wanglab/gogpt-training-data huggingface dataset:
Protein: Dpr-interacting protein delta, isoform D (Dpr-interacting protein delta, isoform E) (A8JNC7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Defective proboscis extension response 12, isoform C
- Common Dpr-interacting protein
Sequence:
MFILTVVKLLLIALNIFPSRFTNRRIMFLIYMTNLVTHVMMDEPRFAQPIPNVTVAVGRDANLPCVVEHLGGYKVAWIHIDRQMILTIHRHVISRIPRYSITYTDNTWLLHVNQAHQDDRGYYMCQVNTNPMISQVGYLQVVVPPNILDIESTPSSVAVRENQNINMTCRADGFPAPKIIWRREDGEEIAVEKKKKVLVYDADVLPLTKVSRNEMGAYLCIATNGVPPSVSKRIILDVEFSPMIWVPNQLVGAPSGTDVTIDCHTEAHPKAIIYWVYNSVMVLPSKKYKTDYTENSYRAHMKLTIRNLQYGDFGNYRCISKNSLGETEGSIRVYEIPLPSTPSKQVTHTTVESRENNIIPSSRNDTTKSLQTDVGYAMKNDLYPGSASSSSSGGSSSAASSSSSMQTSALPGGVAGNSLSSMGSKGSLAIGKSTFYTERPPNEYAASSVAGLLLHRALLFGSGIYLTLL
Protein: Uncharacterized protein Rv0502 (P9WKT1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv0501
- Uncharacterized protein Rv0500B
- Conserved protein TB16.3
Sequence:
MGNVAGETRANVIPLHTNRSRVAARRRAGQRAESRQHPSLLSDPNDRASAEQIAAVVREIDEHRRAAGATTSSTEATPNDLAQLVAAVAGFLRQRLTGDYSVDEFGFDPHFNSAIVRPLLRFFFKSWFRVEVSGVENIPRDGAALVVANHAGVLPFDGLMLSVAVHDEHPAHRDLRLLAADMVFDLPVIGEAARKAGHTMACTTDAHRLLASGELTAVFPEGYKGLGKRFEDRYRLQRFGRGGFVSAALRTKAPIVPCSIIGSEEIYPMLTDVKLLARLFGLPYFPITPLFPLAGPVGLVPLPSKWRIAFGEPICTADYASTDADDPMVTFELTDQVRETIQQTLYRLLAGRRNIFFG
Protein: Erythroid transcription factor (Eryf1) (GATA-binding factor 1) (GATA-1) (GF-1) (NF-E1 DNA-binding protein) (P43429)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS.
Subcellular location: Nucleus.
Interaction partners:
- TAL bHLH transcription factor 1, erythroid differentiation factor
- Rhombotin-2
- LIM domain binding 1
- Zinc finger protein, multitype 1
- Runt-related transcription factor 1
- KLF transcription factor 1
- Bromodomain containing 3
- Transcription factor PU.1
- Growth factor independent 1B
- Transcription factor E2-alpha
Sequence:
MDFPGLGALGTSEPLPQFVDSALVSSTSDSAGFFSSGPESLDTASSSTSPNAATAAATALAYYREAEAYRHSPVFQVYPLLNSMEGIPGSSPYASWAYSKTALYPASTVCPSHEDAPSQTLEDPDGKNNNTFLETLKTERLSPDLLTLGTALPTSLPVTSSAYGGADFPSPFFSPTGSPLSSAAYSSPKFHGSLPLAPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRMIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYYKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSSLAGAGAAEGPAGGFMVVAGGSSSGNCGEVAPGLTLGTAGTAHLYQGLGPVVLSGPVSHLMSFPGPLLGSPTASFPTGPVPTTTSTSVVSPLSS
Protein: Uroporphyrinogen decarboxylase (EC 4.1.1.37) (C6KSS1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Protoporphyrinogen oxidase
- coproporphyrinogen oxidase
- Ferrochelatase
- hydroxymethylbilane synthase
- Threonylcarbamoyladenosine tRNA methylthiotransferase
- Delta-aminolevulinic acid dehydratase
- tRNA 4-demethylwyosine synthase
- Triosephosphate isomerase
- 4-hydroxybenzoate polyprenyltransferase, putative
- Glucose inhibited division protein a homologue, putative
Sequence:
MLKCLVTPLLICILTIKILCFINLKKLRFNIIKTETILNMNEVGEIYSRPENLKYEKFGRPQNDLILNVIENKNEEKKFKKIPLWIMRQAGRYLPEYVEIRKKYDFFEICKSPDLSSYVSIMPYDRFKTDMIVIFSDILIIFVAMGIDIKFVENLGPVFNLEIYNMNDFNKLNLNMKEIIDNLYYVYDSINLTKKKINNDVPILGFCGSPFTLFMYLTKNNKKTYEDSFKFLYEKPNDAHQIINKLSDICLNHLINQIDSGANIIQIFDSNAELVDKNIFNEFSIIYLKKVIEIIKKYRPNIYIILFIKNNFHDDIKNLKIDVLSITHKQLIDNTDQFYFKLFQNNIILQGALDPYILLLNDHELIQKHIIQMMKNITHKNKYIANLGHGILPTTKIKNVNLFIDTIRNNEWS
