wanglab/gogpt-training-data huggingface dataset:
Protein: Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Anthrax edema toxin adenylate cyclase component) (Edema factor) (EF) (P40136)
Organism: Bacillus anthracis
Function: Edema factor (EF), which constitutes one of the three proteins composing the anthrax toxin, causes edema in the host. Acts as a calmodulin-dependent adenylyl cyclase by converting ATP to cAMP, leading to dramatic elevation of intracellular cAMP levels in the host, thereby causing edema. EF is not toxic by itself and only acts as a edema factor when associated with protective antigen (PA) to form the edema toxin (EdTx). Required for the survival of germinated spores within macrophages at the early stages of infection.
Subcellular location: Secreted {ECO:0000269|PubMed:3149607}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:1512256}. Note=Translocation into host cytosol is mediated via interaction with the cleaved form of protective antigen (PA-63): following secretion, EF binds via its N-terminal region to the upper rim of the ring-shaped homooligomer (homoheptamer or homooctamer) formed by PA-63 on the host cell membrane (PubMed:32047164). In this PA-63 pre-pore state, the N-terminal segment of EF refolds into an alpha helix engaged in the alpha-clamp of the PA-63 pre-pore (PubMed:32047164, PubMed:32521227). Recruitment to the PA-63 pre-pore enables domain reorganization of EF (PubMed:32521227). Loaded complexes are then endocytosed, followed by a conformational change of oligomerized PA-63 from the pre-pore to pore state, which is triggered by the low pH in the endosome (PubMed:11207582). EF is then unfolded to pass through the PA-63 pore and translocate into the host cytosol (PubMed:32047164). {ECO:0000269|PubMed:11207582, ECO:0000269|PubMed:32047164, ECO:0000269|PubMed:32521227}.
Interaction partners:
Sequence:
MTRNKFIPNKFSIISFSVLLFAISSSQAIEVNAMNEHYTESDIKRNHKTEKNKTEKEKFKDSINNLVKTEFTNETLDKIQQTQDLLKKIPKDVLEIYSELGGEIYFTDIDLVEHKELQDLSEEEKNSMNSRGEKVPFASRFVFEKKRETPKLIINIKDYAINSEQSKEVYYEIGKGISLDIISKDKSLDPEFLNLIKSLSDDSDSSDLLFSQKFKEKLELNNKSIDINFIKENLTEFQHAFSLAFSYYFAPDHRTVLELYAPDMFEYMNKLEKGGFEKISESLKKEGVEKDRIDVLKGEKALKASGLVPEHADAFKKIARELNTYILFRPVNKLATNLIKSGVATKGLNVHGKSSDWGPVAGYIPFDQDLSKKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIEELKENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENNEVQYKTKEGKITVLGEKFNWRNIEVMAKNVEGVLKPLTADYDLFALAPSLTEIKKQIPQKEWDKVVNTPNSLEKQKGVTNLLIKYGIERKPDSTKGTLSNWQKQMLDRLNEAVKYTGYTGGDVVNHGTEQDNEEFPEKDNEIFIINPEGEFILTKNWEMTGRFIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITKAKINTIPTSAEFIKNLSSIRRSSNVGVYKDSGDKDEFAKKESVKKIAGYLSDYYNSANHIFSQEKKRKISIFRGIQAYNEIENVLKSKQIAPEYKNYFQYLKERITNQVQLLLTHQKSNIEFKLLYKQLNFTENETDNFEVFQKIIDEK
Protein: Thiamine metabolism regulatory protein THI3 (EC 4.1.1.72) (Keto isocaproate decarboxylase 1) (Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase) (2ODC) (Q07471)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) and isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), whereas transaminated valine, transaminated aromatic amino acids, and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins. The enzyme is also positively regulating the thiamine metabolism by a molecular mechanism that may involve thiamine concentration sensing and signal transmission.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Alcohol dehydrogenase 4
- NADP-dependent alcohol dehydrogenase 6
- Transketolase 1
- NADP-dependent alcohol dehydrogenase 7
- Dihydrolipoyl dehydrogenase, mitochondrial
- Transketolase 2
- Pyruvate kinase 1
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Transaldolase
Sequence:
MNSSYTQRYALPKCIAISDYLFHRLNQLNIHTIFGLSGEFSMPLLDKLYNIPNLRWAGNSNELNAAYAADGYSRLKGLGCLITTFGVGELSAINGVAGSYAEHVGILHIVGMPPTSAQTKQLLLHHTLGNGDFTVFHRIASDVACYTTLIIDSELCADEVDKCIKKAWIEQRPVYMGMPVNQVNLPIESARLNTPLDLQLHKNDPDVEKEVISRILSFIYKSQNPAIIVDACTSRQNLIEETKELCNRLKFPVFVTPMGKGTVNETDPQFGGVFTGSISAPEVREVVDFADFIIVIGCMLSEFSTSTFHFQYKTKNCALLYSTSVKLKNATYPDLSIKLLLQKILANLDESKLSYQPSEQPSMMVPRPYPAGNVLLRQEWVWNEISHWFQPGDIIITETGASAFGVNQTRFPVNTLGISQALWGSVGYTMGACLGAEFAVQEINKDKFPATKHRVILFMGDGAFQLTVQELSTIVKWGLTPYIFVMNNQGYSVDRFLHHRSDASYYDIQPWNYLGLLRVFGCTNYETKKIITVGEFRSMISDPNFATNDKIRMIEIMLPPRDVPQALLDRWVVEKEQSKQVQEENENSSAVNTPTPEFQPLLKKNQVGY
Protein: Heat shock 70 kDa protein 5 (Heat shock protein 70-5) (AtHsp70-5) (Heat shock protein 70b) (Q9S9N1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Heat shock protein 90-5, chloroplastic
- Chaperone protein ClpB1
- Heat shock protein 90-1
- Heat stress transcription factor A-2
- Heat shock protein 21, chloroplastic
- 22.0 kDa heat shock protein
- 17.6 kDa class II heat shock protein
- 26.5 kDa heat shock protein, mitochondrial
- 17.7 kDa class II heat shock protein
- Ankyrin repeat family protein
Sequence:
MATKSEKAIGIDLGTTYSCVGVWMNDRVEIIPNDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFSDPSVQSDILHWPFKVVSGPGEKPMIVVSYKNEEKQFSPEEISSMVLVKMKEVAEAFLGRTVKNAVVTVPAYFNDSQRQATKDAGAISGLNVLRIINEPTAAAIAYGLDKKGTKAGEKNVLIFDLGGGTFDVSLLTIEEGVFEVKATAGDTHLGGEDFDNRLVNHFVAEFRRKHKKDIAGNARALRRLRTACERAKRTLSSTAQTTIEIDSLHEGIDFYATISRARFEEMNMDLFRKCMDPVEKVLKDAKLDKSSVHDVVLVGGSTRIPKIQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAILTGEGSEKVQDLLLLDVAPLSLGLETAGGVMTVLIPRNTTVPCKKEQVFSTYADNQPGVLIQVYEGERARTRDNNLLGTFELKGIPPAPRGVPQINVCFDIDANGILNVSAEDKTAGVKNQITITNDKGRLSKEEIEKMVQDAEKYKAEDEQVKKKVEAKNSLENYAYNMRNTIKDEKLAQKLTQEDKQKIEKAIDETIEWIEGNQLAEVDEFEYKLKELEGICNPIISKMYQGGAAAGGMPTDGDFSSSGAAGGPKIEEVD
Protein: GH3 domain-containing protein (Q99J23)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:11735219}. Nucleus envelope {ECO:0000269|PubMed:11735219}.
Interaction partners:
Sequence:
MLLLWLLLLLLLLVPLLAILWQQRSRGARPCWLISLQHRVAWGMLGWAAAWQQWRLDRSTLNVGQSQQQALMWCLKKAQGSCCLPREDTDMRTFRNHLPLTQTSHTQEQESEETLPSPASPQYHGDASLQATLLGLITLNKAYPEALAPGSTACVTPTSPWPCSVPWLGHALGRVSPDGAKDPRTLLLEALISPGLRVLEARTAVELLDVFVGLEADGEELAEAIAAGILGTLLPKRAAELKEALEQGPRGLARRLWPKLQVVVTLDSGGQAEAVAALRVLWCQGLAFFSPAYAASGGVVALNLWPERPQGSYLLPPGVPFIELLPIKEGTQEEAASTLLLTDAQREKEYELVLTNHTSLTRCRLGDVVQVVGTYNQCPVVRFTCRLGQTLNVRGEVTDETVFSVALAQAVGQWPGAKLLDHVCVESRVLDSCEGSAPHYEVFVELRGLRNLSEENRDKLDNCLQEASAQYKSLRFRGSVGPAKVHLVRPGSFRVLREALAAFSSSSCRPPEMPRVIRLRHLAQLLQKRVIS
Protein: CRE-MEC-1 protein (Q5ZR41)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MHLFLLFIPHVIAVKDLAWYSANPVLSSSHPVGPAAIQAATAIDFCQLPVDTGKCSQQLVRYYYDAAVDECKRFTFSGCGGNSNRFMRRAHCRNRCVKQPNKPEVQELKHRRTVTSTTSTPFQTVNEESTVEPSATKRLPVTLPVKKLELVQVRIFNKTESGHGNGLCQDCDPLYGTCLDGKCGCMKGFRSLGKVCIDLNECDNGAVCGPNARCVNEIGSFQCVCDAGFSTDGDCKIGQEACMDEFDVNLTEEDCNNGKQEIKYYYDADSVQCKQFFYGGCKTTSRNFFADLQTCDVICVSNQRDYLKSKGQSLSHHPVLEISSDLNNGNDLKSNHYKIDLFSSPSSPVTPNRPLSADDWPLKPITLKPALNLDFSQGKTKSTAEKHKEADDAEILVHQLTPEHNSCDLKFEPVLREECISADWAEKFFWNSEFKDCEPFWYDSSCDPRDRAGKNFFETFEDCKNKCDGVQSQYVVPITTVPDEQSKIEEVETSETPGIVDETTTTAAPEEESEENGFFFKVKPQNYLEDVLSSETEETQHYGFNPNEFLKQNSQNQKPTEITEILRILPAQTEHDEASELKKEDKIEHDILEHLKNKEPTEKVLSTPSTCDLEYDDALRNECTSADWTELYYWNAQFKECEAFWYDSSCGDQDFSKKNLFKNFDDCNNQCVKKIGEALKKMDPETTTTTSTTTTTTTAPTTTKMEEPKRSNYKQSDPLNLILNKALNPDESSELPEKFPPAHEQGFVNFAIKSEVTATTKFDRLKYMAEFRKKLLALPDNFSTTPKQSSPTSSPTTTRMRSPSTHKSTVSQATKTASSTPQSPSTTTSFDDFVEKEKKTVLETIKILDRPEDLCDEPLHPKLEEDCKNDQWEIQWFFNSDRGACKSFWYGGCEIESRNFFPDHANCRHSCAHKYATPASFSSKVYIPPGELSTPVPPRKDRLTTSLKLTYPHSEDLFPSEEHSTVVELDGNFQRTEKQERIRLFPTKTFRPRAPTPTASNIVNVSEGEKTETAPAFYSHIDRVVHDMKTGEHPGYTKPEEFVRRIESASNDYIKYDLQKPDVVTIIDKSPPTVPSRKERTERTEVTTKLPSTRSINDPCDDEYDPKWDEDCLGDTWVVRSYYDSKAEKCKAFWYGGCHTSSRNIWFDKETCRTSCAHKFPTDMPMYGGAQSSEVSAEILPSPQEENSSKETSSSSSSSSSSNTAHISPEHRFKVDLDQKFADVKREHEGREDLAYSQMVQHPVTVSADCLEVYNASLSKPCGDGKSWSNRYFYDKDTRSCRMFWSNGCFSSSKNNFDDLETCQWKCEGRHPQPAGKSCLDKFDERYLEDCRHGEFTNRFYFDHDRKKCVAFHWGGCQSKSQNFFADMTVCQDLCESPPRELTQACLQPFDTTYETSCSAEKPQQYYYFDMSSGICKMFWFGNCKGENQNIFSTLEACQWICERKRDERKPAICADKFDTKYTESCGDSQWTEKWYFDQSSGDCSSFWWDECTSSSQNIFPDEKSCTSNCKHPGFEISSKLATEESKFRCLEPVEIGSCQETYPAFYYDRASRTCRPFAYSGCGGNSNRFMTVSQCENLCFAFNSMNEAEVDCHLPMHIGYGKNEDSCLPQAGFRFYYDRNYGKCSQMWYLGCGGNANNFYSYEICQRTCSQSDVPRELERKTRASSEGRPKFGIRKIRAKVQQL
Protein: Innexin inx2 (Innexin-2) (G-Inx2) (Q9XYN1)
Organism: Schistocerca americana (American grasshopper)
Function: Structural components of the gap junctions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction.
Interaction partners:
Sequence:
MFDVFGSVKGLLKLDSVCIDNNLFRLHYKATVIILIAFSLLVTSRQYIGDPIDCIVDEIPLAVMDTYCWIYSTFTIPNRLNGKIGLEVAHPGVGAHVAGKDEVKYHKYYQWVCFVLFFQAILFYIPRYLWKTWEGGRIKMLVLDLNSPVVNEQSKADRKKLLVDYFATNLHTQNFYAYRFFICEALNFVNVVGQIYFMDLFLDGEFTTYGSDVVRFTEMEPEERSDPMSRVFPKVTKCTFHKYGPSGSVQTFDGLCVLPLNIVNEKIYVFLWFWFVILSVLTGIGLVYRLATAMGPQMRMYLLRARSRLAPQDQIETISNKCQIGDWFVLYQLGKNIDPLIYKELVADLAKKLEGKEIV
Protein: Acyl-coenzyme A diphosphatase FITM2 (EC 3.6.1.-) (FIT family protein fitm-2) (Fat storage-inducing transmembrane homolog 2) (Fat storage-inducing transmembrane protein 2) (Fat-inducing protein 2) (Q5CZ37)
Organism: Caenorhabditis elegans
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). May play a role in the regulation of cell morphology, ER morphology and cytoskeletal organization (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03230}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03230}.
Interaction partners:
- GB1/RHD3-type G domain-containing protein
- GB1/RHD3-type G domain-containing protein
- Microsomal triglyceride transfer protein homolog
Sequence:
MSTRRSSTRADSTTKRPASPNSTPNAALGIFVAIARQILFIDARKVALFYLAFVTVLSFIESRIELDSTYYLVQKHSVLNQYGVKMGWFWTLVIVGPFIWFSSKAHNRRDRDQPIVDVCRLGVGTACWYFSVQFFHKVLALTSMCDKGRTLTRAQCSEKEGVWTPGYDISGHCFLMIYSILIITEEAIAYRHYQQVTDAVHQMDGDREEHDRLTRCIQYFFVAMLFLHAFWFKQIIISVLYYHIFIEEILGAVAAVVCWFVTYRMLYPAGFLASPIRRTVGRK
Protein: 26S proteasome non-ATPase regulatory subunit 6 (26S proteasome regulatory subunit RPN7) (26S proteasome regulatory subunit S10) (Breast cancer-associated protein SGA-113M) (Phosphonoformate immuno-associated protein 4) (Proteasome regulatory particle subunit p44S10) (p42A) (Q15008)
Organism: Homo sapiens (Human)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Interaction partners:
- Proteasomal ubiquitin receptor ADRM1
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-7
- Proteasome subunit beta type-4
- Ubiquitin carboxyl-terminal hydrolase 14
- Proteasome subunit alpha type-2
- 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 11
Sequence:
MPLENLEEEGLPKNPDLRIAQLRFLLSLPEHRGDAAVRDELMAAVRDNNMAPYYEALCKSLDWQIDVDLLNKMKKANEDELKRLDEELEDAEKNLGESEIRDAMMAKAEYLCRIGDKEGALTAFRKTYDKTVALGHRLDIVFYLLRIGLFYMDNDLITRNTEKAKSLIEEGGDWDRRNRLKVYQGLYCVAIRDFKQAAELFLDTVSTFTSYELMDYKTFVTYTVYVSMIALERPDLREKVIKGAEILEVLHSLPAVRQYLFSLYECRYSVFFQSLAVVEQEMKKDWLFAPHYRYYVREMRIHAYSQLLESYRSLTLGYMAEAFGVGVEFIDQELSRFIAAGRLHCKIDKVNEIVETNRPDSKNWQYQETIKKGDLLLNRVQKLSRVINM
Protein: Chromosome partition protein MukE (Protein KicA) (P22524)
Organism: Escherichia coli (strain K12)
Function: Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Probably acts via its interaction with MukB and MukF.
Subcellular location: Cytoplasm, nucleoid. Note=Restricted to the nucleoid region.
Interaction partners:
- Chromosome partition protein MukF
- Chromosome partition protein MukB
- tRNA 5-carboxymethoxyuridine methyltransferase
- Methylmalonyl-CoA decarboxylase
- Macrodomain Ter protein
- Methylmalonyl-CoA mutase
Sequence:
MSSTNIEQVMPVKLAQALANPLFPALDSALRSGRHIGLDELDNHAFLMDFQEYLEEFYARYNVELIRAPEGFFYLRPRSTTLIPRSVLSELDMMVGKILCYLYLSPERLANEGIFTQQELYDELLTLADEAKLLKLVNNRSTGSDVDRQKLQEKVRSSLNRLRRLGMVWFMGHDSSKFRITESVFRFGADVRAGDDPREAQRRLIRDGEAMPIENHLQLNDETEENQPDSGEEE
Protein: Something about silencing protein 4 (Q04003)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SAS complex, a multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS complex is however unable to acetylate nucleosomal histones. The complex is involved in transcriptional silencing at telomeres and at HML locus. Also involved in rDNA silencing. In the complex, SAS4 is essential for histone acetyltransferase (HAT) activity of the complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:11731480}.
Interaction partners:
- Histone acetyltransferase SAS2
- Something about silencing protein 5
- Histone chaperone ASF1
- Histone acetyltransferase ESA1
- SWR1-complex protein 4
- Chromatin modification-related protein YNG2
- Chromatin modification-related protein EAF1
- Actin
- Chromatin modification-related protein EAF7
- Chromatin modification-related protein EAF6
Sequence:
MGIFQSIEEANNTSERLLRSEIKNSHGEFEKFDFDTEEYEINPKRKLRLVSRINPNAGHLRKSKSCFTVDEHVDETRCQKPVMKSPFMSNVDDEIKKKRETITKMTLEIEHHELSQNIRKPTDDLLPDSTYQPYHKKMLKQENRMIQSDIVNGENEADRLSLISDRLGMLNWEVTLQKVTKINDPTDENEMETKRYQTKELIDSMLHKFESMKKKSRNLARRPASSDSLLKLVSGKDWPKIYTRIDRTFIPDYASSSDEEEEKITVEEIRERRLKKREQQCGGSIIVLLSDHQSQKGMTRFAIVAEPLRKPYLIKTSTKERNSWKNKVPTNPKKFKKAPRISTQIAVKRRREVIPLTMEVEPEVIRDIRQDTQKSMKLNVKAEEISVTETVKSKEMNALRNNAASISPTLSEKAPLGSISSCTASQISQRSSENVGAIINNINPNLAIVPSCNEKTFVKTHNGMKTNSGINILPVRKKKKV
Protein: Mitogen-activated protein kinase kinase 2 (AtMAP2Kbeta) (AtMKK2) (MAP kinase kinase 2) (EC 2.7.12.2) (Q9S7U9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: MEKK1, MKK1/MKK2 and MPK4 function in a signaling pathway that modulates the expression of genes responding to biotic and abiotic stresses and also plays an important role in pathogen defense by negatively regulating innate immunity. Plays a role in abiotic stress tolerance and plant disease resistance through activation of MPK4 and MPK6 by phosphorylation. Acts redundantly with MKK1.
Interaction partners:
- Mitogen-activated protein kinase 4
- Mitogen-activated protein kinase 6
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase kinase kinase 1
- Mitogen-activated protein kinase kinase 1
- Mitogen-activated protein kinase 5
- Mitogen-activated protein kinase 13
- Disease resistance protein SUMM2
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 7
Sequence:
MKKGGFSNNLKLAIPVAGEQSITKFLTQSGTFKDGDLRVNKDGVRIISQLEPEVLSPIKPADDQLSLSDLDMVKVIGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKAIAQELKINQSSQCPNLVTSYQSFYDNGAISLILEYMDGGSLADFLKSVKAIPDSYLSAIFRQVLQGLIYLHHDRHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYAPPNQEETWTSVFELMEAIVDQPPPALPSGNFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYDYSGINLASYFTDAGSPLATLGNLSGTFSV
Protein: Kank, isoform I (A0A0B4KF63)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPMILRKLKYELLRYSCIGGNQSPTGTPRPFLRSNTLPLRQRPSPAEVQYESYVQATVAANAKSPVEQLESAKSPGAPPPPPPRRHHLLATTPTGKPTFKEDRPQENGSVSSSSLQSPVISETGQTTADAQALFQIREQMALSLRRLKDLEEQVKVIPDMELELNSLRSEKQKLLRRNEELMRSQRQTPSPPSPGLKTASPVQFTPQRISPVSLESLGARMRSSSTSASPSPSVVRRDVSTQAVVRPPATRDVSVGHQPTTRNVGVQPSETVYSKEELDKKVEQALTNAQKQQLRKLISVGTQMYVPQRDQKDSGVQTTPERPKLKYHVGVTVKPATRENFTSCKPDVRHVGSSDDRLDDVLCEKCAVSKRSVACGPETPAEKVKPAPQMPGRSNTFSLGENETVSVVRKTIGCQTPVTLVLSSGSQTTTAVVRSTGAQVNPQQQHSGVQCATEQVSRQTDTKGLQRLTRSQTKAEQVSESVPRPTTRHTASNTDKVEEAEPAKVRTSHSACNTEEVRKRDVGCGDIVKPHISIACAANYCDSCKEAIQDLARGFSKASPTATRTGGAVRRSTSADSRIPRPKHLSSPSPVRKEFMRQNTYTLATPSPTPSPQVERKARLSSLQEKPPSVSSFQASEPLPESQSFIRQPQKDSLDLSLLGEDELIVREEKRVSISWSRDASPAPLMTSSGTTKSESPEQEPAMSSSSDSSPPIDVQIAQGARKKSSTPLKSSQSEGSQVTVIEQPATKAQLHQLAQADSEPRKKTELSQSLKDALKIINDSLLKKLGAKPISSQSLKSAKATIQDHWFTNSSTGKSDPHQVEDYLDYFESLSIPLLEYCVNLSDSNGNTAMHYAVSHGNFDVVSILLDSKVCDVNQMNNAGYTSVMLVSLAKLKQPAHRTVVERLFKMADVNIRAKKHCQTALMLAVSHGNGDMVNMLLDAGADINIQDEDGSTALMCAAEHGRVDVIKHLLSHPECDSLVTDVDGSTAFKIAWQAGHRDVGLLIYVHEQMLRSKLPNRGDATRSSLISPPRHKRQPSQ
Protein: HEAT repeat-containing protein 1 (Q5T3Q7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU367065}.
Interaction partners:
Sequence:
MTSLAQQLQRLALPQSDASLLSRDEVASLLFDPKEAATIDRDTAFAIGCTGLEELLGIDPSFEQFEAPLFSQLAKTLERSVQTKAVNKQLDENISLFLIHLSPYFLLKPAQKCLEWLIHRFHIHLYNQDSLIACVLPYHETRIFVRVIQLLKINNSKHRWFWLLPVKQSGVPLAKGTLITHCYKDLGFMDFICSLVTKSVKVFAEYPGSSAQLRVLLAFYASTIVSALVAAEDVSDNIIAKLFPYIQKGLKSSLPDYRAATYMIICQISVKVTMENTFVNSLASQIIKTLTKIPSLIKDGLSCLIVLLQRQKPESLGKKPFPHLCNVPDLITILHGISETYDVSPLLHYMLPHLVVSIIHHVTGEETEGMDGQIYKRHLEAILTKISLKNNLDHLLASLLFEEYISYSSQEEMDSNKVSLLNEQFLPLIRLLESKYPRTLDVVLEEHLKEIADLKKQELFHQFVSLSTSGGKYQFLADSDTSLMLSLNHPLAPVRILAMNHLKKIMKTSKEGVDESFIKEAVLARLGDDNIDVVLSAISAFEIFKEHFSSEVTISNLLNLFQRAELSKNGEWYEVLKIAADILIKEEILSENDQLSNQVVVCLLPFMVINNDDTESAEMKIAIYLSKSGICSLHPLLRGWEEALENVIKSTKPGKLIGVANQKMIELLADNINLGDPSSMLKMVEDLISVGEEESFNLKQKVTFHVILSVLVSCCSSLKETHFPFAIRVFSLLQKKIKKLESVITAVEIPSEWHIELMLDRGIPVELWAHYVEELNSTQRVAVEDSVFLVFSLKKFIYALKAPKSFPKGDIWWNPEQLKEDSRDYLHLLIGLFEMMLNGADAVHFRVLMKLFIKVHLEDVFQLFKFCSVLWTYGSSLSNPLNCSVKTVLQTQALYVGCAMLSSQKTQCKHQLASISSPVVTSLLINLGSPVKEVRRAAIQCLQALSGVASPFYLIIDHLISKAEEITSDAAYVIQDLATLFEELQREKKLKSHQKLSETLKNLLSCVYSCPSYIAKDLMKVLQGVNGEITKPFFAAISDEKVQQKLLRMLFDLLVNCKNSHCAQTVSSVFKGISVNAEQVRIELEPPDKAKPLGTVQQKRRQKMQQKKSQDLESVQEVGGSYWQRVTLILELLQHKKKLRSPQILVPTLFNLLSRCLEPLPQEQGNMEYTKQLILSCLLNICQKLSPDGGKIPKDILDEEKFNVELIVQCIRLSEMPQTHHHALLLLGTVAGIFPDKVLHNIMSIFTFMGANVMRLDDTYSFQVINKTVKMVIPALIQSDSGDSIEVSRNVEEIVVKIISVFVDALPHVPEHRRLPILVQLVDTLGAEKFLWILLILLFEQYVTKTVLAAAYGEKDAILEADTEFWFSVCCEFSVQHQIQSLMNILQYLLKLPEEKEETIPKAVSFNKSESQEEMLQVFNVETHTSKQLRHFKFLSVSFMSQLLSSNNFLKKVVESGGPEILKGLEERLLETVLGYISAVAQSMERNADKLTVKFWRALLSKAYDLLDKVNALLPTETFIPVIRGLVGNPLPSVRRKALDLLNNKLQQNISWKKTIVTRFLKLVPDLLAIVQRKKKEGEEEQAINRQTALYTLKLLCKNFGAENPDPFVPVLNTAVKLIAPERKEEKNVLGSALLCIAEVTSTLEALAIPQLPSLMPSLLTTMKNTSELVSSEVYLLSALAALQKVVETLPHFISPYLEGILSQVIHLEKITSEMGSASQANIRLTSLKKTLATTLAPRVLLPAIKKTYKQIEKNWKNHMGPFMSILQEHIGVMKKEELTSHQSQLTAFFLEALDFRAQHSENDLEEVGKTENCIIDCLVAMVVKLSEVTFRPLFFKLFDWAKTEDAPKDRLLTFYNLADCIAEKLKGLFTLFAGHLVKPFADTLNQVNISKTDEAFFDSENDPEKCCLLLQFILNCLYKIFLFDTQHFISKERAEALMMPLVDQLENRLGGEEKFQERVTKHLIPCIAQFSVAMADDSLWKPLNYQILLKTRDSSPKVRFAALITVLALAEKLKENYIVLLPESIPFLAELMEDECEEVEHQCQKTIQQLETVLGEPLQSYF
Protein: Transcription initiation factor TFIID subunit 6 (C9JTY6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAEEKKLKLSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHAQEFIPFRFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLKSAKPGQEEDGPLKGKGQGATTADGKGKEKKAPPLLEGAPLRLKPRSIHELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVQNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKHCAPVLAKLRPPPDNQDAYRAEFGSLGPLLCSQVVKARAQAALQAQQVNRTTLTITQVLSLSTSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATTAPPSTAPSGPGSVQKYIVVSLPPTGEGKGGPTSHPSPVPPPASSPSPLSGSALCGGKQEAGDSPPPAPGTPKANGSQPNSGSPQPAP
Protein: Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Benzoate--CoA ligase) (EC 6.2.1.25) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1) (Xenobiotic/medium-chain fatty acid-CoA ligase HXM-B) (Q08AH1)
Organism: Homo sapiens (Human)
Function: Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism. Capable of activating medium-chain fatty acids (e.g. butyric (C4) to decanoic (C10) acids), and certain carboxylate-containing xenobiotics, e.g. benzoate. Also catalyzes the activation of lipoate to lipoyl-nucleoside monophosphate (By similarity). Activates lipoate with GTP at a 1000-fold higher rate than with ATP and activates both (R)- and (S)-lipoate to the respective lipoyl-GMP, with a preference for (R)-lipoate (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q91VA0}. Mitochondrion {ECO:0000250|UniProtKB:Q91VA0}.
Interaction partners:
- Lipoyl amidotransferase LIPT1, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Solute carrier family 22 member 16
- Guanylate-binding protein 5
- Hydroxysteroid dehydrogenase-like protein 2
Sequence:
MQWLMRFRTLWGIHKSFHNIHPAPSQLRCRSLSEFGAPRWNDYEVPEEFNFASYVLDYWAQKEKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPRVPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCPSLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM