wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein phosphatase PP2A-like PPG1 (EC 3.1.3.16) (Q5A6B6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Serine/threonine-protein phosphatase that plays an important role in controlling colony morphology, filament extension and agar invasion. Down-regulates expression of NRG1 and affects the expression of multiple filament-specific transcripts in response to serum and 37 degrees Celsius. Plays a crucial role in virulence in a mouse model of systemic candidiasis.
Interaction partners:
- Uncharacterized protein
- Protein phosphatase 2A structural subunit
- Type 2A phosphatase-associated protein 42
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Serine/threonine-protein phosphatase 2A activator 1
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein kinase
- Serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
Sequence:
MTVPFKIPISDLDYCLEQLLDHKPPKILPPETIQQLCHTLKTELLQTPNIISLQSPISVVGDIHGQYHDLLEIFQIGGSPPQTNYLFLGDYVDRGYYSVETISLLLVLKLRYPERVFLIRGNHESRTITTNYGFYTEVLNKYQGSADVWTFITDLFDYLPLGATIDGKIFACHGGLSPSCQQLDQIRAVDRFREIPHDGIMADLVWSDPDVAISDFKLSPRGAGYLFGNDVIDKFCQDNNLVQMIRAHQLCNEGYTSYWKGKCLTVWSAPNYCYRCGNKASVLEILHSNYDSKDPTNGSDGEISSINGEFIGVNTSFESFGDDDDDYNDYRNRFNNSSRLHKQQGVLPGQFFNVFEASKENDEDTLQGKSVNGINFDDELSTSDDTSGSGGNNNKGDFFAAFFQERPKRQQVEYFL
Protein: Syntaxin-121 (AtSYP121) (Protein SYNTAXIN OF PLANTS 121) (Syntaxin-related protein At-Syr1) (Q9ZSD4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vesicle trafficking protein that functions in the secretory pathway (By similarity). Together with SYP61, regulates the post-Golgi trafficking of the aquaporin PIP2-7 to the plasma membrane, thus modulating cell membrane water permeability.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130, ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:25082856}; Single-pass type IV membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:21826108, ECO:0000269|PubMed:25082856}; Single-pass type IV membrane protein {ECO:0000255}.
Interaction partners:
- SNAP25 homologous protein SNAP33
- Syntaxin-61
- Vesicle-associated membrane protein 727
- Potassium channel KAT3
- Vesicle-associated membrane protein 721
- Tlg2p-like protein a
- Vesicle-associated membrane protein 722
- VAMP-like protein YKT62
- Vesicle transport v-SNARE 12
- Putative syntaxin-24
Sequence:
MNDLFSSSFSRFRSGEPSPRRDVAGGGDGVQMANPAGSTGGVNLDKFFEDVESVKEELKELDRLNETLSSCHEQSKTLHNAKAVKDLRSKMDGDVGVALKKAKMIKVKLEALDRANAANRSLPGCGPGSSSDRTRTSVLNGLRKKLMDSMDSFNRLRELISSEYRETVQRRYFTVTGENPDERTLDRLISTGESERFLQKAIQEQGRGRVLDTINEIQERHDAVKDIEKNLRELHQVFLDMAVLVEHQGAQLDDIESHVGRASSFIRGGTDQLQTARVYQKNTRKWTCIAIIILIIIITVVVLAVLKPWNNSSGGGGGGGGGGTTGGSQPNSGTPPNPPQARRLLR
Protein: Syndecan-1 (SYND1) (CD antigen CD138) (P18828)
Organism: Mus musculus (Mouse)
Function: Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:10684261}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P18827}. Note=Shedding of the ectodomain produces a soluble form. {ECO:0000269|PubMed:10684261}.
Interaction partners:
- Fibronectin
- Fibroblast growth factor 2
- Glypican-1
- Thrombospondin-1
- Matrix metalloproteinase-9
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Syndecan-4
- Heparanase
- Inactive heparanase-2
- Integrin beta-3
Sequence:
MRRAALWLWLCALALRLQPALPQIVAVNVPPEDQDGSGDDSDNFSGSGTGALPDTLSRQTPSTWKDVWLLTATPTAPEPTSSNTETAFTSVLPAGEKPEEGEPVLHVEAEPGFTARDKEKEVTTRPRETVQLPITQRASTVRVTTAQAAVTSHPHGGMQPGLHETSAPTAPGQPDHQPPRVEGGGTSVIKEVVEDGTANQLPAGEGSGEQDFTFETSGENTAVAAVEPGLRNQPPVDEGATGASQSLLDRKEVLGGVIAGGLVGLIFAVCLVAFMLYRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA
Protein: NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.9) (Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]) (Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase) (Triosephosphate dehydrogenase) (Q59931)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Interaction partners:
- Phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Enolase
- L-lactate dehydrogenase
- Deoxyribose-phosphate aldolase
- Transketolase
Sequence:
MTKQYKNYVNGEWKLSENEIKIYEPASGAELGSVPAMSTEEVDYVYASAKKAQPAWRSLSYIERAAYLHKVADILMRDKEKIGAVLSKEVAKGYKSAVSEVVRTAEIINYAAEEGLRMEGEVLEGGSFEAASKKKIAVVRREPVGLVLAISPFNYPVNLAGSKIAPALIAGNVIAFKPPTQGSISGLLLAEAFAEAGLPAGVFNTITGRGSEIGDYIVEHQAVNFINFTGSTGIGERIGKMAGMRPIMLELGGKDSAIVLEDADLELTAKNIIAGAFGYSGQRCTAVKRVLVMESVADELVEKIREKVLALTIGNPEDDADITPLIDTKSADYVEGLINDANDKGAAALTEIKREGNLICPILFDKVTTDMRLAWEEPFGPVLPIIRVTSVEEAIEISNKSEYGLQASIFTNDFPRAFGIAEQLEVGTVHINNKTQRGTDNFPFLGAKKSGAGIQGVKYSIEAMTTVKSVVFDIK
Protein: Choline transporter-like protein 3 (Solute carrier family 44 member 3) (Q8N4M1)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MHCLGAEYLVSAEGAPRQREWRPQIYRKCTDTAWLFLFFLFWTGLVFIMGYSVVAGAAGRLLFGYDSFGNMCGKKNSPVEGAPLSGQDMTLKKHVFFMNSCNLEVKGTQLNRMALCVSNCPEEQLDSLEEVQFFANTSGSFLCVYSLNSFNYTHSPKADSLCPRLPVPPSKSFPLFNRCVPQTPECYSLFASVLINDVDTLHRILSGIMSGRDTILGLCILALALSLAMMFTFRFITTLLVHIFISLVILGLLFVCGVLWWLYYDYTNDLSIELDTERENMKCVLGFAIVSTGITAVLLVLIFVLRKRIKLTVELFQITNKAISSAPFLLFQPLWTFAILIFFWVLWVAVLLSLGTAGAAQVMEGGQVEYKPLSGIRYMWSYHLIGLIWTSEFILACQQMTIAGAVVTCYFNRSKNDPPDHPILSSLSILFFYHQGTVVKGSFLISVVRIPRIIVMYMQNALKEQQHGALSRYLFRCCYCCFWCLDKYLLHLNQNAYTTTAINGTDFCTSAKDAFKILSKNSSHFTSINCFGDFIIFLGKVLVVCFTVFGGLMAFNYNRAFQVWAVPLLLVAFFAYLVAHSFLSVFETVLDALFLCFAVDLETNDGSSEKPYFMDQEFLSFVKRSNKLNNARAQQDKHSLRNEEGTELQAIVR
Protein: Cyclin-dependent kinase-like 5 (EC 2.7.11.22) (Serine/threonine-protein kinase 9) (O76039)
Organism: Homo sapiens (Human)
Function: Mediates phosphorylation of MECP2. May regulate ciliogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16935860}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29420175}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:29420175}.
Interaction partners:
- Methyl-CpG-binding protein 2
- Protocadherin-19
- Forkhead box protein G1
- Syntaxin-binding protein 1
- Sodium channel protein type 1 subunit alpha
- Netrin-G1
- Potassium voltage-gated channel subfamily KQT member 2
- Protocadherin-10
- Sodium channel protein type 2 subunit alpha
- Mitochondrial glutamate carrier 1
Sequence:
MKIPNIGNVMNKFEILGVVGEGAYGVVLKCRHKETHEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLELLEEMPNGVPPEKVKSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGNNANYTEYVATRWYRSPELLLGAPYGKSVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPSEQMKLFYSNPRFHGLRFPAVNHPQSLERRYLGILNSVLLDLMKNLLKLDPADRYLTEQCLNHPTFQTQRLLDRSPSRSAKRKPYHVESSTLSNRNQAGKSTALQSHHRSNSKDIQNLSVGLPRADEGLPANESFLNGNLAGASLSPLHTKTYQASSQPGSTSKDLTNNNIPHLLSPKEAKSKTEFDFNIDPKPSEGPGTKYLKSNSRSQQNRHSFMESSQSKAGTLQPNEKQSRHSYIDTIPQSSRSPSYRTKAKSHGALSDSKSVSNLSEARAQIAEPSTSRYFPSSCLDLNSPTSPTPTRHSDTRTLLSPSGRNNRNEGTLDSRRTTTRHSKTMEELKLPEHMDSSHSHSLSAPHESFSYGLGYTSPFSSQQRPHRHSMYVTRDKVRAKGLDGSLSIGQGMAARANSLQLLSPQPGEQLPPEMTVARSSVKETSREGTSSFHTRQKSEGGVYHDPHSDDGTAPKENRHLYNDPVPRRVGSFYRVPSPRPDNSFHENNVSTRVSSLPSESSSGTNHSKRQPAFDPWKSPENISHSEQLKEKEKQGFFRSMKKKKKKSQTVPNSDSPDLLTLQKSIHSASTPSSRPKEWRPEKISDLQTQSQPLKSLRKLLHLSSASNHPASSDPRFQPLTAQQTKNSFSEIRIHPLSQASGGSSNIRQEPAPKGRPALQLPGQMDPGWHVSSVTRSATEGPSYSEQLGAKSGPNGHPYNRTNRSRMPNLNDLKETAL
Protein: FI04477p (Wunen 2) (Wunen-2, isoform A (EC 3.1.3.-, EC 3.1.3.4)) (Q7KGH1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Alkaline ceramidase
- sphingosine kinase
- O-acyltransferase
- Sphingosine-1-phosphate lyase
- Neutral ceramidase
- sphingosine kinase
- LD18904p
- 3-dehydrosphinganine reductase
- Phosphatidate cytidylyltransferase, photoreceptor-specific
- FI05338p
Sequence:
MSTLRPVSVCDTTPLQRFESQSSSGEEPSSPTASSIIAAASGPNHNNNNNVKLDLQLPTFVDSTRSQGSLYAVASNKKPPLRGPRQIFGRILTDLCLLSCVGLPMLGFSLWGEAVKRGFFCDDSSLRHPYRDSTMPSWILYLMCGALPLTVMLVVEFFRGQDKRLHSPFPKSTMCSGYHLCHLELPTWLVECYHRMGIFIFGLGVEQLSTNIAKYSIGRLRPHFYTLCQPVMKDGTTCSDPINAARYIEEFTCAAVDITSKQLKDMRLSFPSGHASFACYSMLYLVIYLHRRMQWKQLRMLCHLLQFLLLMFAWYTALTRVSDYKHHWSDVLAGSGIGLTYAVVVTSTMW
Protein: N-acetyltransferase family 8 member 7 (EC 2.3.1.48) (E0CYR6)
Organism: Mus musculus (Mouse)
Function: Has histone acetyltransferase activity in vitro, with specificity for histone H4.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Aminopeptidase N
- Cytosol aminopeptidase
Sequence:
MAPYHIRKYQDSDHRSVVDLFRRGMEEHIPATFRHMLLLPRTLLLLLGVPLTLFLASGSWLLVLLSILTLFLSLWFLAKYTWEKHVMNCLHTDMADITRTYMSSHSSCFWVAESRGQTVGMVAARPVKDPLLQKKQLQLLHLSVSLQHRREGLGKAMVRTVLQFAQMQGFSEVVLSTSMLQYAALALYQGMGFQKTGETFYTYLSRLRKSPMINLKYSLTSPWEGDL
Protein: Transcription factor COE1 (O/E-1) (OE-1) (Early B-cell factor) (Olf-1) (Olfactory neuronal transcription factor) (Q63398)
Organism: Rattus norvegicus (Rat)
Function: Key pioneer transcription factor of B-cell specification and commitment. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'. Operates in a transcription factor network to activate B-cell-specific genes and repress genes associated with alternative cell fates. For instance, positively regulates many B-cell specific genes including BCR or CD40 while repressing genes that direct cells into alternative lineages, including GATA3 and TCF7 for the T-cell lineage. In addition to its role during lymphopoiesis, controls the thermogenic gene program in adipocytes during development and in response to environmental cold.
Subcellular location: Nucleus.
Interaction partners:
- Zinc finger protein 423
- Zinc finger protein 521
- Paired box 5
Sequence:
MFGIQESIQRSGSSMKEEPLGSGMNAVRTWMQGAGVLDANTAAQSGVGLARAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVGFVEKEKEANSEKTNNGIHYRLQLLYSNGIRTEQDFYVRLIDSMTKQAIVYEGQDKNPEMCRVLLTHEIMCSRCCDKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKNAGNPRDMRRFQVVVSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEAATPCIKAISPSEGWTTGGATVIIIGDNFFDGLQVIFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKSKQFCKGTPGRFIYTALNEPTIDYGFQRLQKVIPRHPGDPERLPKEVILKRAADLVEALYGMPHNNQEIILKRAADIAEALYSVPRNHNQLPALANTSVHAGMMGVNSFSGQLAVNVSEASQATNQGFTRNSSSVSPHGYVPSTTPQQTNYNSVTTSMNGYGSAAMSNLGGSPTFLNGSAANSPYAIVPSSPTMASSTSLPSNCSSSSGIFSFSPANMVSAVKQKSAFAPVVRPQTSPPPTCTSTNGNSLQAISGMIVPPM
Protein: Aldehyde dehydrogenase 22A1 (EC 1.2.1.3) (Novel aldehyde dehydrogenase family 22 member A1) (Q0WSF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Probable aldo-keto reductase 2
- Ketose-bisphosphate aldolase class-II family protein
- Delta-1-pyrroline-5-carboxylate synthase A
Sequence:
MPFWWPLIVLAFAYAICKFLLMLIPPNVPSIDVDASDVLAHGKDTEENSFIYIPPRGRSQQSDKKVQCYEPATMKYLGYFPALSPTEVEERVTLSRKAQKTWAQSSFKLRRQFLRILLKYIIEHQELICEVSSRDTGKTMVDASLGEIMTTCEKITWLLSEGERWLKPESRSSGRAMLHKVSRVEFHPLGVIGAIVPWNYPFHNIFNPMLAAVFSGNGIVIKVSEHASWSGCFYFRIIQAALAAVGAPENLVDVITGFAETGEALVSSVDKMIFVGSTAVGKMIMRNAAETLTPVTLELGGKDAFIICEDADVSHVAQVAVRGTLQSSGQNCAGAERFYVHKDIYTAFIGQVTKIVKSVSAGPPLTGRYDMGAICLQEHSEHLQSLVNDALDKGAEIAVRGSFGHLGEDAVDQYFPPTVLINVNHNMKIMKEEAFGPIMPIMQFSTDEEVIKLANDSRYALGCAVFSGSKHRAKQIASQIQCGVAAINDFASNYMCQSLPFGGVKDSGFGRFAGIEGLRACCLVKSVVEDRFWPLIKTKIPKPIQYPVAENAFEFQEALVETLYGLNIWDRLRSLIDVLKFLTDQSSNVSRTRKSH
Protein: Interleukin-36 gamma (IL-1-related protein 2) (IL-1RP2) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 9) (IL-1F9) (Interleukin-1 homolog 1) (IL-1H1) (Q9NZH8)
Organism: Homo sapiens (Human)
Function: Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T-cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1; also stimulates its own expression and that of the prototypic cutaneous pro-inflammatory parameters TNF-alpha, S100A7/psoriasin and inducible NOS. May play a role in pro-inflammatory responses during particular neutrophilic airway inflammation: activates mitogen-activated protein kinases and NF-kappa B in primary lung fibroblasts, and stimulates the expression of IL-8 and CXCL3 and Th17 chemokine CCL20 in lung fibroblasts. May be involved in the innate immune response to fungal pathogens, such as Aspergillus fumigatus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32272059}. Secreted {ECO:0000269|PubMed:20870894}. Note=The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000269|PubMed:32272059}.
Interaction partners:
- Interleukin-1 receptor-like 2
- Interleukin-36 receptor antagonist protein
- Interleukin-1 beta
- Interleukin-1 alpha
- Interleukin-1 receptor accessory protein
Sequence:
MRGTPGDADGGGRAVYQSMCKPITGTINDLNQQVWTLQGQNLVAVPRSDSVTPVTVAVITCKYPEALEQGRGDPIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDLYGQPEPVKPFLFYRAKTGRTSTLESVAFPDWFIASSKRDQPIILTSELGKSYNTAFELNIND
Protein: Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Long-chain-fatty-acid--CoA ligase, liver isozyme) (Phytanate--CoA ligase) (EC 6.2.1.24) (P18163)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate (By similarity). Preferentially activates arachidonate than epoxyeicosatrienoic acids (EETs) or hydroxyeicosatrienoic acids (HETEs).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33121}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
- Fatty acid synthase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Lipoprotein lipase
- Peroxisomal acyl-coenzyme A oxidase 1
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Lysosomal thioesterase PPT2
- Palmitoyl-protein thioesterase 1
- Palmitoyl thioesterase CPT1C
- Patatin-like phospholipase domain-containing protein 2
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MEVHELFRYFRMPELIDIRQYVRTLPTNTLMGFGAFAALTTFWYATRPKALKPPCDLSMQSVEVTGTTEGVRRSAVLEDDKLLLYYYDDVRTMYDGFQRGIQVSNDGPCLGSRKPNQPYEWISYKQVAEMAECIGSALIQKGFKPCSEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPCLKIIVIMDSYDNDLVERGQKCGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLLDFASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQGSFEELCRNKDINKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYSTIKI
Protein: Metallothionein-1L (MT-1L) (Metallothionein-IL) (MT-IL) (Q93083)
Organism: Homo sapiens (Human)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Interaction partners:
Sequence:
MDPNCSCATGGSCSCASSCKCKECKCTSCKKSCCSCCPMGCAKCAQGCVCKGASEKCSCCA
Protein: RNA binding protein fox-1 homolog 1 (Ataxin-2-binding protein 1) (Fox-1 homolog A) (Q9JJ43)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis.
Subcellular location: Nucleus. Cytoplasm. Note=Predominantly nuclear.
Interaction partners:
- Ataxin-2
- RNA-binding protein 24
- Methyl-CpG-binding protein 2
- RNA-binding protein Nova-1
- Muscleblind-like protein 1
- KH domain-containing RNA-binding protein QKI
- RNA-binding protein Nova-2
- ELAV-like protein 4
- Polypyrimidine tract-binding protein 2
Sequence:
MNCEREQLRGNQEAAAAPDTMAQPYASAQFAPPQNGIPAEYTAPHPHPAPEYTGQTTVPDHTLNLYPPTQTHSEQSADTSAQTVSGTATQTDDAAPTDGQPQTQPSENTESKSQPKRLHVSNIPFRFRDPDLRQMFGQFGKILDVEIIFNERGSKGFGFVTFENSADADRAREKLHGTVVEGRKIEVNNATARVMTNKKTVNPYTNGWKLNPVVGAVYSPDFYAGTVLLCQANQEGSSMYSGPSSLVYTSAMPGFPYPAATAAAAYRGAHLRGRGRTVYNTFRAAAPPPPIPAYGGVVYQDGFYGADIYGGYAAYRYAQPTPATAAAYSDSYGRVYAADPYHHTLAPAPTYGVGAMNAFAPLTDAKTRSHADDVGLVLSSLQASIYRGGYNRFAPY
Protein: HTH-type transcriptional regulator BetI (P17446)
Organism: Escherichia coli (strain K12)
Function: Repressor involved in the biosynthesis of the osmoprotectant glycine betaine. It represses transcription of the choline transporter BetT and the genes of BetAB involved in the synthesis of glycine betaine.
Interaction partners:
- Betaine aldehyde dehydrogenase
- Oxygen-dependent choline dehydrogenase
- High-affinity choline transport protein
Sequence:
MPKLGMQSIRRRQLIDATLEAINEVGMHDATIAQIARRAGVSTGIISHYFRDKNGLLEATMRDITSQLRDAVLNRLHALPQGSAEQRLQAIVGGNFDETQVSSAAMKAWLAFWASSMHQPMLYRLQQVSSRRLLSNLVSEFRRELPREQAQEAGYGLAALIDGLWLRAALSGKPLDKTRANSLTRHFITQHLPTD
Protein: Uncharacterized protein (Q2U5N0)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Vacuolar-sorting protein SNF7
- Uncharacterized protein
- Snf7 family protein
- Snf7 family protein
- Charged multivesicular body protein 5
- SNF7 family protein
- vesicle-fusing ATPase
- Regulator of Vps4 activity in the MVB pathway-domain-containing protein
- Vacuolar protein sorting-associated protein 28
- Vacuolar-sorting protein SNF8
Sequence:
METLKAVFFGPDPQAQMRKCNALIRANTRQLDRDIAQLRTLENKTRQYIMNASRRAERNPSQAKQATQEAKTFARELVRIRKQSTRLHTSRAQLQSVQMQVNEAFSVRKIQGSLKKSTGIMKDVNTLVRLPELNATMRQLSTELVRAGIIEEMVDDAMPDNELYEDELDEAEEEVSKVLQEILQGKLAQVDTVKAEEPLEETPAVEEQFEDQEATLEQMRGRLEALKS
Protein: 26S proteasome regulatory subunit 6A homolog B (26S proteasome AAA-ATPase subunit RPT5b) (Proteasome 26S subunit 6A homolog B) (Regulatory particle triple-A ATPase subunit 5b) (Tat-binding protein 1 homolog B) (TBP-1 homolog B) (O04019)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- 26S proteasome non-ATPase regulatory subunit 7 homolog B
- 26S proteasome non-ATPase regulatory subunit 1 homolog A
- 26S proteasome non-ATPase regulatory subunit 1 homolog B
- 26S proteasome non-ATPase regulatory subunit 3 homolog B
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit 4 homolog A
Sequence:
MATAMAEDTSFEGDQLASMTTDDIGRASRLLANEIRILKEESQRTNLDLESVKEKIKENQEKIKLNKQLPYLVGNIVEILEMSPEDDAEEDGANIDLDSQRKGKCVVLKTSTRQTIFLPVVGLVDPDTLKPGDLVGVNKDSYLILDTLPSEYDSRVKAMEVDEKPTEDYNDIGGLEKQIQELVEAIVLPMTHKEQFEKLGIRPPKGVLLYGPPGTGKTLMARACAAQTNATFLKLAGPQLVQMFIGDGAKLVRDAFLLAKEKSPCIIFIDEIDAIGTKRFDSEVSGDREVQRTMLELLNQLDGFSSDDRIKVIAATNRADILDPALMRSGRLDRKIEFPHPTEEARGRILQIHSRKMNVNADVNFEELARSTDDFNGAQLKAVCVEAGMLALRRDATEVNHEDFNEGIIQVQAKKKASLNYYA
Protein: Neural cell adhesion molecule L1 (N-CAM-L1) (NCAM-L1) (Nerve-growth factor-inducible large external glycoprotein) (NILE) (CD antigen CD171) (Q05695)
Organism: Rattus norvegicus (Rat)
Function: Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain, plays a role in the dynamics of neuronal structure and function, including synaptic plasticity.
Subcellular location: Cell membrane {ECO:0000305|PubMed:1894011}; Single-pass type I membrane protein {ECO:0000305|PubMed:1894011}. Cell projection, growth cone {ECO:0000269|PubMed:18519736}. Note=Colocalized with SHTN1 in close apposition with actin filaments in filopodia and lamellipodia of axonal growth cones of hippocampal neurons (PubMed:18519736). {ECO:0000269|PubMed:18519736}.
Interaction partners:
- Neuropilin-1
- Shootin-1
- Ankyrin 1
- Neural cell adhesion molecule 1
- Receptor protein-tyrosine kinase
- Ankyrin 2
- RAN binding protein 9
- Ezrin
- Contactin-2
- Ankyrin-3
Sequence:
MVMMLWYVLPLLLCSPCLLIQIPDEYKGHHVLEPPVITEQSPRRLVVFPTDDISLKCEARGRPQVEFRWTKDGIHFKPKEELGVVVHEAPYSGSFTIEGNNSFAQRFQGIYRCYASNNLGTAMSHEIQLVAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAAPLRIYWMNSKILHIKQDERVSMGQNGDLYFANVLTSDNHSDYICNAHFPGTRTIIQKEPIDLRVKPTNSMIDRKPRLLFPTNSSSHLVALQGQSLILECIAEGFPTPTIKWLHPSDPMPTDRVIYQNHNKTLQLLNVGEEDDGEYTCLAENSLGSARHAYYVTVEAAPYWLQKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGMSIEKVNKDQKYRIEQGSLILSNVQPSDTMVTQCEARNQHGLLLANAYIYVVQLPARILTKDNQTYMAVEGSTAYLLCKAFGAPVPSVQWLDEEGTTVLQDERFFPYANGHLGIRDLQANDTGRYFCQAANDQNNVTILANLQVKEATQITQGPRSTIEKKGARVTFTCQASFDPSLQASITWRGDGRDLQERGDSDKYFIEDGQLVIKSLDYSDQGDYSCVASTELDEVESRAQLLVVGSPGPVPHLELSDRHLLKQSQVHLSWSPAEDHNSPIEKYDIEFEDKEMAPEKWFSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVRGEGNETNNMVITWKPLRWMDWNAPQIQYRVQWRPLGKQETWKEQTVSDPFLVVSNTSTFVPYEIKVQAVNNQGKGPEPQVTIGYSGEDYPQVSPELEDITIFNSSTVLVRWRPVDLAQVKGHLRGYNVTYWWKGSQRKHSKRHVHKSHMVVPANTTSAILSGLRPYSSYHVEVQAFNGRGLGPASEWTFSTPEGVPGHPEALHLECQSDTSLLLHWQPPLSHNGVLTGYLLSYHPLDGESKEQLFFNLSDPELRTHNLTNLNPDLQYRFQLQATTHQGPGEAIVREGGTMALFGKPDFGNISVTAGENYSVVSWVPREGQCNFRFHILFKALPEGKVSPDHQPQPQYVSYNQSSYTQWDLQPDTKYEIHLMREKVLLHHLAVKTNGTGPVRVSTTGSFASEGWFIAFVSAIILLLLILLILCFIKRSKGGKYSVKDKEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE