wanglab/gogpt-training-data huggingface dataset:
Protein: Papilin (Q9EPX2)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MQLFPLLFSLLLTSTPGSWARNVRRQSDTWGTWGEWSPCSRTCGGGISFRERPCYSQRRDGGTSCVGPARSHRTCHTESCPDGVRDFRAEQCAEFDGTDFQGRRYRWLPYYAAPNKCELNCIPKGQNFYYKHKDAVVDGTPCEPGQRDICVDGVCRVVGCDHKLDSIKQEDKCLQCGGDGSSCYPVTGTFDGNDLSRGYNQIFIIPAGATSIRIEEAAASRNFLAVKSIRGEYYLNGHWTIEAAQALPVASTVLQYERGVEGDLAPERLQARGPTSEPLVIELLSQESNPGVHYEYYLPANDPGRGFSWSHGSWGDCSAECGGGHQSRLVFCTIDNEAYPDHMCQHQPRPTHRRSCNTQPCPKTKRWKVGPWTPCSVSCGGGVQSRSVYCISSDGTGGQEAAEETQCAGLVGKPPTTQACNLQHCAVWSVEPWGECSVTCGTGIRKRSVTCRGDEGSPVHAAACLLKDQPTLTEPCVQEACPVFRGQAWHVGSWSLCSKSCGSGIRRRQVVCTIGPPGRCVDLQSSKPAEMEACNRQPCHLPQEVPSIQDPRTRSSDPRMLSGPRVSPVSDGREQQWAPLERPRAQSNPREGQDPNLSSAGRAPTLQRPPHQPPLRPSSGPRDCRHSPHGCCPDGHTPSLGPQWQGCPLAGASCLQSRYGCCPDGVSAAEGPQQAGCTRSHGSDNTGNRPGSRAVASKNPKIHQPQAHEGEPSECRSSRFGCCYDNVASAAGPLGEGCVGQPSYAYPVRCLLPSAQGSCGDWAARWYFVASVGRCNRFWYGGCHGNANNFASEQECMNTCRGQHGPRRPEAGAAGHRAHVDGGQRGPGGQQEPDWHRAGATIPRLPSPSGSPWRREQEPAPGEPPHIPAYGNRPGGQEIRPRVPGLDREARPAVPPTHSPSYRIRLAGSEPSLVQAAPGQAVQLFCPGNIPSEFQAGWQKEGRPISSNRYQLQADGSLIISRLRPEDAGIYSCGSHRPGHEPQEIQLRVTGGDMAVFPEGQPRHFPEPRNPDLGHGPPHRGTGAEAGGHRVLSPSHPRPATRLRLDRTQPGVVDASPGQRIRLTCRAEGFPVPTIEWQRDGQLVSSPRHQVQPDGSLVISRVDVEDGGYYSCVAFNGQDRDQRWVQLRVLRELTITGLPPAVTVAEGDTARLLCVVAGESVNIRWSRNGLPIQADGHRVHQSPDGTLLIHNLRPRDEGSYTCSAFRGSQAVSRSTEVKVALPAPAAQSRDLGKDCIDQPELANCALILQAQLCGNEYYSSFCCASCSRFQPNAQPVWQQG
Protein: Metal-binding regulatory protein cuf1 (Q09728)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Copper-sensing transcription factor that regulates iron uptake genes. Under copper starvation conditions activates the transcription of the copper transport genes, ctr4, ctr5 and ctr6.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16467469}. Nucleus {ECO:0000269|PubMed:16467469}. Note=Cytoplasmic in presence of excess copper ions. The Cys-His motif (328-342) interacts with the N-terminal nuclear localization signal region leading to sequestration in the cytoplasm. Nuclear under copper starvation conditions.
Interaction partners:
- Copper transport protein ctr4
- Copper transport protein ctr5
- Copper transport protein ctr6
- Copper-transporting ATPase ccc2
- Membrane-anchored protein 1
- Metal homeostasis factor atx1
- Uncharacterized transporter mfc1
- Superoxide dismutase 1 copper chaperone
- Iron-sensing transcriptional repressor
- Probable catechol O-methyltransferase 2
Sequence:
MVVINNVKMACMKCIRGHRSSTCKHNDRELFPIRPKGRPISQCEKCRIARITRHLHVKCTCNSRKKGSKCSTSSTTDLDSSSASNSSCSIPSSISEKLLPRDNVKTHCPKRSASCCGKKPDVMPLKINLESQTDFMGMPLQSQRPHSESYRMLPEPEKFKSEYGYPSQFLPIEKLTSNVAYPPNYNNYLKSPYQQPTNFPPEIQYNYSHSPQHSIQEAEEAAVYGPPVYRSGYQILYNNNTDSIAAAAATHDLYPQPDVPLTFAMLADGNYVPLPSSTNTYGPSNSYGYEININESTNHVDSSYLPHPIQLSNYFTLPSSCAQADAACQCGDNCECLGCLTHPNNATTLAALNHISALEKETISHTDLHHTFKHEVNSSNNYELTNDELAASSPLYTSSSVPPSHITTGST
Protein: Transmembrane protein 151A (Q8N4L1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6GQT5}; Multi-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q6GQT5}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6GQT5}.
Interaction partners:
Sequence:
MPEDGAGDGGEVPALIPDGEPLREEQRPLKQSLGSSLCRESHWKCLLLTLLIHACGAVVAWCRLATVPRLVLGPEAALARGAGGPPPTYPASPCSDGYLYIPLAFVSLLYLLYLAECWHCHVRSCQAPRTDAHTVLALIRRLQQAPPCVWWKATSYHYVRRTRQITRYRNGDAYTTTQVYHERADSRTARGEFDYSAHGVRDVSKELVGLAEHAATRLRFTKCFSFGSAEAEASYLTQRARFFSANEGLDDYLEAREGMHLKDVDFRESLMVFADPRSPPWYARAWVFWLVSAATLSWPLRVVAAYGTAHVHYQVEKLFGASSPPPGAVPSGPPLSRVATVDFTELEWHICSNRQLVPSYSEAVVMGAGSGAYLRGCQRCRRSVSSNSLPPARPSGPRLPFSRSRLSLGAGGRATPGVFRSLSGGPLGRRGEDTEPLESPPCYEDALYFPVLIVHGDSGCQGDGQGAL
Protein: Rab GDP-dissociation inhibitor (Rab GDI) (Secretory pathway GDP dissociation inhibitor) (P39958)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates the GDP/GTP exchange reaction of SEC4 by inhibiting the dissociation of GDP from it, and the subsequent binding of GTP to SEC4. Plays an essential role in the yeast secretory pathway. Extracts GDP-bound YPT7 from vacuolar membranes, antagonizing vacuolar membrane fusion.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- GTP-binding protein YPT1
- GTP-binding protein YPT31/YPT8
- Ras-related protein SEC4
- Ypt/Rab-type GTPase YPT7
- GTP-binding protein YPT6
- GTP-binding protein YPT10
- GTP-binding protein YPT52
- Vacuolar protein sorting-associated protein 21
- Rho GDP-dissociation inhibitor
- GTP-binding protein YPT32/YPT11
Sequence:
MDQETIDTDYDVIVLGTGITECILSGLLSVDGKKVLHIDKQDHYGGEAASVTLSQLYEKFKQNPISKEERESKFGKDRDWNVDLIPKFLMANGELTNILIHTDVTRYVDFKQVSGSYVFKQGKIYKVPANEIEAISSPLMGIFEKRRMKKFLEWISSYKEDDLSTHQGLDLDKNTMDEVYYKFGLGNSTKEFIGHAMALWTNDDYLQQPARPSFERILLYCQSVARYGKSPYLYPMYGLGELPQGFARLSAIYGGTYMLDTPIDEVLYKKDTGKFEGVKTKLGTFKAPLVIADPTYFPEKCKSTGQRVIRAICILNHPVPNTSNADSLQIIIPQSQLGRKSDIYVAIVSDAHNVCSKGHYLAIISTIIETDKPHIELEPAFKLLGPIEEKFMGIAELFEPREDGSKDNIYLSRSYDASSHFESMTDDVKDIYFRVTGHPLVLKQRQEQEKQ
Protein: Non-POU domain-containing octamer-binding protein (C9J4X2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKETRTLAEIAKVELDNMPLRGKQLRV
Protein: ADP-ribosylation factor-like protein 1 (P61211)
Organism: Mus musculus (Mouse)
Function: GTP-binding protein. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P40616}; Lipid-anchor {ECO:0000250|UniProtKB:P40616}.
