wanglab/gogpt-training-data huggingface dataset:
Protein: Probable inactive serine/threonine-protein kinase gdt1 (Growth-differentiation transition protein 1) (Q54XS3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Regulates the transition between growth and differentiation.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKKILLSIFFVVFLLIGSECELIDTPPGYYNLKKIDKFQQFSKIQIERNNKTIYSSSFHDLFYPDICEGTIQNIPGSLYFGRSSFPGAQESSNLMITRGTKMKYRVGNGGIPIYKINVLCIEGTLEIPEGISFFNVGALFILPGGVLNSKSSIRFTDLDPYNSKMDPFNFFPGMMVLGGSLSLIGEKKRIFQATRIDDYQLQIEDFKKIGSLTNNIYLGSKVTIYSQQISEGQTCSFSFGASNDKINLTSSSSSSLRGTNCLPISKNDKNIIVHFNCKYLLGGSSESFIDSTSTVGSSIYITGDSQVQIENFTLDSIGKTTNKLYNDTKLIFSNDKPNQVIDIIKGENQRFRNSLYIEFSNSVVIKGCAIIDRVKESRAPLIFVSSNVSLSESLIVSKSGSNLIAQYGTEFIKSKLNHYFLIPPLPQPFGLNSPINFPSPFSMDYGFEGNGIYSLSPNVQSINDTFISQLIALNFNFIGNRSIITGFDNDCYSPCTNTSILFSNLIQYPVDFKINNSTYFYKLNNNNNDNNNNTNNFNLLNINNENNNNDDNNNNNNSQNHYLLNINNNGNSPGRFFTIKDLVASDTVSAYLPNSALVFNNLNATENFSFNGTVSRLDFINSSFNTNLTSTQKFFDETTTTVTNFQNTYIYGSPETTEPPEKVFGSSITPIYYFSKSVLDSLKVETVYPNEPHKMFFNSSVSLSVKLNNMGLKTPIICIFSSNGMESKEVQYNPISTKCSFLYVSEKLGNHNIRVTIKNEYSKDSSYYFIIDFPIITVYGQSLFNAGWQMIDPTSTTIIPTPTPTSTSTSTSTSTPTTTNNNQLVNDNNNKINELDGLKFQGGCIKTLGCQLSSNAKYVGGLPNVTASSTLNSLFSWGITSDVQYDPVIIDLFINKSIATLQVQLFFTFYKPIDQYSSPLSVSIQKNPVLVMEPFAGDQPFSKNLTFVYNNTQSLDFLNISFTSRGDIYLTSLAIFSVSDSLPQIIDPITPTLLPIESVKASKPAILAIVLSIVLGSLALSIITILIVKHRKRLSQFLSKSNKDIEYAQNNEIEIKVLPKITSHSSYPSISILDTISSDSIFNNQIPKNNNRYKFKNQSLNNNNYFNNNNNNNNSNNNNSNNIIYSNCNSNYSNSNSNNNNNNNNSNSNNNSNSNSNININSNSNSNSNSNSNGNNNYQIYSNKLESFKIDEISNDTIPIINSTFPDEFQTLEFQKLAFEILKREKRLDFSFRTTNDILTCCALSDFKDFSNFPLRFNQSIITFGLINGKAKLGETYYDTLSITNDSTIRFTAFLILPMDNHSATFTSDHSSFDLGPGETFSIKFSITLHCTTRFFENFSIQINSNNIKEMYTLLKIKVESESSTRLDFNDIHFQELIEKYSWEILYRGTVGDKNALLKLIKLKTKNCEEAYRELNIISRLKHQNILPLIGCVISKDYLCLAFEYPPLGSLDYIISKKKLKMSITQKIRILIDVAKGCKFLQQSSIIQKTLRARNIFLYDTNENAEVCAKVLDLTSSKTIKGLACNNYIERVDTPINLTREISIIRDPKQNNDFNNSNNSNNNNNNNNNNNNNNNNNSNNSNNSSSLKYNIHSFAVLSYELLIDEILVGDTRKFGQEKPSIGLDKIDPNIKNFIHKCWNPIDGFTFNEILKTLKDFIESLN
Protein: Interleukin enhancer-binding factor 2 (Nuclear factor of activated T-cells 45 kDa) (Q12905)
Organism: Homo sapiens (Human)
Function: Chromatin-interacting protein that forms a stable heterodimer with interleukin enhancer-binding factor 3/ILF3 and plays a role in several biological processes including transcription, innate immunity or cell growth. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. Together with ILF3, forms an RNA-binding complex that is required for mitotic progression and cytokinesis by regulating the expression of a cluster of mitotic genes. Mechanistically, competes with STAU1/STAU2-mediated mRNA decay. Also plays a role in the inhibition of various viruses including Japanese encephalitis virus or enterovirus 71.
