wanglab/gogpt-training-data huggingface dataset:
Protein: Afadin (ALL1-fused gene from chromosome 6 protein) (Protein AF-6) (Afadin adherens junction formation factor) (P55196)
Organism: Homo sapiens (Human)
Function: Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (By similarity). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:30463011}. Note=Not found at cell-matrix AJs. {ECO:0000250|UniProtKB:O35889}.
Interaction partners:
- Nectin-3
- Tight junction protein 2
- Nectin-2
- Tight junction protein 1
- Nectin-1
- GTPase HRas
- Catenin delta-1
- Nectin-4
- Junctional adhesion molecule A
- Sorbin and SH3 domain-containing protein 1
Sequence:
MSAGGRDEERRKLADIIHHWNANRLDLFEISQPTEDLEFHGVMRFYFQDKAAGNFATKCIRVSSTATTQDVIETLAEKFRPDMRMLSSPKYSLYEVHVSGERRLDIDEKPLVVQLNWNKDDREGRFVLKNENDAIPPKKAQSNGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKDDRPFQGEDVENSRLAAEVYKDMPETSFTRTISNPEVVMKRRRQQKLEKRMQEFRSSDGRPDSGGTLRIYADSLKPNIPYKTILLSTTDPADFAVAEALEKYGLEKENPKDYCIARVMLPPGAQHSDEKGAKEIILDDDECPLQIFREWPSDKGILVFQLKRRPPDHIPKKTKKHLEGKTPKGKERADGSGYGSTLPPEKLPYLVELSPGRRNHFAYYNYHTYEDGSDSRDKPKLYRLQLSVTEVGTEKLDDNSIQLFGPGIQPHHCDLTNMDGVVTVTPRSMDAETYVEGQRISETTMLQSGMKVQFGASHVFKFVDPSQDHALAKRSVDGGLMVKGPRHKPGIVQETTFDLGGDIHSGTALPTSKSTTRLDSDRVSSASSTAERGMVKPMIRVEQQPDYRRQESRTQDASGPELILPASIEFRESSEDSFLSAIINYTNSSTVHFKLSPTYVLYMACRYVLSNQYRPDISPTERTHKVIAVVNKMVSMMEGVIQKQKNIAGALAFWMANASELLNFIKQDRDLSRITLDAQDVLAHLVQMAFKYLVHCLQSELNNYMPAFLDDPEENSLQRPKIDDVLHTLTGAMSLLRRCRVNAALTIQLFSQLFHFINMWLFNRLVTDPDSGLCSHYWGAIIRQQLGHIEAWAEKQGLELAADCHLSRIVQATTLLTMDKYAPDDIPNINSTCFKLNSLQLQALLQNYHCAPDEPFIPTDLIENVVTVAENTADELARSDGREVQLEEDPDLQLPFLLPEDGYSCDVVRNIPNGLQEFLDPLCQRGFCRLIPHTRSPGTWTIYFEGADYESHLLRENTELAQPLRKEPEIITVTLKKQNGMGLSIVAAKGAGQDKLGIYVKSVVKGGAADVDGRLAAGDQLLSVDGRSLVGLSQERAAELMTRTSSVVTLEVAKQGAIYHGLATLLNQPSPMMQRISDRRGSGKPRPKSEGFELYNNSTQNGSPESPQLPWAEYSEPKKLPGDDRLMKNRADHRSSPNVANQPPSPGGKSAYASGTTAKITSVSTGNLCTEEQTPPPRPEAYPIPTQTYTREYFTFPASKSQDRMAPPQNQWPNYEEKPHMHTDSNHSSIAIQRVTRSQEELREDKAYQLERHRIEAAMDRKSDSDMWINQSSSLDSSTSSQEHLNHSSKSVTPASTLTKSGPGRWKTPAAIPATPVAVSQPIRTDLPPPPPPPPVHYAGDFDGMSMDLPLPPPPSANQIGLPSAQVAAAERRKREEHQRWYEKEKARLEEERERKRREQERKLGQMRTQSLNPAPFSPLTAQQMKPEKPSTLQRPQETVIRELQPQQQPRTIERRDLQYITVSKEELSSGDSLSPDPWKRDAKEKLEKQQQMHIVDMLSKEIQELQSKPDRSAEESDRLRKLMLEWQFQKRLQESKQKDEDDEEEEDDDVDTMLIMQRLEAERRARLQDEERRRQQQLEEMRKREAEDRARQEEERRRQEEERTKRDAEEKRRQEEGYYSRLEAERRRQHDEAARRLLEPEAPGLCRPPLPRDYEPPSPSPAPGAPPPPPQRNASYLKTQVLSPDSLFTAKFVAYNEEEEEEDCSLAGPNSYPGSTGAAVGAHDACRDAKEKRSKSQDADSPGSSGAPENLTFKERQRLFSQGQDVSNKVKASRKLTELENELNTK
