wanglab/gogpt-training-data huggingface dataset:
Protein: Trace amine-associated receptor 1 (TaR-1) (Trace amine receptor 1) (Q923Y9)
Organism: Rattus norvegicus (Rat)
Function: Receptor for trace amines, including beta-phenylethylamine (b-PEA), p-tyramine (p-TYR), octopamine and tryptamine, with highest affinity for b-PEA and p-TYR. Unresponsive to classical biogenic amines, such as epinephrine and histamine and only partially activated by dopamine and serotonin. 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. The signal transduced by this receptor is mediated by the G(s)-class of G-proteins which activate adenylate cyclase.
Subcellular location: Endomembrane system {ECO:0000250|UniProtKB:Q96RJ0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96RJ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96RJ0}. Cell membrane {ECO:0000250|UniProtKB:Q96RJ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96RJ0}. Note=Localizes mainly intracellularly. Partially colocalizes with the endoplasmic reticulum; also found at lower lever at the plasma membrane. {ECO:0000250|UniProtKB:Q96RJ0}.
Interaction partners:
Sequence:
MHLCHNSANISHTNSNWSRDVRASLYSLISLIILTTLVGNLIVIISISHFKQLHTPTNWLLHSMAVVDFLLGCLVMPYSMVRTVEHCWYFGELFCKLHTSTDIMLSSASILHLAFISIDRYYAVCDPLRYKAKINLAAIFVMILISWSLPAVFAFGMIFLELNLEGVEELYHNQVFCLRGCFPFFSKVSGVLAFMTSFYIPGSVMLFVYYRIYFIAKGQARSINRANLQVGLEGESRAPQSKETKAAKTLGIMVGVFLLCWCPFFFCMVLDPFLGYVIPPTLNDTLNWFGYLNSAFNPMVYAFFYPWFRRALKMVLFGKIFQKDSSRSKLFL
Protein: DNA replication licensing factor MCM4 (EC 3.6.4.12) (Cell division control protein 54) (P30665)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for S phase execution.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA replication licensing factor MCM6
- Cell division cycle protein CDT1
- Origin recognition complex subunit 5
- Origin recognition complex subunit 1
- Pre-rRNA-processing protein IPI3
- Cell division control protein 7
- DNA replication licensing factor MCM7
- Chromosome segregation in meiosis protein 3
- Cell division control protein 6
- Origin recognition complex subunit 4
Sequence:
MSQQSSSPTKEDNNSSSPVVPNPDSVPPQLSSPALFYSSSSSQGDIYGRNNSQNLSQGEGNIRAAIGSSPLNFPSSSQRQNSDVFQSQGRQGRIRSSASASGRSRYHSDLRSDRALPTSSSSLGRNGQNRVHMRRNDIHTSDLSSPRRIVDFDTRSGVNTLDTSSSSAPPSEASEPLRIIWGTNVSIQECTTNFRNFLMSFKYKFRKILDEREEFINNTTDEELYYIKQLNEMRELGTSNLNLDARNLLAYKQTEDLYHQLLNYPQEVISIMDQTIKDCMVSLIVDNNLDYDLDEIETKFYKVRPYNVGSCKGMRELNPNDIDKLINLKGLVLRSTPVIPDMKVAFFKCNVCDHTMAVEIDRGVIQEPARCERIDCNEPNSMSLIHNRCSFADKQVIKLQETPDFVPDGQTPHSISLCVYDELVDSCRAGDRIEVTGTFRSIPIRANSRQRVLKSLYKTYVDVVHVKKVSDKRLDVDTSTIEQELMQNKVDHNEVEEVRQITDQDLAKIREVAAREDLYSLLARSIAPSIYELEDVKKGILLQLFGGTNKTFTKGGRYRGDINILLCGDPSTSKSQILQYVHKITPRGVYTSGKGSSAVGLTAYITRDVDTKQLVLESGALVLSDGGVCCIDEFDKMSDSTRSVLHEVMEQQTISIAKAGIITTLNARSSILASANPIGSRYNPNLPVTENIDLPPPLLSRFDLVYLVLDKVDEKNDRELAKHLTNLYLEDKPEHISQDDVLPVEFLTMYISYAKEHIHPIITEAAKTELVRAYVGMRKMGDDSRSDEKRITATTRQLESMIRLAEAHAKMKLKNVVELEDVQEAVRLIRSAIKDYATDPKTGKIDMNLVQTGKSVIQRKLQEDLSREIMNVLKDQASDSMSFNELIKQINEHSQDRVESSDIQEALSRLQQEDKVIVLGEGVRRSVRLNNRV
Protein: Membrane cofactor protein (CD antigen CD46) (O02839)
Organism: Sus scrofa (Pig)
Function: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. May act as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Inner acrosomal membrane of spermatozoa. {ECO:0000250}.
Interaction partners:
- CD59 glycoprotein
- Complement factor I
- Moesin
- Membrane cofactor protein
- Uncharacterized protein.
- Complement C4A
- Desmoglein 2
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
- Ectonucleoside triphosphate diphosphohydrolase 1
- CXADR Ig-like cell adhesion molecule
Sequence:
MMAFCALRKALPCRPENPFSSRCFVEILWVSLALVFLLPMPSDACDEPPKFESMRPQFLNTTYRPGDRVEYECRPGFQPMVPALPTFSVCQDDNTWSPLQEACRRKACSNLPDPLNGQVSYPNGDMLFGSKAQFTCNTGFYIIGAETVYCQVSGNVMAWSEPSPLCEKILCKPPGEIPNGKYTNSHKDVFEYNEVVTYSCLSSTGPDEFSLVGESSLFCIGKDEWSSDPPECKVVKCPYPVVPNGEIVSGFGSKFYYKAEVVFKCNAGFTLHGRDTIVCGANSTWEPEMPQCIKDSKPTDPPATPGPSHPGPPSPSDASPPKDAESLDGGIIAAIVVGVLAAIAVIAGGVYFFHHKYNKKRSK
Protein: 40S ribosomal protein S3 (Q389I7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S25
- 40S ribosomal protein S13, putative
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S14
- 40S ribosomal protein S33, putative
- 40S ribosomal protein S27, putative
- 40S ribosomal protein S15, putative
- Small ribosomal subunit protein uS4
- 40S ribosomal protein S5, putative
- 40S ribosomal protein S4
Sequence:
MGPLSKKRMMVRDGVFYAELFEFLKRELADDGFAGVEHRVTPTRTEIVIRSTKTREVLGEKGRRIRELTACLQQRFNYKEGKLQLFAERVEVRGLSAMAQAESLRFKLLSNLQVRRAAMGIIRYVMESGAKGCEVTIGGKIKGQRAKSMTFRDGYMIKSGTAHKHFVDTATRHCHLRAGTIGVNVKIMRPQSMIEEDEVLPDVITVIEPKTIEA
Protein: Phosphoinositide phosphatase (Q4QBX1)
Organism: Leishmania major
Interaction partners:
- Putative ATP-binding cassette protein subfamily A,member 6
Sequence:
MAAHKRIIEAEGLQNCRDLGGYRTRDGKHVVKYRHIYRSDNVGDVTPEGKKMLLEKLRLKYIIDFRGAEEKARSPYAFAGVTYLPIPIETCFVTEHMLTKPSLDGPSAEALLRRIATTFLIDFKDVYKSFFDVFLREAKGQPVLFHCTAGKDRTGVAAALLLTALDVPAETVMEDFMLTNRCCVPPSCETVKVGNCIISKDAVDLLFRAQAFFLELCFGEVCKRYGSVNAYMEKELGLGAVQLQKLRSYYVRPTSSSS
Protein: DNA repair and recombination protein RAD52 (P06778)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.
Subcellular location: Nucleus.
Interaction partners:
- DNA repair protein RAD57
- Replication factor A protein 1
- DNA repair protein RAD55
- DNA repair protein RAD59
- DNA repair protein RAD51
- DNA repair and recombination protein RAD54
- ATP-dependent DNA helicase SRS2
- Replication factor A protein 2
- ATP-dependent helicase SGS1
- ATP-dependent DNA helicase II subunit 1
Sequence:
MNEIMDMDEKKPVFGNHSEDIQTKLDKKLGPEYISKRVGFGTSRIAYIEGWRVINLANQIFGYNGWSTEVKSVVIDFLDERQGKFSIGCTAIVRVTLTSGTYREDIGYGTVENERRKPAAFERAKKSAVTDALKRSLRGFGNALGNCLYDKDFLAKIDKVKFDPPDFDENNLFRPTDEISESSRTNTLHENQEQQQYPNKRRQLTKVTNTNPDSTKNLVKIENTVSRGTPMMAAPAEANSKNSSNKDTDLKSLDASKQDQDDLLDDSLMFSDDFQDDDLINMGNTNSNVLTTEKDPVVAKQSPTASSNPEAEQITFVTAKAATSVQNERYIGEESIFDPKYQAQSIRHTVDQTTSKHIPASVLKDKTMTTARDSVYEKFAPKGKQLSMKNNDKELGPHMLEGAGNQVPRETTPIKTNATAFPPAAAPRFAPPSKVVHPNGNGAVPAVPQQRSTRREVGRPKINPLHARKPT
Protein: LIM domain transcription factor LMO4-A (LIM domain only protein 4-A) (LMO-4-A) (Xlmo4) (Q8AW92)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as a positive cofactor of GATA transcription factors to establish the identity of the ventral mesoderm during gastrulation. Down-regulation in the dorsal mesoderm is necessary for the proper formation of this territory since, when present, lmo4 may bind ldb1 and restrict the availability of this cofactor for Spemman organizer transcription factors. At neurula stages, suppresses primary neuron differentiation and modulates gene expression at the Isthmic Organizer of the midbrain-hindbrain boundary.
Interaction partners:
Sequence:
MVNNRSSESTTTAVSSNGSPPKACAGCGGKIGDRFLLYSMDRYWHTRCLKCSCCQAQLGEIGTSCYTKSGMILCRNDYIRLFGNSGACNACGQSIPASEMVMRAQGSVYHLKCFTCATCRNRLVPGDRFHYVNGTIFCEHDRPTGLLNGHLNPLQSNPLQGSPMLPDQKVC
Protein: Paired amphipathic helix protein sin-3 (Histone deacetylase complex subunit sin-3) (Transcriptional corepressor sin-3) (A5JYW9)
Organism: Caenorhabditis elegans
Function: Probable transcriptional repressor required for the deposition of dimethylated 'Lys-9' of histone H3 (H3K9me2) on asynapsed chromosome pairs (both autosomes and sex chromosomes) during meiosis, but this does not seem to solely affect the transcriptional status. Plays a role in ray fusion and patterning in the male tail, and this may be through activity of the histone deacetylase complex (HDAC).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
Interaction partners:
- PHD-type domain-containing protein
- Coexpressed With Polycystins
- Mortality factor related protein 1
- Nuclear receptor corepressor 1
- Chromo domain-containing protein
- Probable histone-binding protein rba-1
- Probable histone-binding protein lin-53
- Putative histone deacetylase 2
- Histone deacetylase
- Histone deacetylase 1
Sequence:
MYNPPPGGGGGNNGGDQSQQQPTNNATLFLLQMIQQSQHQQQHQNQQQQQLELQIRDQERILIEQQRMQHQQQQNQLLQGLNQFPFNPLGLFQVQAAVQAAQAQFAQNAQGSPIPFHIGSPLQPSHSPAASALQQQYLLPSHSPAITPFARNSEAARNIEQFIAQEEAANVPRANSQQQSPLIRPIPQQQALNIQNLTSTQQAQQILAHHRQVPVQQVQHQQHIPTPPLALPIAQQGPISNEVPSVPPVVPATSAGCPQREPRQQQGGRRQNRPGRRKKPEGPPRVDEALAYLRVIKSTFSSDVPVYHRFLEIMKDFRAQRIETPDVIEQVAELLYDSPELVLGFNTFLPTGYRITLTPDRKYVFSSPQMQPRVLLSPDERRARAIEAGAQAVGAIELGSQEGISKDEDRTIEDEDMDKSKEKDDVDGIDDEDDEESGIEDKNNEEMMEEDNHLIEEIICDDRKKDDCEDSQQEIEMSSELAAHTLNIIELLKKSFLARPTKLVDFMTFIDFFMSDQQYKKDMEKLRKDDEDDEIEENEKIEVDDVPGPSNAPQEIKKPDDIEKKDSSKNLQIEESCSDYLVSMLANCCIGEPDLLAATIDFLPYLGKLLVNGSDAIALKIKTILHFSATNDRNDIPPVNRVNPSDVDMDLVKQMEKCKMGTKKNEKLKLKVAGQGDEGATVELMILKKSYRILYERLKSRTTPNQLSHLMVLINAYANLDITREQLISELPKIMGTSGSDLEMIILQLLGAEKEPKNRPENDMDAVMRKDLPAIQPKRGLRDQKMLQQVKNVEAATVCTLGPSYRFMKDTKATDCSGRVELDDDLKGVLNDTWTSIPSWSSEDTGSQAIKKSNLEEFHFKTEDERYELDIIVDSNRTVIEQLSKTLRDYEAMSDEDKKSFKLDKWLNASSRSTTIRVLAKVFTNSAQDFIDAAQKNPLVGLRRILESLKEKDLLWSRFQQDTNRTWRDALDKQMSAATTILNNQHKNYDQKAFKSKPLVNQIEQICEERRKNNSTDTSPHLILEYTPERKVYRDVNDVTGHFFHDLSGTKCDRDRTKIVLFSYRILMEWLCQEGQQVQIDLDNGEIFKFQGDLNEDENLMTLLNMDGRRICGDRVVPVSTSLESNESSIDHFSENLHQKRTRRTFYGDDSVYMIIRYHHMIQERFAKILSTQAIYAQEHFDNQKKNKRWEDGIGADMHGRKALQENIKQRRAAVNDIRNVRSCPSSSYETTLRELKQLGNAQMDIVAFEEAVKNLFPGDIVLFNNIDKLFSSLAKNIHHATCAEERENPIKLYLKYRQRIMNAERDEDMESVIQEYGQTAEEVLRGKNTYRFEFVEEQNKPFIKIWVIPREEKDDDDDDDEEGNEGGKDEDNVKDEDDGGDGEGRDGPDDDQPPPSNDDGDDEEDEDDEEDGPSGADEPESTSGSGNVPMDHLNIGENFLWSPPEEKVCTGKMTTNEKEQRNSVDYMKVTTTPRLRIHKRMLKEHKGCNVELMTGFQQLSAIVPLM
Protein: Proteasome assembly chaperone 4 (PAC-4) (mPAC4) (Proteasome chaperone homolog 4) (Pba4) (P0C7N9)
Organism: Mus musculus (Mouse)
Function: Chaperone protein which promotes assembly of the 20S proteasome.
Interaction partners:
- Proteasome assembly chaperone 3
- Proteasome assembly chaperone 2
- Proteasome maturation protein
Sequence:
MEESRAAADADVSLHNFSARLWEQLVHFHVMRLTDSLFLWVGATPHLRNLAVAMCSRYDPIPVCTSLFGDTSDTTSTGLAQRLARKTSKQVFVSYNLSNTDSNFTLLVENRIKEEMETFPEKF
Protein: Formate dehydrogenase, alpha subunit, selenocysteine-containing (EC 1.2.1.2) (Q72EJ1)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Subcellular location: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
Interaction partners:
- Formate dehydrogenase, beta subunit, putative
- Formate dehydrogenase, beta subunit, putative
- Formate dehydrogenase 2 subunit beta
- Pyridine nucleotide-disulfide oxidoreductase
- Iron-sulfur protein CooF
- Formate dehydrogenase, alpha subunit, selenocysteine-containing
- Carbon monoxide dehydrogenase
- Formyltetrahydrofolate deformylase
- Formate dehydrogenase 2 subunit alpha
- Formamidase
Sequence:
MTVTRRHFLKLSAGAAVAGAFTGLGLSLAPTVARAELQKLQWAKQTTSICCYCAVGCGLIVHTAKDGQGRAVNVEGDPDHPINEGSLCPKGASIFQLGENDQRGTQPLYRAPFSDTWKPVTWDFALTEIAKRIKKTRDASFTEKNAAGDLVNRTEAIASFGSAAMDNEECWAYGNILRSLGLVYIEHQARIUHSPTVPALAESFGRGAMTNHWNDLANSDCILIMGSNAAENHPIAFKWVLRAKDKGATLIHVDPRFTRTSARCDVYAPIRSGADIPFLGGLIKYILDNKLYFTDYVREYTNASLIVGEKFSFKDGLFSGYDAANKKYDKSMWAFELDANGVPKRDPALKHPRCVINLLKKHYERYNLDKVAAITGTSKEQLQQVYKAYAATGKPDKAGTIMYAMGWTQHSVGVQNIRAMAMIQLLLGNIGVAGGGVNALRGESNVQGSTDQGLLAHIWPGYNPVPNSKAATLELYNAATPQSKDPMSVNWWQNRPKYVASYLKALYPDEEPAAAYDYLPRIDAGRKLTDYFWLNIFEKMDKGEFKGLFAWGMNPACGGANANKNRKAMGKLEWLVNVNLFENETSSFWKGPGMNPAEIGTEVFFLPCCVSIEKEGSVANSGRWMQWRYRGPKPYAETKPDGDIMLDMFKKVRELYAKEGGAYPAPIAKLNIADWEEHNEFSPTKVAKLMNGYFLKDTEVGGKQFKKGQQVPSFAFLTADGSTCSGNWLHAGSFTDAGNLMARRDKTQTPEQARIGLFPNWSFCWPVNRRILYNRASVDKTGKPWNPAKAVIEWKDGKWVGDVVDGGGDPGTKHPFIMQTHGFGALYGPGREEGPFPEHYEPLECPVSKNPFSKQLHNPVAFQIEGEKKAVCDPRYPFIGTTYRVTEHWQTGLMTRRCAWLVEAEPQIFCEISKELAKLRGIGNGDTVKVSSLRGALEAVAIVTERIRPFKIEGVDVHMVGLPWHYGWMVPKNGGDTANLLTPSAGDPNTGIPETKAFMVDVRKV
Protein: F-box/kelch-repeat protein SKIP20 (SKP1-interacting partner 20) (Q9M1Y1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- F-box/kelch-repeat protein At1g23390
- F-box/kelch-repeat protein At4g39580
- U-box domain-containing protein 45
- Probable aspartyl protease At4g16563
- BTB/POZ domain-containing protein At2g30600
- U-box domain-containing protein 29
- F-box protein PP2-A14
- Probable ADP-ribosylation factor At2g15310
- Probable CCR4-associated factor 1 homolog 5
- At2g17880
Sequence:
MGVSKKKSGEIRGDLIPGLPEELAIECLVRVPFQFHSSIKSVCRSWKCVISSRSFIKERIGFGKAESLLCLVQPLTSPPSPAMMEGGEMSQKKKEEEEGESQMTQQLLQPRITGTPLYGLSVYNATLDTWHRVAIPERIPLFCECVAIQDAGKVLLIGGWDPETLQPVRDVFVLDFFAGEGSGRRFRRGRPMSAARSFFACASVGSTKVYVAGGHDDQKNALRSAEVYDVEKDEWSMLPPMTEGRDECHGFSMATDPGFCVLSGYGTETQGQFRSDGEIYDPITNSWSTIENVWPFPDLSPRGRTAAAAAEFPGDFRGCRLWCFIDSERQSQPHWEVEDDSMKWKVIMDTIRLPVTTMTSVFAGSLSGQAVAMIGGGGEESGTMMVKTTAEKNGGKWSHVNTPSGFSSLPFSCSSIYV
Protein: CDK-activating kinase assembly factor MAT1 (CDK7/cyclin-H assembly factor) (Menage a trois) (RING finger protein MAT1) (Q8SX08)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003338}.
Interaction partners:
Sequence:
MDDQACPRCKTTKYRNPSLKLMVNVCGHTLCESCVDLLFLKGSGACPECMVPLRRNNFRVQLFEDPMVEKEVDIRRRILRDYNKREEDFASLAEYNDYLEEIEDIVYNLCNNIDIIETNKRIEAYKRDNREVIQRNKTRVGRDEYALEEMLELEKVQEEARRKELEELENEHKKKKARDKQALIEELMYSGKDAAQIVTEFAEKAEKQREEEKQLPPPKPANEFSTGIKFGQTADPSLLPVPKSEEGPLFVYEPLVPFSEGPAMPPTNEIVSGGYIAHIRAETPQENAGGFTSALACERALQEALQGLYYTATTGVVSGT
Protein: Tricin synthase 1 (EC 2.1.1.175) (Caffeoyl-CoA 3-O-methyltransferase ROMT15) (Q9XGP7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers. No 3',4',5'-trimethylated ester derivatives are produced. Can use caffeoyl-CoA, 5-hydroxyferulic acid, luteolin, tricetin, quercetin, myrcetin and 7,8-dihydroxyflavone as substrates, but not naringenin, apigenin or kaempferol. The 2,3-double bond and the O-dihydroxyl group of the substrate are both required for catalytic activity of the enzyme.
Subcellular location: Nucleus {ECO:0000269|PubMed:15659629}.
Interaction partners:
- 4-coumarate--CoA ligase 2
- 4-coumarate--CoA ligase-like 9
- Agmatine hydroxycinnamoyltransferase 1
- Chalcone synthase 1
- Hydroxycinnamoyltransferase 4
- 4-coumarate--CoA ligase-like 5
- 4-coumarate--CoA ligase-like 6
- Thymidine kinase
- Chalcone synthase 2
- 4-coumarate--CoA ligase-like 3
Sequence:
MTTGNGDAPVIKNAHSDIDSTNKTLLKSDALYKYVLDTTVLPREPECMRDLRLITDKHQWGFMQSSADEAQLLGMLLKMAGAKRTIEVGVFTGYSLLATALALPEDGKVVAIDPDRESYEIGRPFLEKAGVAHKVDFREGKGLEKLDELLAEEAAAGREAAFDFAFVDADKPNYVKYHEQLLQLVRVGGHIVYDNTLWAGTVALPPDTPLSDLDRRFSVAIRDLNSRLAADPRIDVCQLAIADGITICRRLV
Protein: Cytochrome P450 26C1 (Cyp26c1) (EC 1.14.14.1) (Cytochrome P450, family 26, subfamily c, polypeptide 1) (B2RXA7)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Retinal dehydrogenase 2
- Retinaldehyde dehydrogenase 3
- Aldehyde dehydrogenase 1A1
- Cytochrome P450 26A1
- Cytochrome P450 3A
- Cytochrome P450 3A11
- Cytochrome P450 1A1
- Cytochrome P450 1A2
- Aldehyde dehydrogenase, cytosolic 1
- Cytochrome P450 3A25
Sequence:
MISWGLSCLSVLGAAGTTLLCAGLLLGLAQQLWTLRWTLSRDWASTLPLPKGSMGWPFFGETLHWLVQGSRFHSSRRERYGTVFKTHLLGRPVIRVSGAENVRTILLGEHRLVRSQWPQSAHILLGSHTLLGAVGEPHRQRRKVLARVFSRSSLEQFVPRLQGALRREVRSWCAAQRPVAVYQAAKALTFRMAARILLGLQLDEARCTELAHTFEQLVENLFSLPLDVPFSGLRKGIRARDQLYEHLDEAVAEKLQEKQTAEPGDALLLIINSARELGHEPSVQELKELAVELLFAAFFTTASASTSLILLLLQHPAAITKIQQELSAQGLGRACTCTPRASGSPPDCGCEPDLSLAMLGRLRYVDCVVKEVLRLLPPVSGGYRTALRTFELDGYQIPKGWSVMYSIRDTHETAAVYRSPPEGFDPERFGVESGDARGSGGRFHYIPFGGGARSCLGQELAQAVLQLLAVELVRTARWELATPAFPVMQTVPIVHPVDGLLLFFHPLPTSGAGDGLPF
Protein: Stimulator of interferon genes protein (STING) (Transmembrane protein 173) (A8E5V9)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy. Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol. Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome. Exhibits guanine base-specific ligand recognition. Binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP. Lacks the C-terminal tail (CTT) found in other vertebrate orthologs which is essential for interferon signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30842662}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase tbk1 is recruited (PubMed:30842662). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:30842662}.
Interaction partners:
- Serine/threonine-protein kinase TBK1
- CARD_2 domain-containing protein.
- Transmembrane 6 superfamily member 2.
- KIAA1841
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MACVLAIGSILFVWILGKGKYSGAQLIYRMATNFAISQGCCLVTCACELTEEIKHLHTRYNGHYWRALKASFNLSCAAFVTAILCYVFYEPKLMASLPLTIDITLTLLSWLFCWILGIQGPTPATISEITEIKQLNVAHGLAWSYYVGYLQFVLPALKESIQKFNEENHNLLKFPETCRLHILIPLSCRLYGDLKDVDENITFLKEIPPLYIDRAGIKGRVFKNNVYRILDEDGRPYNCIVEYATPLASLLKMTDIPSAAFSADDRLQQTKLFYRTLKDILENAHELQNTYRLIVYEDFPETKDHSRHLLSQEILKHIRQQHSEEYSML
Protein: BTB/POZ domain-containing protein At2g46260 (O82343)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Cullin-3A
- Cullin-3B
- Phytochrome B
- Protein NBR1 homolog
- Transcription factor PIF3
- Phytochrome D
- E3 ubiquitin-protein ligase PRT1
- E3 ubiquitin-protein ligase COP1
- F-box/kelch-repeat protein At4g19330
- Cullin-1
Sequence:
MRGSNNTDLFDPKTEMDSNFSRHGSSSEGDFGFAFNDSNFSDRLLRIEILGGPSDSRSDAEGCTSIADWARHRKRRREDNKKDNGVAISDIVACAEEQILTDNNQPDMDDAPGGDNLDDEGEAMVEEALSGDDDASSEPNWGIDCSTVVRVKELHISSPILAAKSPFFYKLFSNGMRESEQRHVTLRISAQEEGALMELLNFMYSNSLSVTTAPALLDVLMAADKFEVASCMRYCSRLLRNMPMTPDSALLYLELPSSVLMAEAVQPLTDAAKQFLASRYKDITKFHDEVMALPLAGIEAILSSDDLQIASEDAVYDFVLKWARGQYSSLEDRREILGSRLALYIRFPYMTCRKLKKVLTCSDFEHEVASKQVLEALFFKAEAPHRQRILAAEGSDSMNRRFIERAYKYRPVKVVEFELPRPQCVVYLDLKREECAGLFPSGRVYSQAFHLGGQGFFLSAHCNMDQQSSFHCFGLFLGMQEKGAVSFGVDYEFAARDKSTKEEYVSKYKGNYTFTGGKAVGYRNLFGIPWTSFIAEDSQHFINGILHLRAELTIKRSSDLH
Protein: Structural maintenance of chromosomes protein 4 (SMC protein 4) (SMC-4) (Chromosome assembly protein XCAP-C) (Chromosome-associated protein C) (P50532)
Organism: Xenopus laevis (African clawed frog)
Function: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerase.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MPPKKTKTSTAVAREATESPMAERSRAPDALQADPPAPTQESNNELVDSRSLEEILSGIPPPPPPAMTNEAGAPRLMITHIVNQNFKSYAGERILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDVQSCTVEVHFQKIIDKEGDDFEVIPNSNFYVSRTAYKDNSSVYHISGKKATFKDVGLLLRSHGIDLDHNRFLILQGEVEQIAMMKPKGQTEHDEGMLEYLEDIIGSERLKEPIQILCRRVELLNEQRGEKLNRVKMVEKEKDALEGEKNKAIEFLTVENETFKKKNQLCQYYIHDLQKRSRDKEAQKEKIQEDTKDISEKSNTLLETMKEKNKALKDVEKQLNKITKFIEENREKFTQLDLQDVDTREKLKHSKSKVKKLQKQLQKDKEKVDELKNVPANSQKIIAEETNKKDLLEKQKEKEEEKLKNVMDSLKKETQGLQEEKEVKEKELMEISKTVNEARSKMDVAQSELDIYLSRHNSALSQLNKAKEALNTASATLKERRAAIKELETKLPKDEGDLKKREKELESLVSEEGNIKNQVRELRQKVEEARSSLSANRSRGKVLDALIQQKKSGKIPGIFGRLGDLGAIDEKYDVAISSSCGALDHIVVDTIDTAQECVNFLKKQNVGVATFIGLDKMKVWEKGLNKIQTPENIPRLFDMVKVKDEQIKPAFYFALRDTIVANNLDQATRVAFQKDKRWRVVTLQGQIIEQSGTMTGGGGKVMKGRMGSSVMVEISDDQLQKMENKLKTDTTRATEIQDRKAHLEEEVAKLRQATREMKNTFEKYTASLQSLSEQEVHLKAQVKELEVNVAAAAPDKNQQKQMEKNLETLKKEYEKVAEKAGKVEAEVKRLHKLIVDINNHKLKAQQDKLDKVTKEIDECASAITKAQVSIKTADRNLKKSEEAVARTEKEIVANDKSIEELTEDLKKLEEKATTVMNECKEAECSLPEVQEQHRSLLQEIKAIQEKEHALQKEALNIRLNIEQIDSHIAEHQSKIKYWQKEITKISLHKIEDIPEEVLPGLAQEELEAIKDPDQIINQIALLEAKSHEMKPNLGAIAEYKKKEELYLQRVAELDEITNERDSFRRAYEDLRKQRLNEFMAGFNIITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEIADRLIGIYKTHNTTKSVATNPKIIAAKGLAEMQSVGCA