wanglab/gogpt-training-data huggingface dataset:
Protein: Protein X (HBx) (Peptide X) (pX) (Q9QMH9)
Organism: Hepatitis B virus (HBV)
Subcellular location: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04074}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04074}. Host mitochondrion {ECO:0000256|HAMAP-Rule:MF_04074}. Note=Mainly cytoplasmic as only a fraction is detected in the nucleus. In cytoplasm, a minor fraction associates with mitochondria or proteasomes. {ECO:0000256|HAMAP-Rule:MF_04074}.
Interaction partners:
Sequence:
MAARLCCQLDPARDVLCLRPVGAESCGRPFSGPLGALSSPSLPAVPADHGAHLSLRGLPVCAFSSAGPCALRFTSARRMETTVNAHQILPKVLHKRTLGLSAMSTTDLEAYFKDCLFKDWEELGEEIRLKVFVLGGCRHKLVCAPAPCNFFTSA
Protein: Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.143) (Beta-1,2-N-acetylglucosaminyltransferase II) (GlcNAc-T II) (Mannoside acetylglucosaminyltransferase 2) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II) (Q59DT4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
Sequence:
MSKMRGRILIPLPNTGAMGRKRNNFYMRSLFLLALGIFGLLQYNNFNYLDSRDNVLGDAVTNDSDDAILAMVPATLHKYLTPHSRNHSASGAGALNGAALLLNASSPGAATASTISFDVYHPPNITEIKRQIVRYNDMQMVLNEDVFGPLQNDSVIIVVQVHTRITYLRHLIVSLAQARDISKVLLVFSHDYYDDDINDLVQQIDFCKVMQIFYPYSIQTHPNEYPGVDPNDCPRNIKKEQALITNCNNAMYPDLYGHYREAKFTQTKHHWIWKANRVFNELEVTRYHTGLVLFLEEDHYVAEDFLYLLAMMQQRTKDLCPQCNVLSLGTYLKTFNYYTYHSKVEVMPWVSSKHNMGFAFNRTTWSNIRKCARHFCTYDDYNWDWSLQHVSQQCLRRKLHAMIVKGPRVFHIGECGVHHKNKNCESNQVISKVQHVLRIARNSHQLFPRSLTLTVPSLMKKSKLRKGNGGWGDMRDHELCLNMTLATR
Protein: Probable L-asparaginase 4 (EC 3.5.1.1) (L-asparagine amidohydrolase 4) (Q8TFF8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Multifunctional protein ura1
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Argininosuccinate synthase
- Adenylosuccinate synthetase
- Truncated RecQ DNA helicase-like protein C212.06c
- Aspartokinase
Sequence:
MWGFIVTCGIFLVLLCQLRLLSKRKSKSTPYNALLPNVTVFAMGGTIAGCANSSLEIVNYIPGSVGIEKLIEAVPAIKAIANINGVQVTNMGSENLTPADVLKLAKLILAEVAKPNVHGIVITHGTDSLEETAMFLDLTISTAKPIVVVGAMRPSTAIGADGPMNLLNAVAVASSNQSMGRGTLVLLNDRIGSAFYTTKTNGNTLDTFKSYEAGSLGIVLNQKPFYFFSPAVPTGKVFFDIYNIKQLPRVDILYGYQGLNPKLAESAVHLGAKGLVLAAMGATSWTDDGNEVISSLIREHNIPVVYSHRTAEGYSSNSCLGIPSYFLNPQKARYMLMLAISSGYSIRDIEGLFSIK
Protein: Protein lin-7 homolog A (Lin-7A) (mLin-7) (Mammalian lin-seven protein 1) (MALS-1) (Vertebrate lin-7 homolog 1) (Veli-1) (Q8JZS0)
Organism: Mus musculus (Mouse)
Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules. This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction {ECO:0000269|PubMed:15494546}. Postsynaptic density membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction, tight junction {ECO:0000269|PubMed:15494546}. Note=Mainly basolateral in renal epithelial cells.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Amyloid-beta A4 precursor protein-binding family A member 1
- Phagosome assembly factor 1
- Disks large homolog 1
- Protein PALS1
- Kinesin-like protein KIF17
- MAGUK p55 subfamily member 7
- Liprin-alpha-2
- Glutamate receptor ionotropic, NMDA 2B
Sequence:
MLKPSVTSAPTADMATLTVVQPLTLDRDVARAIELLEKLQESGEVPVHKLQSLKKVLQSEFCTAIREVYQYMHETITVNGCPEFRARATAKATVAAFAASEGHSHPRVVELPKTDEGLGFNVMGGKEQNSPIYISRIIPGGVAERHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAKDSVKLVVRYTPKVLEEMEARFEKLRTARRRQQQQLLIQQQQQQQQQQPQQNHMS
Protein: 4Cytl1 protein (Q0VG51)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSPKTLPLLLLLVVVVVIAWPLAVQSAPPTCYSRMLTLSREIMADFQSLQASEPEDSCVRYLPRLYLDIHNYCVLAKLRDFVASPQCWKMAEVDTLKDRVRKLYTIMNSFCRRDLVFLSDDCSALEDPIPEATGPPDWQS
Protein: J domain-containing protein (D7SFQ5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MDVSKMIASAMPVQDLRMIVNFATRRMPTLNTFQFDRYKLLCVRNDRELDGYQRSYGDVDSEDESPILRSARSKSGTKAAETSSSQGNFFDSLQFEDRQEPHHFREQRDSTLLDHHDDVTHHTADLLDGFTIGGTEKLSPANETPILSAPTPASSDYDSMTSSQNRRNPSPATAIDDLLGLGTETSAPAPAPSTHFNNSSSGANLVDFDLGAPIKPTSSASNLSTASPATSSWSNTDLLGGFSPMKPQTTSTPPNTRNPSASNSKPVSQVNSQADFEAFLSNYPEQRQAAPQNTQNVSQKTQQTRPQNTYKPAFGDAATGSAKVSMDAFSDLLNQGGFKPTQRENQKQSIGNMLKVEQSKNLTPEEIQIRDWTQGKERNIRALLGSLHNVLWEGADRWNQPSMGDLLTPDQIKKHYRKACLVVHPDKLTGSPHLSLAKMAFTELNDAYSKYQNDPAAM
Protein: Cystathionine gamma-synthase (CGS) (EC 2.5.1.48) (O-succinylhomoserine (thiol)-lyase) (P9WGB7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction (By similarity). In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable cystathionine beta-synthase Rv1077
- Methionine synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Branched-chain-amino-acid aminotransferase
- O-acetylserine sulfhydrylase
- Sulfite reductase [ferredoxin]
- L-cysteine desulfhydrase Cds1
- Homoserine O-acetyltransferase
- cysteine-S-conjugate beta-lyase
- Putative cystathionine beta-lyase
Sequence:
MSEDRTGHQGISGPATRAIHAGYRPDPATGAVNVPIYASSTFAQDGVGGLRGGFEYARTGNPTRAALEASLAAVEEGAFARAFSSGMAATDCALRAMLRPGDHVVIPDDAYGGTFRLIDKVFTRWDVQYTPVRLADLDAVGAAITPRTRLIWVETPTNPLLSIADITAIAELGTDRSAKVLVDNTFASPALQQPLRLGADVVLHSTTKYIGGHSDVVGGALVTNDEELDEEFAFLQNGAGAVPGPFDAYLTMRGLKTLVLRMQRHSENACAVAEFLADHPSVSSVLYPGLPSHPGHEIAARQMRGFGGMVSVRMRAGRRAAQDLCAKTRVFILAESLGGVESLIEHPSAMTHASTAGSQLEVPDDLVRLSVGIEDIADLLGDLEQALG
Protein: 2'-phosphotransferase (EC 2.7.1.160) (Q385M0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMNISPQFKRWGQNTRNLQQQEAYPLREPPFDTYMVLDFEATCERHQRLEVPEVIEFPIVLVDARNGNTISEFQQYVRPVVNPQLSQFCTELTGITQSVVDRASTFPDVFTAAMNYLHQNNCGEREINKRYLPVTCGDWDLKTMLPIQVKACIQQGFTVNVPPSLRRWFNIKQYMQRVLSPGLGQTVSQPIRDLPDMMSVLGLEMKGRHHSGIDDCRNIAAVLCELIKLGHVITPTTDYNSELTRGTSWVSVGATTSLKPSAGLGKCQQMPHCREEGSNNSAMGRKRAASDTVNNQQSMIKRIHINVLENEDPLQDLLNLKTDDRNRMGSEDMTKEKVVTYSKALSRILRHGADKMKITISDAGYVLADDLVRCAPFSNDKAALTHLAWVVYSNDKKRFKMAYDENRRVYIRANQGHSLSGINPELVPITSETQVPFAVHGTYYSAWERIRGCGYLSTMGRQHIHFAKGMPGSDGVISGMRNTSEVLLVLDVPLLLKESVELWESANGVLLTPGVSGTGRLPLKYISSVVDRRTNDLLPR
Protein: Polyubiquitin, putative (Q383T7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L17, putative
- 40S ribosomal protein S25
- 60S ribosomal protein L35, putative
- 40S ribosomal protein S13, putative
- 60S ribosomal protein L27a
- 60S ribosomal protein L13a, putative
- 40S ribosomal protein S17, putative
- 40S ribosomal protein S24
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S14
Sequence:
MQIFVKTLTGKTIALEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEEGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTIALEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEEGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTIALEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEEGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTIALEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEEGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTIALEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEEGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTIALEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEEGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTIALEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEEGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTIALEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEEGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTIALEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEEGRTLADYNIQKESTLHLVLRLRGGW
Protein: Accessory gland protein Acp53Ea (O46199)
Organism: Drosophila melanogaster (Fruit fly)
Function: Responsible for physiological and behavioral changes in mated female flies.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- ACP53C14B
- Accessory gland protein Acp36DE
- Accessory gland protein Acp63F
- Accessory gland-specific peptide 26Ab
- ACP53C14A
- Accessory gland-specific peptide 26Aa
- Accessory gland protein Acp76A
- Accessory gland protein Acp29AB
- Accessory gland protein Acp62F
- Male-specific opa-containing protein
Sequence:
MKLIKVTLVFSLLALVFVAQTEAQNPIWENWLACNRIGTKALASLLRETIPTVRNLLNCIDFNPPTDIGNSYLSKLKLYYELVKRGALDKTQCLIVPLKESVRLLRPYVKSLETNKCLGE
Protein: Brevinin-2Rg (C0HL01)
Organism: Pelophylax ridibundus (Marsh frog) (Rana ridibunda)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000269|PubMed:28012108}.
Interaction partners:
Sequence:
GILLDKLKNFAKGVAQSLLNKASCALSGQC
Protein: Methanol dehydrogenase activator (EC 3.-.-.-) (MDH activator) (Q8KP10)
Organism: Bacillus methanolicus
Function: Involved in the activation of the NAD-dependent methanol dehydrogenase (MDH). MDH activation by Act involves hydrolytic removal of the nicotinamide mononucleotide (NMN) moiety of the NAD cofactor, changing its ping-pong type of reaction mechanism into a ternary complex reaction mechanism. It requires the presence of magnesium ions and is also able to use ADP-ribose.
Interaction partners:
Sequence:
MGKLFEEKTIKTEQIFSGRVVKLQVDDVELPNGQTSKREIVRHPGAVAVIAITNENKIVMVEQYRKPLEKSIVEIPAGKLEKGEDPRVTALRELEEETGYECEQMEWLISFATSPGFADEIIHLYVAKGLSKKENAAGLDEDEFVDLIELTLDEALQYIKEKRIYDSKTVIAVQYLQLQEALKHK
Protein: Putative sulfoquinovose importer (P32136)
Organism: Escherichia coli (strain K12)
Function: Could be involved in sulfoquinovose import.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sulfoquinovosidase
- Uncharacterized protein YihR
- Sulfoquinovose isomerase
- Sulfofructosephosphate aldolase
- 3-sulfolactaldehyde reductase
- Sulfofructose kinase
- HTH-type transcriptional repressor CsqR
- Porin OmpL
- Ferredoxin-like protein YgcO
Sequence:
MSDHNPLTLKLNLREKIAYGMGDVGSNLMLCIGTLYLLKFYTDELGMPAYYGGIIFLVAKFFTAFTDMLTGFLLDSRKNIGPKGKFRPFILYAAVPAALIATLQFIATTFCLPVKTTIATALFMMFGLSYSLMNCSYGAMIPAITKNPNERAQLAAYRQGGATIGLLICTVAFIPLQSLFSDSTVGYACAALMFSIGGFIFMMLCYRGVKEHYVDTTPTGHKASILKSFCAIFRNPPLLVLCIANLCTLAAFNIKLAIQVYYTQYVLNDINLLSWMGFFSMGCILIGVLLVPLTVKCFGKKQVYLAGMVLWAVGDILNYFWGSNSFTFVMFSCVAFFGTAFVNSLNWALVPDTVDYGEWKTGIRAEGSVYTGYTFFRKISAALAGFLPGIMLTQIGYVPNIAQSDATLQGLRQLIFIWPCALAIIAALTMGFFYTLNEKRFALIIEEINQRKNKEMATEEKTASVTL
Protein: Thiosulfate-binding protein (P16700)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. This protein specifically binds thiosulfate and is involved in its transmembrane transport.
Subcellular location: Periplasm.
Interaction partners:
- Sulfate/thiosulfate import ATP-binding protein CysA
- Sulfate adenylyltransferase subunit 1
- Sulfate transport system permease protein CysT
- Sulfate transport system permease protein CysW
- Sulfate adenylyltransferase subunit 2
- Sulfite reductase flavoprotein alpha-component
- Sulfite reductase hemoprotein beta-component
- Adenylyl-sulfate kinase
- Sulfate-binding protein
- Cysteine synthase A
Sequence:
MAVNLLKKNSLALVASLLLAGHVQATELLNSSYDVSRELFAALNPPFEQQWAKDNGGDKLTIKQSHAGSSKQALAILQGLKADVVTYNQVTDVQILHDKGKLIPADWQSRLPNNSSPFYSTMGFLVRKGNPKNIHDWNDLVRSDVKLIFPNPKTSGNARYTYLAAWGAADKADGGDKGKTEQFMTQFLKNVEVFDTGGRGATTTFAERGLGDVLISFESEVNNIRKQYEAQGFEVVIPKTNILAEFPVAWVDKNVQANGTEKAAKAYLNWLYSPQAQTIITDYYYRVNNPEVMDKLKDKFPQTELFRVEDKFGSWPEVMKTHFTSGGELDKLLAAGRN
Protein: Protein EMP46 (46 kDa endomembrane protein) (Q12396)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the secretion of glycoproteins and in nucleus architecture and gene silencing.
Subcellular location: Golgi apparatus membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
- Protein EMP47
Sequence:
MTTRKTASSLQLLGKITGTKAGTKQKKMNFINGLIWLYMCVWMVHGKVTQKDELKWNKGYSLPNLLEVTDQQKELSQWTLGDKVKLEEGRFVLTPGKNTKGSLWLKPEYSIKDAMTIEWTFRSFGFRGSTKGGLAFWLKQGNEGDSTELFGGSSKKFNGLMILLRLDDKLGESVTAYLNDGTKDLDIESSPYFASCLFQYQDSMVPSTLRLTYNPLDNHLLKLQMDNRVCFQTRKVKFMGSSPFRIGTSAINDASKESFEILKMKLYDGVIEDSLIPNVNPMGQPRVVTKVINSQTGEESFREKMPFSDKEESITSNELFEKMNKLEGKIMANDIDPLLRKMNKIVENERELIQRLRPLLDLKKTAISDDSFQDFLSMNANLDRLIKEQEKIRQDAKLYGKQTKGHDEIFSKISVWLALLIFIMITLAYYMFRINQDIKKVKLL
Protein: 3-hydroxybutyryl-CoA dehydratase (EC 4.2.1.55) (R-specific crotonase) (C5AZ74)
Organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens)
Function: Involved in the regeneration of glyoxylate from a molecule of acetyl-CoA.
Interaction partners:
- Crotonyl-CoA carboxylase/reductase
- Acetoacetyl-CoA reductase
- enoyl-CoA hydratase
- Poly
- 3-methylmercaptopropionyl-CoA dehydrogenase
- 3-hydroxyisobutyryl-CoA hydrolase
- Phosphate acetyltransferase
- Beta-ketothiolase
- Isobutyryl-CoA dehydrogenase
- 3-hydroxybutyryl-CoA dehydratase
Sequence:
MLPELRVLYFEDLEVGLTEILKKEISSSDVVGFAEITGDRNPIHLSEHFAARTPFGTRIAHGLYTAGLISAVLGTRLPGPGAVYISQTLNFRAPVRIGDIVEVKVEVAELIPERRRARLACTCSVGDEVVLDGEALVKVPKKEEADPLAMRMGGGRA
Protein: 8-amino-7-oxononanoate synthase (AONS) (EC 2.3.1.47) (7-keto-8-amino-pelargonic acid synthase) (7-KAP synthase) (KAPA synthase) (8-amino-7-ketopelargonate synthase) (P12998)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate, but it is believed that pimeloyl-ACP rather than pimeloyl-CoA is the physiological substrate of BioF.
Interaction partners:
- ATP-dependent dethiobiotin synthetase BioD 1
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Biotin synthase
- Malonyl-[acyl-carrier protein] O-methyltransferase
- Pimeloyl-[acyl-carrier protein] methyl ester esterase
- ATP-dependent dethiobiotin synthetase BioD 2
- Bifunctional ligase/repressor BirA
- Malonyl CoA-acyl carrier protein transacylase
Sequence:
MSWQEKINAALDARRAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLRQQGCWVTAIRPPTVPAGTARLRLTLTAAHEMQDIDRLLEVLHGNG
Protein: Aspartate aminotransferase, mitochondrial (EC 2.6.1.1) (Transaminase A) (O94320)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Malate dehydrogenase, mitochondrial
- Aromatic amino acid aminotransferase C569.07
- Aromatic amino acid aminotransferase C56E4.03
- Probable L-lactate dehydrogenase
- Aromatic amino acid aminotransferase C1773.13
- Putative alanine aminotransferase
- Probable prephenate dehydrogenase [NADP
- NADP-specific glutamate dehydrogenase
- Aspartate aminotransferase, cytoplasmic
- Probable asparagine synthetase
Sequence:
MLARNLRCLHPNTFASLKTNVSYHGVKCLASQSKRGFKVWADVPMGPPDPIFGITEAYKKDGDVKKMNLGAGTYRDDAGKPYVLPSVRQAETELLSQKLDKEYAPITGIPSFRVQATKLAYGDVYESIKDRLVSAQSISGTGALCIAANFLASFYPSKTIYVSDPTWGNHKNVFSRAGLTVKSYKYYDPATRGLDIKGMLSDLTSAPDGSIILLHACAHNPTGVDPTKAQWDDILKTMQKKNHFALLDMAYQGFASGDFARDAYATRLFASSNVPMLLCQSFAKNMGLYGERAGCFSILANDAEEAARIESQTKILIRALYSNPPVNGARIANHILSNPALREQWAGEVVGMSERLKSMRKALRNILEKDLKNKHSWKHITDQIGMFCYTGLNPQQVDVLAKQYHIYLTKNGRISISGLNTSNVRYFAEAINAVTSN
Protein: Arc, isoform A (Arc, isoform B) (Arc, isoform C) (GH21134p) (PDZ domain protein Arc) (Q9W283)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRLFKTRKSTDTYSTLAAQQQQQQQQQQQHQAEGSNISHSSNSSSNKSHTPATCSNRLNKSIVSSTSISSSLPDLHDKSPVMILSCTTLASNGATATAAVTATATGTAATSGGSLQQQQQQHLQHQQQQQPLRTATPTCLLSGRQTPSAISVMSLQEATSLHRQQQQPHQPPTIYVPVPTKLGNNVNTGNSSATLLLSYGSTSSIANLQQQQQQHAAQYQQYVAQRLHAASSSCLYEKGSNASGGASSNKSSLSLTPNGHLPDYKLVTAMPVVVLDDEHKSNSLPATEASRNSNSSSNMNGSSNSNSLDVSNSNSHSGSSTSLASTTRNVFTWGKRMSRKLDLLKRSDSPAAAHKSHSDLRSLFHSPTHHKSGSGGSSGPSSAKASASPTGGHQNSSGSTTSTLKKCKSGPIETIKQRHQQQQQQQQSVQDVGTGQSQSAQSTPTHQFQAAARPQKALKNFFHRIGSTGMLNHRSHNLLKASEAAQQATPAATTLYRSSSTSQLSSSSYVKCDDPTEGLNLQREQREQRLPRIASLKSSSCDDIAKVSSCLTASTSSGSAAGSLGSPPSSAAAGGGGTANSGQHDPSRRGAFPYAFLRSRLSVLPEENHGNVPGHLKQQIQRQREQHQQHQRDLLQQEQTSSPLPQRRSPEQAMLNNVSRNDSITSKDWEPLYQRLSSCLSSNESGYDSDGGATGARLGNNLSISGGDTESIASGTLKRNSLISLSSSEGVGMGMGMSLGLGAPSTRNSSICSAPVSLGGYNYDYETETIRRRFRQVKLERKCQEDYIGIVLSPKTVMTNSNEQQYRYLIVELEPYGMAQKDGRLRLGDEIVNVNGKHLRGIQSFAEVQRLLSSFVDNCIDLVIAHDEVTTVTDFYTKIRIDGMSTQRHRLSYVQRTQSTDSLSSMQSLQLQQERIQGHNTEQEQEAQGEDQCDARSMASVSTMPTPMPLMQHRRSSTPRHSLDVGAPEHELLRRRARSSSGQRSLALTPTPLFASGSSSCSSSPNHRLLDNENDPANDTDSYTPVYANRAASVCVASSLADDEKWQLLARKRCSEGSALSATPNPQQFGQRTHYARNSINLANSHYRSLRFAHSRLSSSRLSLFMQAPPNSLTVGEGVANTPSSTATTTTDLTNQQQQQQNQQQTHQSLYIKHSPKSVSLFSPNPYVNASSSPASASTSAGAGSSLAPPAAALMHHRPSLPVAKLTIRDEEMAEVIRASMSEGSGRCTPKTITFFKGPGLKSLGFSIVGGRDSPKGNMGIFVKTVFPSGQAADDGTLQAGDEIVEINGNSVQGMSHAETIGLFKNVREGTIVLKILRRKLQKAKSMGC
Protein: Dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) (DHOdehase) (DHOD) (DHODase) (Dihydroorotate oxidase) (P0A7E1)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Subcellular location: Cell membrane; Peripheral membrane protein.
Interaction partners:
- Dihydroorotase
- Orotate phosphoribosyltransferase
- Aspartate carbamoyltransferase catalytic subunit
- Orotidine 5'-phosphate decarboxylase
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
- NAD
- Uracil phosphoribosyltransferase
- Uncharacterized protein YfgD
- Uracil permease
Sequence:
MYYPFVRKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKVPAKPVNCMGLTFKNPLGLAAGLDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLVENVKKAHYDGVLGINIGKNKDTPVEQGKDDYLICMEKIYAYAGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQNDLQAMHHKYVPIAVKIAPDLSEEELIQVADSLVRHNIDGVIATNTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSGFIFKGPPLIKEIVTHI
Protein: Heat shock protein beta-7 (HspB7) (Cardiovascular heat shock protein) (cvHsp) (Heat shock protein 25 kDa 2) (Protein p19/6.8) (P35385)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Note=Resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000250}.
Interaction partners:
- Filamin-C
- Heat shock protein beta-2
- Heat shock protein beta-3
- Filamin-A
- Heat shock protein beta-9
- BAG family molecular chaperone regulator 3
- Heat shock protein beta-8
- Myozenin-2
- Leiomodin-2
Sequence:
MSHRTSSAFRAERSFRSSSSSSSSSSSSASRALPAQDPPMEKALSMFSDDFGSFMLPHSEPLAFPARPGGQGNIKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRAEKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRARRHPHTEHVQQTFRTEIKI
Protein: Core protein (Q8V7L6)
Organism: Hepacivirus hominis
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
Interaction partners:
Sequence:
MSTNPKPQRKTNRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPEGRAWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTIPASA
Protein: Pre-mRNA-splicing factor PRP9 (P19736)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: mRNA splicing factors, PRP9, PRP11, and PRP21, are necessary for binding of the U2 snRNP to the pre-mRNA in an early step of spliceosome assembly.
Subcellular location: Nucleus.
Interaction partners:
- Pre-mRNA-splicing factor SYF1
- Protein HSH49
- Cold sensitive U2 snRNA suppressor 1
- U2 small nuclear ribonucleoprotein A'
- U1 small nuclear ribonucleoprotein A
- Pre-mRNA-processing factor 19
- Pre-mRNA-processing ATP-dependent RNA helicase PRP5
- RDS3 complex subunit 10
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein-associated protein B
Sequence:
MNLLETRRSLLEEMEIIENAIAERIQRNPELYYHYIQESSKVFPDTKLPRSSLIAENKIYKFKKVKRKRKQIILQQHEINIFLRDYQEKQQTFNKINRPEETQEDDKDLPNFERKLQQLEKELKNEDENFELDINSKKDKYALFSSSSDPSRRTNILSDRARDLDLNEIFTRDEQYGEYMELEQFHSLWLNVIKRGDCSLLQFLDILELFLDDEKYLLTPPMDRKNDRYMAFLLKLSKYVETFFFKSYALLDAAAVENLIKSDFEHSYCRGSLRSEAKGIYCPFCSRWFKTSSVFESHLVGKIHKKNESKRRNFVYSEYKLHRYLKYLNDEFSRTRSFVERKLAFTANERMAEMDILTQKYEAPAYDSTEKEGAEQVDGEQRDGQLQEEHLSGKSFDMPLGPDGLPMPYWLYKLHGLDREYRCEICSNKVYNGRRTFERHFNEERHIYHLRCLGIEPSSVFKGITKIKEAQELWKNMQGQSQLTSIAAVPPKPNPSQLKVPTELELEEEDEEGNVMSKKVYDELKKQGLV
Protein: Polyadenylate-binding protein (PABP) (Q5VX58)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
Sequence:
MNPSTPSYPTASLYVGDLHPDVTEAMLYEKFSPAGPILSIRICRDLITSGSSNYAYVNFQHTKDAEHALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFVKNLDKSINNKALYDTVSAFGNILSCNVVCDENGSKGYGFVHFETHEAAERAIKKMNGMLLNGRKVFVGQFKSRKEREAELGARAKEFPNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRTFEQMKQDRITRYQVVNLYVKNLDDGIDDERLRKAFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAYLTNEYMQRMASVRAVPNQRAPPSGYFMTAVPQTQNHAAYYPPSQIARLRPSPRWTAQGARPHPFQNKPSAIRPGAPRVPFSTMRPASSQVPRVMSTQRVANTSTQTVGPRPAAAAAAAATPAVRTVPRYKYAAGVRNPQQHRNAQPQVTMQQLAVHVQGQETLTASRLASAPPQKQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLYMLESPESLRSKVDEAVAVLQAHQAKEATQKAVNSATGVPTV
Protein: Transcription elongation factor S-II (TFIIS) (P49373)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000255|PROSITE-ProRule:PRU00651}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit rpb1
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- Transcription elongation factor spt5
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit rpb4
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MDSADIRSAKAALEKAIQGKNIETIINIMTRLKNEVVATEELLKETRLGLVVGKLRSHPNEKVGEQAREIVKKWKADVSKGRPLKTTTTTSSTPSKHADVGSQAQKQVQKQSSSGQRTFKSDNVNVNVTDDKIRNNCIGLMYNALVIDSDESSSLIIAKAKEIDAQVLARAAGKTGSEYRNRMRSLYMNLKDKNNPKLRASVLRNEITPQRLSTMTSAELASEDRRKEDAKLEQENLFHAQGAKPQKAVTDLFTCGKCKQKKVSYYQMQTRSADEPMTTFCECTVCGNRWKFS