Subcellular location: Nucleus, nucleolus. Cytoplasm {ECO:0000269|PubMed:31212927, ECO:0000269|PubMed:31878072}. Nucleus {ECO:0000269|PubMed:31878072}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Interaction partners:
- Interleukin enhancer-binding factor 3
- Heterogeneous nuclear ribonucleoproteins C1/C2
- ATP-dependent RNA helicase A
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein H
- Matrin-3
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein R
- Y-box-binding protein 1
- RNA-binding protein FUS
Sequence:
MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE
Protein: Vacuolar fusion protein CCZ1 (Ccz1p) (Autophagy-related protein 11) (Calcium-caffeine-zinc sensitivity protein 1) (Cytoplasm to vacuole targeting protein 16) (P38273)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: In complex with MON1, is required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis. The CCZ1-MON1 complex acts at the fusion of vesicles with the vacuole, through its regulation of the SNARE complex during the coordinated priming and docking stages of fusion, and particularly at the stage of tethering/docking. The CCZ1-MON1 complex acts as a guanine nucleotide-exchange factor (GEF) for Rab-type GTPase YPT7, promoting nucleotide exchange on YPT7 and triggering endosomal maturation by activating YPT7 on late endosomes.
Subcellular location: Endosome, multivesicular body membrane; Peripheral membrane protein. Prevacuolar compartment membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. Vesicle {ECO:0000269|PubMed:32391792}. Note=The association of the MON1-CCZ1 complex with the vacuole is regulated by the C-Vps/HOPS complex. Colocalizes with the small GTPase RAB5 homolog YPT10 to vesicular structures near the vacuole (PubMed:32391792). {ECO:0000269|PubMed:32391792}.
Interaction partners:
- E3 ubiquitin-protein ligase PEP5
- Vacuolar morphogenesis protein 6
- Vacuolar fusion protein MON1
- Vacuolar protein sorting-associated protein 41
- Vacuolar membrane protein PEP3
- Vacuolar protein sorting-associated protein 33
- Vacuolar protein sorting-associated protein 16
- Ypt/Rab-type GTPase YPT7
- Syntaxin VAM3
- Vacuolar morphogenesis protein 7
Sequence:
MRLHYITVFDPSRSTNENDTFKQLLLFHYFGTTDSIPSLNEKLSIIGVIQGIWSLTSSCVNKDGEDLEKIIELNNDIIFCIKVESRFFISLAISNISDDQSAIPLQYLSAYLWLSYRFFKLLNGSFSGFNKDFRKLTDLLNEFVIPFWNDIYLNLETVTNRSFTVMWPGFYKRANFQHSSYNPGEKNNVEESWDAIILQNILLDKKSYLGLKDILVYHLPKRTKAANRESMGTKTYGLVRNFTSDLNTLPDISNWLYHLHCTYGEISSHILTGNVHFKEELQVEEEQERSRDTNGRDEEESQEQQRREHQETTQNNTSELSLSERVIHNVTLPISFAYDAIHEVSTTTGVSGSLSMIMDYVPKPHWPFISSSNKSADKNNYSNSNDNANSNAPLMAQSEAVGGTIGNSRFGFLISPLNSDLLPSSYQALKLNLNFENSKDKEDFYNCLFWYFDDFLIVIVCDPDFNKICERDYLKDLSFQLCQSMECLNNEILNSQNCDNVESFAYVIRDNVTKEIDSSVPFGSPKFTSDESISTLQLAINGIDQFINDNSNSLSLANWNPITIMGGSNAISKKNTTEGFGNGVNDKTQKFKRKYLNFLNLMSAEKLWDLQVDVLQFLTSLQNSKRDPDYFQEERLLKLNNGVLCYIKENNSNLIIIIKNWFQNNGTSKAAKQRNRFSSDSSKGSSLFQSLGRDVTDWWESREI
