wanglab/gogpt-training-data huggingface dataset:
Protein: Dihydromethanopterin reductase (acceptor) (H(2)MPT reductase) (EC 1.5.99.15) (Q8PVV3)
Organism: Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Function: Involved in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. Catalyzes the reduction of dihydromethanopterin (H(2)MPT) to tetrahydromethanopterin (H(4)MPT). Ferredoxin may serve as an electron donor.
Interaction partners:
Sequence:
MSFQRIAWGITGAGHFLDRSYQVFKELKLRNPELSVNTYVSRAAEEVLRMYGLEQKLVKISGGDYLEEIFRESEQGSSSPKVGRFALDRYDALFVTPATSNTVSKIAYGIADSLVTNAVSQAVKGRVPVFVVPVDIEGSIISEMPYNIDRKQCKHCETCPPRENCPHEAISEKNGVTDQIDLLKCKGCGICKELCPYNAIKGGPVEVLVRDVDMRNVEIVKSLQGITVLESPEAILELF
Protein: 60 kDa lysophospholipase (EC 3.1.1.5) (Lysophospholipase-transacylase) [Includes: L-asparaginase (EC 3.5.1.1) (L-asparagine amidohydrolase); 1-alkyl-2-acetylglycerophosphocholine esterase (EC 3.1.1.47) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase)] (O88202)
Organism: Rattus norvegicus (Rat)
Function: Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities. Can catalyze three types of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3) transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of 1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2 to -1 transfer). Mediates the synthesis of 1-arachidonoyl species of phospholipids by transferring the arachidonoyl residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-acyl lysophospholipid.
Interaction partners:
- Asparagine synthetase
- Isoaspartyl peptidase/L-asparaginase
Sequence:
MARATGPEQRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLRTLHMLHDEEYARAHSLPEDTLVLPPASSDQRIIYKVLECQPLFDSSDMTITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASWKSHLVVHSNMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVTSDYAPGMAMAGAGIISGFDMTSEAALAKLSYVLGQPGLSLSDRKKLLAKDLRGEMTLPTTDDLLGDDMLGCRATWLLSMNGSQDADAMKDVLLPGLALAAAHAGDLDTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLSPQELEDVGTELCRLASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSLEDRVSAQPQPH
Protein: Peptidyl-tRNA hydrolase (Pth) (EC 3.1.1.29) (P9WHN7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
Interaction partners:
- Large ribosomal subunit protein bL25
- Ribosome-binding ATPase YchF
- Peptide chain release factor 1
- Transcription-repair-coupling factor
- Putative lipoprotein LpqT
- Ribosome-recycling factor
- GMP synthase
Sequence:
MAEPLLVVGLGNPGANYARTRHNLGFVVADLLAARLGAKFKAHKRSGAEVATGRSAGRSLVLAKPRCYMNESGRQIGPLAKFYSVAPANIIVIHDDLDLEFGRIRLKIGGGEGGHNGLRSVVAALGTKDFQRVRIGIGRPPGRKDPAAFVLENFTPAERAEVPTICEQAADATELLIEQGMEPAQNRVHAW
Protein: Uroplakin-3a (UP3a) (Uroplakin III) (UPIII) (P38574)
Organism: Bos taurus (Bovine)
Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12475947}; Single-pass type I membrane protein {ECO:0000269|PubMed:12475947}. Note=Heterodimer formation with UPK1B is a prerequisite to exit out of the endoplasmic reticulum (ER).
