAPQPLKESAVLTPRVPTLPKMGSVGDWEVTAESQEALGPGKHAEKELCKDPPGDDCGNSVCLGVPVSKPSNTSEKEQGPEFWGLSLINSGKRSTADYSLDNEPAQALTWRDSRAWEEQYQWDVEDMKVSGVHWGYEETKTFLAILSESPFSEKLRTCHQNRQVYRAIAEQLRARGFLRTLEQCRYRVKNLLRNYRKAKSSHPPGTCPFYEELEALVRARTAIRATDGPGEAVALPRLGYSDAEMDEQEEGGWDPEEMAEDCNGAGLVNVESTQGPRIAGAPALFQSRIAGVHWGYEETKAFLAILSESPFSEKLRTCHQNSQVYRAIAERLCALGFLRTLEQCRYRFKNLLRSYRKAKSSHPPGTCPFYEELDSLMRARAAVRAMGTVREAAGLPRCGQSSAETDAQEAWGEVANEDAVKPSTLCPKAPDMGFEMRHEDEDQISEQDIFEGLPGALSKCPTEAVCQPLDWGEDSENENEDEGQWGNPSQEQWQESSSEEDLEKLIDHQGLYLAEKPYKCDTCMKSFSRSSHFIAHQRIHTGEKPYKCLECGKNFSDRSNLNTHQRIHTGEKPYKCLECGKSFSDHSNLITHQRIHTGEKPYKCGECWKSFNQSSNLLKHQRIHLGGNPDQCSEPGGNFAQSPSFSAHWRNSTEETAPEQPQSISKDLNSPGPHSTNSGEKLYECSECGRSFSKSSALISHQRIHTGEKPYECAECGKSFSKSSTLANHQRTHTGEKPYKCVDCGKCFSERSKLITHQRVHTGEKPYKCLECGKFFRDRSNLITHQRIHTGEKPYKCRECGKCFNQSSSLIIHQRIHTGEKPYKCTECGKDFNNSSHFSAHRRTHAGGKAS
Protein: Protein HIT1 (P46973)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Ribosome assembly 1 protein
- Uncharacterized protein YJR056C
- Putative uncharacterized protein YJL009W
- Uncharacterized protein YJL028W
- Uncharacterized protein YJL027C
- Mitochondrial membrane protein FMP33
- Box C/D snoRNA protein 1
- A1 cistron-splicing factor AAR2
Sequence:
MVSSAVKCGICRGVDGKYKCPKCGVRYCSLKCYKDAAKHVHKESEQPRAGTEANVEVVNNDKIINSSLAMNKTLKTKAFDDIYQNSAELQELLKYNTVKFHLAKVYRILSSTVNDGSSGKMNSDLQKELAVNYLNTLRYGGIHYNEAIEEFCQILLDKLNAVKK
Protein: Ribonuclease VapC41 (RNase VapC41) (EC 3.1.-.-) (Toxin VapC41) (P9WF59)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB41.
Subcellular location: Secreted. Note=Following 6 weeks of nutrient starvation. {ECO:0000269|PubMed:23345537}.
Interaction partners:
- Antitoxin VapB41
Sequence:
MLLCDTNIWLALALSGHVHHRASRAWLDTINAPGVIHFCRATQQSLLRLLTNRTVLGAYGSPPLTNREAWAAYAAFLDDDRIVLAGAEPDGLEAQWRAFAVRQSPAPKVWMDAYLAAFALTGGFELVTTDTAFTQYGGIELRLLAK
Protein: PTS-dependent dihydroxyacetone kinase operon regulatory protein (P76016)
Organism: Escherichia coli (strain K12)
Function: Positively regulates the dhaKLM operon from a sigma-70 promoter. Represses its own expression.