Protein: Glycerol kinase (Glycerokinase) (EC 2.7.1.30) (ATP-stimulated glucocorticoid-receptor translocation promoter) (ASTP) (ATP:glycerol 3-phosphotransferase) (Q63060)
Organism: Rattus norvegicus (Rat)
Function: Key enzyme in the regulation of glycerol uptake and metabolism (By similarity). Increases the binding of activated glucocorticoid-receptor to nuclei in the presence of ATP.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P32189}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:P32189}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P32189}. Note=Glycerol kinase activity is more cytosolic in some tissues. It probably represents the expression of isoforms lacking a transmembrane domain. {ECO:0000250|UniProtKB:P32189}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P32189}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:P32189}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P32189}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 3
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- 1-acylglycerol-3-phosphate O-acyltransferase 6
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- Aldo-keto reductase family 1 member A1
- aldose reductase
- Aldo-keto reductase family 1 member B1
- Aldo-keto reductase family 1 member B7
- Non-selective voltage-gated ion channel VDAC3
Sequence:
MAAAKKAVLGPLVGAVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKAIGVSNQRETTVVWDKLTGEPLYNAVVWLDLRTQSTVEKLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGINGGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSLEPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKSIGWVTTQSPESGDPSIFCSLPLGFFIVSSMVMLIGARYISGIP
Protein: WW domain containing oxidoreductase (F5H3R5)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAALRYAGLDDTDSEDELPPGWEERTTKDGWVYYANHTEEKTQWEHPKTGKRKRVAGDLPYGWEQETDENGQVFFVDHINKRTTYLDPRLAFTVDDNPTKPTTRQRYDGSTTAMEILQGRDFTGKVVVVTGANSGIGKASCHVGRILKHTRVEELSLLPTAINRELPPPCTVLLSQNWRVWEGCTSTTAAAACPHQKLRAKRRPGPCGRSARG
Protein: rRNA-processing protein UTP23 homolog (Q9CX11)
Organism: Mus musculus (Mouse)
Function: Involved in rRNA-processing and ribosome biogenesis.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- KRR1 small subunit processome component homolog
- WD repeat-containing protein 43
- Something about silencing protein 10
- Probable U3 small nucleolar RNA-associated protein 11
- Neuroguidin
- U3 small nucleolar ribonucleoprotein protein IMP3
- U3 small nucleolar ribonucleoprotein protein IMP4
- U3 small nucleolar RNA-associated protein 14 homolog A
- Ribosomal RNA small subunit methyltransferase NEP1
- WD repeat-containing protein 46
Sequence:
MKITRQKHAKKHLGFFRNNFGVREPYQILLDGTFCQAALRGRIQLRDQLPRYLMGETQLCTTRCVLKELETLGKELYGAKLIAQKCQVRNCPHFKSPVSGSECLLSMVDEGNPHHYFVATQDQNLSVKVKRTPGIPLMFIIQNTIVLDKPSPRTVAFVKAVEAGQLVSVHEKQSIKQLKEEQGLVRNPDLRRRRRKKKKVGGPNPLSCLKKKKKAQDTKSPASEKKRKRKRIRNRSTLKVSSEQQGAEG
Protein: Crossover junction endodeoxyribonuclease RuvC (EC 3.1.21.10) (Holliday junction nuclease RuvC) (Holliday junction resolvase RuvC) (P9WGV9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00034}.
