wanglab/gogpt-training-data huggingface dataset:
Protein: Mitochondrial RNA binding complex 1 subunit (Q4Q6K0)
Organism: Leishmania major
Interaction partners:
Sequence:
MCCAADRVSVARCRLGFVLSFWWRMLHCPPNGATHPSAWRFFACFPLCWLTYSHQICISIAFLAAMRRFSMAPALRAVAPPLPGVFACLSVSCGCASHYQKRWTATQRRVIRPTDESVAELMEDADEEGACISSATASSVAAPAPLSAIAESAALYRKVAAASVDGKTTPAAKRRRRDHAGDGDANTTDDAASATTTHDAVEAEALAGTSAGDGDDAVGEEARGDETYILQQQQYYYELPVQTLTDIATAYLRSTENIVLVSPQEEHVLFPVLMERLQEFHLSQLLDIVDSHWSRSTMLRYGTQYKDMVRDRIAQLATAAATQLEAKRRRQQEQQSSSSAAESTSAAAGALGATRRGEGHSTKTTGAGEECEDDGAVFVAEKQAADAQRSVDAILTHAENEITSATVYRALVVMGISAGHRKRDLAFFQLLGNYLTFFINDYRDPHELVRVLTALARAKIVPSPAFLNMIARRMPVLHKRIPLEPLPAYRALSNFARMGHTSMNTFRFLADCMFAHVEKHISEEKKQLTTMAAASKKPAAATEESDAKIASHAASGSAACMDRAQRCSQEVLEKERLRRMCGLKPSMFTRWLAILARFNAPHQQYLRPLVKPVILPMLPYFPPPSFTRLVSTTRVFKSTDRVLVEALVGRVCDVLAPAGKLTRVDVMELLRLISQDDTPVPTQLDRVLRICKDYLGSSTSTYTAEEVAANSADRSAAPRPRGTVTVVPRPRDMCNVVKLIGSFQKRDEIPLESLTPLLELTEDFAKRLAYLMELCVVSLTQVDAFLELCERHQIPDVSGALEQLMRKRRDVVLHAKRSPEAAAEDRDGRGSATDDEEAEEAYYGQLDIDVRETFNKILLTNDWNTHGRYRPLPGPLQVDFRNELTKVSALELLQAVDLFGKACPGALQDAPRLFLSRSLLEKLGKEGEVVVEEATNSLVIRQPRAELLTREDLQAFTALVERTPLEAVRTSPVVWVFIKEKAERLGLASVEATATARLTELHGMARRAYA
Protein: Cyclosome subunit 1, putative (Q584X1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cell division cycle protein 16, putative
- Cdc23 domain-containing protein
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 11
- Rev7, putative
- Ubiquitin-conjugating enzyme E2, putative
- E2 ubiquitin-conjugating enzyme
- Uncharacterized protein
- Anaphase-promoting complex subunit 10
- Uncharacterized protein
Sequence:
MQSAYTIKVSERQADGVRDVSVFHHGELHFSTSHRNMKWAVLTRFPAPFTQHGGSLHPAAISLPDEKCDVASACRGNEKQRDPVVVGKSDIDSGSKLMYEYLCVFHCDEPRNRLSHYTAHQPWTICSAYSTADPAAVTHFVLNNINPSCVVPGLRGVFVHGTPQSVPTVPSPLIQVGVNTFQPAADLWWMVSQLAINPVYVSVGGGNPATCLPTGDAAANSTRMHIYNCEDNMECVAPKYALVGSTVLAQFQVSEDRMMVVAVGGNDVRLAMTTVSEHVGIMLWVWWPQRLHMPNLRVKGASVSLTVSESCRANVQVLFLFDASRGSLHVLRTPDLLTAKGSLDLLFTISTNCPPVVLPCMCSSMMQPIMVCNRPSVNEVALYYVPELLRTPLSTNYMATMSLSGVLPKNVIVEGVSYHNGSTVVFEAAVAGSDREPSVAASHQQYAFNFPSLLDEQHPLARFILEALEPVFETECVALLQCELLRRSWKSKRKGQVWDFGTGCLELIANIVHNSMSPNSDRRGSPSGGGRYAAAGGSGSGRSVSQMCDAAPSGLELQTSSACTFVDKNFRLCDVVADPILMTADTLQKNAFRFQDRGHHENHGKFSSELDHGNIWTKKQCGLCVFTLHLLYESLKLQERFWILLEPLARLNLRLSEIMQWSQYTRYYSTCLCETETEDFAGHTTTGASRTGTTVSFQRALPENLLIEYFKFHTSSSTAAVMSGAPPLLYTILQRVLKGKARTSGGWPAIRGITSSNPLSLANKLFFMLVDCFDAPQVTARVPTSWWFTLCKGLLEYDIDPKFVSTELCAGVGQPIERALCIAKDHPDDIWNDDFNTIIGRLDRLQHNLTSTRCVNPAGDVVRTAQERAIGREYRATLNDDDGVIMRPDFPKRWGDSRLDIVQSMFNTAAPITLPSQVDGTDAIYGSLRNLSRRATALPVGRGMFTLCTQNFRVRDSVPIPPLNLEGRTSDGITITNNFEEAEPVNIIWPLFHNGCAAGLRFLSLPHFKGHRSAKEEESITRHWVLYQTRNISCPASRSGLLLAAGLLGHLKVLQRTDIYSLLVSPQSQFSGREAVTIAVLLGLSCSLRGTSNPVVFNCVSMHVQSLTPATEDIEVSLDVQTAASVSLGLLYQGTPDAFFVEMLLIQMSRLPSDEHFRDREGYALGAGFGLGLLLLGTGSSHGVPNVENRLLKFMEGARREAAPSACEGLEVFNEVNPDSGHFLTRAQMARNAKESFRNQSTRVYEGDCFNIAVSGPAAVVALGFIYLQTNDALIADKIAPPNRLVGLQGVFPELCLLRTMMSSLIMWSKVEPTQEWIFQNVPSCLLRLVHSPKKSGLAPSQIRYLTMNLGYCIAGAVLAMGMRFAGSMNADAKVTVLAELNGFLRGFIGSTKTGITSIQNSTGAFLPCISACAIALALVTAGTGDVQCLAVMQKLHKRMNVGYGDHLAISMATGLLFLGGGQLTLSNSLSSVAALIMAFYPVWPETASDNRMHLQALRHLYCLAVVPRLIETIDVLTNRPVSVPVRVIVNRGRLFQNEPSSVVKEMWTPVPKGRENQAVRMVTPCLLPELSTVAQIEIRSAQHYNMTICNMDPNVIGDGGIVVRVLEKNVTSTEDGKSGRSLGEELVVSWIQRLFHEQMQLRPGPIEAGVIIDNVNLLFTCQERFLADLSHSEREFSLDFIMNVRRTLNRRYSGLLRHTGRLSTRHPLSQLIKKQKSVYSTASSLVQTLVSDDGHSSDLAPIAEALLMYAEATGMESTGNSEAFHVSFVMQWLSQALHFYGLVGRTKPLSQLLTKYTDVLQRREQRVYALYRMNQTLLLRPEVLEDLVDCCVELAN
Protein: Synaptojanin (EC 3.1.3.36) (Synaptic inositol 1,4,5-trisphosphate 5-phosphatase) (Uncoordinated protein 26) (G5ECL2)
Organism: Caenorhabditis elegans
Function: Probable inositol 5-phosphatase which regulates synaptic vesicle recycling in neurons by regulating clathrin-mediated endocytosis.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}. Synapse {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:18094048, ECO:0000269|PubMed:21029864, ECO:0000269|PubMed:25918845}. Note=Localizes to puncta at neuromuscular junctions in the nerve cord. {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:18094048}.
Interaction partners:
- Endophilin-A homolog
- Amphiphysin
- Dynamin
- Intersectin-1
- Phosphatidylinositol-3-phosphatase SAC1
- PIPK domain-containing protein
- 1-phosphatidylinositol 4-kinase
- 1-phosphatidylinositol-5-phosphate 4-kinase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase daf-18
- Phosphatidylinositol 4-kinase beta
Sequence:
MSVRGIRIWRRNDARFQPSILVEKNGLDGSLLFQGGAIATLDSDSTDVERRSYQKIVDAYGILGVLAITKDEAVLVAVTGVLSVGQLYGADILKITNVEFISLRTFGSVENVDSRIIDLQRLLSSQMFYFSSLQSYDLTRSAQHRDSHDCSDARFFWNRSLHFSFQRYGIDTDNWLLKCMAGSVLVRVVYVGANTGRVALISRLSCERVGTRFNVRGANYLGNVANFVETEQLLLFDEKECSLLQIRGSIPLFWEQPGVNVGSHKVKLRAFETSLPAYHRHLSQLQHRYGEFAIVNLLGRKEGERVLGDAFKTQHKSSHFAPLVDFIDFDYHAQMKISKEAIVQLKKKMSPHMTKHGFFYSMGKEIVKRQTGVIRTNCLDCLDRTNAVQTAIGLQMSHDQVAFLNLNAGKVNVEQRVEEILRDLWQKNGDQCSTIYAGTGALDGKSKLKDASRSLARTIQNNLMDGAKQESFDLFLTGAAYDPRLFDRACNILPPSLIQESYYYHEYADAVSQLVERSPEIAEPQSIKIFVGTWNVNGGKNIHNVAFRNESSLSHWIFANSMTRLVSVEDEQLADIVAIGVEELVDLNASNMVKASTTNQRMWCESIRKTLSEKAPFVLIGSEQLVGVCLFLFARPRVSPYLKDFAVASVKTGMGGATGNKGSVAFRIVVFSTSICFICSHFAAGQNEIRDRNEDFATTLKKIRFPLGREIDSHDVIFWLGDFNYRINLSGDEVKNAVRNGDYAKLVENDQLTQQKALGQTFVGFNEGQLTFAPTYKYDTFSDDYDTSEKCRAPAWTDRILWKDQRKKGKTQLLSYDRSELKTSDHRPVGAVFKVETFKVGGRKCVELIEDVVESMGPPDGTIIVSIAGKPRFPPQMFPPIHEKLKELGAQVQLSKFDDGDLWIVLNSGEMALAALSMDGLKIGGTDQINVKLKSPDWAYALKPHLSDFDLESFEVTAEEEALLGGTDGAVFEFADEDEDAISVSSLTLTGSAPDRPRPPSARSEAISVAKLEWPTEQPNVLSTSMPTRASSASLANSSWYEHVPPLAPPQSNNNKSPPQACLFNPFTQSAPSPAPPPSTIPLPPTRGASVGPGPPAVPVRKAPPPPPRPVIPPRPKNM
Protein: RNA helicase (EC 3.6.4.13) (Q57TW7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- U5 small nuclear ribonucleoprotein component, putative
- PRP8 protein homologue
- PRP1 splicing factor N-terminal domain-containing protein
- Uncharacterized protein
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- Sm protein G
- Pre-mRNA-splicing factor Syf1-like N-terminal HAT-repeats domain-containing protein
- Spliceosomal U5 snRNP-specific protein, putative
- Sm protein F
Sequence:
MNACNNNTGGASPAVRSYDGPTGDVNIAFLHLVEKQLLPVALGCGEGKHSQNSLMPPSVIENSAIYRAVVNYAREEAARKSNDGDGPHPHNIGREGRNNEGKTSAVAGTNATPAVKVSTTLLETAGVPAAAARRGVIPRDPLLLRKLRRQQQSQLQSGTGMSGKTITSSVPTAIHGGYGEERHCSSSSGSNTVSKGSTEENMFRQEVQVGLHWSKRPLKAMTSTGWDVFRQQIGIRIEVVARRRHGSSVTGNINNSGGAGARNSLATAFSGEALQPIRCWEEARLPLALGTVVARRFLLPTPIQSQCVPVALAPSGVDVDASPPLGSGRIDVLAVAETGSGKTAAYLIPLLATIVSPPSRLKGDRSGKTGDDGGNSSAFRKCDEDRFASQGPLALVVVPTRELADQITREAQQLVSGIPDNEMKSLLQHERPVVVPSTEGKRSNDPPYNALDEIRVVKIVGGERADAQYEELLAGAHVVIGTVGQLEALLLQRLLALGSVGIVVMDEADRMLIEQQQQQSLIAVLERCPRPRQTLMFTATLGSVCEGIANKYFSLDGYVVVRVPHSCSTIVQAFEVVPSDPDTSSTVEFHDKEGNKEVKGDDGRKAPATEGKKNGKGGPQVSERRRNPLVHPVKFSRLVNYLVYATPPIVVFANEKRTCDALGNELSAEASRLMNLADTFPLETLVGETPKALQAHKTQRLPRHGQSSSPFDNLRSVAIVHSEQSQVQRQRLVDAFRSGGRRVLITTDLLARGLDVPNVMLVINYDMPSVVQALSSDNASRSDGEEGAVQRYIHRVGRTGRAGASGVAVSLVALPSALVQRAQQHLSRKGDKSGFSIGGDGTNKQRSGGGNDFVLGNASPVTDTWSSEKSRAQKRDRCELTGSRADADTEDLFPELQQDDGEYNDSDEDGNVDGGGDQGRPYGRNGRAKGEESLTRQRTEGKQATNHARSLFQSDEAVLQPLWAFLVSCAEANCTTPAIGSDIIQQQKCRQIQIPSVLAALMQACAQRSPHGTITT
Protein: Calcineurin-interacting protein 2 (Calcineurin binding protein 2) (Q9U2D6)
Organism: Caenorhabditis elegans
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit
Sequence:
MNRGYDSYNRSRSTSSRPLDREPYHAVSELYTKEITHTPIGPASDLPPEILDILKENPRATPQYTPPLIRHRENTWTPENYPIVRVPSAQFTDVMTELYDYHEVEKYTHRSVTPDYEPLRKEPELKEQKLPTYQVIPPTPEKNTPRHQHHSGITLSPSDSSRTLGALPKKPPMYEEYLQMQKKDENRNIPRQVSSADSQRTIRNNNELSHLRHIDSSSSSEASEPAKDLDDRERYVYTHDVYVDSTTGRPFTPGREDVREKKNCDKLKINVYFKPPHPPVEITYKLDEIEIEKNENIVVTKLRPSRSDTILSRSVSTSPSSVTDNIPKTSTSRIPSSENPKTMEHTTTSRRFPTQTSILRKEHEIVQVPLHRSQSLRQSRISEHSKRSLGKTTSTVSTERPIPIHVVEETSSIDMDVVFPKMPHHQTVTNVRVPSSRGSAISRAHSEHRRSIDRSEPRHHHRHHVHSETPELPYTRGISKTPSVREYNVKREGQRSPSRSHRSERSPSEVRIPVTTTHTRPIAKRQSPEELDYGRFADKSQQNRFPGDHQAREEDLPYTRGISKTPSNQDSRSERTPCSDIHIPYNNPEKERAYQQSERSSYRSHKSVTPSEKSLPRNSETPELHYTRGISKTPSDRVEKSRYLSRGVSTPHTPSEVHIPYNNPEKERAYQQSHRPSSPKRRPSGRTNSPNKSSSSSKARPSAAPLEEIVHIKERYERDETIRRFFPTTTAV
Protein: Lipid A biosynthesis myristoyltransferase (EC 2.3.1.243) (Kdo(2)-lauroyl-lipid IV(A) myristoyltransferase) (P24205)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of myristate from myristoyl-[acyl-carrier-protein] (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)-lipid A. Can probably also catalyze the transfer of myristate to Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid A. In vitro, can acylate Kdo(2)-lipid IV(A), but acylation of (KDO)2-(lauroyl)-lipid IV(A) is about 100 times faster. In vitro, can use lauroyl-ACP but displays a slight kinetic preference for myristoyl-ACP.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01944, ECO:0000269|PubMed:9099672}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01944}.
Interaction partners:
- Lipid A palmitoyltransferase PagP
- Phosphoethanolamine transferase EptA
- UDP-2,3-diacylglucosamine hydrolase
- 3-deoxy-D-manno-octulosonic acid transferase
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Lipid A 1-diphosphate synthase
- Lipid-A-disaccharide synthase
- Lipid A biosynthesis palmitoleoyltransferase
- Lipid A biosynthesis lauroyltransferase
- Kdo
Sequence:
METKKNNSEYIPEFDKSFRHPRYWGAWLGVAAMAGIALTPPKFRDPILARLGRFAGRLGKSSRRRALINLSLCFPERSEAEREAIVDEMFATAPQAMAMMAELAIRGPEKIQPRVDWQGLEIIEEMRRNNEKVIFLVPHGWAVDIPAMLMASQGQKMAAMFHNQGNPVFDYVWNTVRRRFGGRLHARNDGIKPFIQSVRQGYWGYYLPDQDHGPEHSEFVDFFATYKATLPAIGRLMKVCRARVVPLFPIYDGKTHRLTIQVRPPMDDLLEADDHTIARRMNEEVEIFVGPRPEQYTWILKLLKTRKPGEIQPYKRKDLYPIK
Protein: Tropomyosin 1 (Alpha) isoform 6 (D9YZV7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDQLYQQLEQNRRLTNELKLALNED
Protein: Serine hydroxymethyltransferase 1, mitochondrial (AtSHMT1) (EC 2.1.2.1) (Glycine hydroxymethyltransferase 1) (Serine Transhydroxymethyltransferase) (STM) (Serine methylase 1) (Q9SZJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions in the photorespiratory pathway in catalyzing the interconversion of serine and glycine. Involved in controlling cell damage caused by abiotic stress, such as high light and salt and the hypersensitive defense response of plants.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:25862457}. Cytoplasm.
Interaction partners:
- Glycine dehydrogenase
- Aminomethyltransferase, mitochondrial
- Glycine dehydrogenase
- Serine--glyoxylate aminotransferase
- Formate--tetrahydrofolate ligase
- Formyltetrahydrofolate deformylase 1, mitochondrial
- Formyltetrahydrofolate deformylase 2, mitochondrial
- Phosphoserine phosphatase, chloroplastic
- Glutamate--glyoxylate aminotransferase 1
- Methylenetetrahydrofolate reductase 1
Sequence:
MAMAMALRRLSSSIDKPIRPLIRSTSCYMSSLPSEAVDEKERSRVTWPKQLNAPLEEVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFRLDPEKWGVNVQPLSGSPANFHVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDESTGYIDYDQMEKSATLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAANVIPSPFDYADVVTTTTHKSLRGPRGAMIFFRKGVKEINKQGKEVLYDFEDKINQAVFPGLQGGPHNHTITGLAVALKQATTSEYKAYQEQVLSNSAKFAQTLMERGYELVSGGTDNHLVLVNLKPKGIDGSRVEKVLEAVHIASNKNTVPGDVSAMVPGGIRMGTPALTSRGFVEEDFAKVAEYFDKAVTIALKVKSEAQGTKLKDFVSAMESSSTIQSEIAKLRHEVEEFAKQFPTIGFEKETMKYKN
Protein: Transthyretin (Prealbumin) (P07309)
Organism: Mus musculus (Mouse)
Function: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
Subcellular location: Secreted.
Interaction partners:
- Retinol-binding protein 4
- Albumin
- Apolipoprotein A-I
- Amyloid-beta precursor protein
- Low-density lipoprotein receptor-related protein 2
- Vitamin D-binding protein
- Thyroxine-binding globulin
- Apolipoprotein E
- Apolipoprotein A-II
- Clusterin
Sequence:
MASLRLFLLCLAGLVFVSEAGPAGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTSEGSWEPFASGKTAESGELHGLTTDEKFVEGVYRVELDTKSYWKTLGISPFHEFADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN
Protein: Lactosylceramide 4-alpha-galactosyltransferase (EC 2.4.1.228) (Alpha-1,4-N-acetylglucosaminyltransferase) (Alpha-1,4-galactosyltransferase) (Alpha4Gal-T1) (Globotriaosylceramide synthase) (Gb3 synthase) (UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase) (Q9JI93)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of galactose from UDP-alpha-D-galactose to lactosylceramide/beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide(d18:1(4E)) to produce globotriaosylceramide/globoside Gb3Cer (d18:1(4E)). Also able to transfer galactose to galactosylceramide/beta-D-Gal-(1<->1')-Cer (By similarity). Globoside Gb3Cer is a glycosphingolipid of the globo serie, one of the major types of neutral root structures of glycosphingolipids, that constitute a significant portion of mammalian cell membranes (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
- Alpha-galactosidase
- Beta-1,4-galactosyltransferase
- Beta-1,4-galactosyltransferase 4
- Beta-1,4-galactosyltransferase 3
- Beta-hexosaminidase subunit alpha
- Beta-1,4-galactosyltransferase
- Syntaxin-1B
- Syntaxin-2
- Beta-galactosidase
Sequence:
MGISRSDLEETMSKPPDCLPRMLRGTPRQRVFTLFIISFKFTFLVSILIYWHTVGAPKDQRRQYSLPVDFPCPQLAFPRVSAPGNIFFLETSDRTNPSFLFMCSVESAARAHPESQVVVLMKGLPRDTTAWPRNLGISLLSCFPNVQIRPLDLQELFEDTPLAAWYLEAQHRWEPYLLPVLSDASRIALLWKFGGIYLDTDFIVLKNLRNLTNMLGIQSRYVLNGAFLAFERKHEFLALCIRDFVAHYNGWIWGHQGPQLLTRVFKKWCSIHSLKESRACRGVTALPPEAFYPIPWQNWKKYFEDVSPEELAQLLNATYAVHVWNKKSQGTHLEATSRALLAQLHARYCPTTHRAMTMYL
Protein: Uncharacterized membrane protein C18A7.02c (Q9Y7Y9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKLLISLLWSIFFSIVYSEKTLLNFKHYELCNGIYSKSESGGSLNPAIYVNWTEPWGQEDEVEVLIFNWKEIRKLGAFRSDDQFTYICDYDAVYTDHLCEADQLGLYLWNSTSAKSIRSYIIPTNADPQNIIYEISQSGYYCIWSHSKKMLPYQALVNWQNAYGGLPASQFPRMPISGGITIAYSVILALWMFFRFQYKHSIVTVQKAIMFLLIFSCAQQAVTSIVLDTENLRNRGNFTWLGETLVSILFACQLVLDLALLLILSWGYTRYSTNMRDRLFTEAKIPLIICFFALFVVRFFAITIQSIHLGLWFCFFFLTACISALYILFGAFVALPSTLRALVEQRYYTLHSIYKIFRIMVLCGVVTIFSFSLVALIFCSNTNNNSTNKLWKIRWYFLDGWIDGVHLTYLITLSSLWRPSQENPDLDPTGLSYPVLDPRLEEELDLLEEDIRADKSK
Protein: PILR alpha-associated neural protein (PILR-associating neural protein) (Paired immunoglobin-like type 2 receptor-associating neural protein) (Q8IYJ0)
Organism: Homo sapiens (Human)
Function: Acts as a ligand for PILRA in neural tissues, where it may be involved in immune regulation.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Paired immunoglobulin-like type 2 receptor alpha
- Neural proliferation differentiation and control protein 1
Sequence:
MESRMWPALLLSHLLPLWPLLLLPLPPPAQGSSSSPRTPPAPARPPCARGGPSAPRHVCVWERAPPPSRSPRVPRSRRQVLPGTAPPATPSGFEEGPPSSQYPWAIVWGPTVSREDGGDPNSANPGFLDYGFAAPHGLATPHPNSDSMRGDGDGLILGEAPATLRPFLFGGRGEGVDPQLYVTITISIIIVLVATGIIFKFCWDRSQKRRRPSGQQGALRQEESQQPLTDLSPAGVTVLGAFGDSPTPTPDHEEPRGGPRPGMPHPKGAPAFQLNRIPLVNL
Protein: Enolase-phosphatase E1 (EC 3.1.3.77) (2,3-diketo-5-methylthio-1-phosphopentane phosphatase) (Q9P6Q2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Acireductone dioxygenase-requiring))
- Methylthioribulose-1-phosphate dehydratase
- Methylthioribose-1-phosphate isomerase
- Spermidine synthase
- Arginyl-tRNA--protein transferase 1
- Methylthioribulose-1-phosphate dehydratase-like protein
Sequence:
MVKNLLLDIEGTVGSISFVKDKLFPYAASRYESYVNENYESDENLRELGKTPEEALINLRKLHAEGSKERSFKMVQGRIWKKGYESNELTSHLFPDVVPAIQRSLQLGMRVYIYSSGSVPAQKLYFEHSDAGNLLKYFSGYYDTTIGLKTECGSYVKIVGNSNPREWLFLSDNINELKAARKVGLHTGLVVRPGNDPVVDTSGFPVYNSFEILFTE
Protein: Protein transport protein bos1 (Q9P7G5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- Protein transport protein bet1
- Protein transport protein sec22
- Integral membrane protein sed5
- Protein transport protein gos1
- Protein sly1
- Synaptobrevin homolog ykt6
- Protein transport protein use1
- Intracellular protein transport protein uso1
- Protein transport protein sec20
- Protein transport protein sft1
Sequence:
MSNTLYNHCTKLFQSIQRSLDELERGVQDESNTISLAGIQGQISASFLSLSRSIDDYDSMVQRELVPAKKKKATIRIQEFRQKHVQLLEKFDELKAHVRDIAQAKNRKELLGRRGYVNSLDSPYGNSTTDAEIVEGPSDLSRQDGLLKEHDFLGRAESQVDEFLERGRMILGDLVEQGSVLKATKTKVLNAANTLGITRHTLSLINRRSKQDKIIFYCGAFLVFVLFYLIYRWLR
Protein: Succinate--CoA ligase [ADP-forming] subunit alpha-2, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha-2) (SCS-alpha-2) (Q6DQL1)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:16270230}.
Interaction partners:
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- succinate dehydrogenase
- Succinate--CoA ligase subunit beta, mitochondrial
- dihydrolipoyllysine-residue succinyltransferase
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- dihydrolipoyllysine-residue succinyltransferase
- ATP citrate synthase
- ATP citrate synthase
Sequence:
MARQATRLISNLSTKLNPSSPTMSASPLWHQYRYFGSPPPPPAVFVDKNTRVICQGITGKNGTFHTEQAIEYGTKMVGGVTPKKGGTEHLGLPVFNTVAEAKVETKANASVVYVPPPFAAAAIMEAMEAELDLVVCITEGIPQHDMVRVKAALKKQLRTRLIGPNCPGIIKPGECKIGIMPGYIHKPGRIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLERFIADPQTEGIVLIGEIGGTAEEDAAALIKESGTQKPVVAFIAGLTAPPGRRMGHAGAIVSGGKGTAQDKIKALKEAGVTVCESPAKIGVTMLDVFKQRGLA
Protein: Infertile crescent, isoform B (EC 1.14.19.17) (M9PC47)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGLHPVAGHFISEHYMFAKGFETYSYYGPLNWITFNVGYHNEHHDFPAVPGSRLPEVKRIAKEFYDTMPQHTSWTRVLYDFIMDPAVGPYARVKRRQRGLAS
Protein: Transcription factor 19 (TCF-19) (Transcription factor SC1) (Q9Y242)
Organism: Homo sapiens (Human)
Function: Potential trans-activating factor that could play an important role in the transcription of genes required for the later stages of cell cycle progression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Coiled-coil alpha-helical rod protein 1
- HLA class I histocompatibility antigen, C alpha chain
- POU domain, class 5, transcription factor 1
- Protein arginine N-methyltransferase 5
Sequence:
MLPCFQLLRIGGGRGGDLYTFHPPAGAGCTYRLGHRADLCDVALRPQQEPGLISGIHAELHAEPRGDDWRVSLEDHSSQGTLVNNVRLPRGHRLELSDGDLLTFGPEGPPGTSPSEFYFMFQQVRVKPQDFAAITIPRSRGEARVGAGFRPMLPSQGAPQRPLSTFSPAPKATLILNSIGSLSKLRPQPLTFSPSWGGPKSLPVPAPPGEMGTTPSAPPQRNRRKSVHRVLAELDDESEPPENPPPVLMEPRKKLRVDKAPLTPTGNRRGRPRKYPVSAPMAPPAVGGGEPCAAPCCCLPQEETVAWVQCDGCDVWFHVACVGCSIQAAREADFRCPGCRAGIQT
Protein: Acetone carboxylase subunit gamma (O25404)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- N-methylhydantoinase
- Hydantoin utilization protein A
Sequence:
MVMSKYTQEQIKNLVEGNLDWNTVLKMLSMPKDHERFQMYLKVLQDKVDFDDKIVLPLGPHLFVVQDAQKKWVIKCSCGHAFCAPEENWKLHANIYVRDTAEKMEEVYPKLLASDTHWQVYREYICPDCGILLDVEAPTPWYPVIHDFEPDIEVFYKDWLGIQPPERR
Protein: tRNA/tmRNA (uracil-C(5))-methyltransferase (EC 2.1.1.-) (EC 2.1.1.35) (tRNA (uracil(54)-C(5))-methyltransferase) (tRNA(m5U54)-methyltransferase) (RUMT) (tmRNA (uracil(341)-C(5))-methyltransferase) (P23003)
Organism: Escherichia coli (strain K12)
Function: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
Interaction partners:
- tRNA pseudouridine synthase B
- tRNA
- tRNA
Sequence:
MTPEHLPTEQYEAQLAEKVVRLQSMMAPFSDLVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMTAMIAGVRNNPVLRHKLFQIDYLTTLSNQAVVSLLYHKKLDDEWRQEAEALRDALRAQNLNVHLIGRATKTKIELDQDYIDERLPVAGKEMIYRQVENSFTQPNAAMNIQMLEWALDVTKGSKGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVREFNRLQGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETLCKNLETLSQTHKVERLALFDQFPYTHHMECGVLLTAK
Protein: Hydroxyproline dehydrogenase (HYPDH) (EC 1.5.5.3) (Kidney and liver proline oxidase 1) (HsPOX1) (Probable proline dehydrogenase 2) (EC 1.5.5.2) (Probable proline oxidase 2) (Q9UF12)
Organism: Homo sapiens (Human)
Function: Dehydrogenase that converts trans-4-L-hydroxyproline to delta-1-pyrroline-3-hydroxy-5-carboxylate (Hyp) using ubiquinone-10 as the terminal electron acceptor. Can also use proline as a substrate but with a very much lower efficiency. Does not react with other diastereomers of Hyp: trans-4-D-hydroxyproline and cis-4-L-hydroxyproline. Ubiquininone analogs such as menadione, duroquinone and ubiquinone-1 react more efficiently than oxygen as the terminal electron acceptor during catalysis.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Pyrroline-5-carboxylate reductase 3
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Pyrroline-5-carboxylate reductase 2
- Prolyl 4-hydroxylase subunit alpha-1
- Prolyl 4-hydroxylase subunit alpha-2
- Ornithine aminotransferase, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 3
Sequence:
MLRTCYVLCSQAGPPSRGWQSLSFDGGAFHLKGTGELTRALLVLRLCAWPPLVTHGLLLQAWSRRLLGSRLSGAFLRASVYGQFVAGETAEEVKGCVQQLRTLSLRPLLAVPTEEEPDSAAKSGEAWYEGNLGAMLRCVDLSRGLLEPPSLAEASLMQLKVTALTSTRLCKELASWVRRPGASLELSPERLAEAMDSGQNLQVSCLNAEQNQHLRASLSRLHRVAQYARAQHVRLLVDAEYTSLNPALSLLVAALAVRWNSPGEGGPWVWNTYQACLKDTFERLGRDAEAAHRAGLAFGVKLVRGAYLDKERAVAQLHGMEDPTQPDYEATSQSYSRCLELMLTHVARHGPMCHLMVASHNEESVRQATKRMWELGIPLDGTVCFGQLLGMCDHVSLALGQAGYVVYKSIPYGSLEEVIPYLIRRAQENRSVLQGARREQELLSQELWRRLLPGCRRIPH