wanglab/gogpt-training-data huggingface dataset:
Protein: Multivesicular body subunit 12A (ESCRT-I complex subunit MVB12A) (Protein FAM125A) (Q17687)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004633}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004633}.
Interaction partners:
- Vacuolar protein sorting-associated protein 28 homolog
- VPS37 C-terminal domain-containing protein
- Tumor susceptibility gene 101 protein
- Signal transducing adapter molecule 1
- Apoptosis-linked gene 2-interacting protein X 1
- MAM domain-containing protein
- Vacuolar protein-sorting-associated protein 36
- Ras family protein
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- Vacuolar protein-sorting-associated protein 25
Sequence:
MTELEFSADNAAPVIPITAICIVADKNKAPRGFLPIIKCQDDQTEADLWRDGFFTINRQVRYICTSTEIPDSNIKTPVQVITNLIIVRESDPIPHGYVAIDYTADSREKSLRKKYVCIRTEPRDRVVDAIGEIIILGKTKKVPRDYTSAGDIDSLLICYKVISIPQTYGIQTSNSTSNIESQAAGGLYPGLPNLSNSTPANLDVTGSSSNSAFTMKNAGAPRVKAIDGIDFKVNPMFVNSSGSNNSSQLPDLSQFNDLDRLDDKYNYSYATEHAVLS
Protein: PIN domain-containing protein (Q386H4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLNITRLRNLPEDLFEVDRRQKNGSNQSGKGWPQHKELIFDFTSLVRAYNQNKFEHLTDTFNNNRILISELVLHQLDEKNKVVRSTDAANAQEDDFHPVRLRDLINFLVTNMTESWLEFQRKGTQEDKQFTQLRCLNENVETPLRLISYALYKKRQGKDVLLVTSDSGLKCEAGLNSIDSQSIENIG
Protein: Zinc finger protein ZIC 4 (Zinc finger protein of the cerebellum 4) (Q61467)
Organism: Mus musculus (Mouse)
Function: Binds to DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:15465018}.
Interaction partners:
- Zinc finger protein ZIC 1
- Delta and Notch-like epidermal growth factor-related receptor
- Amphiphysin
- Leucine-rich glioma-inactivated protein 1
Sequence:
MRLGRVCPRGPGKVRSPRHRFSCTLFVSTTGSSCGHHGPQLAASSNPSVLPGLHEQPPQASHSRPLNGLLRLGIPGDMYARSEPFAPGPMARSDTLATATALHGYGGMNLTMNLTAPHGPGAFFRYMRQPIKQELICKWLGDDSPMSPRPCSKTFSTMHELVTHVTVEHVGGPEQANHICFWEECPRQGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYMCKVRGCDKCYTHPSSLRKHMKVHGRSPPPSSGYDSAITSALASPSLESGREPSVACSAAVVVRGTDVSE
Protein: Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (EC 2.7.11.1) (Myt1 kinase) (Q9ESG9)
Organism: Mus musculus (Mouse)
Function: Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase specifically when CDK1 is complexed to cyclins. Mediates phosphorylation of CDK1 predominantly on 'Thr-14'. Also involved in Golgi fragmentation. May be involved in phosphorylation of CDK1 on 'Tyr-15' to a lesser degree, however tyrosine kinase activity is unclear and may be indirect. May be a downstream target of Notch signaling pathway during eye development (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99640}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99640}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99640}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99640}.
Interaction partners:
- Serine/threonine-protein kinase PLK1
- Cyclin-dependent kinase 1
- Proto-oncogene serine/threonine-protein kinase mos
- Ribosomal protein S6 kinase alpha-1
- Ribosomal protein S6 kinase alpha-6
- Ribosomal protein S6 kinase alpha-2
- Ribosomal protein S6 kinase alpha-3
- G2/mitotic-specific cyclin-B1
- G2/mitotic-specific cyclin-B2
- Cyclin-A2
Sequence:
MTMPTEGTPPPLSGTPIPVPAYFRHAEPGFSLKRPGGLSRSLPPRPPAKGCIPVSRLFPPRTPGWHQPQPRRVSFLCETSEPLQSPGYDPSRPESFFQQNFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRYMSPFRGPKDRTRKLAEVGGHEKVGQHPHCVRLERAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDILLALDHLHSQGLVHLDVKPANIFLGPRGRCKLGDFGLLVELGSAGAGEAQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQLRQGYLPPEFTAGLSSELRSVLAMMLEPDPQLRATAEALLALPMLRQPRPWNVLWYMAAEALSRGWALWQALVTLLCWLWHGLVHPASWLQPPGPPATPPGSPPCSPLLDSTLSSSWDNDSIGPSLSPETVLSRITRRTSTPRGRYIPRDALDLTDVDSEPPRGPCPTFEPRNLLSLFEDSLDPA
Protein: Thymidine phosphorylase (TP) (EC 2.4.2.4) (TdRPase) (Q99N42)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (By similarity).
Interaction partners:
- Uridine phosphorylase 1
- Cytidine deaminase
- Uridine 5'-monophosphate synthase
- Dihydropyrimidine dehydrogenase [NADP
- Thymidine kinase, cytosolic
- Uracil phosphoribosyltransferase homolog
- Thymidine kinase 2, mitochondrial
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- 5'
Sequence:
MAAPGTPPPSASGGGGGEPRQLPELIRLKRDGGHLREADIRNFVHAVIDGRAQDTQIGAMLMAIRLQGMNLEETSVLTRALAESGQQLEWPKAWHQQLVDKHSTGGVGDKVSLVLAPALAACGCKVPMISGRSLGHTGGTLDKLESIPGFGVTQSPEQMLHILEEVGCCIVGQSAKLVPADGILYAARDVTATVDSVPLITASILSKKAVEGLSTLVVDVKFGGAAVFPDQEKARELAKMLVRVGVSLGLKVAAALTAMDNPLGRSVGHTLEVEEALLCLDGAGPPDLRDLVIRLGGAILWISGQAETQDQGAARVAAALDDGSARRRFQLMLSAQGVDPGLAKALCSGSPTQRRQLLPHAREQEELLAPADGIVECVRALPLARVLHDLGAGRSRAGQPIRPGVGAEVLVDVGQCLSRGTPWLRVHLDGPALSSQQRRTLQGALVLSDRAPFKVPSPFAELVLPPTIAQP
Protein: AT3g10020/T22K18_16 (Plant/protein) (Q9SR67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Methionyl-tRNA synthetase
- Uncharacterized protein unannotated coding sequence from BAC F9L11
- DNA polymerase epsilon catalytic subunit A
- Emb|CAB82975.1
- Proline-rich extensin-like family protein
- Nematode resistance protein-like HSPRO2
- Proline-rich extensin-like family protein
- Conserved oligomeric Golgi complex subunit 7
- Proline-rich extensin-like family protein
- Adenine phosphoribosyltransferase 5
Sequence:
MQAVSVDETKNTVVLRAEHKNEEGRKSVDKFEVKTRNPETIKSVERKLMEKGVQRMDRHPSDGIPLRRPPSKSGHGGKYTWEGPDRMEDYEMQPDPPAMDEGDPNYDEEQVKKSGDDVAVELVKGEVEVAKEAPAGVARVEVDPRLVGR
Protein: Exportin 1 (Q382A3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- GTP-binding nuclear protein
- Nucleoporin
Sequence:
MEDILDFSKPVDVQRFDQVVQYLSTGSPQEIVRAQEVLTAFKERPDSFLRVGDLLTKSVNLTTRFFALQVLEDAILHRWNTFTAEQCQEIRNFVVNMIVGECVSFNQIRSRRALLMKMNSALVSIAKREWPVRWPTFIKDVCSSAGPDEPLVENNLNILRMVGEEIFEFSEKTLTTRWLKRKKEALQSDFQAILQLCLSILSTSDEALLKTNLECLEKYLSWVEPASVFNEELLKYLAGLIARKSAVSRCAVRCLTVACSVETDHGSVGDAQAQVMVRVFRTILDNIMNLLPTNHSSVEARIVQFSNMEGSVDAGFVGDLNLLLVAFLKHYTRNIMYDDLLLISANQLIVGMSHINDKELFKSCVDYWWWLGEKMVRSASPTPLHRKLALVLSNVRFTLIKKMARPEEVIIVVEDGEVRRVHMKDVEELQLYKLMRETLVFLTYLDPQDMQAIMTKIVMKLEDLSEWSWHNCNTLSWAVGAISVALTEEQESSLFVVIVRGLLDLCSKLQGKENRAVVASGIMFVVGQYPRFLRAHQPFFRAVVKKVIEFMCDLFPGVQEMAVDTLLKVASQVPDQFVCVKNNGISLAEETAKRWTEITSLLKPQHMHTCFVAAGWMVKGEKPERQPSLLGMFLQDANDSFRIIVERAASKGPAFGEDFSGMGELIHILRVFSSIASSCGTSFVNEMGIIIYDLQGLYRTFFSAQTALVADHGTDAMERQEARYLRLAKREILRIFECFVDNTEECDFVATNCMPSILTTVLEDYRDSLPIVKEAGALALVTACVNKLGTRLAGDCAAILDHTFDTTISMICANAEDFPEFRVNLFKLLHALNTRCFSNFLSYASTKGDVINGMLWVIKHTDFAIMETGLKTLDAFLENVSRSELLQPFYDAFMQQIFVEVLVSAMDSLHAAGFELHCSILIKLFTVSSMFPVDLPKLGRNDIESFLCENLSTIATLTPVLIKQFIAGAYEKYGDPVEFRRSFADFLIEMQVWGAEEENRLQQEEEQRRREEDIPGFAALSVKGPPPTPSFYP
Protein: Lipid phosphate phosphatase epsilon 1, chloroplastic (AtLPPE1) (EC 3.1.3.-) (Phosphatidic acid phosphatase epsilon 1) (Plastidic phosphatidic acid phosphatase epsilon 1) (F4J220)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits phosphatidate phosphatase (PAP) activity in vitro. May play a secondary role as PAP in plastids.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305|PubMed:17652095}; Multi-pass membrane protein {ECO:0000305|PubMed:17652095}.
Interaction partners:
- Lipid phosphate phosphatase gamma
- Phosphatidate phosphatase PAH1
- Phosphatidate phosphatase PAH2
- Lipid phosphate phosphatase 1
- Lipid phosphate phosphatase 2
- Probable carboxylesterase 16
- Triacylglycerol lipase SDP1L
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 14
- Phospholipase A1 PLIP2, chloroplastic
Sequence:
MAASSSLLLLLHCPTCNFYFDSSSYLKRSRLSSYSSIISRGSPLFVSSFGSMTVKRFSSRVGSRSNDGNEQFGALEQESFINNSSEIRKDLVTGGGIEAIVNRLSKWVVSVLFGSIILLRHDGAALWAVIGSISNSALSVVLKRILNQERPTTTLRSDPGMPSSHAQSISFISVFAVLSVMEWLGTNGVSLFLSGLILALGSYFIRLRVSQKLHTSSQVVVGAIVGSLFCILWYTMWNSLLREAFEASLLVQISVFLFAATFALAFAAYVVLNWFKDER
Protein: PHO85 cyclin-6 (P40038)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL7, controls glycogen phosphorylase and glycogen synthase activities in response to nutrient availablility. The PCL6-PHO85 cyclin-CDK holoenzyme has GLC8 kinase activity and phosphorylates and inactivates the phosphatase PP1-2 inhibitor GLC8, causing activation of PP1-2, which then dephosphorylates and activates glycogen phosphorylase. PCL6-PHO85 also phosphorylates YJL084C.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cyclin-dependent protein kinase PHO85
- PHO85 cyclin-8
- PHO85 cyclin-9
- Protein GLC8
- PHO85 cyclin-5
- PHO85 cyclin CLG1
- PHO85 cyclin-2
- Cyclin-dependent kinase 1
Sequence:
MSIKGDSPSSTNASSSPKSTYSIQSDDKANLGSGNVDIRTDNSQQDSNNRRDIVVVTRVASEETLESQSSTSSMGIRPESSFNYEDASNQARVEMNNRVHGSNMNTINKYYPVRFPKNNERQLSDTNNLNEKVQGTHTVQSSTQEDKILDGDTSNSQVTPSLNIAEFPTDKLLKMLTALLTKIIKSNDRTAATNPSLTQEIENGRCLALSDNEKKYLSPVLGFRGKHVPQIGLDQYFQRIQKYCPTTNDVFLSLLVYFDRISKRCNSVTTTPKTNTAKHESPSNESSLDKANRGADKMSACNSNENNENDDSDDENTGVQRDSRAHPQMFVMDSHNIHRLIIAGITVSTKFLSDFFYSNSRYSRVGGISLQELNHLELQFLVLCDFELLISVNELQRYADLLYRFWNNAKAQSQALVTGM
Protein: L-carnitine dehydrogenase (CDH) (L-CDH) (EC 1.1.1.108) (D7URM0)
Organism: Pseudomonas sp
Function: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-dehydrocarnitine. Is specific for L-carnitine and NAD(+) as substrates since D-carnitine, other carnitine analogs such as choline and betaine, and NADP(+) are not substrates. Despite a high similarity to 3-hydroxyacyl-CoA dehydrogenases, cannot dehydrogenate 3-hydroxybutylate and 3-hydroxybutyl-CoA. Is probably involved in a L-carnitine degradation pathway that allows Xanthomonas translucens to grow on L-carnitine as the sole source of carbon and nitrogen.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20530902}.
Interaction partners:
Sequence:
MPFITHIKTFAALGSGVIGSGWVARALAHGLDVIAWDPAPGAEQALRQRVANAWPALEKQGLAAGAAQHRLSFVSSIEECVRDADFIQESAPERLDLKLDLHAKISAAAKPDAIIASSTSGLLPSEFYESSSHPERCVVGHPFNPVYLLPLVEIVGGRHTAPEAIEAAKGIYTELGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGDAGMRHFMQQFGPALKLPWTYLPAPELTERLIDEVVDGTAAQVGERSIAELERYRDDTLLAVLEAIGTSKAKHGMTFSE
Protein: Glutamate--cysteine ligase regulatory subunit (GCS light chain) (Gamma-ECS regulatory subunit) (Gamma-glutamylcysteine synthetase regulatory subunit) (Glutamate--cysteine ligase modifier subunit) (O09172)
Organism: Mus musculus (Mouse)
Interaction partners:
- Glutamate--cysteine ligase catalytic subunit
- Glutathione synthetase
- Gamma-glutamylcyclotransferase
- Glutathione hydrolase 1 proenzyme
- Glutathione hydrolase 6
- 5-oxoprolinase
- Glutathione hydrolase 5 proenzyme
- Branched-chain-amino-acid aminotransferase, cytosolic
- NAD
- Glutathione hydrolase 7
Sequence:
MGTDSRAAGALLARASTLHLQTGNLLNWGRLRKKCPSTHSEELRDCIQKTLNEWSSQISPDLVREFPDVLECTMSHAVEKINPDEREEMKVSAKLFIVGSNSSSSTRSAVDMACSVLGVAQLDSVIMASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIEAQDWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS
Protein: Endoribonuclease Dicer (EC 3.1.26.3) (E9PU15)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- RISC-loading complex subunit TARBP2
- Protein argonaute-2
- Protein argonaute-1
- Interferon-inducible double-stranded RNA-dependent protein kinase activator A
- Microprocessor complex subunit DGCR8
- Protein argonaute-3
- Protein argonaute-4
- Trinucleotide repeat containing adaptor 6A
- Exportin-5
- Ribonuclease 3
Sequence:
MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELAHQIRGDLSPHAKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWSQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCDSCPSCPRILGLTASILNGKCDPDELEEKIQKLEKILKSGAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALDFINDCNVSVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTLLRKIHALCEEYFSPASLDLKYVTPKVMKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDDDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRSKQMEAEFRKQEEVLRKFRAHETNLLIATSVVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYVMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDGAEADVHAVVDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMGCVRLAERVVALICCEKLHKIGELDEHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRESYPKPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFTLSQQMLELVTRLHQYIFSHILRLEKPALEFQPAGAESAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYSKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISTCNSSLAESDNYCKHSTTVVPENAAHQGATRPSLENHDQMSVNCKRLPAESPAKLQSEVSVDLTAINGLSYNKSLANGSYDLVNRDFCQGNQLTYFKQEIPVQPTTSYPIQNLYNYENQPTPSNECPLLSNKYLDGNANTSTSDGSPAGSPRPAMMTAVEALEGRTDSEQSPSVGHSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKQGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNSEKWEKDEMTKDCLLANGKLGEDCEEEEEEELAWRAPKEEAEYEDDLLEYDQEHIQFIDSMLMGSGAFVKKIPLSPFSTSDSAYEWKMPKKASLGSVPFSSDLEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTSRDKASYPAQENSSSQQKSPSGSCAAAVSPRSSAGKDLEYGCLKIPPRCMFDHPDAEKTLNHLISGFENFEKKINYIFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLEVVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPLVPNS
Protein: Rhamnulose-1-phosphate aldolase (EC 4.1.2.19) (P32169)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. Also catalyzes the dephosphorylation of phospho-serine in vitro.
Subcellular location: Cytoplasm.
Interaction partners:
- L-Rhamnulokinase
- L-rhamnose isomerase
- L-fuculose phosphate aldolase
- L-rhamnose mutarotase
- Ribulokinase
- L-ribulose-5-phosphate 4-epimerase AraD
- Fructose-bisphosphate aldolase class 2
- Triosephosphate isomerase
- 2-keto-3-deoxy-L-rhamnonate aldolase
- Fructose-bisphosphate aldolase class 1
Sequence:
MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFHQQPRYIPLSQPMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGAGYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAVFTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVKVYSMGGMKQTISREELIALGKRFGVTPLASALAL
Protein: DEAD-box ATP-dependent RNA helicase 37 (EC 3.6.4.13) (Q84W89)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein STABILIZED1
- Cell division cycle 5-like protein
- Eukaryotic translation initiation factor 2 subunit alpha homolog
- Tetraspanin-8
- Polyadenylate-binding protein RBP47A
- Serine/arginine-rich SC35-like splicing factor SCL30
- Annexin D2
- Annexin D1
- 109 kDa U5 small nuclear ribonucleoprotein component GFL
- 110 kDa U5 small nuclear ribonucleoprotein component CLO
Sequence:
MSASWADVADSENTGSGSSNQNSHPSRPAYVPPHLRNRPAASEPVAPLPANDRVGYGGPPSGSRWAPGGSGVGVGGGGGYRADAGRPGSGSGYGGRGGGGWNNRSGGWDRREREVNPFENDDSEPEPAFTEQDNTVINFDAYEDIPIETSGDNVPPPVNTFAEIDLGEALNLNIRRCKYVKPTPVQRHAIPILLEGRDLMACAQTGSGKTAAFCFPIISGIMKDQHVQRPRGSRTVYPLAVILSPTRELASQIHDEAKKFSYQTGVKVVVAYGGTPINQQLRELERGVDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMDMPPRGVRQTLLFSATFPREIQRLAADFLANYIFLAVGRVGSSTDLIVQRVEFVLDSDKRSHLMDLLHAQRENGIQGKQALTLVFVETKRGADSLENWLCINGFPATSIHGDRTQQEREVALKAFKSGRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFFNDGNTSLARPLAELMQEANQEVPEWLTRYASRSSFGGGKNRRSGGRFGGRDFRREGSFGSGRGGYGGGGGGYGGGGGYGGGGGYGGGGGYGGGYGGASSGGYGGEPPSAWD
Protein: Glycine--tRNA ligase 2 (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Ap4A synthetase) (EC 2.7.7.-) (Glycyl-tRNA synthetase 2) (GlyRS 2) (GlyRS2) (Q06817)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Glycine--tRNA ligase 1, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, mitochondrial
- Lysine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, mitochondrial
- Lysine--tRNA ligase, mitochondrial
- DNA polymerase gamma
- Leucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, mitochondrial
- Valine--tRNA ligase, mitochondrial
Sequence:
MPLMSNSERDKLESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFIMEENMLQVDGPMLTPYDVLKTSGHVDKFTDWMCRNPKTGEYYRADHLIEQTLKKRLLDKDVNPQDMKNMEKILTTIDGFSGPELNLVMQEYNINDPVTNDVLDALTSFNLMFETKIGASGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLMAEIEHFVDPLNKSHAKFNEVLNEEIPLLSRRLQESGEVQLPVKMTIGEAVNSGMVENETLGYFMARVHQFLLNIGINKDKFRFRQHLKNEMAHYATDCWDGEILTSYGWIECVGCADRAAFDLTVHSKKTGRSLTVKQKLDTPKERTEWVVEVNKKFFGSKFKQKAKLIESVLSKFSQDELIRRHEELEKNGEFTCQVNGQIVKLDSSLVTIKMKTTLQHIREYIPNVIEPSFGLGRIIYCIFDHCFQVRVDSESRGFFSFPLQIAPIKVFVTTISNNDGFPAILKRISQALRKREIYFKIDDSNTSIGKKYARNDELGTPFGITIDFETIKDQTVTLRERNSMRQVRGTITDVISTIDKMLHNPDESDWDKSTFGLSPVKI
Protein: Aquaporin PIP2-1 (Plasma membrane intrinsic protein 2-1) (ZmPIP2-1) (ZmPIP2;1) (Q84RL7)
Organism: Zea mays (Maize)
Function: Water channel required to facilitate the transport of water across cell membrane. Active as homomers. Increased activity when heteromerization with PIP1-2.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MGKDDVIESGAGGGEFAAKDYTDPPPAPLIDAAELGSWSLYRAVIAEFIATLLFLYITVATVIGYKHQTDASASGADAACGGVGVLGIAWAFGGMIFVLVYCTAGISGGHINPAVTFGLFLARKVSLVRALLYIVAQCLGAICGVGLVKAFQSAYFDRYGGGANSLASGYSRGTGLGAEIIGTFVLVYTVFSATDPKRNARDSHVPVLAPLPIGFAVFMVHLATIPVTGTGINPARSLGAAVIYNKDKPWDDHWIFWVGPLVGAAIAAFYHQYILRAGAIKALGSFRSNA
Protein: Small ribosomal subunit protein uS14 (40S ribosomal protein S29) (Q6Q419)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Ribosomal protein L3
- Ribosomal protein L4
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein eL27
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein uL10
- 40S ribosomal protein S24
- 60S ribosomal protein L37a
Sequence:
MGHQQLYWSHPRKYGQGSRSCRVCSNRHGLIRKYGLNMCRQCFRQYAKDIGFVKLD
Protein: LD17515p (Q95RP6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPESLADHVYTSKSDVWSFGVLCWELITLGASPYPGIAPQNLWSLLKTGYRMDRPENCSEAVYSIVRTCWADEPNGRPSFKFLASEFEKLLGNNAKYIDLETNAVSNPLYCGDDSALITTELGEPESLQHLWSPPKIAYDIHDQATSYDQSEEEMPVTSTAPPGYDLPRPLLDATANGQVLRYENDLRFPLNIRKSSCTPSYSNMTSEPPATTSLPHYSVPVKRGRSYLDMTNKSLIPDNLDSREFEKHLSKTISFRFSSLLNLSETKEVSPGWQAEDAV
Protein: Small ribosomal subunit protein uS3 (C3SQX2)
Organism: Escherichia coli
Interaction partners:
- GTP pyrophosphokinase
- Small ribosomal subunit protein uS17
- Alternative ribosome-rescue factor A
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL2
- 50S ribosomal protein L16
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS7
- 50S ribosomal protein L11
Sequence:
MGQKVHPNGIRLGIVKPWNSTWFANTKEFADNLDSDFKVRQYLTKELAKASVSRIVIERPAKSIRVTIHTARPGIVIGKKGEDVEKLRKVVADIAGVPAQINIAEVRKPELDAKLVADSITSQLERRVMFRRAMKRAVQNAMRLGAKGIKVEVSGRLGGAEIARTEWYREGRVPLHTLRADIDYNTSEAHTTYGVIGVKVWIFKGEILGGMAAVEQPEKPAAQPKKQQRKGRK
Protein: Prohibitin 1 (B-cell receptor-associated protein 32) (BAP 32) (P67778)
Organism: Mus musculus (Mouse)
Function: Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors in the nucleus. Plays a role in adipose tissue and glucose homeostasis in a sex-specific manner. Contributes to pulmonary vascular remodeling by accelerating proliferation of pulmonary arterial smooth muscle cells (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:29324904}. Nucleus {ECO:0000269|PubMed:20959514}. Cell membrane {ECO:0000305|PubMed:29324904}. Cytoplasm {ECO:0000269|PubMed:29324904}.
Interaction partners:
- Prohibitin-2
- Stomatin-like protein 2, mitochondrial
- Stomatin
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Stress-70 protein, mitochondrial
- 60 kDa heat shock protein, mitochondrial
- RAF proto-oncogene serine/threonine-protein kinase
- Mitochondrial import inner membrane translocase subunit TIM14
- Mitochondrial inner membrane protease ATP23 homolog
Sequence:
MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIYTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ
Protein: Falcilysin (EC 3.4.24.-) (A0A0L7KF24)
Organism: Plasmodium falciparum (isolate HB3)
Function: In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains. In the apicoplast, degrades apicoplast transit peptides after their cleavage (By similarity). Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH. At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg. At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions. The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:10542284}; Peripheral membrane protein {ECO:0000269|PubMed:12876284}. Plastid, apicoplast {ECO:0000250|UniProtKB:Q76NL8}. Vesicle {ECO:0000269|PubMed:12876284}. Note=Localizes to the food (or digestive) vacuole, an acidic vacuole where host hemoglobin is digested (PubMed:10542284, PubMed:12876284). During the trophozoite and early to mid-schizont stages, localizes to the apicoplast (By similarity). {ECO:0000250|UniProtKB:Q76NL8, ECO:0000269|PubMed:10542284, ECO:0000269|PubMed:12876284}.
Interaction partners:
Sequence:
MNLTKLMKVFGYINIITNCVQSFTNRADKKRYNVFAKSFINTINTNLYTFKAVMSKTPEWIHEKSPKHNSYDIIEKRYNEEFKMTYTVYQHKKAKTQVISLGTNDPLDVEQAFAFYVKTLTHSGKGIPHILEHSVLSGSKNYNYKNSIGLLEKGTLHTHLNAYTFNDRTVYMAGSMNNKDFFNIMGVYMDSVFQPNVLENKYIFETEGWTYEVEKLKEDEKGKAEIPQMKDYKVSFNGIVYNEMKGALSSPLEDLYHEEMKYMFPDNVHSNNSGGDPKEITNLTYEEFKEFYYKNYNPKKVKVFFFSKNNPTELLNFVDQYLGQLDYSKYRDDAVESVEYQTYKKGPFYIKKKYGDHSEEKENLVSVAWLLNPKVDKTNNHNNNHSNNQSSENNGYSNGSHSSDLSLENPTDYFVLLIINNLLIHTPESVLYKALTDCGLGNNVIDRGLNDSLVQYIFSIGLKGIKRNNEKIKIFDKVHYEVEDVIMNALKKVVKEGFNKSAVEASINNIEFILKEANLKTSKSIDFVFEMTSKLNYNRDPLLIFEFEKYLNIVKNKIKNEPMYLEKFVEKHFINNAHRSVILLEGDENYAQEQENLEKQELKKRIENFNEQEKEQVIKNFEELSKYKNAEESPEHLNKFPIISISDLNKKTLEVPVNVYFTNINENNNIMETYNKLKTNEHMLKDNMDVFLKKYVLKNDKHNTNNNNNNNNNMDYSFTETKYEGNVPILVYEMPTTGIVYLQFVFSLDHLTVDELAYLNLFKTLILENKTNKRSSEDFVILREKNIGSMSANVALYSKDDHLNVTDKYNAQALFNLEMHVLSHKCNDALNIALEAVKESDFSNKKKVIDILKRKINGMKTTFSEKGYAILMKYVKAHLNSKHYAHNIIYGYENYLKLQEQLELAENDFKTLENILVRIRNKIFNKKNLMVSVTSDYGALKHLFVNSNESLKNLVSYFEENDKYINDMQNKVNDPTVMGWNEEIKSKKLFDEEKVKKEFFVLPTFVNSVSMSGILFKPGEYLDPSFTVIVAALKNSYLWDTVRGLNGAYGVFADIEYDGSVVFLSARDPNLEKTLATFRESAKGLRKMADTMTENDLLRYIINTIGTIDKPRRGIELSKLSFLRLISNESEQDRVEFRKRIMNTKKEDFYKFADLLESKVNEFEKNIVIITTKEKANEYIANVDGEFKKVLIE