wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase) (P00511)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
Interaction partners:
- Fructose-bisphosphate aldolase A
- Fructose-1,6-bisphosphatase 1
- Fructose-bisphosphate aldolase B
- Fructose-bisphosphate aldolase
- 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3
- hexokinase
- Hexokinase-2
- Transketolase
- hexokinase
- Glucose-6-phosphate isomerase
Sequence:
MTHEEHHAARTLGVGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITAEEATRSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRITEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDNWEDHLCRRLSETRTRGSRLNIIIVAEGAIDRNGKPITSEGVKDLVVRRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKRFDEAMKLRGRSFMNNWEVYKLLAHIRPPAPKSGSYTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGPAKGQIEEAGWSYVGGWTGQGGSKLGSKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMAGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELQNQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSEHAHLEHISRKRSGEATV
Protein: Spermitin, isoform F (E1JHY2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLHCQVEGAKAEQRECPVMHSENSAETFSSEESQASDCNQPLDVQSPKLTTNIEESFKVDCKLSLNTLLSPINITDPLRKQIDFQCKLGDLSFFGPVMCSISEFNKEEQTMEPYFIQELDMACAGQEVEQVAEENVFETGPQLKLPENQPINDSITTETNETKLPSTEALNVLNLAEFSEPVMEKSNISIEEVNLTGAEEINEPISDEPNSQLVESAAKLQPKSLGIQIPPLQIEDLISPLVEQPKIATKLGVISFLTGNKLALTPSVRLSFGDRVTTRTNKKSKEIVQQQASKALKALISVFTMQRRLEASQCDNSNNSRSKRFEQLKSSLTFSRVFRQNIFQPTSKIESRQQNTDANSLESGEPNFKSTSAYKEPLPIPYRQDAGEGLTCNGLNVSKDSVFSEVSESDVSETHNKLFAMKKTQEGLSSTRSIGELSNILNNGRVLFSQPVRLFCFNKLKEWKRQGKVPRFHESPYRSPSFSGEGQIEVIEHHGSYYIVLHDKVSGELIIHMRVDEKWRIDYMTKSSYSCRWTNINYANCRDGTLERIACSFREPSHAAEFVARIRNSALQSRLECSS
Protein: TRAF-type domain-containing protein (Q57Y32)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
METESKTTVTSGAPWKYNGALVRDPTKRKSSDLLPKNLRKCPYCRRFGCSEHISRCGQQLVECSCCGMEVEMARLAAHEEYYCKGRERSQTRVLCSEPPTPPCEQKSDVSCSKGHVCEDVLPSATERTAQVCRKHTDRKVKPAVSNGKQAVETNLKGVSPECKIKGDDVQQTATHVYPVEPPPLPNTVQLEERTAVGALTENPSERSKMDGEVVRQKPSFSGFVKASHEVLRDIKNCRSHATHSTKCNTTTSLWGASRRLSGMPYPRLRGSSAFGAFTGFSKVAKGNVGVASRTETRHSRQQKDDTLTETGPSIPPQRVCVRSKSAAAGQ
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (I3L0X6)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein {ECO:0000256|RuleBase:RU365079}.