Interaction partners:
- Holliday junction branch migration complex subunit RuvB
- Holliday junction branch migration complex subunit RuvA
- Protein RecA
- LexA repressor
- Regulatory protein RecX
- UvrABC system protein A
- Uncharacterized protein Rv2897c
- UvrABC system protein B
- Error-prone DNA polymerase
- ATP-dependent DNA helicase UvrD1
Sequence:
MRVMGVDPGLTRCGLSLIESGRGRQLTALDVDVVRTPSDAALAQRLLAISDAVEHWLDTHHPEVVAIERVFSQLNVTTVMGTAQAGGVIALAAAKRGVDVHFHTPSEVKAAVTGNGSADKAQVTAMVTKILALQAKPTPADAADALALAICHCWRAPTIARMAEATSRAEARAAQQRHAYLAKLKAAR
Protein: RE21473p (Stardust, isoform D (EC 2.7.4.8)) (Stardust, isoform K) (Q9W3H7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVVSTLHITLENNGNVAAGQPAAVAAASVVGAATSPTKFAVLSAQQLQLQLQQQQQQQNEKENHMNNNNNNSDYCDMNGNGVGMGNGGSGGPGSLTPQSPDQYVGSPVSSAATPQRTASALRRGIQIQRSSTRLRQQQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPHTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: 23 kDa U4/U6.U5 small nuclear ribonucleoprotein component (Q12368)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor SPP381
- U4/U6 small nuclear ribonucleoprotein PRP3
- Pre-mRNA-splicing helicase BRR2
- LSM complex subunit LSM7
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Pre-mRNA-splicing factor 38
- Small nuclear ribonucleoprotein Sm D3
- Pre-mRNA-splicing factor 6
- U4/U6 small nuclear ribonucleoprotein PRP4
- LSM complex subunit LSM3
Sequence:
MSNFGRRTWDREEYAEQARSGYDDRSLKATLTPIELQALKSKYTNYDHLIKGSLKDLNKRKLTANTESLSSFKRGKKFGFYCDICNLTFKDTLQYIDHLNHKVHAIKFENLFDEPLIIDIRDNDDVPQEEFELCYHNLIKDFVEVRSMETQSKRKRLLDTDVEKAKKVATKPSIESESKVSQMMGFSNFATSKK
Protein: GLC7-interacting protein 3 (Q03016)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Endoplasmic reticulum {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-2
- GLC7-interacting protein 4
Sequence:
MITNTEFDVPVDWLYKGKSRRKTNTKPSRPSTSPASSSSTSSSKNGDNSTSGNRSSNDKPRARSSSVSNAALCNTEKPDLKRNDGNTSASDTDNIPLLTPINSGNRSDSADIDNPATVDAIDLIDNDDNGSSTQFVRKKRSTSISNAVVSSKPRLASSAINATASSSVGKGKHPPISSPSNATLKRSNSTSGEKTKRSIFGSLFSKRSTSSSASTAKKPLPVVNTSTTENESGGIKAVATPDPRVKEISSPMRGVAPTASKPQTPILPSPALAVKDLSTVSLKRVSFAVDKFESDPPQQLPSRTPKKGNILIPDDMISEVPSISVGISSSNQSAKSTNSNIKGPLYTKKSKEYILALENQKLALREAAKHQQEAHFAANRIAFEVANFKTASDAGGKLTEKSSEGTITKQREEVSPPNVEADRELENNKLAENLSKAGIDKPIHMHEHYFKEPDQDKYQDGHSIENNEVTLDVIYTRCCHLREILPIPSTLRQVKDKTAPLQILKFLNPKPTLIDILSFCDFITIAPIHTIVFDNVALNQDMFRIIISALVNSTVLDKLSLRNVRIDQDGWKLLCKFLLLNKSLNKLDISQTKIKSDLAESLYRHNMDWNLFTDVLSQRSHKPIEELLFNGIQFSKIPYSCFARLLTSFATQKNFPESGIRLGLAGATTSNISQDCLKFIFNWMSQYNVQGVDLAFNDLSTMIKPMVGKLSALSYDNLRYFILNSTNISTSYDLALLLKYLSKLPNLIFLDLSNLSQCFPDILPYMYKYLPRFPNLKRIHLDSNNLTLKELAVVCNILIKCKSLSHVSMTNQNVENFYLMNGTDSPVQQTNTDGDLDSSSTLDVKGQFAKNSFSSTLYAFARDSPNLIGLDFDYDLISEEIQSRIALCLMRNMKRTMDSTFQLDELDSQDDLLFDGSLVTMTAESVLEKLNLLSDKSTKVKKDTTKRYLLKKYIEKFHILHHNVQHTIDTMFEKRKSGELPLQEKENLVRLLLLEQNLCNILELFSHNPNLNDVLGSSRDDSKESVDSSEDSKLPALKHVESGYHVPEEKIQPENDVITARPHLMATDSGKTIDVFTGKPLVFKHTSSSTSVGCKKQEEEEGELHKWGFFVQQQRSLYPENESTRQTPFASGDTPINTETAGKSTSSPSVSTSNNETATTSLFSPANPKILPKIPSGAVLRSAIMKAKGIDSIDDLIQNVNSNNIELENIYGESIQNSASTFTPGVDSDVSAPNTDKGSVETLPAVSTDDPNCEVKVTATYDKLLNNLSMERSIRL
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (P18943)
Organism: Gallus gallus (Chicken)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00396}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00396}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b
- NADH-ubiquinone oxidoreductase chain 2
- NADH-ubiquinone oxidoreductase chain 4
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 5
- Cytochrome c oxidase subunit 5A.
- Cytochrome c oxidase subunit 3
- NADH-ubiquinone oxidoreductase chain 3
Sequence:
MTFINRWLFSTNHKDIGTLYLIFGTWAGMAGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFHYLAGVSSILGAINFITTIINMKPPALSQYQTPLFVWSVLITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVRMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGFTHWFPLFTGFTLHPSWTKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISMTAVIMLMFIVWEAFSAKRKVLQPELTATNIEWIHGCPPPYHTFEEPAFVQVQE
Protein: F-box/WD repeat-containing protein pof1 (Skp1-binding protein 1) (P87053)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. Required for the inactivation of zip1 via ubiquitination.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Suppressor of kinetochore protein 1
- Cullin-1
- Transcription factor zip1
- RING-box protein pip1
- Mitosis inhibitor protein kinase wee1
- F-box/WD repeat-containing protein pof10
- F-box protein pof6
- F-box protein pof14
- VEL1-related protein AC977.05c
- Pof6 interactor protein 1
Sequence:
MTTGYESVPTSEPSDNLAPRAELWQRHLLEKKEGDQSISVSAFNISSMHNELSGLSEKSRQRVEAVWAAFSEASCSERKLALQGILNNCSSSLLSFASSTLDSLVRLDFLSLLPVEISFRILSFLDARSLCQAAQVSKHWKELADDDVIWHRMCEQHINRKCEKCGWGLPLLERNTLYAAKASIQKRYERLTKRGVDQAHESSPVKKAKLDDYPTSSNEETISSVKPPSPNSDSKFFLPFKTRPWKEVYAERCRVECNWRHGRCRQVVLSGHSDGVMCLQLVRNILASGSYDATIRLWNLATFQQVALLEGHSSGVTCLQFDQCKLISGSMDKTIRIWNYRTSECISILHGHTDSVLCLTFDSTLLVSGSADCTVKLWHFSGGKRITLRGHTGPVNSVRIIRDRGLVLSGSDDSTIKIWSLETNTCLHTFSAHIGPVQSLALADSRLFSCSLDGTIKQWDIEKKKCVHTLFGHIEGVWEIAADHLRLISGAHDGVVKVWEACECVHTLKNHSEPVTSVALGDCEVVSGSEDGKIYLWLFNNAPNESPVSTQSVPISSLNGQRSNSSVQRALSSVPNYSSSLSNISTRNLNIPPSNANNDDVSIQS
Protein: Aquaporin TIP1-1 (Tonoplast intrinsic protein 1-1) (ZmTIP1-1) (ZmTIP1;1) (ZmTIP1) (O64964)
Organism: Zea mays (Maize)
Function: Water channel required to facilitate the transport of water across cell membrane. May support the rapid influx of water into vacuoles during cell expansion, permit osmotic equilibration between the cytosol and the vacuolar content and rapid transcellular water flow through living cells. Its function is impaired by Hg(2+).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:9701570}; Multi-pass membrane protein {ECO:0000269|PubMed:9701570}. Note=Tonoplast.
Interaction partners:
- Putative NAC domain transcription factor superfamily protein
- Aquaporin SIP1-1
- Putative receptor-like protein kinase
- Putative receptor-like protein kinase
Sequence:
MPINRIALGSHQEVYHPGALKAAFAEFISTLIFVFAGQGSGMAFSKLTGGGPTTPAGLIAAAVAHAFALFVAVSVGANISGGHVNPAVTFGAFVGGNITLFRGLLYWVAQLLGSTVACFLLRFSTGGQATGTFGLTGVSVWEALVLEIVMTFGLVYTVYATAVDPKKGSLGTIAPIAIGFIVGANILVGGAFDGASMNPAVSFGPALVSWEWGYQWVYWVGPLIGGGLAGVIYELLFISHTHEQLPSTDY
Protein: Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (AtUBP14) (TITAN-6 protein) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14) (Q8L6Y1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Involved in seed and embryo development.
Interaction partners:
- Ubiquitin-ribosomal protein eL40y fusion protein
- Ubiquitin-ribosomal protein eL40z fusion protein
- Ubiquitin C-terminal hydrolase 13
- Ubiquitin C-terminal hydrolase 12
- Ubiquitin-ribosomal protein eS31z fusion protein
- Ubiquitin-ribosomal protein eS31y fusion protein
- Ubiquitin-ribosomal protein eS31x fusion protein
- Beclin-1-like protein
- Ubiquitin carboxyl-terminal hydrolase 24
- Ubiquitin carboxyl-terminal hydrolase 26
Sequence:
MELLRSNLSRVQIPEPTHRIYKHECCISFDTPRSEGGLFVDMNSFLAFGKDYVSWNYEKTGNPVYLHIKQTRKSIPEDRPLKKPTLLAIGVDGGFDNNEPEYEESYSIVILPDFVSLPFPSVELPEKVRIAVDTVVNAVGAERKEQVAAWTAEKKLISEHALTLQQIKSGIVIPPSGWKCSKCDKTENLWLNLTDGMILCGRKNWDGTGGNNHAVEHYKETAYPLAVKLGTITADLEAADVYSYPEDDSVLDPLLAEHLAHFGIDFSSMQKTEMTTAERELDQNTNFDWNRIQESGKELVPVFGPGYTGLVNLGNSCYLAATMQIVFSTHSFISRYFSHQSLKMAFEMAPADPTLDLNMQLTKLGHGLLSGKYSMPATQKDATTGDPRQEGIPPRMFKNVIAASHAEFSSMRQQDALDFFLHLVGKVERASNTTPDLDPSRSFKFGIEEKILCPSGKVGYNKREDCILSLNIPLHEATNKDELEAFHKQKAGKGLEENDMRSSDEIVRPRVPLEACLANFASSEPIEDYYSSALKGMTTAIKTTGLTSFPDYLVLHMRKFVMEEGWVPKKLDVYIDVPDVIDISHMRSKGLQPGEELLPDGVPEEVMESAQPVANEEIVAQLVSMGFSQLHCQKAAINTSNAGVEEAMNWLLSHMDDPDIDAPISHQTSDIDQSSVDTLLSFGFAEDVARKALKASGGDIEKATDWVFNNPNASVSDMDVSSSNSAQTPAQSGLPDGGGKYKLFGIVSHMGTSVHCGHYVAHILKEGRWVIFNDDKVGISTDPPKDMGYVYFFQRLD
Protein: EG:BACR19J1.3 protein (Q9NF32)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASSGGACSPFAYVAWALFALLLTHGGDNVVDARRNQGNQRKTSSSSSSSNYGHVTQPSYNTNGHAAGNSHADVAKLSYPNYNSQPNRPMAAGSSGSPGSAPQPGWNVPQGPPPAYSASNPAGGARPNMHEPPPAYHAPNYGAAPPNYGAATGSNVHQPQYSGVPAGATYYPAAGPGSGYSPNIPAGATYYPSAGHVPMGGGYHPAAAPPPGATYYQAGSALPPGATYYSAPPQQSSSGLGFGTGLLAGGLGGALLGHALTPSGGSSSSQPVAAAPAAGQDRIIIINNGVPVNASDGTTVINAAGVAAAPGAVPAAPVPSSNTTQDAQQPAVPMAPMPFNPETSNMTAPDPAAPPPPGGIICVPTKVNETDPADSTKMIEVEKIACYPAPPPPAASAGEGPAPLAPMAADQPGSQQVQQVQQAQDVAAPIQASVRSHTGGARALEGLTMRTLLLVLMSGVVAKRLAGF
Protein: Protein max (dMax) (Myc-associated factor X) (P91664)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor.
Subcellular location: Nucleus.
Interaction partners:
- Myc proto-oncogene protein
- Max-binding protein MNT
- Optomotor-blind-related-gene-1, isoform A
- GEO03726p1
- Polycomb protein Sfmbt
- Transcription factor E2f1
- Transcription-associated protein 1
Sequence:
MSMSDDDRDIDIESDEDGDSDTGLGSSRHTNTANFTQAEKRAHHNALERRRRDHIKESFTNLREAVPTLKGEKASRAQILKKTTECIQTMRRKISENQKDIEEIKRQNNIIAKQIQALESSNGDQFSEFLSDEEVGSEEADDEDLDQDFSRRNKKMKTFHA
Protein: LD10379p (Q7YU00)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSSCERIEWVEIIEPRTKEHMYANLTTGECVWDPPEDVPIKRTDSSQWWELFDTNTQRFYYYNAATQKTVWHRPSKCDIIPLAKLQTLKQNTDPSERREQTTPQKQQQQQVQHASQQQQHPSPMSGPNKKGRGQQRISGGNGTVASSEEKLTSSEVISSPRGRQSFRVSTGDSSRSMDMQQQHPQGYASRRSQDSCNQYKESGKSSDSSLSSAHGYRRFNDSGVPVSGHPDNLRLGSLQKQQRGGGKDNGAFEMLQESTSSHNLPHGSTSTSSSYAGGSGYGDKYFDHQLLPNHLQGYSSKSSDIASPTHSIHTPQSQKKKMSPDAAPAAQYNYAQQQHQQRSAQRSGGGAAGTGAPAGKSYGGDREYKVSLARSGSFMSSSINPAAAGHHSKSYRKSSAEAANGGAASDDSMHEKYFKSVENTPLSRRRHTTNATKSGGGASGSNTATSTAGSGSSSHKKHSSDSSPQSPISPQTKSSRQAKTSATSTVPQLQHSPRLQEPSHSLDLLSLERISLGKSGPISPGGGTENLGLLTHSSRGSNDSARQRQKSNNSSANRSQSHHYPGQSSLRHSASSSLDKRGYHVGGGSGDGRGVTGGEKRRSKQHHYQQQADNSDVEYDNGNTSPLYTNWDQEMPHLLPLKHYIIEQAKLSGRYEYRGGDGGDSDSYHSDSQSEHSLSGHEPDNEDSDGGSDTHGGYLEHNYGMIDDYANMGDSVSYYAYMYPPHDPAGREDISENVEAVLEGIGGNATEPSAPTATAPKPKPRYQISYYDTVSHSPSAGSGYHGQQLYSNTPPYSGARSWTSRSTAVTAPPAAVAPGTERH
Protein: Eukaryotic translation initiation factor 4 gamma 1 (D4AD15)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLTLALDTTFPPSPFAISVGPFLVPSSALSNRCWGDPDVAPNEMNKAPQPTGPPPARSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPSSAASRVQSAAPARPGPAPHVYPAGSQVMMIPSQISYSASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQSVQQFPASVAPAPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGSLEPQPNGESPQVAVIIRPDDRSQGAAIGGRPGLPGPEHSPGTESQPSSPSPTPSPPPILEPGSESNLGVLSIPGDTMTTGMIPISVEESTPISCESGEPYCLSPEPTLAEPILEVEVTLSKPIPESEFSSSPLQVSTSLVPHRAETHEPNGVIPSEDLEPEVESSTEPAPPPLSACASESLVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVPSAALASIVSPTPPVAPSDTSAAQEEEIEEDEDEDGEAESEKGGEDLPLDSTPVPAQLSQNLEVAAAPQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEVDPAVPEVENQPPTGSNPSPESEGSAALPQPEEAEETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHITDVVLDKANKTPLRSLDPSRLPGINCGPDFTPSFANLGRPTLSSRGPPRGGPGGELPRGPAGLGPRRSQQGPRKETRKIISSVIMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFAKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRQSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGGDKRRGGPPGPPVNRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDTASEATRPATLNRFSALQQTLPVENTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRGRDPVKREATLPPVSPPKAALAVDEVERKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRLGIESTLERSTIAREHMGRLLHQLLCAGHLSTAQYYQGLYETLELAEDMEIDIPHVWLYLAELITPILQEDGVPMGELFREITKPLRPMGKATSLLLEILGLLCKSMGPKKVGMLWREAGLSWREFLAEGQDVGSFVAEKKVEYTLGEESEAPGQRALAFEELRRQLEKLLKDGGSNQRVFDWIEANLNEQQIASNTLVRALMTTVCYSAIIFETPLRVDVQVLKVRARLLQKYLSDEQKELQALYALQALVVTLEQPANLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFNWLREAEDEESDHN
Protein: 6,7-dimethyl-8-ribityllumazine synthase (DMRL synthase) (LS) (Lumazine synthase) (EC 2.5.1.78) (P50861)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Interaction partners:
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- Riboflavin synthase
- GTP cyclohydrolase-2
- Riboflavin kinase
- 2,5-diamino-6-ribosylamino-4
- Uncharacterized protein YMR085W
- Bifunctional protein RIB2
- Glutamine--fructose-6-phosphate aminotransferase
- Putative glutamine--fructose-6-phosphate aminotransferase
- Phosphomannomutase
Sequence:
MAVKGLGKPDQVYDGSKIRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFVDRQAKLGKPLDVVIPIGVLIKGSTMHFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDEAHSMHNHGEDWGAAAVEMAVKFGKNAF