Protein: Condensin complex subunit 2 (C9J470)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGPPGPETRGHPHSASSPSERVFPMPLPRKAPLNIPGTPVLEDFPQNDDEKERLQRRRSRVFDLQFSTDSPRLLASPSSRSIDISATIPKFTNTQITEHYSTCIKLSTENKITTKNAFGLHLIDFMSEILKQKDTEPTNFKVAAGTLDASTKIYAVRVDAVHADVYRVLGGLGKDAPSLEEVEGHVADGSATEMGTTKKAVKPKKKHLHRTIEQNINNLNVSEADRKCEIDPMFQKTAASFDECSTAGVFLSTLHCQDYRSELLFPSDVQTLSTGEPLELPELGCVEMTDLKAPLQQCAEDRQICPSLAGFQFTQWDSETHNESVSALVDKFKKNDQVFDINAEVDESDCGDFPDGSLGDDFDANDEPDHTAVGDHEEFRSWKEPCQVQSCQEEMISLGDGDIRTMCPLLSMKPGEYSYFSPRTMSMWAGPDHWRFRPRRKQDAPSQSENKKKSTKKDFEIDFEDDIDFDVYFRKTKAATILTKSTLENQNWRATTLPTDFNYNVDTLVQLHLKPGTRLLKMAQGHRVETEHYEEIEDYDYNNPNDTSNFCPGLQAADSDDEDLDDLFVGPVGNSDLSPYPCHPPKTAQQNGDTPEAQGLDITTYGE
Protein: Epsin-1 (EPS-15-interacting protein 1) (Intersectin-EH-binding protein 1) (Ibp1) (Q80VP1)
Organism: Mus musculus (Mouse)
Function: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 (By similarity). {ECO:0000250}.
Interaction partners:
- Epidermal growth factor receptor substrate 15
- Epidermal growth factor receptor substrate 15-like 1
- Intersectin-1
- Clathrin heavy chain 1
- Clathrin coat assembly protein AP180
- Intersectin-2
- Epsin-3
- AP-2 complex subunit beta
- AP-2 complex subunit alpha-2
- AP-2 complex subunit alpha-1
Sequence:
MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL
Protein: Cytosolic Fe-S cluster assembly factor Nubp1 homolog (Q9VJI9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038}.
Interaction partners:
- Cytosolic Fe-S cluster assembly factor Nubp2 homolog
- Probable cytosolic Fe-S cluster assembly factor CG17683
Sequence:
MQAPPPEHCPGVESEEAGKGSACSGCPNQGLCSDPNKKLEDPGKALVVESMKDVKHKLLILSGKGGVGKSTVTSLLTRYLARSNPDSNFGVLDIDICGPSQPRLMGALGESVHQSGYGWSPVGIEDNVCLMSIGFLLGSVDDAIIWRGPKKNGMIRQFLSEVDWGNLDLLLLDTPPGTSDEHLSVVSYLKDDANPESLRAVMVTTPQEVSLLDVRKEINFCKKQNIPIVGVIENMSSFRCGHCGNSSEIFPAKTGGAAAMCAEMGIPLLGSLPLDQQISKACDSGEDLTEFKNVTTEALEGICSKIMASFS
Protein: Agamous-like MADS-box protein (F4IKW3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MCNYCEFSSNRYGCGSSEQDNVLREKVERLRFLIKRMTGKDDDAHFTELQALESRLKDVSRTVLDQKEKMIKLEEDERKKEAQNESDGTRRGVLVPCNSSEQRQRDDGALLLLKKARFERRYSESLQSEFERLWLVNERMNGRELEGMSSRDLLSLDNQILNALLGLLVQMNRPREEQVAARQREKNNKESTSRLAEQERYSSDNDKDDDTSSPFLKRRRRDLTKDARLLCDFCGLSSSRRYDELRPHKQEHEALSMESEVKRLRLLTRMTGKDLDGLSFEELQVLRNRLDDVLPIVEKHMDKMKLEEAAKKNEAGVDNEGTRRRRVLVPCRFSNRGSGEGQQKQEDGAPPVSRRQREFEKRKAEPMHRELERLWLLKERMNGRELTSMSYMELNILWDQIHHGFHGLHEHLNV
Protein: Pickpocket protein 28 (PPK28) (Q86LG1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Osmosensitive ion channel that mediates the cellular and behavioral response to water. Plays an essential role in gustatory water reception. Part of a complex that plays a role in tracheal liquid clearance. Probable role in sodium transport.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20364123}; Multi-pass membrane protein {ECO:0000269|PubMed:20364123}.
Interaction partners:
- Gustatory receptor for bitter taste 66a
- IP13856p
- Gustatory receptor 5a for trehalose
- Gustatory receptor for sugar taste 64f
Sequence:
MRTLTESRRRQSGSSGCKKDSESDDDENTICSRAAIKRSVVYYLKNSTLHGLKYIAEESITIPERIFFGLAFVLVVILSVFFISNVYVKWSASPIIISTSAKQKLTSNMPFPAITICNLNQALLSKVDRIGRTSTNFSLLMGLCDQGGDTTISYIGTWKYFKAILVDVAQPCEKMLLYCSFGSREEDCSWLFTSILTDDGLCCNFNALHPSYLIRNYSDDVRLETAHPNTRYELIDWTPEKGYARNLPEFYFPRTSGGTGIRMGLTVVLNASIAEYYCTKSMSVGFKVLVHNPAELPKVSNYGFVVTAGREARIPIEPVYEDALPTIRSIKKSVRRCLFSDENDLAYYRTYSRKNCELECEAKLLLRECSCVLYYLPRIDPLARVCGPNDNQCTDRVQTEIESSLTNLSCENCWPGCFELTYRATLSTASIVSDPRFQAGENLPEYIFHGPYSNASEISILHFYYMTNIFRSTTKSEMFGFTEFLSNTGGLLGLFMGFSIFSVIEIFFYITVRPYCASRTLRQRHKRRLEQLSWLTPIRMPVRRALRRNRGGLLRNPPPPAYSDLQKFRGKLDKPETCKRKLWRTLQVRPVVDRADEELPTYPYLD
Protein: DnaJ homolog subfamily B member 13 (Testis and spermatogenesis cell-related protein 6) (Testis spermatocyte apoptosis-related gene 6 protein) (Testis spermatogenesis apoptosis-related gene 3 protein) (Testis spermatogenesis apoptosis-related gene 6 protein) (P59910)
Organism: Homo sapiens (Human)
Function: Plays a role in the formation of the central complex of ciliary and flagellar axonemes.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:27486783}. Note=Localizes both to epithelial motile cilium and the sperm flagellum (PubMed:27486783). In spermatids, rapidly enriched in the coupling apparatus with the elongation of the spermatid. Tightly attached to the implantation fossa during the maturation of the spermatid. In mature spermatzoa evenly distributed along the flagellum (By similarity). {ECO:0000250|UniProtKB:Q80Y75, ECO:0000269|PubMed:27486783}.