Protein: G protein RhoBTB (LD24835p) (Rho-related BTB domain containing, isoform A) (Q9VPG7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPKMDNEQPHQELVKCVLVGDTAVGKTRLICARACNKHVSLSQLLSTHVPTVWAIDQYRIYKDVLERSWEVVDGVNVSLRLWDTFGDHDKDRRFAYGRSDVVLLCFSIASPISLRNCKMMWYPEIRRFCPDVPVILVGCKNDLRYMYRDENYLSYFGEKGTFVRAALKSDLVMPDEARAVAKELGVAYYETSVFTYFGVNEVFENAIRSALIARRQQRFWMTNLKKVQKPLLQAPFRPPKPPPPEVTVMVGNYRQDIYNMFLSQAYTDLVLVGAGGTKFAVHRFMLAAASSIFQRLLSTELTDMGGRSSSESSMVSSTFGEATIADFNDDTEALIRYESRTQRMWEHLKRRSSYQALPLMESKRSNDLYRELHHPVLQSIRLVHVENHRGVNGLQTIVTLSKLISPQALHQCLRFIYTGTIDKDCDNIEEIREAADLLELPQLTQLLSRPQTVMENSSDEPNPHICLRIKESMERHCIGDGCFSDVTFELDDGLMKAHRAVLVGRCDVMRAMLLGDFREAHSNVIVFPGVTIYTFHKLLCYLYTDQIPPISAVKCLNLLELANRLCLPRLLNLVECRVIEDLTLISQNETNETVDHCLKLLEPVKLHNAHQLAEWCMSYLCVNYNLICKFSLKGLKALHQDNQEYLREHRWPPVWYLKDYDYYQRCLNELNKELKLKTSRRESPSDDEGCLCFTGVFSCWLLGKSKRSADVSGTTDNSNADNQIFNSAGNSLNHIDLEADMDLNL
Protein: UspA domain-containing protein (Q384Y8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTFVVMCDGGPASLKAVSWASVPGYMMRQHEGEQLILLHIWERCGLPSPLQFDSPESVPQPPEEAGTAKRLPPSIAIHKTLETIMGSKATRDTLNYKLETMALQETPLNTPRSIRASMEISHGADPPRPGSRQRLSTRGGMSGKRDAEHHQQAAPEQTTEELEAAARELAEEVERRRAGIIAQYAEDRLKHHNAGALLLGAGNTTENKYISVGHVSRAVLSKIRQTYPLWFIKGNGTTLRLNTTALRHVVVLLPRPGEEGALIRDCSVVQYALGRCREGSGDVVCAVVIAEGCTPPEEIELYTQTLERLLQGQEGSINAESLISPKQEQQAPKGNEEQPQNQEAQPMAESMVPSTTEGAADANPTTATEGPAVTQEQDAHQEDEWPKVSVCQLHATKQVTEPTATRVPIQVVKFLQQRKTDVIVIASTVVEELQLALLGMTKQHVLVVPTPEPATLVSRTEPTPDPSKETSIL
Protein: Glycosyltransferase (Homeodomain-like superfamily protein) (Q7X887)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein At4g19900
- Glycosyltransferase-pyrophosphoryl-undecaprenol N-acetylglucosamine transferase)
- Glycosyltransferase
- At3g57630
- At1g19710
- dolichyl-phosphate beta-glucosyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 1
- Pentatricopeptide repeat-containing protein At5g03800
- Beta-arabinofuranosyltransferase RAY1
Sequence:
MGKSSGRNGNGSFNGNKFHGVRPYVRSPVPRLRWTPDLHRCFVHAVEILGGQHRATPKLVLKMMDVKGLTISHVKSHLQMYRGGSKLTLEKPEESSSSSIRRRQDSEEDYYLHDNLSLHTRNDCLLGFHSFPLSSHSSFRGGGGGRTKEQQTSESGGYDDDADFLHIKKMNDTTTFLSHHFPKGTEEWREQEHEEEEEDLSLSLSLNHHHWRSNGSSVVSETSEAAVSTCSAPFVSKDCFGSSKIDLNLSISLLGS
Protein: At3g14430 (GRIP/coiled-coil protein) (Q9LRR8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F7A19.25 protein
- non-specific serine/threonine protein kinase
- Probable protein phosphatase 2C 51
- Protein OXIDATIVE STRESS 3
- Histone-lysine N-methyltransferase SETD1B-like protein
- Probable beta-D-xylosidase 7
- Phospholipid-transporting ATPase 1
- Probable alpha,alpha-trehalose-phosphate synthase 9
- D-3-phosphoglycerate dehydrogenase 1, chloroplastic
- Large ribosomal subunit protein uL14mz
Sequence:
MIGRRAGTNRVGMRRDDSLLTRFVDSVFYFFRLAEFEILFVLFMLITYVIFKDLTSRPEYNRILVEKPGGSDIWPF
Protein: H/ACA ribonucleoprotein complex subunit DKC1 (Dyskerin) (Q7ZUT3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, Cajal body {ECO:0000256|ARBA:ARBA00004408}.
