wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor Sox-9-A (B7ZR65)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development (By similarity). Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including COL2A1 (By similarity). Plays a central role in successive steps of chondrocyte differentiation (By similarity). Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis (By similarity). Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes (By similarity). Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells (By similarity). Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells (By similarity). Involved in development of the cranial neural crest, which is fated to form skeletal elements. Also required for otic placode specification during inner ear development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:11807034}. Cytoplasm {ECO:0000250|UniProtKB:Q6F2E7}. Note=Restricted to the nucleus of Sertoli-like cells in the testis, but localizes to the cytoplasm of previtellogenic oocytes in the ovary before being translocated into the nucleus of vitellogenic oocytes. {ECO:0000250|UniProtKB:Q6F2E7, ECO:0000269|PubMed:11807034}.
Interaction partners:
Sequence:
MNLLDPFMKMTEEQDKCMSGAPSPTMSDDSAGSPCPSGSGSDTENTRPQENTFPKGDQELKKETEDEKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNEGEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQTEQEDGAEQTHISPNAIFKALQADSPHSSSSMSEVHSPGEHSGQSQGPPTPPTTPKTDIQPGKPDLKREGRPLQENGRQPPHIDFRDVDIGELSSEVISTIETFDVNEFDQYLPPNGHPGVGSTQASYTGSYGISSTPSATTGAGPAWMSKQQQQQPQQHSLSTLNSEQSQSQQRTHIKTEQLSPSHYSDQQQQHSPQQLNYSSFNLQHYSSSYPTITRAQYDYTEHQGSSTYYSHASGQNSGLYSTFSYMNPSQRPLYTPIADTTGVPSIPQTHSPQHWEQPVYTQLTRP
Protein: Myelin-associated glycoprotein (Siglec-4a) (P20917)
Organism: Mus musculus (Mouse)
Function: Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid-containing gangliosides and to the glycoproteins RTN4R and RTN4RL2. Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination. Protects motoneurons against apoptosis, also after injury; protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2. Required to prevent degeneration of myelinated axons in adults; this probably depends on binding to gangliosides on the axon cell membrane. Negative regulator of neurite outgrowth that inhibits axon longitudinal growth. Negative regulator of neurite outgrowth; in dorsal root ganglion neurons the inhibition is mediated primarily via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to neuronal gangliosides. In cerebellar granule cells the inhibition is mediated via binding to neuronal gangliosides. In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides (By similarity). Inhibits axon outgrowth by binding to RTN4R. Preferentially binds to alpha-2,3-linked sialic acid. Binds ganglioside Gt1b.
Subcellular location: Cell membrane {ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9482783}; Single-pass type I membrane protein {ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9482783}. Membrane raft {ECO:0000250|UniProtKB:P07722}.
Interaction partners:
- Reticulon-4 receptor
- Paired immunoglobulin-like receptor B
- Reticulon-4
- Oligodendrocyte-myelin glycoprotein
- Myelin basic protein
- Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
- Myelin-oligodendrocyte glycoprotein
- Reticulon-4 receptor-like 2
- Myelin-associated oligodendrocyte basic protein
- Tumor necrosis factor receptor superfamily member 16
Sequence:
MIFLATLPLFWIMISASRGGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGEDGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIFKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQAQAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKKNVTESSSFSGGDNPHVLYSPEFRISGAPDKYESEKQRLGSERRLLGLRGESPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRVK
Protein: Desert hedgehog protein (Q9WUP6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
SVQSCGPGRGPVGRRRYVRKQLVPLLYKQFVPSMPERTLGASGPAEGRVTRGSERFRDLVPNYNPDIIFKDEENSGADRLMTERCKERVNALAIAVMNMWPGVRLRVTEGWDEDGHHAQDSLHYEGRAL
Protein: Notch-regulated ankyrin repeat-containing protein B (Q7T3X9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Regulates independently canonical Wnt and Notch signaling by modulating LEF1 and Notch protein turnover. Stabilizes LEF1, a pivotal transcription factor in the Wnt signaling cascade, by blocking its ubiquitination. Involved in angiogenesis; involved in intersegmental vessel patterning during development.
Interaction partners:
- Neurogenic locus notch homolog protein 1
- unspecific monooxygenase
Sequence:
MSQADMTCSARQRVFQEALRKGNTKELHSLLQNMTNCEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADTRLANRDGWSALHIAAFGGHQDIVLYLITRAKYSSSAL
Protein: ALA-interacting subunit 5 (AtALIS5) (Q8L8W0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the lipid transport activity of the ALA/ALIS P4-ATPase complex.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein {ECO:0000269|PubMed:20053675}. Prevacuolar compartment membrane {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein {ECO:0000269|PubMed:20053675}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein {ECO:0000269|PubMed:20053675}. Note=In a heterologous system, the final intracellular localization after exit from the endoplasmic reticulum is the prevacuolar compartment in the presence of ALA2 and the Golgi in the presence of ALA3.
Interaction partners:
- Phospholipid-transporting ATPase 3
- Phospholipid-transporting ATPase 2
- Phospholipid-transporting ATPase 10
- Probable phospholipid-transporting ATPase 12
- Phospholipid-transporting ATPase 6
- Phospholipid-transporting ATPase 1
- Monogalactosyldiacylglycerol synthase 1, chloroplastic
- U-box domain-containing protein 11
- Galactokinase
- S-protein homolog 1
Sequence:
MSSTAASSTVGGGGSSEISGVKKTSKRPKYSRFTQQELPACKPILTPRWVILTFLVAGVVFIPLGVICLFASQGVVEIVDRYDTDCIPTSSRNNMVAYIQGEGDKICKRTITVTKAMKHPVYVYYQLENFYQNHRRYVKSRNDAQLRSPKEEHDVKTCAPEDNVGGEPIVPCGLVAWSLFNDTYSFSRNSQQLLVNKKGISWKSDRENKFGKNVFPKNFQKGAPIGGGTLNISKPLSEQEDLIVWMRTAALPTFRKLYGKIETDLHAGDTITVLLQNNYNTYSFNGQKKLVLSTTSWLGGRNDFLGIAYLTVGSICLFLAVTFAVLYLVKPRQLGDPSYLSWNRSAGGLQ
Protein: Protein TIC (Q17636)
Organism: Caenorhabditis elegans
Interaction partners:
- WW domain-containing protein
- CWF19-like protein 1 homolog
- DUF2013 domain-containing protein
- Trafficking protein particle complex subunit 5
- C3H1-type domain-containing protein
- GPI mannosyltransferase 1
- DeHydrogenases, Short chain
- SAP domain-containing protein
- Uncharacterized protein C48B4.11
- Zf-tcix domain-containing protein
Sequence:
MGDQDGKKKPPFDMPPPPKPLSFEMPKPPVLQPNIASLLQKTNTTGEDVKSKDAQPSVTPVPPPTFNPVPNPFAPRPKSVSPNPHPDVPAVTVGALSAPADKSETEGEKIEKPSETAQAHVENVKKPEKPSSLGTHPLTTEIPITPMVEEAKPITSPAVVEVSSHAESVKSSIDSSNLFTDKVDMSGGLMSWLTKTVTESKLLSDVAGKAKAGVETVMTTLDPGMKPFLAEHGVIEFALFNCDADLLTVASDAFTKSGAMAICRGLTSVIANFRPLVAGEEKARKMCEIKVEAARKTNKAKEDAAVVVIQPFLMEISGRYYSTCKIVLHHESKYFDAISQLLEIPSTLVEVIQRAAKSEGLPDDEFSTSVTQAIKNVYKTSVTTWEPGSFAPYDSKELLSIAFASVSQQLLRNLAPVN
Protein: Uridine diphosphate glucose pyrophosphatase NUDT22 (UDPG pyrophosphatase) (UGPPase) (EC 3.6.1.45) (Nucleoside diphosphate-linked moiety X motif 22) (Nudix motif 22) (Q9BRQ3)
Organism: Homo sapiens (Human)
Function: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and UDP-galactose to galactose 1-phosphate and UMP. Preferred substrate is UDP-glucose.
Interaction partners:
- tRNA 2'-phosphotransferase 1
- Uridine diphosphate glucose pyrophosphatase NUDT14
- m7GpppN-mRNA hydrolase NUDT17
- NAD-capped RNA hydrolase NUDT12
- ADP-sugar pyrophosphatase
- 8-oxo-dGDP phosphatase NUDT18
Sequence:
MDPEVTLLLQCPGGGLPQEQIQAELSPAHDRRPLPGGDEAITAIWETRLKAQPWLFDAPKFRLHSATLAPIGSRGPQLLLRLGLTSYRDFLGTNWSSSAAWLRQQGATDWGDTQAYLADPLGVGAALATADDFLVFLRRSRQVAEAPGLVDVPGGHPEPQALCPGGSPQHQDLAGQLVVHELFSSVLQEICDEVNLPLLTLSQPLLLGIARNETSAGRASAEFYVQCSLTSEQVRKHYLSGGPEAHESTGIFFVETQNVQRLLETEMWAELCPSAKGAIILYNRVQGSPTGAALGSPALLPPL
Protein: RNA polymerase I and III subunit C (D6RDJ3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDENSLEFDMVGIDAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQGDEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLG
Protein: N-alpha-acetyltransferase daf-31 (EC 2.3.1.255) (Abnormal dauer formation protein 31) (O61219)
Organism: Caenorhabditis elegans
Function: Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity (By similarity). Plays a role in regulating larval development, metabolism and longevity. Functions downstream or alongside daf-3, daf-12 and daf-16 in the dauer formation pathway. Functions upstream of daf-15 to enable animal development.
Interaction partners:
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- Protein MAK10 homolog
- N-terminal methionine N
- N-terminal methionine N
- Nascent polypeptide-associated complex subunit alpha-like UBA domain-containing protein
- N-terminal methionine N
- RSD-2 domain-containing protein
- Beta,beta-carotene 9',10'-oxygenase
- Large ribosomal subunit protein uL3
- Beta,beta-carotene 9',10'-oxygenase
Sequence:
MNIRCARVDDLMSMQNANLMCLPENYQMKYYFYHALSWPQLSYIAEDHKGNVVGYVLAKMEEDPGEEPHGHITSLAVKRSYRRLGLANKMMDQTARAMVETYNAKYVSLHVRVSNRAALNLYKNTLKFEIVDTEPKYYADGEDAYAMRRDLAKWAEERNIEPADREAYTTAKTTDDKKKNRS
Protein: Polyadenylate-binding protein (PABP) (E9AFX7)
Organism: Leishmania major
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
- Probable eukaryotic initiation factor 4A
- Putative eukaryotic translation initiation factor 4e
- Putative eukaryotic translation initiation factor 4 gamma
- ATP-dependent RNA helicase
- ATP-dependent RNA helicase
- ATP-dependent RNA helicase
- Putative eukaryotic translation initiation factor eIF-4E
Sequence:
MAAAVQEAAAPVAHQPQMDKPMQIASIYVGDLDATINEPQLVELFKPFGTILNVRVCRDIITQRSLGYGYVNFDNHDSAEKAIESMNFKRVGDKCVRLMWQQRDPALRYSGNGNVFVKNLEKDVDSKSLHDIFTKFGSILSCKVMQDEEGKSRGYGFVHFKDETSAKDAIVKMNGAADHASEDKKALYVANFIRRNARLAALVANFTNVYIKQVLPTVNKDVIEKFFAKFGGITSAAACKDKSGRVFAFCNFEKHDDAVKAVEAMHDHHIDGITAPGEKLYVQRAQPRSERLIALRQKYMQHQALGNNLYVRNFDPEFTGADLLELFKEYGEVKSCRVMVSESGVSRGFGFVSFSNADEANAALREMNGRMLNGKPLIVNIAQRRDQRYTMLRLQFQQRLQMMMRQMHQPMPFVGSQGRPMRGRGGRQQLGGRAQGHPMPMPSPQQPQAPAQPQGFATPSAVGFVQATPKHSPGDVPETPPLPPITPQELESMSPQEQRAALGDRLFLKVYEIAPELAPKITGMFLEMKPKEAYELLNDQKRLEERVTEALCVLKAHQTA
Protein: rRNA-processing protein CGR1 (Coiled-coil growth-regulated protein 1) (P53188)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11116400, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome biogenesis protein RPF2
- Regulator of ribosome biosynthesis
- Ribosome biogenesis protein NSA2
- Nucleolar GTP-binding protein 2
- Nucleolar GTP-binding protein 1
- Nuclear GTP-binding protein NUG1
- Ribosome biogenesis protein RLP24
- Ribosome biogenesis protein 15
- Probable metalloprotease ARX1
- Pescadillo homolog
Sequence:
MVNETGESQKAAKGTPVSGKVWKAEKTPLRAKSRVVKNKKLTSWELKKQKRLEDKQFKERLKALKDEKEEARQAKITMLKERREKKEENERYERLAAKMHAKKVERMRRREKRNKALKER
Protein: Protein mxl-3 (Basic-helix-loop-helix transcription factor 3) (Max-like protein 3) (Q18711)
Organism: Caenorhabditis elegans
Function: Transcription factor which regulates the expression of genes involved in lipid metabolism in response to nutrient availability. Binds to the E-box motif 5'-CACGTG-3'. Under well-fed conditions, binds to the promoter and represses the expression of lipase genes lipl-1, lipl-2, lipl-3 and to a lesser extent lipl-5, thereby preventing lipolysis. In response to a high-glucose diet, promotes fatty acid synthesis, elongation and desaturation by up-regulating transcription factor sbp-1 expression. Under well-fed conditions, acts remotely in the intestine to up-regulate the expression of chemoreceptor srh-234 gene in the ADL sensory neuron, possibly by regulating the insulin signaling pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:29113111}. Cytoplasm {ECO:0000269|PubMed:29113111}. Note=In response to nutrient levels, shuttles between the cytoplasm and the nucleus (PubMed:29113111). Localizes to the nucleus in response to high glucose levels (PubMed:29113111). {ECO:0000269|PubMed:29113111}.
Interaction partners:
- Mad-like protein 1
- Max-like protein 1
- Mitogen-activated protein kinase pmk-3
- Mitogen-activated protein kinase pmk-2
- Mitogen-activated protein kinase pmk-1
- Helix-loop-helix protein 30
- Helix-loop-helix protein 11
- Helix-loop-helix protein 25
- Lipase lipl-3
- BCL7-like protein
Sequence:
MSAIVEDMYLLSSSMKMEKQFRKRHHSDSSDDDSSSPKSASPSMDDDRRAHHNELERRRRDHIKDHFTILKDAIPLLDGEKSSRALILKRAVEFIHVMQTKLSSQGKAIEDLTRKNELLEERLLERESSGSPSSSRLPALAVSSSQMQLTMPIIPQMQNIAQLSQYPQQANIIAQSTNPAQLDGLIALNNDAILALLGSFQSVSPSLLDSAPGTPPSGFYPCAFSPVDQQMAVKI
Protein: D-glucuronyl C5-epimerase (EC 5.1.3.17) (Heparan sulfate C5-epimerase) (Hsepi) (Heparin/heparan sulfate:glucuronic acid C5-epimerase) (Heparosan-N-sulfate-glucuronate 5-epimerase) (P46555)
Organism: Caenorhabditis elegans
Function: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acids (By similarity). Plays a role in the early migration of AQR and PQR neurons, which descend from the Q neuroblasts.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Secreted, extracellular space, extracellular matrix, basement membrane.
Interaction partners:
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Heparan-sulfate 6-O-sulfotransferase
- Heparan sulfate 2-O-sulfotransferase hst-2
- Sulfotransferase domain-containing protein
- Sulfotransferase domain-containing protein
- GlyPicaN
- Probable syndecan
- Exostosin-like-3 homolog
- Exostosin-1 homolog
- Fibronectin type-III domain-containing protein
Sequence:
MKCLRWRSNRHRIYLLVACGALFLLNRHLTQEESRIDEEDEELTQVDVNEDDKKIECEPPGSIESKCIADNGKSMKCWKDEEDVYFPVSYLKKRFDMTGKLGKDGSTFELYTSYAKMRSPDSTYDPLGPFGHFSTYSVETRDRVRCVSAKTDVPMSTQWDPIPYYYPIQISQYGLQHYSRMKLDSISNKSEASPKDDVILGVNSKEWKGAAGMHETTERLFFNDEQMGKVVNISAGAALANAGAYVYLDKSPDLHVISFDWKPYEANSSFTVLAKMKQDDLLVLINYVYSEGNGKCVWQEEERISDDYIVQKPKKDGQVSYSYSYIGNSPIGEWSTVTRDLLVDVARALSSGDNRKKDDNVVLHAGDLRLVSLGFRGELTVKQKITQRREQHSHAFYAAADWLVKNQNDRGGWSVPVERSIAERKLVLPPGWHSAMAQGHGISVLTRAFKHFNDEKYLKSAAKALKLFKINSSDGGVRGEFFGNIWYEEYPTTPGSFVLNGFLYSLIGLYDLSQLELMIDENDETMRAKIQEAQELYSAGVRSLKQLLPLYDTGSGTIYDLRHVALGTAPNLARWDYHAVHVYLLKWIAGIEKDEVLSKTADRWIGYAYGKRAKHN
Protein: Large ribosomal subunit protein mL38 (39S ribosomal protein L38, mitochondrial) (L38mt) (MRP-L38) (Q3ZBF3)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10600119, ECO:0000269|PubMed:11551941}.
Interaction partners:
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein uL18m
- Large ribosomal subunit protein uL2m
- Large ribosomal subunit protein mL44
Sequence:
MAAPWWRVVLNGSRNWRGFSTSAALSRRAAPLGPMPNEDIDVSNLERLKKYRSFDRYRRRAEREARDPHWWRTYREHFGEESDPKDTVDIGLPPPKVCRTQQLLERKRVLRELRTSVEEERASRLRTASIPLEAVRAEWERTCGPYHKQRLAEYYGLYRDLFHGATFVPRVPLHVAYAIGEDDLVPVYYGNEVTPTEAAQPPEVTYEADEGSMWTLLLTNLDGHLLEPDAEYVHWLVTNIPGSRVAEGEETCPYLPPFPARGSGFHRFAFLLFKQDKPVDFSGDTRPSPCYQLAQRTFHTFDFYKKHQDAMTPAGLAFFQCRWDDSVTHIFHQLLDMREPVFEFVRPPPYHPKQKCFPHRQPLRYLDRYRDSHEPTYGFY
Protein: Kynurenine 3-monooxygenase (EC 1.14.13.9) (Kynurenine 3-hydroxylase) (O88867)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract.
Subcellular location: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:1332540}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:1332540}.
Interaction partners:
- Kynureninase
- Kynurenine formamidase
- Kynurenine--oxoglutarate transaminase 1
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- 3-hydroxyanthranilate 3,4-dioxygenase
- Tryptophan 2,3-dioxygenase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
- Indoleamine 2,3-dioxygenase 1
- Kynurenine--oxoglutarate transaminase 3
Sequence:
MASSDTEGKRVVVIGGGLVGALNACFLAKRNFQVDVYEAREDIRVANFMRGRSINLALSYRGRQALKAVGLEDQIVSKGVPMKARMIHSLSGKKSAIPYGNKSQYILSISREKLNKDLLTAVESYPNAKVHFGHKLSKCCPEEGILTMLGPNKVPRDITCDLIVGCDGAYSTVRAHLMKKPRFDYSQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRNAFMMIALPNMDKSFTCTLFMSFEEFEKLPTHSDVLDFFQKNFPDAIPLMGEQALMRDFFLLPAQPMISVKCSPFHLKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFNNDLSVCLPEFSRFRIPDDHAISDLSMYNYIEMRAHVNSRWFLFQRLLDKFLHALMPSTFIPLYTMVAFTRIRYHEAVLRWHWQKKVINRGLFVLGSLVAIGSAYILVHHLSPRPLELLRSAWTGTSGHWNRSADISPRVPWSH
Protein: ethanolamine kinase (EC 2.7.1.82) (Q8IIB7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- ethanolamine-phosphate cytidylyltransferase
- Phosphoethanolamine N-methyltransferase
- Choline kinase
Sequence:
MEYQLREIDESEKEITQQRKKNSVTTKNFDNLSNSNSQITEMTNEQGVIPLREKDLTINVGDNRNLKVEEFMTNFISNVFENKNALFLYCKYVLLFYGKELLNENNVESLNFEIIKGGITNILVKVEDNIHQNKYLIRLYGPKTSEIINREREKLISNILCDKNISKKIYVFFPNGRIEEFKDGYALSREDIKNKDFQKEIAENLRILHDIQLDDTIYKKLQALQNIQGNRSSFLWSTLWKYFNTLKEERQKKYSFNPKAYILKLIDFDMLESIITEIQELCCKKNSPVVLCHCDLLSSNIIKTEGSSISFIDFEYSCPMERAYDIANHFNEYAGFNCEWDLTPNRSEEYHFIKHYLKTDDEQLINQLIDEIQPFYVCSHIVWGLWALLQGLHSVIDFDFINYGMTRLTAAFSVKFRSKLEKN
Protein: cDNA sequence BC057170 (Q6PG83)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MTQPQMAPICLVENHNEQLLVNQEAIEILEKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLDTEGLGDVEKSNPKNDSWIFALSVLLSSTFVYNSMSTINHQALEQLHYVTELTELIRSKSSRNPHGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPGYNPRVQASNSARECIRCFFPNRKCFVFDRPTHDRELLQKLETISEDQLDLKFREGTKAFVSYVFTYAKIKTLREGIKVTGNRLGTLVTTYVDAINSGAVPCLDDAMTSVAQRENSVAVQKAADHYSEQMAQRLRLPTDTLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVEIISEKIAFFWLKNEEASNKYCQEELDRLSKDFMDNISTFSVPGGHRIYMDMREKIEHDYWQVPRKGVKACEVFQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMMLEKQLKDQKAFLEEGFTNKAEEINAEIERLEHNIKDKKENIGPILELIERAFCAWVFSSLILVALLTHNPSLLRK
Protein: mitogen-activated protein kinase (EC 2.7.11.24) (C8VFS8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Mitogen-activated protein kinase kinae mkk2
- protein-tyrosine-phosphatase
- MADS-box domain-containing protein
- protein-tyrosine-phosphatase
- non-specific serine/threonine protein kinase
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
- Paf1-domain-containing protein
- Protein kinase domain-containing protein
- Mitogen-activated protein kinase kinae kinase bck1
Sequence:
MIWIFPDRTTSNETYLYEELMECDLAAIIRSGQPLTDAHYQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSIDPEENAGYMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGGRPFFKGRDYVDQLNQILHYLGTPNEETLSRIGSPRAQEYVRNLPFMPKVPFQRLFPNANPDALDLLDRMLAFDPSSRISVEEALEHPYLAIWHDASDEPSCPTTFDFHFEVVDDVQEMRRMIYEEVVRFRQSVRMPPQAQSLAQQQQIGNIPIPEHQQGVWRQEEPRPQEAGAVGGNHNDLESSLQRGMDA
Protein: Bitesize isoform 2 (Bitesize, isoform C) (Q6XK19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIAYTTARATPTPPPRVRRQSSDSDSPQVQRRPQQPRNIYCPRIRESDTGTDEEFVLNTESSSQTSSDQTPPPVPPPPHPLSMKTRIKTRFLKNHHHHSHNRCNCNPGQQQQQPQYVPIPVPVPIPVPMAAYPNWPEVSGNPLLEQDEQLAASLQQLWKAAGHQQQFAAIVAAYSQQFAAASGNMFDATPPVTSKSYQQLPTTPPPIPERLRGLGGFKSSAPELSASLGSLMTQSLCSTISSSSSSSTSGYGTAGRSLETLASPMRAANSMQQQQQQYQEQHQQMASSAFKPKPTSLVASRSPTGEQLETSNARRGSSNSESDDNANSNSNNATPTTGRLCNVYDKTGTLPVPQCVQAHVASVDKSAATAAISTKAEPAATPATSTKGTALRVASKYQSRNLCETQSAATTQTYLASKNSHEEVEAADETNIHKNQVPAAAAAATAQIQTATRAAAPAVITRFGGLAVENAVGNVAESASASAASPIPKPKPRAQHPEQIDRHRATAETAKNLSSNRLIENIKMSDEASPSTAAHLQSESYAASSPDEASSNSSQDGDQDRERELEEQAEQKPRRTTQRSYNVAGMMEEQQLGEVDAVEQRHHSTTSDSSSSSSSNSSSSSESCDSDDTGTVRDRRPKRRRFNKVFVVNRQPGGRVRRSSSTEGDSLSSSEANLEDSSDNDTDTERTDCGIVLNYVKPLEEEPKKAEEEPPTAARDCQSSDEDNINDDESERRVANSTDELANCIVVVGGQTDDAAAGVVLHHMRSLPDVEFDGEQSERRQAHEIDASDALAACDELHSISNDVNRLLALHKQNSQLELKLQRLRQGVAEINEDLQLSTTGTDVAATHCTTQPGSAGKPDECNSPSSRKSPSTVLSSNDVGPLSLTCLRQVEAVVEVEANRADGKLRDERNGRTAEQTEERVVTCSQACKINDNSDYSLDSLSATSASLLAPEQQQQQPLQQVEESARLPADAREQRYRRGAKSESAESPVENEMLNVAVASRAALLGSNNNNTHRNDNSNNENTNNNDGELGHNNNDAFAAQKTRNSGSSVVVGCDISDVVSVNSNVSGENECDFDKIFGSHQQNTPSASAAVAATAAAATSDTPATSPSELASPKNSLSAKYRSLVMINKDNESAAGDYEMANSSSNFSNIRHKDPTSSNNSHTVGQNFASDSFRAMEPTELVSSDREAYSVDSLNEPPAVPELSVEDGLADDDSWVEELSQRGEDEDEDLSNATTTPTATDSEDAEGEGEGARRHGYMDREEDLRGYNRSAIDFTLHTIVEESCEESEVASMRADNEDVELEDEDLSERRRQRTLQHHHRLSASELEKYFFFGLGDGRVMSSIDTRGDDTASEVSSECSESLDSLPHEDQLLDTSGASDLASSRLEKYFLSGFMGFSGAEKQAESDESGGSVGSDSEGQPSPSQRRKRLVRARGTPRSHNSSLDNLLLPESDTLDATVTSAGGAAAATVEDTSESEAGCDDTVIHLANAGASDGSSSDTIKRKKQLRKRHDSLDEKKLHDLEPSECRTPTPGSSGQVQMQSQAKKQQQQHHHSRDSGFVGSNDDLLKAAPDCEPPKSPTPALEQISEDREPVHSQISLARMDQPSTSAAAAVASTLSSQLKNLALPNLVRKDSFNNWSSDEETNLMMSKMRQFFKNLIVATANAQQSKPSTPNQGPSTTNVNTTPSSQRRLAKSRPAQLAYFENELTRLMKTVPGINDEQVREIVEYLSSEDTWSDSYDSSDYTSSDLEGGERKGQLKAQISASCQQIINKFEIDEEGDRGDGGLLDESQSVPMEALVYQKLVASFSKVAAGGEPETEATKAVEEAEPSTERSPQLFAKVMQHIGTRLVALMHEVSSGNETPTPSPQGQRHHRRLQAKISATTTEDEEDEVAEQLKAMPIKQLKLRSKSHDLLLDGTTPHSHHLHHHATVHYPAGGVGSGAGGSGGPGHSDNAGEECGVTSDYERFSWRGSFESALLANGDSRTRLSQLSQLDRDNSSSASALAVAKRRSAGDLLFSQHQQSLSREQLDRVRSCGSIGGGDAHHHQLESSPAKPWLSSAGSSIGGDSTKDVRRSSVPDAIYETDSSDEAASHQFGGARSTLPRSLNPNQVVASTNSLPRLPTTGVGAPITSTPKTKSQSALNHTPSNLSTVSATGSAKSARYRSPGLAARAAAVSGAGGGSSGGVGVGASSGSTGKKLGAGFQFLYSKRDARKRLNMSAEEAKVAAEELSRSPVIGQRQADGSGSPIQSRASSETWPTQSDEDIDRLVAMHQNRSSLSSLGVRSESMASVYSGAGEGRYGTVVVKGQVEFAMQYNYKLSALEVHVVRCKDLAAVDAKRNRSDPYVKVYLLPDKSKAGKRKTKVKKHTLNPIFDETMRFHTPISSLESRTLWLTVWHSDMFGRNDFLGEVSVNLQGRLFDNPQSQWYLLQERSEPFDEVATYRGDIVVGLKYIPPENIKSSFFSRGSSITGSSSNLRKFGGSIKSVASKSERTSKGGQLHVLVKEAKHLSPIKANGTCDAFCKSYLLPDRTRSSKQKTPVVKRTLHPSWNYTFVYEDVSLEELSERALELTVWDHDRLASNEFVGGIRFSLGTGRSYGRQVEWMDATGKELSLWQNMLDRPNFWVEGSLVLRSSLDGIRANLP