Interaction partners:
- PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL
- PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK
- PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM
- RNA polymerase sigma-54 factor
- Uncharacterized ABC transporter ATP-binding protein YphE
Sequence:
MSGAFNNDGRGISPLIATSWERCNKLMKRETWNVPHQAQGVTFASIYRRKKAMLTLGQAALEDAWEYMAPRECALFILDETACILSRNGDPQTLQQLSALGFNDGTYCAEGIIGTCALSLAAISGQAVKTMADQHFKQVLWNWAFCATPLFDSKGRLTGTIALACPVEQTTAADLPLTLAIAREVGNLLLTDSLLAETNRHLNQLNALLESMDDGVISWDEQGNLQFINAQAARVLRLDATASQGRAITELLTLPAVLQQAIKQAHPLKHVEATFESQHQFIDAVITLKPIIETQGTSFILLLHPVEQMRQLMTSQLGKVSHTFAHMPQDDPQTRRLIHFGRQAARSSFPVLLCGEEGVGKALLSQAIHNESERAAGPYIAVNCELYGDAALAEEFIGGDRTDNENGRLSRLELAHGGTLFLEKIEYLAVELQSALLQVIKQGVITRLDARRLIPIDVKVIATTTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRRGSIPALVNNKLRSLEKRFSTRLKIDDDALARLVSCAWPGNDFELYSVIENLALSSDNGRIRVSDLPEHLFTEQATDDVSATRLSTSLSFAEVEKEAIINAAQVTGGRIQEMSALLGIGRTTLWRKMKQHGIDAGQFKRRV
Protein: Follistatin (FS) (Activin-binding protein) (P19883)
Organism: Homo sapiens (Human)
Function: Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).
Subcellular location: Secreted {ECO:0000269|PubMed:11279126}. Nucleus, nucleolus {ECO:0000269|PubMed:20843798}.
Interaction partners:
- Growth/differentiation factor 8
- Inhibin beta A chain
- Growth/differentiation factor 11
- Bone morphogenetic protein 7
- Inhibin beta B chain
- Inhibin beta E chain
- Inhibin beta C chain
- Bone morphogenetic protein 4
- Bone morphogenetic protein 15
- WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 1
Sequence:
MVRARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEDTEEEEEDEDQDYSFPISSILEW
Protein: Nod factor hydrolase protein 1 (MtNFH1) (Class V chitinase NFH1) (Mtchit5) (U5N4E3)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Symbiotic enzyme that hydrolytically inactivates Nod factors (NFs) with a C16:2 acyl chain produced by the microsymbiont Sinorhizobium meliloti. NFs are lipo-chitooligosaccharide signaling molecules produced by nitrogen-fixing rhizobia to initiate nodulation (symbiosis) on the roots of legumes. Controls NF hydrolysis at the stage of root hair infection. Involved in the regulation of growth and branching of mature nodules. Modulates NF levels and signaling to complete transition of infected nodules to functional nitrogen-fixing organs. Lacks chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5.
Interaction partners:
- Beta-hexosaminidase
- Beta-hexosaminidase
- Beta-hexosaminidase
- Cytosolic triosephosphate isomerase
Sequence:
MANFLKLKQFLTLVLILLALAAKSSKSTPSPSSTTRVKGIYWIENPLFPPSSIDTSLFTHIFYAFVSPNKFTYKLEEEEEDSTTVATSLTTFTNTFKTKTPPIPTLLSIGGATSNSTLFAFIASDPTARATFINSTIQVARTFGFDGIDFDWEFPTTTKEMNDLGELLFQWRRAISDETASTSRPPLLLTAAVYFAVNFFLSGERRMYPVDSINKNLDWVNVMSYDLRGSGSNVTGAPSGMFDSKSNVSVVSGLFSWIRGGVAPEKIVMGMPLYGKSWKLQDPNVHGIGAPNVGPGPGVDGGMAYFQVVDFNKQMGAKVVYDKETGSVYSYSGSTWIGYDDPFTVSVKVGFAQALKLGGYFFWAAGYDTSDWKVSTASKAWRPES
Protein: Sialic acid-binding Ig-like lectin 10 (Siglec-10) (Siglec-like protein 2) (Q96LC7)
Organism: Homo sapiens (Human)
Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid (By similarity). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Involved in negative regulation of B-cell antigen receptor signaling. The inhibition of B cell activation is dependent on PTPN6/SHP-1 (By similarity). In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90 (By similarity). In association with CD24 may regulate the immune repsonse of natural killer (NK) cells. Plays a role in the control of autoimmunity (By similarity). During initiation of adaptive immune responses by CD8-alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification (By similarity).
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 5]: Secreted.
Interaction partners:
- Signal transducer CD24
- High mobility group protein B1
- Leukocyte surface antigen CD47
- Amine oxidase [copper-containing] 3
- CAMPATH-1 antigen
Sequence:
MLLPLLLSSLLGGSQAMDGRFWIRVQESVMVPEGLCISVPCSFSYPRQDWTGSTPAYGYWFKAVTETTKGAPVATNHQSREVEMSTRGRFQLTGDPAKGNCSLVIRDAQMQDESQYFFRVERGSYVRYNFMNDGFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAALSSQGTKPTTSHFSVLSFTPRPQDHNTDLTCHVDFSRKGVSAQRTVRLRVAYAPRDLVISISRDNTPALEPQPQGNVPYLEAQKGQFLRLLCAADSQPPATLSWVLQNRVLSSSHPWGPRPLGLELPGVKAGDSGRYTCRAENRLGSQQRALDLSVQYPPENLRVMVSQANRTVLENLGNGTSLPVLEGQSLCLVCVTHSSPPARLSWTQRGQVLSPSQPSDPGVLELPRVQVEHEGEFTCHARHPLGSQHVSLSLSVHYSPKLLGPSCSWEAEGLHCSCSSQASPAPSLRWWLGEELLEGNSSQDSFEVTPSSAGPWANSSLSLHGGLSSGLRLRCEAWNVHGAQSGSILQLPDKKGLISTAFSNGAFLGIGITALLFLCLALIIMKILPKRRTQTETPRPRFSRHSTILDYINVVPTAGPLAQKRNQKATPNSPRTPLPPGAPSPESKKNQKKQYQLPSFPEPKSSTQAPESQESQEELHYATLNFPGVRPRPEARMPKGTQADYAEVKFQ
Protein: Metal regulatory transcription factor 1 (MRE-binding transcription factor) (Transcription factor MTF-1) (Q14872)
Organism: Homo sapiens (Human)
Function: Zinc-dependent transcriptional regulator of cellular adaption to conditions of exposure to heavy metals. Binds to metal responsive elements (MRE) in promoters and activates the transcription of metallothionein genes like metallothionein-2/MT2A. Also regulates the expression of metalloproteases in response to intracellular zinc and functions as a catabolic regulator of cartilages (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:8065932}. Cytoplasm {ECO:0000250|UniProtKB:Q07243}. Note=Translocation to the nucleus is induced by metals. {ECO:0000250|UniProtKB:Q07243}.
Interaction partners:
- Metallothionein
- Cysteine and glycine-rich protein 1
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Beta-synuclein
- Proton-coupled zinc antiporter SLC30A1
Sequence:
MGEHSPDNNIIYFEAEEDELTPDDKMLRFVDKNGLVPSSSGTVYDRTTVLIEQDPGTLEDEDDDGQCGEHLPFLVGGEEGFHLIDHEAMSQGYVQHIISPDQIHLTINPGSTPMPRNIEGATLTLQSECPETKRKEVKRYQCTFEGCPRTYSTAGNLRTHQKTHRGEYTFVCNQEGCGKAFLTSYSLRIHVRVHTKEKPFECDVQGCEKAFNTLYRLKAHQRLHTGKTFNCESEGCSKYFTTLSDLRKHIRTHTGEKPFRCDHDGCGKAFAASHHLKTHVRTHTGERPFFCPSNGCEKTFSTQYSLKSHMKGHDNKGHSYNALPQHNGSEDTNHSLCLSDLSLLSTDSELRENSSTTQGQDLSTISPAIIFESMFQNSDDTAIQEDPQQTASLTESFNGDAESVSDVPPSTGNSASLSLPLVLQPGLSEPPQPLLPASAPSAPPPAPSLGPGSQQAAFGNPPALLQPPEVPVPHSTQFAANHQEFLPHPQAPQPIVPGLSVVAGASASAAAVASAVAAPAPPQSTTEPLPAMVQTLPLGANSVLTNNPTITITPTPNTAILQSSLVMGEQNLQWILNGATSSPQNQEQIQQASKVEKVFFTTAVPVASSPGSSVQQIGLSVPVIIIKQEEACQCQCACRDSAKERASSRRKGCSSPPPPEPSPQAPDGPSLQLPAQTFSSAPVPGSSSSTLPSSCEQSRQAETPSDPQTETLSAMDVSEFLSLQSLDTPSNLIPIEALLQGEEEMGLTSSFSK