Interaction partners:
- Uroplakin-1a
- Uroplakin-2
- Uroplakin-1b
- Keratin, type I cytoskeletal 20
Sequence:
MPPLWVVLALGCLRLGSGVNLQPQLASVTFATNNPTLTTVALEKPLCMFDSSAALHGTYEVYLYVLVDSASFRNASVQDSTKTPLSSTFQQTQGGRTGPYKAAAFDLTPCSDSPSLDAVRDVSRASEILNAYLIRVGTNGTCLLDPNFQGLCNPPLSAATEYRFKYVLVNMSSGLVQDQTLWSDPIRTDRLTLYSAIDTWPGRRSGGMIVITSILGSLPFFLLIGFAGAIVLSLVDRGDADGATSHDSQITQEAVPKSLGTSEPSYTSVNRGPSLDRAEVYASKLQD
Protein: Always early (Q2PNN1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRHQLKKPRKMVAAWQNDELFIKRPNFAPRIRISEKPEIQGRVKPGVASKRIENFTKKPSKISVDVSEDEKAKEKEKEQDPYSNDFILGKRLYNFLKYLSSHRWIWCEFVDSFLDKPTLTMGYDMKRFIAEYCPLLHSCFMPRRGWQLVRRNMGKARRFSAAFIELEREELECQRRIVRQLQQHKFNPKENVGYLDQIPKRVPLPLAKDATVSSFLHGKSFEGIVNGTVMGYDPQDYTYLVRFNRNDNAVVLSLPDSQLYSDEETAAVPLSIIMRGNKSSSVISESAKTEKFGNKRYTKELLESVLRVGKLQDVKHKILMDLARMNEDFETFKEIGSSSSRRDAKVTPQRENLQRRYSASMITLHRVNADILEPLRILHDYLVEYQKQDEEEESKRGRPASEVYQKCRMQAEQDLKTAADERFLKIESNRTQEFVRDLHTILYLNGKLGRENSSNLETIIADLVTHMVDNIQPSLGRKLKDGVDSLEPLRQQVVQIFKDVKKPERFQITQQAPMQTEDGIYNFVVEAQPDTPS
Protein: CS domain-containing protein (Q381N7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MADTEAVAGTEAIPPTQNEQHDSAAKKKQANSYYYWHNHEKERAKVGDVAPMPKPVLLKKSDPSVLPASTASYPITKHSWCDGKKNVTVYIDTKLDEKETMVEDTLQVEFGKRRLTVSYIANVQTSKDVATQRRKQLVLCLAKAIKSKESSYKVKDPSGQIVIRLAKAEETSWWELAKKDGKLSDADDSDEENEGKADEGDGAAEEKA
Protein: CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase (EC 2.4.3.6) (Beta-galactoside alpha-2,3-sialyltransferase 3) (Alpha 2,3-ST 3) (Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase) (N-acetyllactosaminide alpha-2,3-sialyltransferase) (ST3Gal III) (ST3GalIII) (ST3N) (Sialyltransferase 6) [Cleaved into: CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase soluble form] (Q02734)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
Interaction partners:
- Beta-1,4-galactosyltransferase
- Beta-1,4-galactosyltransferase
- Galactoside alpha-
- Hexosyltransferase
- Beta-1,4-galactosyltransferase 3
- Galactoside alpha-
- Beta-galactoside alpha-2,6-sialyltransferase 1
- Hexosyltransferase
- Beta-galactoside alpha-2,6-sialyltransferase 2
- Hexosyltransferase
Sequence:
MGLLVFVRNLLLALCLFLVLGFLYYSAWKLHLLQWEDSNSLILSLDSAGQTLGTEYDRLGFLLKLDSKLPAELATKYANFSEGACKPGYASAMMTAIFPRFSKPAPMFLDDSFRKWARIREFVPPFGIKGQDNLIKAILSVTKEYRLTPALDSLHCRRCIIVGNGGVLANKSLGSRIDDYDIVIRLNSAPVKGFEKDVGSKTTLRITYPEGAMQRPEQYERDSLFVLAGFKWQDFKWLKYIVYKERVSASDGFWKSVATRVPKEPPEIRILNPYFIQEAAFTLIGLPFNNGLMGRGNIPTLGSVAVTMALDGCDEVAVAGFGYDMNTPNAPLHYYETVRMAAIKESWTHNIQREKEFLRKLVKARVITDLSSGI
Protein: Ada2a-containing complex component 3, isoform D (Ada2a-containing complex component 3, isoform E) (M9NFF9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ada2a-containing complex component 2
- Transcriptional adapter 2A
- Ada2a-containing complex component 1
- Molybdopterin synthase catalytic subunit
- DNA polymerase epsilon subunit 3
- DNA-binding protein Ets97D
- Protein will die slowly
- SAGA-associated factor 29kDa
- Transcriptional adaptor 3, isoform C
- Host cell factor
Sequence:
MHSLGASKVVATLRADGHVYPMENSNLMHYEIRTEGDVQQKKGILVGPATCVDLGKQLLQCARDSDVAGVKAALAHGAPFASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAELEAARQAQASKKLHEESEQQAHKTKKETNEAVSSIMDEPEVIKTVDDKEMSVEERMDVLENMRGHANVLRNTALYILKTHEIADMVQDNDDEDSKEMLNTALQNGRQLVLSEGGRMLLHETKSGISGKQSTNGNARPSVAALRTNVNNSHPKIRMNVLKQKDLPSPAGVAKNKNIRIISLTDFKKLYGSDSTAKSLQKIPASLASSGMVRHLPDGTKLVNMRQLQARQLKLPSLQRPQDLTALEESHSQNEAAVPSPLPSGHPASGSSLRGQVGTVQTIQLRPSLSAGSGQGAVNNGAAPGKTIVNATKQSPKSPNVMPLLTSSEICRQLHELRRQNEDLRRRADSFQREKEEMLRRIDRLEQMVLVQESEADLDFGEDV
Protein: Proline-rich protein 5 (Protein observed with Rictor-1) (Protor-1) (Q812A5)
Organism: Mus musculus (Mouse)
Function: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in regulation of PDGFRB expression and in modulation of platelet-derived growth factor signaling. May act as a tumor suppressor in breast cancer (By similarity).
Interaction partners:
- Target of rapamycin complex 2 subunit MAPKAP1
- Serine/threonine-protein kinase mTOR
- Rapamycin-insensitive companion of mTOR
- Target of rapamycin complex subunit LST8
- TELO2-interacting protein 1 homolog
- DEP domain-containing mTOR-interacting protein
- Proline-rich protein 5-like
- Telomere length regulation protein TEL2 homolog
- Proline-rich AKT1 substrate 1
- Regulatory-associated protein of mTOR
Sequence:
MRTLRRLKFMSSPSLSDLGKREPGAAGTDERGTQQRRACANATWNSIHNGVIAVFQRKGLPDQELFILNEGVRQLLKTELGSFFTEYLQNQLLTKGMVILRDKIRFYEGQKLLDSLAETWDFFFSDVLPTLQAIFYPVQGKEPSVRQLALLHFRNTITLSVKLEDALARSHARVPPAIAQMLLVLQGVHESRGVTEDYLRLETLIQKVVSPYLGTYGLYSNEGPCTHSCILEKRFLRRSRSGDILAKNPVVRSKSYNTPLLNPVAEHEAEGTAASGTSIRRHSVSEMTSCPEPQGFVDTPGQGPSGTFRSSPTPHSGPCPSRLYPPAHSPEQGPGHGSPSTSSPETLVDQILESADSDSEGIFIDFGRGSRSSVSDFEAPGGRPSVV
Protein: G protein-coupled receptor 88 (Striatum-specific G-protein coupled receptor) (Q9GZN0)
Organism: Homo sapiens (Human)
Function: Probable G-protein coupled receptor implicated in a large repertoire of behavioral responses that engage motor activities, spatial learning, and emotional processing. May play a role in the regulation of cognitive and motor function.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9ESP4}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium membrane {ECO:0000269|PubMed:23936473}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9ESP4}. Nucleus {ECO:0000250|UniProtKB:Q9ESP4}. Note=Localized to cilia in ciliated cells; whereas in non-ciliated cells, distributed throughout the cell membrane (PubMed:23936473). During cortical lamination, subcellular location shifts, on the day of birth, from expression at the plasma membrane and in the cytoplasm to the nuclei of neurons. This intranuclear localization remains throughout adulthood. {ECO:0000250|UniProtKB:Q9ESP4, ECO:0000269|PubMed:23936473}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- G-protein coupled receptor 6
- G-protein coupled receptor 52
Sequence:
MTNSSSTSTSSTTGGSLLLLCEEEESWAGRRIPVSLLYSGLAIGGTLANGMVIYLVSSFRKLQTTSNAFIVNGCAADLSVCALWMPQEAVLGLLPTGSAEPPADWDGAGGSYRLLRGGLLGLGLTVSLLSHCLVALNRYLLITRAPATYQALYQRRHTAGMLALSWALALGLVLLLPPWAPRPGAAPPRVHYPALLAAAALLAQTALLLHCYLGIVRRVRVSVKRVSVLNFHLLHQLPGCAAAAAAFPGAQHAPGPGGAAHPAQAQPLPPALHPRRAQRRLSGLSVLLLCCVFLLATQPLVWVSLASGFSLPVPWGVQAASWLLCCALSALNPLLYTWRNEEFRRSVRSVLPGVGDAAAAAVAATAVPAVSQAQLGTRAAGQHW
Protein: Kinetochore protein mis14 (NMS complex subunit mis14) (Q9P6M3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Required for correct chromosome segregation where it has a role in the formation and/or maintenance of specialized chromatin at the centromere.
Subcellular location: Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore.
Interaction partners:
- Kinetochore protein mis13
- Inner kinetochore subunit mis15
- Inner kinetochore subunit fta2
- Outer kinetochore KNL1 complex subunit spc7
- Inner kinetochore subunit mal2
- Centromere protein mis12
- Inner kinetochore subunit fta3
- Inner kinetochore subunit mis17
- Kinetochore protein spc24
- Kinetochore protein nuf2
Sequence:
MSSHGDASVLPKIALESINDYSYVKSVFRQAIQEKLAIHLPEQASREAGMGREDQLRIRVKEMLNELIESTFSIIQENVTINGFDANSALQDPKNSDQIEPFDLALRTRVQQLFNEVEDAHVLVARYRKSVPAQYEKAYVDAMEQQTAFLRNVKDDYVSLQDKEVENPDEQTSTTVFRKEDIDRYEQTIAKVAYLKKNLPRVVARLEKTP
Protein: Ribosome biogenesis protein WDR12 homolog (WD repeat-containing protein 12 homolog) (Q54W52)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03029}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029}.
Interaction partners:
- Pescadillo homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Ribosome biogenesis protein BOP1 homolog
- WD repeat-containing protein DDB_G0290555
- RRM domain-containing protein
- Ribosome biogenesis protein BRX1 homolog
- Ribosome assembly factor mrt4
- Nucleolar complex protein 2 homolog
- Guanine nucleotide-binding protein-like 3 homolog
- Eukaryotic translation initiation factor 6
Sequence:
MESENKNNNKKVKEESKVKVKFITNDANIRVTDTPIAVPVRLGRLGLSEVIHHLREEENETSKPFDFLINGKFIRTTLDKHIKNANLSEEQIITIEYLEAITEPKREKECQHDDWVSCVDGSNFGLVVSGSYDLGVRVWGYDGELISTGTGHLAGVKSVCWISDKNADNLSFVSASMDKTLRVWNFNKSQSEIKALACLKEHTGTIESVYVSPDSSRIVSASMDSTIKLWSIKDIPNQHATTSSSIEKSNSKKRRLANNTNNETAAVDQQSEIIHNITESLASVTVPNSQGVTVVNWTTQFQMLSGSMDSKIRLWDVSTLVANDTIPTPAPLTDLDYSMESGLIVTAHKDRIVRIWDPRSSDETKSQTQSLISHKTWVTSVNWNPSSKYHCCSTSHDGTVKYWDIRTKIPLYTIDTLEKSKDKVLSSSFISNKNKNINDYSIVSGGTDSKLRIHYNDKQEQQQ
Protein: Glyceraldehyde-3-phosphate dehydrogenase GAPA2, chloroplastic (EC 1.2.1.13) (NADP-dependent glyceraldehydephosphate dehydrogenase A subunit 2) (Q9LPW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-diphosphoglycerate by NADPH (By similarity).
Subcellular location: Plastid, chloroplast stroma {ECO:0000305}.
Interaction partners:
- Triosephosphate isomerase, chloroplastic
- Triosephosphate isomerase, cytosolic
- Phosphoglycerate kinase 1, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPB, chloroplastic
- Phosphoglycerate kinase 3, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic
- Phosphoglycerate kinase 2, chloroplastic
- Transketolase-1, chloroplastic
- Transketolase-2, chloroplastic
- Fructose-bisphosphate aldolase 2, chloroplastic
Sequence:
MASATFSVAKPSLQGFSEFSGLRNSSALPFAKRSSSDEFVSFVSFQTSAMRSNGGYRKGVTEAKIKVAINGFGRIGRNFLRCWHGRKDSPLDVVVINDTGGVKQASHLLKYDSTLGIFDADVKPSGDSALSVDGKIIKIVSDRNPSNLPWGELGIDLVIEGTGVFVDRDGAGKHLQAGAKKVLITAPGKGDIPTYVVGVNAELYSHEDTIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKTFAEEVNAAFRDAAEKELKGILDVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK
Protein: Suppressor of SWI4 1 homolog (Ssf-1) (Brix domain-containing protein 3) (Peter Pan homolog) (Q9NQ55)
Organism: Homo sapiens (Human)
Function: May have a role in cell growth.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
Interaction partners:
- P2Y purinoceptor 11
- RRP15-like protein
- Pescadillo homolog
- Ribosome biogenesis protein BOP1
- WD repeat-containing protein 74
- Probable rRNA-processing protein EBP2
- Ribosome biogenesis regulatory protein homolog
- Ribosomal RNA processing protein 1 homolog B
- mRNA turnover protein 4 homolog
- Nucleolar complex protein 2 homolog
Sequence:
MGQSGRSRHQKRARAQAQLRNLEAYAANPHSFVFTRGCTGRNIRQLSLDVRRVMEPLTASRLQVRKKNSLKDCVAVAGPLGVTHFLILSKTETNVYFKLMRLPGGPTLTFQVKKYSLVRDVVSSLRRHRMHEQQFAHPPLLVLNSFGPHGMHVKLMATMFQNLFPSINVHKVNLNTIKRCLLIDYNPDSQELDFRHYSIKVVPVGASRGMKKLLQEKFPNMSRLQDISELLATGAGLSESEAEPDGDHNITELPQAVAGRGNMRAQQSAVRLTEIGPRMTLQLIKVQEGVGEGKVMFHSFVSKTEEELQAILEAKEKKLRLKAQRQAQQAQNVQRKQEQREAHRKKSLEGMKKARVGGSDEEASGIPSRTASLELGEDDDEQEDDDIEYFCQAVGEAPSEDLFPEAKQKRLAKSPGRKRKRWEMDRGRGRLCDQKFPKTKDKSQGAQARRGPRGASRDGGRGRGRGRPGKRVA
Protein: Inositol-3-phosphate synthase 1 (IPS 1) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (MI-1-P synthase) (MIP synthase) (MIPS) (Q8I3Y8)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner (By similarity). Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity). De novo-synthesized myo-inositol is essential for incorporation into GPI (glycosylphosphatidylinositol) glycolipids during intra-erythrocytic development.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A, putative
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Oocyst capsule protein
Sequence:
METYKGIQFFSNKGTVKNAFKKSNLGYEVMLDRKEDENFIYSNYEHVETQVEKDSKGMVVCKKYKNTYEILVEKVKEKRLGVLLVGIGGNNATTMLGGICANAKDLSYMNKCDLKRSNYLGSVFLSSNIRLGYNEKDKEHAYAPIYKLIDIYNPENIVYGGWDINNMNLKDCLVRNKVFDNEVIEKIKDDLDYVPLKSVYFKGNFIAGNQQRRVNNILYGKNKLEILEQVREQIRNFKKQNNLNELIVLWSGNTEKNIPHIPGVNDTFLNILHACKKNHESVSPSVIYALAAILENSPFINSSPQNTLVSAVVQLAQQKGIFIIGNDLKTGQTKIKNFLLDFYFGTGLKPKSIVSYNHLGNNDGKNLSSDLQFYSKKVSKSNLICDYVRANENLYVDDEKDTNVLVKKSIDYCEGDSLNEKGKVSADIEDDCTYVESLEKQKVNSEIVIKYVPYVGDDKKAIDEYISEIFMNGKNTIVLYNICQDSMLASPILIDLILLVELSQRVFFKPNQEKKTNEDEHLLNENIQIEDYKLSHTILKPKYSSFKNLDSVLFLSSLFCKSPFNSTVYKTRHSFFSQLESLWNFVRIISGLPIDAHIDLPYMI
Protein: Multicilin (Multiciliate differentiation and DNA synthesis-associated cell cycle protein) (McIdas protein) (Protein Idas) (Q08B36)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription regulator specifically required for multiciliate cell differentiation. Acts in a multiprotein complex containing E2F4 and E2F5 that binds and activates genes required for centriole biogenesis. Activates genes required for centriole assembly (plk4, cep152) and genes specifically required for motile cilia formation (foxj1). Also promotes the deuterosome pathway of centriole biogenesis by activating expression of ccdc67/deup1, but not its paralog cep63.
