wanglab/gogpt-training-data huggingface dataset:
Protein: BRCA1 associated RING domain 1 (C9IYG1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPDNRQPRNRQPRIRSGNEPRSAPAMEPDGRGAWAHSRAALDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNIFGLRPVDYTDDESMKSLLLLPEKNESSSASHCSVMNTGQRRDGPLVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDAVQSTLKCMLGILNGCWILKFEWVKACLRRKVCEQEEKYEIPEGPRRSRLNREQLLPKLFDGCYFYLWGTFKHHPKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYHARPDSDQRFCTQYIIYEDLCNYHPERVRQGKVWKAPSSWFIDCVMSFELLPLDS
Protein: Myo-inositol transporter 2 (P87110)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transporter for myo-inositol.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Inositol polyphosphate multikinase
Sequence:
MDFNNIPLATIKSSDDKGKDFIVEMTTRPSETKKKVPFSEDMREIPSLPNEEEANATDPQANEVADENGEGFEAEKISSWIWVLSAVAGISGLLFGYDTGVISGALAVLGSDLGHVLSSGQKELITSATSFAALISATTSGWLADWVGRKRLLLCADAIFVIGSVIMAASRNVAMMVVGRFIVGYGIGLTSLIVPMYITELAPARLRGRLVIIYVVFITGGQLIAYSLNAAFEHVHQGWRIMFGIGAAPALGQLISLFWTPESPRYLLRHNHVEKVYKILSRIHPEAKPAEIAYKVSLIQEGVKVDFPEGNKFQHFFHSLKVLFTVPSNRRSLFIGCFLQWFQQFSGTNAIQYFSAIIFQSVGFKNSISVSIVVGATNFVFTIVAFMFIDRIGRRRILLCTSAVMIAGLALCAIAYHFLPADTTQNTNSGWQYVVLASIIIFLASYASGIGNIPWQQAELFPMEVRALGAGFSTAINWVGNLIISASFLTMMESITPTGTFALFAGFCFVGLVTSYFTYPELAGMSIENIHKLLEKGFWQAVKESTKRVRKGRIDEA
Protein: Protein S-acyltransferase 8 (EC 2.3.1.225) (Probable palmitoyltransferase At4g24630) (Zinc finger DHHC domain-containing protein At4g24630) (Q9SB58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: S-acyltransferase involved in protein lipid modification.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Camphor resistance CrcB family protein
- Uncharacterized protein At3g28850
- AP-3 complex subunit delta
- AP3-complex subunit beta-A
- Urea-proton symporter DUR3
Sequence:
MTQRVFQVWKGSNKFILGGRLIFGPDARSLPLTLLLIIVPVVLFCVFVARHLRHEFSPYNAGYAIMVVAILFTIYVLILLFFTSARDPGIVPRNSHPPEEDLRYETTVSADGRQTPSVQIPRTKEVIVNGVSVRVKYCDTCMLYRPPRCSHCSICNNCVERFDHHCPWVGQCIGLRNYRYFFMFVSSSTLLCIYIFSMSAVYIKILMDHQQATVWRAMKESPWAVVLMIYCFIALWFVGGLTAFHLYLISTNQTTYEKLRYRSSHSRSIVYNRGCPNNFLEVFCSKVKPSRNNFRAFIEEEPPRVITLPSTTRESGEAEDENVTRRQKVEDDLDIGDDLMNLSRRCNAEDANNNQPHHTLDIDHERAGSIRTEARHESWGRRSGSWDVAATDVRESRSYATAKDGRG
Protein: Cyclic diguanosine monophosphate-binding protein PA4608 (c-di-GMP-binding protein PA4608) (Pilz domain-containing protein PA4608) (Q9HVI1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Binds the second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP). Can bind two c-di-GMP molecules per monomer. May play a role in bacterial second-messenger regulated processes. Binding to c-di-GMP induces a conformational change of the C- and N-termini resulting in the exposure of a highly negative surface on one side of the protein to a possible effector protein.
Interaction partners:
- PilZ domain-containing protein
- PilZ domain-containing protein
- Chemotaxis protein methyltransferase 1
- PilZ domain-containing protein
- HDOD domain-containing protein
- CheW-like domain-containing protein
- Pentapeptide repeat-containing protein
- Pilin assembly protein
- Leucine dehydrogenase
- Flagellar protein FliL
Sequence:
MSDQHDERRRFHRIAFDADSEILQGERRWEVLLHDVSLHGILVGQPQDWNGDPQRPFEARLYLGLDVLIRMEISLAWARDGLLGFECQHIDLDSISHLRRLVELNLGDEELLERELALLVSAHDD
Protein: Translation initiation factor IF-2, mitochondrial (Q68FQ5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MNQKLLKLEKLLRFHTICRQLHSLSQRRLLAWWKHGSAPASPVWADWLCARPWPTDVLTGSALHQHRLLVTKKEKRPPRSQLSPIKTKKEVEVWVGMTVEELARAMAKDTDCVYEALLNTAIDIDSLEANSHLDEVWIKEVIKKAGMKLKWSKLKLERIRENKDAVRRPGADPALLKPRSPVVTIMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGKNLMALAEATIALAEMLELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLKKGSILVAGKSWAKVRLMFDENGKTVNEAYPSMPVGIIGWRDLPSAGDEILEVQSEPRAREVVDWRKSEQKEEKGKDDLKIMEEKRKEHQEAHRKAREKYGSLHWKQRSYIKYLERKEQRPLKPKEKVERDSNVLPIIIKGDVDGSVEAILNLLDTYDASHECELELVHFGLGDISENDVTFAETFDGVIYGFNVDAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSNRLPYKVEEYPIGEASILATFTITEGKKKVPVAGCRVQKGQLERQKKFKLIRNGQVIWKGSLTSLKHHKDDVLVIKTGVDCGLSLDEENVEFKVGDQVICYEENKVPTKTSWDPGF
Protein: Myosin heavy chain, skeletal muscle (P02562)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
Sequence:
SAETEKEMANMKEEFEKTKESLAKAEAKRKELEEKMVALMQEKNDLQLQVQAEADSLADAEERQDLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQETSMDIENDKQQLDEKLKKLEFMTNLQSKIEDEQALMTNLQRIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFEKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLAGNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEHQRLINELSAQKARLHTESGEFSRQLDEKDAMVSQLSRGGQAFTQQIEGLKRQLEEETKAKSALAHALQSSRRDCDLLREQYEEEQEAKAELQRAMSKANSEVSQWRTKCETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEAEDLMIDVERSNATCARMDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTEVFKVKNAYEESLDHLETLKRENKNLQQEISDLTEQIAESAKHIHELEKVKKQIDQEKSELQAALEEAEGSLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIKNLRNTQGILKDTQLHLDDAVRGQDDHKEQLAMVERRANLMQAEIEELRASLEQTERSRRVADQDLLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQQRLDEAEQLALKGGKKQIQKLEARVKELENEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNINLSKFRKLQHELEEAEERADIAESQVNKLRVKSRDVHSKVISEE
Protein: Keratin-associated protein 7-1 (High tyrosine-glycine keratin-associated protein 7.1) (Q8IUC3)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 8-1
- Keratin-associated protein 13-1
- Keratin-associated protein 11-1
- Keratin-associated protein 19-3
- Keratin-associated protein 24-1
- Keratin-associated protein 15-1
- Keratin-associated protein 20-1
- Keratin-associated protein 20-2
- Keratin-associated protein 13-3
- Keratin-associated protein 6-2
Sequence:
MTRYFCCGSYFPGYPIYGTNFHGTFRATPLNCVVPLGSPLNYGCGCNGYSSLGYSFGGSNINNLGGCYGGSFYRPWGSGSGFGYSTY
Protein: Contactin-1 (Neural cell surface protein F3) (P12960)
Organism: Mus musculus (Mouse)
Function: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Contactin-associated protein 1
- Neurofascin
- Neuronal cell adhesion molecule
- Receptor-type tyrosine-protein phosphatase zeta
- Contactin-associated protein-like 2
- Major prion protein
- Receptor-type tyrosine-protein phosphatase beta
- Hyaluronan and proteoglycan link protein 2
- Receptor-type tyrosine-protein phosphatase gamma
Sequence:
MKMPLLVSHLLLISLTSCLGDFTWHRRYGHGVSEEDKGFGPIFEEQPINTIYPEESLEGKVSLNCRARASPFPVYKWRMNNGDVDLTNDRYSMVGGNLVINNPDKQKDAGVYYCLASNNYGMVRSTEATLSFGYLDPFPPEERPEVKVKEGKGMVLLCDPPYHFPDDLSYRWLLNEFPVFITMDKRRFVSQTNGNLYIANVESSDRGNYSCFVSSPSITKSVFSKFIPLIPIPERTTKPYPADIVVQFKDIYTMMGQNVTLECFALGNPVPDIRWRKVLEPMPSTAEISTSGAVLKIFNIQLEDEGLYECEAENIRGKDKHQARIYVQAFPEWVEHINDTEVDIGSDLYWPCIATGKPIPTIRWLKNGYSYHKGELRLYDVTFENAGMYQCIAENAYGSIYANAELKILALAPTFEMNPMKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTEWLVNSSRILIWEDGSLEINNITRNDGGIYTCFAENNRGKANSTGTLVITNPTRIILAPINADITVGENATMQCAASFDPALDLTFVWSFNGYVIDFNKEITHIHYQRNFMLDANGELLIRNAQLKHAGRYTCTAQTIVDNSSASADLVVRGPPGPPGGLRIEDIRATSVALTWSRGSDNHSPISKYTIQTKTILSDDWKDAKTDPPIIEGNMESAKAVDLIPWMEYEFRVVATNTLGTGEPSIPSNRIKTDGAAPNVAPSDVGGGGGTNRELTITWAPLSREYHYGNNFGYIVAFKPFDGEEWKKVTVTNPDTGRYVHKDETMTPSTAFQVKVKAFNNKGDGPYSLVAVINSAQDAPSEAPTEVGVKVLSSSEISVHWKHVLEKIVESYQIRYWAGHDKEAAAHRVQVTSQEYSARLENLLPDTQYFIEVGACNSAGCGPSSDVIETFTRKAPPSQPPRIISSVRSGSRYIITWDHVVALSNESTVTGYKILYRPDGQHDGKLFSTHKHSIEVPIPRDGEYVVEVRAHSDGGDGVVSQVKISGVSTLSSSLLSLLLPSLGFLVYSEF
Protein: Delta-aminolevulinic acid dehydratase (ALAD) (ALADH) (EC 4.2.1.24) (Porphobilinogen synthase) (P0ACB2)
Organism: Escherichia coli (strain K12)
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
Interaction partners:
- Glutamate-1-semialdehyde 2,1-aminomutase
- Porphobilinogen deaminase
- Glutamyl-tRNA reductase
- Uroporphyrinogen-III synthase
- Uroporphyrinogen decarboxylase
- Ferrochelatase
- Siroheme synthase
- Oxygen-dependent coproporphyrinogen-III oxidase
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- Oxygen-independent coproporphyrinogen III oxidase
Sequence:
MTDLIQRPRRLRKSPALRAMFEETTLSLNDLVLPIFVEEEIDDYKAVEAMPGVMRIPEKHLAREIERIANAGIRSVMTFGISHHTDETGSDAWREDGLVARMSRICKQTVPEMIVMSDTCFCEYTSHGHCGVLCEHGVDNDATLENLGKQAVVAAAAGADFIAPSAAMDGQVQAIRQALDAAGFKDTAIMSYSTKFASSFYGPFREAAGSALKGDRKSYQMNPMNRREAIRESLLDEAQGADCLMVKPAGAYLDIVRELRERTELPIGAYQVSGEYAMIKFAALAGAIDEEKVVLESLGSIKRAGADLIFSYFALDLAEKKILR
Protein: D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (EC 3.1.3.82) (D,D-heptose 1,7-bisphosphate phosphatase) (HBP phosphatase) (Q9JXI5)
Organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)
Function: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphoheptose isomerase
- D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
- ADP-heptose synthase
- ADP-L-glycero-D-manno-heptose-6-epimerase
- 1-
- lipopolysaccharide heptosyltransferase II
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Imidazole glycerol phosphate synthase subunit HisF
- YgjP-like metallopeptidase domain-containing protein
- Histidinol-phosphate aminotransferase
Sequence:
MKLIILDRDGVINQDRDDFVKSVDEWIPVEGSMDAVAFLTQAGYTVAVATNQSGIGRKYFTVQNLTEMHAKMHRLVRQAGGEINGIWFCPHTDADNCNCRKPKPGMIEDIIGRFNAQASETWLVGDSLRDLQAIDAVGGKPALVLTGKGKKTLSQHGHELPEHTQVFDTLLDFSQYIMQENTAPQAD
Protein: Beta-amyrin 28-monooxygenase (EC 1.14.14.126) (Beta-amyrin 28-oxidase) (Cytochrome P450 CYP716A52v2) (Oleanic acid synthase) (PgOAS) (I7C6E8)
Organism: Panax ginseng (Korean ginseng)
Function: Component of the oleanane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway. Catalyzes the carboxylation of beta-amyrin at the C-28 position to form oleanolic acid during ginsenoside biosynthesis, a class of tetracyclic triterpenoid saponins.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MELFYVPLLSLFVLFISLSFHFLFYKSKPSSSGGFPLPPGKTGWPIIGESYEFLSTGWKGYPEKFIFDRMTKYSSNVFKTSIFGEPAAVFCGAACNKFLFSNENKLVQAWWPDSVNKVFPSSTQTSSKEEAIKMRKMLPNFFKPEALQRYIGLMDQIAANHFESGWENKNEVVVFPLAKSYTFWIACKVFVSVEEPAQVAELLEPFSAIASGIISVPIDLPGTPFNSAIKSSKIVRRKLVGIIKQRKIDLGEGKASATQDILSHMLLTSDESGKFMGEGDIADKILGLLIGGHDTASSACTFVVKFLAELPQIYEGVYQEQMEIVKSKKAGELLKWEDIQKMKYSWNVACEVLRLAPPLQGAFREALSDFTYNGFSIPKGWKLYWSANSTHINSEVFPEPLKFDPSRFDGAGPPPFSFVPFGGGPRMCPGKEYARLEILVFMHHLVKRFKWEKVIPDEKIVVNPMPIPANGLPVRLFPHKA
Protein: BRISC and BRCA1-A complex member 2 (C9J2G0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368019}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368019}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000256|RuleBase:RU368019}.
Interaction partners:
Sequence:
MSPEVALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGEDAEFLPDPSALQNLASWNPSNPECLLLVVKELVQQYHQFQCSRLRESSRLMFEYQTLLEEPQYGE
Protein: RE64552p (Sphingosine kinase 1, isoform A) (Sphingosine kinase 1, isoform B (EC 2.7.1.91)) (Q9VYY8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Neutral ceramidase
- LD18904p
- Sphingosine-1-phosphate lyase
- Alkaline ceramidase
- Sphingolipid delta
- GH04282p
- 3-dehydrosphinganine reductase
- FI20175p1
- Putative phosphatidate phosphatase
- sphingosine kinase
Sequence:
MTANTGTSGENLMGNGGKTHEPSTPTSDTEVASGTPTELSEIFFVDNSRRKQSIKIQVKLCPEGVYLRRETEEDDHINEQLIRIDDIIGSRYGRRLKKRARGGLNSCRNPNVPGQEADSEPDSDNSAYLYIYAYLKKEKPLRRVQTLRILRFRSSNDYGVNLQTAEMWHHTIRKHKRGNGSSSPADCGKQLLILLNPKSGSGKGRELFQKQVAPLLTEAEVQYDLQITTHPQYAKEFVRTRRDLLTRYSGIVVASGDGLFYEVLNGLMERMDWRRACRELPLGIIPCGSGNGLAKSVAHHCNEPYEPKPILHATLTCMAGKSTPMDVVRVELATRDKHFVMYSFLSVGWGLIADIDIESERLRSIGAQRFTLWAIKRLIGLRSYKGRVSYLLGKGKKEPPVEAARELPAESTAAGIRSSLPLNAGEFHDLPEEEEGEAVLDGEQFADAISLDRSVYRQHADSWHSAMSRRTAYYSLGGPSMRSNRSRMSISQRIEAANAEFAERVPTGTIPPLQMPLLSSDGWICEDGDFVMVHAAYTTHLSSDVFFAPESRLDDGLIYLVIIRRGVSRHQLLNFMLNLNAGTHLPIGEDPFIKVVPCRAFRIEPSSSDGILVVDGERVEYGPIQAEVMPGLINVMTTSGQ
Protein: Mitochondrial peptide methionine sulfoxide reductase (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Protein-methionine-S-oxide reductase) (PMSR) (Q9UJ68)
Organism: Homo sapiens (Human)
Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Subcellular location: [Isoform 1]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Methionine-R-sulfoxide reductase B3
- Methionine-R-sulfoxide reductase B2, mitochondrial
- Thioredoxin
- Retinitis pigmentosa 1-like 1 protein
- Methionine-R-sulfoxide reductase B1
- Glutaredoxin-1
- Thioredoxin, mitochondrial
- Transcription factor SOX-7
- Glutaredoxin-2
- Thioredoxin domain-containing protein 3
Sequence:
MLSATRRACQLLLLHSLFPVPRMGNSASNIVSPQEALPGRKEQTPVAAKHHVNGNRTVEPFPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCSEKTGHAEVVRVVYQPEHMSFEELLKVFWENHDPTQGMRQGNDHGTQYRSAIYPTSAKQMEAALSSKENYQKVLSEHGFGPITTDIREGQTFYYAEDYHQQYLSKNPNGYCGLGGTGVSCPVGIKK
Protein: Dual specificity protein kinase zak2 (EC 2.7.12.1) (Tyrosine-protein kinase 4) (Zaphod K Kinase 2) (Zaphod kinase 2) (Q552C6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Positive regulator of gsk3/gskA activity required for cell pattern formation and a downstream effector of carC. The kinases, gsk3/gskA, zakA and zak2, form part of a signaling pathway that responds to extracellular cyclic AMP. The pathway has a role in transcriptional regulation; required to direct prespore/spore fates during development. Zak2 negatively regulates prestalk differentiation by regulating expression of ecmA. Phosphorylates Y-214 of gsk3/gskA, in vitro.
Interaction partners:
Sequence:
MNSHKKEEWEEISSIGSCNSKSRVLKCRKKNGLIENEKVDIVAVKIINKKFFKRNETDILEKIRLFNIPRYYSHAEDDNYIYIYMEYIEDKKQLRFKESEIISMIADLTETLSFLHKHQILHRDIKPSNIILDKNGVLKLIDFGSSIIDQQQDDGDNICKESSFAITGTHTYMAPEVKKLHRSTKKSDVWSLGCTVLEIVGGNPKKIFDGIPIIPNHVSEIMVDFIKRCLIIDPNKRSHMEELLTHRLISSMVGQNKNRENNIEPKFNNDYLSSKFPERFAPRFEKPKWEIEFNELKFNKDDTVGGDGFFSVVKKGYYNETEVAIKLIKKAHGENVTVCDTFYHEVLIISNLRHPNIVQFIAACIKFDNKEVNHCIVSEWMSGGNLSQFISNERKILEINPHLRVKILLDIAKGMLYSHRQGIIHRDLTSNNVLLNFRKKKLLNNNSSNNDEQFYDSDEIIAKVCDFGLSSNQSESKKLRGGSIHYMAPENLNGSPINEKSDIYSFGLLVWQMFSYASPNTIYSPKEMASMVSDEKLNYRPQIPFNVPLKFKELITQCWDRNPLNRPKDFSEIIDKLKDINQIYFQDNSNASTISSTAITTTISTISISNSGNSSYSTSDDSSTYGSGFYNSGFL
Protein: Flagellin (A0A0H3NMJ6)
Organism: Salmonella typhimurium (strain SL1344)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362073}. Bacterial flagellum {ECO:0000256|RuleBase:RU362073}.
Interaction partners:
Sequence:
MAQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR
Protein: Glycine N-acyltransferase-like protein 1 (EC 2.3.1.68) (Acyl-CoA:glycine N-acyltransferase-like protein 1) (Glutamine N-acyltransferase) (Q969I3)
Organism: Homo sapiens (Human)
Function: Acyltransferase which transfers an acyl group to the N-terminus of glutamine. Can use phenylacetyl-CoA as an acyl donor.
Interaction partners:
- Histone acetyltransferase KAT2A
- Histone acetyltransferase KAT2B
- N-acetyltransferase ESCO1
- N-acetyltransferase ESCO2
- N-alpha-acetyltransferase 80
- Melanopsin
- Cyclic nucleotide-gated channel alpha-3
- Diamine acetyltransferase 1
- Thialysine N-epsilon-acetyltransferase
- Regulator of G-protein signaling 9-binding protein
Sequence:
MILLNNSHKLLALYKSLARSIPESLKVYGSVYHINHGNPFNMEVLVDSWPEYQMVIIRPQKQEMTDDMDSYTNVYRMFSKEPQKSEEVLKNCEIVNWKQRLQIQGLQESLGEGIRVATFSKSVKVEHSRALLLVTEDILKLNASSKSKLGSWAETGHPDDEFESETPNFKYAQLDVSYSGLVNDNWKRGKNERSLHYIKRCIEDLPAACMLGPEGVPVSWVTMDPSCEVGMAYSMEKYRRTGNMARVMVRYMKYLRQKNIPFYISVLEENEDSRRFVGQFGFFEASCEWHQWTCYPQNLVPF
Protein: Zinc finger protein 543 (Q08ER8)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAASAQVSVTFEDVAVTFTQEEWGQLDAAQRTLYQEVMLETCGLLMSLGCPLFKPELIYQLDHRQELWMATKDLSQSSYPGDNTKPKTTEPTFSHLALPEEVLLQEQLTQGASKNSQLGQSKDQDGPSEMQEVHLKIGIGPQRGKLLEKMSSERDGLGSDDGVCTKITQKQVSTEGDLYECDSHGPVTDALIREEKNSYKCEECGKVFKKNALLVQHERIHTQVKPYECTECGKTFSKSTHLLQHLIIHTGEKPYKCMECGKAFNRRSHLTRHQRIHSGEKPYKCSECGKAFTHRSTFVLHHRSHTGEKPFVCKECGKAFRDRPGFIRHYIIHTGEKPYECIECGKAFNRRSYLTWHQQIHTGVKPFECNECGKAFCESADLIQHYIIHTGEKPYKCMECGKAFNRRSHLKQHQRIHTGEKPYECSECGKAFTHCSTFVLHKRTHTGEKPYECKECGKAFSDRADLIRHFSIHTGEKPYECVECGKAFNRSSHLTRHQQIHTGEKPYECIQCGKAFCRSANLIRHSIIHTGEKPYECSECGKAFNRGSSLTHHQRIHTGRNPTIVTDVGRPFMTAQTSVNIQELLLGKEFLNITTEENLW
Protein: CHK domain ov1 (CHKov1) (Q107I8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cytochrome P450 6g1
- Protein ref
- Enhancer of mRNA-decapping protein 4 homolog
Sequence:
MAAGKIPDWVTAERFEDVLKSNVDGYSKVRNFKAEMGSAAGDNYATNMLRVNIEVELQDGTTKELSYMVKLPRQREINKEMMKHNNIFEIERTMYNLVVPEMEALYKAAGVEVTFGAKSYELKNAQTEYISLEDLCIKGFKNANRLEGLDQAHTERVLRKLAQWHAATAVRVATKGQYPEIVLNGFFKEENRPMMNDMMNGMGQVFVKCCSTYEGNEAYIEKVKALKDVMIDELFKMCVVDPTEFNVLNHGDSWSNNIMFQYDESGKIKEVYMVDFQVSKYGTVAQDLYYFLISSTKLEDKLSKFDYYVKVYHDNLVEHLKILKYSKPLPSLRDIHKSLYKYGTFAYSVATGVMAAVLVDPTESASFENFVGDSAEGADFQMKMYNNPRYRKHMQAILPWLLNRGALDFN
Protein: T. brucei spp.-specific protein (Q381P6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKALKTNITVYSVSLGRLLNEFNNRYFRLKKRSRSEDLKRMPVREEAFLRLLPWHHNVTGSCESGVSESDSDRVNGDLTRCRFLFGRCQMNVEYQFALSVGTRKDVASSKCTGEGSEGGAVLLRFTKIPNKSGGSSTVTCSIRVNKEVQYFNREEVVVAMKFCREIYA
Protein: Centrosomal protein 103 kDa (Q55CA1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Uncharacterized protein
- SNARE-complex protein Syntaxin-18 N-terminal domain-containing protein
- Uncharacterized protein
- t-SNARE coiled-coil homology domain-containing protein
- Vesicle-trafficking protein SEC22b
- Coatomer subunit delta
- Coatomer subunit alpha
- Sec1-like family protein
- Sec1 family domain-containing protein 1 homolog
- Coatomer subunit beta
Sequence:
MGIDNKKIVDELNESTSSSSSSSSSTSIKHVIDKVLIRSTNTTTISPNLKSSKKPKKTILDNKKDSEDLFEQPDQLETNVSSTISYLIESKKKLFNQVQIELDKSSNKKIGIINLQNDIKTLEIEKEEAIKRIKDAEDGIINRIEKTVSFDRELRSRLSSIESVINIIEYFEHYNHLLQQYQQEIKSQQFISATNTFIKMSDWFNQSNNQPYELSMILSAPTQQPRIIPSIKDQLKKRKNQLKSTLLESFTNSIIITSNFEIQLFQIENNNKKYQSSSSSSQSYTVDLIQSLELLGLFNHTITSFTSTLFQSFLQPIIKKLNSLVQDDNYFINKINKQQQQQRNLYKEEEIDNGELICFKFCENDDNNNNNNIGKIITIPMIYEFIIKLFEFLKRNLFGSSNEEIIKKFGQEIWSDLSQCILDELLKYRIPKDINQLNQYHSTIKNSTIDFESKITNDILFLTNNNNIINSSLSSSSSSSKIIKTNQLTEFVNNIEFHYSERKRMLLLSKAREIILKDRYQSIQSNDSILFSNCNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSICTIQGYYFENRLILESTNSLLSLCISTLKESKNDSNISFQSCRDIFDIYQAIYLKHHISKLEKVPTLACLFYNSCLFFSHCFLILSIENNNNNNNNNDNNNKNEIFTFIDFSNKFKEIGNIFFSKYIREQLKWILSFLENTEFSNRLENTKDQLVFSKIQNNFTNMNNELNRLSCIWKDVFPREDYFELISKFSESIIATIIKMILKLQNIEMVETQKLSELISSLYPVFIRFFIFNGESEDLHKNRMKLVKSWKKFWQIKMVLELPLSEIVALYNKGHLNKLSNNELRLLILSIFDDFDLKTQFLSQLNKQIQQQSKQ
Protein: Myosin motor domain-containing protein (Q20456)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Netrin receptor unc-40
Sequence:
MDNLIELPDQSEAGIAQNLHERFKKGVTYTKASNVLVFVNDFNDKDSEDQLSWETSSTSGVNAVAKNALNKIFNMSSNAESIVFGGESGSGKSYNVFKAFKYLTSQPKSKVSTKHSSSIEFVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYTVPLEVPRVISQKPGERNFNIFYEVYHGLSDEMKAKFGIKGLQKFFYINQGNSSENIQHDVNRFKHLESALHVLGFSDDHCMSIYKIISTILHIGNIYFRTKRNPNVEQDVVEIGNLAELKWIAFLLEVDFDQLVKFLLPTSEDGSTIELNAALDNRDSFAMMIYEELFKWVLNRIGLQLKCSLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHCFHDQLIDYAKDGISVDYKVPNSIENGKTVELLFKKPYGLLSLLTDECKFPKGTHETYLEHCNLNHTDRSAYGKARNKERLEFGVRHCIGTTWYNVTDFFARNKRIISLSAVQLMRNSKNPIIGLLFESYGGNTSDIIVSQAQFVLRGAQDIADKINVSHVHFVRCIKSNNERQSTKFDIPLVNRQIKNLLLAELLSFRVKGYPVKISKTTFARQYRCLLPGDIAQCQNEKEIIQDILQGQGVKYEDDFKIGTEYVFLRERLAERYDGLQNKICGDAAIIIQKNMKSFVAQKVYKRMRAAIIKLQSGLRGWKARRDYIIKREEMFKAIGRTMKRNKRLDAYHQALGTENSGQLQQTLVGYIDINEDAKKFLERPTSDSDATETLTHYLTVPMKNFLSNMNSITLEQFAEENFKGHLLEPRREPIMTPFLHKESDYDFRLSVEIFKLILKYMNDIKLTKKQREDLGRYIVQQGISNPCQRDEILVQTINQINKNQDKTASDNGWKLVHMAISVFPPTENIIPMLIGFFNKESVPMKEQLFATLQRRLKIYDSEIARELPPSNLELIATPNIPNTVAEINCYDGLCCDVHLSPWSTTSEIAERILKQRGVGIALGWTVEVETPNRVFAPTGNHFIHDVFSQIEGANMDSENQQNIFFNFPPEKLVKKPPVVPKEVVQEQEIVSQNTNGTIPKAARTYPTPEEWINQPPQRTESRNTPRDHQKPDEESDESLVREYNEEAGYAYTLPRKNKPAPQAVEDNETSESEEDDEDAANRVGYETVRPEENMKMMETIQDHSHILKSPVLPRKTYSRNEQHEEYTPMNFAPPPTFTYPQQMPMMQYVPVMMTSSMMTPSMMTPSMMPGQQIAMVPQQMMMQPHFSYVPQYPQIPQYCPPEPILSPQSVRSEVPPMMAPVMHDGHGSTRSRDYRIMKRGEVPSQYSTIRNMPVPEHGKDVDQFLDAVFDQVLSKDEQRAAHFNSNQLANTIKGGKLRPEGYYEPPVQTYSPVPPRYPTLRRVDDSPLRSRAKSLPRIISPRHEHFVRRPHSRNSYSNESTSSDDQMNYRTRSRERSLPRFHSNNGYNYDPSQPVYMMPVQMNGHGEMILLSPVASEHKAQSRHRTHDRSHRHHVPSGVERYMAKRSPSVDILKPPMSRRTPDAMVEQTYVRPHLAQSPVGRQTSRFEEFSALPRGDSRARERMENPLLARQIPRAYPYQNGNVVPPPPSSYRAPSPAPTSGDRRGLNRLPQESYTEPAVKNTKNNSEYLSPHRFNLDEQKAVIRHEKETAKNAINMLSDRLRKLPPPVDNVRLIRPITPAQPPITQSPVPSEPVVVRTPSPVPQPTPPPPPPPVREEWVIRDSVERDPVTQGRIRGSFRKEPLVPQPPRPPVVAEKPAVKFVKAPWKLTIRKEMFYPGEVLNDIQIIDQVFAQIVEDCKKSYPYRIREQDRKQVETVLRQYEIPPSDLNNQSNIHPDVKVAVIELARLWPLYFNQVYEVVEKRPDESVSTIFAISEHGIRLIVHTPHDLENPLKIQDFFPFETIADVSLEANDILSVHVRHEDEENAYSAVRIKTNQAPQIKKTLDRCLSGGVVPKRKFVRALEDYVTSEVNHLSFKQGDVIELLQEPEGETPPVGNWLYGKIENRFGFLLAQYVDSTDGDNVPPIRHETSEDRDERVRFFDDEVPFSSERYTMIDFATKYFRKPKDKKKQETWAWEDISQIVRFSEKPISQSLLADLGNEESKYAVETFHAIMKFMGDEPLKKSESMTDVVFKVLLICHRQPTLRDEVYCQLIKQTTSNISQKPNSALRAWRLLTIITAYFPSSLTLKPYVLQYLGDNADEWQRPFHGTARICQTNMIQTFKYGGRKVLLNALEVQQITDGCQLRRQAFYISKDHNVSQTLRPITVAEEMIQELCNLLNVRSLHEQQEFSLCYTVGKDKHLNYCKNDNYLMDIITESEHKKLPFQFYLKRTVWVHPLRYDNAAYIDSMFDQVIDDYLRGSLISTNSLGQLTAATTEEIIKLAAYLFLLLPDNPKGLNAKTLPQIVPKSVIEPKHRHQEEMVTRISRQLKMFGGRMRPAEAKSHFLELLSTWPTFGVLHYRLKSVVENGHQLPEVILTINKSGIQLLQPKSKEVFKERNYDQIVSVESIRKTAYKIVRLVINTMQGEETLDIKTDEADEISHLIGQYMFVTGGAEERGSTEL
Protein: UPF0561 protein C2orf68 (Q2NKX9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEAGPHPRPGHCCKPGGRLDMNHGFVHHIRRNQIARDDYDKKVKQAAKEKVRRRHTPAPTRPRKPDLQVYLPRHRDVSAHPRNPDYEESGESSSSGGSELEPSGHQLFCLEYEADSGEVTSVIVYQGDDPGKVSEKVSAHTPLDPPMREALKLRIQEEIAKRQSQH