Interaction partners:
- Golgin subfamily A member 4
- Arfaptin-2
- Ras-related protein Rab-6A
- Golgin subfamily A member 1
- Short coiled-coil protein
- Brefeldin A-inhibited guanine nucleotide-exchange protein 1
- Conserved oligomeric Golgi complex subunit 6
- GRIP and coiled-coil domain-containing protein 2
- Ras-related protein Rab-6B
- Syntaxin-16
Sequence:
MGGFFSSIFSSLFGTREMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVETLKSRQ
Protein: Centrosomal protein 148 kDa (Q54XP9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- ATP synthase subunit a
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase subunit alpha
- ATP synthase F
- ATP synthase F
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase proteolipid subunit
- ATP synthase subunit 9, mitochondrial
- Histone-lysine N-methyltransferase SETD7
Sequence:
MLPNNSPFSPSYISGNNNNNNNNSKNERSPPPPLPPKPQQLHINDLGSTPIKKPINNSSINTPDNKNKNNNNNNNNNEQKQQQQFSYNSTPVSTQKNNTTTTTSTTATPSPSGSKPSLIKPRTPSSIFNNSSINSMNGSKYNNLNFNNNNNNNIPSSAQPSNIGEVILEELVPTNDSDYSNKNNFPSSPLTPANGMRSTSKTPRRWRLVPANCTCLLHENNLNSSANTNANNNNNNSSSNNNNNNNSNNNNNSSSFCPRCSQQINSDDNNNNNSNFGNLDEAFKSNYSVNSRNNSNINNNNNNFNNSGGTGLNGLNNSSSSKNNNNNNNNNNNNNNNNNLNGGFNRSSSTTTTTTANNFSYHTPLKKVTYKVECTGDFERELDLLKNEVSELEDEFGLLKLNSSLNKSHGPITTNSTSILNDYNNLHNHQQQQQQHHHNNQNNHNNNNNNSHSGINTNSTDNSTNIPFNRTSSTSSTSKSPFFSNYTSSYSIPNNKLQQQQQQQKGDNNNNNNNNNNNNNNNNNNNNNNNNNNEDKVQEVEKDDENKIKKFTINKPYQYEFKSNGTSSKNNLLEQISNLIDDLEKEKNESATIKQERNEFERLMKELEKTLALKERDITSIKQLNLQIEQQLIEKEKSTIQLLNQLKQYQNELIEKAVDLETLKELEVEIYSIKNQYNEKINELSEKNQLLHQNEKEIQQLNNNIQRMRLELTNQEKAEQLLLEIGKLKKYITDLEHSSKTLLENEFLKYQSLKQQSDSEKQRSNDTISRLELTVAQREKQIQLLENEKIGKILIDKLEFDQLNQEMTLALQHLSELDIDHNQLKHDYNTSQEQLNQLHLDNQQINQQLLDQKKLINRLKSENDDMKERLSKVHFIVQDSPKKQLSQHQLNQIYQTPYRSLNFSNSPLNNNSNNSNIDNKINQLSSSSSSSSPTNINTNSNSGNSGVSGGINNLDNTNNNTNNNTNNNSIKVLNFKESQSTSESIFNSVLSEHSTISNDDNNNNNSSNNNDSNNSINQSLTPITPMSLPKLNGFLNHNNNNNNNNNNNNNNNNNNNNNNNKNKNNNNSITFNIQNDVNKTQKQNEDSIVKNTEYQIQHDVDQNGIHENDNNHNNHDNDNNDDNDNNDDNDDHFVSEEDYRKYINSDSNQQDEEYEQEYDQQLYQQDYQQEYEQEYDQQQEGEEQEEQEEQEQEEQQEEEQEQEEEQLEYNHNHDGNEEQENYHNNQDDEDDYISEEQDDWNNSLNSKSSSRLNGIRRRDDDDDKDNDKTLDDEYFNDKDFEINVDEEKDEEKDDRGL
Protein: Chorismate pyruvate-lyase (CL) (CPL) (EC 4.1.3.40) (P26602)
Organism: Escherichia coli (strain K12)
Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Subcellular location: Cytoplasm.
Interaction partners:
- 4-hydroxybenzoate octaprenyltransferase
- Isochorismate synthase EntC
- Isochorismate synthase MenF
- Bifunctional chorismate mutase/prephenate dehydratase
- T-protein
- Anthranilate synthase component 1
- Aromatic-amino-acid aminotransferase
- Bifunctional protein TrpGD
- Chorismate synthase
- Aspartate aminotransferase
Sequence:
MSHPALTQLRALRYCKEIPALDPQLLDWLLLEDSMTKRFEQQGKTVSVTMIREGFVEQNEIPEELPLLPKESRYWLREILLCADGEPWLAGRTVVPVSTLSGPELALQKLGKTPLGRYLFTSSTLTRDFIEIGRDAGLWGRRSRLRLSGKPLLLTELFLPASPLY
Protein: Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease alpha) (Matrix processing peptidase) (MPP) (Mitochondrial assembly protein 2) (Mitochondrial import function protein 2) (P11914)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:2007593}.
Interaction partners:
- Mitochondrial-processing peptidase subunit beta
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- RNA polymerase I-specific transcription initiation factor RRN11
- Acyl carrier protein, mitochondrial
Sequence:
MLRNGVQRLYSNIARTDNFKLSSLANGLKVATSNTPGHFSALGLYIDAGSRFEGRNLKGCTHILDRLAFKSTEHVEGRAMAETLELLGGNYQCTSSRENLMYQASVFNQDVGKMLQLMSETVRFPKITEQELQEQKLSAEYEIDEVWMKPELVLPELLHTAAYSGETLGSPLICPRELIPSISKYYLLDYRNKFYTPENTVAAFVGVPHEKALELTEKYLGDWQSTHPPITKKVAQYTGGESCIPPAPVFGNLPELFHIQIGFEGLPIDHPDIYALATLQTLLGGGGSFSAGGPGKGMYSRLYTHVLNQYYFVENCVAFNHSYSDSGIFGISLSCIPQAAPQAVEVIAQQMYNTFANKDLRLTEDEVSRAKNQLKSSLLMNLESKLVELEDMGRQVLMHGRKIPVNEMISKIEDLKPDDISRVAEMIFTGNVNNAGNGKGRATVVMQGDRGSFGDVENVLKAYGLGNSSSSKNDSPKKKGWF
Protein: Mitochondrial Rho GTPase 2 (AtMIRO2) (EC 3.6.5.-) (Calcium-binding GTPase) (AtCBG) (Miro-related GTPase 2) (F4J0W4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-binding mitochondrial GTPase involved in calcium signaling during salt stress response. May play a role in the progression of embryonic cell division, development of haploid male and female gametes, and pollen tube growth.
Subcellular location: Mitochondrion outer membrane {ECO:0000305|PubMed:18344283}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Protein MOR1
- Prohibitin-2, mitochondrial
- Probable transmembrane GTPase FZO-like, chloroplastic
- Kinesin-like protein KIN-14E
- Dynamin-related protein 3A
- Peroxisomal and mitochondrial division factor 1
- Transducin family protein / WD-40 repeat family protein
- Prohibitin-7, mitochondrial
Sequence:
MMLGGKSSAGGRTSLRVAVAGDKGTGKSSLISAVASETFPDNVPRVLPPITLPADAFPDYIPITIVDTPSSIDNRIKLIEEFRKADVVLLTYACDQPSTLDRLSSYWLPELRRLEIKAPVIVVGCKLDLRDERSPARLEDIMSPIMKEYREIETCIECSALTLIQVPDVFYFASKAVLHPTFPLFDQEKQCLKPRLRRAVQRIFNLCDHDLDGALNDAELNDFQVNCFGAPLDPVELMGVKKVVQERQPDGVTDLGLTLPGFLFLFSLFIERGRPETAWAILRKCGYNDSLELHAELLPVPAKQSPDQSIELTNEAMDFLSGIFQLYDLDNDGALQPAELDDLFQTAPDSPWLEDPYKEAAEKTPGGSLTINGFLSEWALMTLLDPRKSLANLTYIGYGHDPASTFSVTRKRSVDRKKQRTERNVFQCFVFGPKKSGKSALLDSFLGRKFSNSYKATMGERYAANVIDQPGGSKKTLILREIPEDRVKKFLTNKESLAACDVAVVVYDSSDVYSWRKAREILMEVARRGEERGYGTPCLLVAAKDDLDPYPMSVQESDRVCMELGIDIPVSLSMKLGEPNSLFSRIVSTAENPHMSIPETESGRRSRNIRQLVNSSLLFVSVGTAVGFAGLAAYRAYSARKNA
Protein: Intraflagellar transport protein 22 (Q381A3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Required for flagellum formation.
Subcellular location: Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:19240117}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:19240117}. Note=ColocaliZes with intraflagellar transport (IFT) proteins at the basal body and in the flagellum matrix.
Interaction partners:
- C2H2-type domain-containing protein
- Intraflagellar transport protein 56 homolog
- Intraflagellar transport protein component, putative
- Intraflagellar transport protein 57/55
- Intraflagellar transport protein IFT88, putative
- Intraflagellar transport protein 80
- Intraflagellar transport protein A1
- IFT80/172/WDR35 TPR domain-containing protein
- Intraflagellar transport protein 27 homolog
- Intraflagellar transport protein-like protein
Sequence:
MSDDLVKILVLGPSKSGKSTVTNFLAGTRDTPTKEYHETNPLRVLEVEIALDDTRRSGRQAAGLKKAVVQLWDVGGSSKHQAGWPAIASNADGIIYVFNPEVKGSEKELLLWYKNFALNQDELDDDNNFKMRVTDGHSLIFSHHSSLPEFAVGDNAIPPMPKQLQGIRALETSLDYQSDNFKEAFDALVEQIIASRLAAEENDLLQKEREAKDYPRLKR
Protein: Major facilitator superfamily (MFS) profile domain-containing protein (G8B6C7)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKVQIFTLHRGNDRQNSHMTSIDDKSAPVKEELESASVDVEPEISEEHKQYLIAKHGTYHLSPLPTMNDNDPLNWSNGMKFLQLGMVAFHGFMTTFLTTGLVPVAGVYAQKFNMPTSRIAYLISVQILVVGVFPIVWVPFMDRYGKRLLLIISTVGSMAFSLGSVFCNTYGSMMAMRIMQSVFISPGIAVGGSIVNETTFSHQRGSRSGIWAISVNLGTMVGAFLMGFVAGHQDAKYIHVVFTCINFGQAVCYVFLGKESSYNYNDLTRNEPNRFKQLRFKTIFPENRITLKRIVYPLKFFGNLKIFIPTFAYSVCFLQANIAMNIEIPEVMVAKFALGPQALGLQFISFIIGTAIGEVGGYMSDRLVAWGQKNGKGPSFRLWLTYPGFIACCVGLIIFGVQIEHAKTWNVTPLVGCAFASFGLQIMTSPIIAFCIDMDHKDASAIVVFITAVRQVLAFIGPFYFPHMYSDLGFAKSYGIMASLIGALSLIPMFILHYLAASKGK
Protein: Lymphotoxin-beta (Tumor necrosis factor C) (Tumor necrosis factor ligand superfamily member 3) (Q6MG45)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Lymphotoxin-alpha
- Lymphotoxin B receptor)
- TNF superfamily member 13b
- CD40 ligand
- Tumor necrosis factor receptor superfamily, member 5, isoform CRA_a.
- TNF superfamily member 14
- C-C motif chemokine receptor 7
- Tumor necrosis factor ligand superfamily member 12
- Transcription factor RelB
Sequence:
MGTRGLQGLGGRPQGRGCLLLAVAGATSLVTLLLAVPITVLAVLALVPQDQGRQVEKIVIGSGAQAQKGLDNKPSCISPSPSSLSETPDPRLHPQRSYSSRNLDPTSQRPVAQPSREASAWVTTLSPAVDSILDPGVQQLPLGEPETDFSPELPAAHLIGAWMSGQGLSWEASQEEAFLRSGAQFSRTHGLALPQDGVYYLYCHVGYRGRTPPAGRSRARLFTLRSALYRAGGAYGRGSPELLLEGAETVTPVVDPIGYGSLWYTSVGFGGLAQLRSGERIYVNISHPDMVDYRRGKTFFGAVMVG
Protein: Aklavinone 12-hydroxylase DnrF (EC 1.14.13.180) (Aklavinone 11-hydroxylase) (P72495)
Organism: Streptomyces peucetius subsp. caesius
Function: Involved in the biosynthesis of the anthracyclines carminomycin, rhodomycin, daunorubicin (daunomycin) and doxorubicin (adriamycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the incorporation of a hydroxyl group at position C-11 of aklavinone, resulting in epsilon-rhodomycinone.
Interaction partners:
Sequence:
MALTKPDVDVLVVGGGLGGLSTALFLARRGARVLLVERHASTSVLPKAAGQNPRTMELFRFGGVADEILATDDIRGAQGDFTIKVVERVGGRVPAQLRESFEELVGATEQCTPMPWALAPQDRVEPVLVAHAAKHGAEIRFATELTSFQAGDDGVTARLRDLGTGAESTVSARYLVAADGPRSAIRESLGITRHGHGTLAHFMGVIFEADLTAVVPPGSTGWYYLQHPDFTGTFGPTDRPNRHTFYVRYDPERGERPEDYTPQRCTELIRLAVDAPGLVPDILDIQAWDMAAYIADRWREGPVLLVGDAAKVTPPTGGMGGNTAIGHGFDVAWKLAAVLRGEAGERLLDSYGADGSLVSRLVVDESLAIYAQRMAPHLLGSVPEERGTAQVVLGFRYRSTAVAAEDDDPEPTEDPRRPSGRPGFRAPHVWIEQDGTRRSTVELFGDCWVLLAAPEGGAWGQAAARAARIWASASTSISSAAMSPPPPAN
Protein: tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ (EC 2.1.1.200) (TrMet(Xm32)) (tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase) (tRNA Cm32/Um32 methyltransferase) (P0AE01)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. Can also methylate adenosine or guanosine, even though these nucleosides are rare or absent at position 32 in the anticodon loop of tRNA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- 23S rRNA
- tRNA1
- tRNA-dihydrouridine
Sequence:
MLQNIRIVLVETSHTGNMGSVARAMKTMGLTNLWLVNPLVKPDSQAIALAAGASDVIGNAHIVDTLDEALAGCSLVVGTSARSRTLPWPMLDPRECGLKSVAEAANTPVALVFGRERVGLTNEELQKCHYHVAIAANPEYSSLNLAMAVQVIAYEVRMAWLATQENGEQVEHEETPYPLVDDLERFYGHLEQTLLATGFIRENHPGQVMNKLRRLFTRARPESQELNILRGILASIEQQNKGNKAE
Protein: MAP kinase-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (MAP kinase signal-integrating kinase 2) (MAPK signal-integrating kinase 2) (Mnk2) (Q8CDB0)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Enhances the formation of EIF4F complex in pachytene spermatocytes, thus promoting mRNA translation during spermatogenesis. Displays a high basal kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Eukaryotic translation initiation factor 4E type 1B
- MAP kinase-interacting serine/threonine-protein kinase 1
- Cyclic AMP-dependent transcription factor ATF-4
- Eukaryotic translation initiation factor 4E type 2
- Neuronal migration protein doublecortin