Interaction partners:
- Heat shock 70 kDa protein 6
- Uncharacterized protein C17orf47
- Heat shock 70 kDa protein 1-like
Sequence:
MGQDYYSVLGITRNSEDAQIKQAYRRLALKHHPLKSNEPSSAEIFRQIAEAYDVLSDPMKRGIYDKFGEEGLKGGIPLEFGSQTPWTTGYVFHGKPEKVFHEFFGGNNPFSEFFDAEGSEVDLNFGGLQGRGVKKQDPQVERDLYLSLEDLFFGCTKKIKISRRVLNEDGYSSTIKDKILTIDVKPGWRQGTRITFEKEGDQGPNIIPADIIFIVKEKLHPRFRRENDNLFFVNPIPLGKALTCCTVEVRTLDDRLLNIPINDIIHPKYFKKVPGEGMPLPEDPTKKGDLFIFFDIQFPTRLTPQKKQMLRQALLT
Protein: Cytochrome P450 2C11 (EC 1.14.14.1) (CYPIIC11) (Cytochrome P-450(M-1)) (Cytochrome P450-UT-2) (Cytochrome P450-UT-A) (Cytochrome P450H) (P08683)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and fatty acids. Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes testosterone to 2alpha- and 16alpha-hydroxytestosterone. Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFAs). Converts arachidonic acid (ARA, C20:4(n-6)) primarily to epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, with both R,S and S,R stereochemistry. Preferentially produces 11R,12S-EET enantiomer. To a lesser extent, catalyzes the hydroxylation of arachidonic acid producing hydroxyeicosatetraenoates (HETEs). Metabolizes eicosapentaenoic acid (EPA, C20:5(n-3)) to epoxyeicosatetraenoic acid (EETeTr) regioisomers, 8,9-, 11,12-, 14,15-, and 17,18-EETeTr, preferentially producing 17R,18S-EETeTr enantiomer. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:2434473}; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:2434473}; Peripheral membrane protein.
Interaction partners:
- Bifunctional epoxide hydrolase 2
- Cytochrome P450 1A2
- Epoxide hydrolase 1
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- Cytochrome P450 1A1
- Cytochrome P450 2U1
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Cytochrome P450 2E1
- Prostaglandin G/H synthase 2
- Cytochrome P450, family 2, subfamily j, polypeptide 4
Sequence:
MDPVLVLVLTLSSLLLLSLWRQSFGRGKLPPGPTPLPIIGNTLQIYMKDIGQSIKKFSKVYGPIFTLYLGMKPFVVLHGYEAVKEALVDLGEEFSGRGSFPVSERVNKGLGVIFSNGMQWKEIRRFSIMTLRTFGMGKRTIEDRIQEEAQCLVEELRKSKGAPFDPTFILGCAPCNVICSIIFQNRFDYKDPTFLNLMHRFNENFRLFSSPWLQVCNTFPAIIDYFPGSHNQVLKNFFYIKNYVLEKVKEHQESLDKDNPRDFIDCFLNKMEQEKHNPQSEFTLESLVATVTDMFGAGTETTSTTLRYGLLLLLKHVDVTAKVQEEIERVIGRNRSPCMKDRSQMPYTDAVVHEIQRYIDLVPTNLPHLVTRDIKFRNYFIPKGTNVIVSLSSILHDDKEFPNPEKFDPGHFLDERGNFKKSDYFMPFSAGKRICAGEALARTELFLFFTTILQNFNLKSLVDVKDIDTTPAISGFGHLPPFYEACFIPVQRADSLSSHL
Protein: Palmitoyltransferase ZDHHC15 (EC 2.3.1.225) (Acyltransferase ZDHHC15) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 15) (DHHC-15) (Q8BGJ0)
Organism: Mus musculus (Mouse)
Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable). Palmitoylates IGF2R and SORT1, promoting their partitioning to an endosomal membrane subdomain where they can interact with the retromer cargo-selective complex (By similarity). Thereby, regulates retrograde transport from endosomes to the Golgi apparatus of these lysosomal sorting receptors and plays a role in trafficking of lysosomal proteins (By similarity). In the nervous system, catalyzes the palmitoylation of DLG4/PSD95 and regulates its synaptic clustering and function in synaptogenesis. Could be involved in the differentiation of dopaminergic neurons and the development of the diencephalon (By similarity). Could also catalyze the palmitoylation of GAP43. Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane. Could also palmitoylate FYN as shown in vitro (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:18596047}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F1QXD3}. Postsynaptic density {ECO:0000250|UniProtKB:Q2TGJ4}.
Interaction partners:
Sequence:
MRRGWKMALSGGLRCCRRVLSWVPVLVIVLVVLWSYYAYVFELCLVTVLSPAEKVIYLILYHAIFVFFAWTYWKSIFTLPQQPNQKFHLSYTDKERYKNEERPEVQKQMLVDMAKKLPVYTRTGSGAVRFCDRCHLIKPDRCHHCSVCAMCVLKMDHHCPWVNNCIGFSNYKFFLQFLAYSVLYCLYIATTVFSYFIKYWRGELPSVRSKFHVLFLLFVACMFFVSLVILFGYHCWLVSRNKTTLEAFCTPVFTSGPEKNGFNLGFIKNIQQVFGDNKKFWLIPIGSSPGDGHSFPMRSMNESQNPLLANEEPWEDNEDDSRDYPEGSSSLAVESET
Protein: Serine/threonine/tyrosine-interacting protein (Inactive tyrosine-protein phosphatase Styx) (Phosphoserine/threonine/tyrosine interaction protein) (Q60969)
Organism: Mus musculus (Mouse)
Function: Catalytically inactive phosphatase. Acts as a nuclear anchor for MAPK1/MAPK3 (ERK1/ERK2) (By similarity). Modulates cell-fate decisions and cell migration by spatiotemporal regulation of MAPK1/MAPK3 (ERK1/ERK2) (By similarity). By binding to the F-box of FBXW7, prevents the assembly of FBXW7 into the SCF E3 ubiquitin-protein ligase complex, and thereby inhibits degradation of its substrates (By similarity). Plays a role in spermatogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8WUJ0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WUJ0}. Note=Predominantly localizes to the nucleus. {ECO:0000250|UniProtKB:Q8WUJ0}.
Interaction partners:
Sequence:
MEDVKLEFPSLPQCKDDAEEWTYPMRREMQEVLPGLFLGPYSSAMKSKLPILQKHGITHIICIRQNIEANFIKPNFQQLFRYLVLDIADNPVENIIRFFPMTKEFIDGSLQNGGKVLVHGNAGISRSAAFVIAYIMETFGMKYRDAFAYVQERRFCINPNAGFVHQLQEYEAIYLAKLTIQMMSPLQIERSLAVHSGTTGSVKRTHEEDDDFGNMQVATAQNG
Protein: Cytochrome c oxidase subunit 3 (Q2F9A2)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGVKGGLHTTGAKWFMIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGATLLSLGLIFLLYTMFVWWRDVLRESTLEGHHTKAVQLGPRYGSILFIVSEVMFLFAFFWASSHSSLAPTVEIGGIWPPKGIGVLDPWEIPLLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVSTGFQGMEYYQAPSTISDSIYGSTFFLATGFHGFHVIIGTLFLIVCGIRQYLGHLTKKHHVGFEAAAWYWHFVDVVRLFPFVSIYWWGGI
Protein: ADP/ATP translocase (ADP,ATP carrier protein) (O45865)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU368008}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU368008}.
Interaction partners:
- Probable voltage-dependent anion-selective channel
- ATP synthase subunit beta, mitochondrial
- Peptidyl-prolyl cis-trans isomerase
- Oligomycin sensitivity conferral protein
- ATP synthase subunit alpha, mitochondrial
- TspO/MBR family protein
- Cytochrome b-c1 complex subunit 1, mitochondrial
- ATP synthase subunit delta, mitochondrial
- Phosphate carrier protein, mitochondrial
- CYclophyliN
Sequence:
MSKEKSFDTKKFLIDLASGGTAAAVSKTAVAPIERVKLLLQVQDASKAIAVDKRYKGIMDVLIRVPKEQGVAALWRGNLANVIRYFPTQAMNFAFKDTYKAIFLEGLDKKKDFWKFFAGNLASGGAAGATSLCFVYPLDFARTRLAADIGKANDREFKGLADCLIKIVKSDGPIGLYRGFFVSVQGIIIYRAAYFGMFDTAKMVFASDGQKLNFFAAWGIAQVVTVGSGILSYPWDTVRRRMMMQSGRKDILYKNTLDCAKKIIQNEGMSAMFKGALSNVFRGTGGALVLAIYDEIQKFL
Protein: Fumarylacetoacetase (FAA) (EC 3.7.1.2) (Beta-diketonase) (Fumarylacetoacetate hydrolase) (Q00770)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Use of phenylalanine and phenylacetate as a carbon source.
Interaction partners:
- Maleylacetoacetate isomerase
- Homogentisate 1,2-dioxygenase
- Fumarylacetoacetase
- 3-hydroxybutyryl-CoA dehydrogenase, putative
- fumarate hydratase
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Uncharacterized protein
- Succinate dehydrogenase cytochrome b small subunit
- homogentisate 1,2-dioxygenase
Sequence:
MASWLQIPKNSPFSLANIPFGIISSSKLSSRVPAIAIGDYALDLSKFASSGGFSQLPVIQPHLNVFNQSTLNAFAALGRPVHRQVREYIQKVFSTETPFPQILRDNAALQKEALLPLSEVTNHLPMQIGDYTDFYAGLNHAYNVGVLFRGPDNALQPNYKHLPVAYHGRASSVVTSGTPLHRPQGQILTNPAANPKLPTFSPCKKLDIELELAFFVSTPNDLGHPVHIDKAEDHIFGVVLMNDWSARDIQAWEYVPLGPFNAKNFGTTITPWVVLIDALEPFRTVGLEPGNRESLLPYLREKRADTAYDIPLEVEVTNAGGEPTVISHSNAKNLLYSFPQMLAHHTITGCNLNTGDLLGSGTISGKENQTEGSFLEQTNGKNPIKLADGSERLFLEDGDTVILRGMAGTEGNYVGFGDCAGTILPPVQLDL
Protein: Pyruvate decarboxylase isozyme 2 (EC 4.1.1.-) (EC 4.1.1.43) (EC 4.1.1.72) (EC 4.1.1.74) (Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase) (2ODC) (P16467)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Second most abundant of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pyruvate decarboxylase isozyme 3
- Pyruvate decarboxylase isozyme 1
- Alcohol dehydrogenase 4
- Pyruvate kinase 1
- Alcohol dehydrogenase 1
- Fructose-bisphosphate aldolase
- Transketolase 1
- Pyruvate kinase 2
- NADP-dependent alcohol dehydrogenase 6
- Pyruvate carboxylase 2
Sequence:
MSEITLGKYLFERLSQVNCNTVFGLPGDFNLSLLDKLYEVKGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIANAPAEIDRCIRTTYTTQRPVYLGLPANLVDLNVPAKLLETPIDLSLKPNDAEAEAEVVRTVVELIKDAKNPVILADACASRHDVKAETKKLMDLTQFPVYVTPMGKGAIDEQHPRYGGVYVGTLSRPEVKKAVESADLILSIGALLSDFNTGSFSYSYKTKNIVEFHSDHIKIRNATFPGVQMKFALQKLLDAIPEVVKDYKPVAVPARVPITKSTPANTPMKQEWMWNHLGNFLREGDIVIAETGTSAFGINQTTFPTDVYAIVQVLWGSIGFTVGALLGATMAAEELDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYIFVLNNNGYTIEKLIHGPHAEYNEIQGWDHLALLPTFGARNYETHRVATTGEWEKLTQDKDFQDNSKIRMIEVMLPVFDAPQNLVKQAQLTAATNAKQ
Protein: Transcription factor E2F3 (E2F-3) (O35261)
Organism: Mus musculus (Mouse)
Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters.
Subcellular location: Nucleus.
Interaction partners:
- Retinoblastoma-associated protein
- Retinoblastoma-like protein 2
- Transcription factor Dp-2
- Transcription factor Dp-1
- Cyclin-A2
- Retinoblastoma-like protein 1
- Cyclin-A1
- Cyclin-dependent kinase 2
- Transcription factor E2F1
- Transcription factor E2F2
Sequence:
MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAPGTYIQILTTNPSTTSCATSLQSGALTAGPLLPSVPGTEPAASSLYTTPQGPSSRVGLLQQPPAPGRGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHRPMKTNNQDHNGNIPKPTSKDLASNNSGHSDCSVSTANLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS
Protein: Furin-like protease 2 (Furin-2) (EC 3.4.21.75) (P30432)
Organism: Drosophila melanogaster (Fruit fly)
Function: Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- ADAM10 endopeptidase
- ADAM10 endopeptidase
- Paramyosin, long form
- Protein serrate
- Nicastrin
- Ankyrin, isoform B
- ADAM metalloprotease
- Membrane-bound transcription factor site-1 protease
- Ankyrin 2, isoform U
Sequence:
MSNTTRSSRVTIGRIGTTPQITDPWSSGLEKQRPSRCGGPKSLAEPTYRKIGRRKMMLHMRVHDPGTTVTQRAKETATAKLNRIYLCTFNRMAQSCIYFVLFLVILSPNTSCALRSSAGETQNYVGILSNDSATTTYDVSSLHSSRRTNPPSSSSSSSSNVDVDYRNDRELHKVDLVGLGGERAGQAETISGGKYDYNYENTHTNASAKDEIVERQSNSLDFDGVDMFGAFSIPEEAIYTNEFAVNIPAGKQMADVIATKHGFINRGQIGSLDNYYLFQHHHVSKRSLRSSRKHQGALKSENEVKWMQQQHEKVRRKRDGPYQDLPTYSPYNLLRQHGGYVVDPNPHLSFSPESISLASHSQRMEYRDVSSHFIFPDPLFKEQWYLNGGAKDGLDMNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGKVNDVVEAQALSLNPSHIDIYSASWGPEDDGSTVDGPGPLARRAFIYGVTSGRQGKGSIFVWASGNGGRYTDSCNCDGYTNSIFTLSISSATQAGFKPWYLEECSSTLATTYSSGTPGHDKSVATVDMDGSLRPDHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPLEKENGWTLNGVKRKYSHKFGYGLMDAGAMVSLAEQWTSVPPQHICKSRENNEDRKIDGAYGSTLSTHMDVNGCAGTINEVRYLEHVQCRITLRFFPRGNLRILLTSPMGTTSTLLFERPRDIVKSNFDDWPFLSVHFWGEKAEGRWTLQVINGGRRRVNQPGILSKWQLIFYGTSTQPMRLKSELLNSSPQLRSPSSSNPFLFPSASNIGQPANEGGNFNTDSFASYLNYQNIFSSAGSDPEPATATLDGQNVTAAIAGGSSAESLGFTASAAQLVAAPETRDGDKKILHSCDAECDSSGCYGRGPTQCVACSHYRLDNTCVSRCPPRSFPNQVGICWPCHDTCETCAGAGPDSCLTCAPAHLHVIDLAVCLQFCPDGYFENSRNRTCVPCEPNCASCQDHPEYCTSCDHHLVMHEHKCYSACPLDTYETEDNKCAFCHSTCATCNGPTDQDCITCRSSRYAWQNKCLISCPDGFYADKKRLECMPCQEGCKTCTSNGVCSECLQNWTLNKRDKCIVSGSEGCSESEFYSQVEGQCRPCHASCGSCNGPADTSCTSCPPNRLLEQSRCVSGCREGFFVEAGSLCSPCLHTCSQCVSRTNCSNCSKGLELQNGECRTTCADGYYSDRGICAKCYLSCHTCSGPRRNQCVQCPAGWQLAAGECHPECPEGFYKSDFGCQKCHHYCKTCNDAGPLACTSCPPHSMLDGGLCMECLSSQYYDTTSATCKTCHDSCRSCFGPGQFSCKGCVPPLHLDQLNSQCVSCCQNQTLAEKTSSAACCNCDGETGECKATSTGGKRRTVVGSGSAYKSSESKHGSFENDGNAREFVLRLDSPLTAITAIAVAICLLIITIFSIIFAVLQRNSNHVSRNSVRYRKIANTSSGRRKNLSAKPTSDARFIFNIGEDDDTDGDNSDDELDGNVGTDINNRIVYDRKGNDHGHEFYIESTNDIDAIEFHCNGAGAQKAETQLQRCNANGDDDDILHYDRHTNAERKNHPSSTTSRTNIRS
Protein: Phospholipase A1, putative (EC 3.1.1.32) (Q4GY96)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Checkpoint protein HUS1
Sequence:
MSEPVDQLLKTYLQSCDYSIDSSSRKKALEMSCLCCHVYGGEGHLPDGWLVCTREVEGLKKRDESCGFRSELYTNGSKYVLAFAGVHDNRSAFESALQLVGKSDAYKLAAANAALVVSAFGLSNVSFTGHSLGGGLATAAAVFTGAPAITFNPAWLSSSTRSELLKFPSVEVINYVIFAEALDVFQRHPQLLNSVPAGAFFAGLLSNSKIQQFGTFKYIYCKVIHDRPHYIDAHLIETIIEELRKENGEKISASDLAASSLHEDVMGGMAQLVQQKMSVIMEVVASVMSKQFSAGGFGSS