wanglab/gogpt-training-data huggingface dataset:
Protein: PLD phosphodiesterase domain-containing protein (Q9HU94)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Sel1 repeat family protein
- Type VI secretion system spike protein VgrG5
- Tle cognate immunity protein 4 C-terminal domain-containing protein
- Alpha/beta hydrolase
- Sel1 repeat family protein
- Phospholipase D
- Antibacterial effector protein Tle3
- Ion-translocating oxidoreductase complex subunit A
Sequence:
MSDLYKPQTLKLYAQQAGSVRLTLDWFANKAFYPPRAGVHIKPLINGQAAFDAVHAAMEAARHSIDIITWGFDPAMRFKRPDGPRIGELLQTKGREGVQARVLVWSNQLARLKENTIPGAGVGGSGGTWVGSGVASGSAVDNEVLRLEQRRQHNLNLIARQQEALERSERLHREGRLPSFDPRGAAHARTRIAELEAENAEIQRTLDSSGAQGYGGKRGSGGTRQDPWGQIFTRDWFKAVRGGGLQNVEFRTRDFEQTARPVMNGEQVRLVNGRLQSLIHLLRADGIDDLGIGQLLVLTQFASHHQKMVLVDYGSPQAIGFVMGHNMHRNYWDTSAHLFDDRAAGRDPGFGPWQDISMQVQGPVLADLSRNFSEAWDLETPWYKRWFSTPSLTAERDALPLPKIATPASNSVAQICRTQPQDDERSILEHYLKALGNATDYVYMENQYFRYAGFAERLRKTAQVRKARGVPGDLYLFVVTNTPDSSDASKTTYDMMKGLGQEQLMPQVQRDLAHDLREKREQLKQVRENLHPDPYVRRGQENNIERLERKIEALEEKGVTPEVEQRLGDLGAQEIPGLAKNTGEDDKPYQLVEVPGLKVVVATLATSDPAPGSPPPARLSAEAEAALGAPPLKARYKHIYVHSKLLLVDDLYTLLSSANINVRSMHGDSELGVAQPNPDLARAMREELWELHAQKVATTTEKNFKLWNQKMDANWRQQRKDEPLVANLLRFWDVVTPYSPGLTVD
Protein: Protein BREAST CANCER SUSCEPTIBILITY 2 homolog A (AtBRCA2A) (Q7Y1C5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in double-strand break repair and/or homologous recombination by mediating RAD51- and DMC1-facilitated DNA repair. Plays an essential role in both somatic and meiotic homologous recombination. Is crucial for the formation of RAD51 and DMC1 foci during male meiotic homologous recombination in prophase I.
Interaction partners:
- Protein DSS1 HOMOLOG ON CHROMOSOME V
- Protein DELETION OF SUV3 SUPPRESSOR 1
- Meiotic recombination protein DMC1 homolog
- DNA repair protein RAD51 homolog 1
- DNA repair protein RAD51 homolog 3
- BRCA1-associated RING domain protein 1
- DNA repair protein XRCC3 homolog
- Protein BREAST CANCER SUSCEPTIBILITY 1 homolog
- DNA repair protein RAD51 homolog 4
- Fanconi anemia group D2 protein
Sequence:
MSTWQLFPDSSGDGFRWEVAGRILQSVSDSTPTKALESTAPLPSMADLLLQGCSKLIAREEAMPGEIPMFRTGLGKSVVLKESSIAKAKSILAEKVTYSDLRNTNCSIPQMRQVDTAETLPMFRTASGKSVPLKESSIAKAMSILGSDKIIDSDNVLPRESGFGVSNSLFQTASNKKVNVSSAGLARAKALLGLEEDDLNGFNHVNQSSSSSQQHGWSGLKTHEEFDATVVKHHSGTPGQYEDYVSGKRSEVLNPSLKVPPTKFQTAGGKSLSVSAEALKRARNLLGDPELGSFFDDVAGGDQFFTPEKDERLSDIAINNGSANRGYIAHEEKTSNKHTPNSFVSPLWSSSKQFSSVNLENLASGGNLIKKFDAAVDETDCALNATHGLSNNRSLASDMAVNNSKVNGFIPRGRQPGRPADQPLVDITNRRDTAYAYNKQDSTQKKRLGKTVSVSPFKRPRISSFKTPSKKHALQASSGLSVVSCDTLTSKKVLSTRYPEKSPRVYIKDFFGMHPTATTRMDYVPDHVRRIKSSNADKYVFCDESSSNKVGAETFLQMLAESGASLQHASRKWVTNHYRWIVWKLACYDIYYPAKCRGNFLTITNVLEELKYRYEREVNHGHCSAIKRILSGDAPASSMMVLCISAINPKTDNDSQEAHCSDSCSNVKVELTDGWYSMNAALDVVLTKQLNAGKLFVGQKLRILGAGLSGWATPTSPLEAVISSTICLLLNINGTYRAHWADRLGFCKEIGVPLALNCIKCNGGPVPKTLAGIKRIYPILYKERLGEKKSIVRSERIESRIIQLHNQRRSALVEGIMCEYQRGINGVHSQNDTDSEEGAKIFKLLETAAEPEFLMAEMSPEQLRSFTTYKAKFEAAQQMRKEKSVAETLEDAGLGERNVTPFMRIRLVGLTSLSYEGEHNPKEGIVTIWDPTERQRTELTEGKIYMMKGLVPINSDSEILYLHARGSSSRWQPLSPKDSENFQPFFNPRKPISLSNLGEIPLSSEFDIAAYVVYVGNAYTDVLQKKQWVFVTDGSAQHSGEISNSLLAISFSTSFMDDSSVSHISHNLVGSVVGFCNLIKRAKDVTNEIWVAEAAENSVYFINAEAAYSSHLKTSSAHIQTWAKLSSSKSVIHELRQRVLSIIGACKSPSC
Protein: Radixin (E9PT65)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
- Ezrin
- Moesin
- Na
- CD44 antigen
- Intercellular adhesion molecule 2
- Sodium/hydrogen exchanger 1
- Leukosialin
- Na
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
Sequence:
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLRQIEEQTMKAQKELEEQTRKALELEQERQRAKEEAERLDRERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMCAPPPPPPPAVVPPTENEHDEQDEHSAEASAELSSEGVTNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAMWGPKLYALFQMRSCQSSIKQM
Protein: Elongator complex protein 4 (A0A1W2PRF5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAVATCGSVAASTGSAVATASKSNVTSFQRRGPRASVTNDSGPRLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQELPAPLLDDKCKKEFDEDVYNHKTPESNIKMKIAWRYQLLPKMEIGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPEKISSTLKVEPCSLTPGYTKLLQFIQNIIYEEGFDGSNPQKKQRNILRIGIQNLGSPLWGDDICCAENGGNSHSLTKFLYVLRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESFIGSERETNPLYKDYHGLIHIRQIPRLNNLICDESDVKDLAFKLKRKLFTIEWVQDNYLRQERNIYPPGFSYLLKQKDSAWGEGSLQHSTFLMSFLAKATAFASRLVRHSEPLKQNGSGRIRQAAGPRLWHDGRRQEAPGLLGIPP
Protein: U1 small nuclear ribonucleoprotein component PRP42 (U1 snRNP protein PRP42) (65 kDa snRNP protein) (Pre-mRNA-processing factor 42) (Q03776)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway. U1 snRNP is cotranscriptionally recruited to intron-containing genes. Required for U1 snRNP biogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein LUC7
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing factor 39
- U1 small nuclear ribonucleoprotein 70 kDa homolog
- U1 small nuclear ribonucleoprotein A
- Nuclear cap-binding protein subunit 2
- Pre-mRNA-processing protein PRP40
- Protein NAM8
- 56 kDa U1 small nuclear ribonucleoprotein component
- U1 small nuclear ribonucleoprotein C
Sequence:
MDKYTALIHDENFSTLTLNVSRYPKSLAYWEKLLNYIVKASAPICKSTEPQLLKLIRCTYSSMLNEFPYLENYYIDFALLEYKLGNVSMSHKIFQRGLQAFNQRSLLLWTSYLKFCNNVISHQKQLFKKYETAEEYVGLHFFSGEFWDLYLEQISSRCTSSKKYWNVLRKILEIPLHSFSKFYALWLQRIDDIMDLKQLSQLTSKDELLKKLKIDINYSGRKGPYLQDAKKKLKKITKEMYMVVQYQVLEIYSIFESKIYINYYTSPETLVSSDEIETWIKYLDYTITLQTDSLTHLNFQRALLPLAHYDLVWIKYSKWLINSKNDLLGAKNVLLMGLKFSLKKTEIIKLLYSVICKLNEYVLLRNLLEKIESSYSDNVENVDDFEIFWDYLQFKTFCQNSLYSSRYSDSQSNGLLNKELFDKVWKRLSCKEKKSGQEILLNNLVQFYSKDTVEFVEKNIFQKIIEFGWEYYLQNGMFWNCYCRLIYFDTSRSYLDKRQYIVRKIWPQIDKKFAQSVLPSLTEFCESYFPEEMDTLEEMFTEEP
Protein: Farnesyl pyrophosphate synthase 2 (FPP synthase 2) (FPS 2) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase 2) (Dimethylallyltranstransferase 2) (EC 2.5.1.1) (Farnesyl diphosphate synthase 2) (Geranyltranstransferase 2) (Q43315)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Subcellular location: Cytoplasm.
Interaction partners:
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Phytoene synthase 1, chloroplastic
- Solanesyl diphosphate synthase 3, chloroplastic/mitochondrial)
- Hydroxymethylglutaryl-CoA synthase
- Squalene synthase 1
- Dehydrodolichyl diphosphate synthase 1
- Isopentenyl-diphosphate Delta-isomerase II, chloroplastic
- Inactive squalene synthase 2
Sequence:
MADLKSTFLDVYSVLKSDLLQDPSFEFTHESRQWLERMLDYNVRGGKLNRGLSVVDSYKLLKQGQDLTEKETFLSCALGWCIEWLQAYFLVLDDIMDNSVTRRGQPCWFRKPKVGMIAINDGILLRNHIHRILKKHFREMPYYVDLVDLFNEVEFQTACGQMIDLITTFDGEKDLSKYSLQIHRRIVEYKTAYYSFYLPVACALLMAGENLENHTDVKTVLVDMGIYFQVQDDYLDCFADPETLGKIGTDIEDFKCSWLVVKALERCSEEQTKILYENYGKAEPSNVAKVKALYKELDLEGAFMEYEKESYEKLTKLIEAHQSKAIQAVLKSFLAKIYKRQK
Protein: RAB33B, member RAS oncogene family (F1LW77)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037868}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037868}.
Interaction partners:
- Autophagy-related protein 16-1
- Protein Atg16l2
- TBC1 domain family member 25
- Guanine nucleotide exchange factor subunit RIC1
- Homeobox protein aristaless-like 4
- RAB33A, member RAS oncogene family
- Autophagy protein 5
- Ubiquitin-like protein ATG12
Sequence:
MASEMESSLEVSFSSSCAVSGASGCLPPARSRIFKIIVIGDSNVGKTCLTYRFCAGRFPDRTEATIGVDFRERAVDIDGERIKIQLWDTAGQERFRKSMVQHYYRNVHAVVFVYDMTNMASFHSLPSWIEECKQHLLANDIPRILVGNKCDLRSAIQVPTDLAQKFADTHSMPLFETSAKNPNDNDHVEAIFMTLAHKLKSHKPLMLSQLPDNRISLKPETKPAVTCWC
Protein: Probable transmembrane GTPase FZO-like, chloroplastic (EC 3.6.5.-) (Q1KPV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable membrane-remodeling GTPase that plays a unique role in the in the determination of thylakoid and chloroplast morphology and regulates organization of the thylakoid network. Not involved in the determination of mitochondrial morphology or ultrastructure.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:16617119}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:16617119}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in a punctate pattern in chloroplasts. {ECO:0000269|PubMed:16617119}.
Interaction partners:
- Autophagy protein 5
- Dynamin-like protein ARC5
- Protein NBR1 homolog
- Dynamin-related protein 3B
- Dynamin
- Dynamin-related protein 3A
- Phragmoplastin DRP1A
- E3 ubiquitin-protein ligase PRT1
- Mitochondrial Rho GTPase 3
- Dynamin-related protein 5A
Sequence:
MRTLISHRQCVTSPFLISAASPPFPGRCFKLSSFTPPRHRRFSSLSIRNISHESADQTSSSRPRTLYPGGYKRPELAVPGLLLRLDADEVMSGNREETLDLVDRALAKSVQIVVIDGGATAGKLYEAACLLKSLVKGRAYLLIAERVDIASAVGASGVALSDEGLPAIVARNTLMGSNPDSVLLPLVARIVKDVDSALIASSSEGADFLILGSGEEDTQVADSLLKSVKIPIYVTCRGNEEAKEELQLLKSGVSGFVISLKDLRSSRDVALRQSLDGAYVVNNHETQNMNELPEKKNSAGFIKLEDKQKLIVEMEKSVLRETIEIIHKAAPLMEEVSLLIDAVSRIDEPFLMVIVGEFNSGKSTVINALLGKRYLKEGVVPTTNEITFLCYSDLESEEQQRCQTHPDGQYVCYLPAPILKDINIVDTPGTNVILQRQQRLTEEFVPRADLLVFVLSADRPLTESEVAFLRYTQQWKKKFVFILNKSDIYRDARELEEAISFVKENTRKLLNTENVILYPVSARSALEAKLSTASLVGRDDLEIADPGSNWRVQSFNELEKFLYSFLDSSTATGMERIRLKLETPMAIAERLLSSVEALVRQDCLAAREDLASADKIISRTKEYALKMEYESISWRRQALSLIDNARLQVVDLIGTTLRLSSLDLAISYVFKGEKSASVAATSKVQGEILAPALTNAKELLGKYAEWLQSNTAREGSLSLKSFENKWPTYVNSKTQLGIDTYDLLQKTDKVSLKTIQNLSAGTTSKRLEQDIREVFFVTVGGLGAAGLSASLLTSVLPTTLEDLLALGLCSAGGYVAIANFPYRRQAIIGKVNKVADALAQQLEDAMQKDLSDATSNLVNFVNIVAKPYREEAQLRLDRLLGIQKELSDIRSKLQLLQVDIDNLHVSRDEMRL
Protein: Transcriptional activator of proteases prtT (Zn(2)-C6 zinc finger-containing protein prtT) (A2QJF9)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Transcription factor required for protein utilization and degradation. Regulates transcription of major secreted proteases.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
Interaction partners:
Sequence:
MTRTVDEIKYETPSSWEHKSLDVAEDGRRLAPHSDTARPKGRIRRSMTACHTCRKLKTRCDLDPRGHACRRCLSLRIDCKLPETTDRFQDSAAMWPDATSAIPSIEERLTSLERCMREMTGMMRQMLDHSPGFANASVPHLTKSIITDENASMEGSPSSPFLPKPVRLIQDLQSDFFGEAETSPVDSPLSSDGNAKGAIDSKLSLKLLQTFVDHFGACVSIYNLSDIHNDMKAPDSLLYNTACLLASRYVPGIPTSTVHAIYLQVRHAVVNILWEKPPLKYETLQALALLCLWPATAQKEPPMDSWLLSGISINHAIIALDFLNYAPSEVMVDNETAAQLRLWNTYCLTQLHFAVGNARPFHIQQRYLDHCPRILEHPAATLEDARVVAEIQLYLMTLRLQSNSSRMRLADLDYEEIERWKREWAHLFSGESSTLELSLWFCQTLLHRTAMRLQPRSDRLASEVLQTSRLIISRFLQIRYSTALSLVDQVYFIVGYAALNLCDFNLMDPLIEQVQMFLLHLSPNEDHIAYRFSCMVAEFKRRCGSAECNDPSSTVKGSPLSSYGDSRKMSMGQAPFMPPLMDGMIEGYGFEQLMPEVMPSSFPDGILNGMPVTGLAAYRSATL
Protein: Uroplakin-3b (UP3b) (Uroplakin IIIb) (UPIIIb) (p35) (Q9BT76)
Organism: Homo sapiens (Human)
Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1B is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000269|PubMed:12446744}.
Interaction partners:
Sequence:
MGLPWGQPHLGLQMLLLALNCLRPSLSLGEWGSWMDASSQTQGAGGPAGVIGPWAPAPLRLGEAAPGTPTPVSVAHLLSPVATELVPYTPQITAWDLEGKVTATTFSLEQPRCVFDGLASASDTVWLVVAFSNASRGFQNPETLADIPASPQLLTDGHYMTLPLSPDQLPCGDPMAGSGGAPVLRVGHDHGCHQQPFCNAPLPGPGPYREDPRIHRHLARAAKWQHDRHYLHPLFSGRPPTLGLLGSLYHALLQPVVAGGGPGAAADRLLHGQALHDPPHPTQRGRHTAGGLQAWPGPPPQPQPLAWPLCMGLGEMGRWE
Protein: Cytochrome c oxidase subunit 3 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide III) (P18945)
Organism: Gallus gallus (Chicken)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00415}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00415}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 3
- Cytochrome c oxidase subunit 5A.
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 2
- Cytochrome b
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 2
- Cytochrome c oxidase subunit 5B.
- Cytochrome c oxidase subunit 4
Sequence:
MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHYSSTTLLTMGLLSMLLVMLQWWRDVVRESTFQGHHTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGVKPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNRKQAIHALTLTILLGFYFTALQAMEYHEASFSIADSVYGSTFFVATGFHGLHVIIGSSFLTVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDIIWLFLYMSMYWWGS
Protein: FTSH protease 6 (F4K9Q6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MKMASSSSALSFPLSNIPTCSKKSQQFQKPASLSKSSHTHKPSLKTQILHHKFTKRNLLSLTTALGFTSALGTVLAHPAKAEPEAPIEATSNRMSYSRFLQHLKENEVKKVDLIENGTVAIVEISNPVVGKIQRVRVNLPGLPVDLVREMKEKNVDFAAHPMNVNWGAFLLNFLGNLGFPLILLVSLLLTSSSRRNPAGPNLPFGLGRSKAKFQMEPNTGITFEDVAGVDEAKQDFEEIVEFLKTPEKFSALGAKIPKGVLLTGPPGTGKTLLAKAIAGEAGVPFFSLSGSEFIEMFVGVGASRARDLFNKAKANSPCIVFIDEIDAVGRMRGTGIGGGNDEREQTLNQILTEMDGFAGNTGVIVIAATNRPEILDSALLRPGRFDRQVCWLILKPNKSNRFGIMSTCFKQVSVGLPDIRGREEILKVHSRSKKLDKDVSLSVIAMRTPGFSGADLANLMNEAAILAGRRGKDKITLTEIDDSIDRIVAGMEGTKMIDGKSKAIVAYHEVGHAI
Protein: Zinc finger protein YPR022C (Q12139)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized protein YMR074C
- Zinc finger protein YGR067C
- Uncharacterized protein YBL081W
- Nucleoporin NSP1
- Uncharacterized protein YOL098C
Sequence:
MHGKELAGRLRKRENDNDLSPNSSSSPAERFRCPHPECNKTFSRQEHLSRHKLNHWPKEIYVCSYVLPTTNAPCNKTFVRKDLLIRHEKRHSKVKNRLSRPSKDQISSSNKDFSKNAPYNPSEVPLSTQSGTSTINLIKNSVNPPPSITQESKFRPFLQQAQQPQQVQQSQQPQQIQQLQQLQFPQQLRAPLQQPMLQQQMHPQQASPTFPSYDPRIRNNGQNGNQFFNLIFDNRTGVNGFEVDAANNNGNGNDQNMNINPAVQQQRYQDRNFASSSYQQPLQPLTQDQQQEQYFQQQKLAQQQQQQQQQQQQQQQLPPQNPFGDPLTSSSSGANLSVMQDLFSTNFLNSDPLQSFMQELSEAPQVSIEDTFSDKNTIPPNEKPVQQDEGFQNPPVMFELPQDNIKIPKAQPKFNDNPSTSVKDNLSSQKLNINELKRRSSKDSGVGNNSSLNYKEQLRHSMKSVPSFFHPDPLTKYKISKEKCQEMFSFVPELRYVSIESIHKSLKSFWLNFHPQYGLLHKPSFHVDKQPAILNLALIMTGASFLGSEYREQISDPICGPLRWIIFSHADFQPPSKTYIIQSLLLVEGYEKTSTNRYLHERSFLHHGTTIQLLRRTPSLGGHPLMVKTGKTSGENSIQDPQEVYKRWIDFEMLKRIAFYAFYMDTTHAVVFGYWNLFINSNQIQLTLPCPDQVWESYDLSYETLMEHGYGSTKRDENNTFLSALMQLMKNVIQILRNNNIRRNKVNNGGIESTPTDLESTTDWNIQSLFGKKILLAGIISILFQCQEEVNGDYFITNFRGGITDHLGLSWKDILSFAMNYWLHEVQKSCTDPKACRISTPSEETLTNRKIDEDNGDGLCDDDLDLLSSDNPSNCKIPVIHISQIVLRILHHDYYIYAGAPWRMNVPIGRDEYDMISRRILQFAKDPYNGGVAVVYAFQFLFEMFIIKENNVPTVVKSYNINSDPVITRPYAIALTSLLIWSCNFALHGCEVSIWDNTEASKDECFQPDDSNGGNILGNTDNNGSTIANNNLKEKNNYIPIESFEVYLLRMYRNLYVDSSLDVVSFQNDVWAKASLLQHISNTHFLCGMMQFMRDIFNKSYWDLGREFGKLFDNCLERSLGKTSPTCHNMFDV
Protein: Glutamate dehydrogenase (Q8ILF7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- glutamate synthase
- Glutamine synthetase, putative
- Aspartate aminotransferase
- Isocitrate dehydrogenase
- Glutamate dehydrogenase
- Glutamate dehydrogenase, putative
- 2-oxoglutarate dehydrogenase E1 component
- Citrate synthase
- Dihydrolipoyl dehydrogenase, apicoplast
- Dihydrolipoyl dehydrogenase
Sequence:
MILYSCVVCFIVFVFHVKAYSKNKVLKYAKPGFITNEIDIGAYAKRRGKSRLGSLHNYGYTSTKSVDNQIEELREKVVSKNKNEPEFLQAFEEVLSCLKPVFKKDNVYIGVLENIAEPERVIQFRVPWINDKGEHKMNRGFRVQYNSVLGPYKGGLRFHPTVNLSVIKFLGFEQIFKNSLTTLPMGGGKGGSDFDPKGKSENEILKFCQSFMTNLFRYIGPNTDVPAGDIGVGGREIGYLFGQYKKLKNSFEGVLTGKNIKWGGSNIRAEATGYGVVYFAENVLKDLNDNLENKKCLVSGSGNVAQYLVEKLIEKGAIVLTMSDSNGYILEPNGFTKEQLNYIMDIKNNQRLRLKEYLKYSKTAKYFENQKPWNIPCDIAFPCATQNEINENDADLFIQNKCKMIVEGANMPTHIKALHKLKQNNIILCPSKAANAGGVAVSGLEMSQNSMRLQWTHQETDMKLQNIMKSIYEQCHNTSKIYLNESDLVAGANIAGFLKVADSFLEQGGL
Protein: Phosphatidylinositol 4-phosphate 5-kinase-like protein 1 (PI(4)P 5-kinase-like protein 1) (PtdIns(4)P-5-kinase-like protein 1) (Phosphatidylinositol phosphate kinase homolog) (PIPKH) (Q6U7H8)
Organism: Mus musculus (Mouse)
Function: May act as a scaffold to localize and regulate type I phosphatidylinositol 4-phosphate 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment and conversion to PI(3,4,5)P3.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14701839}. Membrane {ECO:0000269|PubMed:14701839}. Note=Localized to large cytoplasmic vesicular structures.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol-3-phosphatase SAC1
Sequence:
MATPSLRSHEIPAHSQEAGNKSISSGSRRGLLWHLRARQSRVGLFEVGPGHELHRMTRMMQEGLWAATQVSKNNPPTGPTTQKDYLEVMTQVHEEGFELGTLAGPAFARLRKSIGLTEEDYQATLGPGDPYLQFFSTSKSKASFFLTHDQRFFVKTQRRHEVHVLLAHLPRYVEHLQQYPHSLLARLLGVYSLRVAQGKKKYFIIMQCIFYPTSRISERYDIKGCNISRWVDPAPEGSPLVLVLKDLNFQEKTMRLGAQRSWFLRQMELDTAFLREVNVLDYSLLVAIQFLHEDEKGIHHSVFSTFKSIQGVSKSKGTGDQNCRMLPDLPNALHILDGPDQRYFLGLVDMTTVYGFRKRLEHVWKMVRYPGQSVSTVSPAHYARRLCRWAEVHTE
Protein: Nitrite oxidoreductase subunit A (Similar to nitrate reductase subunit NarG (EC 1.7.99.4)) (Q1PZD8)
Organism: Kuenenia stuttgartiensis
Interaction partners:
Sequence:
MKLTRRAFLQVAGATGATLTLAKNAMAFRLLKPAVVVDNPLDTYPDRRWESVYRDQYQYDRTFTYCCSPNDTHACRIRAFVRNNVMMRVEQNYDHQNYSDLYGNKATRNWNPRMCLKGYTFHRRVYGPYRLRYPLIRKGWKRWADDGFPELTPENKTKYMFDNRGNDELLRASWDEAFTYASKGIIHITKKYSGPEGAQKLIDQGYPKEMVDRMQGAGTRTFKGRGGMGLLGVIGKYGMYRFNNCLAIVDAHNRGVGPDQALGGRNWSNYTWHGDQAPGHPFSHGLQTSDVDMNDVRFSKLLIQTGKNLIENKMPEAHWVTEVMERGGKIVVITPEYSPSAQKADYWIPIRNNTDTALFLGITKILIDNKWYDADYVKKFTDFPLLIRTDTLKRVSPKDIIPNYKLQDISDGPSYHIQGLKDEQREIIGDFVVWDAKSKGPKAITRDDVGETLVKKGIDPVLEGSFKLKTIDGKEIEVMTLLEMYKIHLRDYDIDSVVSMTNSPKDLIERLAKDIATIKPVAIHYGEGVNHYFHATLMNRSYYLPVMLTGNVGYFGSGSHTWAGNYKAGNFQASKWSGPGFYGWVAEDVFKPNLDPYASAKDLNIKGRALDEEVAYWNHSERPLIVNTPKYGRKVFTGKTHMPSPTKVLWFTNVNLINNAKHVYQMLKNVNPNIEQIMSTDIEITGSIEYADFAFPANSWVEFQEFEITNSCSNPFIQIWGKTGITPVYESKDDVKILAGMASKLGELLRDKRFEDNWKFAIEGRASVYINRLLDGSTTMKGYTCEDILNGKYGEPGVAMLLFRTYPRHPFWEQVHESLPFYTPTGRLQAYNDEPEIIEYGENFIVHREGPEATPYLPNAIVSTNPYIRPDDYGIPENAEYWEDRTVRNIKKSWEETKKTKNFLWEKGYHFYCVTPKSRHTVHSQWAVTDWNFIWNNNFGDPYRMDKRMPGVGEHQIHIHPQAARDLGIEDGDYVYVDANPADRPYEGWKPNDSFYKVSRLMLRAKYNPAYPYNCTMMKHSAWISSDKTVQAHETRPDGRALSPSGYQSSFRYGSQQSITRDWSMPMHQLDSLFHKAKIGMKFIFGFEADNHCINTVPKETLVKITKAENGGMGGKGVWDPVKTGYTAGNENDFMKKFLNGELIKVDA
Protein: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60) (4-diphosphocytidyl-2C-methyl-D-erythritol synthase) (MEP cytidylyltransferase) (MCT) (P9WKG9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Interaction partners:
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 1-deoxy-D-xylulose-5-phosphate synthase
- RNA polymerase-binding transcription factor CarD
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 2
- Uncharacterized tRNA/rRNA methyltransferase Rv3579c
- Cysteine--tRNA ligase
Sequence:
MVREAGEVVAIVPAAGSGERLAVGVPKAFYQLDGQTLIERAVDGLLDSGVVDTVVVAVPADRTDEARQILGHRAMIVAGGSNRTDTVNLALTVLSGTAEPEFVLVHDAARALTPPALVARVVEALRDGYAAVVPVLPLSDTIKAVDANGVVLGTPERAGLRAVQTPQGFTTDLLLRSYQRGSLDLPAAEYTDDASLVEHIGGQVQVVDGDPLAFKITTKLDLLLAQAIVRG
Protein: Uncharacterized protein (Q57W98)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTFQRRKRVTTALSVNVQDRRHHTRTLMETRQRKSALLALDSEEVVHRLRAMRPPEGLLDSEFPKADVEDFQSRARSRGGDSASNEEGKELPPVPPPPRTFKQWADKGFPTTSWRPLLSEELYHPLEAQKMILTNKYTPSQKLKSKMKDNAEPDS