wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (Q67YS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transcription factor bHLH121
Sequence:
MEDTTFTKVFVGGLAWETHKVSLRNYFEQFGDIVEAVVITDKSSGRSKGYGFVTFCDPEAAQKACVDPAPVIDGRRANCNLAAFGVQRSKPSSPIHGHVGGRGMKVTSPFKTHFGTAATAIPSPLPFSHYTLPYTNPFGFSSYSMDYNYPTQSYYNVYGGATAQHPMYGSGPMTGVAAAPAAGFYPYLQFAEGNGPVTGYAPLHYPNHMFHYSAPGGNYPHHNGSPVSLAPSPVIPSVCFAVPQA
Protein: rRNA 2'-O-methyltransferase fibrillarin 1 (AtFbr1) (AtFib1) (EC 2.1.1.-) (Fibrillarin-like protein 1) (Histone-glutamine methyltransferase) (SKP1-interacting partner 7) (Q9FEF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins (Probable). Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (Probable). Site specificity is provided by a guide RNA that base pairs with the substrate (Probable). Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (Probable). Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity). Binds monophosphate phosphoinositides in vitro.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10806224, ECO:0000269|PubMed:10829025}. Note=Localizes to the fibrillar region of the nucleolus. {ECO:0000305}.
Interaction partners:
- Nucleolar protein 56
- Nucleolar protein 56
- H/ACA ribonucleoprotein complex subunit 2-like protein
- Nucleolar protein
- Periodic tryptophan protein 2
- rRNA biogenesis protein RRP5
- Probable nucleolar protein 5-2
- Probable nucleolar protein 5-1
- Uncharacterized protein At3g06530
- Putative nucleolar protein 5-3
Sequence:
MRPPVTGGRGGGGFRGGRDGGGRGFGGGRSFGGGRSGDRGRSGPRGRGRGAPRGRGGPPRGGMKGGSKVIVEPHRHAGVFIAKGKEDALVTKNLVPGEAVYNEKRISVQNEDGTKVEYRVWNPFRSKLAAAILGGVDNIWIKPGAKVLYLGAASGTTVSHVSDLVGPEGCVYAVEFSHRSGRDLVNMAKKRTNVIPIIEDARHPAKYRMLVGMVDVIFSDVAQPDQARILALNASFFLKTGGHFVISIKANCIDSTVAAEAVFQSEVKKLQQEQFKPAEQVTLEPFERDHACVVGGYRMPKKQKTPAS
Protein: Uncharacterized protein C11E3.02c (O13683)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C1F5.05c
Sequence:
MNCRRKPLPLHSNEVQAAESISKDELYSWTLKNVLILFLVQYRASTPSALQTSSFSTPVEKKTNGAFSGSLFSAKEKKDNPKYPKDFIKYLSLALESISMGKEPEYQDQLIRGCFAAFYNNINKSHISKQLKDSRKIEDMFLIFASSVSSELTKRLGTAYDSNLADRITASFIELCKRVTLKGQLASPSSEFVSHLDMYHSKLLNKSEILSTKRVNRGQDQFDLSSFPLLKVFSSVFKVAYSKALLDAEKLFPSIDEAAIAEDIGILIEDLESDACKFSHSVVDFSNYKSYSTWKARELQTLEQHRKIMLSLIPLSSSPNHPIQPIGFPASRKTPTYVPPIARPYFRQLLSLCLEYRLQVTDPVEVKQINTFIRECSIYWRILPSTRCALSMDFAREHLQKGLITSADVLTHFGELHKSLKEWEITYWPKIDVSIFSSALFGIRNALAQLLKKSLLDLLHEKKADFHRWLNIMSICVEDGKVINQDLSPKSEISSVALALQEHCKVIFDEEFDLSKLPSSNFLDEIILASNRISVRIKFLERNCSECIYGVLSLPQIFINIVLPNYIRAALVVAKEYLREKANADINDLTKDMLEIYSDLKQMIHVLQEYHNEEYRIGSFEGFFQPFIDSWLDNVEASAEQWFLRSLEKDNFDENSSEGQYSSSIVDLFHAFHQAFRTLEGFEWEDDLANARFFTRFFRVIYIVLSKYTQWTTQKFFEEANKQDDTSEVQNDNSSSWFSKARNILSGSNEVLPFRFSPTMCILLNNIHFAMHAYEELEQKIDLQRLIEALDVAESTKRHKISATNYLYTIKVVRGEGLHPDGAGKIRTSYIVLTDNKGRRIGKTRPIHSMNPRWDDTFEVKTKDALMITANLWSKGKFNDHEIFGRSSFTLSPKIYGDYLPREEWFDLNPHGELLLRIEMEGEREHIGFYVGRTYHDLERAQREMIKFIVNKMEPVINQNLSTATLKKLLSANTWMDLDKTMTSVTSLLNRTGFSSKSSENVKKEGELTDVQIEAAIYELLDYFDLNFSIIAKHLTKDVFVTVMSYVWDEVVCTTEELLLPPVSVKPINRKPLSPAQMAIVYRWLQFLKDYFYANGEGVKLPVLETDHYKELLRVQEYYDKPTDFLLQECDKIASQLYLSSRMVNNEPVESLPRHSRIKFANKEIYRSGTIRKVHIQTNESELERNERIILRILRMRADSKRFLSKHFQRKGRLLMADAMRNGYVMPLGHLKKLDSR
Protein: Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] (Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase) (C0H4F3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- CTP synthase
- Inosine triphosphate pyrophosphatase
- GTP cyclohydrolase 1
- nucleoside-diphosphate kinase
- Nucleoside diphosphate kinase
- pyruvate kinase
- Guanylate cyclase beta
- Pyruvate kinase
- NAD
- mRNA-decapping enzyme subunit 1, putative
Sequence:
MKINIIKAFGILLCRLKKYNPVTTGDINKFEFLFLKASYADKHWTPPKGLHENNESGLETAVRETLEETGINKDKYKLLNYQKTLKYNVKDKPKETTYYLAMLLNNEENVILSDEHTDYKWIGSHESDTYNLPESLADLLKEAEEFLNKEQL
Protein: Eukaryotic translation initiation factor 3 subunit B (eIF3b) (eIF-3-eta) (eIF3 p110) (p82) (Q9C5Z1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit D
Sequence:
MEVVDIDARAAKLGIDWSQVNFDSIQLPPGEDFGIESDDEAVYQDDQSEFDTGFGNIIVVDHLPVVPKEKFEKLEGVVKKIYNQLGVIKENGLWMPVDPDTKMTLGYCFIEFNTPQEAQNAKEKSHGYKLDKSHIFAVNMFDDFDRLMNVKEEWEPPQARPYVPGENLQKWLTDEKARDQLVIRSGPDTEVFWNDTRQKAPEPVHKRPYWTESYVQWSPLGTYLVTLHKQGAAVWGGADTFTRLMRYQHSMVKLVDFSPGEKYLVTYHSQEPSNPRDASKVEIKVFDVRTGRMMRDFKGSADEFSIGGPGGVAGASWPVFRWAGGKDDKYFAKLSKNTISVYETETFSLIDKKSMKVDNVVDICWSPTDSILSLFVPEQGGGNQPAKVALVQIPSKVELRQKNLFSVSDCKMYWQSSGEYLAVKVDRYTKTKKSTYSGFELFRIKERDIPIEVLELDNKNDKIIAFAWEPKGHRFAVIHGDQPRPDVSFYSMKTAQNTGRVSKLATLKAKQANALFWSPTGKYIILAGLKGFNGQLEFFNVDELETMATAEHFMATDIEWDPTGRYVATAVTSVHEMENGFTIWSFNGIMLYRILKDHFFQLAWRPRPPSFLTAEKEEEIAKTLKKYSKKYEAEDQDVSLLLSEQDREKRKALKEEWEKWVMQWKSLHEEEKLVRQNLRDGEVSDVEEDEYEAKEVEFEDLIDVTEEIVQES
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FUZ5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MSNLLNKISDKLHGNDDKEESNSSMSYNTSSNKNLDRDDYESGQSYGFNDSNNYDTNARSHEGYGQGGSNTMPSKHGDTYYNPNERTNDFSETRGMSGTTNLDTDDWGEDVEADVIDSKRYNKGSGAFPSYNSGNMNQNDEY
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (A0A8I6GJ67)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MADEEKLPSGWEKRMSRSSGRVYYFNHITNASQWERPSGGSTVGGGSKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRSKEEALELINGEQGQGSRGLLEGLFQLGQRAYLTFFSCSCDKVLLTRANKRVQQAKALAAKAAGLGSIPGCMWWRAHSWEFSHPTMECMLSCPNKSVQFNC
Protein: Pleckstrin homology domain-containing family M member 1 (PH domain-containing family M member 1) (Q7TSI1)
Organism: Mus musculus (Mouse)
Function: Acts as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. Acts as a dual effector of RAB7A and ARL8B that simultaneously binds these GTPases, bringing about clustering and fusion of late endosomes and lysosomes. Required for late stages of endolysosomal maturation, facilitating both endocytosis-mediated degradation of growth factor receptors and autophagosome clearance. Interaction with Arl8b is a crucial factor in the terminal maturation of autophagosomes and to mediate autophagosome-lysosome fusion. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. May be involved in negative regulation of endocytic transport from early endosome to late endosome/lysosome implicating its association with Rab7. May have a role in sialyl-lex-mediated transduction of apoptotic signals (By similarity). Involved in bone resorption.
Subcellular location: Autolysosome membrane {ECO:0000250|UniProtKB:Q9Y4G2}. Endosome membrane {ECO:0000250|UniProtKB:Q9Y4G2}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Y4G2}. Lysosome membrane {ECO:0000250|UniProtKB:Q9Y4G2}. Note=In case of infection colocalizes with Salmonella typhimurium sifA in proximity of Salmonella-containing vacuole (SCV). {ECO:0000250|UniProtKB:Q9Y4G2}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- Synaptosomal-associated protein 29
- Microtubule-associated protein 1 light chain 3 beta
- Osteopetrosis-associated transmembrane protein 1
- Vam6/Vps39-like protein
- V-type proton ATPase subunit a
- Syntaxin-17
- ADP-ribosylation factor-like protein 8B
- H
- Vesicle-associated membrane protein 8
Sequence:
MLSVENGLDPRAAIQVIKKKLVGSVKALQKQHVSLDTVVTSEDGDANTMCSALEAVFIHGLHAKHIRAEAGGKRKKHTHQKALPQPVFWPLLKAITHRHIVSDLEHLVFINTDVGRCRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFELSYKSAILNEWTLTPLSLSGLCPLSELDPLTTSGAELQRKESLDSISHSSGSEDIEVQHSGHKIRRNRKLTASSLSLDTASSSQLSCSLNSDSCLLQENGPKSPDHSEEPMSYDSDLGMANTDDPDRSLQEVLSEFSKAQVNSAPSSGPNQEPDTPMFQTPLSLHSLATSTHLHFEGSEELFPAHKSSGTSSGGHKHQLLPQETPDEKQLGTAQAGPAQSTSDQQPSSPVGGAAGQGSGPWKALEYGRVGPKLVVSSPTSPKGKSWISEDDFCRPPQEPALKSAAGLCTSPVQDTPESRAALHGPFSQGPRKSCSLGALDKACVPSQACGNAQPAPAPAPAPAPAPAPAPGVTQDHKNFCVVHRRQMGLSNPFRGLMKLGTVARRGAMGIWKEFFCELSPLEFRLYLSDEERTCVESCSLLRCEAVGPAHSDGRFELVFSGKKLALRASSQDEAEDWLDRVREALQKVRPQQEDEWVNIQYPDQAEDAPEAPPDSLPPYSTLLPEPAGAQGMQLDWTSAQVPEPDAIKESLLYLYADRTWVPYIFSLSLESLKCFRVRNNEKMLSDSHGVETIRDILPDTSLGGPAFFKIITAKAVLKLQAKNTEEATHWRDLVRKVLASYLESAEEAVTLGGSLDEKCQEVLKFATRENGFLLQYLVAIPTEKGLDSQGCFCAGCSRQIGFSFVRPKLCAFSGLYYCDFCHQDDASVIPARIIHNWDLTKRPVCRQALKFLAQIRAQPLINLQLVNASLYEHVERMHLIGRSREQLKLLGDYLGLCRSGALKELCKRLSHRNYLLESPHRFSVADLQQIAEGVYEGFLKALIEFASQHVYHCDLCTQRGFICQICHHQDIIFPFEFDTTVRCAECRTVFHQSCQAVVRKGCPRCARRRKYQEQNVVS
Protein: Translation initiation factor IF-2, mitochondrial (IF-2(Mt)) (IF-2Mt) (IF2(mt)) (P25038)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Subcellular location: Mitochondrion.
Interaction partners:
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL11m
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS17m
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL23
Sequence:
MLRRHGLFWLKTCPRLNVLLNQSIPIPHLLHSRDICQQRWYAKGKRRNQISKKELKPLNFSIPNYISVNKLANLLNCRVERLIKDLTALGFENITTTYILSKEYVELILQEYNFALPNLSTSTNLDNVYDELKSPVNPKLLTKRAPVVTIMGHVDHGKTTIIDYLRKSSVVAQEHGGITQHIGAFQITAPKSGKKITFLDTPGHAAFLKMRERGANITDIIVLVVSVEDSLMPQTLEAIKHAKNSGNEMIIAITKIDRIPQPKEREKKIEKVINDLIVQGIPVEKIGGDVQVIPISAKTGENMDLLEESIVLLSEVMDIRAENSPKTIAEGWIIESQVKKQVGNVATVLVKKGTLQKGKILICGNTFCKIKNLIDDKGIPILKATPSYATEVLGWKDVPHVGDEVIQVKSEAIAKKFISKRQDLIEVQKNSSIVEKLNEERALAKEQHLNKELEHENTVQEHEQNTGPKLINYIIKCDVSGSAEAVSESISSLGNDEVRCNVISSSVGIPTESDLKMAQITESTILCFNLGNLPSEVINNRAGIKIKQYNVIYKLIEDVTETLTENLKPIFEKKIVSTVDVRETFDFRLKKKIIRIAGCKVNNGVIKKNSLVQVVRGPNEDVIFDGKISTLKHNKDDVAEVSKGHECGITFESGFEGFKPGDKILVYENVRVPRYL
Protein: UDP-N-acetylglucosamine diphosphorylase (EC 2.7.7.23) (Q8IGT8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GCALVTTYSGTQQSPDNPTTVFLPHSPNNQSASGEKPGGATSKSPNAAKTSPTMTDYLSLHSRLAQVGQEHLLKFWPELTNDERIDLVRDIEELNLDEIKLYFDRATVSMNENGIKLDDRLQPLPEGKLISIARAPLEKLDAYRDEGLLQISNGHVAVLLMAGGQGTRLGFDHPKGMYDVGLQSRKTLFRIQAERILKLEELAQEANGKRGHITWYIMTSEHTVQPTYDYFVANNFFGLKAENVLLFEQGSLPCFEYDGRIILDEKHRVARAPDGNGGIYRAMKRQGILDDMQKRGVLYLHAHSVDNILIKVADPVFIGYCVQEKADCAAKVVEKAAPNEAVGVVAIVDGKYQVVEYSEISAKTAEMRNSDGRLTFSAGNICNHFFSSNFLQKIGSTYEQELKLHVAKKKIPFVDNAGKRLTPDKPNGIKIEKFVFDVFEFAQKFVAMEVPRDEEFSALKNSDAAGKDCPSTARSDLHRLHKKYIEGAGGIVHGEVCEISPFVTYAGENLASHVEGKSFTSPVYLRDSRDPLHGHL
Protein: Alkyl hydroperoxide reductase subunit F (EC 1.8.1.-) (Alkyl hydroperoxide reductase F52A protein) (P35340)
Organism: Escherichia coli (strain K12)
Function: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein.
Interaction partners:
- Alkyl hydroperoxide reductase C
- Catalase-peroxidase
- Catalase HPII
- DNA-binding transcriptional dual regulator OxyR
- Glutaredoxin 1
- Superoxide dismutase
- Superoxide dismutase
- Thioredoxin 1
- Thioredoxin 2
- Superoxide dismutase
Sequence:
MLDTNMKTQLKAYLEKLTKPVELIATLDDSAKSAEIKELLAEIAELSDKVTFKEDNSLPVRKPSFLITNPGSNQGPRFAGSPLGHEFTSLVLALLWTGGHPSKEAQSLLEQIRHIDGDFEFETYYSLSCHNCPDVVQALNLMSVLNPRIKHTAIDGGTFQNEITDRNVMGVPAVFVNGKEFGQGRMTLTEIVAKIDTGAEKRAAEELNKRDAYDVLIVGSGPAGAAAAIYSARKGIRTGLMGERFGGQILDTVDIENYISVPKTEGQKLAGALKVHVDEYDVDVIDSQSASKLIPAAVEGGLHQIETASGAVLKARSIIVATGAKWRNMNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKADQVLQDKLRSLKNVDIILNAQTTEVKGDGSKVVGLEYRDRVSGDIHNIELAGIFVQIGLLPNTNWLEGAVERNRMGEIIIDAKCETNVKGVFAAGDCTTVPYKQIIIATGEGAKASLSAFDYLIRTKTA
Protein: Beta-porphyranase A (EC 3.2.1.178) (D7GXG0)
Organism: Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
Function: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone. Displays a strict requirement for C6-sulfate in the -2 and +1-binding subsites.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Kappa-carrageenase, family GH16
- 3,6-anhydro-alpha-L-galactosidase
- Uncharacterized protein
- Glycoside hydrolase
- Conserved hypothetical lipoprotein
- Glycoside hydrolase
- Conserved hypothetical periplasmic protein
Sequence:
MKKVLLFLIFLVSANLSAQLPSPTNGKKWEKVEQLSDEFNGNSIDTNKWYDYHPFWEGRAPSNFKKGNAFVSDGFLNLRSTLRKEPSSVQDPFKDIWVDAAAAVSKTKAQPGYYYEARFKASSLSMTSSFWFRVGQFSEIDVIEHIGNPSKENRQDDLPYQYHVNTHYYGKHAGLQPLGTEYKMPGRGRDNFYTYGFWWKSPNELLFYFNGKQVMRIVPRVPLDEELRMIFDTEVFPFATAGVANIGLPKPENLRDNSKNTMKVDWVRVYKLVDGTAAEDSSDAPIGSYISLKKTQGDGKFVTGEKDGSQLVARGSTVQSWEKFKVEKHPKGGITLKANSNGKYVQVQGSDINKPVRAAGDFQGDWEQFEWKSKGNGLVALKNVLTGKWLQAPWTENNAIIRPKGPVDNGWETFAWKKETSPTASTALSAQLETKTVDGIRVYPSPASETLTIEGVEGENGLRVFDSTGNPVLKKEGILGRKERLNVSGLIKGNYLLRTGSGEQTWFQKN
Protein: Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (FK506-binding protein 4) (FKBP-4) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed] (Q9TRY0)
Organism: Bos taurus (Bovine)
Function: Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90) (By similarity). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening (By similarity). Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Shuttles from mitochondria to nucleus; colocalizes in mitochondria with the glucocorticoid receptor. {ECO:0000250}.
Interaction partners:
- Glucocorticoid receptor
- Prostaglandin E synthase 3
- Progesterone receptor
- peptidylprolyl isomerase
- Nuclear receptor subfamily 3 group C member 2
- Androgen receptor
- Heat shock 70 kDa protein 1A
- Stress-induced-phosphoprotein 1
- Adenylosuccinate lyase
- Heat shock protein HSP 90-beta
Sequence:
MTAEETKAAESGAQSAPLRLEGVDISPKQDEGVLKVIKREGTGTETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDRFSFDLGKGEVIKAWDIAVATMKVGEVCHITCKPEYAYGLAGSPPKIPPNATLVFEVELFEFKGEDLTEEEDGGIIRRIRTRGEGYAKPNEGALVEVALEGYFKDQVFDRRELRFEVGEGESMDLPCGLEKAIQRMEKGEHSIVYLKPRYAFGSAGKEKFQIPPNAELKYEIHLKSFEKAKESWEMSSEEKLEQSTIVKERGTVYFKEGKYKQAVLQYKKIVSWLEYESSFSDEDAEKAQALRLASHLNLAMCHLKLQAFSAAIENCNKALELDSNNEKGLFRRGEAHLAVNDFDLARADFQKVLQLYPSNKAAKAQLVVCQQRIRKQLEKEKKLYANMFERLAEEETKAKATVAAGDQPADAEMRDEPKNDVAGGQPQVEAEA
Protein: Enkurin (A0A4X1TZW7)
Organism: Sus scrofa (Pig)
Function: Adapter that functions to localize a calcium-sensitive signal transduction machinery in sperm to a calcium-permeable ion channel (By similarity). Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:E1B836}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q6SP97}. Note=Sperm acrosomal crescent and flagellar principal piece. {ECO:0000250|UniProtKB:Q6SP97}.
Interaction partners:
Sequence:
MDPTYSSESIYNLIPSDWKEPPQPPRYISIFKATVKDDMQKFKTAMKTMGPAKLEVPSPKDFLKKHSKEKTLPPKKKFDRHEPKKPPVPLRTEHPVMGIQSEKNFINTNAANVIMGVAKKPKPVYVDKRTGDKHDLETSGLVPKYINKKDYGVTPEYICKRNEEVKKAQEEYDNYIQENLRKAAMKRLSDEEREAVLQGLKKNWEEVHKEFQSLSVFIDSIPKKMRKQKLEEEMKQLEHDIAVLEKHKIIYIANKK
Protein: GH06265p (Q961U4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVGSNGAANGNNGAGGVGLMLSHQNHQQHHAGHHQQQHMHHQHHQNHHQQLQQQQLPHLHTLQLHGPPSPCPSEHMLGAYSSASSSLSEGSSGHRSHEDDISIVTDKSLGDTSDIISDSSGVGTNSDSAACSIGHPSTTVVCMEPYAGNTVGHIRLQPGDVIEVVGSTDCGLLEGYVRGTNQSGFFPADCVQEVSLRQKHITNVMTASTGMAPQQQQQQHLQQAPAGSSAASYQGSPQLSLGGHSGSSSTLLQQPHQSPSLSVASNGSCQQPLESNEGGASGNGINNRNNNHSVGQYSSATAPRIKKSAYNAPRSVVLHRAKRGFGFILRGAKASSQLMQLRPSERFPALQYLDDVDPGGVADMAGLRPGDFLLTINGEDVTSASHEQVVEMIRSAGALVNLTLVSPQFPHQMQASAQYLPSGARAGSHHLNSGPSTPQSSHRQCATLPRKMTGPGGSGPGSSSGGSVRMAPMPPRRDPKTTLSVGRARAKSMVAGLENGGEKEDDLPHTKSNSVESIATPTPTGIQTGPGTPVQLRTASIKARPTSSRITAAELEELFQRQQGEGSAANASRYATMMTSSRFQSGTDSGAATPPASNGSPMRSGPLVYGSVAEMKRKTARSKHGSGTLRGKPVATPTVGPGGAGGGRDLKRFHSTPDLHGPQLHGSASSIWQASGKGHHSQDDVATLHASLQRLNSNQGELKLGGLGAGSATGAGGAVLPPPNHPPPPPPVGQVVKVETRSSVSEYESTISLQQKLKKRTENDAVTSAAIDGVQSSFNPSANAKIYASPQELRNVMAWKLRQAQEKPSQETSAGSQQPVSQYAAPTQMRPAQQQQQAQQPPTALASHYAAPQVQVQQVQQVQQSPQQSAPQSPPAPPLPQAAPVPAQNGNGNGSTSGAGSAPPIPEPDYSCSESDGEDENSILVARNTKLNEKIALFDVPETSGNSQASGSSSNSGSASISHSLSVEEIQRIRSNLKTSKSSPNGFAKKPEEEKPQQEQQQSHQQPQQLLQPGEDECDNSSSGVSSEQEQLALAAGVTLPGGGKPTDTIKKKPSVTIVEEPKTIPDQPSSNTSHTTKPMAKTTISIGGGGSAVPTATLTVKQLVQQQHAPVIQQQQQQLGSKQPVTAASTNKFTQLSNINSNVMSPQVLGRIPSHHHQQQSSNPNQKLIATQQQILQQQQQQLAHQQHLQQILKAKAAAAGGASNTAVLVAKHQQKLHKGTSSGHESEMETRSDLEDDDGDLSPSPPAKAFQRHNSLTRKQAAAIAMQRGATRTTAVSLMQLPPPLEADSDGEPSQLTLQRQQSHHPSQTHPHPHQLQQQLQLQQQQQQQQQQQQPMAAHIVGMLPSGQLVAVASGAVAGVPGVGATAVQQGNNNLQQLCTDNLVLAPPPQFCDCNDAKHAPQPHLPTSQYHPQQQQQQQHQQQQQQQQQLQQQLQQQQMLQMHQRLSGGAGAGAVGTLGRVRIVGAMPKANHHRLH
Protein: Protein-tyrosine kinase 6 (EC 2.7.10.2) (SRC-related intestinal kinase) (Q64434)
Organism: Mus musculus (Mouse)
Function: Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been identified. These include the RNA-binding proteins: KHDRBS1/SAM68, KHDRBS2/SLM1, KHDRBS3/SLM2 and SFPQ/PSF; transcription factors: STAT3 and STAT5A/B and a variety of signaling molecules: ARHGAP35/p190RhoGAP, PXN/paxillin, BTK/ATK, STAP2/BKS. Associates also with a variety of proteins that are likely upstream of PTK6 in various signaling pathways, or for which PTK6 may play an adapter-like role. These proteins include ADAM15, EGFR, ERBB2, ERBB3 and IRS4. In normal or non-tumorigenic tissues, PTK6 promotes cellular differentiation and apoptosis. In tumors PTK6 contributes to cancer progression by sensitizing cells to mitogenic signals and enhancing proliferation, anchorage-independent survival and migration/invasion. Association with EGFR, ERBB2, ERBB3 may contribute to mammary tumor development and growth through enhancement of EGF-induced signaling via BTK/AKT and PI3 kinase. Contributes to migration and proliferation by contributing to EGF-mediated phosphorylation of ARHGAP35/p190RhoGAP, which promotes association with RASA1/p120RasGAP, inactivating RhoA while activating RAS. EGF stimulation resulted in phosphorylation of PNX/Paxillin by PTK6 and activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. PTK6 activates STAT3 and STAT5B to promote proliferation. Nuclear PTK6 may be important for regulating growth in normal epithelia, while cytoplasmic PTK6 might activate oncogenic signaling pathways.
Subcellular location: Cytoplasm. Nucleus. Membrane. Cell projection, ruffle {ECO:0000250}. Note=Also found to be membrane-associated. Colocalizes with KHDRBS1, within the nucleus.
Interaction partners:
- Signal-transducing adaptor protein 2
- KH domain-containing, RNA-binding, signal transduction-associated protein 1
- Breast cancer anti-estrogen resistance protein 1
- Epidermal growth factor receptor
- Paxillin
- Rho GTPase-activating protein 35
- RAC-alpha serine/threonine-protein kinase
- Tyrosine-protein phosphatase non-receptor type 1
- Suppressor of cytokine signaling 3
- Transmembrane glycoprotein NMB
Sequence:
MVSWDKAHLGPKYVGLWDFKARTDEELSFQAGDLLHVTKKEELWWWATLLDAEGKALAEGYVPHNYLAEKETVESEPWFFGCISRSEAMHRLQAEDNSKGAFLIRVSQKPGADYVLSVRDAQAVRHYRIWKNNEGRLHLNEAVSFSNLSELVDYHKTQSLSHGLQLSMPCWKHKTEPLPHWDDWERPREEFTLCKKLGAGYFGEVFEALWKGQVHVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGNLLQLLRDSDEKALPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSHEHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLTGITRYENLV
Protein: Basal body component (Q57YK8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Intraflagellar transport
- Epsilon tubulin
Sequence:
MAQLDQLLEEYLRVINAKDGEIHELIRVLEELRCEGKKKDEAHKSHAQKISNELDKVMRKAKKLEQKNRTCEDQIDKLVKENEALSIDFQKVQHSLMDAEKIIEENKRAHETALEELQQTYSGVVSKFSTEREELKAHQSEIQKELEEALKSVDECRLKEEEIRKLEVRIAALTQSVEDARREMQSMVPAERVKQIVSEHEEELRTVRKACAEEFDEVSAQLSDAQKSGRKMKEKLKELKESYGQLKDKLDETTCELEEVRKLRQKEQETHNEVRSRQQEEIEQAIHAAKSSTEKLCAMTGQLRQCEVDAQTMEQRWKEVSATLEQERSRNTRDREQMNSQLEASQAQVTEIKAEMSRLRVQLEQGATKLKECQDALASSKEASSRAAADSRESIALIASDRDRLKEDRDRVAFELKEAEHRLSMERDRASDARRELSRRLDDAAHTIERMRDQLKDKEHQLQLLSTAHEKKIQELAFEHNNKLGDCKSQKKNAIDDVRRQLEAANLRLTEEMSGNKALQCELNSAREALANVRDECERWAKEAKESARRQEAATSEASSLRASLAKQQELLAAAAECEKTLCKAAEHANAEKEMEIKRRELLERTLEDTKREVVARRDEVQELRTRIDKENNNTLAKELMECEARFRESQRSLERTQREMVDVQRCGETLQATNKALEEKCRVAERSQREVEEELRRLKGEILSKETECARVAQHAREAEDAAKQSCEHMEREITQRETTIAALQQEISALSEERTKVALLEERMQHQVDMARRDSDNLQARVEFLEREVQDREEKIQQKHKEMLQTVDRLQTLQERAVELEEAMAPKEKKHTMRKEALRKALQQVDEVNKLRSELERHLEKVKASREEESRIYKAQIHQQDERMRVLLEKHREMERQLVAQERDLKAAANEQMTLQQRLAVIRDREQVNVGKHSEEQQKMQEKLDAMSSELARAHATIKSVEEEKNNSVCEASDVQRRTAVNSNRLLITYADDALMTKEMFGEFAISIATRLLRGVNSIANKGCDSALLCMREYTEEAEKQQLRLKREIDDLKYAHAERVRKLEEENSKEMAKQAQHHAAELAKLRQELSDASARAGQEIENQLKDYRRKEEQFHREKTELECARVEMAHQMGQISSLKDQLRTLEQRMDTERIALEQEKRVIQQQYDRASRRLDECATVQSQSEVELRELRSELTNAQQALHEKEKALLVEREKNSQAVYQLEAVNTAKEMLYTQLNDANRKALNIKQQLLSARQEAQQATAAATAERQRLEERISDLAKAVSAHDMENRRLDGQIRSDEKKFIALERELAESRKREAEMSCQLQARRLENSSLRERCANLESLKNINDVTLAETRMREKDLFEKIEEMRSAQQLMQLCFDKQQEQLEAGRRMHEEDTGTNEFMFGGVD