wanglab/gogpt-training-data huggingface dataset:
Protein: Solute carrier organic anion transporter family member 1C1 (Organic anion transporter 2) (OATP2) (Organic anion transporter F) (OATP-F) (Organic anion-transporting polypeptide 14) (OATP-14) (Solute carrier family 21 member 14) (Thyroxine transporter) (Q9ERB5)
Organism: Mus musculus (Mouse)
Function: Mediates the Na(+)-independent high affinity transport of thyroid hormones at the plasma membrane of brain capillary endothelial cells. The transport activity of substrates L-thyroxine (T4) and 3,3',5'-triiodo-L-thyronine (reverse T3, rT3) is much greater than that of 3,3',5-triiodo-L-thyronine (T3). The prehormone, T4, is the major form in the circulating blood and is converted to the active form, T3, by the iodothyronine-deiodinase in peripheral organs. T3 plays an essential role in brain development via binding to specific nuclear receptors (thyroid hormone receptor). Also transports organic anions such as the conjugated steroid 17-beta-glucuronosyl estradiol (17beta-estradiol 17-O-(beta-D-glucuronate)). Transports T4 and estrone-3-sulfate in a pH-insensitive manner (By similarity). May serve as a drug efflux system at the blood brain barrier (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15166123, ECO:0000269|PubMed:18687783}; Multi-pass membrane protein {ECO:0000269|PubMed:18687783}. Note=Expressed at the basolateral membrane of the choroid plexus epithelial cells. {ECO:0000269|PubMed:15166123}.
Interaction partners:
- Monocarboxylate transporter 8
- Monocarboxylate transporter 10
Sequence:
MDTSSKENAHLFHKNSAQPAGGPSFTVGYPSTEEARPCCGKLKVFLGALSFVYFAKALAEGYLKSTVTQIERRFEIPSSLVGIIDGSFEIGNLLVITFVSYFGAKLHRPKIIGAGCLVMGFGTMLIAVPQFFMEKYSYEKYERYSPSSNVTPSISPCYLESSSPSPSSILGKSQNKISHECVGDSSSSMWVYVFLGNLLRGLGETPIQPLGIAYLDDFASEDNAAFYIGCVQTVAIIGPIFGFLLGSLCAKLYVDIGFVNLDHITITPKDPQWVGAWWLGYLIAGFLSLLAAVPFWCLPKTLPRSQSRENSGSTSEKSKFIDDPIHYQMAPGDDKMKIMEMAKDFLPSLKTLFRNPVYILYLCASTVQFNSLFGMVTYKPKYIEQQYGQSSSKANFVIGLINIPAVALGIFSGGIVMKKFRLGICEATKLYLGSSVFGYLLFLSLFALGCENSSVAGLTVSYQGTKPVSYHERALFSDCNSRCKCSDSKWEPMCGDNGITYVSACLAGCQSSSRSGKNIIFSNCTCVGFAAPKSGNWSGMMGRCQKDNGCSQMFLYFLVISVITSYTLSLGGIPGYILLLRCIQPQLKSFALGIYTLAVRVLAGIPAPVYFGVLIDTSCLKWGFKKCGSRGSCRLYDSHAFRHIYLGLTTLLGTVSVFLSMAVLFVLKKKYVSKHSSLITTREKIGMSSSIKKETCAARDRGLQPKYWPGKETRL
Protein: Ras association domain family member 9 (E1B705)
Organism: Bos taurus (Bovine)
Interaction partners:
- Ras association domain-containing protein 7
Sequence:
MDSEEKEIVVWVCQEEKIVCGLTKRTTSADVIQALLEEHETTFGEKRFLLGNPSDYCIIEKWRGSERVLPPLTRILKLWKAWGDEQPNMQFVLVKADAFLPVPLWRTAEAKLVQNTEKLWELSPANYMKTLPPDKQKRIVRKTFRKLAKIKQDTVSQERDSMETLVHLIISQDHTINQQVKRMKELDLEIEKCEAKFHLDRVENNGENYVQDAYLMPSFSEVEQKLGLEYDERQMLEDLRESNGIVQLEERLTYYRKLIDKLSAEIEKEVKSVCMEINEDAEGAAASELESSNLESVKCDLEKSMKAGLKIHSHLSGIQKEIKYSDSLLQMKAKEYELLAKEFNSLHISNADDCQLKENRGKESEVPTSNGVVSPFTQRIFNMYTNDTDSDTGISSNHSQDSETTAGDVVLLST
Protein: Trace amine-associated receptor 6 (TaR-6) (Trace amine receptor 6) (Trace amine receptor 4) (TaR-4) (Q96RI8)
Organism: Homo sapiens (Human)
Function: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood.
Subcellular location: Cell membrane {ECO:0000269|PubMed:37225986}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- DBH-like monooxygenase protein 1
Sequence:
MSSNSSLLVAVQLCYANVNGSCVKIPFSPGSRVILYIVFGFGAVLAVFGNLLVMISILHFKQLHSPTNFLVASLACADFLVGVTVMPFSMVRTVESCWYFGRSFCTFHTCCDVAFCYSSLFHLCFISIDRYIAVTDPLVYPTKFTVSVSGICISVSWILPLMYSGAVFYTGVYDDGLEELSDALNCIGGCQTVVNQNWVLTDFLSFFIPTFIMIILYGNIFLVARRQAKKIENTGSKTESSSESYKARVARRERKAAKTLGVTVVAFMISWLPYSIDSLIDAFMGFITPACIYEICCWCAYYNSAMNPLIYALFYPWFRKAIKVIVTGQVLKNSSATMNLFSEHI
Protein: Chorion protein b at 7F, isoform B (IP12210p) (Q058X8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRYSMAMIPILGLLLVALIHAAPVEVVYTGESCACPTQLGYQLNVPNTPKPKKYVGGEYGYRVEKPVQTKAKITYSFDFTVEQPRTPAPPKNNPAKLYAKVDRITVNKADCQAKNKSTCGCSSCSGQKPSYGEDAGYGY
Protein: Peptidylprolyl isomerase domain and WD repeat containing 1 (D6R9Q1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYERSYMHRDVITHVVCTKTDFIITASHDGHVKFWKKIEEGIEFVKHFRSHLGVIESIAVSSEGALFCSVGDDKAMKVFDVVNFDMINMLKLGYFPGQCEWIYCPGDAISSVAASEKSTGKIFIYDGRGDNQPLHIFDKLHTSPLTQIRLNPVYKAVVSSDKSGMIEYWTGPPHEYKFPKNVNWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVFDESL
Protein: Transmembrane protein 41A (Q96HV5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRPLLGLLLVFAGCTFALYLLSTRLPRGRRLGSTEEAGGRSLWFPSDLAELRELSEVLREYRKEHQAYVFLLFCGAYLYKQGFAIPGSSFLNVLAGALFGPWLGLLLCCVLTSVGATCCYLLSSIFGKQLVVSYFPDKVALLQRKVEENRNSLFFFLLFLRLFPMTPNWFLNLSAPILNIPIVQFFFSVLIGLIPYNFICVQTGSILSTLTSLDALFSWDTVFKLLAIAMVALIPGTLIKKFSQKHLQLNETSTANHIHSRKDT
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial (Q9M9M6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250, ECO:0000305|PubMed:25732537}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase flavoprotein 2, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 13-A
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 9
- NADH dehydrogenase subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 10-A
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
Sequence:
MASNLLKALIRSQILPSSRRNFSVATTQLGIPTDDLVGNHTAKWMQDRSKKSPMELISEVPPIKVDGRIVACEGDTNPALGHPIEFICLDLNEPAICKYCGLRYVQDHHH
Protein: STAM-binding protein (C9JK83)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDHGDVSLPPEDRVRALSQLGSAVEVNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAVIPEKKDTVKKLKEIAFPKAEELKAELLKRYTKEYTEYNEEKKKEAEELARNMAIQQELEKEKQRVAQQKQQQLEQEQFHAFEEMIRNQELEKERLKIVQEFGKVDPGLGGPLVPDLEKPSLDVFPTLTVSSIQPSDCHTTVRPAKPPVVDRSLKPGALSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTITHVLIPKQSAGSDYCNTENEEE
Protein: DUF1844 domain-containing protein (Q72ES6)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- N-acetyl-gamma-glutamyl-phosphate reductase
Sequence:
MTDEGKSGCGCGGARGDATPQMPQVTFSTFILSLASSALVQLGEVPDPDTGRISENLLMGKHTIDVLTMLQDKTRACIDDDERRLLDGILYELRMKYVVKAK
Protein: T-complex protein 1 subunit zeta-2 (TCP-1-zeta-2) (CCT-zeta-2) (CCT-zeta-like) (Chaperonin containing T-complex polypeptide 1 subunit 6B) (TCP-1-zeta-like) (Testis-specific Tcp20) (Testis-specific protein TSA303) (Q92526)
Organism: Homo sapiens (Human)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8812458}.
Interaction partners:
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit theta
- MOB-like protein phocein
- T-complex protein 1 subunit theta-like 2
- T-complex protein 1 subunit zeta
Sequence:
MAAIKAVNSKAEVARARAALAVNICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEKLVKAERKFIEDRVQKIIDLKDKVCAQSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK
Protein: Scytalone dehydratase arp1 (EC 4.2.1.94) (Conidial pigment biosynthesis oxidase arp1) (O14434)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Scytalone dehydratase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall. The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA. The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening. 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone. The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN. 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone. Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN. Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin. DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize. DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins. DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses. DHN-melanin protects also conidia against amoeba predation.
Subcellular location: Endosome {ECO:0000269|PubMed:26972005}.
Interaction partners:
- Hydroxynaphthalene reductase arp2
- Heptaketide hydrolyase ayg1
- Laccase abr2
- Conidial pigment polyketide synthase alb1
- Multicopper oxidase abr1
Sequence:
MVEKKPNLTLEFHDYLALKKVLFDWADSYDAKDWDRLRSIIAPTLTVDYRQIGLRKWDDMPAEDYMAMISDMDFLGDPTVKTQHLLGESWWEKISDTEVIGHHQLRAAHQVYTDSTLQTVKLKGHGHATNEHYYRKVDGVWKFAGLKPTVRWNEYQFEDVFRAAKPSV
Protein: Translin-associated protein X (Translin-associated factor X) (Q9JHB5)
Organism: Rattus norvegicus (Rat)
Function: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:9681436}. Nucleus {ECO:0000250}. Note=Expressed in the cytoplasm in the presence of TSN. Accumulate in the Golgi complex of mid-late pachytene spermatocytes (By similarity). {ECO:0000250}.
Interaction partners:
- Translin
- Protein argonaute-2
- Protein argonaute-1
- Endoribonuclease Dicer
- Protein argonaute-4
- Protein argonaute-3
- Ribonuclease 3
- Interferon-inducible double-stranded RNA-dependent protein kinase activator A
- Ribonuclease P protein subunit p30
- RISC-loading complex subunit TARBP2
Sequence:
MNGKEGPGGFRKRKHDNFPHNQRREGKDASSSSPVMLAFKSFQQELDTRHDKYERLVKLSRDITVESKRTIFLLHRITSAPDMEEILTESESKLDGVRQKMLQVAQELSGEDMHQFHRAVTTGLQEYVEAVSFQHFIRTRSLISMEEINRQLTFTTDDSGKESKAPPADGQDKQLVTWRLKITPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVSKKLYTLKQSLSKVENACYALKVRGSEIPKHMLADVFSVKTEMIDQEESIS
Protein: Myosin heavy chain-like, isoform I (A0A0B4KGR6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPPLSPANEATAEIAASGEENAGPVESDRLEKEKFLARVLAAMNGGPRSGNLASNNSSGSSLNSTLSGSAPLARPPKPPASQARKQLRLLPKQREQSPVLSNGHTTRSTLSHQHTTNKYTLKSTGGNAGSSTLSSSLLGADSDRHRLVNRSPSPALSVSSRCSTQSQSSISNFTSNSRLQTPPRRVFPQSYTRGSGGVDPYEMRQLESSPVVFDGNLSFVLGCQRQPVYQSMRASPSFEDPRTSSAYLSEKIQNFLKRTDHVQEEWTAMSRRTRRINSNSGRAGGSESRCTTPGSTCSGYDDYDTISLIERQRERNSMERCGSVGRTRSSQNILTKAFQLAKQLPHTPTSRGNSVARDRESSVATISLTTGDNDDDDDRTIREEDDELSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLRPVHVKRSSQQSLNGSIGGGGGSVVSSTRTVVFEKDDNSPRNNAK
Protein: Tubby protein (P50586)
Organism: Mus musculus (Mouse)
Function: Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight. Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages (By similarity).
Subcellular location: Cytoplasm. Nucleus. Secreted. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Binds phospholipid and is anchored to the plasma membrane through binding phosphatidylinositol 4,5-bisphosphate. Is released upon activation of phospholipase C. Translocates from the plasma membrane to the nucleus upon activation of guanine nucleotide-binding protein G(q) subunit alpha. Does not have a cleavable signal peptide and is secreted by a non-conventional pathway.
Interaction partners:
Sequence:
MTSKPHSDWIPYSVLDDEGSNLRQQKLDRQRALLEQKQKKKRQEPLMVQANADGRPRSRRARQSEEQAPLVESYLSSSGSTSYQVQEADSIASVQLGATRPPAPASAKKSKGAAASGGQGGAPRKEKKGKHKGTSGPATLAEDKSEAQGPVQILTVGQSDHDKDAGETAAGGGAQPSGQDLRATMQRKGISSSMSFDEDEDEDENSSSSSQLNSNTRPSSATSRKSIREAASAPSPAAPEPPVDIEVQDLEEFALRPAPQGITIKCRITRDKKGMDRGMYPTYFLHLDREDGKKVFLLAGRKRKKSKTSNYLISVDPTDLSRGGDSYIGKLRSNLMGTKFTVYDNGVNPQKASSSTLESGTLRQELAAVCYETNVLGFKGPRKMSVIVPGMNMVHERVCIRPRNEHETLLARWQNKNTESIIELQNKTPVWNDDTQSYVLNFHGRVTQASVKNFQIIHGNDPDYIVMQFGRVAEDVFTMDYNYPLCALQAFAIALSSFDSKLACE
Protein: RNA binding protein fox-1 homolog 2 (Fox-1 homolog B) (RNA-binding motif protein 9) (RNA-binding protein 9) (B0QYY6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVQPFTTIPFPPPPQNGIPTEYGVPHTQDYAGQTGEHNLTLYGSTQAHGEQSSNSPSTQNGSLTTEGGAQTDGQQSQTQSSENSESKSTPKRLHVSNIPFRFRDPDLRQMFGFGKILDVEIIFNERGS
Protein: Epididymis secretory sperm binding protein (A0A384N6B9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLETLSQSPPKGVTIPYRPKPSSSPVIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWAGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS
Protein: Aromatic/aminoadipate aminotransferase 1 (2-aminoadipate aminotransferase) (EC 2.6.1.39) (2-aminoadipate transaminase) (Alpha-aminoadipate aminotransferase) (AadAT) (Aromatic amino acid aminotransferase 1) (EC 2.6.1.57) (Aromatic amino acid aminotransferase I) (Aromatic amino acid-requiring protein 8) (P53090)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: General aromatic amino acid transaminase involved in several otherwise unrelated metabolic pathways. Responsible for phenylalanine and tyrosine biosynthesis. Active with glutamate, phenylalanine, tyrosine and tryptophan as amino donors and with phenylpyruvate, hydroxyphenylpyruvate, 2-oxoglutarate and pyruvate as amino acceptors. Also active with methionine, alpha-aminoadipate and leucine as amino donors when phenylpyruvate is the amino acceptor and in the reverse reactions with the corresponding oxo acids and phenylalanine as amino donor. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) as the amino donors. Catalyzes the formation of alpha-aminoadipate from alpha-ketoadipate in the lysine biosyntheic pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transaminated amino acid decarboxylase
- Probable prephenate dehydratase
- Prephenate dehydrogenase [NADP
- Chorismate mutase
- Aromatic amino acid aminotransferase 2
- Chorismate synthase ARO2
- Tryptophan synthase
- Aspartate aminotransferase, cytoplasmic
- Multifunctional tryptophan biosynthesis protein
- Homoisocitrate dehydrogenase, mitochondrial
Sequence:
MTLPESKDFSYLFSDETNARKPSPLKTCIHLFQDPNIIFLGGGLPLKDYFPWDNLSVDSPKPPFPQGIGAPIDEQNCIKYTVNKDYADKSANPSNDIPLSRALQYGFSAGQPELLNFIRDHTKIIHDLKYKDWDVLATAGNTNAWESTLRVFCNRGDVILVEAHSFSSSLASAEAQGVITFPVPIDADGIIPEKLAKVMENWTPGAPKPKLLYTIPTGQNPTGTSIADHRKEAIYKIAQKYDFLIVEDEPYYFLQMNPYIKDLKEREKAQSSPKQDHDEFLKSLANTFLSLDTEGRVIRMDSFSKVLAPGTRLGWITGSSKILKPYLSLHEMTIQAPAGFTQVLVNATLSRWGQKGYLDWLLGLRHEYTLKRDCAIDALYKYLPQSDAFVINPPIAGMFFTVNIDASVHPEFKTKYNSDPYQLEQSLYHKVVERGVLVVPGSWFKSEGETEPPQPAESKEVSNPNIIFFRGTYAAVSPEKLTEGLKRLGDTLYEEFGISK
Protein: Oxidation resistance protein 1 (Protein C7) (Q4V8B0)
Organism: Rattus norvegicus (Rat)
Function: May be involved in protection from oxidative damage.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Hypocretin neuropeptide precursor
- Orexin receptor type 2
- Orexin/Hypocretin receptor type 1
Sequence:
MDYLTTFTGKSGRLLRGTASRLWGLGGGGEARQVRFEDYLREPAPGDPGCGPGELRPPSPTSPEGPDTGQKKTLDKKDGRRMSFQKPKGTIEYTVESRDSLNSIALKFDTTPNELVQLNKLFSRAVVTGQVLYVPDPEYVSSVESSPSLSPVSPLSPTSSEAEFDKTTTPDVVHPKEAPPSSTESSIRPARVVSSTSEEEEAFTEKFLKINCKYITNGKGTVSGVLLVTPNNIMFDPHKTDPLVQENGCEEYGIMCPMEEVMSAAMYKEILDSKLKESLPIEVDQLSGRGFCHSKKMTGVPAEETDSRSRDQGNDSVSTAPRSTEESLSEDVFTESELSPIREELPSSELRQEKSSDASSESVQTVSQIEVESLTAASESADVPDHTNANSGRSSSEVGALSHETGLSSLEIATKEGDKATGNLQEVSGPKEQSTDIKGQDNQDSFHHENSLQQEAGEDSLSSGETVELTEKPTVLKDQQGKELKRDSETEVEELRKLWKTHSMQQAKQQRDTIQQVAQRESKHRGAPADAHGEGSSLLKEKRRHRLHKFLCLRVGKPMRKTFVSQASATMQQYAQRDKKHEYWFAVPQERTDHLYAFFIQWSPEIYAEDTGEYTREPGFIVVKKMAESGPDEAPAGEAAAREWEITTREDINSKQAAPAKADLEPESFRPNLSDPSELLLPDQIEKLTKHLPPRTIGYPWTLVYGTGKHGTSLKTLYRTMTGLDTPVLMVIKDSDGQVFGALASEPFKVSDGFYGTGETFVFTFCPEFEVFKWTGDNMFFIKGDMDSLAFGGGGGEFALWLDGDLYHGRSHSCKTFGNHTLSKKEDFFIQDIEIWAFE
Protein: Thioredoxin domain-containing protein 12 (EC 1.8.4.2) (Endoplasmic reticulum resident protein 19) (ER protein 19) (ERp19) (Thioredoxin-like protein p19) (Q9CQU0)
Organism: Mus musculus (Mouse)
Function: Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol-disulfide oxidase activity.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12930873}.
Interaction partners:
- Glutathione hydrolase 6
- Glutathione hydrolase 7
- Glutathione hydrolase 5 proenzyme
- Glutathione hydrolase 1 proenzyme
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Glutathione synthetase
- Glutathione S-transferase Mu 7
- Glutathione S-transferase Mu 4
- Glutathione S-transferase A3
Sequence:
MSLRFGATCLLSFSFLLLITSSDGRTGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPRDEDFSPDGGYIPRILFLDPSGKVRPEIINESGNPSYKYFYVSAEQVVQGMKEAQERLTGDAFREKHFQDEL
Protein: Serine/threonine-protein kinase spk-1 (EC 2.7.11.1) (Q03563)
Organism: Caenorhabditis elegans
Function: Required for embryogenesis and germline development in both adult hermaphrodites and males. SR-protein kinase (SRPK) that binds directly to and phosphorylates the RS domain of rsp-3/CeSF2 in vitro.
Interaction partners:
- Uncharacterized protein ZK643.6
- Probable splicing factor, arginine/serine-rich 3
Sequence:
MFVVLFCRWLNGFSQHRERLYKFEDEAVQRRRRFRVHSEESEELNDHESYSETDICTQLLASSADVTCHINVDLVNQNRFYFFVKQRNKKENSTNEEEEISSQEINTSTQNEETEVNLVFASAEDNGGVASNFDISDALMVTSNISEVSKLPETLCEEGETVQQKSVVNENDHSNEDDEQSLQSQDGSRCSDEDMNSCVSASDEEDVESQDDSFHVNDATEESIDSVSSIESQEAEESATEDLASCHSNDDKNEKDVLVDEDTSKYDNLPVEMRSAKEGEESEGTIDSSVSSSTSSSSTGDDGDDSATSYDSEDIEIQMFEYDLGTACASASISIPRPSIIPRNNKKTEVNANEERLDDLSVSPGRSDSPGGGGGGHSDSFQDPMDPGEQLGSDDEEQEDPRDYKRGGYHPVNIGDVFNARYHVIRKLGWGHFSTVWLAWDTQDKRFVAMKIVKSAEHYTEAALDEIKLLLSVRSADPNDIGCHKVVQLLDEFTVTGINGQHVAMVFEVLGCNLLKLIIRSNYRGLHLEQVRKICRQVLEALGYMHEKCGIIHTDIKPENVLITMSREEIKIMAQHAVVARKMNMKMSGSAVSTAPDHLVKMAQENMTKNKKKKMKKKAKKQREKLEAELAGLEGLKMDANGLQEAYNNAPELENFNASQVEDVTMEDTVNENGNRNKVEIRSPDRFDRTTLTPFSDPESKFGDLASPSAEYLSSPMSQLPPGGILPAPPVGPNIGDPYCDIDVKIADLGNACWVNHHYTDDIQTRQYRALEVLIGSGYGPPADIWSTACMAFELATGDYLFEPHQGDNYSRDEDHLAHISELLGAIPPSIYKKGKHWREFFHKNGHLLHIHQLKPWSLYEVLRQKYEWSHEDAQQFESFLRPMLDFDQEKRSTAKIALKHPFLLPFGGRAPKSDCPPELLSKMFPDGLIPEPFDGNEHQEVYRDENDSRSASERSANSRSAGGSDDDDEEEFNMNRPGPSGVITNNETTDISDIERFQLDLQ
Protein: Interleukin 9 (D4A8I9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Interleukin 9 receptor.
- Interleukin 2 receptor, gamma, isoform CRA_a.
- Interleukin-7
- Interleukin-4
- Interleukin-5
- Interleukin-2
- Interleukin-6
- Tyrosine-protein kinase JAK3
- Interleukin-15
- Interleukin-13
Sequence:
MFVTYVLASALLFGSVLGQRCSTSWGIQHTSYLIENLKDDPSSKCSCSANVTSCLCLPIPSDDCTTPCFQEGMSQVTNATQQSKFSPFFFRVKRIVETLKSNKCQFFSCEKPCNQTTAGNTVSFLKSLLKTFQKTEVQVQRSRA
Protein: Rifin (Q8IIZ9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYTKILLFSLLLNILAHNKNKSYTTIHTPITTSRVLIECNVYIPNYDNDPDMKSVKENFDRQTSQRFEEYNERMIDKRQKCKEQCEKDIQKIILKDKIEKELAEKFVTLQTDISINDIPTCVCEKSVADKVEKTCLKCGGVLGGGITPGWGLISGIVYTGWKAAALAAAKKAAIAEGAAKGLAEGIKEGIQEVMKGLCRDFRLSEVDVKKLGLVFDGKNYNNTEYIFKAIFSKFDESCMPSSTGAVRGASEPICNSVWSKFVFTNRSSSRNSIINAIKENVETIVSQAETTAGATKEMVTQEVTSAAIKTNTTAVNATYASCQTVIIASVVAIVVIVLVMIIIYLVLRYRRKKKMKKKLEYIKLLKE
Protein: DPP6 amino-terminal domain protein (F8K7.9) (Q9XI11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKLTNALFFFFLICLLSLSSASSNKPQLSNGSTILFTTIGRPTFEFDIFTLPTSHRPPSPADEHRLTDGKSINFNGYFASPSTALISLLPKRTQIQPQDVHLIYVTERAGTPSLNYDVVHSDNVGSRIQVPLFSGEEQQSGMNVNSMKDTPVLTNGYLVHVSTHENPGKPMASWAAVYSTELRTKSTRRLTPLGIADFSPAVSPSGKWTAVASFGEKGWTWSMVEKEISSDVYVFLTQDGTQRVKVVEQGGWPRWVDDSTLYFHRKSDDGWISVYRAILPKTGPVTTKSVTIQRVTPPGLHAFTPATSPNNNNFIAVATRRPGSEIRHVELFDLKKNEFVELTRLVSPKSHHFNPFLSPDSSRVGYHSCRGDATGRKTPRNLLQSLKTTSNDLSLFRFDGAFPSISPEGDRFAFVSFTGVFVVNPDGSGLRQLLPQMGFGTVWDPIRHGIVYTSSGPALAPGKSQIDILAINVDAPSPATAVKKLTTTGENNAFPWPSPDGKRIVFRSARSGTKNLYIMDAEKGESGGLFRLTNGNWNDTIATWSPDGNWIVFASNREFPGTLLMNIYVVHPDGTGLRKLAQNLTGLVSMHPMFSPDSKRIVFTTIYAGISAEQIGNPHFNVPSSEIFTVNLDGSGLTRLTHNSVEDGPPMWFPKIKATGDVAWPKRFGPSCSIQDFKTQNTTVKMKMNKPATMSSMCVVPSQ