Interaction partners:
Sequence:
MADTESKKEKKRKSKKISDEEVGDIQESGDFLIKPESKVASLDTSQWPLLLKNFDKLNIRTAHYTPLPHGSNPLKRGIHDYVRSGFINLDKPANPSSHEVVAWIKRILRVEKTGHSGTLDPKVTGCLIVYVERATRLVKSQQSAGKEYVGIVRLHNALENEHQLARALECLTGALFQRPPLIAAVKRQLRVRTIYESKLIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVLGEKDNLVTMHDVLDAQWQFDHNKDETYLRRVIFPLEKLLISHKRIVMKDSAVNAICYGAKIMLPGVLRYEDGIEVNQDIVVITTKGEAICTAVALMTTAVISTCDHGVVAKIKRVIMERDTYPRKWGLGPKASQKKMMIQKGLLDKHGKPNNSTPSDWKEGYVDYSTTKVKKGGEASAKRKRDESGSEGEAAAAAQDTSKTEEESKKEKKKKKKEKKQKLAEEAAAEAPAEEETEVTESAKKKKKKKK
Protein: Pectate lyase L (EC 4.2.2.2) (Q76EC9)
Organism: Thermoclostridium stercorarium (Clostridium stercorarium)
Function: Cleaves polygalacturonate or partially methylated pectin. When assayed on polygalacturonate or on pectin, it releases monogalacturonate as the principal product.
Subcellular location: Secreted {ECO:0000269|PubMed:16306696}.
Interaction partners:
Sequence:
MRNCKGLSILLCFLLVFFAMPFPAVAEEAEAMPVSEASEWSFSAFGSNTSVEKNPDPMINSDGSVKIVANGGKIASNEQGISFYYREVPSDANFEIKAKAEVLNFKGDDKQVSFGLMLMDQIGQHRNSEKHNSNYIAVGALDTIIKAFYMQESLTKTDMLSQTPSQGDIFELSIKKSGDNYVLTCNGTTETFTLPGLFSDTIYVGIYAARNAEIKFSDLNFTLDTKDIVDLSVDLSGMKTSYLVDEPLNLKGLKVTAHYSDGTSEELTEEDYIVTGFDSSTPGTNTICINVGEISKTIDLEILPLTCTKLTVKYLPAKTDYYLGDSFNPEGLKVIAEYNDGYKVTELTEDKYALYIAGKAAEDYVFSKAGTQKVEVISRENPSVKTGFEVNISDASIESLEISRKPEKTAYFIGDEPDLTGLVVYARYSDGSKVRLDKSEYEVKGFDSSAPGEKEITVYHKGKTVAFSVVVKEKEVMGIEVTKYPKTTYYIGETFNAEGLEVSKVYDNGDREPLTDFSVDASAFDGSTPGVYDVIISADGFDPITLKVTVREKTEYEWKAIRFGQSTSDSKNYVNFLDNGAVEIVALEGGGKIATDHDGITFYYTEIDAKDNFVLSADIKVKEYAKNPHDGQESFGIMARDAIGTPGDSSIFASNIAAIGGFSGGTKSPNGTQLFIRTGVSSPDGAGSKGIRRIMIKDEKPGPDNTYPAAEYRLTLAKTNSGFVGKLNDGEEVIFYEPDILNVQDSKIYVGFFAARLATIEVSNIELYVSSSETDAPRYIPPEAPVTPSLQILSLDKTSNVNYSLVVKPNVNGSITVKQGAEILVRDVTVNAGEKYSVDAVLEKNSENPFTVIFIPDDTQNLSSYEKIIKNFSVTMRTYNEGGNIYVSPNGTPYGDGTKDNPLDLDTAIAFVKEGQKIILMNGVYKRDSALVISRYNDGTAENRKYLVAEPGSRPVIDFDKKGQGVTLSGNYWYIEGIDFARSAPNYPGFIIGGNYNIVENCRFYENGDTGLQISRTDSSENIAEWPSYNKIINCESFDNRDPSENNADGFAAKLTCGVGNMFIGCVSHHNIDDGWDLYTKAGTGAIGPVIIDSCIAYENGTLTDGTVGKGDKNGFKLGGEGVPVQHIIKNSIAFNNGAVGFTSNSNPSVIAINNIAYNNAKGNLVFTSYSGIETHFVVDGFVSYNTEGAPRDSATGVPASDDNYLFDGTKSVNKSGEELTEKEFIERLLELISKIKSIK
Protein: Baculoviral IAP repeat-containing protein 1b (Neuronal apoptosis inhibitory protein 2) (Q9QUK4)
Organism: Mus musculus (Mouse)
Function: Sensor component of the NLRC4 inflammasome that specifically recognizes and binds type III secretion system (T3SS) rod proteins such as S.typhimurium (Salmonella) PrgJ and B.thailandensis BsaK from pathogenic bacteria. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri. Prevents motor-neuron apoptosis induced by a variety of signals.