Subcellular location: Nucleus {ECO:0000269|PubMed:22231168}.
Interaction partners:
Sequence:
MQNRRKAFYKLCPNAMPDLSNRLSKKQSKTEKKLHKNIFAHTGPVTIYVDPPSSAVDSALATIDWQDLVDCNSVIQQDAAGGAITQQQDHCLSGEPDFDLQEFRDAVDQFIADQPSLMQPSLGPPEFQLPACNVPVFEPCMTNPLQAQPEHLLPINVQTIPSTEQYWRDVADHNQKALGDALVENNQLQVSLTEKQEEIVSLKEKNIQLNELANQAKHLSSVLDKLMKERTKQNSGATQGRLPVKRSLEDFYPQSNEPDSTQVDEILREISKKCNIALMGSDLSERKRPRLEPMDSMDWQEEGVTEIKMCGAFHGLKTSTGLNSVNLGDTDLEDVSFRTSIKEHSTIRTLAFPQGNAFTIRTSGGGYKFRWVPN
Protein: Uncharacterized protein (Q385G7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRGADQVLVINRSLSAPCATLRHLSTLSERCAVEDTGVVLALRNPRLPLPRAVSLFPNFITSSSSFSCRHAAKVGKAIVATEPVDACEGGSPADATALRDRLGAAELQISLLDNASKISLERYTVLDEANTLLRQQLQEARSEIKRLRVENQQLRELLEKRELV
Protein: Transcription initiation factor TFIID subunit 6 (TAFII-60) (TAFII-62) (Transcription initiation factor TFIID 62 kDa subunit) (p62) (P49847)
Organism: Drosophila melanogaster (Fruit fly)
Function: TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 10b
- Transcription initiation factor TFIID subunit 8
- TBP-associated factor 3
- TATA-box-binding protein
Sequence:
MSGKPSKPSSPSSSMLYGSSISAESMKVIAESIGVGSLSDDAAKELAEDVSIKLKRIVQDAAKFMNHAKRQKLSVRDIDMSLKVRNVEPQYGFVAKDFIPFRFASGGGRELHFTEDKEIDLGEITSTNSVKIPLDLTLRSHWFVVEGVQPTVPENPPPLSKDSQLLDSVNPVIKMDQGLNKDAAGKPTTGKIHKLKNVETIHVKQLATHELSVEQQLYYKEITEACVGSDEPRRGEALQSLGSDPGLHEMLPRMCTFIAEGVKVNVVQNNLALLIYLMRMVRALLDNPSLFLEKYLHELIPSVMTCIVSKQLCMRPELDNHWALRDFASRLMAQICKNFNTLTNNLQTRVTRIFSKALQNDKTHLSSLYGSIAGLSELGGEVIKVFIIPRLKFISERIEPHLLGTSISNTDKTAAGHIRAMLQKCCPPILRQMRSAPDTAEDYKNDFGFLGPSLCQAVVKVRNAPASSIVTLSSNTINTAPITSAAQTATTIGRVSMPTTQRQGSPGVSSLPQIRAIQANQPAQKFVIVTQNSPQQGQAKVVRRGSSPHSVVLSAASNAASASNSNSSSSGSLLAAAQRSSDNVCVIAGSEAPAVDGITVQSFRAS
Protein: Vascular cell adhesion protein 1 (V-CAM 1) (VCAM-1) (CD antigen CD106) [Cleaved into: Soluble Vascular Cell Adhesion Molecule-1] (P29533)
Organism: Mus musculus (Mouse)
Function: Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.
Subcellular location: [Vascular cell adhesion protein 1]: Cell membrane {ECO:0000250|UniProtKB:P19320}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P19320}.; SUBCELLULAR LOCATION: [Soluble Vascular Cell Adhesion Molecule-1]: Secreted {ECO:0000250|UniProtKB:P19320}.
Interaction partners:
- Integrin beta-1
- Integrin alpha-4
- Intercellular adhesion molecule 1
- Integrin beta-2
- Integrin alpha-M
- Integrin alpha-L
- CD44 antigen
- Integrin alpha-9
- C-X-C chemokine receptor type 4
- Moesin
Sequence:
MPVKMVAVLGASTVLWILFAVSQAFKIEISPEYKTIAQIGDSMALTCSTTGCESPLFSWRTQIDSPLNAKVRTEGSKSVLTMEPVSFENEHSYLCTATCGSGKLERSIHVDIYSFPKDPEIQFSGPLEVGKPVTVKCLAPDIYPVYRLEIDLFKGDQLMNRQEFSSEEMTKSLETKSLEVTFTPVIEDIGKALVCRAKLHIDQIDSTLKERETVKELQVYISPRNTTISVHPSTRLQEGGAVTMTCSSEGLPAPEIFWGRKLDNEVLQLLSGNATLTLIAMRMEDSGVYVCEGVNLIGRDKAEVELVVQEKPFIVDISPGSQVAAQVGDSVVLTCAAIGCDSPSFSWRTQTDSPLNGVVRNEGAKSTLVLSSVGFEDEHSYLCAVTCLQRTLEKRTQVEVYSFPEDPVIKMSGPLVHGRPVTVNCTVPNVYPFDHLEIELLKGETTLMKKYFLEEMGIKSLETKILETTFIPTIEDTGKSLVCLARLHSGEMESEPKQRQSVQPLYVNVAPKETTIWVSPSPILEEGSPVNLTCSSDGIPAPKILWSRQLNNGELQPLSENTTLTFMSTKRDDSGIYVCEGINEAGISRKSVELIIQVSPKDIQLTVFPSKSVKEGDTVIISCTCGNVPETWIILKKKAKTGDMVLKSVDGSYTIRQAQLQDAGIYECESKTEVGSQLRSLTLDVKGKEHNKDYFSPELLALYCASSLVIPAIGMIVYFARKANMKGSYSLVEAQKSKV
Protein: 60S ribosomal protein L19, putative (Q57ZI7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L2, putative
- 40S ribosomal protein S15a, putative
- Large ribosomal subunit protein uL5
- Ribosomal protein
- 60S ribosomal protein L4
- Ribosomal protein S19, putative
- 60S ribosomal protein L18a
- 60S ribosomal protein L27, putative
- 60S ribosomal protein L7a
- Elongation factor 2
Sequence:
MVSLKLQARLAADILRCGRGRVWLDPNEAVEIRNANSRKSVRKLIKDGLVMRKPVKVHSRSRWRQMKLAKSMGRHEGTGRREGTREARMPSKDLWMRRLRILRRLLRKYREEKKIDRHIYRELYMKAKGNVFRNKRNLMEHIHKVKNEKKKARQLAEQLAAKRLKDEQNRRKARKQELKKREKERERARRDDAAAAAAAKQRAAAKKAAAPAAKKGGKAVAPATPAKAAPAKAAAAKVAPAKAAPAKAASPAGKKAAGKK
Protein: Cis-aconitate decarboxylase (CAD) (aCAD) (EC 4.1.1.6) (Aconitate decarboxylase) (Cis-aconitic acid decarboxylase) (Q0C8L3)
Organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Function: Involved in the production of itaconic acid, a soluble unsaturated dicarboxylic acid mainly produced from sugars.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P54987}.
Interaction partners:
Sequence:
MTKQSADSNAKSGVTAEICHWASNLATDDIPSDVLERAKYLILDGIACAWVGARVPWSEKYVQATMSFEPPGACRVIGYGQKLGPVAAAMTNSAFIQATELDDYHSEAPLHSASIVLPAVFAASEVLAEQGKTISGIDVILAAIVGFESGPRIGKAIYGSDLLNNGWHCGAVYGAPAGALATGKLLGLTPDSMEDALGIACTQACGLMSAQYGGMVKRVQHGFAARNGLLGGLLAYGGYEAMKGVLERSYGGFLKMFTKGNGREPPYKEEEVVAGLGSFWHTFTIRIKLYACCGLVHGPVEAIEKLQRRYPELLNRANLSNIRHVYVQLSTASNSHCGWIPEERPISSIAGQMSVAYILAVQLVDQQCLLAQFSEFDDNLERPEVWDLARKVTPSHSEEFDQDGNCLSAGRVRIEFNDGSSVTETVEKPLGVKEPMPNERILHKYRTLAGSVTDESRVKEIEDLVLSLDRLTDITPLLELLNCPVKSPLV