wanglab/gogpt-training-data huggingface dataset:
Protein: Phytanoyl-CoA dioxygenase domain-containing protein 1 (Protein PHYHD1) (EC 1.14.11.-) (Q5SRE7)
Organism: Homo sapiens (Human)
Function: 2-oxoglutarate(2OG)-dependent dioxygenase that catalyzes the conversion of 2-oxoglutarate to succinate and CO(2) in an iron-dependent manner. However, does not couple 2OG turnover to the hydroxylation of acyl-coenzyme A derivatives, implying that it is not directly involved in phytanoyl coenzyme-A metabolism. Does not show detectable activity towards fatty acid CoA thioesters.
Interaction partners:
Sequence:
MACLSPSQLQKFQQDGFLVLEGFLSAEECVAMQQRIGEIVAEMDVPLHCRTEFSTQEEEQLRAQGSTDYFLSSGDKIRFFFEKGVFDEKGNFLVPPEKSINKIGHALHAHDPVFKSITHSFKVQTLARSLGLQMPVVVQSMYIFKQPHFGGEVSPHQDASFLYTEPLGRVLGVWIAVEDATLENGCLWFIPGSHTSGVSRRMVRAPVGSAPGTSFLGSEPARDNSLFVPTPVQRGALVLIHGEVVHKSKQNLSDRSRQAYTFHLMEASGTTWSPENWLQPTAELPFPQLYT
Protein: FYN-binding protein 1 (Adhesion and degranulation promoting adaptor protein) (ADAP) (FYB-120/130) (p120/p130) (FYN-T-binding protein) (SLAP-130) (SLP-76-associated phosphoprotein) (O15117)
Organism: Homo sapiens (Human)
Function: Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton. Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2. May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9671755}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction {ECO:0000250|UniProtKB:O35601}. Note=Colocalizes with TMEM47 at cell-cell contacts in podocytes. {ECO:0000250|UniProtKB:O35601}.
Interaction partners:
- Lymphocyte cytosolic protein 2
- Src kinase-associated phosphoprotein 1
- Src kinase-associated phosphoprotein 2
- GRB2-related adapter protein 2
- Tyrosine-protein kinase Fyn
- Proto-oncogene vav
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Caspase recruitment domain-containing protein 11
- SH2/SH3 adapter protein NCK1
- Vasodilator-stimulated phosphoprotein
Sequence:
MAKYNTGGNPTEDVSVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPAGPSNVPKFGSPKPPVAVKPSSEEKPDKEPKPPFLKPTGAGQRFGTPASLTTRDPEAKVGFLKPVGPKPINLPKEDSKPTFPWPPGNKPSLHSVNQDHDLKPLGPKSGPTPPTSENEQKQAFPKLTGVKGKFMSASQDLEPKPLFPKPAFGQKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKDHAGEISSLPFPGVVLKPAASRGGPGLSKNGEEKKEDRKIDAAKNTFQSKINQEELASGTPPARFPKAPSKLTVGGPWGQSQEKEKGDKNSATPKQKPLPPLFTLGPPPPKPNRPPNVDLTKFHKTSSGNSTSKGQTSYSTTSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPPFDLKSPVNEDNQDGVTHSDGAGNLDEEQDSEGETYEDIEASKEREKKREKEEKKRLELEKKEQKEKEKKEQEIKKKFKLTGPIQVIHLAKACCDVKGGKNELSFKQGEQIEIIRITDNPEGKWLGRTARGSYGYIKTTAVEIDYDSLKLKKDSLGAPSRPIEDDQEVYDDVAEQDDISSHSQSGSGGIFPPPPDDDIYDGIEEEDADDGFPAPPKQLDMGDEVYDDVDTSDFPVSSAEMSQGTNVGKAKTEEKDLKKLKKQEKEEKDFRKKFKYDGEIRVLYSTKVTTSITSKKWGTRDLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYLADNDGEIYDDIADGCIYDND
Protein: Thyroid hormone receptor alpha (Nuclear receptor subfamily 1 group A member 1) (c-erbA-1) (c-erbA-alpha) (P63059)
Organism: Rattus norvegicus (Rat)
Function: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.
Subcellular location: Nucleus.; SUBCELLULAR LOCATION: [Isoform Alpha-2]: Cytoplasm {ECO:0000250|UniProtKB:P63058}. Nucleus {ECO:0000250|UniProtKB:P63058}. Note=When overexpressed found in the cytoplasm where it colocalizes with TACC1. {ECO:0000250|UniProtKB:P63058}.
Interaction partners:
- Nuclear receptor corepressor 1
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Retinoic acid receptor RXR-alpha
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Mediator of RNA polymerase II transcription subunit 1
- Actin, cytoplasmic 1
- Retinoic acid receptor RXR-beta
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Histone deacetylase 1
- Histone deacetylase 1
Sequence:
MEQKPSKVECGSDPEENSARSPDGKRKRKNGQCPLKSSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYDSCCVIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHVATEAHRSTNAQGSHWKQRRKFLPDDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDDTEVALLQAVLLMSTDRSGLLCVDKIEKSQEAYLLAFEHYVNHRKHNIPHFWPKLLMKEREVQSSILYKGAAAEGRPGGSLGVHPEGQQLLGMHVVQGPQVRQLEQQFGEAGSLRGPVLQHQSPKSPQQRLLELLHRSGILHSRAVCGEDDSSEASSLSSSSSDEDTEVFEDLAGKAASP
Protein: 2'-phosphotransferase (EC 2.7.1.160) (Q5A7N4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- tRNA ligase
- U3 small nucleolar RNA-associated protein 11
- Cytochrome c oxidase assembly factor 6
- Pre-mRNA-splicing factor ISY1
- Mitochondrial zinc maintenance protein 1
Sequence:
MPPPDKARRDVLISKALSYLLRHGAEKEKLSIDDQGYVKISDVLSHQRLKSLKTTRDDINRIVQENDKKRFTIKDDMICANQGHSLKAVKNDNLTPMTVDELNQLRIYHGTYRTKLPLIKSSGGLSKMNRNHIHFTCEQYSTCSGIRYNANVLIYINASKCIEHGIVFYKSLNNVILTSGDKDGKLSWEFIDRIVGLDGNEINKEQV
Protein: Uncharacterized protein (Q38BK5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
Sequence:
MVQQGNHVALFPTPRLYTADVVGNVYVTTFPASSVGETNKAEPPAKRRRVDNQSSGGVDEHPFWEPVVAASTSGAEAYGARGWCGLTPLADDQVVCCREFFFDLRLLDARNCGAVIRQYGTLHAPTGMATCGGIFPHGVVVAEGPVASVYDTRCSGAVMTKQTEAMSGGQRSVPLVSSRFTDATTRVADVCATCNEFEVAIAVGRAVCVHDIRKWTRVSITTSVLKYDIGSIAPFACGKGVVAAGIDAEVRLVLLTEKLNGASSTTGTVVHGEGNCCGGNGSKKEVDVDVNGGAAVKSDELTSVTSFRNRIDSVVSCRSTWQGGWVPSVDASCATGISADHEFFMAF
Protein: Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) (Isopentenyl pyrophosphate isomerasee) (IPP isomerase) (Q10132)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Isopentenyl-diphosphate delta-isomerase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway. Idi1 catalyzes the 1,3-allylic rearrangement of isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). 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 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 fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Diphosphomevalonate decarboxylase
- Farnesyl pyrophosphate synthase
- Geranylgeranyl pyrophosphate synthase
- Hydroxymethylglutaryl-CoA synthase
- Squalene epoxidase erg1
- Lanosterol 14-alpha demethylase erg11
- Lanosterol synthase erg7
- Acetyl-CoA acetyltransferase
- C-4 methylsterol oxidase erg25
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Sequence:
MIMSSQQEKKDYDEEQLRLMEEVCIVVDENDVPLRYGTKKECHLMENINKGLLHRAFSMFIFDEQNRLLLQQRAEEKITFPSLWTNTCCSHPLDVAGERGNTLPEAVEGVKNAAQRKLFHELGIQAKYIPKDKFQFLTRIHYLAPSTGAWGEHEIDYILFFKGKVELDINPNEVQAYKYVTMEELKEMFSDPQYGFTPWFKLICEHFMFKWWQDVDHASKFQDTLIHRC
Protein: WAS/WASL-interacting protein family member 3 (Corticosteroids and regional expression protein 16 homolog) (A6NGB9)
Organism: Homo sapiens (Human)
Function: May be a regulator of cytoskeletal organization. May have a role in spermatogenesis (By similarity).
Subcellular location: Cytoplasm. Note=In hippocampal neurons colocalizes with WASL in the cell body, axons and the growth cone. {ECO:0000250}.
Interaction partners:
- Actin nucleation-promoting factor WASL
- SH2/SH3 adapter protein NCK1
- Cytoplasmic protein NCK2
- WAS/WASL-interacting protein family member 1
- Actin nucleation-promoting factor WAS
- WAS/WASL-interacting protein family member 2
- Growth factor receptor-bound protein 2
- Actin-related protein 2
Sequence:
MPVPPPPPPPLPPPPPPLGAPPPPPPSAPPVSTDTSSLRRADPKGRSALLADIQQGTRLRKVTQINDRSAPQIESSKGTNKEGGGSANTRGASTPPTLGDLFAGGFPVLRPAGQRDVAGGKTGQGPGSRAPSPRLPNKTISGPLIPPASPRLGNTSEAHGAARTAPPRPNVPAPPPPTPPPPPPPLPPPLPSSSPIKTPLVSPPGPLTKGNLPVVAPPVPCAPPPPPPPPPPTPPPLPPASVLSDKAVKPQLAPLHLPPIPPPLPLLPPCGYPGLKAEPASPAQDAQEPPAPPPPLPPYASCSPRASLPAPPLPGVNSSSETPPPLPPKSPSFQAPPQKAGAQALPAPPAPPGSQPFLQKKRHGRPGAGGGKLNPPPAPPARSPTTELSSKSQQATAWTPTQQPGGQLRNGSLHIIDDFESKFTFHSVEDFPPPDEYKPCQKIYPSKIPRSRTPGPWLQAEAVGQSSDDIKGRNSQLSLKTLR
Protein: Cohesin subunit SA-1 (xSA-1) (SCC3 homolog 1) (Stromal antigen 1 homolog) (Q9DGN1)
Organism: Xenopus laevis (African clawed frog)
Function: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
Subcellular location: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
Interaction partners:
Sequence:
MITSELSVLQDSTNESAVMHTDMTAVSADLSTELVEDLEVKGKRKRGRPGRPPSAIKKPRKTPGDRSRAEPGSRGRGRANGHPQQNGEGDPVTLFEVVKMGKSAMQAVVDDWIESYKQDRDIALLDLINFFIQCSGCKGTVRIEMFRNMQNAEIIRKMTEEFDEDSGDYPLTMPGPHWKKFRCNFCEFISVLIRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYETERNKIINKRANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKMYSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSMTLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLVYSAHRPVAVAAGEFLHKKLFSRHDPQAEEALAKRRGRSSPNGNLVKMLVLFFLESELHEHAAYLVDSLWESSQELLKDWECMTELLVEEPMQGEEVMSERQESALVELMVCTIRQAAEAHPPVGRGTGKRVLTAKERKTQLDDKTKLTEHFIVALPVLLSKYSADAEKVANLLQIPQYFDLELYSTGRMEKHLDSLLKQIRFVVEKHIESDVLEACSKTYSILCSEEYTIQNRVEIAHSQLIDELADRFSHAVEELLQEAEEADEDEIYNVMASLKRLTCFHNAHDLTKWDFFGNCYRLLRAGIEHEGMMEQIVVQALQCSHYSILWQLVKITEGNPSKEEMLALRKTVKSFLAVCQQCLSSMTTLVKEQAFMLLCDLLMIFSHQLTTGGRENLLLLVFNPDVGLQSELLSFVMDHVFIDQDDENQSMEGDEEDEANKIEALHKRRNLLASFCKLIIYDIVDMNAAADIFKHYMKYYNDYGDIIKETLSKTRQMDKIQCAKTLILSLQQLFNELVQEQGPNLDRTSAHVSGIKELARRFALTFGLDQIKTREAVATLHKDGIEFAFKYQNPKGPEYPPLNLAFLEVLSEFSSKLLRQDKKTVHSYLEKFLTDLMMERREDVWLPLISYRNSLVTGGDEDRLSVNSGGSNSKGSSVRSKKGRPPLHKKRVIEEESIDNSWVTRNDTIQTPGALTTPQLTSTVLRENPRQIPEQIPEQESEPSSEPDFLHSPQMQMSWLGQQKLEDLNRKDRTSMSYMKVRSGVRHAVRGLMEDDAEPIFEDVMMSSRGQLEDMNEEFEDTMVIDLPPSRNRRERAELRPDFFDSAAIIEDDSGFGMPMF
Protein: Gamma-2-syntrophin (G2SYN) (Syntrophin-5) (SYN5) (Q9NY99)
Organism: Homo sapiens (Human)
Function: Adapter protein that binds to and probably organizes the subcellular localization of a variety of proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex (By similarity).
Subcellular location: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane.
Interaction partners:
- Dystrophin
- Dystrobrevin beta
- Alpha-1-syntrophin
- Beta-1-syntrophin
- Dystrobrevin alpha
- Beta-2-syntrophin
- Utrophin
- Phospholipid-transporting ATPase IG
- Dystroglycan 1
- Delta-sarcoglycan
Sequence:
MGTEGPPPPAASRGRQGCLLVPARTKTTIALLYDEESENAYDIRLKLTKEVLTIQKQDVVCVGGSHQGRNRRTVTLRRQPVGGLGLSIKGGSEHNVPVVISKIFEDQAADQTGMLFVGDAVLQVNGIHVENATHEEVVHLLRNAGDEVTITVEYLREAPAFLKLPLGSPGPSSDHSSGASSPLFDSGLHLNGNSSTTAPSSPSSPIAKDPRYEKRWLDTLSVPLSMARISRYKAGTEKLRWNAFEVLALDGVSSGILRFYTAQDGTDWLRAVSANIRELTLQNMKMANKCCSPSDQVVHMGWVNEKLQGADSSQTFRPKFLALKGPSFYVFSTPPVSTFDWVRAERTYHLCEVLFKVHKFWLTEDCWLQANLYLGLQDFDFEDQRPYCFSIVAGHGKSHVFNVELGSELAMWEKSFQRATFMEVQRTGSRTYMCSWQGEMLCFTVDFALGFTCFESKTKNVLWRFKFSQLKGSSDDGKTRVKLLFQNLDTKQIETKELEFQDLRAVLHCIHSFIAAKVASVDPGFMDSQSLARKYMYSS
Protein: Na(+)/H(+) antiporter (P36606)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Sodium export from cell, takes up external protons in exchange for internal sodium ions. Involved in regulation of pH.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9094438}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized Na
- Putative cation exchanger C3A12.06c
- Potassium transport protein 1
- K
Sequence:
MGWRQLDIDKVHLALIVAGGFITFFCYFSEVFRKKLLVGEAVLGSITGLIFGPHAAKLVDPFSWGDHGDYLTVEICRIVLDVRVFASAIELPGAYFQHNFRSIIVMLLPVMAYGWLVTAGFAYALFPQINFLGSLLIAGCITSTDPVLSALIVGEGPLAKKTPERIRSLLIAESGCNDGMAVPFFYFAIKLLTVKPSRNAGRDWVLLVVLYECAFGIFFGCVIGYLLSFILKHAQKYRLIDAISYYSLPLAIPLLCSGIGTIIGVDDLLMSFFAGILFNWNDLFSKNISACSVPAFIDQTFSLLFFTYYGTIIPWNNFNWSVEGLPVWRLIVFSILTLVCRRLPVVFSVKPLVPDIKTWKEALFVGHFGPIGVCAVYMAFLAKLLLSPDEIEKSIYESTTVFSTLNEIIWPIISFVILSSIIVHGFSIHVLVIWGKLKSLYLNRKVTKSDSDLELQVIGVDKSQEDYV
Protein: Cytochrome P450 26C1 (EC 1.14.14.1) (Cytochrome P450, family 26, subfamily C, polypeptide 1) (A1L1M2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Aldehyde dehydrogenase 1 family member A3
- Cytochrome P450, family 3, subfamily A, polypeptide 65
- Cytochrome P450 26A1
- Cytochrome P450 1A
- Aldehyde oxidase 6
- Cytochrome P450 26B1
- Xanthine dehydrogenase/oxidase
- Aldehyde dehydrogenase 1 family, member A2
Sequence:
MFGHDFCLVSALLSVADAVLPTVLLLAVSRLLWEFRWSITRDRTCKLPLPQGSMGWPLVGETFHWLFQGSSFHISRREKHGKVFKTHLLGKPLIRVTGAENIRKILLGEHTVVCTQWPQSTRIILGPNTLVNSVGDLHKRKRKVLAKVFSRGALEAYLTRLQDVVKSEIAKWCTETGSVEVYTAAKSLTFRIAVRVLLGLHLEEQQITYLSKTFEQLMNNLFSLPIDTPVSGLRKGIRAREILHSAMEKIIEEKLKKQQASDYCDAFDYMLSSARENDYELTMQELKETAVELIFAAHSTTASASTSLIMQLLRHPDVSERARAELESEGLITDGHGHCRSRCNGNAISEEGEAAEKSTSDRRSAINKATYFEAGDKEEGRRSRTHVPYLSLEKLSQLSYLDCVVKEVLRFLPPVSGGYRTVLQTFELNGYQIPKGWSVMYSIRDTHETAEAYQNPELFDPDRFCVGREESKSERFSYVPFGGGVRRCIGRELALIVLKTLAVELLATADCTLATQTYPRMQTVPIVHPVNGLHVFFNYRTQGIERNRRESTHI
Protein: NEFL protein (I6L9F6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISVMQDTINKLENELRTTKSEMARYLKEYQDLLT
Protein: General odorant-binding protein 56a (Q9V8Y2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MNSYFVIALSALFVTLAVGSSLNLSDEQKDLAKQHREQCAEEVKLTEEEKAKVNAKDFNNPTENIKCFANCFFEKVGTLKDGELQESVVLEKLGALIGEEKTKAALEKCRTIKGENKCDTASKLYDCFESFKPAPEAKA
Protein: Cyclic nucleotide-binding domain-containing protein (TAX2) (G5EEE2)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Cyclic nucleotide-gated channel
- Cyclic nucleotide-binding domain-containing protein
- Receptor-type guanylate cyclase daf-11
- Cyclic nucleotide-binding domain-containing protein
- Guanine nucleotide-binding protein alpha-17 subunit
- Guanine nucleotide-binding protein alpha-3 subunit
- Cyclic nucleotide-binding domain-containing protein
- Cyclic nucleotide-binding domain-containing protein
- Receptor-type guanylate cyclase gcy-10
- Receptor-type guanylate cyclase gcy-8
Sequence:
MYQVPKRAKTNLAREIRKREFSYVDRQKASKPTQLSEKEWKSPRSEDSFDLLDPANASKEPSASTRPLPYPPTRPPEVVIQIDEVESPILGLIDETDDHELDGRLDPASSFDANSLSATRASSIIEDDVRSQISFIMRERLHSIAKEVHRRTSAVREDLIRETPEDTVSMASNVPKQNEHRPSLMSLIGLQNRSESPTVDTVKNCFGFSLKGTFHPYGRFYMTWLSLVTLCFLFNAFCIPLRSSYPYQTADNWMYWFIVDYSCDLVYVIDMLLIKPRLRFTRGGIQVKIYKDTQRHYLMTRTFKLDILSILPTDLMYFFFGKMPIWRINRVLKINSFWLLFDMLDNSFANPYAIRIARTLSYMIYIIHCNSCVYYKLSALQAFGQIAYLENGKWYLNKWVYNNQGNAYIRCFYFTAAVATSTGNNPAPTNVIEYIYMTCSWMMGVFVFALLLGQIRDIVSNANRNREEFQRKMDLALGECKKLGLKMETTNRVRDWFIYTWQQQKTLDEKKLIEKLPLKLQTDLALSVHYTTLSKVQLFQDCDRALLRDLVLKLRPVIFLPGDMICLKGDVGKEMYIINQGILQVVGGDHNEKIFAELAQGAVFGEISLLAIGGNNRRTASIRAKGYCTLFVLAKEDLNDVIRYYPQAQTILRRKAAAMLKNDKKSDEKTEKIKAQAELEDRCKINPRQVPKLITLIANMTEMNENKGVQELKKVIEEETEKSRRQSIYYPWSTLQRDDDDEEEWNDEEDLSDVGEDFDLDPTNHSDDEDPMEDVDLAPEVHDDDWDQPGTSGTQKLHAD
Protein: ATP-dependent 6-phosphofructokinase isozyme 2 (ATP-PFK 2) (Phosphofructokinase 2) (EC 2.7.1.11) (6-phosphofructokinase isozyme II) (Phosphohexokinase 2) (P06999)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Interaction partners:
- ATP-dependent 6-phosphofructokinase isozyme 1
- Fructose-bisphosphate aldolase class 1
- Fructose-1,6-bisphosphatase class 1
- PTS system fructose-specific EIIB'BC component
- Glucose-6-phosphate isomerase
- PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component
- Uncharacterized protein YdiZ
- Transketolase 2
- Fructose-bisphosphate aldolase class 2
- Fructose-like PTS system EIIBC component
Sequence:
MVRIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATVEAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRCIVDSSGEALSAALAIGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYAYLSR
Protein: At2g28430/T1B3.5 (Expressed protein) (Zinc finger, C3HC4 type family protein) (Q9SKM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- MICOS complex subunit, putative
- At5g14105
- At1g68680
- Mitochondrial import inner membrane translocase subunit TIM22-1
- Mitochondrial import inner membrane translocase subunit TIM22-4
- Mitochondrial import inner membrane translocase subunit TIM23-2
Sequence:
MISILAQERLLGYTLGSALTGFIVFEQRKLIHDSVSDPKSQSIDQAQVSDRIFGKKYRMEFASLWNKAVDQTFEPAIEYLSSRKW
Protein: Ureidoglycolate hydrolase (AtUAH) (EC 3.5.1.116) (Allantoate amidohydrolase 2) (AtAHH2) (Ureidoglycolate amidohydrolase) (Q8VXY9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the catabolism of purine nucleotides. Can use (S)-ureidoglycolate as substrate, but not (R)-ureidoglycolate or allantoate. The sequential activity of AAH, UGLYAH and UAH allows a complete purine breakdown without the intermediate generation of urea.
Subcellular location: Endoplasmic reticulum {ECO:0000305|PubMed:23940254}.
Interaction partners:
- (S)-ureidoglycine aminohydrolase (AtUGLYAH)
- Urease
- Allantoinase
- Glycerate dehydrogenase HPR, peroxisomal
- Malate synthase
- Glyoxylate/succinic semialdehyde reductase 1
- Dihydropyrimidinase
- Glutamate--glyoxylate aminotransferase 2
- Glycolate oxidase 1
- Dihydropyrimidine dehydrogenase
Sequence:
MESLKRFLCSIALLLISLLLPSSLAQQQQHESIRTMEDFSGYPIHEPGQFGSINLASSLSVDAPGLQNQIDELSSFSDAPSPSVTRVLYTDKDVSARRYVKNLMALAGLTVREDAVGNIFGKWDGLEPNLPAVATGSHIDAIPYSGKYDGVVGVLGAIEAINVLKRSGFKPKRSLEIILFTSEEPTRFGISCLGSRLLAGSKELAEALKTTVVDGQNVSFIEAARSAGYAEDKDDDLSSVFLKKGSYFAFLELHIEQGPILEDEGLDIGVVTAIAAPASLKVEFEGNGGHAGAVLMPYRNDAGLAAAELALAVEKHVLESESIDTVGTVGILELHPGAINSIPSKSHLEIDTRDIDEARRNTVIKKIQESANTIAKKRKVKLSEFKIVNQDPPALSDKLVIKKMAEAATELNLSHKMMISRAYHDSLFMARISPMGMIFIPCYKGYSHKPEEYSSPEDMANGVKVLSLTLAKLSLD
Protein: B-related factor 1 (D4A8W8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- B double prime 1, subunit of RNA polymerase III transcription initiation factor IIIB
- General transcription factor IIIC subunit 3
- TATA box binding protein
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit beta
- RNA polymerase I and III subunit C.
- DNA-directed RNA polymerase III subunit RPC3
- RNA polymerase III subunit E
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MTGRVCRGCGGTDIELDAARGDAVCTGCGSVLEDNIIVSEVQFVENSGGGSSAVGQFVSLDGAGKTPTLGGGFHVNLGKESRAQTLQNGILYFILADHGVGQDAGVGAAPHPPPGEPVATEPALPGHSLQLLQDGCKQASYPRTENGPCDCCLPLLDMLLDLSDLLQVNVYVLGKTFLLLARELCINAPAIDPCLYIPRFAHLLEFGEKNHEVSMTALRLLQRMKRDWMHTGRRPSGLCGAALLVAARMHDFRRTVKEVISVVKVCESTLRKRLTEFEDTPTSQLTIDEFMKIDLEEECDPPSYTAGQRKLRMKQLEQVLSKKLEEVEGEISTYQDAIEIELENSRPKAKGALANLSKDGSGEDATSSPFCEEDTEDEELEAAASHMNKDFYRELLGADGGSEAAEDADGGSRPLALESLLGPLPTAASLGISDSIRECISSPSGDPKDSSGDGELDLSGIDDLEIDRYILNESEARVKAELWMRENAEYLREQKEKEARIAKEKELGIYKEHKPKKSCKRREPILASTAGEAIEKMLEQKKISSKINYSVLRDLNSKGGGSPPRDDSQPPEHTSTKKLSRRKRAATRNSADPGTSMGKRLRPLVSAQPAKKAAVGEALLLNSPALGAEPVKPSAVLVESGPVSYHPEEDADEEDAEEEDGEPCVSALQMMGGNDYGCDGDEDDGY
Protein: Adaptor-related protein complex 1 subunit mu 2 (F1R3L9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
- AP-1 complex subunit gamma
- AP complex subunit beta
- AP-1 complex subunit gamma.
- AP complex subunit sigma
- AP complex subunit sigma
- AP complex subunit beta
- AP complex subunit sigma
- AP complex subunit beta
- AP-4 complex subunit epsilon
- AP-3 complex subunit sigma-2
Sequence:
MSASAVFVLDLKGKVLICRNYKGDVDMSEIDHFFTLLMQQEEDGLISPVMSHGNVHFLWIKHNNLYLVATTNKNSNASLVYAFLYKLVEVFTEYFKELEEESIQDNFVVVYELLDELMDFGFPQTTDSKILQEYITQQGQKLEVAKTKVPTTVTNAVSWRSEGIRYKKNEVFIDVIESINVLVNANGSVMSSDIVGCIRLKTMLSGMPELRLGLNDRVLFALTGRDKGKTVVMEDVKFHQCVRLSRFESDRTISFIPPDGESELMSYRINTHVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEIRVPVPSDADSPKFKTSTGHAKYVPEKNLVVWSIKSFPGGKEFLMRAHFGLPSVENDELEGKPPITVKFEIPYFTVSGIQVRYMKIIEKSGYQALPWVRYITQSGDYQLRTNS
Protein: Interferon-induced protein with tetratricopeptide repeats (A0A068FR04)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDSLLKGELEKLECHFTWDLGQYQNELQGMKRKMDHVDPQKISSPVHYYNLLGFIQKSLGSDREALESLQKAESVIQEQGTEETAVRLLVNKANLAWVYFYLGELEKSRGYLEELEELQRIHPAPPGCPLHPEVSGEKGWTLVKFNKSKKSQAIGYFKMALEAEPERKEWHKGLAISMSKACLWYKCTPEQKAEILEKVKTAAEIDPNDLFLQSLYVLKKFEVQGENVDEEIQSLLKKSISTANLVGLNYIIEYFKGISYGRAIEEVQRVREIFPSSSTLLKILANLYKWKVFSMKEDSRERRIWVQKSIELFEEVVRHYPDCVKGRSDLASLHRYAHNTERAEEIYQQLLSEDHTLPPHSQQLLYYSYACYVHHTGQSRDKSINFLMKAAEIKNYSYNKDKCIEILQTTVQNGRNSRCEEIKRFLKNVLKEE
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q9NHP2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDEHTLNDLLECSVCLERLDTTSKVLPCQHTFCRKCLQDIVASQHKLRCPECRILVSCKIDELPPNVLLMRILEGMKQNAAAGKGEEKGEETETQPERAKPQPPAESVAPPDNQLLQLQSHQQSHQPARHKQRRFLLPHAYALFDFASGEATDLKFKKGDLILIKHRIDNNWFVGQANGQEGTFPINYVKVSVPLPMPQCIAMYDFKMGPNDEEGCLEFKKSTVIQVMRRVDHNWAEGRIGQTIGIFPIAFVELNAAAKKLLDSGLHTHPLCHPPKQQGQRALPPVPVIDPTVVTESSSGSSNSTPGSSNSSSTSSSNNCSPNHQISLPNTPQHVVASGSASVRFRDKGAKEKRHSLNALLGGGAPLSLLQTNRHSAEILSLPHELSRLEVSSSTALKPTSAPQTSRVLKTTVQQQMQPNLPWGYLALFPYKPRQTDELELKKGCVYIVTERCVDGWFKGKNWLDITGVFPGNYLTPLRARDQQQLMHQWKYVPQNADAQMAQVQQHPVAPDVRLNNMLSMQPPDLPPRQQQATATTTSCSVWSKPVEALFSRKSEPKPDTATASTTSSSSSGAVGLMRRLTHMKTRSKSPGASLQQVPKEAISTNVEFTTNPSAKLHPVHVRSGSCPSQLQHSQPLNETPAAKTAAQQQQFLPKQLPSASTNSVSYGSQRVKGSKERPHLICARQSLDAATFRSMYNNAASPPPPTTSVAPAVYAGGQQQVIPGGGAQSQLHANMIIAPSHRKSHSLDASHVLSPSSNMITEAAIKASATTKSPYCTRESRFRCIVPYPPNSDIELELHLGDIIYVQRKQKNGWYKGTHARTHKTGLFPASFVEPDC
Protein: Galectin-6 (Gal-6) (O54891)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAYVPAPGYQPTYNPTLPYKRPIPGGLSVGMSFYIQGTAKENMRRFHVNFAVGQDDGADVAFHFNPRFDGWDKVVFNTKQSGRWGKEEEKSMPFQKGKHFELVFMVMPEHYKVVVNGSPFYEYGHRLPVQMVTHLQVDGDLELQSINFFGVQPAETKYPAMTGPPVFNPCLPYVGALQGGFTVRRTIIIKGYVLPTAKTFAINFRVGSSEDIALHINPRIGDCLVRNSYMNGSWGTEERMVAYNPFGPGQFFDLSIRCGMDRFKVFANGIHLFNFSHRFQALRKINTLEINGDLTLSYVHI