Interaction partners:
- NLR family CARD domain-containing protein 4
- Baculoviral IAP repeat-containing protein 1e
- Caspase-1
- NACHT, LRR and PYD domains-containing protein 1a
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 6
- Baculoviral IAP repeat-containing protein 1f
- NACHT, LRR and PYD domains-containing protein 3
- Gasdermin-D
- Apoptosis-associated speck-like protein containing a CARD
Sequence:
MAAQGEAVEEIICEFDDDLVSELSTLLRVDALSVLKRQQEEDHKTRMKMKKGFNSQMRSEAKRLKTFETYDKFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFSTRLRKLPIENHKKLRPECEFLLGKDVGNIGKYDIRVKSPEKMLRGDKARYHEEEARLESFEDWPFYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLQSKKSPEEITQYVQSYEGFLHVTGEHFVNSWVRRELPMVSAYCNDSVFANEELRMDTFKDWPHESPGAVEALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQTLKSSAEVIPALQSHCALPEAMETTSESNHDDAAAVHSTVVDVSPSEAQELEPASSLVSVLCRDQDHSEAQGRGCASSGTYLPSTDLGQSEAQWLQEARSLSEQLRDTYTKATFRHMNLPEVYSSLGTDHLLSCDVSIISKHISQPVQGSLTIPEVFSNLNSVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLYRFQLVFYLSLSSITPGQELAKIICAQLLGAGGCISEVCLSSIIQQLQHQVLFLLDDYSGLASLPQALHTLITKNYLSRTCLLIAVHTNKVRGIRPYLDTSLEIKEFPFYNTVSVLRKLFSHDIMRVRKFINYFGFHEELQGIHKTPLFVAAVCTDWFKNPSDQPFQDVALFKAYMQYLSLKHKGAAKPLQATVSSCGQLALTGLFSSCFEFNSDNLAEAGVDEDEELTTCLMSKFTAQRLRPVYRFLGPLFQEFLAAVRLTELLSSDRQEDQDLGLYYLRQINSPLKAMSIYHTFLKYVSSHPSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPEALLWIECLRGLWQLSPESFSLFISENLLRICLNFAHESNTVAACSPVILQFLRGRTLDLKVLSLQYFWDHPETLLLLKSIKISLNGNNWVQRIDFSLIEKSFEKVQPPTIDQDYAIAFQPINEVQKNLSEKKHIIKKYEDMKHQIPLNISTGYWKLSPKPYKIPKLEVQVTNTGPADQALLQVLMEVFSASQSIEFRLSDSSGFLESIRPALELSKASVTKCSMSRLELSREDQKLLLTLPTLQSLEVSETNQLPDQLFHNLHKFLGLKELCVRLDSKPDVLSVLPGEFPNLHHMEKLSIRTSTESDLSKLVKLIQNSPNLHVFHLKCNFLSNCEPLMTVLASCKKLREIEFSGRCFEAMTFVNILPNFVFLKILNLRDQQFPDKETSEKFAQALGSLRNLEKLFVPTGDGIHQVAKLIVRQCLQLPCLRVLVFAETLDDDSVLEIAKGATRGGFQKLENLDLTLNHKITEEGYRNFFQVLDNLPNLKNLDISRHIPECIQIQAITVKALGQCVSRLPSLTRLGMLSWLLDEEDIKVINDVKERHPQSKRLTVHWRWVVPFSPVIQK
Protein: Polyribonucleotide nucleotidyltransferase 1, mitochondrial (EC 2.7.7.8) (3'-5' RNA exonuclease OLD35) (PNPase old-35) (Polynucleotide phosphorylase 1) (PNPase 1) (Polynucleotide phosphorylase-like protein) (Q8TCS8)
Organism: Homo sapiens (Human)
Function: RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Also plays a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16055741}. Mitochondrion matrix {ECO:0000269|PubMed:12798676, ECO:0000269|PubMed:16055741}. Mitochondrion intermembrane space {ECO:0000269|PubMed:16966381}; Peripheral membrane protein {ECO:0000269|PubMed:16966381}.