Interaction partners:
Sequence:
MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPVSRNRLAQVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWY
Protein: Serpin B7 (Megsin) (TP55) (O75635)
Organism: Homo sapiens (Human)
Function: Might function as an inhibitor of Lys-specific proteases. Might influence the maturation of megakaryocytes via its action as a serpin.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLPENDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIRKDDIILFSGKVSCP
Protein: Anaphase-promoting complex subunit 9 (Q12107)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit DOC1
- Anaphase-promoting complex subunit SWM1
- Anaphase-promoting complex subunit MND2
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit CDC27
Sequence:
MNQNGDKNEGKLFQLPSLPPWKTPRFNKANFNNFTTPLRKRSTRVINDDSMPITGEVLEERTADDLYGINMDVDEVDYLNTLSHIEEEKQYDYSPFCERNTLRESRIDSFLKAERAAHCLVFHKVGHLDGIDSYRPDIDIMCGEEANKYDSANPEGNGSMLLESVPGCNKEDLERLSRREFVTNSKPNMRRLDDIINHETNALKSFWNDSGLVNSLQSHHLHEEYLLLQEELKNVYKIKCHDRVPIESLRDKCRRHYSNEDSSFL
Protein: Apolipoprotein A-V (Apo-AV) (ApoA-V) (Apolipoprotein A5) (Regeneration-associated protein 3) (Q9QUH3)
Organism: Rattus norvegicus (Rat)
Function: Minor apolipoprotein mainly associated with HDL and to a lesser extent with VLDL (By similarity). May also be associated with chylomicrons (By similarity). Important determinant of plasma triglyceride (TG) levels by both being a potent stimulator of apo-CII lipoprotein lipase (LPL) TG hydrolysis and an inhibitor of the hepatic VLDL-TG production rate (without affecting the VLDL-apoB production rate) (By similarity). Activates poorly lecithin:cholesterol acyltransferase (LCAT) and does not enhance efflux of cholesterol from macrophages (By similarity). Binds heparin (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q6Q788}. Early endosome {ECO:0000250|UniProtKB:Q6Q788}. Late endosome {ECO:0000250|UniProtKB:Q6Q788}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q6Q788}. Note=In the presence of SORL1, internalized to early endosomes, sorted in a retrograde fashion to late endosomes, from which a portion is sent to lysosomes and degradation, another portion is sorted to the trans-Golgi network. {ECO:0000250|UniProtKB:Q6Q788}.
Interaction partners:
- Apolipoprotein C-III
- Alanine--glyoxylate aminotransferase
- Apolipoprotein C-I
- Beta-2-glycoprotein 1
- Apolipoprotein C-II
- Apolipoprotein A-II
- Apolipoprotein B-100
- Histidine-rich glycoprotein
- Apolipoprotein E
- Apolipoprotein C-IV
Sequence:
MAAVITWALALLSVFATVQARKSFWEYFGQNSQGKGMMGQQQKLAQESLKGSLEQDLYNMNNFLEKLGPLREPGKEPPRLAQDPEGIRKQLQQELEEVSTRLEPYMAAKHQQVGWNLEGLRQQLKPYTVELMEQVGLSVQDLQEQLRMVGKGTKAQLLGGVDEAMSLLQDMQSRVLHHTDRVKELFHPYAERLVTGIGHHVQELHRSVAPHAVASPARLSRCVQTLSHKLTRKAKDLHTSIQRNLDQLRDELSTFIRVSTDGADNRDSLDPQALSDEVRQRLQAFRHDTYLQIAAFTQAIDQETEEIQHQLAPPPPSHSAFAPELGHSDSNKALSRLQSRLDDLWEDIAYGLHDQGHSQNNPEGHSG
Protein: SWI/SNF chromatin-remodeling accessory subunit 1 (Abnormal HSN migration protein 3) (Q09646)
Organism: Caenorhabditis elegans
Function: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (By similarity). Required for the blmp-1-mediated transcriptional activation or repression of several hypodermal genes such as bed-3. Involved in regulating differentiation, migration and axon pathfinding of specific serotonergic neurons (HSNs). Probably regulates vulva development through the let-60/Ras pathway. May be involved in regulation of developmental processes in the embryo driven by the Wnt pathway. Involved in gonadogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96GM5}.
Interaction partners:
- SWI/SNF complex subunit SMARCC2
- Actin-related protein 4
- HMG box domain-containing protein
- SWI/SNF Subunit INI1 DNA binding domain-containing protein
- SWI/SNF chromatin remodeling complex core catalytic subunit swsn-4
- Bromo domain-containing protein
- PHD finger protein 10
- ARID domain-containing protein
- Bromo domain-containing protein
- Zinc finger protein dpff-1
Sequence:
MQTQARPPVPQGPRFNHPATPQQVRRPINAPLPGQTAQIQGNRGPQPPKKKKRYADKLIQPKVRELVPESQAYMDLLAFEQKLDSTITRKKIDVQEALKRPQKIKKRLRIYISHTFIAGKEPEKEGDDASVPMWELRVEGRLLDDMQHPTVGANPRPAPKRKFSSFFKSLVIELDKDIYGPDNHLVEWHRTPQTNETDGFQVKRPGDRPVKCTILLLLDYQPMKFKLHPRLAKVLGIAAETRPRIIEALWQYIKTHKLQDPQDRDTINNDLFLEQCFGVSKMRFMEIPQRLHQLLQQPDPLVLNHIIQRPDDGQDKTSACYDIDVELEDPVKQQMANFVHNQTNANDIQLLDQKIFDLVDQINEMKLRRDFFLRFSNEPSGFIKKWVVSQNSDLKTLTESSGDGESDRYATTYSTTDTDEGVSRYMYQKIQQKRAELEQSLGIRNN
Protein: Negative regulator of genetic competence ClpC/MecB (P37571)
Organism: Bacillus subtilis (strain 168)
Function: Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK.
Interaction partners:
- Protein-arginine kinase
- Adapter protein MecA 1
- ATP-dependent Clp protease proteolytic subunit
- Transcriptional regulator CtsR
- Protein-arginine kinase activator protein
- Chaperone protein DnaK
- Competence transcription factor
- Protein GrpE
- Heat-inducible transcription repressor HrcA
- Chaperonin GroEL
Sequence:
MMFGRFTERAQKVLALAQEEALRLGHNNIGTEHILLGLVREGEGIAAKALQALGLGSEKIQKEVESLIGRGQEMSQTIHYTPRAKKVIELSMDEARKLGHSYVGTEHILLGLIREGEGVAARVLNNLGVSLNKARQQVLQLLGSNETGSSAAGTNSNANTPTLDSLARDLTAIAKEDSLDPVIGRSKEIQRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQQIINNEVPEILRDKRVMTLDMGTVVAGTKYRGEFEDRLKKVMDEIRQAGNIILFIDELHTLIGAGGAEGAIDASNILKPSLARGELQCIGATTLDEYRKYIEKDAALERRFQPIQVDQPSVDESIQILQGLRDRYEAHHRVSITDDAIEAAVKLSDRYISDRFLPDKAIDLIDEAGSKVRLRSFTTPPNLKELEQKLDEVRKEKDAAVQSQEFEKAASLRDTEQRLREQVEDTKKSWKEKQGQENSEVTVDDIAMVVSSWTGVPVSKIAQTETDKLLNMENILHSRVIGQDEAVVAVAKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESIFGDEESMIRIDMSEYMEKHSTSRLVGSPPGYVGYDEGGQLTEKVRRKPYSVVLLDEIEKAHPDVFNILLQVLEDGRLTDSKGRTVDFRNTILIMTSNVGASELKRNKYVGFNVQDETQNHKDMKDKVMGELKRAFRPEFINRIDEIIVFHSLEKKHLTEIVSLMSDQLTKRLKEQDLSIELTDAAKAKVAEEGVDLEYGARPLRRAIQKHVEDRLSEELLRGNIHKGQHIVLDVEDGEFVVKTTAKTN
Protein: GATA-type domain-containing protein (GATA-type transcription factor) (G5EF71)
Organism: Caenorhabditis elegans
Interaction partners:
- GATA-type domain-containing protein
- GATA transcription factor END-1
- Transcription factor elt-7
- Transcription factor elt-2
- T-box transcription factor tbx-35
- Transcription factor elt-6
- Transcription factor elt-1
- Protein pop-1
- Protein skinhead-1
- Probable transcription factor elt-4
Sequence:
MAYPYPVFNAENVFDNTQQQVGFYDYSTPFNGTYSFTTDYSYYNNYYDYVNTYASYYPTAMDSSSLNISSTTGSPNSSHFTTFTHFSTPSTSPSTSTQSSTTPSNSDNKKSFQCSNCSVTETIRWRNIRSKEGIQCNACFIYQRKYNKTRPVTAVNKYQKRKLKVQETNGVDSF
Protein: PH-interacting protein (PHIP) (DDB1- and CUL4-associated factor 14) (IRS-1 PH domain-binding protein) (WD repeat-containing protein 11) (Q8WWQ0)
Organism: Homo sapiens (Human)
Function: Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization.
Subcellular location: Nucleus {ECO:0000269|PubMed:25593309}.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4B
- Cullin-4A
- Transcriptional regulator ATRX
Sequence:
MSCERKGLSELRSELYFLIARFLEDGPCQQAAQVLIREVAEKELLPRRTDWTGKEHPRTYQNLVKYYRHLAPDHLLQICHRLGPLLEQEIPQSVPGVQTLLGAGRQSLLRTNKSCKHVVWKGSALAALHCGRPPESPVNYGSPPSIADTLFSRKLNGKYRLERLVPTAVYQHMKMHKRILGHLSSVYCVTFDRTGRRIFTGSDDCLVKIWATDDGRLLATLRGHAAEISDMAVNYENTMIAAGSCDKMIRVWCLRTCAPLAVLQGHSASITSLQFSPLCSGSKRYLSSTGADGTICFWLWDAGTLKINPRPAKFTERPRPGVQMICSSFSAGGMFLATGSTDHIIRVYFFGSGQPEKISELEFHTDKVDSIQFSNTSNRFVSGSRDGTARIWQFKRREWKSILLDMATRPAGQNLQGIEDKITKMKVTMVAWDRHDNTVITAVNNMTLKVWNSYTGQLIHVLMGHEDEVFVLEPHPFDPRVLFSAGHDGNVIVWDLARGVKIRSYFNMIEGQGHGAVFDCKCSPDGQHFACTDSHGHLLIFGFGSSSKYDKIADQMFFHSDYRPLIRDANNFVLDEQTQQAPHLMPPPFLVDVDGNPHPSRYQRLVPGRENCREEQLIPQMGVTSSGLNQVLSQQANQEISPLDSMIQRLQQEQDLRRSGEAVISNTSRLSRGSISSTSEVHSPPNVGLRRSGQIEGVRQMHSNAPRSEIATERDLVAWSRRVVVPELSAGVASRQEEWRTAKGEEEIKTYRSEEKRKHLTVPKENKIPTVSKNHAHEHFLDLGESKKQQTNQHNYRTRSALEETPRPSEEIENGSSSSDEGEVVAVSGGTSEEEERAWHSDGSSSDYSSDYSDWTADAGINLQPPKKVPKNKTKKAESSSDEEEESEKQKQKQIKKEKKKVNEEKDGPISPKKKKPKERKQKRLAVGELTENGLTLEEWLPSTWITDTIPRRCPFVPQMGDEVYYFRQGHEAYVEMARKNKIYSINPKKQPWHKMELREQELMKIVGIKYEVGLPTLCCLKLAFLDPDTGKLTGGSFTMKYHDMPDVIDFLVLRQQFDDAKYRRWNIGDRFRSVIDDAWWFGTIESQEPLQLEYPDSLFQCYNVCWDNGDTEKMSPWDMELIPNNAVFPEELGTSVPLTDGECRSLIYKPLDGEWGTNPRDEECERIVAGINQLMTLDIASAFVAPVDLQAYPMYCTVVAYPTDLSTIKQRLENRFYRRVSSLMWEVRYIEHNTRTFNEPGSPIVKSAKFVTDLLLHFIKDQTCYNIIPLYNSMKKKVLSDSEDEEKDADVPGTSTRKRKDHQPRRRLRNRAQSYDIQAWKKQCEELLNLIFQCEDSEPFRQPVDLLEYPDYRDIIDTPMDFATVRETLEAGNYESPMELCKDVRLIFSNSKAYTPSKRSRIYSMSLRLSAFFEEHISSVLSDYKSALRFHKRNTITKRRKKRNRSSSVSSSAASSPERKKRILKPQLKSESSTSAFSTPTRSIPPRHNAAQINGKTESSSVVRTRSNRVVVDPVVTEQPSTSSAAKTFITKANASAIPGKTILENSVKHSKALNTLSSPGQSSFSHGTRNNSAKENMEKEKPVKRKMKSSVLPKASTLSKSSAVIEQGDCKNNALVPGTIQVNGHGGQPSKLVKRGPGRKPKVEVNTNSGEIIHKKRGRKPKKLQYAKPEDLEQNNVHPIRDEVLPSSTCNFLSETNNVKEDLLQKKNRGGRKPKRKMKTQKLDADLLVPASVKVLRRSNRKKIDDPIDEEEEFEELKGSEPHMRTRNQGRRTAFYNEDDSEEEQRQLLFEDTSLTFGTSSRGRVRKLTEKAKANLIGW
Protein: Ion-transporting P-type ATPase (Q59Q34)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Calcium channel YVC1 channel YVC1)
Sequence:
MSDLVANPAIQGAELLVPKAVFLRPYVWPFSIIYPIFLQIYFQQYDKYIGGKEWTFVYTIAIVSVNLLFWLMPHWNIDINAKFNYTKVDKISDASYIKITPAPNSGMGEICEINRETFHDGEKQVSFLYQKRRYLFHSKIGKFSPPEFVFDEAPKLAVYQNTKGLSGDLEKMIRNYGSNRFDIPIPTFMELFKEHAVAPFFVFQIFCVALWCMDEQWYYSLFSLFMLVSFEMTTVFQRRTTMAEFQSMGIKPYDVYAYRDGKWVKIPTTDLLPGDLISITRTNEGSALPCDLLLVDGSAIVNEAMLSGESTPLLKESIKLRPADEQLQPEGFDKNSILHGGTMALQVTKPESPIVPVAPDNGAFAVVTKTGFETSQGSLVRMMIFSSERVSVGNKEAFFFILFLLIFAIAASWYVWVEGTRMGRIQSKLILDCIIVITSVVPPELPMELTMAVNSSLSKLQKFYIYCTEPFRIPLAGRIDVCCFDKTGTLTAEDLVFEGLAGFKNDDIHHLHICEDAPETTSYVLGSAHALVRLDDGEVVGDPMEQATLKAAHWNVGTHDTVERESKKGKGKSEKIKILRRFQFSSALKRSSTISQINTISGKNFVAAKGAPETIRNMIVDAPENYEKIYKSFTRSGSRVLALAYKYLESSVNVNKVKREDIESDLHFAGFIVFHCPLKDDAIETIKMLNESSHRSIMITGDNPLTACHVAKEVNITTKEVLILDAPEDHHEIGEYDNLVWRNVTESVVIPFKSSDKINLELFSKYDICITGYALNYLSDHEQILELLKHTWVYARVSPTQKEFIITSLKDAGYNTLMCGDGTNDVGALKQANIGVALLNGTEEGMNKIAENRKIEATLKVYEKQSQIFNNWGKPAPPVPAIIAHLYPPGPLNPKYLEAMEKKGVTITDDMRKAVVEAMKEPVKVPEKNAANGGFNTNSNFADTILGAMNDAEAEDEAPVLKLGDASVAAPFTSKLANVNTVTHIIRQGRVALVSTIQMYKILALNCLISSYSLSVLYLAGMKFGDGQATISGILLSVCFLSISRGRPLEKLSKERPQDGIFNIYIMGSILGQFAVHIITLIYITREIYILEPREPKVDLEKEFSPSLLNTGMFLLQLAQQVSTFAVNYIGLPFRESITSNKGMYYGLLGVAGLTFSCSTEFIPELNEVMQFVPMTIDFKTKLTGCIILDLVVTFAIEYVLKYFFMNSKAADIALREEDEVDA
Protein: Deoxyhypusine hydroxylase (DOHH) (EC 1.14.99.29) (Deoxyhypusine dioxygenase) (Deoxyhypusine monooxygenase) (D9IFD5)
Organism: Leishmania donovani
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate produced by deoxyhypusine synthase/DHPS on a critical lysine of the eukaryotic translation initiation factor 5A/eIF-5A. This is the second step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function.
Interaction partners:
Sequence:
MSALNSRTVEEVRKDYAKLLDPQEPLDSRMRELYRLKEDCLKTAAGVTVILETIDTTDSVLLQHELAYNAGQSGREEAVPELERILRTTSYDVVTRHEAAEALGAIGSPLALQVLEAHSDPTTEPEAPIRETCELALARIAMKETKGDAAVAPPSGCEFVSVDPSPAFSALYSSTDEPVPHTVEELEAVLLDTSGRTRLFRRYMAMFTLRNLATEAAVAALCRGLREDNVSALFRHEVAFVLGQLERPSSQPALIAALKDEEEAPMVRHEAAEALGAIADPATLPVLESYATHHEPIVRDSCVVALEMHKYWANFNGLAHQQQQEA
Protein: Phosphomevalonate kinase (PMKase) (EC 2.7.4.2) (Q9VIT2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15126}.
Interaction partners:
- Mevalonate kinase
- Diphosphomevalonate decarboxylase
- isopentenyl-diphosphate Delta-isomerase
- Hydroxymethylglutaryl-CoA synthase
- Farnesyl pyrophosphate synthase
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Sequence:
MMKIVLISGKRKCGKDYISERLQRRLGSRSCIVRISEPIKSEWARKLQLDLDALLGDGPYKEKYRRDMIVWSDEVRAQDYGYFCRVAMEEALSRQQTPYILVSDVRRKNDIRWFRETYGPERVITLRLTSRPETRSARGWTFTAGIDDVPSECDLDDLADGFDVVLANDEELDQEAIDILLDRLQLQYR
Protein: 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS) (P9WPY5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
Interaction partners:
- Probable shikimate 5-dehydrogenase AroE
- Chorismate synthase
- 3-dehydroquinate synthase
- Shikimate kinase
- Ribosome small subunit-dependent GTPase A
- Cytidylate kinase
- Abasic site processing protein
- Prephenate dehydrogenase
- Phosphoserine aminotransferase
- Intracellular chorismate mutase
Sequence:
MKTWPAPTAPTPVRATVTVPGSKSQTNRALVLAALAAAQGRGASTISGALRSRDTELMLDALQTLGLRVDGVGSELTVSGRIEPGPGARVDCGLAGTVLRFVPPLAALGSVPVTFDGDQQARGRPIAPLLDALRELGVAVDGTGLPFRVRGNGSLAGGTVAIDASASSQFVSGLLLSAASFTDGLTVQHTGSSLPSAPHIAMTAAMLRQAGVDIDDSTPNRWQVRPGPVAARRWDIEPDLTNAVAFLSAAVVSGGTVRITGWPRVSVQPADHILAILRQLNAVVIHADSSLEVRGPTGYDGFDVDLRAVGELTPSVAALAALASPGSVSRLSGIAHLRGHETDRLAALSTEINRLGGTCRETPDGLVITATPLRPGIWRAYADHRMAMAGAIIGLRVAGVEVDDIAATTKTLPEFPRLWAEMVGPGQGWGYPQPRSGQRARRATGQGSGG
Protein: Lipin, isoform L (EC 3.1.3.4) (A0A0B4JD31)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSGEAFFVEECLEDEDEELPANLATSPIPNSFLASRDKANDTMEDISGVVTDKNASEELLLPLPLPRRNSIDFSKEEPKEAVVEGSKFENQVSDYTQRRHTDNTLERRNLSEKLKEFTTQKIRQEWAEHEELFQGEKKPADSDSLDNQSKASNEAETEKAIPAVIEDTEKEKDQIKPDVNLTTVTTSEATKEVSKSKTKKRRKKSQMKKNAQRKNSSSSSLGSAGGGDLPSAETPSLGVSNIDEGDAPISSATNNNNTSSSNDEQLSAPLVTARTGDDSPLSEIPHTPTSNPRLDLDIHFFSDTEITTPVGGGGAGSGRAAGGRPSTPIQSDSELETTMRDNRHVVTEESTASWKWGELPTPEQAKNEAMSAAQVQQSEHQSMLSNMFSFMKRANRLRKEKGVGEVGDIYLSDLDAGSMDPEMAALYFPSPLSKAASPPEEDGESGNGTSLPHSPSSLEEGQKSIDSDFDETKQQRDNNRYLDFVAMSMCGMSEQGAPPSDEEFDRHLVNYPDDAIEQLMSQTVDGKCLPGDEKQEAVAQADNGGQTKRYWWSWRRSQDAAPNHLNNTHGMPLGKDEKDGDQAAVATQTSRPTSPDITDPTLSKSDSLVNAENTSALVDNLEELTMASNKSDEPKERYKKSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRDLFPDKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSYCSMTYIVDQLFPPVKLDEASAEFSNFNYWRDPIPDLEIPELETALVPPSTKVDMATLRPIPEK
Protein: Alpha/beta-Hydrolases superfamily protein (At1g11090) (Lysophospholipase isolog; 25331-24357) (Putative lysophospholipase isolog) (O04083)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Triacylglycerol lipase SDP1L
- Triacylglycerol lipase SDP1
- Alpha/beta-Hydrolases superfamily protein
- Alpha/beta-Hydrolases superfamily protein
- Glycerol kinase
- 
- Aldo-keto reductase family 4 member C10
- Non-specific phospholipase C3
- 
- RHOMBOID-like protein 5
Sequence:
MSDQQLETEINFWGETSEEDYFNLKGIIGSKSFFTSPRGLNLFTRSWLPSSSSPPRGLIFMVHGYGNDVSWTFQSTPIFLAQMGFACFALDIEGHGRSDGVRAYVPSVDLVVDDIISFFNSIKQNPKFQGLPRFLFGESMGGAICLLIQFADPLGFDGAVLVAPMCKISDKVRPKWPVDQFLIMISRFLPTWAIVPTEDLLEKSIKVEEKKPIAKRNPMRYNEKPRLGTVMELLRVTDYLGKKLKDVSIPFIIVHGSADAVTDPEVSRELYEHAKSKDKTLKIYDGMMHSMLFGEPDDNIEIVRKDIVSWLNDRCGGDKTKTQV
Protein: 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34) (Q58ER2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU361219}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU361219}. Peroxisome membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004585}.
Interaction partners:
Sequence:
MMLSRLFRLHGLFVASHPWEVIVGTVAVTMCLMSMNAFAGNDQICGWNHQCPKVQEKIISGDMAILTITRCIAIIYIYIQFKNLRQLGSKYILGIAGLFTIFSSFVFSTVVVHFLGKELTGLNEALPFFLLLIDLSKACTLAKFALSSNSQEEVRENIAQGMAILGPTFTLDAVVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEEGNKPNPVTQRVKMIMSLVLALVHAHSRLKTESPAHNISSSDVVLPTSNMESDRSMSSVDLEQVITLSLALLLAAKYVFFEQAETESSLSIKTTVATPNCSLINRRGGEERCQRDSAPPKAIKGVNENKSEREAPDRSFSIGNPEDEERDKIQCRPVQECLAILKDPKRGAGFLSNAEVMALVESRGILGYRLEAVMESPERGVAIRREMLSGKLPDSSALENLPYKHYDYSKVVGSNCENVIGYVPVPVGVAGPLLLDGKEFHVPMATTEGCLVASTNRGCRAVTLSGGVSSRVLADGMTRGPVVQMPSACRAAEVKGWLESSEGFTEIKQAFDHTSRFARLDRLQVSLAGRNLYIRFQSQTGDAMGMNMLSKGTEQALGRLQERYPDMRLLAVSGNYCTDKKPAAVNWIHGRGKSTVCEAVIPARVVKEVLKSSTAALVELNISKNLVGSAMAGSIGGFNAHAANIVTAIYIACGQDPAQTVGSSNCITLMECVGTSGEDLYVSCTMPSLELGTIGGGTGLPAQHACLQMLGVGGASVQCPGENSRTLARIVCASVLAGELSLMAALAAGHLVQSHMTHNRSKVNLREPEGQPKEAS
Protein: Mechanosensitive ion channel protein 1, mitochondrial (Mechanosensitive channel of small conductance-like 1) (MscS-Like protein 1) (Q8VZL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer.
Subcellular location: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mechanosensitive ion channel protein 10
- Mechanosensitive ion channel protein 8
- Mechanosensitive ion channel protein 4
- Mechanosensitive ion channel-like protein
- Mechanosensitive ion channel protein 5
- Mechanosensitive ion channel protein 9
- Mechanosensitive ion channel protein 6
- Protein MID1-COMPLEMENTING ACTIVITY 2
- Large ribosomal subunit protein eL21z/eL21y
- Mechanosensitive ion channel protein 7
Sequence:
MAGVRLSLLKSIQRSIKPHATAKSCSGLLNSHARAFTCGNLLDGPKASPSMISFSSNIRLHNDAKPFNYLGHSSYARAFSSKSDDFGSIVASGVTGSGDGNGNGNDWVEKAKDVLQTSVDAVTETAKKTKDVSDEMIPHVQQFLDSNPYLKDVIVPVSLTMTGTLFAWVVMPRILRRFHTYAMQSSAKLLPVGFSNEDVPYEKSFWGALEDPARYLVTFIAFAQIAAMVAPTTIAAQYFSPTVKGAVILSLVWFLYRWKTNVITRMLSAKSFGGLDREKVLTLDKVSSVGLFAIGLMASAEACGVAVQSILTVGGVGGVATAFAARDILGNVLSGLSMQFSRPFSMGDTIKAGSVEGQVIEMGLTTTSLLNAEKFPVLVPNSLFSSQVIVNKSRAQWRAIASKIPLQIDDLDMIPQISNEIKEMLRSNTKVFLGKEAPHCYLSRVEKSFAELTIGCNLIRMGKEELYNTQQEVLLEAVKIIKKHGVSLGTTWDNSTL