wanglab/gogpt-training-data huggingface dataset:
Protein: Plac8 onzin-related protein 1 (E7F147)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAAISTTVVSTQRTSSGTWTTGICDCCSDMSTCCCGFWCFPCMQCQTASQFGWCFCMPLLDCCMVVSCCLRKKMREQYSINGSCCDDFCTLCFCYPCAWCQMSREIKTRARSGTTATVVTQQIRY
Protein: p80 coilin (Q923T0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAASETVRVRLQFDYPPPATPHCTVFWLLVDLNRCRVVTDLISLIRQRFGFSSGALLGLYLEGGLLPPSESARLVRDNDCLRVKLEDQGLPEALIVSNGGDSNFPCRKSKKRAFKLVEDEETDQGYKYPDKYWKRQEDSGPNEKASDLETKLFPDEVRRTKNKRKSKVAGIPAEEDEEETKKKSSKRKEKCEQKKQTRASKSPKQQTHKEGGSQNCSFPRASYRSSLAKARRRSSTGAKGSPSYLSESESCPDSVSDGHCSVTTMQGVTLSEKLSAELLKDGATKTAAANRQSSKPSFTFSSGKGKASRASSSSSDSSSESEDQFLVSKNMLEGTSDFLKTTGLFAGQGCSSPGLSLETPGIMGWKPSDSNRGRQAPGPNVPVPSSLGRGWGRGEDFLFGKGLRGRGIRGRGRGRGQTVSCILNRSSESQKQKQLNDILTNSSTVIQNPVETSKKDYSLLPLLAAAPQVGEKIAFKLLELTSDYSPDVSDYKEGKILSHDPETQQVDIEVLSSLPALKEPGKFDLVYHNENGTEVVEYAVTQEKRITVFWKELIDPRLIIDSSSSISSK
Protein: Ankyrin 2, isoform E (RE55168p) (Q3KN55)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAQFVTHIQPTLMEASQGHVPHHHGHQVGVQHSSHLPHSGHNMPSPPTHNHHHAHGHGHHTSSGGHHGGAGGHSQKQAAHHSTTSGHAAKGQHHSPPSRIHSPPTEHHPDHVGHYEYFQHQHEQIFHHEGANGGASHKQQTHHHPNKHEHCPTGHQSAGDGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLESDTRGKVRLPALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKEGQDEVKDLIAKKITDHIDTVYLMQLFWIRHQEFFI
Protein: S-adenosylmethionine synthase isoform type-1 (AdoMet synthase 1) (EC 2.5.1.6) (Methionine adenosyltransferase 1) (MAT 1) (Methionine adenosyltransferase I/III) (MAT-I/III) (P13444)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Interaction partners:
- Methionine adenosyltransferase 2 subunit beta
- Betaine--homocysteine S-methyltransferase 1
- Methionine synthase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- S-adenosylmethionine synthase isoform type-2
- Tyrosine aminotransferase
- S-adenosylmethionine decarboxylase proenzyme
- Methylenetetrahydrofolate reductase
- DNA
- DNA
Sequence:
MNGPVDGLCDHSLSEEGAFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCKTGMVLLCGEITSMAMIDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQCVHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIVLAHKLNTRMADLRRSGVLPWLRPDSKTQVTVQYVQDNGAVIPVRVHTIVISVQHNEDITLEAMREALKEQVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSKKTERDELLEVVNKNFDLRPGVIVRDLDLKKPIYQKTACYGHFGRSEFPWEVPKKLVF
Protein: ADP-ribosylation factor 1 (EC 3.6.5.2) (P84078)
Organism: Mus musculus (Mouse)
Function: Small GTPase involved in protein trafficking between different compartments. Modulates vesicle budding and uncoating within the Golgi complex (By similarity). In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane (By similarity). The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (By similarity). The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasticity of excitatory synapses and spine shrinkage during long-term depression (LTD) (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000250|UniProtKB:P84080}; Cytoplasmic side {ECO:0000305}. Synapse, synaptosome {ECO:0000250|UniProtKB:P84079}. Postsynaptic density {ECO:0000250|UniProtKB:P84079}. Note=In the GDP-bound form, associates transiently with the membranes via its myristoylated N-terminus where guanine nucleotide-exchange factor (GEF)-mediated nucleotide exchange occurs (By similarity). Following nucleotide exchange, the GTP-bound form undergoes a conformational change, leading to the exposure of a myristoylated N-terminal amphipathic helix that provides stable membrane anchorage (By similarity). {ECO:0000250|UniProtKB:P84080}.