Interaction partners:
- ATP-dependent RNA helicase SUPV3L1, mitochondrial
- Exosome complex component 10
- Exosome complex exonuclease RRP44
- Exosome complex component RRP41
- Exosome complex component MTR3
- Exosome complex component RRP46
- DIS3-like exonuclease 1
- Exosome complex component RRP42
- Exosome complex component RRP4
- Exosome complex component RRP43
Sequence:
MAACRYCCSCLRLRPLSDGPFLLPRRDRALTQLQVRALWSSAGSRAVAVDLGNRKLEISSGKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRREIGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLSDIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQDFCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFTDYEHDKVSRDEAVNKIRLDTEEQLKEKFPEADPYEIIESFNVVAKEVFRSIVLNEYKRCDGRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKDKNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESNGSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYNGDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSAMHEARDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIKHPTALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSSNSQ
Protein: HMG2-induced ER-remodeling protein 1 (Q12276)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for HMG2-induced endoplasmic reticulum-remodeling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-2
Sequence:
MSSKLKYTDIDVPLDWLYKGKRRNRTKSAASTRTSEATTTSVKKTATLPSTAAVPTKTIASPQRPLSGQNVNNELSNSKPAVSAEKVSQQGQVPTRRTRSHSVSYGLLQKKNNNDDTTDSPKISRIRTAQDQPVKETKSSTLAEPIVSKKGRSRSSSISTSLNERSKKSLFGSLFGRRPSTTPSHVVERPLSSQNDHKKSTELPPIDTRQSKISTPTSTPTTASSKPSSSGGNRHSDGSLTSKLLSIPHNILETSSTNFNAHHHIQSHHSSGREQDSPHSESSDLPPILEKETTQKQLQKVSKVNLKRVTIAVQEFNSDPPQQLPSRKPKRGNVLIPEDMISAPPLISLGITNSSDQSSFQSNISPSYSKDSKEYKLALENFKKAAKEAEKHQKDAYYVAERMAQEVANYKARQLKTSPLTGATNSAADSATDQESSSLDARASKLHIDKPINVGAHPFETHQDDNIKYSSHLEQTLDVAYTRCCHLREILPIPSTLRQVKGKTAPLQTLKFLNPKPTLVDILSFCDFIAITPIHNIIFDNVSLTHDMFKIVICSLVTSPVVEKLGLRNVVINEQSWKLLCKFLLQNKTLIKLDISQTKARTDLNDSNYRDQMDWELFCEVLRNREGRPLEELLLNGLRFDKMSFSHFKNILLTFAQMNPKNPIRLGMANVEFSTECFDFLFNWMSEYNVQGVDLAYNNLESLAKRMIKKLARLPYKHLEYFTLNSTNITSVDDMSYILKYLSRLPSIKFLDLSNLPQLFPGILTSGYKYFPQFPQLKRIHFDFDDLSIKETTMLVSILAKCETLSHVSLIGQSPMPDASKISDSTDEPDKSKDEKKEQIVFMRNTLWASLYAFVRDSHNLVSLDVDYDQVPDEIQSRIALCLMHNMKRIMDSSFKLDELTVQDDLIFDGSLITETAEEVLKRLNDKSLLQNDVGKKYLLKKYFEKMEKVHHNVQNTIDSMFEKRKSGELPLQEKENLLRLLLLEKNLSNILDIFASMPNIADVVPFSKADNSFPNIGDSTVSANYNDGIRPSLKHLDSDRLINDVSIPENDSSIRPHLMATDSGRIIDVTTGKALLFKSSSNTSLAGKRQEEEEGELHKWGVFVQHQSSRHNSGLPSSANSSRISGSLTPDSSVAGGKKGESSRTSGTRPKILPKIPTGAELRDAIIKAKGIDSVDDLIKNVTSEKVGLESLYGDELNSRSPSNDSLQESQQKAPLQRPLVEDETVTKKYDKLLNDLSNVRHSKT
Protein: Glial fibrillary acidic protein (F1RR02)
Organism: Sus scrofa (Pig)
Interaction partners:
- Aquaporin-4
- Neurotrophic factor BDNF precursor form
- Oligodendrocyte transcription factor 2
- Microtubule-associated protein
- Paired box 6.
- Caspase-3
- Lactoperoxidase
- Myelin basic protein
- Doublecortin
- Interleukin-6
Sequence:
MERRRVTSAARRSYVSSLETVGGGRRLGPGPRLSLARMPPPLPARVDFSLAGALNTGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANGARLEVERDNLAQDLGTLRQKLQDETNLRLEAENNLATYRQEADEATLARLDLERKIESLEEEIRFLRKIHDEEVRELQEQLAQQQVHVEMDVTKPDLTAALREIRTQYEAVATSNMQEAEEWYRSKFADLTDAAARNAELLRQAKHEANDYRRQLQALTCDVESLRGTNESLERQMREQEERHAREAASYQEALTRLEEEGQSLKDEMARHLQEYQELLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRGGKSTKEGEGHKVTRHLKSLTIQVIPIQAHQIVNGAPPALETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVV
Protein: Echinoid, isoform C (M9PCI6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRRKTTTKGTAIVNSRSARRAATTICNFFLIALVALSSTTLADESIDTRENADLTLKCRFNDKYEANDFSFFWTRWTANPAQFDNVAIGEVQLSSGYRLDFQPERGIYDLQIKNVSYNRDNGRFECRIKAKGTGADVHQEFHNLTVLTPPHPPVISPGNIAVATEDKPMELTCSSIGGSPDPTITWYREGSNTPLPATVLKGGTKDQPTNATLSIIPRREDDGAKYKCVVRNRAMNEGKRLEATATLNVNYYPRVEVGPENPLRVERDRTAKLECNVDAKPKVPNVRWNRNGRFISSSLVHTIHRVSVQDAGKYTCIADNGLGKTGEQELILDILYPPMVVIESKTREAEEGDTVTIRCNVTANPAPVTIEWLKENSPDFRYNGDVLTLTSVRADHAGNYICRAVNIMQSQGMERSERVGNSTVALLVRHRPGQAYITPNKPVVHVGNGVTLTCSANPPGWPVPQYRWFRDMDGEFSSTQKILAQGPQYSIPKAHLGNEGKYHCHAVNELGIGMMATIVLEIHQPPQFLAKLQQHMTRRVADTDYTVTCSAKGKPAPSVKWLKDAVEILPEENLYEVQTNPDQGLNGMVTVQSQLKFRGKARPNGNALVPGDRGLYTCLYQNEVNSANSSMQLRIEHEPIVLHQYNKVAFDIRETAEVVCKVQAYPKPEFQWQFGNNPSPLTMSSDGHYEISTTTDNNDIYTSVLKINSLTHSDYGEYTCRVANTLDTIRAPIRLQQKGPPEKPTNLRATEVGHNYVSLSWDPGFDGGLSKTKFFVSYRRVAMPREEQLIPDCATLANSNSAWVEVDCQRDIPCKVTALEQHQSYAFKVKALNPKSDSPYSSEIMVTTKVSRIPPPLQVTYEPNTRTLGIDVGATCLNLVAVVESMVNADSPMAAWEVVTTMDNLQLSGNGPTHKEKIIDRIIGARRVGGGRALGHTISEDEDDNGLNSLALEDENSPTVRVKLCLRTNPEHCGDYTDAEIGRPYIAEANALATPTLIAIIVSCVVFALFAGLILMFCRCKRNQSKKSAAAKDYEMDSVRPSIVAAQQNQAPPPYYPASGLDNKALEHSMDLALSMEDQKTALYATQNGYSYHPGSGVVGVGMGGGVVGVGVGGSVVSGMGGGVGGIGGSGVGVNGIPGLSAHTMPGNEWVNMGYMENNYSNSNNGGSVNSQDSLWQVKMSAAAVGNQQGMVQAPMNQYVEQQPAYGYDPLTHGGYGAVDDYAPYPHLTATPSQVGDEYHNLRNSQNPSRQDYCSDPYASVQKPKKRVDQHLADIIQDVTL
Protein: Glucokinase-1 (EC 2.7.1.2) (Glucose kinase 1) (GLK-1) (P17709)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Two isoenzymes, hexokinase-1 and hexokinase-2, can phosphorylate keto- and aldohexoses in yeast, whereas a third isoenzyme, GLK, is specific for aldohexoses. All glucose phosphorylating enzymes are involved in glucose uptake.
Interaction partners:
- Hexokinase-1
- Hexokinase-2
- Glucose-6-phosphate isomerase
- Phosphoglucomutase 2
- Glucose-6-phosphate 1-dehydrogenase
- ATP-dependent 6-phosphofructokinase subunit alpha
- Invertase 2
- High glucose sensor RGT2
- Fructose-1,6-bisphosphatase
- Low glucose sensor SNF3
Sequence:
MSFDDLHKATERAVIQAVDQICDDFEVTPEKLDELTAYFIEQMEKGLAPPKEGHTLASDKGLPMIPAFVTGSPNGTERGVLLAADLGGTNFRICSVNLHGDHTFSMEQMKSKIPDDLLDDENVTSDDLFGFLARRTLAFMKKYHPDELAKGKDAKPMKLGFTFSYPVDQTSLNSGTLIRWTKGFRIADTVGKDVVQLYQEQLSAQGMPMIKVVALTNDTVGTYLSHCYTSDNTDSMTSGEISEPVIGCIFGTGTNGCYMEEINKITKLPQELRDKLIKEGKTHMIINVEWGSFDNELKHLPTTKYDVVIDQKLSTNPGFHLFEKRVSGMFLGEVLRNILVDLHSQGLLLQQYRSKEQLPRHLTTPFQLSSEVLSHIEIDDSTGLRETELSLLQSLRLPTTPTERVQIQKLVRAISRRSAYLAAVPLAAILIKTNALNKRYHGEVEIGCDGSVVEYYPGFRSMLRHALALSPLGAEGERKVHLKIAKDGSGVGAALCALVA
Protein: Zinc finger BED domain-containing protein 39 (Abnormal cell migration protein 39) (P34418)
Organism: Caenorhabditis elegans
Function: Regulates the timing and orientation of distal tip cell migration during gonadal development. May act in parallel to cacn-1 and Rac GTPases to control the anterior and posterior migration of distal tip cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:25446539}. Cytoplasm {ECO:0000269|PubMed:25446539}. Note=Expressed in the nucleus of distal tip cells and in the cytoplasm of germ cells. Localized to the peripheral chromatin region of the nucleus. {ECO:0000269|PubMed:25446539}.
Interaction partners:
- Nuclear speckle splicing regulatory protein 1 homolog
- E3 ubiquitin ligase rnf-121
Sequence:
MSSVSSDIDGPPETKRFRIDVDTQVGIDTPSVSTNCAPPVAGEASQDGQSPAAPSSASYRSSNSSVISSSESPIKDEDVDVHDGQDDTEDIAMDVSGSTGSIVNNSEIFEMLNKTFGGVFNCDLEGIMRPSALMHPSSPPTPIQSAGIPGALAVAQSPAAQLFSGDDWSWHRNPAASIRSGGTNKQTPVWKYFVYNKTENLSRCIVGDCTYMLKGPHTSTLACHLKKHTREYSEFQKLKTEYSRTKLDQQPKIPDGAPHPLTLQTQNTPRQTGSPASTCNTNSNTSSSVSSGSGIGSGSGSTMDLSMKKPKKEPSSAKLNEMLFNGLRQATNNSNGSPPTTPHAPQLPNIPSFVTNMMLQMNPLHMMLAQSLPGATPPTPTSSNAGLNALQQAGLTLAANGQIIQSKKWRNDDKKQKELCTKFALALATSHVDFEVVQNPLWKEVFEMAQPKFSIPTESQYEHIVNSTSHKLIQSLKSQLSASKKLNLLLDITKITADISRVTVSVALTGGAGNSYETQVILLAFRNINGNQSEDLTAVFEKVLQDYNISPSSINRVICSGLNELAEPAELPKQMDSFSSRLANCFKSWLETSPTVEVLKKNVYAMLVSYLTVPAAIQLASQMLKAKFEVPLTEPFHVIVEHLVAHRDIYQMNMEGITLISEREWNKVTGIHHLMNIFKPFMTYSTDMTTVDTVIPTIVQIQNVLEKDIYHLGDIGSDLLTSLKQTVAPIMNPEHENFDSTYIQATALNPQLAVTLTSDQMTTAKSLIETEISRRTKKMRKAQSDKKLAMGVDSLLANVMRKNDGGSDGGCETALAIYGDLFQSITGNSSESKENIVNQYFDEISSTTSVESMFMLRTFGNPMQAPLSYWKSCSSRCSELSDLATELLSIPIFTLTAERVLSFSPDSSSLNTNLILTNLDSTDQFEKQVLLRFNRQIVSKLFN