wanglab/gogpt-training-data huggingface dataset:
Protein: Leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) (Q09996)
Organism: Caenorhabditis elegans
Function: Involved in protein synthesis. Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Interaction partners:
- Isoleucine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- glutamate--tRNA ligase
- Threonine--tRNA ligase, cytoplasmic
- Cysteine--tRNA ligase, cytoplasmic
- proline--tRNA ligase
- Valine--tRNA ligase
Sequence:
MSKINKERKKVAQLQEIEKSIQELWESKKAFEADARDDGKPKYLVTFPFPYMNGRLHLGHTFSASKCEFAAGFQRLQGKEVLFPFGFHCTGMPIKACADKLKREMQDFGYPPNFPEDVVEEVKEEVSAVDEIIKDKSKGKKSKLVAKTGNAKYQWQIMKSLGLCDEEIKEFSDPNHWLYYFPPHCIADLKKMGLKADWRRSFITTDVNPYFDSFVRWQFNLLRAAKKIDFGKRYTIYSPKDGQPCMDHDRASGEGVGPQEYTLIKLKVLDPKPQALSHIKEDIYLVAATLRPETMYGQTNCYLHPDIQYSVFYATENEKQVFVATARSARIMSYQGLTKENGKVNYVLGLEKIAGSKILGAPLSAPLAKYERVYALPMLTIKDDKGTGVVTSVPSDSPDDFAALSDLKKKKPLREKYGLTDEMVLPFEPVPIIKIEGLGDLAAVEMCSRLKIESQNEKDKLEEAKKEVYLKGFYDGVMLVGKYAGKKTADVKKVIQDDLTAEGLATKYVEPEKKVMSRSGDECVVALCDQWYLNYGEAEWKAAAKKVLEPLRTFNDETRRGLETTVDWLHEYACSRSYGLGTKLPWDTQYLIESLSDSTIYNAYYTVAHLLQQGAFDGSVVGPAGIKADQMTDASWSYVFLGEIYDSKTMPVEEEKLKSLRKEFMYWYPIDMRASGKDLIGNHLTYLLFNHAAIWPTDTSKWPKGIRANGHLLLNNEKMSKSTGNFMTLEEAIEKFSADGMRLSLADAGDGLEDANFVYAMADAAILRLFTMIEWIKEMIEQRDAGLLRKDAKKFADRVFANEMNSLIAATEQNYEATNFKDALKTGFFEYQAIRDTYRELCAGIDEPMSESLVFRFIETQMLILSPICPHIAEYIWQLLGKDGLIVNAPWPTVDPVDEKLAIGARFITESLAEFRARLKTYMTPKKKALKEIPEVPTEAVIYVAKEYPPWQKTILDILEKQAKANNGALPDNKAISQLIGKEESLKKFAKKAMPFVQMIKERFEQKGVSALASSSPVDQTSILNENIDFIMNALDLDRVTIRHTDEEGIDANIVETTVPLVPMLNFTPNRPTIKLVARNVQICNAMFDVDVPIVNGDSVSMVIRKMRRISKAIKPKFEVSLWRYKNAVWGDRQMISYRNPFEENIQLSDADIFNFEADNKISVTSGSEKFDLGRTIVYKANVPEN
Protein: Iduronate 2-sulfatase precursor (EC 3.1.6.13) (Zgc:158245) (A1A5V0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNVMFVFTCWWFVFIFHLLGRDVFAAKSKNFNVLYLIADDLRPTLGCYSDPVVKSPNIDQLASLSVVFHNAYAQQAVCGPSRVSFLTSRRPDTTKLYDFNSYWRVHAGNYTTLPQYFKSNGYTTLSVGKVFHPGIASNHSDDYPYSWSVPPYHPPSFEYEKRKVCKDKDGTLHSNLLCPVNVSEMPLGTLPDMENTEEAIRLLRSMKGSQKPFFLSVGFYKPHIPFRIPQEYLKLYPIENMTLAPDPDVPKKLPDVAYNPWTDIRKREDVQALNLSFPYGPIPKDFQLRIRQHYFASVSYVDAQVGKILQTLDDVGLAKNTIVVLSSDHGWSLGEHGEWAKYSNFDVATRVPLMVYKAGVSSRRSRPGAKTFPFIDVFQDTREHFGKGKIVNSVVELLDVFPTLANLAGLPSVHHCPSPSFKMDLCTEGSNLANLIRNPKHLNREAYSFSQYPRPSDSIQENSDLPNLADIRIMGYSIRSNDYRYTLWVGFDPLHCKPNMTEIHAGELYILTEDPGQDNNLFDEFGHAALLNKFGTMPSWTESLKQHMMYFSSGLKSKGLS