Sequence:
MVQKRTAELQGFHRSFKGQNPFELAFSLDLAQHRDSDFSPQCEARPDMPSSQPIDIPDAKKRGRKKKRCRATDSFSGRFEDVYQLQEDVLGEGAHARVQTCVNLITNQEYAVKIIEKQLGHIRSRVFREVEMLYQCQGHRNVLELIEFFEEEDRFYLVFEKMRGGSILSHIHRRRHFNELEASVVVQDVASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGSGIKLNGDCSPISTPELLTPCGSAEYMAPEVVEAFSEEASIYDKRCDLWSLGVILYILLSGYPPFVGHCGSDCGWDRGEACPACQNMLFESIQEGKYEFPDKDWSHISFAAKDLISKLLVRDAKQRLSAAQVLQHPWVQGCAPENTLPTPLVLQRNSCAKDLTSFAAEAIAMNRQLAQCEEDAGQDQPVVIRATSRCLQLSPPSQSKLAQRRQRASLSATPVVLVGDRA
Protein: Neuromedin-B [Cleaved into: Neuromedin-B-32; Neuromedin-B] (P08949)
Organism: Homo sapiens (Human)
Function: Stimulates smooth muscle contraction (By similarity). Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). Contributes to the induction of sneezing following exposure to chemical irritants or allergens which causes release of NMB by nasal sensory neurons and activation of NMBR-expressing neurons in the sneeze-evoking region of the brainstem (By similarity). These in turn activate neurons of the caudal ventral respiratory group, giving rise to the sneezing response (By similarity). Contributes to induction of acute itch, possibly through activation of the NMBR receptor on dorsal root ganglion neurons (By similarity). Increases expression of NMBR and steroidogenic mediators STAR, CYP11A1 and HSD3B1 in Leydig cells, induces secretion of testosterone by Leydig cells and also promotes Leydig cell proliferation (By similarity). Plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6. Plays a role in CSF1-induced proliferation of osteoclast precursors by contributing to the positive regulation of the expression of the CSF1 receptor CSF1R (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9CR53}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9CR53}. Note=In neurons of the retrotrapezoid nucleus//parafacial respiratory group, expressed on neuron projections which project into the pre-Botzinger complex. {ECO:0000250|UniProtKB:Q9CR53}.
Interaction partners:
- Neuromedin-B receptor
- Gastrin-releasing peptide
- Bombesin receptor subtype-3
- Gastrin-releasing peptide receptor
- Neuromedin-S
- Toll-like receptor 4
- Kininogen-1
- Neuropeptide S receptor
- Elongator complex protein 3
Sequence:
MARRAGGARMFGSLLLFALLAAGVAPLSWDLPEPRSRASKIRVHSRGNLWATGHFMGKKSLEPSSPSPLGTAPHTSLRDQRLQLSHDLLGILLLKKALGVSLSRPAPQIQYRRLLVQILQK
Protein: YLP motif-containing protein 1 (Nuclear protein ZAP3) (Q9R0I7)
Organism: Mus musculus (Mouse)
Function: Plays a role in the reduction of telomerase activity during differentiation of embryonic stem cells by binding to the core promoter of TERT and controlling its down-regulation.
Subcellular location: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000269|PubMed:10716735}. Note=Migrates to nucleolar caps upon blockage of transcription. {ECO:0000250}.
Interaction partners:
Sequence:
MYPNWGRYGGSSHYPPPPVPPPPPPVALPEASPGPGYSSSTAPAAPSSSGFMSFREQHLAQLQQLQQMHQKQMQCVLQPHHLPPPPLPPPPVMPGGGYGDWQPPPPPMPPPPGPALSYQKQQQYKHQMIHHQRDGPPGLVPMELESPPESPPVPPGSYMPPSQSYMPPPQPPPSYYPPSSAQPYLPPAQPGPSKPQLPPPPSIPSGNKTAIQQEPLESGAKNKTAEQKQAAPEPDPSTMTPQEQQQYWYRQHLLSLQQRTKVHLPGHKKGLVTAKDVPEPIKEEAPGPAASQVAEPLAAEKPPLPPPNEEAPPPLSPEEPQSEDSEDSEDSEEDARFKQLKAIAAHWQAAAAHWQQQQQQRVGFQYQGIMQRHTQLQQILQQYQQVIQHSPHIQTMSLDVQLRHYEMQQQQFQHLFQDWEREFQLWEEQLHSYPHKDQLQEYEKQWKTWQGHMKATQTYLQEKVNSFQTVKSQYLGNMAMPPPFVPYSQMPPPLPTMPPPVLPPSLPPPVMPPALPTSIPPPGMPPPVMPPSLPTSVPPPGMPPSLSSGPPPVLPPPALSSAGSPPVLPPPALPGGPPILPLPPLSSATPPPGIPPPGAPQGMPPQLTAPLPPASGSQNSQIPEKPRQALLPTPVSFGSTPPSPYHPPPQSEQVNSKPLNKVFSSEQGLGESSALSQSIIAAKDTPVKSGGLLADPPKGSFLEGPRGPREQKEQLQKLKDFGSEPQMADHLPPPDSRLQNPSRPGMYPPPGSYRPPPPMGKPPGSIVRPSAPPARSSIPMTRPPVPIPPPPPPPPPPPPPPPVIKSKTSSVKQERWDEDSFFGLWDTNDDQGLNSEFKRDTATIPSAPVLPPPPVHSSIPPPGPMPMGMPPMSKPPPVQHTVDYGHGRDMPTNKVEQIPYGERITLRPDPLPERSTFDADHAGQRDRYDRDRDREPYFDRPSNITDHRDFKRDRETHRDRDRDRVLDYERDRFDRERRPRDDRNQSYRDKKDHSSSRRGGFDRPSYDRKSDRPPYEGPPMFGGERRTYPEERMPLPAPALGHQPPPVPRVEKKPESKNVDDILKPPGRESRPERIVVIMRGLPGSGKTHVAKLIRDKEVEFGGPAPRVLSLDDYFIAEVEKEEKDPDSGKKVKKKVMEYEYEADMEETYRTSMFKTFKKTLDDGFFPFIILDAINDRVRHFDQFWSAAKTKGFEVYLAEMSADNQTCGKRNIHGRKLKEINKMAEHWEVAPRHMMRLDIRSLLQDAAIEEVEMEDFDANIEDQKEEKKDAEEEESELGYIPKSKWEMDTSEAKLDKLDGLRTGTKRKRDWEAIASRMEDYLQLPDDYETRASEPGKKRVRWADLEEKKDADRKRAIGFVVGQTDWEKITDESGHLAERALNRTKYI
Protein: Outer membrane porin PhoE (Outer membrane pore protein E) (P02932)
Organism: Escherichia coli (strain K12)
Function: Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:2464593}; Multi-pass membrane protein.
Interaction partners:
- Protein TonB
- Translation initiation factor IF-2
- Outer membrane porin F
- Maltoporin
- Outer membrane porin C
- Outer membrane protein A
- Malate dehydrogenase
- Glucose-6-phosphate isomerase
- Tol-Pal system protein TolB
- Glyceraldehyde-3-phosphate dehydrogenase A
Sequence:
MKKSTLALVVMGIVASASVQAAEIYNKDGNKLDVYGKVKAMHYMSDNASKDGDQSYIRFGFKGETQINDQLTGYGRWEAEFAGNKAESDTAQQKTRLAFAGLKYKDLGSFDYGRNLGALYDVEAWTDMFPEFGGDSSAQTDNFMTKRASGLATYRNTDFFGVIDGLNLTLQYQGKNENRDVKKQNGDGFGTSLTYDFGGSDFAISGAYTNSDRTNEQNLQSRGTGKRAEAWATGLKYDANNIYLATFYSETRKMTPITGGFANKTQNFEAVAQYQFDFGLRPSLGYVLSKGKDIEGIGDEDLVNYIDVGATYYFNKNMSAFVDYKINQLDSDNKLNINNDDIVAVGMTYQF