wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein ZIC 1 (XZic1) (XlZic1) (ODD-paired-like) (Xopl) (ZIC-related protein 1) (ZIC-r1) (Zinc finger protein of the cerebellum 1) (O73689)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional activator that induces expression of multiple genes including pax3, en2, snai2/slug, feb and a subset of wnt genes. Has multiple key roles in the regulation of neural induction and neurogenesis: acts as a neural competence factor, sensitizing the presumptive neuroectoderm to respond to subsequent neuralizing signals. Promotes both preplacodal cell fates and neural crest cell fates, two of the cell populations that arise from the neural plate border. Cooperates with pax3 in concert with wnt signaling to determine neural crest fate. Synergizes with the bmp-inhibitor noggin/nog and acts through the wnt pathway to induce expression of en2. May bind to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:9655809}. Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MLLDAGAQYPAIGVTTFGSSRHHSAGDVTDREVALGINPFADGMGAFKLNPSSHDLASGQTAFTSQAPGYAAAALGHHHHPGHVSSYSSAAFNSTRDFLFRNRGFGEAASAQHSLFASAAGGFPGPHGPHADTTGHLIFPGLHEQAASHASPNVVNGQMRLGFSGDMYGRPDQYGQVTSPRSEHYASSQLHGYGPMNMNMAAHHGAGAFFRYMRQPIKQELICKWIEPEQLANPKKSCNKTFSTMHELVTHVTVEHVGGPEQSNHICVWEECPREGKPFKAKYKLINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHEASSQGSQPSPAASSGYESSTPPTIVSPSAENQSTSSLSPSSSAVHHTSNHSTLSSNFNEWYV
Protein: Pyrimidine-specific ribonucleoside hydrolase RihA (EC 3.2.-.-) (Cytidine/uridine-specific hydrolase) (P41409)
Organism: Escherichia coli (strain K12)
Function: Hydrolyzes with equal efficiency cytidine or uridine to ribose and cytosine or uracil, respectively.
Interaction partners:
- Ribokinase
- Glutamate/aspartate import permease protein GltK
- Glutamate/aspartate import ATP-binding protein GltL
- Chaperone protein HscC
- Cytidine deaminase
Sequence:
MALPILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADNVHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGLGNWTPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDEKWGFVGAPLHDPCTIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRLKFYA
Protein: At1g59940 (Q29PQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAKDGGVSCLRRSEMIGIGIGELESPPLDSDQVHVLAVDDSLVDRIVIERLLRITSCKVTAVDSGWRALEFLGLDDDKAAVEFDRLKVDLIITDYCMPGMTGYELLKKIKESTSFKEVPVVIMSSENVMTRIDRCLEEGAEDFLLKPVKLADVKRLRSYLTRDVKVAAEGNKRKLTTPPPPPPLSATSSMESSDSTVESPLSMVDDEDSLTMSPESATSLVDSPMRSPGLA
Protein: Dual specificity phosphatase 3 (K7ELG5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XAYFERAADFIDQALAQKNDGVSLLLPRLKSNGAILAHRNLHLPGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSIVRQNREIGPNDGFLAQLCQLNDRLAKEGKLKP
Protein: DNA replication licensing factor MCM4 (EC 3.6.4.12) (CDC21 homolog) (P1-CDC21) (P49717)
Organism: Mus musculus (Mouse)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. 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.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P30664}. Chromosome {ECO:0000250|UniProtKB:P30664}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000250|UniProtKB:P30664}.
