wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha hemolysin (Necrotic enteritis toxin B) (NetB) (A8ULG6)
Organism: Clostridium perfringens
Interaction partners:
Sequence:
MKRLKIISITLVLTSVISTSLFSTQTQVFASELNDINKIELKNLSGEIIKENGKEAIKYTSSDTASHKGWKATLSGTFIEDPHSDKKTALLNLEGFIPSDKQIFGSKYYGKMKWPETYRINVKSADVNNNIKIANSIPKNTIDKKDVSNSIGYSIGGNISVEGKTAGAGINASYNVQNTISYEQPDFRTIQRKDDANLASWDIKFVETKDGYNIDSYHAIYGNQLFMKSRLYNNGDKNFTDDRDLSTLISGGFSPNMALALTAPKNAKESVIIVEYQRFDNDYILNWETTQWRGTNKLSSTSEYNEFMFKINWQDHKIEYYL
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (O14344)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:16823372}.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase
- Bifunctional purine biosynthesis protein ade10
- AMP deaminase
- Inosine triphosphate pyrophosphatase
- Putative glutamine amidotransferase-like protein C13C5.04
- CTP synthase
- IMP-specific 5'-nucleotidase 1
- Amidophosphoribosyltransferase
- Golgi apyrase
Sequence:
MSAFKPYTEALEVLKKYEKKDGLSIDDLIRHNFQGGLTFNDFLILPGYIDFVPNNVSLETRISRNIVLKTPFMSSPMDTVTEDQMAIYMALLGGIGVIHHNCTPEEQAAMVRKVKKYENGFILDPVVFSPQHTVGDVLKIKETKGFSGIPITENGKLRGKLVGIVTSRDVQFHKDTNTPVTEVMTPREELITTAEGISLERANEMLRKSKKGKLPVVDKDDNLVALLSLTDLMKNLHFPLASKTSDTKQLMVAAAIGTRDDDRTRLALLAEAGLDAVVIDSSQGNSCFQIEMIKWIKKTYPKIDVIAGNVVTREQTASLIAAGADGLRVGMGSGSACITQEVMACGRPQATAIAQVAEFASQFGIGVIADGGIQNVGHMVKSLSLGATAVMMGGLLAGTTESPGEYYVREGQRYKSYRGMGSIAAMEGTGVNKNASTGRYFSENDAVRVAQGVSGLVVDKGSLLRFLPYLYTGLQHALQDIGTKSLDELHEAVDKHEVRFELRSSAAIREGDIQGFATYEKRLY
Protein: Protein ORGAN SIZE RELATED 1 (Q8RWS1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with ARGOS and ARL, regulates organ growth and final organ size. Promotes both cell expansion and proliferation-dependent organ growth, in an ANT-dependent manner.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q7X6L2}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:21457262}. Nucleus {ECO:0000250|UniProtKB:Q6NMD6}. Cytoplasm {ECO:0000250|UniProtKB:Q6NMD6}.
Interaction partners:
- Transmembrane protein
- Uncharacterized protein
- AT4g29480/F17A13_300
- Uncharacterized acetyltransferase At3g50280
- ARGOS-like protein
- CAP superfamily protein
- Protein AUXIN-REGULATED GENE INVOLVED IN ORGAN SIZE
- Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.3
- GDSL esterase/lipase EXL3
- Myb family transcription factor PHL11
Sequence:
MRVHDQRLRFDVTPKPMGLNGSSLITARSVALLLFLSLLLLILPPFLPPLPPPPATLLLLPLLLMILLIFLAFSPSNEPSLAVEPLDP
Protein: Homeobox protein Hox-D1 (Homeobox protein Hox-4.9) (Q01822)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-B1
Sequence:
MSSYLEYVSCAAGGGSGGVGGDVLGFAPKFCRADARPVALQPAFPLGSGDGAFVSCLPLATARPTPSPPAGPAQSPVPQPAAPRYAPCTLEGAYERGAAPASAAEYGFLGSGPAFDFPGALGRAADEGGAHVHYATSAVFSGGGSFLLSGQVDFAAFGEPGPFPACLKEPADGHPGPFQTVSPAPGACPKPASPTSSLPAAHSTFEWMKVKRNAPKKSKLSEYGATSPPSAIRTNFSTKQLTELEKEFHFNKYLTRARRIEIANCLQLNDTQVKIWFQNRRMKQKKREREGLLATAASVASIKLPRSETSPIKSGRNLGSPSQAQEPS
Protein: Protein fantom (RPGRIP1-like) (E7F4E7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
- Si:dkey-202c5.1 protein.
- Nephronophthisis 1.
- Centrosomal protein of 290 kDa
- Coiled-coil and C2 domain-containing 2A.
- Meckelin isoform X1
- Abelson helper integration site 1.
- Proteasome 26S subunit, non-ATPase 2.
- Proteasome 26S subunit, non-ATPase 2.
- Transmembrane protein 231
- Retinitis pigmentosa GTPase regulator a.
Sequence:
MFSRADETAADIPVRDTNGAALPDSLLSQNIRERQNVSKLSREELEDKYLRLQDENLTLKQHTCKQEDKIRRMATKLIRLVKDRKQRDGGRDVEMEEMMEELQEKVQELEKQNEGLKRRLLAAKQQLQVQSRRHTPYAHIQSRINTGLRRVPDTHTPVTTSRPHTPKAALRHVEGEMSAKPPQSLLPRYGHSLLDEARAEIRNLENVIESQQMQMEELERSAEMMRDQLKRRDREFEESLLQVREQQASGQRLTIKDNVEMIKLQKLLSEKANTLAVLEGRFLQQQESMKTLKASHDAALLKVEDGNRQLKEERLKSLQLETQITSRALEHRHLLELQERIQDLEKERDLLKENCDKLVKSAFDVSQEQKWRTREQQLKLQVAQLETALKSDLADKNQILDKIKAERDVNENLTQENKQLQLRYLEQKQQLEEIKDRMKFFTKESEIDAAELSEALMLIKVRRSQKSGELGFLEKVEEDVKVDVERSLKELQATYAETVQELEKTRNMLIIQHKINKDYQAEVEAVNRMMDDLKLEYELKSEKLAQLLDMRAAKIRKLEAQLKDIAYGTKTHVFRPDETSDDVTDEFEGTVQLARGENLLEIHLGKGQFSPEAVESLKDKDPSTFCTYAFYDFELQSTPVVHGERPDYSFSSQYLVRVDDLFLNYLHTNSITVEIQLAEGLNFRTVAAGQIRLNQLLERDGKVFSTIQLVGVSDEIQVFGSLEYWLKLKVSMDQAIRLYKERVKALGFLKTSLRDSKAFSVPAPSSSSLMNGDLNELSISIHSCCNLKPKGPHTQPSPYIVYKLYDFPDHDTPIIPCTTEPQFEDHMVFPMTMNSNLDAFLRSEALVVYVFDDLDVENQLYLGKARVPLDSLAHDKTITGLFELTDPAGLPSGQINVTLKWSFTYLPPSSTVFSTQQTPERQTSHEKDKIETETHMITEELQPSLSETPMPRPRQRTLPKSTIKRVSFVDVTELEKQMEQHTPTDEEDDDDNEEQRAPVTPASKTVIRLDAGSSSAVSEEEEDEEESQFSEGQLITGSSQSEESEISEQLQTDAQAEDDDDDDSDDCIVPAHSTQQKKQPSECIRVEIVSLSLKPGSRVAEDSRIVRLFVEYAFLGLQSVETPLSLKKPLPGRSVSYNFSNVIHVDMENNQARRQTLRAVLEGRNRQLEHIKFTVVSDPPEEAEQEEECEDVGVAFLRLLDIMDRRRDMKDVSVNIVDVQDSSAVIGHLVVTVEALEALMSIMKDPERDRPLTTLA
Protein: Protein BIC2 (BLUE-LIGHT INHIBITOR OF CRYPTOCHROMES 2) (Q9M280)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates the blue-light dependent dimerization of CRY2 and formation of photobodies. Inhibits CRY phosphorylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:27846570}.
Interaction partners:
- Cryptochrome-2
- Cysteine/Histidine-rich C1 domain family protein
- Ankyrin repeat family protein
- At2g15020
- Serine/threonine-protein kinase MPS1
- AT3g45210/T14D3_150
- Spindle assembly abnormal protein
- Probable folate-biopterin transporter 8
- Cryptochrome-1
- Protein kinase superfamily protein
Sequence:
MKNTNLPEETKEPISPGSSHRKQNKTGTKTCFPETTVLSGRDRLKRHREEVAGKVPIPDSWGKEGLLMGWMDFSTFDAAFTSSQIVSARAALMADSGDDAGARGSRPQRLRVESSC
Protein: Branched-chain-amino-acid aminotransferase 3, chloroplastic (Atbcat-3) (EC 2.6.1.42) (EC 2.6.1.88) (Q9M401)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts 2-oxo acids to branched-chain amino acids. Acts on leucine, isoleucine and valine. Also involved in methionine chain elongation cycle of aliphatic glucosinolate formation. Catalyzes the conversion of 5-methylthiopentyl-2-oxo and 6-methylthiohexyl-2-oxo acids to their respective Met derivatives, homomethionine and dihomo-methionine, respectively.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:25070638}.
Interaction partners:
- Dihydroxy-acid dehydratase, chloroplastic
- 2-isopropylmalate synthase 1, chloroplastic
- 2-isopropylmalate synthase 2, chloroplastic
- Methylthioalkylmalate synthase 1, chloroplastic
- Cystathionine gamma-synthase 1, chloroplastic
- 2-oxoisovalerate dehydrogenase subunit alpha 2, mitochondrial
- Methylthioalkylmalate synthase 3, chloroplastic
- 3-methyl-2-oxobutanoate hydroxymethyltransferase 1, mitochondrial
- 3-methyl-2-oxobutanoate hydroxymethyltransferase 2, mitochondrial
- Threonine dehydratase biosynthetic, chloroplastic
Sequence:
MERAAILPSVNQNYLLCPSRAFSTRLHSSTRNLSPPSFASIKLQHSSSSVSSNGGISLTRCNAVSSNSSSTLVTELADIDWDTVGFGLKPADYMYVMKCNIDGEFSKGELQRFGNIEISPSAGVLNYGQGLFEGLKAYRKKDGNNILLFRPEENAKRMRNGAERMCMPAPTVEQFVEAVTETVLANKRWVPPPGKGSLYVRPLLMGTGAVLGLAPAPEYTFIIYVSPVGNYFKEGVAPINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCIYKRYLEEVSSCNIFIVKDNVISTPEIKGTILPGITRKSMIDVARTQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSVTYKGKRVSYGEGTFGTVSKQLYTVLTSLQMGLIEDNMKWTVNLS
Protein: Alpha-1,3-rhamnosyltransferase WapR (Q9HUG5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Spore protein YkvP/CgeB glycosyl transferase-like domain-containing protein
- UTP--glucose-1-phosphate uridylyltransferase
- O-antigen ligase
- GNAT family N-acetyltransferase
- Uncharacterized protein
- GDP-6-deoxy-D-mannose reductase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Lipopolysaccharide export system protein LptC
- Alginate biosynthesis protein AlgA
Sequence:
MALVDDGSQPLVSVIIASYNHEKYIEASIASVAAQTYRNVELLVVDDGSSDGSVELLRGLQAKYGFDLRVQQNQGLSRTLNEAITRARGNLIVPFGSDDIMLPQRLEKQVAHMWDKPEVGICAGNIEIIDSNGRVMPGKEQRKRDLPFRRLDFDDLFLDRKPGPMAPTLMFRREALEKVGGFDPDIRLEDVYIELAVTKAGYVIDILGEVLAQYRKHPTNTYKNARFMVDNVFKTYSQFSDHPDYEQVIMRFRNSMFLKCSNRDKVLARELLSGLPLKYWNEKTFRGIARLFFS
Protein: Inhibitor of growth protein 5 (p28ING5) (Q8WYH8)
Organism: Homo sapiens (Human)
Function: Component of the HBO1 complex, which specifically mediates acetylation of histone H3 at 'Lys-14' (H3K14ac) and, to a lower extent, acetylation of histone H4. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator. Inhibits cell growth, induces a delay in S-phase progression and enhances Fas-induced apoptosis in an INCA1-dependent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:18794358}. Chromosome {ECO:0000269|PubMed:24065767}. Note=Localizes to transcription start sites. {ECO:0000269|PubMed:24065767}.
Interaction partners:
- Peregrin
- Histone acetyltransferase KAT6A
- Chromatin modification-related protein MEAF6
- Histone acetyltransferase KAT7
- Histone acetyltransferase KAT6B
- Bromodomain-containing protein 1
- Protein Jade-1
- Bromodomain and PHD finger-containing protein 3
- Cellular tumor antigen p53
- E3 ubiquitin-protein ligase Jade-2
Sequence:
MATAMYLEHYLDSIENLPCELQRNFQLMRELDQRTEDKKAEIDILAAEYISTVKTLSPDQRVERLQKIQNAYSKCKEYSDDKVQLAMQTYEMVDKHIRRLDADLARFEADLKDKMEGSDFESSGGRGLKKGRGQKEKRGSRGRGRRTSEEDTPKKKKHKGGSEFTDTILSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPKGKWFCPRCVQEKRKKK
Protein: 2-haloacrylate reductase (EC 1.3.1.103) (Q59I44)
Organism: Burkholderia sp
Function: Involved in the degradation of unsaturated organohalogen compounds. Catalyzes the NADPH-dependent reduction of the carbon-carbon double bond of 2-chloroacrylate to produce (S)-2-chloropropionate, which is probably further metabolized to (R)-lactate by (S)-2-haloacid dehalogenase. Can also use 2-bromoacrylate as substrate. Does not act on acrylate, methacrylate, 1,4-benzoquinone and 1,4-naphthoquinone.
Interaction partners:
Sequence:
MVMAAVIHKKGGPDNFVWEEVKVGSPGPGQVRLRNTAIGVNFLDTYHRAGIPHPLVVGEPPIVVGFEAAAVVEEVGPGVTDFTVGERVCTCLPPLGAYSQERLYPAEKLIKVPKDLDLDDVHLAGLMLKGMTAQYLLHQTHKVKPGDYVLIHAAAGGMGHIMVPWARHLGATVIGTVSTEEKAETARKLGCHHTINYSTQDFAEVVREITGGKGVDVVYDSIGKDTLQKSLDCLRPRGMCAAYGHASGVADPIRVVEDLGVRGSLFITRPALWHYMSNRSEIDEGSKCLFDAVKAGVLHSSVAKTFPLREAAAAHKYMGGRQTIGSIVLLPQA
Protein: Solute carrier organic anion transporter family member (A0A2R8QFF0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362056}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362056}.
Interaction partners:
Sequence:
MEGSANRMEYSGGNQKTSQTKCCSSLKIFICALAFSYFSKSMTGSYTKSTITQIEKRFEIPSSTVGFIDGSFEMGNMLVITLVSYIGAKFHRPKIIGAGVLLMGIGTLLMASPHFLMGRYKYGTAATHTNDAGNFTVISTCSSDSQETLQQPFSGCQKEEAESSPFWVIVVLGNTMRGIGEASIVPLGMSFIDDYARPENSAFYIGCLNTLKGIGPIFGYMLGSLCANLYVDFGLVDQESVTITPQDSRWVGAWWLGYVVSGLLTLLAAFPFWFLPKVLPENSQISLLDNTPQQHKTTPSLTEIVKDFAPTFKRLLTNKIYILYLAYSIVAFNDFAIVATYTPKYLEQQFGQSASKANFLIGVTSIPAVALGVFLSGLMMKRFKWGLLASARVNLLTIVATVFLAVPFFALSCENLDIAGVTVPYQGSTEVQGVTSDVLPSCNADCGCPDLQWDPVCGENGVTYISPCHAGCNSTQGAGRNMTFHDCRCIQSWGLSVGNSSAVLGQCSRDPKCNRMIYIYLGLQSLAFFLCGLGIIPFFTMSLRIVDPELKSLSVGMLLLAVRVLGGIPAPIYFGALIDSTCLKWGQNKSCGRGACRIYDIETFRFLFQGLTMCLRVLACSLLWIATIEIKRKNTEQQTNVSRH
Protein: SUMO1 activating enzyme subunit 1 (M0QZS6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVEKEEAGGGISEEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAKVVFCPVKEALEVDWSSEKAKAALKRTTSDYFLLQVLLKFRTDKGRDPSSDTYEEDSELLLQIRNDVLDSLGISPDLLPEDFVRYCFSEMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKGNGIVECLGPK
Protein: Transketolase-like 1 (A2ID95)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAFLIHNAPESSSACGKATDEFKHVKEYSCQRHKGNLPRVHGALRHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAKRLSFVDVATGWLGQGLGVACGMAYTGKYFDRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIYQRRCEAFGWNTYVVDGRDVEALCQ
Protein: Cryptochrome 2 (Photolyase-like), isoform CRA_a (Growth-inhibiting protein 37) (Photolyase-like cryptochrome 2) (A2I2P1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAATVATAAAVAPAPAPGTDSASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPWFAASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEYDSEPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQAIISRMELPKKPVGLVTSQQMESCRAEIQENHDETYGVPSLEELGFPTEGLGPAVWQGGETEALARLDKHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNSTPPLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWLSCSAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKAFPSRYIYEPWNAPESIQKAAKCIIGVDYPRPIVNHAETSRLNIERMKQIYQQLSRYRGLCLLASVPSCVEDLSHPVAEPSSSQAGSMSSAGPRPLPSGPASPKRKLEAAEEPPGEELSKRARVAELPTPELPSKDA
Protein: DNA (cytosine-5-)-methyltransferase (EC 2.1.1.37) (Q588C6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA
- S-adenosylmethionine decarboxylase proenzyme
- DNA
- S-adenosylmethionine synthase
- S-adenosylmethionine synthase
- Methionine adenosyltransferase 2 subunit beta
- S-adenosylmethionine synthase
- S-adenosylmethionine synthase
Sequence:
MRKEEIKKSTEIVMPSNKYPSAESDKMTATAAMNRDTSVGDGLSENDSGLEMTSENSPLTPAEPPSPFCPKQNGGAASPADESVNSIRRKRSRKRSDTEEDSAWDSSYSEEKAEVGSGCETGLRQRPRPRTIFQAGLTAHSKPRSRERGHSKEDHSDLVASVPEGPALELMEQDSKDSAQSSTTSTSTTETASQPEYKDNKGFGIGELVWGKIKGFSWWPGMVVTWRATGRRQASHGMRWLQWFGDGKFSEVSADKLDSITAFPKFFNQSSYTKLASYRRAIFQALEVASLRAEKTFPPSEADSLEEQVKPMLDWAHGGFLPKGQEGLKPKENAEYCVFPLASESSTLLESSPPEFPPSAKRARLPLNKAKPGIEEVYSREQMVNEVLKNHRSIEEFCLSCGKTRVATFHPLFEGGLCLTCKDAYLENSYMYDDDGYQSYCTVCCGGREMLLCGNANCCRCICVDCLDILVGAGAANSARNLDPWRCYMCQPLQQYGVLKKRHDWSLKLQEFFVNDSGQEFESPKIYPAVPAEQRRPIRVLSLFDGIATGYLVLRDLGFKVDLYIASEVCEDSISVGAVRHEGKIQYVHDVRNITRKNIAEWGPFDMVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLSEAKPKEGEDRPFFWMFENVVAMSVNDKRDISRFLECNPVMIDAIEVSAAHRARYFWGNLPGMKRPLCASGMDKLELQDCLEHGRVAKFGKVRTITTRSNSIKQGKDQHFPVMMNGKEDILWCTELERIFGFPVHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE
Protein: Ferredoxin, apicoplast (Q8IED5)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. By transferring electrons to 4-hydroxy-3-methylbut-2-enyl diphosphate reductase LytB/IspH, plays a role in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Subcellular location: Plastid, apicoplast {ECO:0000305|PubMed:17251200}.
Interaction partners:
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Ferredoxin--NADP reductase, apicoplast
- Apoptosis-inducing factor, putative
- NADH-cytochrome b5 reductase, putative
- Cytosolic Fe-S cluster assembly factor NAR1, putative
- Multidrug resistance protein 2
- Chloroquine resistance transporter
- Cytochrome b-c1 complex subunit Rieske, putative
- Iron-sulfur cluster assembly protein IscU
- FAD-dependent monooxygenase, putative
Sequence:
MNIVILLLILTFSIKHSNTYKLKNTYIPINYMYHNNKNILRSQKSKLFLNFLSNNQLANSNKQTCFFKSNIKSSISNIDNYDYIRKRYINTSNKNKLFYNITLRTNDGEKKIECNEDEYILDASERQNVELPYSCRGGSCSTCAAKLVEGEVDNDDQSYLDEEQIKKKYILLCTCYPKSDCVIETHKEDELHDM
Protein: Membrane transporter protein, putative (Q38DL3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVTMEGTLAAVSGISNVGRHPPITVLLMELFKIAMPMSISQIAQFSFMVVMLICAGHIGVHELGAVSIALGILNATGFAFGSGLCGALETLLSQSYGQNPRSTMYGVYAQRMFFILMVFVVPLSVFLLFVEGMLNALGEPPDVAVRAGHFCHIAIFGLPFFMVLELLRRYYASQHQSNPVFVTLLAAALVNPIVEGVLVYIFGYTGIALGWVFVMLGMDIALVCFLKWSGLHTRTWGGWSSAAFRNWYPMLKLAIPSLGMAFSEWTAMEVNSLCAGLLSTEELGAYAVTSQIANLCWSVVSGLFIAATVLVGNSLGAGNPDLGKQYALLSSVLVLVVSLLNAAVVYKFRDRIPRIFTHEDGISKHFSDMVPYFLTFHVLDAVQSNFLAILRGCGLQLVGVAIVFVCLTIIGTPLGIYLAFARHYGVVGLWVGPVASCAAFGIPAYLYVLFCRIDWASLRPHLEECEMKKFVEVTLVDEDELT
Protein: Diacylglycerol O-acyltransferase 2 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase 2) (Q70VZ8)
Organism: Bos taurus (Bovine)
Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides (By similarity). Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
Interaction partners:
Sequence:
MKTLIAAYSGVLRGTGSSILSALQDLFSVTWLNRAKVEKQLQVISVLQWVLSFLVLGVACSVILMYTFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTSRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPRLERPTQQDIDLYHAMYVQALVKLFDQHKTKFGLPETEVLEVN
Protein: Uncharacterized protein, isoform B (M9PE69)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLIEIYDYAAKLLNNMTARGVRNSVGKSAESRTKESTGKLGSLLGRTLAKVAKVARSNPAQHVTNLPVSALLLQALDVADVARGQGIDYPITSTTGTTFNIITTTTTTTTTTTGSDPTDVLGSQPPAFSFPANVTGAPGSAGNANAYLPAGNLSGFIESSTTAVMSTLPIPTSTMATLQAQTVATFIAATGSKNRPTTIVVYPTVSPESIVIPIVSCIFGFPILALLVICCLRRRAKLARERDRRRNYDMQDHAVSLITDRRELSVYVLNEA
Protein: RING-H2 finger protein ATL48 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase ATL48) (YGHL1-C3HC4 RING fusion protein) (Q7X843)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836}.
Interaction partners:
- Cytochrome c oxidase subunit 6a, mitochondrial
- Cytochrome c oxidase subunit 6b-1
- Cytochrome c oxidase subunit 5b-2, mitochondrial
- Cytochrome c oxidase subunit 6b-3
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 5b-1, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 6b-2
Sequence:
MSSVEPDMEDLFQEKKRVRNPLVPLGALMTAGVLTAGLISFRRGNSQLGQVLMRARVVVQGATVALMVGTGYYYGDNPWKKLLLSEIHETEALSPKSSSAATLTLMNQKDPSSSSIVSVLCLVISGLALIIVFLGVLYLIFKFLRKSSTLFPIPHFNYNPDLFSFSSPQLQHLFFLHDSGLDQTAIDALPVFLYGNVTISLEQPFDCAVCLNEFSDTDKLRLLPVCSHAFHLHCIDTWLLSNSTCPLCRRSLSTSNVCYNHSETLVAPLSGHQQVDDGKASLAKRVFSVRLGRFKSTNESQSQRHDVKDEIGVRMPRRCYSMGTQQYLVCDQDFVVALSSSPREGNIGR
Protein: Kanosamine kinase (EC 2.7.1.179) (G0FS68)
Organism: Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei)
Function: Involved in the biosynthesis of 3-amino-5-hydroxybenzoate (AHBA), a compound that then serves as the starter unit for the assembly of a polyketide during the biosynthesis of rifamycin B and other ansamycin antibiotics. Catalyzes only the phosphorylation of kanosamine to yield kanosamine 6-phosphate.
Interaction partners:
- COG0637 Predicted phosphatase/phosphohexomutase.
- Putative UDP-kanosamine synthase oxidoreductase subunit
- COG1940 Transcriptional regulator/sugar kinase.
- COG1940 Transcriptional regulator/sugar kinase.
- COG1940 Transcriptional regulator/sugar kinase.
- COG1940 Transcriptional regulator/sugar kinase.
- COG1940 Transcriptional regulator/sugar kinase.
- COG1940 Transcriptional regulator/sugar kinase.
- Glucokinase
- COG1940 Transcriptional regulator/sugar kinase.
Sequence:
MGTPYHLGIDVGGTKVAFRVESGSACIEETSFSWGARHSAEDDLAQLAGHVARLRERIGTPLEAVGVAMPGTVGADGRVATWPSRPEWTGVDLKTALHSLFPEAAVAWADDGDLGALAESRASGCENLLYIGIGTGIGGGLVLGGVPCPGLGRGSFEIGHVIVEMGGVRCVCGRRGCLQALASGPATLRRASLLRGADVTYYRLQRALRNGEPWAADALEGSTRALAAAVTGVQELVHPDRVLIGGGFAAGIPEIVPSVSGFLADLVRQGQAPLPVEPAALGGLSSLRGAVALAGLVAAGEVP
Protein: Fatty acid activator Faa4, putative (AFU_orthologue AFUA_2G09910) (C8V333)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- AMP-binding enzyme, putative
- Palmitoyl-protein thioesterase 1
- Uncharacterized protein
- Fatty acid synthase subunit alpha
- Fatty acid synthase subunit alpha reductase
- Fatty acid synthase subunit beta
- Fatty acid synthase alpha subunit pkiB reductase
- Fatty acid synthase beta subunit aflB dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Fatty acid synthase alpha subunit stcJ reductase]
- Fatty acid synthase beta subunit stcK dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase]
Sequence:
MTKDGSVVYPRMSKKGPFTVEAPGVEPVPGETVPRRHPRAKDGLLLRPAEDLATTYDAFRWAARSYGNAKAVASRRLIKTHIETKKVKKVIDGVEQEVDKQWTYFEKGPYSYKSFIEYETLALELGKGLRKIGLNKGDKVHLYGATSANWLAMSHGSASQSLTVVTAYDTLGEEGLAHSIVQTESDAIFLDPTLIKSLTNVLDRAKSIKHVIWNSDEELKQEDMDRLKTEFSHLNILSFEDLRKLGEENHYDPVPPAPEDLCCIMYTSGSTGPPKGVPLTHANVVAAMAGVDAIIGPYVGPSDALLTYLPQSHILEFMFENLCLFWGGTMGYGNPRTLSDASMRNCKGDIREFRPTILVGVPAVWESVKKGVLNNLNKNSALVKGLFWGALSAKNFLMSTGFPGASMGAWFLDNVIFRKLKDATGGRLRVVMNGGGPVSKETQKFLSMAIAPMISGYGLTETSAMGALNDPGAWNPNALGEIPACIEVKLVDFADAGYFTKNNPPQGEIWIRGGSVSTHYFKNEEETKAAYAEGGWFMTGDIGEFDKNGHLKIIDRKKNLVKTQNGEYIALEKLESVYRSSPIVGNICVYAAEDQDKPIAIIVPVEIALKKIASENGIEGDSVETLVHNEKLKSIVLKQLQTAGRASGLKGIEIINGVVLSDEEWTPQNGFMTAAQKLQRKKIINRYHKDIDRAYGKK
Protein: Fumarate hydratase isoform 7 (A0A0S2Z408)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYRALRLLARSRPLVRAPAAALASAPGLGGAAVPSFWPPNAARMASQNSFRIEYDTFAENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK
Protein: Tyrosine-protein phosphatase domain-containing protein (O44136)
Organism: Caenorhabditis elegans
Interaction partners:
- Tyrosine-protein phosphatase domain-containing protein
- non-specific serine/threonine protein kinase
- Tyrosine-protein kinase
- Putative casein kinase I C03C10.2
- SPK domain-containing protein
Sequence:
MKSIFGTKNKKRSKNKDGKLMSTASRNGDEATKPNGTKTSKKRKPSRGNDDKGREPEPTAQSKKAKKMKPKRDSKAPSPALSPGPREQLSDQKKTVEDDPPPAPIATSVSGTVTSTVNAMPAILSSEVSNKQPKEVNSMKKTKGAPNSTTDTPVSHKTSITGNADKWVGEDVAKTWMDSIDLAEVKKDFEKLQTMKIDIDKDCKTWKANSKLNQSEHFPALDSNLLKIEKGYVNISHVEVPLGRNVHIGQFPVKDTEETFWKAVFDKRITSIDVLVGDEPIEFFPKKAEDYKNYGQMWINNRKVEHVIDEVFRFSIEVLPHGCSNSIICNVTVFGNWKVDSVPVKQAIAIKEALGLNYFLLKTPADDNAMIISPHGAGRAGYFLALAVAVHTIDTKIAEPNIADIVKSIRTQRPRAVDSFCQYCSLYISLLYFIKKKVTKPADGDKKSTPTNKYLFKKSVELTKQFTNVLLEANQPSMMGPG
Protein: DnaJ homolog subfamily B member 5 (Heat shock protein Hsp40-3) (Heat shock protein cognate 40) (Hsc40) (O89114)
Organism: Mus musculus (Mouse)
Interaction partners:
- Heat shock 70 kDa protein 1B
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 4
- Endoplasmic reticulum chaperone BiP
- Nucleotide exchange factor SIL1
- Heat shock 70 kDa protein 1-like
- Stress-70 protein, mitochondrial
Sequence:
MGKDYYKILGIPSGANEDEIKKAYRKMALKYHPDKNKEPNAEEKFKEIAEAYDVLSDPKKRSLYDQYGEEGLKTGGGSSGGSGGSFHYTFHGDPHATFASFFGGSNPFDIFFASSRSTRPFSGFDPDDMDVDEDEDPFGAFGRFGFNGLSRGPRRAPEPLYPRRKVQDPPVVHELRVSLEEIYHGSTKRMKITRRRLNPDGRTVRTEDKILHIVIKRGWKEGTKITFPKEGDATPDNIPADIVFVLKDKPHAHFRRDGTNVLYSALISLKEALCGCTVNIPTIDGRVIPLPCNDVIKPGTVKRLRGEGLPFPKVPTQRGDLIVEFKVRFPDRLTPQTRQILKQHLPCS