Interaction partners:
- Cytohesin-2
- Pleckstrin homology domain-containing family A member 3
- Cytohesin-3
- Cytohesin-4
- Cytohesin-1
- Phospholipase D1
- Coatomer subunit beta
- Phospholipase D2
- Abl interactor 1
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
Sequence:
MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
Protein: Methionine-R-sulfoxide reductase B1 (MsrB1) (EC 1.8.4.12) (EC 1.8.4.14) (Selenoprotein X) (SelX) (Q9NZV6)
Organism: Homo sapiens (Human)
Function: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to actin repolymerization in macrophages.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9JLC3}. Nucleus {ECO:0000250|UniProtKB:Q9JLC3}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9JLC3}.
Interaction partners:
- Mitochondrial peptide methionine sulfoxide reductase
- Selenoprotein K
- Protein adenylyltransferase SelO, mitochondrial
- Thioredoxin reductase-like selenoprotein T
- Glutathione peroxidase 3
- Glutathione peroxidase 2
- Selenide, water dikinase 2
- Thioredoxin reductase 2, mitochondrial
- Selenoprotein S
- Glutathione peroxidase 7
Sequence:
MSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRSEALKVSCGKCGNGLGHEFLNDGPKPGQSRFUIFSSSLKFVPKGKETSASQGH
Protein: Probable transcriptional regulator (Q9I670)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable transcriptional regulator
- Probable transcriptional regulator
- HotDog ACOT-type domain-containing protein
Sequence:
MRRKIPSTAALVSFESAARHESFTKAAEELSLTQSAICRQIATLEEFLGVELFRRSRRGVKLTEAGLSYSRRVAVRLDAVERDTLAVMGHQGGGAIELAVVPTFGTQWLLPRLKRFQRLHPEVTINLTNRTRPFLFADTEFDAALYFGDADWSGTVSHFLMRENPVPVCSPELLGGRRTLSAEQVAGLPLMQQSTRPYAWRQWFHSQGLNVAHDMSGPRYELFSMLAQAAMHGMGVALIPPFLIQDELADGRLIVPMQHAYLSENAYYLIIPERRVESAMLNAFRDWLVEEARQYREANGLG
Protein: Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (X-linked nuclear protein) (A0A096LNN3)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMENSKEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQSLPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLKKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKVDSEKSNKVYEHTSRFSPKKTSSNCNGEEKKLDDSCSGSVTYSYSALIVPKEMIKKAKKLIETTANMNSSYVKFLKQATDNSEISSATKLRQLKAFKSVLADIKKAHLALEEDLNSEFRAMDAVNKEKNTKEHKVIDAKFETKARKGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVT
Protein: Helix-loop-helix DNA-binding domain containing protein (Q8LSP3)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGQTGGRPGGGGGPALQRLRRHAAGKVASRSLARCREGARRRGRQAAGQRHSGRQGSNESTTQSQPTVTVIEDLKLEIDCQHVKKNIAHSPGQQCSPSERFDEWKSSSRRRPKCDVATNLHWCHLHPFQMSTLSNKVSLSSNLLNLQTGLAEEPEELTYMYHQEEHARMQEQFAGTPLVEQPVRFDQFYPASMAPNQFHPSHCSSFPAFGGSSALPSLAFGAVATTKKEQVQQPSPSSSNVLSFAGQVQGSTTTLDFSGRGWQQDDGVGVFQQPPERRSRPPANAQEHVIAERKRREKLQQQFVALATIVPGLKKTDKISLLGSTIDYVKQLEEKVKALEEGSRRTAEPTTAFESKCRITVDDDDGGSASSGTDDGSSSSSSPTVEASIHGNTVLLKICCKERRGLLVMILSELEKQGLSIINTSVVPFTDSCLNITITAKARLALPVYYS
Protein: Tubulin-specific chaperone A (Altered polarity protein 31) (Tubulin-folding cofactor A) (CFA) (Q9Y703)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the maintenance of microtubule structures and cell polarity. Beta-tubulin-folding protein; may have a regulatory role in the tubulin-folding pathway.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Cell polarity protein alp21
- Cell polarity protein alp11
- Tubulin beta chain
- Tubulin-folding cofactor D
- Inner kinetochore subunit mis6
- Probable prefoldin subunit 1
Sequence:
MSNTVRSLVIKTNVVKRIIKDVELAHIDINEAEKRVQSKIDNGEDSAEIEHQKFVLKKHLEALPDALVRLRNATNDLESISSDSAYEGTPELEQANEYLEKAKEVIEKEQTNFPTNGYH
Protein: 1-propanol dehydrogenase PduQ (EC 1.1.-.-) (Propanediol utilization protein PduQ) (Q9XDN0)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: An iron-dependent alcohol dehydrogenase required for optimal 1,2-propanediol (1,2-PD) degradation. NAD(+) and NADH are regenerated internally within the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by the PduP and PduQ enzymes, which reduce NAD(+) and oxidize NADH respectively, although there must also be cofactor transport across the BMC.
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:12923081}. Note=Probably located inside the BMC shell. {ECO:0000305|PubMed:23077559}.
Interaction partners:
- Propanal dehydrogenase
- Propanediol dehydratase large subunit
- Propanediol dehydratase medium subunit
- Propanediol dehydratase small subunit
- Acetaldehyde dehydrogenase
- Phosphate propanoyltransferase
- Corrinoid adenosyltransferase PduO
- Propionate kinase PduW
- Bacterial microcompartment shell protein PduK
- Cobalamin reductase PduS
Sequence:
MNTFSLQTRLYSGQGSLAVLKRFTNKHIWIICDGFLAHSPLLDTLRNALPADNRISVFSEITPDPTIHTVVQGIAQMQALQPQVVIGFGGGSAMDAAKAIVWFSQQSGINIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALYPDMAILDPELVVSVPPQITANTGMDVLTHALEAWVSPRASDFTDALAEKAAKLVFQYLPTAVEKGDCVATRGKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAGVPRAAKRYARLAKACGFCPAEANDIAAINALIQQIELLKQRCVLPSLAVALKEGRSDFSARIPAMVQAALADVTLRTNPRPANAEAIRELLEELL
Protein: NR1D2 protein (Nuclear receptor subfamily 1 group D member 2) (Q6NSM0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEVNAGGVIAYISSSSSASSPASCHSEGSENSFQSSSSSVPSSPNSSNSDTNGNPKNGDLANIEGILKNDRIDCSMKTSKSSAPGMTKSHSGVTKFSGMVLLCKVCGDVASGFHYGVHACEGCKGFFRRSIQQNIQYKKCLKNENCSIMRMNRNRCQQCRFKKCLSVGMSRDAVRFGRIPKREKQRMLIEMQSAMKTMMNSQFSGHLQNDTLVEHHEQTALPAQEQLRPKPQLEQENIKSSSPPSSDFAKEEVIGMVTRAHKDTFMYNQEQQENSAESMQPQRGERIPKNMEQYNLNHDHCGNGLSSHFPCSESQQHLNGQFKGRNIMHYPNGHAICIANGHCMNFSNAYTQRVCDRVPIDGFSQNENKNSYLCNTGGRMHLYSVHIQPKFHQKQQYHTISSLNHEVL
Protein: At1g31870 (Pre-mRNA-splicing factor of RES complex protein) (Q9C6S8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Zinc finger CCCH domain-containing protein 42
- Cell division cycle 5-like protein
- At2g32600/T26B15.16
- Nuclear protein-like
- Pre-mRNA-processing factor 17
- Transmembrane protein
- AT3G18790 protein
- FHA domain-containing protein DDL
- SMAD/FHA domain protein
- Pre-mRNA-processing protein 40C
Sequence:
MAGNQSLKDYLKKYESSDVVEKKKKKKKQKKPSKPEPRGVLVVDEDPVWQKQVDPEEDENEDDSAEETPLVDEDIEVKRMRRLEEIKARRAHNAIAEDGSGWVTLPLNREDTQSNISPPRRQRTRNDSPSPEPGPRRSVADRVDTDMSPPRRRKRHNSPSPEPNRKHTKPVSLDSDMSPPRKRKARNDSPSPEPEAKYLSEDLSPPRRRHVHSPSRESSRKRSDSVELDDDLSPPRRKRDLHGSPVSDVKKKSNDLSPPRRRRYHSPSPEPARRSSKSFGSNADLSPPGRNINMKDSQDSDLSPQRKAADLRRSSENVSRSSNFDSSPPRRPRRDSSPPQISKEQRKTGLISGKDIGSEYRKKKEDEKLRFKNMDSELTGQNAEAVFRDKITGKRISKEEYLKSKQKKVIEKPKEIKLEWGKGLAQKREAEARLQELELEKDKPFARTRDDPELDQMMKERVRFGDPMAHLVKKRKYETTLVDLGDDEEMKKSGFIIPQSVPKHSWLTRRLEAASNRYGIKPGRHWDGVDRSNGTEKDLIKKTNERKATEIEAYLWSVADM
Protein: Low affinity inorganic phosphate transporter 3 (PhPT3) (PhPht1;3) (Arbuscular mycorrhiza-induced phosphate transporter PT3) (AM-induced phosphate transporter PT3) (H(+)/Pi cotransporter PT3) (B2CPI5)
Organism: Petunia hybrida (Petunia)
Function: Low-affinity transporter for external inorganic phosphate (Pi) probably involved in the acquisition of phosphate released by arbuscular mycorrhizal (AM) fungi during AM symbiosis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8GSG4}; Multi-pass membrane protein {ECO:0000255}. Note=Present on the periarbuscular membrane in cells containing arbuscules during arbuscular mycorrhizal (AM) symbiosis with AM fungi. {ECO:0000250|UniProtKB:Q8GSG4}.
Interaction partners:
Sequence:
MAKDQLQVLNALDVAKTQLYHFTAIVIAGMGFFTDAYDLFCISLVTKLLGRIYYFHEGAPKPGILPSGISAAVNGVAFIGTLSGQLFFGWLGDKLGRKKVYGMTLMLMVICSIACGLSFGKTANGVIATLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFIAAVFAMQGFGILAGGIVALIVSAGFKNAYPAPTYSAHGKDSTPPEADYVWRIIVMIGALPALLTYYWRMKMPETARYTALVAKNTVKAAADMSKVLNVEIEEDKATVEKIEENGNSFGLFSKEFLRRHGLHLLGTTSTWFLLDIAFYSQNLFQKDIFSKIGWIPPPETMNALDEVFRIARAQTLIALCSTVPGYWFTVAFIDKMGRFAIQLMGSFFMTVFMFALAIPYDHWTKKENRIGFVIMYSLTFFFANFGPNATTFVVPAEIFPARLRSTCHGISAAAGKAGAIVGAFGFLYAAQSTDPKKVDAGYPTGIGVKNALIVLGCVNFLGMLSTLLVPESKGKSLEEMSKENEGEEENYGTETKGENAQTVPV
Protein: Ghrelin/obestatin prepropeptide precursor (Preproghrelin-1) (Q4LET9)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLGHGRVGHMMLLLCAFSLWAETVMCGSSFLSPTQKPQNRGDRKPPRVGRRTAAELEAPLPSEEKIMVSAPFQLAVSLSDAEYEDYGPVLQRMLLDVLGDPPTLDGAN
Protein: Proton-coupled folate transporter (Heme carrier protein 1) (PCFT/HCP1) (Solute carrier family 46 member 1) (Q6PEM8)
Organism: Mus musculus (Mouse)
Function: Proton-coupled folate symporter that mediates folate absorption using an H(+) gradient as a driving force. Involved in the intestinal absorption of folates at the brush-border membrane of the proximal jejunum, and the transport from blood to cerebrospinal fluid across the choroid plexus. Functions at acidic pH via alternate outward- and inward-open conformation states (By similarity). Protonation of residues in the outward open state primes the protein for transport (By similarity). Binding of folate promotes breaking of salt bridge network and subsequent closure of the extracellular gate, leading to the inward-open state and release of protons and folate (By similarity). Also able to transport antifolate drugs, such as methotrexate and pemetrexed. Involved in FOLR1-mediated endocytosis by serving as a route of export of folates from acidified endosomes (By similarity). Also acts as a lower-affinity, pH-independent heme carrier protein and constitutes the main importer of heme in the intestine. Imports heme in the retina and retinal pigment epithelium, in neurons of the hippocampus, in hepatocytes and in the renal epithelial cells. Hence, participates in the trafficking of heme and increases intracellular iron content (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:16143108}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:19074442}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:16143108}. Note=Shifts from the apical membrane of intestinal cells iron-deficient cells to the cytoplasm in response to increased in iron stores (PubMed:16143108). Localizes to the basolateral membrane of choroid plexus (PubMed:19074442). {ECO:0000269|PubMed:16143108, ECO:0000269|PubMed:19074442}.
Interaction partners:
- Reduced folate transporter
- Folate receptor alpha
- Choline/ethanolamine transporter FLVCR1
- Natural resistance-associated macrophage protein 2
- Plasma membrane ascorbate-dependent reductase CYBRD1
- Folate receptor beta
Sequence:
MEGRVSSVGSPHSFLNAPVLFRGPVEPLVFLANFALVLQGPLTTQYLWHRFSTELGYNGTRHRENCGNQSADPLMKEVETLTSHWTLYMNVGGFLVGLFWSTLLGAWSDRVGRRPLLVLASLGLLLQAVVSIFVVQLELHVGFFVLGRALCALLGDFNGLLAASFASVADVSSNHSRTFRMALLEACIGVAGTLASLLGGHWLRAQGYANPFWLALALLIVMALYAAFCFGETVKEPKSTRLFTLRHHRSIARLYVVPAPEKSRMHLALYSLAIFVVVTVHFGAQDILTLYELSAPLCWDSKLIGYGSAAQHLPYLTSLLGLRLLQFCLADTWVAEIGLAFNILGMVVFAFATITPLMFTGYGLLFLSLVTTPVIRAKLSKLVSESEQGALFSAVACVNSLAMLMASGIFNSIYPATLNFMKGFPFLLGAGLLFIPAILIGVLEKVNPHPEFQQFPQSP
Protein: Aryl hydrocarbon receptor (Q9PTI7)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNPNVTYASRKRRKPVQKIVKPSPAEGVKSNPSKRHRDRLNAELDRLASLLPFPQDVIAKLDKLSVLRLSVSYLRAKSFFDVALKSSNSTRLERNGIQESRTAKLGEGMQILEGELLLQALNGFVLVVTADALVFYVSSTIQDYLGFQQSDIIHQSVFELIHTEDRPEFQRQLHWALNPTQSADSGPSVQGDNGFSQPANYYNPDQLPPENSSFMERNFICRLRCLLDNSSGFLAMNFQGRLKFLHGQNKKGKDGAALSPQLALFAVATPLQPPSILEIRTKNFIFRTKHKLDFTPTGCDAKGKIVLGYTEAELCMRGTGYQFIHAADMLYCAENHVRMMKTGESGMTVFRLLTKENRWAWVQANARLVYKNGRPDYIISTQRPLTDEEGAEHLRKRNMKLPFMFATGEAVLYELTFPMSSLSDTSQPRSKTTTGKGGKTTLHGDSVDPNSLLGAMLRQDESVYLCPPASHKLSFERNFFADSRDELSGVVSSDWTDSLLPAGSHNILKQELMECSQDSSVPLPEDSAALFQDNKTNDLYSIMKNLGIDFEDLKCIQQDEEFFKTELSGMDDIGDIDITDEILTYVQDSLNKSDFLYSGCNQQQPLVQNAGCLVQQELDQHQIHQHQKQLMEQQQQQQQQLCQKMKHMQVNGMFTNWSSGTSMPLGCSQQQPQQYTSPGMQATAAEFYKSEVNASPYACRQEFVPYKQPTAMMPQLSTFAQMDFPVAGLDRSAYSASSNLEDFLGCLQQVPENLDCGINSESVMLTPQTCYAGAVSMYQCTQEAQPNCMDQMQYDPMMANQQTLLNKFQNGFNGGNVNEAYPSQLDVISNSQTATHLQPVHHPTEPRSFPDLASSGFM
Protein: Pre-mRNA-splicing factor CLF1 (Crooked neck-like factor 1) (PRP19-associated complex protein 77) (Synthetic lethal with CDC40 protein 3) (Q12309)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-mRNA splicing and cell cycle progression. Required for the spliceosome assembly by promoting the functional integration of the U4/U6.U5 tri-snRNP particle into the U1-, U2-dependent pre-spliceosome. Also recruits PRP19 to the spliceosome, as a component of the NTC complex (or PRP19-associated complex). The association of the NTC complex to the spliceosome mediates conformational rearrangement or stabilizes the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. Required for initiation of the DNA replication by binding the RNA replication origins, probably through its interaction with the origin recognition complex (ORC).
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor CEF1
- Small nuclear ribonucleoprotein G
- Pre-mRNA-splicing factor PRP21
- Small nuclear ribonucleoprotein Sm D1
- Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein PRP2
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor CWC23
- U2 snRNP component HSH155
- Pre-mRNA-splicing factor 8
- Small nuclear ribonucleoprotein E
Sequence:
MDTLEPTAVDTHVSAEQILRDVYKKGQKARGSTNIDILDLEELREYQRRKRTEYEGYLKRNRLDMGQWIRYAQFEIEQHDMRRARSIFERALLVDSSFIPLWIRYIDAELKVKCINHARNLMNRAISTLPRVDKLWYKYLIVEESLNNVEIVRSLYTKWCSLEPGVNAWNSFVDFEIRQKNWNGVREIYSKYVMAHPQMQTWLKWVRFENRHGNTEFTRSVYSLAIDTVANLQNLQIWSDMEVAKLVNSFAHWEAAQQEYERSSALYQIAIEKWPSNQLLKAGLLDFEKQFGDINSIEETISYKRKMEYETILSNNAYDYDTWWLYLDLISESFPKQIMQTFEKAIVDSRPKELSKNVQWKRYIYLWMRYICYVELELENSLLEEELFQRLIDDIIPHKHFTFSKIWLMYAKFLIRHDDVPKARKILGKAIGLCPKAKTFKGYIELEVKLKEFDRVRKIYEKFIEFQPSDLQIWSQYGELEENLGDWDRVRGIYTIALDENSDFLTKEAKIVLLQKYITFETESQEFEKARKLYRRYLELNQYSPQSWIEFAMYQTSTPTEQQLLDLAKLQSENVDEDIEFEITDENKLEARKVFEEAIVFFKEKDDKQGRLSILEALKDYEETYGTELDQETVKKRFPKVIKKVRLQNGVEEEFVDYIFPDDIDDDKPKPSKFLELAKKWKQEQAL
Protein: Ceramide-1-phosphate transfer protein (Glycolipid transfer protein domain-containing protein 1) (S4S694)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004150}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004150}. Nucleus outer membrane {ECO:0000256|ARBA:ARBA00004509}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004509}.
Interaction partners:
Sequence:
MDDSETGFNLKVVLVSFKQCLDEKEEVLLDPYIASWKGLVRFLNSLGTIFSFISKDVVSKLRIMERLRGGPQSEHYRSLQAMVAHELSNRLVDLERRSHHPESGCRTVLRLHRALHWLQLFLEGLRTSPEDARTSALCADSYNASLAAYHPWVVRRAVTVAFCTLPTREVFLEAMNVGPPEQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
Protein: Probable phosphoglucomutase, cytoplasmic 1 (PGM 1) (EC 5.4.2.2) (Glucose phosphomutase 1) (O49299)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This enzyme participates in both the breakdown and synthesis of glucose.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P93804}.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Alpha-glucan phosphorylase 1
- Alpha-glucan phosphorylase 2, cytosolic
- UTP--glucose-1-phosphate uridylyltransferase 2
- UTP--glucose-1-phosphate uridylyltransferase 1
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
- Hexokinase-1
- Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic
Sequence:
MVFKVSTVSTSPIDGQKPGTSGLRKKVKVFKQPNYLENFVQATFNALTAEKVKGATLVVSGDGRYYSKDAVQIIIKMAAANGVRRVWVGKNTLLSTPAVSAVIRERSGADGSKATGAFILTASHNPGGPTEDFGIKYNMENGGPAPESITDKIYENTKTIKEYPIAQDLPNVDISAVGVTSFEGPEGKFDVEVFDPADDYVKLMKSIFDFEAIRKLLSSPKFTFCYDALHGVAGAYAHRIFVEELGAQESALLNCTPKEDFGGGHPDPNLTYAKELVARMGLGKSDTGGEPPEFGAAADGDADRNMILGKRFFVTPSDSVAIIAANAIGAIPYFSSGLKGVARSMPTSAALDVVAKSLNLKFFEVPTGWKFFGNLMDAGMCSVCGEESFGTGSDHIREKDGIWAVLAWMSILAHKNKGNIDGNAKLVSVEDIVRQHWATYGRHYYTRYDYENVDAGKAKELMEHLVKLQSSIPEVNKIVKGIRSDVASVASADEFEYKDPVDGSISKHQGIRYLFEDGSRLVFRLSGTGSEGATIRLYIEQYEKDASKTGRESQEALSPLVDLALKLSKMEEFTGRSAPTVIT
Protein: Protein C-ets-1 (p54) (P14921)
Organism: Homo sapiens (Human)
Function: Transcription factor. Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts. May control the differentiation, survival and proliferation of lymphoid cells. May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion.
Subcellular location: Nucleus {ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:19377509}. Cytoplasm {ECO:0000269|PubMed:19377509}. Note=Delocalizes from nucleus to cytoplasm when coexpressed with isoform Ets-1 p27. {ECO:0000269|PubMed:19377509}.
Interaction partners:
- Runt-related transcription factor 1
- Paired box protein Pax-5
- Mitogen-activated protein kinase 1
- Forkhead box protein O1
- Cellular tumor antigen p53
- Protein C-ets-2
- Histone acetyltransferase p300
- Mitogen-activated protein kinase 3
- Nuclear factor NF-kappa-B p100 subunit
- Serum response factor
Sequence:
MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMNGAALCALGKDCFLELAPDFVGDILWEHLEILQKEDVKPYQVNGVNPAYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPLQTDTLQNDYFAIKQEVVTPDNMCMGRTSRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE