wanglab/gogpt-training-data huggingface dataset:
Protein: Inactive tyrosine-protein kinase 7 (Protein chuzhoi) (Protein-tyrosine kinase 7) (Pseudo tyrosine kinase receptor 7) (Tyrosine-protein kinase-like 7) (Q8BKG3)
Organism: Mus musculus (Mouse)
Function: Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis.
Subcellular location: Membrane; Single-pass type I membrane protein. Cell junction {ECO:0000250}. Note=Colocalizes with MMP14 at cell junctions. Also localizes at the leading edge of migrating cells.
Interaction partners:
- Protein Wnt-5a
- Segment polarity protein dishevelled homolog DVL-1
- Periostin
- Low-density lipoprotein receptor-related protein 6
- Protein Wnt-2
- Protein Wnt-4
- Vang-like protein 2
- Low-density lipoprotein receptor-related protein 5
- Protein Wnt-11
- Frizzled-2
Sequence:
MGARPLTLLRALLLPLLAGAQAAIVFIKEPSSQDALQGRRALLRCEVEAPDPVHVYWLLNGVPVQDTERRFAQGSSLSFAAVDRLQDSGAFQCVARDNVTGEEVRSTNASFNIKWIEAGPVVLKHPASEAEIQPQTQVTLRCHIDGHPRPTYQWFRDGTPLSDDQSTHTVSSRERNLTLRPASPEHSGLYSCCAHNAFGQACSSQNFTLSVADESFARVVLAPQDVVVARNEEAMFHCQFSAQPPPSLQWVFEDETPITNRSRPPHLRRAVVFANGSLLLTQVRPRNAGVYRCIGQGQRGPPIVLEATLHLAEIEDMLPFEPRVFIAGDEERVTCPAPQGLPTPSVWWEHAGVPLPAHGRVHQKGLELVFVTIAESDTGVYTCHASNLAGQRRQDVNITVATVPTWLRKPQDSQLEEGKPGYLHCLTQATPKPTVIWYRNQMLISEDSRFEVSKNGTLRINSVEVYDGTLYRCVSSTPAGSIEAQARVQVLEKLKFTPPPQPQQCMEFDKEATVPCSATGREKPTVKWVRADGSSLPEWVTDNAGTLHFARVTRDDAGNYTCIASNEPQGQIRAHVQLTVAVFITFKVEPERTTVYQGHTALLRCEAQGDPKPLIQWKGKDRILDPTKLGPRMHIFQNGSLVIHDVAPEDSGSYTCIAGNSCNIRHTEAPLLVVDKPVMEDSEGPGSPPPYKMIQTIGLSVGAAVAYIIAVLGLMFYCKKRCKAKRLQKQPEGEEPEMECLNGGPLQNGQPSAEIQEEVALTSLGSGPPATNKRHSAGDRMHFPRASLQPITTLGKSEFGEVFLAKAQGVEEGATETLVLVKSLQSRDEQQQLDFRREVEMFGKLNHANVVRLLGLCREAEPHYMVLEYVDLGDLKQFLRISKNKDEKLKSQPLSTKQKVALCSQVALGMEHLSNNRFVHKDLAARNCLISAQRQVKVSALGLSKDVYNSEYYHFRQAWVPLRWMSPEAVLEGDFSTKSDVWAFGVLMWEVFTHGEMPHGGQADDEVLADLQAGKARLPQPEGCPSKLYRLMQRCWAPNPKDRPSFSEIASTLGDSPADSKQ
Protein: Major facilitator superfamily (MFS) profile domain-containing protein (G8BL03)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTTTESIASDIEKGGITSHHENLDPVALTEELDPEHHKYLISRHGSVQLDPLPSADPEDPLNWPDWQKNYEILLIAFGTFSSTFMAAGLTPAFETMAEEYGVDLPTAAYFTSAQIAVFGVLPLFWVPLMNAYGRKPFLTVAALACCILNIGGGFAKTYGQQMATRVLVAVFVSAVTAAGSSVVGDLAFAHERGKKNGWWSLALLIGTPGGPFFTGFIQQHAGTKWIFFVFAIMNFIQFVLWIFARETIYTRASPEYYSQGLLKVVGIRKSSSRPFSWKMFFRPLKQAANLNITIAVIAASVTFCYANIVLVVEMPQVMVPLFHLDAQQMSLQYISIIIGSIIGEVLAGPLSDWWMRRSTAKRNGQRVIADRLWVCYNGYILVIVGLLVWGIYLFKATPGHWSIKPLVGAAIAAAGNNIVATVVTTFAIDNAPHKAGDVGLYINFVRSLFGFLGPFYFPDMFENLNFAGSAGLMCGLVLLFAWVPTVVVHFIGARRAIKA
Protein: UfSP1/2/DUB catalytic domain-containing protein (Q580A1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin-fold modifier 1
- Ubiquitin-fold modifier-conjugating enzyme 1
Sequence:
MATVANEFATLDEGVLPILVVRKNGKTIAVVRDNSLQGTFLPFYLPTCETLHVSRTEELQEARESGVLNVAAVEWPVVAKLRMALGILKEERYWLLFSRGGVSNEGLTSHMFKGDEEGVHDAVSWLSGFQLSGPCDILLASEPSVTNGPANGDVGRLRLKKEDEDVNERVVFGESATDVARYIGDLLRAHLFQNVTAPTAVFWPPQLVHPVNIHYGMANRRVLEHDALLLPILSLFRVEKRLKNWDAVKGLQVSAGCDMPRTGQAWEKHLVRNIHKSLKEYIPVSGGEVYITSGSYDYYHYLIDGFKDSGWGCAYRSLQTILSWFQYEGLMQGAIPSIHTIQEILSVKDTDKMNRKGFVGSKDWIGSFEIMIVLQHYIPGLDCTIRRMESGAELETNPEIQALLAEHFRGKRSCPVMIGGSSYAHTILGVDMNLATTEARYLIADPHYASNETSTKTVVSKGYVGWKEARNFFEANSWYNLCIPQVATFDPR
Protein: Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease alpha) (P-55) (Q9DC61)
Organism: Mus musculus (Mouse)
Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P20069}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q10713}.
Interaction partners:
- Mitochondrial-processing peptidase subunit beta
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Cytochrome b-c1 complex subunit 7
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
Sequence:
MATAVWAAARLLRGSAVLCARPRFGSPAHRRFSSGATYPNIPLSSPLPGVPKPIFATVDGQEKFETKVTTLDNGLRVASQNKFGQFCTVGILINSGSRYEAKYLSGIAHFLEKLAFSSTARFDSKDEILLTLEKHGGICDCQTSRDTTMYAVSADSKGLDTVVDLLADVVLHPRLTDEEIEMTRMAVQFELEDLNMRPDPEPLLTEMIHEAAFRENTVGLHRFCPVENIAKIDREVLHSYLKNYYTPDRMVLAGVGVEHEHLVECARKYLVGAEPAWGAPGTVDVDRSVAQYTGGIIKVERDMSNVSLGPTPIPELTHIMVGLESCSFLEDDFIPFAVLNMMMGGGGSFSAGGPGKGMFSRLYLNVLNRHHWMYNATSYHHSYEDTGLLCIHASADPRQVREMVEIITKEFILMGRTVDLVELERAKTQLMSMLMMNLESRPVIFEDVGRQVLATHSRKLPHELCTLIRNVKPEDIKRVASKMLRGKPAVAALGDLTDLPTYEHIQAALSSRNGHLPRSYRLFR
Protein: Cryptic outer membrane porin BglH (P26218)
Organism: Escherichia coli (strain K12)
Function: Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin.
Subcellular location: Cell outer membrane {ECO:0000305|PubMed:10027967}; Multi-pass membrane protein {ECO:0000305|PubMed:10027967}. Note=Can be easily removed from the outer membrane by treatment with detergent.
Interaction partners:
- Uncharacterized protein YieL
- Uncharacterized protein YieK
- 6-phospho-beta-glucosidase BglB
- PTS system beta-glucoside-specific EIIBCA component
- Uncharacterized protein YciQ
- Cryptic beta-glucoside bgl operon antiterminator
Sequence:
MFRRNLITSAILLMAPLAFSAQSLAESLTVEQRLELLEKALRETQSELKKYKDEEKKKYTPATVNRSVSTNDQGYAANPFPTSSAAKPDAVLVKNEEKNASETGSIYSSMTLKDFSKFVKDEIGFSYNGYYRSGWGTASHGSPKSWAIGSLGRFGNEYSGWFDLQLKQRVYNENGKRVDAVVMMDGNVGQQYSTGWFGDNAGGENYMQFSDMYVTTKGFLPFAPEADFWVGKHGAPKIEIQMLDWKTQRTDAAAGVGLENWKVGPGKIDIALVREDVDDYDRSLQNKQQINTNTIDLRYKDIPLWDKATLMVSGRYVTANESASEKDNQDNNGYYDWKDTWMFGTSLTQKFDKGGFNEFSFLVANNSIASNFGRYAGASPFTTFNGRYYGDHTGGTAVRLTSQGEAYIGDHFIVANAIVYSFGNDIYSYETGAHSDFESIRAVVRPAYIWDQYNQTGVELGYFTQQNKDANSNKFNESGYKTTLFHTFKVNTSMLTSRPEIRFYATYIKALENELDGFTFEDNKDDQFAVGAQAEIWW
Protein: Cytochrome bd-II ubiquinol oxidase subunit 2 (EC 7.1.1.3) (Cytochrome bd-II oxidase subunit II) (P26458)
Organism: Escherichia coli (strain K12)
Function: A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Cytochrome bd-II ubiquinol oxidase subunit 1
- Cytochrome bd-I ubiquinol oxidase subunit 1
- Putative cytochrome bd-II ubiquinol oxidase subunit AppX
- Phytase AppA
- Glutathione/L-cysteine transport system ATP-binding/permease protein CydD
- Hydrogenase 1 maturation protease
- Cytochrome bd-I ubiquinol oxidase subunit X
- Cytochrome bd-I ubiquinol oxidase subunit 2
- Hydrogenase-1 operon protein HyaF
- Probable Ni/Fe-hydrogenase 1 B-type cytochrome subunit
Sequence:
MFDYETLRFIWWLLIGVILVVFMISDGFDMGIGCLLPLVARNDDERRIVINSVGAHWEGNQVWLILAGGALFAAWPRVYAAAFSGFYVAMILVLCSLFFRPLAFDYRGKIADARWRKMWDAGLVIGSLVPPVVFGIAFGNLLLGVPFAFTPQLRVEYLGSFWQLLTPFPLLCGLLSLGMVILQGGVWLQLKTVGVIHLRSQLATKRAALLVMLCFLLAGYWLWVGIDGFVLLAQDANGPSNPLMKLVAVLPGAWMNNFVESPVLWIFPLLGFFCPLLTVMAIYRGRPGWGFLMASLMQFGVIFTAGITLFPFVMPSSVSPISSLTLWDSTSSQLTLSIMLVIVLIFLPIVLLYTLWSYYKMWGRMTTETLRRNENELY
Protein: Sperm acrosome-associated protein 7 (Q96KW9)
Organism: Homo sapiens (Human)
Function: Involved in fertilization. Seems not to play a direct role in sperm-egg binding or gamete fusion.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9D2S4}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:22495889}. Cytoplasmic vesicle, secretory vesicle, acrosome lumen {ECO:0000250|UniProtKB:Q9D2S4}. Note=Localized in perinuclear pro-acrosomal granules in round spermatides. Localized between the inner and outer acrosomal membranes (matrix or lumen) in spermatozoa. Secreted during acrosome exocytosis. {ECO:0000250|UniProtKB:Q9D2S4}.
Interaction partners:
Sequence:
MAVSQGDGTLCFVLLLCCWQETELRPRTVIPGSPTEIPFSSKQEDMSELLDEILVQEILDLNKTTPSEMPSTASTLSTPLHAGIDENYQAGGSENYHELLENLQFSPGIEVKISNDEANANANLHGDPSENYRGPQVSPGSEKSVSSKEKNSKNTQYENLSILDQILQNIGRSSGNIFHKEQQRTSAQRRSQGSQ
Protein: Phosphatidylinositol 4,5-bisphosphate 5-phosphatase INP51 (EC 3.1.3.36) (Synaptojanin-like protein 1) (P40559)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Controls the cellular levels and subcellular distribution of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Does not utilize phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), nor phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in endocytosis and acts as a negative regulator of the Slm pathway which modulates polarized actin assembly and growth.
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Polyphosphatidylinositol phosphatase INP52
- Polyphosphatidylinositol phosphatase INP53
- Phosphatidylinositol 4-phosphate 5-kinase MSS4
- Phosphatidylinositol 4-kinase STT4
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol 4-kinase PIK1
- Probable phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase TEP1
- Phosphatidylinositol 4-kinase LSB6
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1
- Increased rDNA silencing protein 4
Sequence:
MRLFIGRRSRSIVISSNNYCLSFQRLRSIPGASSQQRQLSKTPSVTIKSYPDTDLSSDSNYLEVKSCIFNGLLGLVCLNGDIYVAVISGVQNVGFPRWKLIDHQVRPSESIYKVLDVDFYSLENDVFDYLLCERSEQNYDKLIHEHPCGPLKKLFSDGTFYYSRDFDISNIVKNHGLSHNLEYTVDNQDLSFIWNANLASEVINWRSKISNEEKQLFANAGFLTFVIRGYCKTALIEDGPNTASITIISRISTESKQDTLELEGISEDGRVSLFVETEIVVTTEKFIFSYTQVNGSIPLFWESVESQLLYGKKIKVTKDSIEAQGAFDRHFDNLTSKYGVVSIVNIIKPKSESQEKLALTYKDCAESKGIKITNIEYSSSVLTKSPHKLLYLLKQDIYEFGAFAYDISRGIYFAKQTGVLRISAFDSIEKPNTVERLVSKEVLELTTNEIDVFELTSPFLDAHDKLWSENYYWLDRTYTKHTKNSGKYTKVYSKLFGSRVRLYDPLHIYISQYLKQLRSKYTFEKDISIFAGTFNISGKIPKDDIKDWIFPKSMSKEDEMADLYVIGLEEVVELTPGHMLATDPYVRQFWEKKILTLLNGPGRKKKYIRLWSTQLGGILLLLFMNETEYSKVKHIEGDVKKTGFGGMASNKGAVAVSFKYSATRFCVLVSHLAAGLENVEQRHNDYKTIAKSIRFSKGLRIKDHDAIIWMGDFNYRILMSNEDVRRKIVSKEYASLFEKDQLNQQMIAGESFPYFHEMAIDFPPTYKFDPGTKNYDTSEKMRIPAWTDRILSRGEVLEQLEYKCCEDILFSDHRPVYAIFRARVTVVDEQKKTTLGTQIYEKIMERLEGLDDDEKIAVLSDDAFVIESFEGSDSIAGPTHSPTPIPEPKRGRKLPPPSSDLKKWWIGSGKQVKVVLDVDPAVYMINPKRDPNPFVENEDEPLFIER
Protein: ATP synthase F(0) complex subunit e, mitochondrial (ATPase subunit e) (ATP synthase membrane subunit e) (P29419)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit ATP5MPL, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MVPPVQVSPLIKFGRYSALILGMAYGAKRYSYLKPRAEEERRIAAEEKKRLDELKRIERELAEAEDVSIFK
Protein: Acetyl-CoA carboxylase, putative (EC 6.4.1.2) (Q57YR7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Biotin--acetyl-CoA-carboxylase ligase, putative
- Acetyl-coenzyme A synthetase
- Malonyl-CoA decarboxylase, mitochondrial, putative
- Dihydrolipoamide acetyltransferase, putative
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Citrate synthase
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Fatty acid desaturase, putative
Sequence:
MSLSSPVTTMRPQLHGMKELCRFLGGKRPIERLLIANNGLAAVKGIDSVRSWLYVHTGNTEAVEFTVMATPEDLHANAEFISLSDRHVAVPGGPNRNNYANVDIIMQTAVQNSCNAIYPGWGHASENPALPRECVKTGERVIFLGPSAKAMFALGDKIASTIVAQSNGVPTVPWSGDEILLPPGVFEVDPLVYEKAYISTAEECEELCGRLGFPVMIKASEGGGGKGIRRCLRKEDVRDMFFAVAEEVKGCHIFVMRMLENVRHLEVQLLADDYGDCIAVHTRDCSVQRRHQKIIEEGPVFGVDASIINDMEAAAVRLAKAVKYRGLGTVEYMYDKSTQKFFFLELNPRIQVEHPVSELVSGVNLPAALLCVGMGVPLHRIPEVRTFFGEQPYDTSPIDFTRRRCLAAKGHTIAVRVTAEDTDEGFRPTSGRVEEIAFKNSKECWGYFSVGAGGEIHQFADSQFGHIFSSAETREEARRGMVMALRNLVIRGEIHTSVSYVLGLLERPEFCNCDVSTDWLDRLISARILQSAQHNQQDVYIALTAACTLRMLSKRDENHGRYVSFLSAGHVPTTEFLSNYESESYVNRSTNFNVTMGLTSPTEISISLNGSVISVPFRKLKSGALQLRVGGKTAIAYAEKEPSSLRISIGGKETTFTGDIDPTKLFAAVPGRFVRYLVCDGGHVEEGTIVAEVEVMKMILPLRASTVGALHHKVAPGSTIALGTLVAEITPDDPSKVARPREATEPWPPELLDAADKEDQMERLDSLARARRGAEALWNMLRGYHFSGIPLDRRLKSAFSDLGALSLSSVSLTALNLPFISERVVGSDHATPNYKLRVVLETLISEYVEVERSFVRCNRQEAIHQVRETTGDTRKVFEIDFAHNQPSHHGVIKAVLNTLENNMVLLKSLMPSLSTLVNLRSTGDGTLQMQARYLLRQCSLPSFVERKIAFTRELEEGSMMDLIQGSYGTDLLCATMFDRQVPHLIQLCLEFHVQREYFGQSRITNLDVCTRDGCWYCYYEYEPLEEHDPLLAGVLHCHAPDATAGSAENQGAGVVLMLPDVKVLQKTWAETLNLNLQQTSRCPSVCTVFVSVCRQFTEEEVARLCEGALRDNAEALRQHVKLERVTFIVHGVDRGPRTFTYRSAHDWREDTLIRNVAPLSARRLELQRLENYDVVMYPTPFKEIHVFHATPKKKSVSFLEHRIFARACVTPRDLGVAPWTVMNEIDAGHMFDICLDALDVIRSDSTIKYPKHNHLFIKMVELTFDLSSLRKVLSQVGKSYKWRTMHLGVAEVELSFLLPVSSGYVPFRVIVSSSSGASAAMRIYHEWNEGGKPCLRRAQNSEDILMNSLYTSSDSVQEQAADAQKVEPPSGCPAGAVGGTLTRALAKLEALRSLLPSRGDEGDAIDDGEECIPLQPYPLLNAKQLKRLQAWMIHTVYVHDWPELLQYALREEWKQHARGRRFPLSRIPPSVLKATELYLDPADKKTLLEEKPQGHVPCGVIVWLVDINPPSYYDSESNIAGSRRFVMVANDITFQSGSFAVPEDDVFSAASVLARQLRIPFVYISANSGARIGLSAEVKKRFRVAFNDAEEAEYLYLVQSDYDELVSRGVRLAVEKLEPRQVEGDEGGEVRYVIRGVVGGTEEYLGVENLRGSGLIAGHMSKNYSNVPTISIVTGRSVGIGAYLNRIGRRVIQTGDAPLILTGAAALNRLLGKEVYSDNSQLGGRQVMVPNGVTHWYAKNNRLAAETLLRWLDYVPPVVHPLRCSPRILALRQPDPIDRDVTYEPSGVESYDPRGLVRGVGDKLGLFDRDSWVESLEGWAKTVVTGRATLGGIPCGIVLVETRPTRKCKPADPADPTSSEAFVAQAGQVWFPDSARKTADALDDFHRERLPCFIFANWRGFSGGMRDMFEEVLKFGASIVDNLRVYNCPVFIYIPPRGELRGGAWVVVDPSINHCGAVEMYCDGSARGGVLEAAGIAEIKFREADVRELIRRNEPRLRSLSPDHRHAEENRLLPRYNDVALRFADLHDTHVRMEATGVVRGVIPWKDSRRRFYEKLQRKLKELSLAATLVERRMAGDLADGVRYLEQAFAQKHPGVLWGSDDALQLQWLIEYESELNVSTHNIVSPTSASAEILEALRRHVPLHGEQNEAGEGLEGCFEELFKDERMRRAAMQALERTTAK
Protein: Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH 1) (EC 1.2.1.12) (P78958)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Fructose-bisphosphate aldolase
- Transaldolase
- Probable transketolase
- Glucose-6-phosphate isomerase
- Response regulator mcs4
- Probable phosphoketolase
- Glucose-6-phosphate 1-dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase 2
Sequence:
MAIPKVGINGFGRIGRIVLRNALVAKTIQVVAINDPFIDLEYMAYMFKYDSTHGRFDGSVEIKDGKLVIDGNAIDVHNERDPADIKWSTSGADYVIESTGVFTTQETASAHLKGGAKRVIISAPSKDAPMYVVGVNEEKFNPSEKVISNASCTTNCLAPLAKVINDTFGIEEGLMTTVHATTATQKTVDGPSKKDWRGGRGASANIIPSSTGAAKAVGKVIPALNGKLTGMAFRVPTPDVSVVDLTVKLAKPTNYEDIKAAIKAASEGPMKGVLGYTEDAVVSTDFCGDNHSSIFDASAGIQLSPQFVKLVSWYDNEWGYSRRVVDLVAYTAAKDN
Protein: Luciferin 4-monooxygenase (Luciferase) (EC 1.13.12.7) (Q26304)
Organism: Luciola mingrelica (Southern Russian firefly)
Function: Produces green light with a wavelength of 570 nm.
Subcellular location: Peroxisome {ECO:0000250}.
Interaction partners:
Sequence:
MEMEKEENVVYGPLPFYPIEEGSAGIQLHKYMHQYAKLGAIAFSNALTGVDISYQEYFDITCRLAEAMKNFGMKPEEHIALCSENCEEFFIPVLAGLYIGVAVAPTNEIYTLRELNHSLGIAQPTIVFSSRKGLPKVLEVQKTVTCIKKIVILDSKVNFGGHDCMETFIKKHVELGFQPSSFVPIDVKNRKQHVALLMNSSGSTGLPKGVRITHEGAVTRFSHAKDPIYGNQVSPGTAILTVVPFHHGFGMFTTLGYFACGYRVVMLTKFDEELFLRTLQDYKCTSVILVPTLFAILNKSELIDKFDLSNLTEIASGGAPLAKEVGEAVARRFNLPGVRQGYGLTETTSAFIITPEGDDKPGASGKVVPLFKVKVIDLDTKKTLGVNRRGEICVKGPSLMLGYSNNPEATRETIDEEGWLHTGDIGYYDEDEHFFIVDRLKSLIKYKGYQVPPAELESVLLQHPNIFDAGVAGVPDPDAGELPGAVVVMEKGKTMTEKEIVDYVNSQVVNHKRLRGGVRFVDEVPKGLTGKIDAKVIREILKKPQAKM
Protein: Molybdenum storage protein subunit alpha (Mo storage protein subunit alpha) (MoSto subunit alpha) (P84308)
Organism: Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Function: Intracellular storage of molybdenum. Binds polyoxomolybdates. Can bind at least 90 molybdenum atoms per protein molecule.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15651045}.
Interaction partners:
- Molybdenum storage protein subunit beta
- Ribosome-recycling factor
- Elongation factor Ts
- Small ribosomal subunit protein uS2
- Uridylate kinase
- Phenylalanine--tRNA ligase beta subunit
- DUF2023 domain-containing protein
Sequence:
MTDTTNSIKHVISPLARQTLQDRDLTRPVAGKRPIRLLPWLQVVKIGGRVMDRGADAILPLVEELRKLLPEHRLLILTGAGVRARHVFSVGLDLGLPVGSLAPLAASEAGQNGHILAAMLASEGVSYVEHPTVADQLAIHLSATRAVVGSAFPPYHHHEFPGSRIPPHRADTGAFLLADAFGAAGLTIVENVDGIYTADPNGPDRGQARFLPETSATDLAKSEGPLPVDRALLDVMATARHIERVQVVNGLVPGRLTAALRGEHVGTLIRTGVRPA
Protein: Replication protein A 70 kDa DNA-binding subunit (RP-A p70) (Replication factor A protein 1) (RF-A protein 1) (D8UYN9)
Organism: Tetrahymena thermophila (strain SB210)
Function: As part of the heterotrimeric replication protein A (RPA) complex, binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress (By similarity). It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism (By similarity). Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (By similarity). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation (By similarity).
Interaction partners:
Sequence:
MVTQLTKNAIDSLINSTNPDEQYVIQVLKAPQSVAENLFKICISDGFCKFKKGYFVSDAATKCQDLKDLCIIKCKKYIDDSNHDKERIIISNYELIYSNIQEQIGKPIEYKQYKSSGFSNPEGSTVIPSQYLSRNAQILQQNQVSQPKQMVTPPVSNINKPTPAVNNTFAQKPAVTNQNIQRVNQNPQQMNKTAPVKQNNNNNNNNNGNNKNNSSLQISTDGDEQNLEYIRNLQPNGQPQTIKVRITKKGDLKSFKEKQGKLFSIDVIDKFGDECSISFFNEIAEQYDGLFKVGQVIVLKQFSVKVNNNHQYNKGDHTVTVNKESKILICQEDPSIPMIKLNRQFIQDMQNKQKGDLIDLIVVVKADTEVKTMILKKDNQQQSKRDIISFDESLIETEITLWGETAKDYDAKQGDIIVFKDAKIGEFKDKKQINIGYGTQIFMNPDEQLFPQIHDVKKWYLSLNSDQLSTIQKAQGNDTGPREVTSFESSLNILKEEIKNLQTDPEMKIWKEIRGQIMYIKDTPLYYNACFSCKKKIARNNEVWTCINCNKDFNEPDSRYILSLNISDSTDTIWVSAFDEVGQKILGVKGDVFRYADEDTEHGTETKKKLLMAAQNKEYRFLLLTKQERDQNGNARDKTVIHAIKDFQPAYEAKKIINSLEKFMVIEENNP
Protein: Cytosolic iron-sulfur assembly component 2B (H3BNV7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XVGGGGVGGGLLENANPLIYQRSGERPVTAGEEDEQVPDSIDAREIFDLIRSINDPEHPLTLEELNVVEQVRVQVSDPESTVAVAFTPTIPHCSMATLIGLSIKVKLLRSLPQRFKMDVHITPGTHASEHAGPECVRLQQRRRQPGGGILRRQISEQATCR
Protein: Uncharacterized protein C895.08c (O94535)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDNSRDKIHILGAVSDTFQEVQHPCSILKYKVYFVTTDTFYCKYLTASFTGLKKFPTERQLPLECHFNHIDWDLGNNFKVKEGVFYTFDIIAPLPRCTPRTIVTQEGSISYKLTVKLYTEDDCRMPKSANVPVVVPFTLNPDRIPESQHIRYGAPLNDACFTSLSMKSSKYSFLTAFFKYPQQCYKGPGCVCPLLIDLESEDADVLSSTPGSAGTDDPHIDPIAINSQDSQFIFQDRLPRLSNDCDMKGRSSLSRTSSPVVEKKLKRYYIRVLLVQSITFFLFNDAFRNSITVLFEDGKWSPPIVPGLHSRVEFTIPVNDLIHGSCTENPHLLVRHSIYVSIHSREPSSLSRKLAPPFLRTHKAKSNSLFSMKRPSSSSSSLSGSWHGDTENSVKQSLASPSEASLPNLSKYSRKNAKKLNEWLDSLDFKLPIYLFHRKLESELSHLPPYSPYRDSYFYLEDDDGDADTPSTASLDYFSNISPPDFLNKA
Protein: p-hydroxybenzoate hydroxylase (PHBH) (EC 1.14.13.2) (4-hydroxybenzoate 3-monooxygenase) (P20586)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.
Interaction partners:
- Protocatechuate 3,4-dioxygenase, beta subunit
- Protocatechuate 3,4-dioxygenase, alpha subunit
- Thioesterase domain-containing protein
- catechol 1,2-dioxygenase
- 3-dehydroshikimate dehydratase
- Probable transcriptional regulator
- Vanillate O-demethylase oxygenase subunit
- 4-carboxymuconolactone decarboxylase
- Vanillate O-demethylase oxidoreductase
- 4-hydroxyphenylacetate 3-monooxygenase reductase component
Sequence:
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
Protein: Keratin, type II cuticular Hb5 (Hair keratin K2.12) (Keratin-85) (K85) (Type II hair keratin Hb5) (Type-II keratin Kb25) (P78386)
Organism: Homo sapiens (Human)
Interaction partners:
- Keratin, type I cuticular Ha5
- Keratin-associated protein 11-1
- Keratin, type II cytoskeletal 71
Sequence:
MSCRSYRISSGCGVTRNFSSCSAVAPKTGNRCCISAAPYRGVSCYRGLTGFGSRSLCNLGSCGPRIAVGGFRAGSCGRSFGYRSGGVCGPSPPCITTVSVNESLLTPLNLEIDPNAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKWQFYQNQRCCESNLEPLFSGYIETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLRRLYEEEIRVLQAHISDTSVIVKMDNSRDLNMDCIIAEIKAQYDDVASRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHRLCEGVGSVNVCVSSSRGGVSCGGLSYSTTPGRQITSGPSAIGGSITVVAPDSCAPCQPRSSSFSCGSSRSVRFA
Protein: CD40 molecule, TNF receptor superfamily member 5 (TNFR superfamily member 5) (Tumor necrosis factor receptor superfamily member 5 precursor) (B8X730)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- CD154
- CD83 molecule.
- TNF receptor-associated factor
- TNF superfamily member 11
- Interleukin family protein
- TNF superfamily member 13b
- Tumor necrosis factor ligand superfamily member 6
- Lymphotoxin-alpha
- TNF receptor-associated factor 6
- CD28 molecule.
Sequence:
MTVILRVCLLVTLICLVSCCEKETHYTNSQGKCCKMCGPGTRMMKDDNCDDPRCKECEVGEYQSGYTKETICERQPSCDTNLNFLPQMNSNKTSRNECQCKPGYYCDLDHGCEVCRKHTVCEPGQRVAVKGSPIRDNVCEECSDGTFSTNHSADTCKEWTKCEYGEVDTPGSSTSDQTCVGTRDRTAVIVVVCVLLILIAAAALVGCLFFKKGKSPLFKLQKQTFMEIRPDDDVTIAVQQQPEEEDENAPVSPTLSNMTENGNFVVQEHGKDAIIPCHESTSNTYQ