Interaction partners:
- DNA replication licensing factor MCM3
- Cell division cycle 7-related protein kinase
- Cell division control protein 6 homolog
- Cell division control protein 45 homolog
- DNA replication complex GINS protein PSF2
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM2
- WD repeat and HMG-box DNA-binding protein 1
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM6
Sequence:
MSSPASTPSRRSSRRGRVTPTQSLRSEESRSSPNRRRRGEDSSTGELLPMPTSPGADLQSPPAQNALFSSPPQMHSLAIPLDFDVSSPLTYGTPSSRVEGTPRSGVRGTPVRQRPDLGSARKGLQVDLQSDGAAAEDIVPSEQSLGQKLVIWGTDVNVATCKENFQRFLQCFTDPLAKEEENVGIDITQPLYMQQLGEINITGEPFLNVNCEHIKSFSKNLYRQLISYPQEVIPTFDMAVNEIFFDRYPDSILEHQIQVRPFNALKTKSMRNLNPEDIDQLITISGMVIRTSQLIPEMQEAFFQCQVCAHTTRVEIDRGRIAEPCSCVHCHTTHSMALIHNRSFFSDKQMIKLQESPEDMPAGQTPHTIVLFAHNDLVDKVQPGDRVNVTGIYRAVPIRVNPRVSNVKSVYKTHIDVIHYRKTDAKRLHGLDEEAEQKLFSEKRVKLLKELSRKPDIYERLASALAPSIYEHEDIKKGILLQLFGGTRKDFSHTGRGKFRAEINILLCGDPGTSKSQLLQYVYNLVPRGQYTSGKGSSAVGLTAYVMKDPETRQLVLQTGALVLSDNGICCIDEFDKMNESTRSVLHEVMEQQTLSIAKAGIICQLNARTSVLAAANPIESQWNPKKTTIENIQLPHTLLSRFDLIFLMLDPQDEAYDRRLAHHLVSLYYQSEEQVEEEFLDMAVLKDYIAYAHSTIMPRLSEEASQALIEAYVNMRKIGSSRGMVSAYPRQLESLIRLAEAHAKVRFSNKVEAIDVEEAKRLHREALKQSATDPRTGIVDISILTTGMSATSRKRKEELAEALRKLILSKGKTPALKYQQLFEDIRGQSDTAITKDMFEEALRALADDDFLTVTGKTVRLL
Protein: Protein kinase C and casein kinase II substrate protein 3 (Q99JB8)
Organism: Mus musculus (Mouse)
Function: Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11082044}. Cell membrane {ECO:0000269|PubMed:11082044}; Peripheral membrane protein {ECO:0000269|PubMed:11082044}; Cytoplasmic side {ECO:0000269|PubMed:11082044}. Note=Detected at the inner aspect of the plasma membrane in myotubes.
Interaction partners:
- Protein kinase C and casein kinase substrate in neurons protein 1
- Protein kinase C and casein kinase substrate in neurons protein 2
- Transient receptor potential cation channel subfamily V member 4
- Disintegrin and metalloproteinase domain-containing protein 9
- F-BAR domain only protein 1
Sequence:
MAPEEDAGGEVLGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGAVEKGPQYGTLEKAWHAFFTAAERLSELHLEVREKLHGPDSERVRTWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHTARKDEKTAQTRESHAKADSSMSQEQLRKLQERVGRCTKEAEKMKTQYEQTLAELNRYTPRYMEDMEQAFESCQAAERQRLLFFKDVLLTLHQHLDLSSSDKFHELHRDLQQSIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRAISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPSSPGSGQDEDWSDEESPRKVATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQLQSGRIGLYPANYVECVGA
Protein: Spectrin alpha chain, non-erythrocytic 1 (Alpha-II spectrin) (Fodrin alpha chain) (P07751)
Organism: Gallus gallus (Chicken)
Function: Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Interaction partners:
- Spectrin beta chain
- Uncharacterized protein.
- Caspase-3
- Calponin-homology
- SANT domain-containing protein.
Sequence:
MDPSGVKVLETAEDIQERRQQVLDRYHRFKELSSLRRQKLEDSYRFQFFQRDADELGKWIQEKLQIASDENYKDPSNLQGKLQKHQAFEAEVQANSGAIVKLDETGNQMINEGHFASETIRTRLQELHRLWELLLEKMREKGVKLLQAQKLVQFLRECEDVMDWINDKEAIVTSEELGQDLEHVEVLQKKFEEFQTDLAAHEERVNEVNQFAGKLIQEQHPEEELIKSKQDEVNASWQRLKGLAQQRQGKLFGAAEVQRFNRDVDETISWIKEKGQLMASDDFGRDLASVQALLRKHEGLERDLAAFHHKVKALCAEADRLQQSHPINASQIQVKREELIANWEQIRTLAAERHARLNDSYRLQRFLADFRDLTSWVTEMKALINADELANDVAGAEALLDRHQEHKGEIDAHEDSFRSADESGQALLAAGHYASDEVKEKLTILSDERSALLELWELRRQQYEQCMDLQLFYRDTEQVDNWMSKQEAFLLNEDLGDSLDSVEALLKKHEDFEKSLSAQEEKITALDEFATKLIQNNHYAMDDVATRRDALLSRRNALHERAMKRRAQLADSFHLQQFFRDSDELKSWVNEKMKTATDEAYKDPSNLQGKVQKHQAFEAELSANQSRIDALEKAGQKLIDVNHYASDEVAARMNEVISLWKKLLEATELKGIKLREANQQQQFNRNVEDIELWLYEVEGHLASDDYGKDLTSVQNLQKKHALLEADVAAHQDPIDGITIQARQFQDAGHFDADNIKKKQEALVARYEALKDPMVARKQKLADSLRLQQLFRDIEDEETWIREKEPIAASTNRGKDLIGVQNLLKKHQALQAEIAGHEPRIKAVTQKGNAMVEEGHFAAEDVKIKLNELNQKWDSLKAKASQRRQDLEDSLQAQQYFADANEAQSWMREKEPIVGSTDYGKDEDSAEALLKKHEALMSDLSAYGSSIQALREQAQSCRQQVAPTDDETGKELVLALYDYQEKSPREVTMKKGDILTLLNSTNKDWWKVEVNDRQGFVPAAYVKKLDPAQSASRENLLEEQGSIALRQEQIDNQTLITKEVGSVSLRMKQVEELYHSLLELGEKRKGMLEKSCKKFMLFREANELQQWINEKEAALTNEEVGADLEQVEVLQKKFDDFQKDLKANESRLKDINKVANDLESEGLMAEEVQAVEHQEVYGMMPRDETDSKTVSPWKSARMMVHTVATFNSIKELNERWRSLQQLAEERSQLLGSADEVQRFHRDADETKEWIEEKNQALNTDNYGHDLASVQALQRNDEGFERDLAALGDKVNSLGETAQRLIQSHPELAEDLQEKCTELNQAWSSLGKRADQRKEKLGDSHDLQRFLSDFRDLMSWINGIRGLVSSDELAKDVTGAEALLERHQEHRTEIDARAGTFQAFEQFGQQLLARGHYASPEIKEKLDILDQERTDLEKAWVQRRMMLDQCLELQLFHRDCEQAENWMAAREAFLNTEDKGDSLDSVEALIKKHEDFDKAINVQEEKIAVLQSFADQLIAADHYAKGVIANRRNEVLDRWRRLKAQMIEKRSKLGESQTLQQFSRDVDEIEAWISEKLQTASDESYKDPTNIQLSKLLSKHQKHQAFEAELHANADRIRGVIEMGNPLIERGACAGSEDAVKARLAALADQWEFLVQKSSEKSQKLKEANKQQNFNTGIKDFDFWLSEVEALLASEDYGKDLASVNNLLKKHQLLEADISAHEDRLKDLNSQADSLMTSSAFDTSQVKDKRETINGRFQRIKSMAAARRAKLNESHRLHQFFRDMDDEESWIKEKKLLVSSEDYGRDLTGVQNLRKKHKRLEAELAAHEPAIQGVLDTGKKLSDDNTIGKEEIQQRLAQFVDHWKELKQLAAARGQRLEESLEYQQFVANVEEEEAWINEKMTLVASEDYGDTLAAIQGLLKKHEAFETDFTVHKDRVNDVCANGEDLIKKNNHHVENITAKMKGLKGKVSDLEKAAAQRKAKLDENSAFLQFNWKADVVESWIGEKENSLKTDDYGRDLSSVQTLLTKQETFDAGLQAFQQEGIANITALKDQLLAAKHIQSKAIEVRHASLMKRWNQLLANSAARKKKLLEAQEHFRKVEDLFLTFAKKASAFNSWFENAEEDLTDPVRCNSLEEIKALREAHDAFRSSLSSAQADFNQLAELDRQIKSFRVASNPYTWFTMEALEETWRNLQKIIKERELELQKEQRRQEENDKLRQEFAQHANAFHQWIQETRTYLLDGSCMVEESGTLESQLEATKRKHQEIRAMRSQLKKIEDLGAAMEEALILDNKYTEHSTVGLAQQWDQLDQLGMRMQHNLEQQIQARNTTGVTEEALKEFSMMFKHFDKDKSGRLNHQEFKSCLRSLGYDLPMVEEGEPDPEFESILDTVDPNRDGHVSLQEYMAFMISRETENVKSSEEIESAFRALSSERKPYVTKEELYQNLTREQADYCISHMKPYMDGKGRELPSAYDYIEFTRSLFVN
Protein: Cytochrome b559 subunit beta (PSII reaction center subunit VI) (Q6ENF7)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00643}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00643}.
Interaction partners:
- Photosystem II reaction center protein L
- Cytochrome b559 subunit alpha
- Photosystem II CP43 reaction center protein
- Photosystem II D2 protein
- photosystem II
- Photosystem II protein D1
- Photosystem II CP47 reaction center protein
- Photosystem II protein D1
- Uncharacterized protein
- Photosystem II reaction center protein J
Sequence:
MTIDRTYPIFTVRWLAVHGLAVPTVFFLGSISAMQFIQR
Protein: Interleukin 12 receptor subunit beta 1 (A0A8I5ZPZ3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDMTGLPGTSKHIIFLLLCQLSASSRGDSCCVEKISYPDEASGPSLGPRDLSCYRVSGTDYECSWQYDGPEDNVAHFLWCCFAHPNPTHTSFGQECCCYFSSGRSRTVQFWEQDGISTLSKVNFWVESRLGNRTLKSQEISQYLYNWTKLTPPLGHIRVSRSRGELRMDWNVSDGAGAEVQLRRRMPTTNWTLGDCGPQVSSGLGVIGDIHGSSSESCLCPSENMAQEIQIRRRRRLSSGAPGGPWSNWSMSVCVPPEFLPQAEIKFLVEPLNQDGRRRLTMEGQTPQLAVPEGCRDRPGAQVKKHLVLVHMLACRCQARTWKTVPLGKTLDLSGAAYDLDVLAQTRFGRSIIQKWPLPAQELTETRTLNVIVEGNVTSMQWAAQPPGTAYCLEWQPWGQDRNHTDCTLIAPEEEDPAKMVTHTWSSKPTLDQEECYRITVFASKNPKNPMMWATVLSSYYFGGNVSRVGTPRHVSVRNHTEDSVSVEWTASQLSTCPGVLTQYVVRCEAEDGTWESELLVPPTKTQVTLNSLRSRVVYKVQVRADTAMLPGSWSRPQRFSVGLPGTCAHLCLRPVAALLWSSLAARTSRLGNGATLRTSPRCCTHETRWWWRCPGTEMMRQSRPRPPLSAPWTQGGPWELRGRCKDSQRPGSRTWLERTVPVVTWPT
Protein: Long-chain fatty acid transport protein 4 (FATP-4) (Fatty acid transport protein 4) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 4) (Very long-chain acyl-CoA synthetase 4) (ACSVL4) (EC 6.2.1.-) (Q91VE0)
Organism: Mus musculus (Mouse)
Function: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport across cell membranes. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake (By similarity). Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Probably involved in fatty acid transport across the blood barrier (By similarity). Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23407971}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Long-chain fatty acid transport protein 1
- Platelet glycoprotein 4
- Scavenger receptor class B member 1
- Peroxisome proliferator-activated receptor alpha
- Magnesium transporter NIPA4
Sequence:
MLLGASLVGALLFSKLVLKLPWTQVGFSLLLLYLGSGGWRFIRVFIKTVRRDIFGGMVLLKVKTKVRRYLQERKTVPLLFASMVQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLPSHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSRVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIIQQDPLRRFDGYLNQGANNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSVVKDPLFYLDARKGCYVALDQEAYTRIQAGEEKL
Protein: Peptidyl-prolyl cis-trans isomerase CYP19-3 (PPIase CYP19-3) (EC 5.2.1.8) (Cyclophilin of 19 kDa 3) (Cyclophilin-4) (Rotamase cyclophilin-2) (Q38867)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- UPF0235 protein At5g63440
- Probable cysteine protease RD21B
- At1g09850
- Cysteine proteinase RD21A
- Probable cysteine protease RD21C
- Cathepsin B-like protease 1
- Putative sterol 14-demethylase-like protein
- Tetratricopeptide repeat
- Pre-mRNA-splicing factor SYF2
- Cathepsin B-like protease 2
Sequence:
MANPKVFFDILIGKMKAGRVVMELFADVTPRTANNFRALCTGENGIGKAGKALHYKGSAFHRIIPGFMCQGGDFTRGNGTGGESIYGSKFEDENFKLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPSERVVIEDCGELKNPSS
Protein: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase cnrN (EC 3.1.3.67) (Q54JL7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Protein phosphatase that negatively regulates PI3K-dependent pathways. Regulates cAMP signal transduction to control territory size. During development, a lawn of Dictyostelium cells breaks up into territories where cells aggregate in dendritic streams to form groups of 20'000 cells.
Interaction partners:
- Serine/threonine-protein kinase pakD
- Autocrine proliferation repressor protein A
Sequence:
MNQVFFSKIRSLVSADRHRFKSKEMDLDLDLSYITDNILAMGFPGTGLEASWRNSIDDVCELLKQKHHGKYMIWNLSERVYDYSKLNNQILEFPFLDHHPPPLSLLFEIVNSLSNWLKADAENVAVVHCKGGKGRTGTIICCYLYYSCQFEIMDDAKNHFAEKRSKMKKGVTQPSQQRYINYFKEIVSGSHMVEEFVLTFRSIELGPLTKDQANSLSFEIFEHAKEPILNFASSSNSIQIVPINNDNSESNNNNNNNNNNNNNNNNQQQQLYKIIILIQKKVQNDVLIRVYRGDTGKGKGKMKKQIFHLIFNIAFVNLDQCLFGMNEFDHFKSSKKYDPNLQMECRFQNNCTGAPDHSFKIWNIMALQYQRTKSSLNNSITDIKSINEINSTNNNNILASSAPTPLTTTTTTTTTTTTTSLPSSEHSTPQILISSSDANLDLKNCNINCDSSSGGGSNSSRNSNSNSRGGSSNSSSNRSSTSSRSSITTDSIKPSCSSDSICNNSSICNNSCNNNNNNNNNNNNNNNNNNNNNNNNNNNKNSNNNNNESSSNSNDDSDSEASIRKRKNTLWSSGSSIKLKPSPNLSRLSLFNGHRQSFTKKINPNNNEENVDQKTLPILKKETNDPSESDIKNVEIIQD
Protein: Uncharacterized protein (Q385Q7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MALNVVSMVIKINRVLLIGCVAYLLSRVVDGLIRGDDLLGRENHQRFSVLPNGNAIHLNFVIRKNRNCTDHHSSHSDEGIKDSISGISTAADAIPKKRSSTAPHHVKQPSSTGVMAVFTFGRPHLPNGAITDTFKKRLVHAVRMALLTGAPWIIVPCSRGERTNSEAFLRNMGSPGDLLFNDAVVEDLPPELQELAKQLRDSMRFAASLDEWIQSGNPIEHFARVANVEGTGVSIASPRLLRHGQSQWIIPEFVWVDRNESWVVNTKEDIKHGLLVLLRRVLQIDFYGENSESQSKQDADAAWLERGIFDIIVVGSMHNEGFLYSATSRELSFLSRAHRQSTVLQRQGRENLLVSWLSKNINVRITSAEDSVPEITVPEPWIVDAQPEPRALRKAWWLFRMLAPLSHTIHLNYCRWSACIRCSLTSVRIINFVFEFFAAIEAILTEKVNMLGYF
Protein: Histidine-containing phosphotransfer protein (Q67XQ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU369004}. Nucleus {ECO:0000256|RuleBase:RU369004}.
Interaction partners:
Sequence:
MNTIVVAQLQRQFQDYIVSLYQQGFLDNQFSELRKLQDEGTPDFVAEVVSLFFDDCSKLINTMSISLERPDNVDFKQVDSGVHQLKGSSSSVGARRVKNVCISFKECCDVQNREGCLRCLQQVDYEYKMLKTKLQDLFNLEKQILQAGGTIPQVDIN
Protein: Transcription initiation factor TFIID subunit 7 (Q6R1L1)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF7 forms a promoter DNA binding subcomplex of TFIID, together with TAF1 and TAF2. Part of a TFIID complex containing TAF10 (TFIID alpha) and a TFIID complex lacking TAF10 (TFIID beta).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9R1C0}.
Interaction partners:
Sequence:
MSKSKDDAPHELESQFILRLPPEYASTVRRAVQSGHVNLKDRLTIELHPDGRHGIVRVDRVPLAAKLVDLPCVMESLKTIDKKTFYKTADICQMLVSTVDGDLYPPVEEPVAPADPKASKKKDKDKEKKFVWNHGITLPLKNVRKRRFRKTAKKKYIESPDVEKEVKRLLSTDAEAVSTRWEIIAEDETKETENQGLDISSPGMSGHRQGHDSLEHDELREIFNDLSSSSEDEEDVNVIDTEEDLERQLQDKLNESDEQHQENEGTNQLVMGIQKQIDNMKGKLQETQDRAKRQEDLIMKVENLALKNRFQAVLDELKQKEDREKEQLSSLQEGLESLLEK
Protein: Threonylcarbamoyl-AMP synthase (EC 2.7.7.87) (Ischemia/reperfusion-inducible protein) (mIRIP) (Q3U5F4)
Organism: Mus musculus (Mouse)
Function: Cytoplasmic and mitochondrial threonylcarbamoyl-AMP synthase required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Participates in t(6)A37 formation in cytoplasmic and mitochondrial tRNAs (By similarity). May regulate the activity of some transporters.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86U90}. Mitochondrion {ECO:0000250|UniProtKB:Q86U90}. Cell membrane {ECO:0000269|PubMed:16024787}; Peripheral membrane protein {ECO:0000269|PubMed:16024787}. Note=A large fraction localizes in the cytoplasm, whereas a smaller fraction is imported to mitochondria. {ECO:0000250|UniProtKB:Q86U90}.
Interaction partners:
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- EKC/KEOPS complex subunit Tprkb
- tRNA dimethylallyltransferase
- Queuine tRNA-ribosyltransferase accessory subunit 2
Sequence:
MSTARPCAGLRAAVAAGMGLSDGPASSGRGCRLLRPPEPAPALPGARLLRLPESEPVEAASPERSGWTEALRAAVAELRAGAVVAVPTDTLYGLACSASSSAALSCVYRLKGRSEAKPLAVCLGRVADVYRYCQVRVPRELLEDLFPGPVTLVMERSEELNKDLNPFTRLVGIRIPDHAFMLDLAQMFGGPLALTSANLSSQASSLSVEEFQDLWPHLSLVIDGGPIGDSQSPECRLGSTVVDLSVPGKFGIIRPGCALENTTSILQQKYGLLPSQGSCS
Protein: Glycolipid transfer protein (F5H0U5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MALLAEHLLKPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNITKIKAVYDTNPAKFRTLQNILEVEKEIGLRFIQVFLQSICDGERDENHPNLIRVNATKAYEMALKKYHGWIVQKIFQAALYAAPYKSDFLKALSKGQNVTEEECLEKIRLFLVNYTATIDVIYEMYTQMNAELNYKV
Protein: Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2) (Q8IU57)
Organism: Homo sapiens (Human)
Function: The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. Determines the cell type specificity of the lambda interferon action. Shows a more restricted pattern of expression in the epithelial tissues thereby limiting responses to lambda interferons primarily to epithelial cells of the respiratory, gastrointestinal, and reproductive tracts. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Tyrosine-protein kinase JAK1
- Interleukin-10 receptor subunit beta
- Interferon lambda-1
- Interferon lambda-2
- Interferon lambda-3
- Interferon alpha/beta receptor 1
- Non-receptor tyrosine-protein kinase TYK2
- Interferon alpha-1/13
- Interleukin-10 receptor subunit alpha
- Interleukin-10
Sequence:
MAGPERWGPLLLCLLQAAPGRPRLAPPQNVTLLSQNFSVYLTWLPGLGNPQDVTYFVAYQSSPTRRRWREVEECAGTKELLCSMMCLKKQDLYNKFKGRVRTVSPSSKSPWVESEYLDYLFEVEPAPPVLVLTQTEEILSANATYQLPPCMPPLDLKYEVAFWKEGAGNKTLFPVTPHGQPVQITLQPAASEHHCLSARTIYTFSVPKYSKFSKPTCFLLEVPEANWAFLVLPSLLILLLVIAAGGVIWKTLMGNPWFQRAKMPRALDFSGHTHPVATFQPSRPESVNDLFLCPQKELTRGVRPTPRVRAPATQQTRWKKDLAEDEEEEDEEDTEDGVSFQPYIEPPSFLGQEHQAPGHSEAGGVDSGRPRAPLVPSEGSSAWDSSDRSWASTVDSSWDRAGSSGYLAEKGPGQGPGGDGHQESLPPPEFSKDSGFLEELPEDNLSSWATWGTLPPEPNLVPGGPPVSLQTLTFCWESSPEEEEEARESEIEDSDAGSWGAESTQRTEDRGRTLGHYMAR
Protein: Ubiquitin-conjugating enzyme E2 D2 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D2) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D2) (Ubiquitin carrier protein D2) (Ubiquitin-conjugating enzyme E2(17)KB 2) (Ubiquitin-conjugating enzyme E2-17 kDa 2) (Ubiquitin-protein ligase D2) (P62838)
Organism: Mus musculus (Mouse)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by RIGI in response to viral infection. Essential for viral activation of IRF3.
Interaction partners:
- E3 ubiquitin-protein ligase RBX1
- CCR4-NOT transcription complex subunit 4
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-conjugating enzyme E2 variant 1
- Baculoviral IAP repeat-containing protein 2
- Baculoviral IAP repeat-containing protein 3
- E3 ubiquitin-protein ligase TRIP12
- S-phase kinase-associated protein 1
- SUMO-activating enzyme subunit 2
- E3 ubiquitin-protein ligase CHIP
Sequence:
MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAM