wanglab/gogpt-training-data huggingface dataset:
Protein: Heat shock transcription factor 1 (F1MAF1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock protein HSP 90-beta
- Heat shock 70 kDa protein 4
- DnaJ heat shock protein family
- Elongation factor 1-alpha 1
- Elongation factor 1-alpha 2
- Transitional endoplasmic reticulum ATPase
- Heat shock 70 kDa protein 1A
- STIP1 homology and U-Box containing protein 1, isoform CRA_b.
- Prostaglandin E synthase 3
Sequence:
MDLAVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTRLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLSDSSSAHSVPKYGRQYSLEHVHGPGPYSAPSPAYSSSSLYSSDAVTSSGPIISDITELAPTSPLASPGRSIDERPLSSSTLVRVKEEPPSPPHSPRVLEASPGRPASMDTPLSPTAFIDSILRESEPTPAASNTAPMDTTGAQAPAPPAPSTPEKCLSVACLDNLARAPQMSGVARLFPCPSSFLHGRVQPGNELSDHLDAMDSNLDNLQTMLTSHGFSVDTSALLDLFSPSVTMPDMSLPDLDSSLASIQELLSPQEPPRPIEAENSNADSGKQLVHYTAQPLFLLDPDAVDTGSSELPVLFELGESSYFSEGDDYTDDPTISLLTGTEPHKAKDPTVS
Protein: Pro-MCH [Cleaved into: Neuropeptide-glycine-glutamic acid (NGE) (Neuropeptide G-E); Neuropeptide-glutamic acid-isoleucine (NEI) (Neuropeptide E-I); Melanin-concentrating hormone (MCH)] (P14200)
Organism: Rattus norvegicus (Rat)
Function: MCH inhibits ACTH secretion at the end of the light on period which corresponds to the peak of the circadian rhythm in ACTH. Inhibits also stress induced ACTH release during the light off period of the cycle. Involved as a neurotransmitter or neuromodulator in a broad array of neuronal functions. Stimulates sexual behavior when injected into the ventromedial nucleus, this effect is antagonized by NEI. In the medial preoptic area, stimulates anxiety and sexual behavior. Antagonizes inhibitory effect of melanotropin alpha on exploration behavior.
Subcellular location: Secreted.
Interaction partners:
- Hypocretin neuropeptide precursor
- Melanin-concentrating hormone receptor 1
- Pro-neuropeptide Y
- Agouti-related protein
- Pro-opiomelanocortin
- Oxytocin-neurophysin 1
- Adenylyl cyclase-associated protein 1
- Cholecystokinin
- Galanin peptides
- Corticoliberin
Sequence:
MAKMSLSSYMLMLAFSLFSHGILLSASKSIRNVEDDIVFNTFRMGKAFQKEDTAERSVVAPSLEGYKNDESGFMKDDDDKTTKNTGSKQNLVTHGLPLSLAVKPYLALKGPAVFPAENGVQNTESTQEKREIGDEENSAKFPIGRRDFDMLRCMLGRVYRPCWQV
Protein: Chymase (EC 3.4.21.39) (Alpha-chymase) (Mast cell protease I) (P23946)
Organism: Homo sapiens (Human)
Function: Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.
Subcellular location: Secreted. Cytoplasmic granule. Note=Mast cell granules.
Interaction partners:
- Mast cell carboxypeptidase A
- Tyrosine-protein kinase Fyn
- Angiotensinogen
- Kit ligand
- Carboxypeptidase A4
- Angiotensin-converting enzyme
- High affinity immunoglobulin epsilon receptor subunit beta
- Dipeptidyl peptidase 1
- Renin
- Tryptase alpha/beta-1
Sequence:
MLLLPLPLLLFLLCSRAEAGEIIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
Protein: Scamp, isoform D (Q8IR34)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGSGLDENPFGEPNLDNPFADPAIQQARRLQSGAALVSLEDYNPFEEQAKPQLQINSTNTAAVVQPLSQNIPPPQTSSLGASAPSTSIQITSEELQVTHLAGRLALPPTQQ
Protein: Protein SIC1 (CDK inhibitor p40) (P38634)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate and inhibitor of the cyclin-dependent protein kinase CDC28. Its activity could be important for faithful segregation of chromosomes to daughter cells. It acts in response to a signal from a post-start checkpoint.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cell division control protein 4
- G2/mitotic-specific cyclin-2
- Cyclin-dependent kinase 1
- S-phase entry cyclin-5
- G1/S-specific cyclin CLN2
- Tyrosine-protein phosphatase CDC14
- APC/C activator protein CDH1
- Cell division control protein 15
- Cell cycle protein kinase DBF2
- Protein TEM1
Sequence:
MTPSTPPRSRGTRYLAQPSGNTSSSALMQGQKTPQKPSQNLVPVTPSTTKSFKNAPLLAPPNSNMGMTSPFNGLTSPQRSPFPKSSVKRTLFQFESHDNGTVREEQEPLGRVNRILFPTQQNVDIDAAEEEEEGEVLLPPSRPTSARQLHLSLERDEFDQTHRKKIIKDVPGTPSDKVITFELAKNWNNNSPKNDARSQESEDEEDIIINPVRVGKNPFASDELVTQEIRNERKRAMLRENPDIEDVITYVNKKGEVVEKRRLTDEEKRRFKPKALFQSRDQEH
Protein: Pleckstrin homology domain containing A5 (cDNA FLJ59284, highly similar to Pleckstrin homology domain-containing family A member 5) (B4DJX4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTSEEKKERPISMINEASNYNVTSDYAVHPMSPVGRTSRASKKVHNFGKRSNSIKRNPNAPVVRRGWLYKQDSTGMKLWKKRWFVLSDLCLFYYRDEKEEGILGSILLPSFQIALLTSEDHINRKYAFKAAHPNMRTYYFCTDTGKEMELWMKAMLDAALVQTEPVKRVDKITSENAPTKETNNIPNHRVLIKPEIQNNQKNKEMSKIEEKKALEAEKYGFQKDGQDRPLTKINSVKLNSLPSEYESGSACPAQTVHYRPINLSSSENKIVNVSLADLRGGNRPNTGPLYTEADRVIQRTNSMQQLEQWIKIQKGRGHEEETRGVISYQTLPRNMPSHRAQIMARYPEGYRTLPRNSKTRPESICSVTPSTHDKTLGPGAEEKRRSMRDDTMWQLYEWQQRQFYNKQSTLPRHSTLSSPKTMVNISDQTMHSIPTSPSHGSIAAYQGYSPQRTYRSEVSSPIQRGDVTIDRRHRAHHPKHVYVPDRRSVPAGLTLQSVSPQSLQGKTLSQDEGRGTLYKYRPEEVDIDAKLSRLCEQDKVVHALEEKLQQLHKEKYTLEQALLSASQEIEMHADNPAAIQTVVLQRDDLQNGLLSTCRELSRATAELERAWREYDKLEYDVTVTRNQMQEQLDHLGEVQTESAGIQRAQIQKELWRIQDVMEGLSKHKQQRGTTEIGMIGSKPFSTVKYKNEEEEVVPPRPPLPRSYDFTEQPPIIPPLPSDSSSLLCYSRGPVHLPEEKKMYQVQGYPRNGSHCGPDYRLYKSEPELTTVAEVDESNGEEKSEPVSEIETSVVKGSHFPVGVVPPRAKSPTPESSTIASYVTLRKTKKMMDLRTERPRSAVEQLCLAESTRPRMTVEEQMERIRRHQQACLREKKKGLNVIGASDQSPLQSPSNLRDNPFRTTQTRRRDDKELDTAIRENDVKPDHETPATEIVQLKETEPQNVDFSKELKKTENISYEMLFEPEPNGVNSVEMMD
Protein: Gremlin-1 (Cell proliferation-inducing gene 2 protein) (Cysteine knot superfamily 1, BMP antagonist 1) (DAN domain family member 2) (Down-regulated in Mos-transformed cells protein) (Increased in high glucose protein 2) (IHG-2) (O60565)
Organism: Homo sapiens (Human)
Function: Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as a BMP antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4 signaling in a dose-dependent manner (By similarity). Antagonist of BMP2; inhibits BMP2-mediated differentiation of osteoblasts (in vitro). Acts as inhibitor of monocyte chemotaxis. Can inhibit the growth or viability of normal cells but not transformed cells when is overexpressed (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Bone morphogenetic protein 2
- Bone morphogenetic protein 4
- Bone morphogenetic protein 7
- Gremlin-2
- Formin-1
- Sonic hedgehog protein
- Noggin
- Bone morphogenetic protein 6
- Bone morphogenetic protein 5
- Fibroblast growth factor 4
Sequence:
MSRTAYTVGALLLLLGTLLPAAEGKKKGSQGAIPPPDKAQHNDSEQTQSPQQPGSRNRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD
Protein: CCR4-NOT transcription complex subunit 10 (CNOT10) (Q9V3G6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Is not required for association of CNOT7 to the CCR4-NOT complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Not1, isoform H
- Regulator of gene activity
- CCR4-NOT transcription complex subunit 9
- CCR4-NOT transcription complex subunit 11
- CCR4-NOT transcription complex subunit 3
- poly
- CCR4-NOT transcription complex subunit 4
- poly
- FI22161p1
- IP12282p
Sequence:
MDSAESPTKTQAGEDENYSLLCQAHEQFNNSEFDRCLELLQELETRGESSGPVLRHNRAVVSYYKTGCTQHSVLLKELEALTADADAPGDVSSGLSLKQGAAAATVARYNRAVIYYHRHMFGTALEKLAPLVARLEALEKAMAALVATLQLQLLLATNQLNRAEAFLDYLQYKLNLVATAPSSNAAEEAAVVGTAPPSAATNSSVVASPGGAAVEGAVPGLGGSLQLLQLITLVLNRKPVVIQEDGTPEYAALKAQQYYIMKDFQMAAKQLMRINNECTQAGTITPQLSTCIANNMGVIHLRVRHYAIAAKFFQNALNFDQQLARNLRQSTLQTMSSARSCEILYNLGVAMLHLRRPKEAFQCFLVPVKQFHSNPRLWLRMAEACIMEHEAKLVEEERQSQSETPSTKPYAPQSAGVPEPTLEFAVLCLRSALTLTQHYKTRFHMAAVSSEDVEAPEPKDPTQESWRHPQDNNFCNPSKPVSLESLENMMAAIYAAHSFVSLRLGDHVTALEMSEKLLACERLSDAHKLLGHMYAGEALMLMDKASEARDHLDPTFVGTLNAFDFETRDWQLKSVDAAQNVVRYNLAVAMALQNDLPQAKALLANLTHSLVANKALALRRFMDLKMGPVPGGTPS
Protein: Myosin light chain kinase 2, skeletal/cardiac muscle (MLCK2) (EC 2.7.11.18) (P20689)
Organism: Rattus norvegicus (Rat)
Function: Implicated in the level of global muscle contraction and cardiac function (By similarity). Phosphorylates a specific serine in the N-terminus of a myosin light chain.
Subcellular location: Cytoplasm {ECO:0000250}. Note=Colocalizes with phosphorylated myosin light chain (RLCP) at filaments of the myofibrils. {ECO:0000250}.
Interaction partners:
- Calmodulin-like protein 4
- Myosin light chain 3
- Myosin regulatory light polypeptide 9
- Myosin regulatory light chain RLC-A
- Myosin regulatory light chain 12B
- Calmodulin-1
- Myosin light polypeptide 6
- Calmodulin-like protein 3
- Myosin light chain 4
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MATENGAVELGTQSLSTDHPPTDAAGDGSPASEKEPSLPDTEKDLGPTNTKKDPGAPDPKKNPDPPSLKKTPEAPGPEKKGDSAPASASNQGPSGEGDGGGGPAEGGTGPPAVLPQPTATADASIQKLDATQAPSGNQESGEAKAGKKAAECREAGRRGSPAFLHSPSCPAIISCSEKTLAMKPLSETTELIFAGVSETPDPQDPGPAKDEGGTNTLADGKEEAEAGQAEQAKVQGDTSQRIGFQAVPSERAEVGQALCLTAKEEDCFQILDDCPPPPAPFPHRIVELRTGNVSSEFSMNSKEALGGGKFGAVCTCTERSTGLKLAAKVIKKQTPKDKEMVLLEIEVMNQLNHRNLIQLYSAIETSHEIILFMEYIEGGELFERIVDEDYQLTEVDTMVFVRQICDGILFMHKMRVLHLDLKPENILCVNTTGHLVKIIDFGLARRYNPNEKLKVNFGTPEFLSPEVVNYDQISDKTDMWSLGVITYMLLSGLSPFLGDDDTETLNNVLSANWYFDEETFEAVSDEAKDFVSNLITKDQSARMSAEQCLAHPWLNNLAEKAKRCNRRLKSQILLKKYLMKRRWKKNFIAVSAANRFKKISSSGALMALGV
Protein: Malonyl CoA-acyl carrier protein transacylase (MCT) (EC 2.3.1.39) (P0AAI9)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Enoyl-[acyl-carrier-protein] reductase FabI
- Acyl carrier protein
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Biotin carboxylase
Sequence:
MTQFAFVFPGQGSQTVGMLADMAASYPIVEETFAEASAALGYDLWALTQQGPAEELNKTWQTQPALLTASVALYRVWQQQGGKAPAMMAGHSLGEYSALVCAGVIDFADAVRLVEMRGKFMQEAVPEGTGAMAAIIGLDDASIAKACEEAAEGQVVSPVNFNSPGQVVIAGHKEAVERAGAACKAAGAKRALPLPVSVPSHCALMKPAADKLAVELAKITFNAPTVPVVNNVDVKCETNGDAIRDALVRQLYNPVQWTKSVEYMAAQGVEHLYEVGPGKVLTGLTKRIVDTLTASALNEPSAMAAALEL
Protein: Heat shock protein 68 (O97125)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heat shock protein 83
- Heat shock protein 26
- Heat shock protein 23
- DnaJ protein homolog 1
- Heat shock protein 22
- Heat shock protein 27
- DnaJ-like-2, isoform A
- Stress-induced-phosphoprotein 1
- Heat shock protein 67B3
- Hsc70Cb, isoform G
Sequence:
MPAIGIDLGTTYSCVGVFQYGKVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPKNSVFDAKRLIGRRFDDSKIQEDIKHWPFKVINDNGKPKISVEFKGANKCFSPEEISSMVLTKMKETAEAYLGTTVKDAVITVPAYFNDSQRQATKDAGAIAGINVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSILTIDEGSLFEVRSTAGDTHLGGEDFDNRLVNHFAEEFKRKYKKDLRSNPRALRRLRTAAERAKRTLSSSTEASLEIDALYEGHDFYSKVSRARFEELCGDLFRNTLEPVEKALKDAKMDKSQIHDIVLVGGSTRIPKVQNLLQNFFGGKTLNLSINPDEAVAYGAAIQAAILSGDKSSEIKDVLLVDVAPLSLGIETAGGVMTKLIERNSRIPCKQSKTFTTYADNQPAVTIQVFEGERALTKDNNVLGTFDLTGVPPAPRGVPKIDVTFDLDANGILNVTAKEQGTGNAKNITIKNDKGRLSQADIDRMLSEAEKYAEEDERHRQRIAARNQLETYLFGVKEAAENGGDRISAADKSSIVERCSEAMKWLDSNTTAEKEEYEYKLKELEQFCSPIMTKMHKGGGDGQQAPNFGQQAGGYKGPTVEEVD
Protein: Multimerin-2 (EMILIN-3) (Elastin microfibril interface located protein 3) (Elastin microfibril interfacer 3) (EndoGlyx-1 p125/p140 subunit) (Q9H8L6)
Organism: Homo sapiens (Human)
Function: Inhibits endothelial cells motility and acts as a negative regulator of angiogenesis; it down-regulates KDR activation by binding VEGFA.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11559704}.
Interaction partners:
- C-type lectin domain family 14 member A
- Harmonin-binding protein USHBP1
- Roundabout homolog 4
Sequence:
MILSLLFSLGGPLGWGLLGAWAQASSTSLSDLQSSRTPGVWKAEAEDTGKDPVGRNWCPYPMSKLVTLLALCKTEKFLIHSQQPCPQGAPDCQKVKVMYRMAHKPVYQVKQKVLTSLAWRCCPGYTGPNCEHHDSMAIPEPADPGDSHQEPQDGPVSFKPGHLAAVINEVEVQQEQQEHLLGDLQNDVHRVADSLPGLWKALPGNLTAAVMEANQTGHEFPDRSLEQVLLPHVDTFLQVHFSPIWRSFNQSLHSLTQAIRNLSLDVEANRQAISRVQDSAVARADFQELGAKFEAKVQENTQRVGQLRQDVEDRLHAQHFTLHRSISELQADVDTKLKRLHKAQEAPGTNGSLVLATPGAGARPEPDSLQARLGQLQRNLSELHMTTARREEELQYTLEDMRATLTRHVDEIKELYSESDETFDQISKVERQVEELQVNHTALRELRVILMEKSLIMEENKEEVERQLLELNLTLQHLQGGHADLIKYVKDCNCQKLYLDLDVIREGQRDATRALEETQVSLDERRQLDGSSLQALQNAVDAVSLAVDAHKAEGERARAATSRLRSQVQALDDEVGALKAAAAEARHEVRQLHSAFAALLEDALRHEAVLAALFGEEVLEEMSEQTPGPLPLSYEQIRVALQDAASGLQEQALGWDELAARVTALEQASEPPRPAEHLEPSHDAGREEAATTALAGLARELQSLSNDVKNVGRCCEAEAGAGAASLNASLHGLHNALFATQRSLEQHQRLFHSLFGNFQGLMEANVSLDLGKLQTMLSRKGKKQQKDLEAPRKRDKKEAEPLVDIRVTGPVPGALGAALWEAGSPVAFYASFSEGTAALQTVKFNTTYINIGSSYFPEHGYFRAPERGVYLFAVSVEFGPGPGTGQLVFGGHHRTPVCTTGQGSGSTATVFAMAELQKGERVWFELTQGSITKRSLSGTAFGGFLMFKT
Protein: Histone H1 (Q9P8F8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Could act as an H1-type linker histone.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}.
Interaction partners:
- Histone H2A
- Cyclin-dependent kinase 1
- Histone H4.1
- Possible replication factor-a protein
- OB-fold nucleic acid binding domain
- Histone H4.2
- Importin-95
- Histone H2B
- Histone H3
- Histone H2A.Z
Sequence:
MPPKKAPTTAKKAASGPTHTSYRDMIKDAILNLKERNGSSRQSIKKYVLANNKLAPASQNAFDSQFNKAIKAGVEKGDFIQPKGTSGPVKLAKKQAPAKPAPKKPATTTKTAAPKKTATKKADKAEKAEKPKTKKTNAGVKKPAGRPKANTAKPRKASTAAPAVVDKPKVVSVTKSGRKTTTTAKPTEKATKKTAKNKKA
Protein: D-xylose-proton symporter (D-xylose transporter) (P0AGF4)
Organism: Escherichia coli (strain K12)
Function: Uptake of D-xylose across the boundary membrane with the concomitant transport of protons into the cell (symport system). Glucose is not transported, but can compete for xylose binding sites and can inhibit xylose transport (in vitro).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:23075985}; Multi-pass membrane protein {ECO:0000269|PubMed:23075985}.
Interaction partners:
- Xylose isomerase
- L-fucose-proton symporter
- Lactose permease
- Xylulose kinase
- D-xylose-binding periplasmic protein
- Xylose import ATP-binding protein XylG
- Xylose operon regulatory protein
- Inner membrane transport protein YajR
Sequence:
MNTQYNSSYIFSITLVATLGGLLFGYDTAVISGTVESLNTVFVAPQNLSESAANSLLGFCVASALIGCIIGGALGGYCSNRFGRRDSLKIAAVLFFISGVGSAWPELGFTSINPDNTVPVYLAGYVPEFVIYRIIGGIGVGLASMLSPMYIAELAPAHIRGKLVSFNQFAIIFGQLLVYCVNYFIARSGDASWLNTDGWRYMFASECIPALLFLMLLYTVPESPRWLMSRGKQEQAEGILRKIMGNTLATQAVQEIKHSLDHGRKTGGRLLMFGVGVIVIGVMLSIFQQFVGINVVLYYAPEVFKTLGASTDIALLQTIIVGVINLTFTVLAIMTVDKFGRKPLQIIGALGMAIGMFSLGTAFYTQAPGIVALLSMLFYVAAFAMSWGPVCWVLLSEIFPNAIRGKALAIAVAAQWLANYFVSWTFPMMDKNSWLVAHFHNGFSYWIYGCMGVLAALFMWKFVPETKGKTLEELEALWEPETKKTQQTATL
Protein: 3-oxoacyl-[acyl-carrier-protein] synthase 1 (EC 2.3.1.41) (3-oxoacyl-[acyl-carrier-protein] synthase I) (Beta-ketoacyl-ACP synthase I) (KAS I) (P0A953)
Organism: Escherichia coli (strain K12)
Function: Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can also use unsaturated fatty acids. Catalyzes a key reaction in unsaturated fatty acid (UFA) synthesis, the elongation of the cis-3-decenoyl-ACP produced by FabA. Can use acyl chains from C-6 to C-14. Has an absolute requirement for an ACP substrate as the acyl donor, and no activity is detected when both substrates are based on CoA.
Subcellular location: Cytoplasm.
Interaction partners:
- Acyl carrier protein
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- Enoyl-[acyl-carrier-protein] reductase FabI
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Biotin carboxylase
Sequence:
MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVMRKLKD
Protein: NAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 2.3.1.-) (Regulatory protein SIR2 homolog 5) (SIR2-like protein 5) (Q8K2C6)
Organism: Mus musculus (Mouse)
Function: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (By similarity). Activates SHMT2 by mediating its desuccinylation (By similarity). Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as Uox.
Subcellular location: Mitochondrion. Cytoplasm, cytosol. Nucleus. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-3
- NAD-dependent protein deacylase sirtuin-6
- NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
- NAD-dependent protein deacetylase sirtuin-2
- NAD-dependent protein deacetylase sirtuin-7
- Cytochrome c, somatic
- Nicotinamide phosphoribosyltransferase
- NAD-dependent protein deacetylase sirtuin-1
- NAD kinase
- Glutamine-dependent NAD
Sequence:
MRPLLIAPGRFISQLCCRRKPPASPQSKICLTMARPSSNMADFRKCFANAKHIAIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPQAFARNPSQVWEFYHYRREVMRSKEPNPGHLAIAQCEARLRDQGRRVVVITQNIDELHRKAGTKNLLEIHGTLFKTRCTSCGTVAENYRSPICPALAGKGAPEPETQDARIPVDKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDRELALCDLCLVVGTSSVVYPAAMFAPQVASRGVPVAEFNMETTPATDRFRFHFPGPCGKTLPEALAPHETERTS
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (A0A0L0LUA6)
Organism: Bifidobacterium breve
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318}. Secreted {ECO:0000256|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000256|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000256|HAMAP-Rule:MF_00318}.
Interaction partners:
Sequence:
MAAIESVYARQILDSRGNPTVEVYLETEDGAQGKGLVPSGASTGEAEAWERRDGDKSVYGGKGVLNAVKAVNEVIAPKIIGMDAADQRALDDLMIELDGTPNKGKLGANAILGVSLAALYASAESAGLPLYRYIGGTNGHILPVPNMNIMNGGAHADFATDIQEYMISPYGFDTYSEALRAGVEVYHTLKNVLKKEGLNTGLGDEGGFAPKMKSNEDSLKYIMDAISAAGYEPGKQIGICLDVASSEFYNKETGKYRFDGEERDSAYMLDYYENLINEYPIVSIEDPFNEEGWEDWAAITARLGDRLQFVGDDLLVTNPARLQKAIDLGAANSLLVKLNQIGSVTETLDAIELATANGYTSMVSHRSGETPDTTISDLAVAKNTRQIKTGAPARGERVAKYNRLLEIEEELGSTAQYAGYSAFKACKKYLAK
Protein: Proteasome 26S subunit, non-ATPase 7 (H3BTM8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPELAVQKVVVHPLVLLSVVDHFNRIGKVGNQKRVVGVLLGSWQKKVLDVSNSFAVPFDEDDKDDSVWFLDHDYLENMYGMFKKVNARERIVGWYHTGPKLHKNDIAINELMKRYCPNSVLVIIDVKPKDLGLPTEAYISVEEVHDDGTPTSKTFEHVTSEIGAEEAEEVGVEHLLRCRTSSTCCQMSACRSSSRPFT
Protein: Alpha-keto acid-binding periplasmic protein TakP (Extracytoplasmic solute receptor protein TakP) (TRAP transporter alpha-keto acid-binding subunit P) (TRAP-T family sorbitol/mannitol transporter, periplasmic binding protein, SmoM) (Q3J1R2)
Organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides)
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system TakPQM involved in the uptake of alpha-keto acids. This protein specifically binds alpha-keto acids including pyruvate, oxobutyrate, oxovalerate and 4-methyl-2-oxovalerate. Ligand-binding affinity increases with the increasing chain length of the aliphatic backbone of the ligand. Is not able to bind alpha-ketoglutarate.
Subcellular location: Periplasm {ECO:0000250|UniProtKB:P44542}.
Interaction partners:
- TRAP transporter small permease protein
- TRAP-T family sorbitol/mannitol transporter, DctM
- TRAP transporter large permease protein
- TRAP transporter small permease protein
- TRAP transporter large permease protein
- TRAP transporter small permease protein
Sequence:
MDRRSFITKAAVGGAAASALAAPALAQSAPKVTWRLASSFPKSLDTIFGGAEVLSKMLSEATDGNFQIQVFSAGELVPGLQAADAVTEGTVECCHTVGYYYWGKDPTFALAAAVPFSLSARGINAWHYHGGGIDLYNEFLSQHNIVAFPGGNTGVQMGGWFRREINTVADMQGLKMRVGGFAGKVMERLGVVPQQIAGGDIYPALEKGTIDATEWVGPYDDEKLGFFKVAPYYYYPGWWEGGPTVHFMFNKSAYEGLTPTYQSLLRTACHAADANMLQLYDWKNPTAIKSLVAQGTQLRPFSPEILQACFEAANEVYAEMEASNPAFKKIWDSIKAFRSEHYTWAQIAEYNYDTFMMVQQNAGKL
Protein: Sb:cb157 protein (Q7SXI8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
IQTRQLIVRAGSILHPLEAMSEQQKYKYENDYKSSEDRNKGASRWSQCRKRGADGILRKSHADEEPDKDRRCSKRSESFTTPESEGPVSRIKNWGDEVEEQEMRTNVRRDFHRYRRRILASDFPQRDRKISSGSSDSRDSRDSKESPAKGDIETDETTLIRRQKQINYGKNTLAYDRYIKEVPKHLRQPGVHPKTPNKFKKYSRRSWDQQIKLWRVKLHAWDPPAEEGGDLQQIEEIDLGEIMDFELDVEMTENTESQCSSSNGAAQSLQEDAFMETPKKMMKIEDSDMS
Protein: Probable CoA-transferase Rv1866 (EC 2.8.3.-) (P95149)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probable CoA-transferase.
Interaction partners:
- Conserved protein
Sequence:
MLDLSDGCSAGGTDMVTRLLADLGADVLKVEPPGGSPGRHVRPTLAGTSIGFAMHNANKRSAVLNPLDESDRRRFLDLAASADIVVDCGLPGQAAAYGASCAELADRYRHLVALSITDFGAAGPRSSWRATDPVLYAMSGALSRSGPTAGTPVLPPDGIASATAAVQAAWAVLVAYFNRLRCGTGDYIDFSRFDAVVMALDPPFGAHGQVAAGIRSTGRWRGRPKNQDAYPIYPCRDGYVRFCVMAPRQWRGLRRWLGEPEDFQDPKYDVIGARLAAWPQISVLVAKLCAEKTMKELVAAGQALGVPITAVLTPSRILASEHFQAVGAITDAELVPGVRTGVPTGYFVVDGKRAGFRTPAPAAGQDEPRWLADPAPVPPPSGRVGGYPFEGLRILDLGIIVAGGELSRLFGDLGAEVIKVESADHPDGLRQTRVGDAMSESFAWTHRNHLALGLDLRNSEGKAIFGRLVAESDAVFANFKPGTLTSLGFSYDVLHAFNPRIVLAGSSAFGNRGPWSTRMGYGPLVRAATGVTRVWTSDEAQPDNSRHPFYDATTIFPDHVVGRVGALLALAALIHRDRTGGGAHVHISQAEVVVNQLDTMFVAEAARATDVAEIHPDTSVHAVYPCAGDDEWCVISIRSDDEWRRATSVFGQPELANDPRFGASRSRVANRSELVAAVSAWTSTRTPVQAAGALQAAGVAAGPMNRPSDILEDPQLIERNLFRDMVHPLIARPLPAETGPAPFRHIPQAPQRPAPLPGQDSVQICRKLLGMTADETERLINERVMFGPAVTA