wanglab/gogpt-training-data huggingface dataset:
Protein: Transcriptional regulator of RNA polII, SAGA, subunit (O82785)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- SAGA-associated factor 11
- AT4g29790/F27B13_30
- Transcription initiation factor TFIID subunit 6b
- Transcription initiation factor TFIID subunit 9
- Transcription and mRNA export factor ENY2
- Transcription initiation factor TFIID subunit 10
- SAGA-associated factor 29 homolog B
- SAGA-associated factor 29 homolog A
Sequence:
MGSDQCFSRLNSLEIKALIYQKIGHQRADTYFDQLGKFLTSRISKSEFDKLCSKTVGRENISLHNRLVRSILKNASVAKSPPPRYPKKSLYGDPVFPPSPRKCRSRKFRDRPSPLGPLGKPQSLTTTNDESMSKAQRLPMEVVSVEDGEEVEQMTGSPSVQSRSPLTAPLGVSFHLKSKARFSTYNGINRETCQSSGELPDMITLRARLEKKLEMEGIKLSMDSANLLNRGLNAYMRRLIEPCLSLASQQKRAVSNVSMLDFHAAMEVNPRVLGEEWPIQLEKICCRASEE
Protein: hypoxia-inducible factor-proline dioxygenase (EC 1.14.11.29) (F8W1G2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPLGHIMRLDLEKIALEYIVPCLHEAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALTED
Protein: KH domain-containing, RNA-binding, signal transduction-associated protein 3 (Sam68-like mammalian protein 2) (SLM-2) (rSLM-2) (Q9JLP1)
Organism: Rattus norvegicus (Rat)
Function: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro. Binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). RNA-binding abilities are down-regulated by tyrosine kinase PTK6 (By similarity). Involved in splice site selection of vascular endothelial growth factor. In vitro regulates CD44 alternative splicing by direct binding to purine-rich exonic enhancer. Can regulate alternative splicing of neurexins NRXN1-3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners such as neuroligins and LRRTM family members. Targeted, cell-type specific splicing regulation of NRXN1 at AS4 is involved in neuronal glutamatergic synapse function and plasticity. May regulate expression of KHDRBS2/SLIM-1 in defined brain neuron populations by modifying its alternative splicing. Can bind FABP9 mRNA (By similarity). May play a role as a negative regulator of cell growth. Inhibits cell proliferation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10332027}.
Interaction partners:
- Tyrosine-protein kinase
- KH domain-containing, RNA-binding, signal transduction-associated protein 1
Sequence:
MEEKYLPELMAEKDSLDPSFTHALRLVNREIEKFQKGEAKDEEKYIDVVINKNMKLGQKVLIPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSILGKGSMRDKAKEEELRKSGEAKYFHLNDDLHVLIEVFAPPAEAYARMGHALEDIKKFLIPDYNDEIRQAQLQELTYLNGGSENADVPVVRGKSTLRTRGVTTPAITRGRGGVTARPVAVGVPRGTPTPRGVLSTRGPVSRGRGLLTPRARGVPPTGYRPPPPPPTQETYGEYDYDDGYSTAYDDQSYDSYDNSYSTPAQSGADYYDYGHGLGEEAYDSYGQEDWTNSRHKAPSARTAKGVYREQPYGRY
Protein: Sodium- and chloride-dependent betaine transporter (Na(+)/Cl(-) betaine/GABA transporter) (Solute carrier family 6 member 12) (P48056)
Organism: Rattus norvegicus (Rat)
Function: Transports betaine and GABA. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation (By similarity).
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:P31651}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P31651}; Multi-pass membrane protein {ECO:0000255}. Note=In kidney, locates in basolateral membranes of renal medulla. In liver, locates in hepatocytes cell membrane. {ECO:0000250|UniProtKB:P31651}.
Interaction partners:
- Cytosolic arginine sensor for mTORC1 subunit 2
- Glutamate decarboxylase 1
- Parvalbumin alpha
- Glutamate decarboxylase 2
- Vesicular inhibitory amino acid transporter
Sequence:
MDRKVTVHEDGCPVVSWVPEEGEMMDQKDKDQVKDRGQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYFIFFFSCGIPVFFLEVALGQYSSQGSVTAWRKICPLLQGIGMASVVIESYLNIYYIIILAWALFYLFSSFTWELPWTTCTNSWNTEHCVDFLNYSSTRAASYSENFTSPVMEFWERRVLGITSGIHDLGSLRWELALCLLLAWIICYFCIWKGVKSTGKVVYFTATFPYLMLIILLIRGVTLPGAYQGIVFYLKPDLLRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYRDSIALCFLNSATSFVAGFVVFSILGFMAQEQGVPISEVAESGPGLAFIAFPKAVTMMPLSQLWSCLFFLMLLFLGLDSQFVCMECLVTASMDMFPQQLRKRGRRELLILAVAIVCYLMGLLLVTEGGMYIFQLFDYYASSGICLLFLSLFEVICIGWVYGADRFYDNVEDMIGYRPWPLVKISWLFLTPGLCLATFFFSLSKYTPLKYNNVYIYPSWGYSIGWLLAFSSMACVPLFIIITLLKTQGSFKKRLQRLITPDPSLPQPGRRSPQDGSSAQNCSTSPVKQELIAWEKETHL
Protein: Nuclear envelope pore membrane protein POM 121 (Nuclear envelope pore membrane protein POM 121A) (Nucleoporin Nup121) (Pore membrane protein of 121 kDa) (Q96HA1)
Organism: Homo sapiens (Human)
Function: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL).
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17900573}. Nucleus membrane {ECO:0000269|PubMed:17900573}; Single-pass membrane protein {ECO:0000269|PubMed:17900573}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}.
Interaction partners:
- Nuclear pore complex protein Nup93
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup160
- Nuclear envelope pore membrane protein POM 121C
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup85
- POM121-like protein 2
- Protein ELYS
Sequence:
MSPAAAAAGAGERRRPIASVRDGRGRGCGGPARAVLLGLSLVGLLLYLVPAAAALAWLTVGATAAWWGLSREPRGSRPLSSFVRKARHRRPLSSFVRKARHRRTLFASPLAKSTANGNLLEPRTLLEGPDPAELLLMGSYLGKPGPPQPAAAPEGQDLRDRPGRRPPARPAPRSPPPRSPPPRSPPPSPPTHRAHHVYPSLPTPLLRPSRRPSPRDCGTLPNRFVITPRRRYPIHQAQYSCLGVLPTVCWNGYHKKAVLSPRNSRMVCSPVTVRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKEKKRTVEEEDQIFLDGQENKRRRHDSSGSGHSAFEPLVANGVPASFVPKPGSLKRGLNSQSSDDHLNKRSRSSSMSSLTGAYASGIPSSSRNAITSSYSSTRGISQLWKRNGPSSSPFSSPASSRSQTPERPAKKIREEELCHHSSSSTPLAADRESQGEKAADTTPRKKQNSNSQSTPGSSGQRKRKVQLLPSRRGEQLTLPPPPQLGYSITAEDLDLEKKASLQWFNQALEDKSDAASNSVTETPPITQPSFTFTLPAAAPASPPTSLLAPSTNPLLESLKKMQTPPSLPPCPESAGAATTEALSPPKTPSLLPPLGLSQSGPPGLLPSPSFDSKPPTTLLGLIPAPSMVPATDTKAPPTLQAETATKPQATSAPSPAPKQSFLFGTQNTSPSSPAAPAASSAPPMFKPIFTAPPKSEKEGPTPPGPSVTATAPSSSSLPTTTSTTAPTFQPVFSSMGPPASVPLPAPFFKQTTTPATAPTTTAPLFTGLASATSAVAPITSASPSTDSASKPAFGFGINSVSSSSVSTTTSTATAASQPFLFGAPQASAASFTPAMGSIFQFGKPPALPTTTTVTTFSQSLHTAVPTATSSSAADFSGFGSTLATSAPATSSQPTLTFSNTSTPTFNIPFGSSAKSPLPSYPGANPQPAFGAAEGQPPGAAKPALAPSFGSSFTFGNSAAPAAAPTPAPPSMIKVVPAYVPTPIHPIFGGATHSAFGLKATASAFGAPASSQPAFGGSTAVFFGAATSSGFGATTQTASSGSSSSVFGSTTPSPFTFGGSAAPAGSGSFGINVATPGSSTTTGAFSFGAGQSGSTATSTPFAGGLGQNALGTTGQSTPFAFNVSSTTESKPVFGGTATPTFGLNTPAPGVGTSGSSLSFGASSAPAQGFVGVAPFGSAALSFSIGAGSKTPGARQRLQARRQHTRKK
Protein: Cytoskeleton-associated protein CAP5.5, putative (Q57XZ9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proteasome subunit beta
Sequence:
MGCGGSKVKPQPPQAAAPPPPKPPTPPPKSPSVPSEASVVEEVEEVPLTPRAARLQNVIAVKETGFVYNKCTVTGEVTSFFPPKGQCFRIIDEEGRWFFYNDTMNYEMCVQVVIAPESYVEHCEATTVNTKENGETVISAVVYPLETLEFLSGSVVLNTVDVYAHPLSQQYYNHLQIISEEGKKDVEAVMALPWEEVDDEELLKLCSDSLVRYADINFLPSNSMFSRLDGDGRFIQPVEVRRPSEFAQCGEENIDAVRGVVLSSCVEAGTLGDSWFVSALSLLATDEERVKAMFASTTPAEKQMGAYRVLLNKDGWWKNILVDDFLPTVGGVPCYARCIDDSGELWPSLLQKAYAKLYGSYASITGGDTLLALQNFTGAPVYRFDKAWRDAATDEEKKNALIQKITGYVEAHNPVILSVPTGRKAATAVANGLREGYSYALLSVHNFPEENITLLKMFNPWEPAMPWSGQWREGSDKWTEHSEIQSSCEPCFEAHDGIFFIEWSEAVEVFNGCGVLYLDEKPVYDYRVAGEFDNEHPNLVLMIRAKETVEVVLTLSQRDKRGLPLESPDVKLSPVLLCVSRAEGNKQFVYQCSSSDPETPAEGFNFVVGRDVAMKCTFEASETPYFVIPRIHRGGTCEGRRKGFVIGIRSSTPLDEKLDIHFTTLEPTCRVFRNCVTFTSYRVPGAVREWQVKAADAEPTPFWGWGLSPAEVYYENNEEDAEAIREYIVTEAEEPVSLNAETILNDDQPQMDKEVSQAAHEESCELTEELEAEEGPEAEEIATEPAAEEVPVVEETQADEPEPAMDVPQPQAPPSPQNHGNDNSESSEDGLDRFRVAASDAFEIPGDETDSDE
Protein: CAAX prenyl protease 1 homolog (EC 3.4.24.84) (Zinc metalloproteinase Ste24 homolog) (Q3Y6B8)
Organism: Taenia solium (Pork tapeworm)
Function: Zinc-dependent metalloproteinase. Proteolytically removes the C-terminal three residues of farnesylated proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P47154}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDVGGALDLYGCSVNVYNAILIFIWVLFLWETYINLRQLKVAKRVTESPEEIKCLMNDVDFDKSRRYAIDKMNFDIVSGFYNILSLSAVLYFQLIAWAWHKSQEHMLFVCSYAPRSFGTTEGSEILFSLLFTVYVALFQFFESLPWSYYRHFVIEERYGFNKQTIGFFIKDRLKSLAVGLVIGLPIISMLVWIIKAGGHYFYIYAYGFTFVVSFIIMFIYPEFIAPIFDRYEHFPDCELRKKIEELAASIEFPLKKLYVVEGSKRSSHSNAYFYGFGKNKRIVLFDTLIKGFKMPGVEADSSANADESSDETQNRGCGDDEEILATLAHELGHWKLKHMTFNLIIAQINIFFMFFAFGQLINVDQLFVDFGFPPSTAPILIRLIVVFQFIFMPYSSVLEFLMTMLSRKFEFQADAFAVSLKSGEKLKSALLVLTKDNLSFPVYDWLYSMCNHSHPPIIERLAAIDAKMGKEK
Protein: V-type proton ATPase subunit c (V-ATPase subunit c) (Guanine nucleotide exchange factor 2) (V-ATPase 16 kDa proteolipid subunit 1) (Vacuolar proton pump c subunit) (P25515)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:9030535}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase subunit a, Golgi isoform
- V-type proton ATPase subunit F
- V-type proton ATPase subunit C
- V-type proton ATPase subunit E
- V-type proton ATPase subunit D
- V-type proton ATPase subunit G
- V-type proton ATPase subunit H
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit B
Sequence:
MTELCPVYAPFFGAIGCASAIIFTSLGAAYGTAKSGVGICATCVLRPDLLFKNIVPVIMAGIIAIYGLVVSVLVCYSLGQKQALYTGFIQLGAGLSVGLSGLAAGFAIGIVGDAGVRGSSQQPRLFVGMILILIFAEVLGLYGLIVALLLNSRATQDVVC
Protein: 2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) (Citrate synthase) (EC 2.3.3.16) (Q8EJW2)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle II (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Catalyzes the condensation of oxaloacetate with acetyl-CoA (By similarity).
Interaction partners:
- 2-methylisocitrate lyase
- 2-methylcitrate dehydratase
- Propionyl-CoA synthetase PrpE
- Acetyl-coenzyme A synthetase
- Phosphate acetyltransferase
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Fatty acid oxidation complex subunit alpha
- methylmalonate-semialdehyde dehydrogenase
- 2-methyl-aconitate isomerase
- Malate dehydrogenase
Sequence:
MSDAKKLTGAGLRGQSAGETALSTVGVSGSGLTYRGYDVKDLAENATFEEVAYLILYGELPTTAQLAAYKTKLKGMRGLPQALKEVLERIPADAHPMDVMRTGCSMLGNLEAEHSFSEQSQIADRLLAAFPSIICYWYRFSHDGVRIDTETDDDQIGAHFLHLLHGKAPSALHTKVMDVSLILYAEHEFNASTFTARVCASTLSDMHSCVTGAIGSLRGPLHGGANEAAMELIQDMKDEADARDVLMGKLERKEKIMGFGHAIYRDSDPRNAIIKEWSEKLAADYGDDRLYRVSVACEALMWEQKKLFCNADFFHASAYHFMGIPTKLFTPIFVCSRVTGWTAHVMEQRSNNRIIRPSADYVGVSPRKVIPIANR
Protein: Transcription factor TGAL8 (bZIP transcription factor 49) (OsbZIP49) (Q69T21)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional regulator involved in defense response.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- BTB/POZ domain and ankyrin repeat-containing protein NPR1
Sequence:
MAYPSTSGMIQASSSLHGSITRRNPEGYDMPSDLDQALLLYFDGQEQDKPSTQEEPHKPLNFVKETLNIFPSQPMDGEPTPTPKASMSAPPIAGFSRRSPAPAAADGRPLTLGKTSKAAFKKEGGSGSGGAMAASASSELKGPKTPDPKTLRRLAQNREAARKSRLRKKAYIQQLETGRIRLAHLEQEIQFTRAQGAFCGAGILSPDAALFNLEYERWQEAHHQVISRLRAAVEEHRPDGELQPHVDEAMSHYGVLMAHKARLVGADPLHLLSGLWKGAVEQCFLWIGGFRPSELIKVVVRHVEPLTEQQLAAVYSAQQAARQEEDALDGGLQALLRSLSDVVSSSDAPSSSQQTPPVMYHPSAAAAMAAASFMGQYGSYSNLQLAMDKLANLAIFLRQADEERMRTLHALRRMLTVRQAARCFVAVDDYFGRLRALALFWTTTRPHPAAG
Protein: ATP synthase subunit alpha, mitochondrial (P0C521)
Organism: Oryza sativa subsp. indica (Rice)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Subcellular location: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.
Interaction partners:
Sequence:
MEFSPRAAELTTLLESRMTNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGKGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRGTNESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVSKQPQYEPLPIEKQIVVIYAAVNGFCDRMPLDRISQYEKAILSTINPELLKSFNEKGGLTNERKIELDAFLKQTAKEIN
Protein: Clathrin coat assembly protein AP180B (P53309)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in endocytosis and clathrin cage assembly.
Subcellular location: Bud {ECO:0000269|PubMed:14562095}. Bud neck {ECO:0000269|PubMed:14562095}. Cell membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}; Cytoplasmic side {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- EH domain-containing and endocytosis protein 1
- Actin cytoskeleton-regulatory complex protein PAN1
- Epsin-2
- Clathrin heavy chain
- Epsin-1
- Protein SLA2
- Actin cytoskeleton-regulatory complex protein END3
- Clathrin light chain
- Actin cytoskeleton-regulatory complex protein SLA1
- Protein GTS1
Sequence:
MSSLYTKLVKGATKIKMAPPKQKYVDPILSGTSSARGLQEITHALDIRLSDTAWTIVYKALIVLHLMIQQGEKDVTLRHYSHNLDVFQLRKISHTTKWSSNDMRALQRYDEYLKTRCEEYGRLGMDHLRDNYSSLKLGSKNQLSMDEELDHVESLEIQINALIRNKYSVSDLENHLLLYAFQLLVQDLLGLYNALNEGVITLLESFFELSIEHAKRTLDLYKDFVDMTEYVVRYLKIGKAVGLKIPVIKHITTKLINSLEEHLREETKRQRGEPSEPQQDRKPSTAISSTSSHNNNSNDKNKSIAQKKLEQIREQKRLLEQQLQNQQLLISPTVPQDAYNPFGSQQQDLNNDTFSFEPTQPQMTAQVPQPTANPFLIPQQQQQALQLTSASTMPQPSEIQITPNLNNQQTGMYASNLQYTPNFTGSGFGGYTTTENNAIMTGTLDPTKTGSNNPFSLENIAREQQQQNFQNSPNPFTLQQAQTTPILAHSQTGNPFQAQNVVTSPMGTYMTNPVAGQLQYASTGAQQQPQMMQGQQTGYVMVPTAFVPINQQQQQQQHQQENPNLIDI
Protein: Cytochrome f (P0C389)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Photosystem I reaction center subunit II
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
- Cytochrome b6-f complex subunit 4
- Cytochrome b6-f complex subunit 5
- Cytochrome b6
- Cytochrome b
- Cytochrome b
- Photosystem II CP47 reaction center protein
- Os03g0178950 protein
- Os04g0380500 protein
Sequence:
MENRNTFSWVKEQMTRSISVSIMIYVITRTSISNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVLRIPYDMQLKQVLANGKKGGLNVGAVLILPEGFELAPPDRISPELKEKIGNLSFQSYRPNKKNILVIGPVPGKKYSEIVFPILSPDPAMKKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATSTGVVRKILRKEKGGYEISIVDASDGRQVIDLIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFFASVILAQVFLVLKKKQFEKVQLYEMNF
Protein: Translation initiation factor eIF2B subunit beta (eIF2B GDP-GTP exchange factor subunit beta) (Q9BPX4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MPGSAAKGSELSERIESFVETLKRGGGPRSSEEMARETLGLLRQIITDHRWSNAGELMELIRREGRRMTAAQPSETTVGNMVRRVLKIIREEYGRLHGRTDESDQQESLHKLLTSGGLNEDFSFHYAQLQSNIIEAINELLVELEGTMENIAAQALEHIHSNEVIMTIGFSRTVEAFLKEAARKRKFHVIVAECAPFCQGHEMAVNLSKAGIETTVMTDAAIFAVMSRVNKVIIGTKTILANGALRAVTGTHTLALAAKHHSTPLIVCAPMFKLSPQFPNEEDSFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPELITLFISNIGGNAPSYIYRLMSELYHPDDHVL
Protein: Chitin disaccharide deacetylase (EC 3.5.1.105) (Chitin oligosaccharide deacetylase) (Q99PX1)
Organism: Vibrio alginolyticus
Function: Specifically catalyzes the degradation of N,N'-diacetylchitobiose. Key enzyme in the chitin catabolic cascade.
Interaction partners:
- Glycosyl transferase
- Glycosyltransferase
- Chromosome partitioning protein ParB
- RTX toxin
- Hypothetical protein
- Prepilin peptidase
- AraC family transcriptional regulator
- DNA mismatch repair protein MutT
- Histidine phosphotransferase
- AsmA family protein
Sequence:
MKLNKLAIATLVSAALSQYAFAQTDTKGTIYLTFDDGPINASIDVINVLNQEEVKATFYFNAWHLDGIGDENEDRALEALKLALDSGHIVANHSYDHMVHNCVEEFGPNSAAECNATGDHQINSYQDPAYDASMFAENLSVLEKYLPNITSYPNYKANEFARLPYTNGWRVTKDFKADGLCATSDDLKPWEPGYSCDTANPSNSVKAAIAVQNILANNGYQTHGWDVDWAPENWGIAMPANSLTEAEPFLGYVDSALNTCAPTTINPINSKAQEFPCGTPLHADKVIVLTHEFLFEDGKRGMGATQNLPKLAKFIQLAKQAGYVFDTMDNYTPNWQVGNNYSAGDYVLHLGTVYQAVTSHTAQQDWAPSPTSSLWTNADPATNWTQNVSYKQGDVVTYQGLRYLVNVPHVSQADWTPNSQNTLFTAL
Protein: RE74969p (Smooth, isoform H) (Q6NND8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYNGASNGSGASGAGGGGATIVVTEGPQNKKIRTGVQQPGENDVHMHARSTPQQNQQQALMNKSNDDLRRKRPETTRPNHILLFTIINPFYPITVDVLHKICHPHGQVLRIVIFKKNGVQAMVEFDNLDAATRARENLNGADIYAGCCTLKIDYAKPEKLNVYKNEPDTSWDYTLSTGEILPKPPLLGPGAAFPPFGAPEYHTTTPENWKGAAIHPTGLMKEPAGVVPGRNAPVAFTPQGQAQGAVMMVYGLDHDTSNTDKLFNLVCLYGNVARIKFLKTKEGTAMVQMGDAVAVERCVQHLNNIPVGTGGKIQIAFSKQNFLSEVINPFLLPDHSPSFKEYTGSKNNRFLSPAQASKNRIQPPSKILHFFNTPPGLTEDQLIGIFNIKDVPATSVRLFPLKTERSSSGLIEFSNISQAVLAIMKCNHLPIEGKGTKFPFIMKLCFSSSKSMNGAWNNAASEGMIEKENEVDTKVDIYN
Protein: F-box protein pof12 (O60053)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- F-box protein pof13
- F-box protein pof9
- Suppressor of kinetochore protein 1
- F-box protein pof6
- La-related protein 7 homolog
Sequence:
MTTDVKAKNPASIFSHETLLHVLNDLSAHDLAALERVSRSWNSIVRRSSVWHNLYLSEFGTKHLRRHGRIEKKRRNWKGLFRRQSNWKDGRCKKVESMLPQLLNSEKSVGEDRLGLTLTHQNNIYFCNDVQISKWSSVGNSLKCQAISSFRDETVKSGPAVMCLDNASLYIGLKDGNLLHVTVHETGFGNIENLATFSTKFVALSSHKNYICGLTNDNNLYILQHSHQAGTKLKVLGKYHVSSIEKQVAIHFQQSKEGYEVVHVVFNDYVLSGGWTVSLQEFVFNEYCVKSSRLALHDNKDIEYSQQPASAIFMYGSYILTSHPDNSLILQRLYSTNNELRIKFLGRLLGHVCGVQISKLFSCGRIVSVSKNCADICVWDLHDTNYQSIVSPLMLTCTNIHNKPVSDYEKECKVQDIGLYEDTILITLSDGRILKFLFNI
Protein: Zinc-dependent sulfurtransferase SufU (EC 2.-.-.-) (Putative iron-sulfur cluster assembly scaffold protein SufU) (Sulfur acceptor protein SufU) (O32163)
Organism: Bacillus subtilis (strain 168)
Function: Part of the SUF-like system that mediates the biosynthesis of iron-sulfur (Fe-S) clusters. Acts as a sulfurtransferase and thus transfers sulfur from SufS to SufB. Mechanistically, the transfer from SufS to SufU is triggered by zinc-ligand swapping that provides a free thiol from SufU to accept sulfur from SufS.
Interaction partners:
- Vegetative protein 296
- Cysteine desulfurase SufS
- Iron-sulfur cluster assembly protein SufB
- Iron-sulfur cluster assembly protein SufD
- Putative cysteine desulfurase NifS
- Putative cysteine desulfurase IscS 1
- Putative cysteine desulfurase IscS 2
- Uncharacterized aminotransferase YcbU
- Chaperone protein DnaK
- Intracellular iron chaperone frataxin
Sequence:
MSFNANLDTLYRQVIMDHYKNPRNKGVLNDSIVVDMNNPTCGDRIRLTMKLDGDIVEDAKFEGEGCSISMASASMMTQAIKGKDIETALSMSKIFSDMMQGKEYDDSIDLGDIEALQGVSKFPARIKCATLSWKALEKGVAKEEGGN
Protein: Autophagy-related 7, isoform B (A1ZBA9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTEKEIILQFAPWESFVSPTFWHKLAELKLDHDRLSDSKRSITGHYTNRNASGCLLEVDYTAYNSPSFVGKPLKFLGLRHNQQMNIDDSLVWKVIQTEACDLSQSENIKFVGWELNKNGKMGPRMVCMRDSMDPAKLAENSVNLNLKLMKWRLVPDLNLEIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAVAGNRMKATTAAQRLKEINPSAETAGYVLEIPMPGHTIGESLLAQTKEHLKVIEKLVQDHDVIFLLTDSRESRWLPTLLGAAKEKIVINAALGFDSYLVMRHGTTRKEAGDDGQEIEGLKCINGDQLGCYFCNDVTAPGNSLKDRTLDQQCTVTRPGVSNIAASYAVELLVALLQHPRKELAPAYYAQSGRGRSEETEEKVPEGLLGILPHSIRGMLCNYENILPATQKFAQCIACSAAVLNEYKKEGHAFLFKTFETAKFLEDLTGISEFKRLNSEIIDFDDEEFDMSDSDED
Protein: Carboxylesterase SOBER1 (EC 3.1.1.-) (Phospholipase A2 SOBER1) (Protein SUPPRESSOR OF AVRBST-ELICITED RESISTANCE 1) (Q84WK4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses carboxylesterase activity in vitro with a preference for short acyl chain substrates. Functions as a negative regulator of the hypersensitive response (HR) triggered by the bacterial type III effector protein AvrBsT. Possesses phospholipase A2 (PLA2) activity and hydrolyzes phosphatidylcholine (PC), a lipid that is hydrolyzed by phospholipase D (PLD) to produce phosphatidic acid (PA). Required to suppress AvrBsT-dependent HR and PLD-dependent production of PA in response to AvrBsT elicitation.
Interaction partners:
- Photosystem I assembly factor PSA3, chloroplastic
- Ankyrin repeat 30A-like protein
- Cytochrome P450 71B23
- Receptor-like protein 39
- Amino acid transporter AVT3B
- Non-functional pseudokinase ZED1
- RAB6-interacting golgin
- RAB6-interacting golgin
- Transcriptional activator
- Expressed protein)
Sequence:
MARTFILWLHGLGDSGPANEPIQTQFKSSELSNASWLFPSAPFNPVTCNNGAVMRSWFDVPELPFKVGSPIDESSVLEAVKNVHAIIDQEIAEGTNPENVFICGLSQGGALTLASVLLYPKTLGGGAVLSGWVPFTSSIISQFPEEAKKTPILWSHGTDDRMVLFEAGQAALPFLKEAGVTCEFKAYPGLGHSISNKELKYIESWIKRRLKGSSSTCLQLNCLKEMFH
Protein: DNA ligase A (LigA) (EC 6.5.1.2) (Polydeoxyribonucleotide synthase [NAD(+)]) (P9WNV1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Interaction partners:
- DNA ligase B
- DNA ligase C
- Putative methyltransferase Rv1407
- Multifunctional non-homologous end joining DNA repair protein LigD
- Holliday junction branch migration complex subunit RuvB
- DNA polymerase I
- Leucine--tRNA ligase
- RecBCD enzyme subunit RecB
- Cobalamin-independent methionine synthase MetE C-terminal/archaeal domain-containing protein
- ATP-dependent DNA helicase UvrD1
Sequence:
MSSPDADQTAPEVLRQWQALAEEVREHQFRYYVRDAPIISDAEFDELLRRLEALEEQHPELRTPDSPTQLVGGAGFATDFEPVDHLERMLSLDNAFTADELAAWAGRIHAEVGDAAHYLCELKIDGVALSLVYREGRLTRASTRGDGRTGEDVTLNARTIADVPERLTPGDDYPVPEVLEVRGEVFFRLDDFQALNASLVEEGKAPFANPRNSAAGSLRQKDPAVTARRRLRMICHGLGHVEGFRPATLHQAYLALRAWGLPVSEHTTLATDLAGVRERIDYWGEHRHEVDHEIDGVVVKVDEVALQRRLGSTSRAPRWAIAYKYPPEEAQTKLLDIRVNVGRTGRITPFAFMTPVKVAGSTVGQATLHNASEIKRKGVLIGDTVVIRKAGDVIPEVLGPVVELRDGSEREFIMPTTCPECGSPLAPEKEGDADIRCPNARGCPGQLRERVFHVASRNGLDIEVLGYEAGVALLQAKVIADEGELFALTERDLLRTDLFRTKAGELSANGKRLLVNLDKAKAAPLWRVLVALSIRHVGPTAARALATEFGSLDAIAAASTDQLAAVEGVGPTIAAAVTEWFAVDWHREIVDKWRAAGVRMVDERDESVPRTLAGLTIVVTGSLTGFSRDDAKEAIVARGGKAAGSVSKKTNYVVAGDSPGSKYDKAVELGVPILDEDGFRRLLADGPASRT