Protein: E3 ubiquitin-protein ligase TRIM33 (EC 2.3.2.27) (Ectodermin homolog) (Protein moonshine) (RING-type E3 ubiquitin transferase TRIM33) (Transcription intermediary factor 1-gamma) (TIF1-gamma) (Tripartite motif-containing protein 33) (Q6E2N3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May act as an E3 ubiquitin-protein ligase and a transcriptional repressor (By similarity). Involved in the regulation of embryonic and adult hematopoiesis. Required for normal development and survival of both committed erythroid progenitor cells and posterior mesenchymal cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:15314655}.
Interaction partners:
- Mothers against decapentaplegic homolog.
- GATA-binding protein 1a.
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog
- Transcriptional activator Myb isoform 1
Sequence:
MEVEASGTEDNGDGGAKEPEAVVSIDTETKEAADEAKSQETVPQTPTTSSDSSSSGGGGEATDGTPNAESADPPPPPPPPPPPPPSTPADSTAAAASPAVLTEMSPPPPASTSSSSSTPAAPINLLDTCAVCKQSLQNRDCEPKLLPCLHSFCLKCIPQPDRKITMPVQGPHGQDTRIVNVMRCTVCHQDYKQIDMVDNYFVKDTSEATNTSVENSTQVCTSCEDNASAIGFCVECGEWLCKTCIEAHQRVKFTKDHKIRKKEEVSPESVGTSGQRPVFCPVHKQEALKLFCETCDTLTCRDCQLLEHKEHRYQFLDEACQNQKGIIATFMTKLQEKRGLVEYSASEVQKRLKEVAETHKKVEHEIKIAVFTLINEINKKGKSLLQQLESVTKDRSMKLLSQQRDISVLAQQIIHVLNFTNWAITNGSSTALLYSKRLITYQLRLIMKARVDAVPPANGAVRFFCDPTFWAKNVVNLGNLVIEKVAPTAPPSNMMVNQQISPGHNHPGKHSGQINLAQLRLQHMQQAAIAQKHQQQHQHHQQQQHQHQHQQQQQQQQQQQQQQQQQQQQQQHQQQIQQQMRIASQMSQHPRQGAPQMIQQPPPRLISMQALHRGGVNGSSHMFPPHHLRMVSAQNRMPSAQPRLNGQPYPMMQPQLQRQHSNPGHAGPFPVASLHNISAANPTSPTSASMANAHMHRGPSSPVITPIELIPSVTNPENLPCLPDIPPIQLEDAGSSTLDNILSRYISANAYPTVGPTNPSPGPSTHSPGSSGLSNSHTPARPSSTSSTGSRGSSGTTVDQVKVKQEPGVEEECSYSGANVKTERTKDGRRSACMMSSPEGSLTPPLPILGSVSTGSVQDILRTLGENVKSEPQSDNLSSCTNPNSRATLTNGTSGSNGGQRGGATNANSQTTAGKEDDPNEDWCAVCQNGGELLCCDHCPKVFHITCHIPTLKSSPSGDWMCTFCRNLANPEIEYNCDDDPPRNKEKNEMAMSPEEQRRCERLLLHVFCHELSTEFQEPVPTSVPNYYKIIKHPMDLTLVKRKLQRKHPLHYKSPKEFVSDVRLVFSNCAKYNEMSRIIQVYDEEKQSNVQADSEVAEAGKAVSLYFEERLLEIFPEQTFPVVMEKETQIEAEKEDSDDSDDDIIQPKRKRLKVDTEMLLHIK
Protein: Adiponectin receptor protein 1 (Progestin and adipoQ receptor family member 1) (Progestin and adipoQ receptor family member I) (Q91VH1)
Organism: Mus musculus (Mouse)
Function: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism. Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17268472}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96A54}. Note=Localized to the cell membrane and intracellular organelles. {ECO:0000250|UniProtKB:Q96A54}.
Interaction partners:
- Adiponectin
- DCC-interacting protein 13-alpha
- Adiponectin receptor protein 2
- Leptin
- Cadherin-13
- Resistin
- Insulin-2
- Insulin-1
- DCC-interacting protein 13-beta
- Nicotinamide phosphoribosyltransferase
Sequence:
MSSHKGSAGAQGNGAPSGNREADTVELAELGPLLEEKGKRAASSPAKAEEDQACPVPQEEEEEVRVLTLPLQAHHAMEKMEEFVYKVWEGRWRVIPYDVLPDWLKDNDYLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGFVLFLFLGILTMLRPNMYFMAPLQEKVVFGMFFLGAVLCLSFSWLFHTVYCHSEKVSRTFSKLDYSGIALLIMGSFVPWLYYSFYCSPQPRLIYLSIVCVLGISAIIVAQWDRFATPKHRQTRAGVFLGLGLSGVVPTMHFTIAEGFVKATTVGQMGWFFLMAVMYITGAGLYAARIPERFFPGKFDIWFQSHQIFHVLVVAAAFVHFYGVSNLQEFRYGLEGGCTDDSLL
Protein: Serum amyloid A-1 protein (SAA) [Cleaved into: Amyloid protein A (Amyloid fibril protein AA); Serum amyloid protein A(2-104); Serum amyloid protein A(3-104); Serum amyloid protein A(2-103); Serum amyloid protein A(2-102); Serum amyloid protein A(4-101)] (P0DJI8)
Organism: Homo sapiens (Human)
Function: Major acute phase protein.
Subcellular location: Secreted {ECO:0000269|PubMed:7115671}.
Interaction partners:
- Serum amyloid A-2 protein
- Serum amyloid P-component
- Interleukin-6
- Apolipoprotein A-I
- Apolipoprotein C-III
- Apolipoprotein B-100
- Scavenger receptor class B member 1
- Interleukin-8
- C-reactive protein
- Apolipoprotein C-II
Sequence:
MKLLTGLVFCSLVLGVSSRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVITDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY
Protein: Mitochondrial brown fat uncoupling protein 1 (UCP 1) (Solute carrier family 25 member 7) (Thermogenin) (W5PSH7)
Organism: Ovis aries (Sheep)
Function: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance (By similarity). Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP. Regulates the production of reactive oxygen species/ROS by mitochondria (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:26038550}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04633}.
Interaction partners:
- Vasopressin V1b receptor
- Lipid transferase CIDEA
- Peroxisome proliferator-activated receptor gamma
- Beta-3 adrenergic receptor
- PR/SET domain 16
- Adipocyte fatty acid-binding protein 4
- Transmembrane protein 26
- Iodothyronine deiodinase
- Leptin
- Adiponectin, C1Q and collagen domain containing
Sequence:
MVGHAATDVPPTMAVKIFSAGVAACVADIITFPLDTAKVRLQIQGECLTSSAFRYKGVLGTIITLAKTEGPVKLYSGLPAGLQRQISFASLRIGLYDTVQEFFTTGKEASLGSKISAGLTTGGVAVFIGQPTEVVKVRLQAQSHLHGPKPRYTGTYNAYRIIATTEGLTGLWKGTTPNLTRNVIINCTELVTYDLMKEALVKNKLLADDVPCHFVSAVVAGFCTTVLSSPVDVVKTRFVNSSPGQYTSVPNCAMMMLTREGPSAFFKGFVPSFLRLGSWNIIMFVCFEQLKRELMKSRQAMDCAT
Protein: U3 small nucleolar RNA-associated protein 4 homolog (Cirhin) (UTP4 small subunit processome component) (Q969X6)
Organism: Homo sapiens (Human)
Function: Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Involved in small subunit (SSU) pre-rRNA processing at sites A', A0, 1 and 2b. Required for optimal pre-ribosomal RNA transcription by RNA polymerase. May be a transcriptional regulator. Acts as a positive regulator of HIVEP1 which specifically binds to the DNA sequence 5'-GGGACTTTCC-3' found in enhancer elements of numerous viral promoters such as those of HIV-1, SV40, or CMV.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16225863, ECO:0000269|PubMed:24219289, ECO:0000269|PubMed:34516797}. Chromosome {ECO:0000269|PubMed:20813266}. Note=Found predominantly at the fibrillar center. {ECO:0000269|PubMed:24219289}.
Interaction partners:
- Nucleolar protein 56
- DDB1- and CUL4-associated factor 13
- U3 small nucleolar RNA-associated protein 6 homolog
- U3 small nucleolar RNA-associated protein 15 homolog
- WD repeat-containing protein 75
- HEAT repeat-containing protein 1
- Nucleolar protein 58
- Nucleolar complex protein 4 homolog
- Nucleolar protein 11
- KRR1 small subunit processome component homolog
Sequence:
MGEFKVHRVRFFNYVPSGIRCVAYNNQSNRLAVSRTDGTVEIYNLSANYFQEKFFPGHESRATEALCWAEGQRLFSAGLNGEIMEYDLQALNIKYAMDAFGGPIWSMAASPSGSQLLVGCEDGSVKLFQITPDKIQFERNFDRQKSRILSLSWHPSGTHIAAGSIDYISVFDVKSGSAVHKMIVDRQYMGVSKRKCIVWGVAFLSDGTIISVDSAGKVQFWDSATGTLVKSHLIANADVQSIAVADQEDSFVVGTAEGTVFHFQLVPVTSNSSEKQWVRTKPFQHHTHDVRTVAHSPTALISGGTDTHLVFRPLMEKVEVKNYDAALRKITFPHRCLISCSKKRQLLLFQFAHHLELWRLGSTVATGKNGDTLPLSKNADHLLHLKTKGPENIICSCISPCGSWIAYSTVSRFFLYRLNYEHDNISLKRVSKMPAFLRSALQILFSEDSTKLFVASNQGALHIVQLSGGSFKHLHAFQPQSGTVEAMCLLAVSPDGNWLAASGTSAGVHVYNVKQLKLHCTVPAYNFPVTAMAIAPNTNNLVIAHSDQQVFEYSIPDKQYTDWSRTVQKQGFHHLWLQRDTPITHISFHPKRPMHILLHDAYMFCIIDKSLPLPNDKTLLYNPFPPTNESDVIRRRTAHAFKISKIYKPLLFMDLLDERTLVAVERPLDDIIAQLPPPIKKKKFGT
Protein: Beta-adducin (Add97) (Erythrocyte adducin subunit beta) (Q9QYB8)
Organism: Mus musculus (Mouse)
Function: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to the erythrocyte membrane receptor SLC2A1/GLUT1 and may therefore provide a link between the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Alpha-adducin
- Dematin
- Protein 4.1
- Ankyrin-1
- Ankyrin-2
- Tropomodulin-1
- Tropomodulin-2
- Tropomodulin-4
- Tropomodulin-3
- Band 3 anion transport protein
Sequence:
MSEDTVPEAASPPPSQGQHYFDRFSEDDPEYLRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPASSMNFSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALSSAGGTENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGVPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRNMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLDMRNKIREQNRQDIKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDADTKDESEETVPNPFSQLTDQELEEYKKEVERKKLEQEQEGEKDIATEKPGSPVKSTPASPVQSPSKAGTKSPAVSPSKTSEDTKKTEVSEANTEPEPVKPEGLVVNGKEEEPSVEEALSKGLGQMTTNADTDGDSYKDKTESVTSGPLSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES
Protein: Uncharacterized protein C23H4.16c (O13957)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Cell differentiation protein rcd1
- ABC transporter domain-containing protein C20G4.01
- Mitochondrial division protein 1
- General negative regulator of transcription subunit 3
- General negative regulator of transcription subunit 1
- General negative regulator of transcription subunit 2
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- Putative general negative regulator of transcription C16C9.04c
- Poly
Sequence:
MLGKEWENTSFAEIGLLHQAPNDNDLEKFQHALTLMSEADNSSDLLIPLISDFLIWFYYQKTPLKWIPFLGHFFNTWQSCSFPPRRYLLAKILSGRISELLKVSPFELAASVTSQDVVEADSLVEENELQAWLEKQELVPSSSNFLNSFWISGGERELTEEEQNSLLQSNTTYTNSDLPASKQLESFISMNLSYSKVFFLHLLQHSDSSFNDKFLLLLANIPVTVSNVEVLLYLLQQEESLAQFDLNGKSFLYHMLVSLHNQVTNTSHLEKQRISTVATLFISKLFEIPSLSEYLSSTLFLDLQAFCIVALPQSAKLFQKVKALKNNP
Protein: Protein Hook homolog 1 (mHK1) (Q8BIL5)
Organism: Mus musculus (Mouse)
Function: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell (By similarity). Required for spermatid differentiation. Probably involved in the positioning of the microtubules of the manchette and the flagellum in relation to the membrane skeleton.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12075009}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12075009, ECO:0000269|PubMed:28003339}. Note=Localizes to punctate cytoplasmic foci which do not appear to overlap with early or late endosomes, the endoplasmic reticulum, multivesicular bodies (MVBs), lysosomes, or mitochondria (PubMed:12075009). Often found in close association with microtubules (PubMed:12075009). Does not associate with the Golgi complex (PubMed:12075009). During spermiogenesis, it localizes to the manchette in spermatids from steps 8-10 (PubMed:12075009). It is also present between the microtubule manchette and the nucleus (PubMed:12075009). During manchette elongation, it is preferentially localized to the nuclear ring of the manchette, whereas the strong localization to the manchette decreases (PubMed:12075009). In more mature spermatids, while the manchette migrates posteriorly, it localizes to punctuates spots (PubMed:12075009). At later stages of spermatid differentiation, the punctuate expression pattern is found at both the attachment site and the proximal end of the elongated manchette (PubMed:12075009). In contrast, it is not present in mature spermatozoa (PubMed:12075009). {ECO:0000269|PubMed:12075009}.
Interaction partners:
- RIMS-binding protein 3
- FHF complex subunit HOOK-interacting protein 1B
- Vacuolar protein sorting-associated protein 18 homolog
- AKT-interacting protein
- Protein Hook homolog 2
- Protein Hook homolog 3
- Vacuolar protein sorting-associated protein 41 homolog
- Vam6/Vps39-like protein
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 33A
Sequence:
MEDPQPLPQSELPLCDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEELIPDLNQITECADPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVISPASDTVGELEQQLKRALEELQEAIAEKEELKQRCQELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVAKLRDYEEKLIVSAWYNKSLAFQKLGMESRLVSGASACKDSVAAAPARSFLAQQRHITNTRRNLSVKVPAAASD
Protein: Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Ergosterol biosynthesis protein 19) (Mevalonate pyrophosphate decarboxylase) (MPD) (Mevalonate-5-diphosphate decarboxylase) (MDD) (MDDase) (P32377)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Diphosphomevalonate decarboxylase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway. MVD1/ERG19 converts diphosphomevalonate into isopentenyl diphosphate. The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Interaction partners:
- Isopentenyl-diphosphate delta-isomerase
- Mevalonate kinase
- Phosphomevalonate kinase
- Farnesyl pyrophosphate synthase
- Geranylgeranyl pyrophosphate synthase BTS1
- Hydroxymethylglutaryl-CoA synthase
- Acetyl-CoA acetyltransferase
- Lanosterol synthase ERG7
- Squalene synthase ERG9
- Squalene epoxidase ERG1
Sequence:
MTVYTASVTAPVNIATLKYWGKRDTKLNLPTNSSISVTLSQDDLRTLTSAATAPEFERDTLWLNGEPHSIDNERTQNCLRDLRQLRKEMESKDASLPTLSQWKLHIVSENNFPTAAGLASSAAGFAALVSAIAKLYQLPQSTSEISRIARKGSGSACRSLFGGYVAWEMGKAEDGHDSMAVQIADSSDWPQMKACVLVVSDIKKDVSSTQGMQLTVATSELFKERIEHVVPKRFEVMRKAIVEKDFATFAKETMMDSNSFHATCLDSFPPIFYMNDTSKRIISWCHTINQFYGETIVAYTFDAGPNAVLYYLAENESKLFAFIYKLFGSVPGWDKKFTTEQLEAFNHQFESSNFTARELDLELQKDVARVILTQVGSGPQETNESLIDAKTGLPKE
Protein: Sodium/potassium-transporting ATPase subunit beta-3 (Sodium/potassium-dependent ATPase subunit beta-3) (ATPB-3) (CD antigen CD298) (P54709)
Organism: Homo sapiens (Human)
Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein {ECO:0000255}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit alpha-4
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta-2
- Phospholemman
- Protein ATP1B4
- Mitogen-activated protein kinase 3
Sequence:
MTKNEKKSLNQSLAEWKLFIYNPTTGEFLGRTAKSWGLILLFYLVFYGFLAALFSFTMWVMLQTLNDEVPKYRDQIPSPGLMVFPKPVTALEYTFSRSDPTSYAGYIEDLKKFLKPYTLEEQKNLTVCPDGALFEQKGPVYVACQFPISLLQACSGMNDPDFGYSQGNPCILVKMNRIIGLKPEGVPRIDCVSKNEDIPNVAVYPHNGMIDLKYFPYYGKKLHVGYLQPLVAVQVSFAPNNTGKEVTVECKIDGSANLKSQDDRDKFLGRVMFKITARA
Protein: Calcitonin gene-related peptide 1 (CGRP1) (Alpha-type CGRP) (Calcitonin gene-related peptide I) (CGRP-I) (P01256)
Organism: Rattus norvegicus (Rat)
Function: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P06881}.
Interaction partners:
Sequence:
MGFLKFSPFLVVSILLLYQACGLQAVPLRSTLESSPGMAATLSEEEARLLLAALVQNYMQMKVRELEQEQEAEGSSVTAQKRSCNTATCVTHRLAGLLSRSGGVVKDNFVPTNVGSEAFGRRRRDLQA
Protein: Peroxisome proliferator-activated receptor alpha (PPAR-alpha) (Nuclear receptor subfamily 1 group C member 1) (P23204)
Organism: Mus musculus (Mouse)
Function: Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:20159955}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Retinoic acid receptor RXR-alpha
- Period circadian protein homolog 2
- Nuclear receptor corepressor 2
- Nuclear receptor coactivator 1
- Nuclear receptor corepressor 1
- Transcription factor Jun
- Phosphatidate phosphatase LPIN1
- Fatty acid-binding protein, liver
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MVDTESPICPLSPLEADDLESPLSEEFLQEMGNIQEISQSIGEESSGSFGFADYQYLGSCPGSEGSVITDTLSPASSPSSVSCPVIPASTDESPGSALNIECRICGDKASGYHYGVHACEGCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSEKAKLKAEILTCEHDLKDSETADLKSLGKRIHEAYLKNFNMNKVKARVILAGKTSNNPPFVIHDMETLCMAEKTLVAKMVANGVEDKEAEVRFFHCCQCMSVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYEAIFTMLSSLMNKDGMLIAYGNGFITREFLKNLRKPFCDIMEPKFDFAMKFNALELDDSDISLFVAAIICCGDRPGLLNIGYIEKLQEGIVHVLKLHLQSNHPDDTFLFPKLLQKMVDLRQLVTEHAQLVQVIKKTESDAALHPLLQEIYRDMY
Protein: Peptide chain release factor 1, mitochondrial (MRF-1) (MtRF-1) (O75570)
Organism: Homo sapiens (Human)
Function: Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain non-cognate termination stop codons AGG and AGA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17803939, ECO:0000269|PubMed:37141370}.
Interaction partners:
- MTRF1L release factor glutamine methyltransferase
- Large ribosomal subunit protein mL62
- Methyltransferase HEMK2
- Ribosome-releasing factor 2, mitochondrial
- Translation initiation factor IF-2, mitochondrial
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein uS7m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL9m
Sequence:
MNRHLCVWLFRHPSLNGYLQCHIQLHSHQFRQIHLDTRLQVFRQNRNCILHLLSKNWSRRYCHQDTKMLWKHKALQKYMENLSKEYQTLEQCLQHIPVNEENRRSLNRRHAELAPLAAIYQEIQETEQAIEELESMCKSLNKQDEKQLQELALEERQTIDQKINMLYNELFQSLVPKEKYDKNDVILEVTAGRTTGGDICQQFTREIFDMYQNYSCYKHWQFELLNYTPADYGGLHHAAARISGDGVYKHLKYEGGIHRVQRIPEVGLSSRMQRIHTGTMSVIVLPQPDEVDVKLDPKDLRIDTFRAKGAGGQHVNKTDSAVRLVHIPTGLVVECQQERSQIKNKEIAFRVLRARLYQQIIEKDKRQQQSARKLQVGTRAQSERIRTYNFTQDRVSDHRIAYEVRDIKEFLCGGKGLDQLIQRLLQSADEEAIAELLDEHLKSAK
Protein: Uncharacterized protein YDR179W-A (Q03983)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Structural protein MDM1
- Nucleus-vacuole junction protein 2
- Nucleus-vacuole junction protein 1
- Vacuolar protein 8
- Very-long-chain enoyl-CoA reductase
Sequence:
MPTILYNTNSSLITKYRRPNASNQYKGFLSKKGHTRLNSKSSGDIWEKDCSHTKNSGNDVSFESEFEKDSVEYLRDLCFSIYPNSLHQKIRSIEALPDLQVNTFIALIFQNFVKSWYGIKIPTDDSKFLTELYNLVQDLITYLKSSKINYHALLLDYIPCLLSSHLKALNDSSQNNDLVYEQYCKLTLYDSKRYPMLFTEIIQSKMSTKSLLQRSFLDSFLNELVFGHIFNSIAEPYYLLEGLNKICIRIKLNSAGNTRNEVTHGKPKCDPWLFVSNVKHKILQMTRLLAYSTSTEAANMNTAEIQETAFLQRYIFTFFTDDFFKLSMRKPFLFSICRTLQHWISKLNALNRVMYRTFDNIVQTKITSPVTIGNLFSLLRHSLFPNDNMMGPPRVLPVGDAFLEFREECISNLWDVCMTYKLDHILAIKRSDIADLIICISKNRDCNKLLIYRIIDCVIAQLP