wanglab/gogpt-training-data huggingface dataset:
Protein: Dual specificity protein phosphatase 10 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 5) (MAP kinase phosphatase 5) (MKP-5) (Q9Y6W6)
Organism: Homo sapiens (Human)
Function: Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- JNK1/MAPK8-associated membrane protein
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 3
Sequence:
MPPSPLDDRVVVALSRPVRPQDLNLCLDSSYLGSANPGSNSHPPVIATTVVSLKAANLTYMPSSSGSARSLNCGCSSASCCTVATYDKDNQAQTQAIAAGTTTTAIGTSTTCPANQMVNNNENTGSLSPSSGVGSPVSGTPKQLASIKIIYPNDLAKKMTKCSKSHLPSQGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDSFKRIFSKEIIVYDENTNEPSRVMPSQPLHIVLESLKREGKEPLVLKGGLSSFKQNHENLCDNSLQLQECREVGGGASAASSLLPQPIPTTPDIENAELTPILPFLFLGNEQDAQDLDTMQRLNIGYVINVTTHLPLYHYEKGLFNYKRLPATDSNKQNLRQYFEEAFEFIEEAHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTPKLMGVETVV
Protein: ADP-ribosylation factor-like protein 1 (Q4QEJ1)
Organism: Leishmania major
Interaction partners:
- C2 domain-containing protein
- Small GTP binding protein rab6-like protein
- PB1 domain-containing protein
- Proteophosphoglycan ppg4
- Uncharacterized protein
- Uncharacterized protein
- Integral membrane protein
- Uncharacterized protein L8530.02
- Uncharacterized protein
- K Homology domain-containing protein
Sequence:
MGAWLASLKQTLGLLPADRKIRVLMLGLDNAGKTSILYRLHLGDVVTTVPTVGVNLETLQYKNISFEVWDLGGQTGVRPYWRCYFSDTDAVIYVVDSTDRDRMGVAKHELYALLDEDELRKSLLLIFANKQDLPDAASEAEIAEQLGVSSIMNRTWTIVKSSSKTGDGLVEGMDWLVERLREQGLGA
Protein: Putative glycyl-radical enzyme activating enzyme YjjW (GRE activating enzyme YjjW) (EC 1.97.1.-) (P39409)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YjjI
- Probable dehydratase PflD
- Formate acetyltransferase 1
- Probable dehydratase YbiW
- PFL-like enzyme TdcE
- Uncharacterized sugar kinase YeiI
- UPF0253 protein YaeP
- Autonomous glycyl radical cofactor
Sequence:
MNSRCALVSKIIPFSCVDGPGSRLALFLQGCNLRCKNCHNPWTMGRCNDCGECVPQCPHQALQIVDGKVVWNAVVCEQCDTCLKRCPQHATPMAQSMSVDEVLSHVRKAVLFIEGITVSGGEATTQLPFVVALFTAIKNDPQLRHLTCLVDSNGMLSETGWEKLLPVCDGAMLDLKAWGSECHQQLTGRDNQQIKRSIYLLAERGKLAELRLLVIPGQVDYLQHIEELAAFIKGLGDVPVRLNAFHAHGVYGEAQSWASATPEDVEPLADALKVRGVSRLIFPALYL
Protein: Kinetochore-associated protein NSL1 homolog (Q96IY1)
Organism: Homo sapiens (Human)
Function: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}. Note=Associated with the kinetochore (PubMed:15502821, PubMed:16585270).
Interaction partners:
- Outer kinetochore KNL1 complex subunit KNL1
- Protein MIS12 homolog
- Kinetochore-associated protein DSN1 homolog
- Polyamine-modulated factor 1
- Outer kinetochore KNL1 complex subunit ZWINT
- Kinetochore protein Spc24
- Kinetochore protein Nuf2
- PMF1-BGLAP readthrough
- Kinetochore protein NDC80 homolog
- Chromobox protein homolog 5
Sequence:
MAGSPELVVLDPPWDKELAAGTESQALVSATPREDFRVRCTSKRAVTEMLQLCGRFVQKLGDALPEEIREPALRDAQWTFESAVQENISINGQAWQEASDNCFMDSDIKVLEDQFDEIIVDIATKRKQYPRKILECVIKTIKAKQEILKQYHPVVHPLDLKYDPDPAPHMENLKCRGETVAKEISEAMKSLPALIEQGEGFSQVLRMQPVIHLQRIHQEVFSSCHRKPDAKPENFITQIETTPTETASRKTSDMVLKRKQTKDCPQRKWYPLRPKKINLDT
Protein: Protein O-mannosyl-transferase 2 (EC 2.4.1.109) (Dolichyl-phosphate-mannose--protein mannosyltransferase 2) (DmPOMT2) (dPOMT2) (Protein twisted) (Q9W5D4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Rt/POMT1 and tw/POMT2 function as a protein O-mannosyltransferase in association with each other to generate and maintain normal muscle development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16219785}; Multi-pass membrane protein {ECO:0000269|PubMed:16219785}.
Interaction partners:
- Protein O-mannosyltransferase 1
- Dystroglycan 1
- FI03527p
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichol phosphate-mannose biosynthesis regulatory protein
- GDP-fucose protein O-fucosyltransferase 2
- EGF domain-specific O-linked N-acetylglucosamine transferase
- GPI mannosyltransferase 2
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
Sequence:
MAASVVKTPKCPRRGSVKDVAQNAPRTAPTSSKEANWNWWLLLATVFLVTFATRFYKVTEPDHICWDETHFGKMGSWYINRTFFFDVHPPLGKMLIGLSGYLTGYNGTFPFEKPGDKYNETRYQGMRYFCTTLGALIMPMGFDTVYDLTRSHEAALLAAAYLIFDVGLLTLNQYILLDPILLFFMMASVWGMVKVSKSTASGGSYGLRWWLWLFLTGTMLSCTISVKFVGLFVVLLVGLHTATELWLILGDLGQPILETVKQLACRAITLIVWPVLLYILFFYIHLSVLNRSGNGDGFYSSAFQSRLIGNSLYNASMPRDVAYGSLVTIKNHKTGGGYLHSHHHLYPKGSGARQQQVTTYTHKDENNKWLIRPHNKPGPPKGKVQILRHGDLVRLTHMATRRNLHSHNEPAPMTKKHLQVTGYGELGLGDANDVWRVLIVGGKVNETVHTVTSRLKFIHLLQNCALTSSGKQLPKWGFEQQEVSCNPNVRDKNSQWNVEDNEHKLMPSVSFSVYAPGFFARFLESHAVMLQGNAGLKPKEGEVTSRPWQWPINYRGQFFSGSSYRIYLLGNPLIWWSNLVFLALFVTVFLCNAVVQQRRAGFARSAAQNQAQVPDSETVAQDEESEHSTTDICSCCTPAKEIVPKAVPSGSPEAPNPAQSLRAAAWLFLGWMLHYLPFWAMGRVLYFHHYFPALIFNSLLTGVMYNYILRVLPKWIHHVILGLVLSILVYSFAAFSPLAYGMSGPLANEPNSTMYNLKWLSTWEF
Protein: Macrophage immunometabolism regulator (Q96GV9)
Organism: Homo sapiens (Human)
Function: Regulates the macrophage function, by enhancing the resolution of inflammation and wound repair functions mediated by M2 macrophages. The regulation of macrophage function is, due at least in part, to its ability to inhibit glycolysis. May also play a role in trafficking of proteins via its interaction with UNC119 and UNC119B cargo adapters: may help the release of UNC119 and UNC119B cargo or the recycling of UNC119 and UNC119B. May play a role in ciliary membrane localization via its interaction with UNC119B and protein transport into photoreceptor cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22085962, ECO:0000269|PubMed:30659109}. Cell projection, cilium {ECO:0000269|PubMed:22085962}. Note=Localizes to the transition zone and proximal cilium in addition to being found throughout the cytoplasm. {ECO:0000269|PubMed:22085962}.
Interaction partners:
- Protein unc-119 homolog A
- SAM pointed domain-containing Ets transcription factor
Sequence:
MEVDINGESRSTLTTLPFPGAEANSPGKAEAEKPRCSSTPCSPMRRTVSGYQILHMDSNYLVGFTTGEELLKLAQKCTGGEESKAEAMPSLRSKQLDAGLARSSRLYKTRSRYYQPYEIPAVNGRRRRRMPSSGDKCTKSLPYEPYKALHGPLPLCLLKGKRAHSKSLDYLNLDKMIKEPADTEVLQYQLQHLTLRGDRVFARNNT
Protein: Lipopolysaccharide biosynthesis protein (ORF_11; potential multiple membrane spanning domains) (Oligosaccharide flippase family protein) (Wzx) (P72137)
Organism: Pseudomonas aeruginosa
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSAAFINRVARVLVGTLGAQLITIGVTLLLVRLYSPAEMGAFSVWLSFATIFAVVVTGRYELAIFSTREEGELQAIVKLILQLTLLIFVAVAIAVVIGRHLIESMPVVIGEYWFALAVASLGLGINKLVLSLLTFQQSFNRLGVARVSLAACIAVAQVSAAYLLEGVSGLIYGQLFGVVVATALAALWVGKSLILNCIETPWRMVRQVAVQYINFPKFSLPADLVNTVASQVPVILLAAKFGGDSAGWFALTLKIMGAPISLLAASVLDVFKEQAARDYREFGNCRGIFLKTFRLLAVLALPPFIIFWFIGEWAFGLVFGEAWAESGRYAVLMVPLFYMRFVVSPLSYTIYIAQRQSMDLLWQLALLLLTFICFTLPDSVDSVLWFYSIAYAVMYFVYFWMSFQCAKGDAK
Protein: Ubiquitin-conjugating enzyme E2 1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 1) (Ubiquitin carrier protein 1) (Ubiquitin-protein ligase 1) (O74810)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Polyubiquitin
- Ubiquitin-activating enzyme E1 1
- Ubiquitin-conjugating enzyme spm2
- SUMO-conjugating enzyme ubc9
- AN1-type zinc finger protein C1271.05c
- Anaphase-promoting complex subunit 11
- RING-box protein pip1
- Ubiquitin-like protein pmt3/smt3
- RNA polymerase I-specific transcription initiation factor rrn7
- Ubiquitin-ribosomal protein eL40B fusion protein
Sequence:
MSDNRSRRIAKELADVQQDKQAGIQVWTINDDISHLKGMFRGPEGTPYEGGYFVVDIEIPIDYPFRPPKMNFDTKIYHPNVSSQTGAICLDILKDQWSPVYTMKSALISLQSLLCTPEPSNPQDAQVAQVYLQNYQQFVRTAREWTSSYAAAPAGVDLDAENTEFGGIDPNIITNLQQFGFSTELIVRVLQREHIKSQEDLKDYPNGINGILDQLLH
Protein: Uncharacterized protein (Q8IFJ4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRTNKKTQRQIILVPHTECRLPLRRGHLGAAACPPDQGLPNSTSTASLHHAYLPAANENFQQWHNKLRRQRRQRTPCKRSATPNTTYEKHSAAQLRSRIHQPKTPPRSKRPEPRRKRTNSKSQRRRQSAIKKLHRARVTPSSSPQRLHYPKERRRPVLFPRLADIDAKTAPATRNVVADAPKKNPADHIGQRSLPSPADYRPPSELVRFLEEKPEIFPIASPVTDTGVVIGGRYV
Protein: Vang-like protein 2 (Protein strabismus) (Protein trilobite) (Van Gogh-like protein 2) (Q8UVJ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in non-canonical Wnt/planar cell polarity (PCP) signaling to regulate convergent extension cell movements during gastrulation. Acts together with scrib and prickle1 and localizes prickle1 and dvl2/dsh to the plasma membrane. Has an overlapping role with kny during both convergent extension and eye development. In the eye, involved in establishing proper alignment of the anterior neural plate and midline cells expressing shha and shhb/twhh. Has indirect effects on a number of other developmental processes including notochord shape formation, neural progenitor cell morphogenesis, segregation of somites and adaxial cell development. Together with prickle1, required for the posterior (caudal) movement of branchiomotor neurons in the hindbrain independently of, and a few hours after, convergent extension. May be required for cell surface localization of fzd3 and fzd6 in the inner ear (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Prickle homolog 1a
- Prickle homolog 1b
- Prickle homolog 2b
- Prickle homolog 2a.
- Dishevelled segment polarity protein 2.
- Dishevelled segment polarity protein 1b
- Dishevelled segment polarity protein 3a
- Dishevelled segment polarity protein 3b
- Cadherin EGF LAG seven-pass G-type receptor 1
- T-box transcription factor TBX1
Sequence:
MDNESQYSGYSYKSSHSRSSRKHRDRRDRHRSKSRDSSSRGDKSVTIQAPGEPLLDAESTRGDDRDDNWGETTTVVTGTSEHSVSNEDLTRASKELEDSSPLECRRFAGPIVSGVLGLFALLTPLAFLLLPQLLWRDSLEPCGTPCEGLYVSLAFKLLVLLISSWALFLRPSRSTLPRFFVFRCLLMALVFLFVASYWLFYGVRVLEPRERDYRGIVGYAVSLVDALLFIQYLALVLLEVRHLRPAFCLKVVRTTDGASRFYNVGHLSIQRAAVWVLDHYYTDFPVYNPALLNLPKSILSKKMSGFKVYSLGEENSTNNSTGQSRAMIAAAARRRDNSHNEYYYEEAEMDRRVRKRKARLVVAVEEAFTHIKRLQDDEAAASPKHPREVMDPREAAQAIFAPMARAMQKYLRTTRQQPYHSMESIISHLQFCITHNMTPKAFLERYLTPGPTMQYQRENGRGRQWTLVSEEPVTAALRQGLVFSLRRLDFALVVTVTPLPFLNLGEEFIDPKSHKFVMRLQSETSV
Protein: Glutamate [NMDA] receptor subunit 1 (DNMDAR-I) (dNR1) (Q24418)
Organism: Drosophila melanogaster (Fruit fly)
Function: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors. Plays a role in associative learning and in long-term memory consolidation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15823532}; Multi-pass membrane protein {ECO:0000269|PubMed:15823532}. Postsynaptic cell membrane {ECO:0000269|PubMed:15823532}. Postsynaptic density {ECO:0000269|PubMed:15823532}.
Interaction partners:
- NMDA receptor 2, isoform C
- Disks large 1 tumor suppressor protein
- FI23915p1
- FI04462p
- Peripheral plasma membrane protein CASK
- Glutamate receptor 1
- Glutamate receptor IB, isoform B
- Glutamate receptor IIA
- Calcium/calmodulin-dependent protein kinase type II alpha chain
- Neuropilin and tolloid-like, isoform B
Sequence:
MAMAEFVFCRPLFGLAIVLLVAPIDAAQRHTASDNPSTYNIGGVLSNSDSEEHFSTTIKHLNFDQQYVPRKVTYYDKTIRMDKNPIKTVFNVCDKLIENRVYAVVVSHEQTSGDLSPAAVSYTSGFYSIPVIGISSRDAAFSDKNIHVSFLRTVPPYYHQADVWLEMLSHFAYTKVIIIHSSDTDGRAILGRFQTTSQTYYDDVDVRATVELIVEFEPKLESFTEHLIDMKTAQSRVYLMYASTEDAQVIFRDAGEYNMTGEGHVWIVTEQALFSNNTPDGVLGLQLEHAHSDKGHIRDSVYVLASAIKEMISNETIAEAPKDCGDSAVNWESGKRLFQYLKSRNITGETGQVAFDDNGDRIYAGYDVINIREQQKKHVVGKFSYDSMRAKMRMRINDSEIIWPGKQRRKPEGIMIPTHLRLLTIEEKPFVYVRRMGDDEFRCEPDERPCPLFNNSDATANEFCCRGYCIDLLIELSKRINFTYDLALSPDGQFGHYILRNNTGAMTLRKEWTGLIGELVNERADMIVAPLTINPERAEYIEFSKPFKYQGITILEKKPSRSSTLVSFLQPFSNTLWILVMVSVHVVALVLYLLDRFSPFGRFKLSHSDSNEEKALNLSSAVWFAWGVLLNSGIGEGTPRSFSARVLGMVWAGFAMIIVASYTANLAAFLVLERPKTKLSGINDARLRNTMENLTCATVKGSSVDMYFRRQVELSNMYRTMEANNYATAEQAIQDVKKGKLMAFIWDSSRLEYEASKDCELVTAGELFGRSGYGIGLQKGSPWTDAVTLAILEFHESGFMEKLDKQWIFHGHVQQNCELFEKTPNTLGLKNMAGVFILVGVGIAGGVGLIIIEVIYKKHQVKKQKRLDIARHAADKWRGTIEKRKTIRASLAMQRQYNVGLNSTHAPGTISLAVDKRRYPRLGQRLGPERAWPGDAADVLRIRRPYELGNPGQSPKVMAANQPGMPMPMLGKTRPQQSVLPPRYSPGYTSDVSHLVV
Protein: Anaerobic glycerol-3-phosphate dehydrogenase, B subunit, putative (Q72AQ3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Anaerobic glycerol-3-phosphate dehydrogenase, A subunit, putative
- Anaerobic glycerol-3-phosphate dehydrogenase, subunit A, truncation
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate acyltransferase
- DAK2 domain protein
- phosphoenolpyruvate--glycerone phosphotransferase
- Diacylglycerol kinase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase, putative
- Glycerol kinase
Sequence:
MSDRTYDCDLVVAGTGMAGMAAALFAARRGLSVVQAGSTGEIVFASGLFDVLGVHPMAEGRRLASPWEGMARLAADEPKHPYGVIAPSRMKDALAEFTGWLEAHGLPYRNGGDSNVRVLSPMGTVKTSWAVPSTMWAGVEALAEKKPCLLVDFEGLREYSARQIADTVGGAWPGLRTVRVEFPGTPMRPLLTGIMGQALELRVTREQLAEVIRPHLGDCACVGLPAILGIFHPGTVLAEMEAMLGVPVFEIPTLPASVPGLRLKNVFEGHIGTEGVDLMLQRKVLDVHRQDGALQVSIGQGSVERVVRARGMILATGRFLGHGLFAERDRIRETVLDLPVHQPAGRSQWHSLDLFDPAGHPVSRAGVVTDSSFRPVDEEGRVLHEDVRCVGTLLAHQDWMRQKCGVGLAVGSSAVAVDAFVAQFSAG
Protein: Glucose transporter type 1 (Q8IRI6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Facilitative glucose transporter.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAFLCAPGLTFFLTYSIFSAVLGMLQFGYNTGVINAPEKNIENFMKDVYKDRYGEDISEEFIQQLYSVAVSIFAIGGMLGGFSGGWMANRFGRKGGLLLNNVLGIAGACLMGFTKVSHSYEMLFLGRFIIGVNCGLNTSLVPMYISEIAPLNLRGGLGTVNQLAVTVGLLLSQVLGIEQILGTNEGWPILLGLAICPAILQLILLPVCPESPRYLLITKQWEEEARKALRRLRASGSVEEDIEEMRAEERAQQSESHISTMELICSPTLRPPLIIGIVMQLSQQFSGINAVFYYSTSLFMSSGLTEESAKFATIGIGAIMVVMTLVSIPLMDRTGRRTLHLYGLGGMFIFSIFITISFLIKEMIDWMSYLSVVATLGFVVFFAVGPGSIPWMITAELFSQGPRPSAMAIAVLVNWMANFVVGIGFPSMKTALENYTFLPFSVFLAIFWIFTYKKVPETKNKTFEEILALFRHNNGRSMLNCTNSLEPQSMNSGIEHAALMVSEEKTQHDSLFGTTSFSLTVEGMGPYPLSDSTNLLGPGSSSYGPGGVLGLAGSGSGLGGQCYTNYGTNLQTPQAARKCHYDEVDDYSFRRHSAHGRITQMKGKPLILGPTIKKDKKKERTDWLTASERFLEGGRSTHQGRSAASAPHHPRQPPPVCPSSGPXLRSASPPDSASVRSTSRAEEPHQPQQVHHQQQQVHHQQQHQSRYATHEYVHCSYEKEVVCDQANPSQAPPQQPAPPVQQHQQQPPPPLHHCQQRKHSHSPHHSRHTSPHSHHHHSHHSRHSRRSRRQGSGSLPGAHQGSANHSVMRPSICTSRRHRSVTDISTTNVCQDPACSDREVQEIMVRRTCCNTTATNSSSRTELAQCFAEDLYGSSRRPSSCCTSSDYCYQTDSTSLYGSRSSLSRNNSIKSASALVRKHHRSQRSLLPEHRHPSYTSISLRGLNASRPNSQLGSLTSIFDRAKNMAPEGSTLERQSSKGALGSSELPEYACSPSPIRWSFLADGRSPSEMEGAVGGGPEREQEEEDKLDAWQVPEPEPEKKPCRKITTSSSVYDEGPSTSAAAARKRRGSKGSRGSKGSGSYHCEFEDEATTTVMFHQDAGEAYNNCCSNNYNYIQCNTYLDQDLQITSEDIHQYLSKGDATASDILNNSKNYPFQPSNALEFQYKNNFQQGQANANNNNTNTTNTASSDAAECFQNYRAISKETNLNQTSTEQLSPTNINLSTSSNNINIVFSSSLERNANEVKFINNRSGASGGSEMGCEVGHHAGYLPYTYPSYDYTNMSGNSHFEKPLGIDELPKEFCGLEGAGGGGASTTSEHSSSLPSPQPLTHHQQLHHFESFDAASEHNLLAAQPMSPGSPLSGSVNPAGDDFVQMHHYHHANSPHSQSHHSHAHTHTHGHHVHHLLNHPAYDLTDDQFRLGSALKRVRKRARKYTDFLRKK
Protein: Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21 (EC 2.7.1.49) (EC 2.7.4.7) (Hydroxymethylpyrimidine kinase) (HMP kinase) (Hydroxymethylpyrimidine phosphate kinase) (HMP-P kinase) (HMP-phosphate kinase) (HMPP kinase) (Q08975)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probably that of HMP to HMP-P.
Interaction partners:
- Thiamine biosynthetic bifunctional enzyme
- Thiamine pyrophosphokinase
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI5
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI12
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI13
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI11
- Constitutive acid phosphatase
- Thiamine thiazole synthase
- Probable acid phosphatase DIA3
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20
Sequence:
MTYSTVNINTPPPYLALASNEKLPTVLSIAGTDPSGGAGVEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVSQILDANLQDMKCDVIKTGMLTTAAIEVLHEKLLQLGENRPKLVVDPVLVATSGSSLAGKDIASLITEKIAPFADILTPNIPECFKLLGEDREISKLRDIFEVAKDLAKITKCSNILVKGGHIPWNDEEGKYITDVLYLGAEQRFITFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVYGGIEYVQNAVAIGCDVTKETVKDNGPINHVYAIEIPLEKMLSDECFTASDAVHKKPVKSSLNKIPGGSFYKYLINHPKVKPHWDSYVNHDFVRKVADGSLEPKKFQFFIEQDYLYLVNYARISCIAGSKSPCLEDLEKELVIVECVRNGLCQHERRLREEFGIKDPDYLQKIQRGPALRAYCRYFNDVSRRGNWQELVIALNPCLMGYVHALTKIKDEVTAAEGSVYREWCETYSSSWCHEAMLEGEKLLNHILETYPPEKLDTLVTIYAEVCELEANFWTAALEYE
Protein: Euchromatic histone lysine methyltransferase 1 (A0A1B0GVZ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHEVLNRIQWSQIPV
Protein: Regulator of G-protein signaling 9 (RGS9) (O75916)
Organism: Homo sapiens (Human)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction; key element in the recovery phase of visual transduction (By similarity).
Subcellular location: [Isoform 3]: Membrane; Peripheral membrane protein. Note=Isoform 3 is targeted to the membrane via its interaction with RGS9BP. {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Regulator of G-protein signaling 9-binding protein
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pre-mRNA-processing factor 40 homolog B
Sequence:
MTIRHQGQQYRPRMAFLQKIEALVKDMQNPETGVRMQNQRVLVTSVPHAMTGSDVLQWIVQRLWISSLEAQNLGNFIVRYGYIYPLQDPKNLILKPDGSLYRFQTPYFWPTQQWPAEDTDYAIYLAKRNIKKKGILEEYEKENYNFLNQKMNYKWDFVIMQAKEQYRAGKERNKADRYALDCQEKAYWLVHRCPPGMDNVLDYGLDRVTNPNEVKVNQKQTVVAVKKEIMYYQQALMRSTVKSSVSLGGIVKYSEQFSSNDAIMSGCLPSNPWITDDTQFWDLNAKLVEIPTKMRVERWAFNFSELIRDPKGRQSFQYFLKKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDITVKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKDMLAKAIEPQETTKKSSTLPFMRRHLRSSPSPVILRQLEEEAKAREAANTVDITQPGQHMAPSPHLTVYTGTCMPPSPSSPFSSSCRSPRKPFASPSRFIRRPSTTICPSPIRVALESSSGLEQKGECSGSMAPRGPSVTESSEASLDTSWPRSRPRAPPKARMALSFSRFLRRGCLASPVFARLSPKCPAVSHGRVQPLGDVGQQLPRLKSKRVANFFQIKMDVPTGSGTCLMDSEDAGTGESGDRATEKEVICPWESL
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FNA6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Glutamine-dependent NAD
- Nicotinamide-nucleotide adenylyltransferase
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Purine nucleoside phosphorylase
- NAD
- Candida glabrata strain CBS138 chromosome B complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MSDESSTRRSKRLKTGPSPTSSSASSTSVSPMGPFSSGRTLRSSRLSPNRHSALGSPMMTAEEIAQQESLMPREPPSPILIGKNVKDGKFVVTAFTRKDTINACMYLKYYGLRKFWTAYFPPEINSLHLYYMIRLLGFQLKDREVLNHISKNVEEWKANKKYTISYADMNDPLDKKFTIRLLRNLYKAINKVLSTRLRLMNFFTIDHLVERLEKAKRIVVLTGAGISTSLGIPDFRSSEGFYTKIKYLGLEDPQDVFNYEIFLRDPSVFYNIANMVLPPENIYSPLHSFIKLLQDKRKLLRNYSQNIDNLESYAGIEVSKLIQCHGSFATASCVTCKWSLPGEKIFKNIRNFEIPLCPHCYKKRTKYLELYERELDGEEHIPEWFDQVDKDTIKSFGVIKPDITFFGEPLPSRFHKTVKEDIFRCDLLLCIGTSLKVAPVSEIVNMLPAHVPQVLINRDPVRHAEFDISLLGYCDDIATMIAQKCGWKIPHQKWDKELTNKKFEIKESAVSVYSVVSAD
Protein: 3-ketoacyl-CoA thiolase FadA (EC 2.3.1.16) (Acetyl-CoA acyltransferase) (Beta-ketothiolase) (Fatty acid oxidation complex subunit beta) (P21151)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids.
Subcellular location: Cytoplasm.
Interaction partners:
- Fatty acid oxidation complex subunit alpha
- Fatty acid oxidation complex subunit alpha
- Acyl-coenzyme A dehydrogenase
- Acetyl-coenzyme A synthetase
- 3-ketoacyl-CoA thiolase FadI
- Acetyl-CoA acetyltransferase
- Long-chain-fatty-acid--CoA ligase
- 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
- 2,3-dehydroadipyl-CoA hydratase
- Acetaldehyde dehydrogenase
Sequence:
MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPHSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSAAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDPVNGMVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSASDIGVFEMNEAFAAQILPCIKDLGLIEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV
Protein: tRNA wybutosine-synthesizing protein 3 homolog (tRNA-yW-synthesizing protein 3) (EC 2.1.1.282) (tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase) (Q6IPR3)
Organism: Homo sapiens (Human)
Function: Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA (By similarity).
Interaction partners:
- tRNA wybutosine-synthesizing protein 2 homolog
- S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase TYW1
- tRNA wybutosine-synthesizing protein 4
- tRNA
- tRNA wybutosine-synthesizing protein 5
Sequence:
MDRSAEFRKWKAQCLSKADLSRKGSVDEDVVELVQFLNMRDQFFTTSSCAGRILLLDRGINGFEVQKQNCCWLLVTHKLCVKDDVIVALKKANGDATLKFEPFVLHVQCRQLQDAQILHSMAIDSGFRNSGITVGKRGKTMLAVRSTHGLEVPLSHKGKLMVTEEYIDFLLNVANQKMEENKKRIERFYNCLQHALERETMTNLHPKIKEKNNSSYIHKKKRNPEKTRAQCITKESDEELENDDDDDLGINVTIFPEDY