wanglab/gogpt-training-data huggingface dataset:
Protein: Carnitine O-palmitoyltransferase 2, mitochondrial (EC 2.3.1.21) (Carnitine palmitoyltransferase II) (CPT II) (P52825)
Organism: Mus musculus (Mouse)
Function: Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites. Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Mitochondrial carnitine/acylcarnitine carrier protein
- Carnitine O-palmitoyltransferase 1, liver isoform
- Peroxisomal acyl-coenzyme A oxidase 3
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Palmitoyl thioesterase CPT1C
- 3-ketoacyl-CoA thiolase, mitochondrial
Sequence:
MMPRLLLRDWPRCPSLVLGAPSRPLSAVSGPAEYLQHSIVPTMHYQDSLPRLPIPKLEDTMKRYLSAQKPLLNDSQFRKTEVLCKDFENGIGKELHAHLLAQDKQNKHTSYISGPWFDMYLTARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNLTVSAVRFLKTLRAGLLEPEVFHLNPARSDTDAFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRIPKPSRDELFTDTKARHLLVLRKGHFYVFDVLDQDGNIVNPSEIQAHLKYILSDSSPVPEFPLAYLTSENRDVWAELRQKLIHGGNEETLRKVDSAVFCLCLDDFPMKDLVHLSHTMLHGDGTNRWFDKSFNLIVAKDGTAAVHFEHAWGDGVAVLRFFNEVFRDSTQTPAIAPQSQPAATDSSVSVQKLSFKLSSALKAGVTAAKEKFDATMKTLTIDAIQFQRGGKEFLKKKKLSPDAVAQLAFQMAFLRQYGQTVATYESCSTAAFKHGRTETIRPASIFTKRCSEAFVREPSKHSVGELQHMMAECSKYHGQLTKEAAMGQGFDRHLFALRYLAAARGVTLPELYQDPAYQRINHNILSTSTLSSPAVSLGGFAPVVPDGFGIAYAVHDDWIGCNVSSYSGRNAREFLHCVQKCLEDMFDALEGKAIKT
Protein: Circadian clock protein PASD1 (Cancer/testis antigen 63) (CT63) (OX-TES-1) (PAS domain-containing protein 1) (Q8IV76)
Organism: Homo sapiens (Human)
Function: Functions as a suppressor of the biological clock that drives the daily circadian rhythms of cells throughout the body. Acts as a nuclear repressor of the CLOCK-BMAL1 heterodimer-mediated transcriptional activation of the core clock components. Inhibits circadian clock function in cancer cells, when overexpressed.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:25936801}. Note=Associates preferentially at the periphery of the nucleus with heterochromatin (PubMed:25936801). {ECO:0000269|PubMed:25936801}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:25936801}. Note=Associates preferentially at the periphery of the nucleus with heterochromatin (PubMed:25936801). {ECO:0000269|PubMed:25936801}.
Interaction partners:
- Basic helix-loop-helix ARNT-like protein 1
- Basic helix-loop-helix ARNT-like protein 2
- Melanoma-associated antigen 10
Sequence:
MKMRGEKRRDKVNPKSSQRKLNWIPSFPTYDYFNQVTLQLLDGFMITLSTDGVIICVAENISSLLGHLPAEIVGKKLLSLLPDEEKDEVYQKIILKFPLLNSETHIEFCCHLKRGNVEHGDSSAYENVKFIVNVRDICNEFPVVFSGLFSSHLCADFAACVPQEDRLYLVGNVCILRTQLLQQLYTSKAVSDEAVLTQDSDEEPFVGELSSSQGQRGHTSMKAVYVEPAAAAAAAAISDDQIDIAEVEQYGPQENVHMFVDSDSTYCSSTVFLDTMPESPALSLQDFRGEPEVNPLYRADPVDLEFSVDQVDSVDQEGPMDQQDPENPVAPLDQAGLMDPVDPEDSVDLGAAGASAQPLQPSSPVAYDIISQELELMKKLKEQLEERTWLLHDAIQNQQNALELMMDHLQKQPNTLRHVVIPDLQSSEAVPKKQQKQHAGQVKRPLPHPKDVKCFCGLSLSNSLKNTGELQEPCVAFNQQQLVQQEQHLKEQQRQLREQLQQLREQRKVQKQKKMQEKKKLQEQKMQEKKKLQEQRRQKKKKLQERKKWQGQMLQKEPEEEQQKQQLQEQPLKHNVIVGNERVQICLQNPRDVSVPLCNHPVRFLQAQPIVPVQRAAEQQPSGFYQDENCGQQEDESQSFYPEAYQGPPVNQLPLIDTSNSEAISSSSIPQFPITSDSTISTLETPQDYIRLWQELSDSLGPVVQVNTWSCDEQGTLHGQPTYHQVQVSEVGVEGPPDPQAFQGPAAYQPDQMRSAEQTRLMPAEQRDSNKPC
Protein: Isopentenyl-diphosphate Delta-isomerase 1 (EC 5.3.3.2) (Isopentenyl pyrophosphate isomerase 1) (IPP isomerase 1) (IPPI1) (P58044)
Organism: Mus musculus (Mouse)
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:O35586}.
Interaction partners:
- Diphosphomevalonate decarboxylase
- Farnesyl pyrophosphate synthase
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Geranylgeranyl pyrophosphate synthase
- Squalene monooxygenase
- Lanosterol synthase
- Lanosterol 14-alpha demethylase
- Methylsterol monooxygenase 1
- Squalene synthase
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Sequence:
MPEINTSHLDEKQVQLLAEMCILIDENDNKIGADTKKNCHLNENIDKGLLHRAFSVFLFNTENKLLLQQRSDAKITFPGCFTNSCCSHPLSNPGELEENNAIGVKRAAKRRLKAELGIPLEEVDLNEMDYLTRIYYKAQSDGIWGEHEVDYILFLRKNVTLNPDPNEIKSYCYVSKEEVREILKKAASGEIKLTPWFKIIADTFLFKWWDNLNHLSPFVDHEKIHRL
Protein: 25S rRNA (cytosine-C(5))-methyltransferase nop2 (EC 2.1.1.-) (Nucleolar protein 2) (O94268)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of a cytosine in 25S rRNA. Required for 60S ribosomal subunit synthesis and processing (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Probable nucleolar GTP-binding protein 1
- 60S ribosome subunit biogenesis protein nip7
- GTPase grn1
- AdoMet-dependent rRNA methyltransferase spb1
- Probable rRNA-processing protein ebp2
- Uncharacterized RNA-binding protein C1827.05c
- Ribosome biogenesis protein erb1
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein rlp24
- Ribosome biogenesis protein brx1
Sequence:
MGRKQKSKQGIPPTLEENHNSSHKVTENAKKRKHSKEKPQNSRKRQLAEEKKSLFENSDSENEKDLIDADEFEEAETLSDLEHDEEPQTFADEFIDDEAKECEGEEEDSVFDSDEEHEVKPMFSDDSGDEEDLELANMEAMSRKLDEEAELEEKEAEEELHTNIHPEAPTVLPPIDGFTDSQPISTLPQDLSQIQLRIQEIVRVLNDFKNLCEPGRNRSEYVDQLLNDICAYYGYSRFLAEKLFELFSVSEAVEFFEANEMPRPVTIRTNTLKTQRRELAQALINRGVNLEPIGKWSKVGLQVFESQVPIGATPEYLAGHYILQAASSFLPVMALAPQPNERILDMSSAPGGKVTYVAALQKNTGIIFANDSNKARTKALSANIHRLGVRNAIVCNYDGRKFPNEVIGGFDRVLLDAPCSGTGVIYKDQSVKTNKSERDFDTLSHLQRQLLLSAIDSVNADSKTGGFIVYSTCSITVDEDEAVIQYALKKRPNVKLVSTGLEFGREGFTRFREKRFHPSLKLTRRYYPHVHNIDGFFVAKLKKISDKIPTVNVADDMKDGTNNDVEIEKNSTEIDNITFNDEADKEIIEQNRRKWLKSKGYKVAKKKD
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (D4A2D5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Tyrosine-protein kinase CSK
- Tyrosine-protein kinase
- Tyrosine-protein kinase
- T-cell surface glycoprotein CD4
- Proline-serine-threonine phosphatase-interacting protein 1
- Proto-oncogene tyrosine-protein kinase LCK
- T-cell surface glycoprotein CD3 zeta chain
- Glycerophosphodiester phosphodiesterase 1
- Interleukin-2 receptor subunit alpha
- Cytotoxic T-lymphocyte protein 4
Sequence:
MDQREILQQLLKEAQKKKINREEFANEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELFKRHVDIISDNHREREIQAECSIPEQKLTIEADSYPLDFPKNAVRDAKMTNQQSKQGAEAESTEVSSFGLRTSKISAKEELVLHSKSSPSFDCLELNCECNKAVITRNGQARASLVVGEPLQKYQSLDFGSILFGSCPSALPINTASRCHNSKGPVKRTKSTPFELIQQRKTNELAVEDGSSCLESQLLEHGLMELQAQKVAHASSEELNYSLPRACERPACDASCVPQDGPGALREHLCMSLAEDPYFSSSPPNSAGSKMSFDLPEKQDGATSPGAQLPASSAASSSYSNPRDSLMESTLTSFPPPINQETAIEATSARTDDEIPPPLPERTPESFIVAEAAGEPSPSITESLPLAGKSGVTLECGGTSESQSHDLVAFTSSKNVELGSPKSDQHQDGSPPPPLPERTLESFFLADEDCIQAQPMKPSSISYPETTEISTSSKQTLKTPGKSFTRSKSLKIFRNMKKSVCNSPSPSKPTECVQPKNSSSFLNFGFGTRFSKPKGPRNPPSTWNI
Protein: IP01061p (RH36186p) (Q9VSX2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP07647p
Sequence:
MSLVPTTYRDLSREFDRLRPLYHPPYDFQLYPYLWDDSRLWWPSPHTSRSDLLRPLDELVSRRVRNQLIQSTPYEWAHPMRWDNYYSGERVHVDEKGFRIDIDVRQFHPHDIVVKTNDDYVIVQGNHNRRDEGSNGLVERHFVRKYLLPRGYNANEVISDISSDGILTIKAPPPPPAKYYTPGERLVRVHETGKLALPWK
Protein: Nicotinic acetylcholine receptor alpha4, isoform H (A0A0S0WNY8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MVHGAVAGNPDAKRLYDDLLSNYNKLVRPVVNTTDVLKVCIKLKLSQLIDVNLKNQIMTTNLWVEQSWYDYKLRWEPKEYGGVHMLHVPSDHIWRPDIVLYNNADGHYEVTLMTKAIVYNNGLVIWQPPAVYKSSCSIDVEYFPYDVQTCILKLGSWTYDGFKVDLRHMDEQQGSNVVAVGVDLSEFYMSVEWDILEVPAVRNEKFYTCCDEPYLDITFNITMRRKTLFYTVNIIIPCMGISFLTVLTFYLPSDSGEKVTLSISILISLHVFFLLVVEIIPPTSLVVPLLGKYLIFAMILVSISICVTVVVLNVHFRSPQTHKMAPWVKRVFIDFLPAFLFIKRPTYNFETSKLLLKDTHACFYPYYSATNIDRLVSSGYNNSLPKEDLSQSITANGPFGGSCQVHGPVPPLTHCSSDEIAAVPDMDIGPLGMKSPILNNPAFSHSKCLPKIHKSCFCVRFIAEHTKMQEDSTKVKEDWKYVAMVLDRLFLWIFTLAVVVGTAGIILQAPTLYDDRIPIIEQKDLDFSGTSAGRCRPPQ
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform B) (Q9VAT8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Accessory gland protein Acp29AB
- Aquarius
- Accessory gland-specific peptide 26Aa
- Accessory gland protein Acp36DE
- Lectin-46Ca
- Serpin 28F
- AT03573p
- Uncharacterized protein, isoform B
- Accessory gland protein Acp62F
- Seminal metalloprotease 1
Sequence:
MLRPLCIIQILLLAFLANESESSNTHLHRYMLDTYKPQHNRKTQMNYKRRRTVRSDHEMAIDPNNPNNPNNPNNSDSPDNPNNLNNPNNPNNDTVQYGHSKEPVVTLTNSDKKVPLHELMVRLYQQNKYICMGTVISEMLVITTSTCFNLASSEVVTMKMYDDEVLEGKRVALNQTYLKGADPMLVAIQLTKSPKNSKVTGDTVKLCDSELEIYEPIELPLWIRSRHSIHSQTTYIIPMQACRLRMRDPEAMVATDTMICVKNMKYTAQCQLAMGNPLVHDERICGINVAGHNCPAYTGVDLYIRVYDALAFSIMGMEIIKNSRIEDTIL
Protein: Fumarate hydratase, mitochondrial (Fumarase) (EC 4.2.1.2) (O94552)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. In mitochondrion, catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH. In cytoplasm and nucleus, involved in DNA repair in response to DNA damage: following DNA double-strand breaks (DSBs), translocates from the cytosol to the nucleus and promotes DNA repair by catalyzing the dehydration of L-malate to fumarate.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P08417}. Cytoplasm {ECO:0000250|UniProtKB:P08417}. Nucleus {ECO:0000250|UniProtKB:P08417}. Note=Translocates from the cytosol to the nucleus in response to DNA damage. {ECO:0000250|UniProtKB:P08417}.
Interaction partners:
- Probable succinate dehydrogenase flavoprotein subunit, mitochondrial
- Malate dehydrogenase, mitochondrial
- Succinate dehydrogenase cytochrome B subunit
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- NAD-dependent malic enzyme
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- NAD-dependent malic enzyme
- Probable citrate synthase, mitochondrial
- Aspartate aminotransferase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
Sequence:
MASVAHISTAKAIFRAGGLPCRRLITPTLTGLPLKTHRMNSTTPTYHLIPKGGKHGEFRQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEKERLPLPLVRAFGVLKRAAASVNREFGLDPKLADAIEQAAQEVIDGRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGFDVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIMPGKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHLRDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMISAKKV
Protein: Thrombopoietin (P49745)
Organism: Rattus norvegicus (Rat)
Function: Lineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P40225}.
Interaction partners:
- Thrombopoietin receptor
- Erythropoietin
- Granulocyte colony-stimulating factor
- Leptin
- Kit ligand
- Prolactin
- Prolactin-6A1
- Interleukin-3
- Ciliary neurotrophic factor
- Erythropoietin receptor
Sequence:
MELTDLLLVAILLLTARLTLSSPVPPACDPRLLNKLLRDSYLLHSRLSQCPDVNPLSIPVLLPAVDFSLGEWKTQTEQSKAQDILGAVSLLLEGVMAARGQLEPSCLSSLLGQLSGQVRLLLGALQGLLGTQLPPQGRTTAHKDPSALFLSLQQLLRGKVRFLLLVEGPALCVRRTLPTTAVPSRTSQLLTLNKFPNRTSGLLETNFSVVARTAGPGLLNRLQGFRAKIIPGQLNQTSGSLDQIPGYLNGTHEPVNGTHGLFAGTSLQTLEAPDVVPGAFNKGSLPLNLQSGLPPIPSLAADGYTLFPPSPTFPTPGSPPQLPPVS
Protein: BTB domain-containing protein (Q18097)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSLSELSVLSAETAISFHEMDLEILKESQKALREEAGGKEEVEETVENPNPIVFIAVDDQNLPNGEEEDSFIFEKLQFRVKQVMENGTRRVYLSVQATTPAEWQLLVQLRIKTGCQSNILNVVDKDVYKFDSFSYPLNVEIQNSDVKFLKFEMRVLNLMYLDLPTFEEGDEVIEFDDGSRIRVHSNILSLLSDYLGKSEKEYASRTDCPAIKATCSEKEAFLELLYQAYPTRRPIFASFRRLTAGAVGYKCDNLIYQLSKHLIDYNYRPMTFLQRFQAAIENRLEPAISELAFRAALDGTWNQMIQSGFEPENFCGRQVYTKIVCPAILLARNAKPDATTLKKPENNLKFIELEEGDTTKSAILFRGTIFYINSGILAAHGKEMLCIGQNGEYIARYTAEFHRECARGDLIPGEVLVQLLTYMHPMGEVPHPDMIRACIVFAFDHGWNIVKENLENEFEPPITPDEYMSQLMFGDKFDLKNLLRVNIQRAESSCRELAEVLERHGKLKILKDRTHEGIMDRMCSGWGLNPMVNRLSTRFPTTFHHRTVNLQRGKAVVVGEGRAVDTLNSLASDHAFGEPTELIVVD
Protein: HL05789p (Q5U0W6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQVPSSRQVLCSREPLYSQPLIGVEKTMRGHMPFRKYLSSEFGVADTQINRKTTLDNPAILEQQLEALAYHKLQMEKKGLLGVQAKPTQPLNSFTKPLSKTLSKSLIYSNLGSVRKEIETLELLTDETKISASTYSNVNETAMDSSHSSTQKMLSVCTNFISDNEKDELPPPPSPESAVSSSYSELRHATLEFNKPIDYLQNNQTTNPLQIYANQYAMQHDATGKSSSTYDSIYEPINPRPCVADTLPRESYNLHNSYVNDNNPNISHEYNISNSIEANQTLYIHGNARTTFYDVNSIHRNDKEGLKNYISIPTEPVQELENYGRCVKCNSRVLGESSGCTAMDQIYHIFCFTCTDCQINLQGKPFYALDGKPYCEYDYLQTLEKCSVCMEPILERILRATGKPYHPQCFTCVVCGKSLDGLLFTVDATNQNYCITDFHKKFAPRCCVCKQPIMPDPGQEETIRVVALDRSFHLECYKCEDCGLLLSSEAEGRGCYPLDDHVLCKSCNAKKGSGFNKPHDVRTLN
Protein: Dynein light chain 1, cytoplasmic (8 kDa dynein light chain) (Cut up protein) (Q24117)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a non-catalytic accessory component of a dynein complex.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8628263}.
Interaction partners:
- Cytoplasmic dynein 1 intermediate chain
- Dynein light chain Tctex-type
- Protein swallow
- Sperm-specific dynein intermediate chain 1, isoform A
- Sperm-specific dynein intermediate chain 2, isoform A
- GH16657p
- FI21737p1
- Dynein heavy chain, cytoplasmic
- Dynein light chain 2, cytoplasmic
- Dynein light intermediate chain
Sequence:
MSDRKAVIKNADMSEEMQQDAVDCATQALEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETRHFIYFYLGQVAILLFKSG
Protein: 3-methylcrotonyl-CoA carboxylase, putative (Q57YQ4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- methylcrotonoyl-CoA carboxylase
- Biotin--acetyl-CoA-carboxylase ligase, putative
- Isovaleryl-coA dehydrogenase, putative
- Methylglutaconyl-CoA hydratase, mitochondrial, putative
- Probable enoyl-CoA hydratase, mitochondrial
- hydroxymethylglutaryl-CoA lyase
- DNA-directed RNA polymerase subunit beta
- beta-ketoacyl-[acyl-carrier-protein] synthase I
- Plastid-encoded RNA polymerase subunit alpha
- Spt4/RpoE2 zinc finger domain-containing protein
Sequence:
MLRYNVFYHGDFKKVLVANRGEIACRVFRTCREMNIRTVAVCCEGEPNAKHVLEADEAFVLGPPPASTSYLRGDRIICAAKKLQADAVHPGYGFLSENAEFASAVLAAGLKFVGPPPAAMLSMGSKSESKRIMEAAGVPIVPGYYGEDQNPDRLLHEAKTIGFPVLIKAVSGGGGKGMKIVMEETEFHLMLESAKREAINFFKDDRVILERYVMHPRHIECQIFFDSFGNGVFFFERDCSVQRRHQKVIEEAPAPGLSVDMRRRIGDVALTAARAVGYVGAGTVEFIFDTEKDEFFFMEMNTRLQVEHPVTEQVCQVRGRPLDLVRLQLQTAMGLPLGFRQEDISMSGASVEARIYAESPRNGFLPVGGRLRYLKEPPQGNRGTVKVRLDTGFRAGDDVLVHYDPMIAKLVVWGDNRATALEGLRTALASYHIVGVETNIDFLQCCLSNPGFVEGGVTTRFIEDNSVNLLQPREIPNNVLALAAVSYLCSQRGTSTLFWPNRQISQGVCFTVGGNPVVVRVTVSTKMCFTCDFDSSSVTVYVESTTNMPDSSTFIRVTVDGETRFGFTSFVTDSEVAVALPQGFYTLALQPLATDFGSTSAQANGSASVLSPMPGKVTKLLVADGTLVQQGQAILILEAMKMEHVVKASCDGEVKFCVHADGIVGGSTLLAHIASAAV
Protein: Probable protein phosphatase 2C 21 (AtPP2C21) (EC 3.1.3.16) (AtPPC4;2) (O81716)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein SMALL AUXIN UP-REGULATED RNA 9
- Auxin-responsive protein SAUR19
Sequence:
MGTYLSSPKTEKLSEDGENDKLRFGLSSMQGWRATMEDAHAAILDLDDKTSFFGVYDGHGGKVVAKFCAKYLHQQVISNEAYKTGDVETSLRRAFFRMDDMMQGQRGWRELAVLGDKMNKFSGMIEGFIWSPRSGDTNNQPDSWPLEDGPHSDFTGPTSGCTACVALIKDKKLFVANAGDSRCVISRKSQAYNLSKDHKPDLEVEKERILKAGGFIHAGRINGSLNLTRAIGDMEFKQNKFLPSEKQMVTADPDINTIDLCDDDDFLVVACDGIWDCMSSQELVDFIHEQLKSETKLSTVCEKVVDRCLAPDTATGEGCDNMTIILVQFKKPNPSETEPEDSKPEPSEDEPSSSS
Protein: Protein leg1a (Leg1-A) (Liver-enriched gene protein 1-A) (A5PF61)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Important for early development of liver, exocrine pancreas and intestine, probably through cell cycle regulation. In liver, its function is partially redundant with leg1b function.
Subcellular location: Secreted {ECO:0000269|PubMed:21857963}.
Interaction partners:
- Microtubule cross-linking factor 3
- Acyl-CoA thioesterase 17
- Baculoviral IAP repeat-containing 5a.
Sequence:
MSEMGFLRSVAAVLLLAVFSHAAVVTENGLPIQWGKAPSDLSHLPISDTGVQVNPWDYSQRMTMYKMLINATNAYMSSMGPGEQENPLWSLPLQLGWKLKSGRLADPTLDSSSTCGSEASDPVCISPLSWFACVNYYLSVLPFLAAVETGVVSSGGHQVLIQVPAEVAQDYCSSYSDCSTKHPNAMAKWHLFFQSLRQVSQSEDSDFNKKDSILGLMWAAEEESLQTASGACTERQKLYSSPEVSFQQSWLNSAAFVSAAHFHANIERSEKFMAPLPSRVLQEADSPPNIADLSTEENHTLYIFGWMNSVNQLLGGSLVNLWRKAMCSAQAREKGQALLHDLILDPKFPGSSLWSILSEMSTSC
Protein: Syncrip, isoform E (Q8IN48)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLSQMEASKVQKDEGGGEALSRTILKTPSSFRTPSPIPSCSKMAEGNGELLDDINQKADDRGDGERTEDYPKLLEYGLDKKVAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLDNHEIKPGKCLKINISVPNLRLFVGNIPKSKGKDEILEEFGKLTAGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGNLSPTHPSIMSLTPMRPGARMPLRTPIPREYVVGKRKFDGGHQNPADVKRRYPSGLIGNGGSWGSLPLPQQPLGTNGEQWYMDTFSAWS
Protein: Type I interferon 1 (Q70I18)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MQSVCHCCDWIRHHYGHLSAEYLPLLDQMGGDITKQNAPVLFPTSLYRHIDDAEFEDKVIFLKETIYQITKLFDGNMKSATWDKKNLDDFLNILERQLENLNSCVSPAMKPERRLKRYFKKLNSKVLRKMNYSAQAWELIGKETKRNLQRLDILAAQMY
Protein: Ly49H (Q49U25)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
METQMSEQDVTLPTMRFHKSSGLNSQVRLEGTQRSRKAGLIVCSVPWQLIVIALGILCSLRLVIVAVFVTKIFQYSQHKQEINETLNHHHNCSNMQSDIKLKEEMSTTESIDCRPSNELLEYIKREQERWNSETKTVLDSSRDTGRGVKYWFCYGTKCYYFIMNKTTWNGCKANCQHYSFPIVKIEAEDELKFLQRHVIPESYWIGLSYDKKKKEWAWIDNGQSKLDMKRKMNFTSRGCVF
Protein: N-acetylglutamate synthase, mitochondrial (EC 2.3.1.1) (Amino-acid acetyltransferase) [Cleaved into: N-acetylglutamate synthase long form; N-acetylglutamate synthase short form; N-acetylglutamate synthase conserved domain form] (Q8N159)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of ureagenesis by producing the essential cofactor N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (CPS1) activity.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:7126172}.
Interaction partners:
- Ornithine aminotransferase, mitochondrial
- Argininosuccinate synthase
- Argininosuccinate lyase
- Ornithine transcarbamylase, mitochondrial
- Argininosuccinate lyase
- Glutamate dehydrogenase 1, mitochondrial
- Glutamate dehydrogenase 2, mitochondrial
- Alanine aminotransferase 2
- Alanine aminotransferase 1
- Aspartate aminotransferase, mitochondrial
Sequence:
MATALMAVVLRAAAVAPRLRGRGGTGGARRLSCGARRRAARGTSPGRRLSTAWSQPQPPPEEYAGADDVSQSPVAEEPSWVPSPRPPVPHESPEPPSGRSLVQRDIQAFLNQCGASPGEARHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAPTAPSGCLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPRLHSIYVSEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHKPASDPGS
Protein: 2-oxoisovalerate dehydrogenase subunit alpha (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDH E1-alpha) (Q5SLR4)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Interaction partners:
Sequence:
MVKETHRFETFTEEPIRLIGEEGEWLGDFPLDLEGEKLRRLYRDMLAARMLDERYTILIRTGKTSFIAPAAGHEAAQVAIAHAIRPGFDWVFPYYRDHGLALALGIPLKELLGQMLATKADPNKGRQMPEHPGSKALNFFTVASPIASHVPPAAGAAISMKLLRTGQVAVCTFGDGATSEGDWYAGINFAAVQGAPAVFIAENNFYAISVDYRHQTHSPTIADKAHAFGIPGYLVDGMDVLASYYVVKEAVERARRGEGPSLVELRVYRYGPHSSADDDSRYRPKEEVAFWRKKDPIPRFRRFLEARGLWNEEWEEDVREEIRAELERGLKEAEEAGPVPPEWMFEDVFAEKPWHLLRQEALLKEEL
Protein: Pre-rRNA-processing protein TSR1 homolog (Q2NL82)
Organism: Homo sapiens (Human)
Function: Required during maturation of the 40S ribosomal subunit in the nucleolus.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Protein LTV1 homolog
- RNA-binding protein NOB1
- Serine/threonine-protein kinase RIO2
- RRP12-like protein
- Dimethyladenosine transferase
- Bystin
- RNA-binding protein PNO1
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS19
Sequence:
MAAHRPGPLKQQNKAHKGGRHRGRGSAQRDGKGRLALKTLSKKVRKELSRVDQRHRASQLRKQKKEAVLAEKRQLGGKDGPPHQVLVVPLHSRISLPEAMQLLQDRDTGTVHLNELGNTQNFMLLCPRLKHRWFFTSARPGDLHVVLDMAKVADTILFLLDPLEGWDSTGDYCLSCLFAQGLPTYTLAVQGISGLPLKKQIDTRKKLSKAVEKRFPHDKLLLLDTQQEAGMLLRQLANQKQQHLAFRDRRAYLFAHAVDFVPSEENNLVGTLKISGYVRGQTLNVNRLLHIVGYGDFQMKQIDAPGDPFPLNPRGIKPQKDPDMAMEICATDAVDDMEEGLKVLMKADPGRQESLQAEVIPDPMEGEQTWPTEEELSEAKDFLKESSKVVKKVPKGTSSYQAEWILDGGSQSGGEGDEYEYDDMEHEDFMEEESQDESSEEEEEYETMTIGESVHDDLYDKKVDEEAEAKMLEKYKQERLEEMFPDEVDTPRDVAARIRFQKYRGLKSFRTSPWDPKENLPQDYARIFQFQNFTNTRKSIFKEVEEKEVEGAEVGWYVTLHVSEVPVSVVECFRQGTPLIAFSLLPHEQKMSVLNMVVRRDPGNTEPVKAKEELIFHCGFRRFRASPLFSQHTAADKHKLQRFLTADMALVATVYAPITFPPASVLLFKQKSNGMHSLIATGHLMSVDPDRMVIKRVVLSGHPFKIFTKMAVVRYMFFNREDVLWFKPVELRTKWGRRGHIKEPLGTHGHMKCSFDGKLKSQDTVLMNLYKRVFPKWTYDPYVPEPVPWLKSEISSTVPQGGME
Protein: Pyridoxal phosphate homeostasis protein (PLP homeostasis protein) (P38197)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- L-2-aminoadipate reductase
- Pyrroline-5-carboxylate reductase
- Cu
- Altered inheritance rate of mitochondria protein 29
Sequence:
MSTGITYDEDRKTQLIAQYESVREVVNAEAKNVHVNENASKILLLVVSKLKPASDIQILYDHGVREFGENYVQELIEKAKLLPDDIKWHFIGGLQTNKCKDLAKVPNLYSVETIDSLKKAKKLNESRAKFQPDCNPILCNVQINTSHEDQKSGLNNEAEIFEVIDFFLSEECKYIKLNGLMTIGSWNVSHEDSKENRDFATLVEWKKKIDAKFGTSLKLSMGMSADFREAIRQGTAEVRIGTDIFGARPPKNEARII