wanglab/gogpt-training-data huggingface dataset:
Protein: LD01527p (Short spindle 3, isoform A) (Q9VJ35)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
- GEO13330p1
- GH04035p
Sequence:
MEMREVLSREGREAKNLLVYQFCDETTSSGATSGFGSTGGDVGGGSGGDGPAVGSGGVLLNGDCYRKPPMVPPKSPNGTPKNCQSPTSPRLKSSASVGCGGGSSGGPRVRSASTGRDKKSELQARYWALLFGNLQRAINEIYQTVECYENISSCQETILVLENYVRDFKALCEWFKVSWDYESRPLQQRPQSLAWEVRKSNPTPRVRTRSLCSPNNSGKSSPALFPGTQSGETSPFCDNGQISPRKLLRAYDQVPKGAMRLNVRELFAASKRATQGSSQSDNMEGPLDLSGDKSNFVLRSTQYAQTDLEDPHLTLADVREKMRMEAEEREAQNRIENEALEEVTIPIDNEDATESLNKQEPSSLELPIHNVADLSKEPELMEAASEATALEMTVASLESMENALLNQQANKEPTPPSTVIKPLAEILKKPQPLNPLSGNNVQNSPLKYSSVLNRPSKKMIPPPGGVAAQKTISTKPGLVKPNLTTTVNGLRSTKTATAPPAIKTTGRSGLQRHPRPSSKTECYGPPNNVASRLSARSRTMLEINGRNTNSSARTLPKKTNPGSILSTATRTKMSSRLSSREDITSSTSTLKASNEQLSNSRNTLKAENQHSEPKQIQPPTDADDGWLTVKNRRRTSMHWANRFNQPTGYASLPTLALLNEQQKEQEHKEKQKGEDDGKVIVKTISAKTKAPIEVAKAKAKTSIVITRPEIKNAKAKVNSFPVQKSNTNQVKKPEKQEKSDTTAPAAIASSSNTRNSSHSICVGRNSIIKRQKSDLTGLKMTSLHKEYMRSEKNALRKLQQKEQGNQQHNSSSSSAETVVESCNEDHSKIDIKIQTNCEFSKTIGELYESIAHCKLPSGSLKTNASTLSACDENEEQNTDDNEEERNERILGEVQESLERQIRELEQTEIDVDTETDETDCEVQLEEQDDGVDGLEMGSGDDSAVFVTMSDDENASLELRYQALLSDMSWNERAEALATLQAYVARHPGRAQELHQKLSSPSRRRSLQETLKKYQAKQARAQQKRNLLQQEKAAKLQQLFSRVEDVKAAKNQIIEDKRQKMQGRLQRAAENREQYLKQIIEKAHDEEKKLKEINFIKNIEAQNKRLDLLESSKETEGRLQDLEQERQKRVEEKLAKEAAVERRRQALEKERLLKLEKMNETRLEKEQRIGKMQEQKEKQRQALAREKARDREERLLALQVQQQQTTEELQRKILQKQMESARRHEENIEHIRQRALELTIPTRQADEGRGDQDVSEDILNGNATSTTNEDCDLSSSLSEVGGNNAHTRSYKKKMKKLKQRMNQCAAEYLESLEALPAHARRDSTVPKLLNLVVKGGGAQGLDRNLGNLLRVIPKAQTLDFLAFLCMDGLGILANHVISKGMDENSEISRKSVYLAAQLYRNACSVCPQIARHALLGNSITVLFDAINKSFQLPEEKSPQHPVELSTELMLACTEALSSSYVKKNTHPKVPERLPDMINYAVITGLIEILSRRIQKVRESIESNKSVMLSLLTTLGFLSRFIDVCQPGPADPTRLLSAAKSTELFGTVSMLYGCVMPMGECIPPRTTALAASTFHLYVSLASLDVNTFQETLTVEGPLSLKLLDVMTVILNCSLVNDQWTTNSESCPMLIDLVASMAFFCVNNRRHQDLLISEQYAVIFKRMAKLPTQFNPVIYPFLVTVSFNNPPAREFLSKDFDLTFLDEYSKSEMAQRNVVIKLINSRTKDKISAGNKKNA
Protein: Protein tyrosine phosphatase-like protein egg-3 (Egg sterile protein 3) (Q20402)
Organism: Caenorhabditis elegans
Function: Probable pseudophosphatase required for the oocyte-to-zygote transition during which it regulates the polarized dispersal of the cortical actin cytoskeleton, the synthesis of the eggshell chitin layer and the formation of the polar bodies after meiosis I and II. Acts as scaffold to tether kinase mbk-2 and pseudophosphatases egg-4 and egg-5 to the oocyte cortex and thus restricts mbk-2 activity to the cortex during meiosis I. Regulates mbk-2 localization to cytoplasmic foci during meiosis II. Also required for chitin synthase chs-1 localization to the cell cortex of unfertilized oocytes and to cytoplasmic foci in the fertilized embryo.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:17869112, ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:19879147, ECO:0000269|PubMed:19879842, ECO:0000269|PubMed:20971008}. Cytoplasm {ECO:0000269|PubMed:17869112, ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:19879147, ECO:0000269|PubMed:19879842, ECO:0000269|PubMed:20971008}. Note=Co-localizes with mbk-2 to the oocyte cell membrane during most of meiosis I, relocalizes to subcortical foci during anaphase I which become cytoplasmic during meiosis II (PubMed:17869112, PubMed:17869113, PubMed:19879842). At the end of meiosis II, egg-3 is degraded releasing mbk-2 in the cytoplasm (PubMed:17869112, PubMed:17869113, PubMed:19879842). Co-localizes with egg-4 to the cell cortex in developing oocytes and in newly fertilized embryos (PubMed:19879147). Cortical localization in developing oocytes is egg-1, egg-2 and chs-1-dependent (PubMed:17869112, PubMed:20971008). Co-localizes in the fertilized egg with chs-1 to cytoplasmic foci (PubMed:17869112). {ECO:0000269|PubMed:17869112, ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:19879147, ECO:0000269|PubMed:19879842, ECO:0000269|PubMed:20971008}.
Interaction partners:
- Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2
- Chitin synthase chs-1
- LDL receptor repeat-containing protein egg-1
- LDL receptor repeat-containing protein egg-2
- Chitin-binding domain protein cbd-1
- Pumilio domain-containing protein 5
- Zinc finger protein mex-6
- Meiotic spindle formation protein mei-1
- CCCH-type zinc finger protein oma-1
- RING-type domain-containing protein
Sequence:
MRTSDSHLPLSNLARSDSIEFKDAVINEKWVHSANRRKGHLTPKAPEKKSGWFGGQKSEEELLMERVEQHELEELQTFIAQKLFRVDGIICDEETRILLVEKLMNAKEYPTINHDELAHRYGSSMAGWLRDRLVPSMSDCSSVLQRAAAEFYQNKMSDPLCNWGQLNPEHVSMVAARIAKFSEEMSSKVKWSLLVEPGKFSCHLTEFVQEFNRLDRMFVSNELSDEESLQTAFNANYLTKARSKMVPCAEFSRVKLNDGLGRLDDRNELRNGMFSDEHEFLQEEGYTAKSTYGTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSSTLGPLDSANRNHCPYYWPRAENESLRFGSFHITCMKVDSKADPLFTITKLKVQKVGGNLLDAEFDEELFLEHWQWDWQYLGDVHWPFRVLRKARQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQSCVFVRLQRRLSVSSVLLYLFIYRVILRWIEPYVNKWYHRAALGLRFKSIGFIQKYNAMIQEFSRITPAY
Protein: Ppp1r9a protein (Q80ZL7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVLQTCPNYFCLDICFLQLQAAENEKVRWELEKNQLQQNIEENKERMLKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIKRQEVERKKREEVEKAHLLEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRPSPGEVSKGDTMENVEVKQTSCQDGLSQGLGSGSVGKVFSTPYKDLNSDSQH
Protein: Sodium/pyruvate cotransporter BASS2, chloroplastic (Bile acid transporter 1) (Bile acid-sodium symporter family protein 2) (Q1EBV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sodium-coupled metabolite transporter that plays a crucial role in pyruvate transport across the chloroplast envelope. Is required for sodium-coupled pyruvate import into plastids.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Plastid, chloroplast envelope {ECO:0000305}.
Interaction partners:
- Sodium/proton antiporter 1
- Ascorbate transporter, chloroplastic
- Dicarboxylate transporter 2.1, chloroplastic
- Dicarboxylate transporter 1, chloroplastic
- Probable sodium/metabolite cotransporter BASS4, chloroplastic
- Pyruvate, phosphate dikinase regulatory protein 1, chloroplastic
- Pyruvate, phosphate dikinase 1, chloroplastic
- Phosphoenolpyruvate/phosphate translocator 2, chloroplastic
- Nucleotide-sugar transporter family protein
Sequence:
MASISRILPTDGRLSQCRINTSWVPSTTRTQTHLDFPKLVSVSNSGISLRIQNSKPISPVFALEATSSRRVVCKAAAGVSGDLPESTPKELSQYEKIIELLTTLFPLWVILGTLVGIFKPSLVTWLETDLFTLGLGFLMLSMGLTLTFEDFRRCLRNPWTVGVGFLAQYMIKPILGFLIAMTLKLSAPLATGLILVSCCPGGQASNVATYISKGNVALSVLMTTCSTIGAIIMTPLLTKLLAGQLVPVDAAGLALSTFQVVLVPTIIGVLANEFFPKFTSKIITVTPLIGVILTTLLCASPIGQVADVLKTQGAQLILPVALLHAAAFAIGYWISKFSFGESTSRTISIECGMQSSALGFLLAQKHFTNPLVAVPSAVSVVCMALGGSGLAVFWRNLPIPADDKDDFKE
Protein: Protein-serine/threonine kinase (EC 2.7.11.-) (O82424)
Organism: Zea mays (Maize)
Subcellular location: Mitochondrion matrix {ECO:0000256|RuleBase:RU366032}.
Interaction partners:
Sequence:
MASEPVARAVAEEVGRWGSMKQTGVTLRYMMEFGSRPTQRNLLLSAQFLHKELPIRFARRALELDSLPFGLSNKPAILKVRDWYLDSFRDIRYFPEVRSRNDELAFTQMINMVKVRHNNVVPTMALGVQQLKKELGRSRKVPFEFDEIDEFLDRFYMSRIGIRMLIGQHVALHDPKPEPGVIGLINTRLSPIQVAQAACEDARSVCLREYGSAPDINIYGDPNFTFPYVTLHLHLMLFELVKNSLRAVQERYMNSDKDVPPVRIIVADGEEDVTIKVSDEGGGIPRSGLPRIFTYLYSTAKNPPELDRPNTERVTMAGYGFGLPISRLYARYFGGDLQIISMEGYGTDAYLHLSRLGDSEEPLP
Protein: F-box/LRR-repeat protein 4 (F-box and leucine-rich repeat protein 4) (F-box protein FBL4/FBL5) (Q9UKA2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm. Nucleus. Mitochondrion outer membrane {ECO:0000269|PubMed:36896912}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- Cyclin-F
Sequence:
MSPVFPMLTVLTMFYYICLRRRARTATRGEMMNTHRAIESNSQTSPLNAEVVQYAKEVVDFSSHYGSENSMSYTMWNLAGVPNVFPSSGDFTQTAVFRTYGTWWDQCPSASLPFKRTPPNFQSQDYVELTFEQQVYPTAVHVLETYHPGAVIRILACSANPYSPNPPAEVRWEILWSERPTKVNASQARQFKPCIKQINFPTNLIRLEVNSSLLEYYTELDAVVLHGVKDKPVLSLKTSLIDMNDIEDDAYAEKDGCGMDSLNKKFSSAVLGEGPNNGYFDKLPYELIQLILNHLTLPDLCRLAQTCKLLSQHCCDPLQYIHLNLQPYWAKLDDTSLEFLQSRCTLVQWLNLSWTGNRGFISVAGFSRFLKVCGSELVRLELSCSHFLNETCLEVISEMCPNLQALNLSSCDKLPPQAFNHIAKLCSLKRLVLYRTKVEQTALLSILNFCSELQHLSLGSCVMIEDYDVIASMIGAKCKKLRTLDLWRCKNITENGIAELASGCPLLEELDLGWCPTLQSSTGCFTRLAHQLPNLQKLFLTANRSVCDTDIDELACNCTRLQQLDILGTRMVSPASLRKLLESCKDLSLLDVSFCSQIDNRAVLELNASFPKVFIKKSFTQ
Protein: N-acetyltransferase ECO1 (EC 2.3.1.-) (Chromosome transmission fidelity protein 7) (Establishment of cohesion protein 1) (P43605)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for establishment of sister chromatid cohesion during S phase but not for its further maintenance during G2 or M phases or for loading the cohesin complex onto DNA. Interacts with the three known alternate replication factor C (RFC) complexes, suggesting that these complexes have essential but redundant activity in cohesion establishment. Acts by acetylating the cohesin complex component SMC3. In vitro, possesses acetyltransferase activity where it can acetylate itself and components of the cohesin complex (MCD1, IRR1 and PDS5), but is unable to acetylate histones.
Subcellular location: Nucleus {ECO:0000269|PubMed:9990855, ECO:0000269|PubMed:9990856}. Note=Associated with chromatin.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein PDS5
- Protein RAD61
- Sister chromatid cohesion protein 1
- Chromosome transmission fidelity protein 18
- ATP-dependent DNA helicase CHL1
- Cohesin subunit SCC3
- Structural maintenance of chromosomes protein 1
- Proliferating cell nuclear antigen
- Separin
Sequence:
MKARKSQRKAGSKPNLIQSKLQVNNGSKSNKIVKCDKCEMSYSSTSIEDRAIHEKYHTLQLHGRKWSPNWGSIVYTERNHSRTVHLSRSTGTITPLNSSPLKKSSPSITHQEEKIVYVRPDKSNGEVRAMTEIMTLVNNELNAPHDENVIWNSTTEEKGKAFVYIRNDRAVGIIIIENLYGGNGKTSSRGRWMVYDSRRLVQNVYPDFKIGISRIWVCRTARKLGIATKLIDVARENIVYGEVIPRYQVAWSQPTDSGGKLASKYNGIMHKSGKLLLPVYI
Protein: Abhydrolase domain-containing protein lid-1 (Lipid droplet protein 1) (O02218)
Organism: Caenorhabditis elegans
Function: Acts coordinately with atgl-1 within the lipolytic cascade to distribute stored energy to tissues during nutritional deprivation.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:25202121}. Note=Forms ring-like structures on the surface of lipid droplets. {ECO:0000269|PubMed:25202121}.
Interaction partners:
- Patatin-like phospholipase domain-containing protein atgl-1
- Fatty acid synthase
- Hormone-sensitive lipase
- AB hydrolase-1 domain-containing protein
- Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-1
- Acyltransferase
- Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-2
- Perilipin-1 homolog
Sequence:
MAIATTKTALTTIMNWMTFTDDSKEQLKIVEGRLFQSCEVSYEAKYVPVRFKRGEVYTVTVRPREAENLNGEAIVFIPGLGAGVAMFTANFNSCAKNHAVHSFDPLGFGRSSRSRFSDDNAIAELEMVEVMEDWRKAMGIEKMYIIGHAFGGYLASAYALENPSRVAHLILVDPWGFAEKVETTEKLIKPYAWMSFLGGVAGYFNPFSPMRWMGPYAPAIVKKLRPDLLLRFPGLHDYDIYKYVYYLNLPNPTGETAFMNMTLPVGWAKRPMIKRFNGIDKNVGVSFIYGSKSWIDPGPAIDIQSTRENAYVDIKIVRGAGTHVYADDPAAFNEIVSDVVEGRLSNPSNDFEIEECCHSD
Protein: Serine O-acetyltransferase (SAT) (EC 2.3.1.30) (A0A120HUS7)
Organism: Lacticaseibacillus casei (Lactobacillus casei)
Function: Catalyzes the formation of O-acetylserine (OAS) from L-serine and acetyl-CoA. To a lesser extent, is also able to use succinyl-CoA and propionyl-CoA as acyl donors, but not butyryl-CoA. Does not acylate D-serine and L-homoserine.
Interaction partners:
- Aspartate kinase
- Aspartate kinase
- Cysteine synthase
- 5,10-methylenetetrahydrofolate reductase
- Homoserine dehydrogenase
- Cystathionine beta-lyase
Sequence:
MEKSPLKIGILNVMHDKADTKTRLQHVLTHTAIPVDLHFYYPMTHYAGRTVPEAVSSILDPLDIHEVATMDGFIITGSPIETLEFDQVHYIAEVRTLLKTLSQHVPNQLYLCWGGMVALNYFFGISKLILPHKLFGVYPQTILEPHPLLKGLKNDFKSPHARYAEMDVRGIHADPRLTINATTTKGKLFMVTEPTDTQTFVFSHIEYDRWGLDSEYKREVAAHPEIDYVRAKHYYHHKNDYDHPKFNWKKTQRTIFDNWIQHVADHRNDNH
Protein: Serum amyloid A-2 protein [Cleaved into: Amyloid protein A] (P05367)
Organism: Mus musculus (Mouse)
Function: Major acute phase reactant.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0DJI8}.
Interaction partners:
- Serum amyloid A-1 protein
- Haptoglobin
- Serum amyloid A-3 protein
- Alpha-1-acid glycoprotein 2
Sequence:
MKLLTSLVFCSLLLGVCHGGFFSFIGEAFQGAGDMWRAYTDMKEAGWKDGDKYFHARGNYDAAQRGPGGVWAAEKISDARESFQEFFGRGHEDTMADQEANRHGRSGKDPNYYRPPGLPAKY
Protein: Segmentation protein cap'n'collar (P20482)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in posterior cephalic patterning. Probable subunit of a heterodimeric regulatory protein involved in the control of head morphogenesis. Isoform B may have a repressive effect on Dfd response elements, thereby modifying the activity and specificity of the Hox system and moving the body anterior/posterior axis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:9778513}.
Interaction partners:
- Maf-S, isoform B
- FI11917p
- RAC serine/threonine-protein kinase
- Protein kinase shaggy
- histone acetyltransferase
- Cullin 3, isoform F
- Putative glycogen synthase kinase-3 homolog
- Homeotic protein deformed
- Glutamate--cysteine ligase
Sequence:
MISNKKSYAMKMLQLALALSLLHYNPDYLLHRWDSQLELGTHGDGWELEMLRTVHRLDMDHNPYGNRKGLSPRIEDLLNFDDPSLGGMANGIGGCKLPPRFNGSTFVMNLHNTTGNSSVQTAALQDVQSTSAAATGGTMVVGTGGAPTSGGQTSGSALGEIHIDTASLDPGNANHSPLHPTSELDTFLTPHALQDQRSIWEQNLADLYDYNDLSLQTSPYANLPLKDGQPQPSNSSHLDLSLAALLHGFTGGSGAPLSTAALNDSTPHPRNLGSVTNNSAGRSDDGEESLYLGRLFGEDEDEDYEGELIGGVANACEVEGLTTDEPFGSNCFANEVEIGDDEEESEIAEVLYKQDVDLGFSLDQEAIINASYASGNSAATNVKSKPEDETKSSDPSISESSGFKDTDVNAENEASAASVDDIEKLKALEELQQDKDKNNENQLEDITNEWNGIPFTIDNETGEYIRLPLDELLNDVLKLSEFPLQDDLSNDPVASTSQAAAAFNENQAQRIVSETGEDLLSGEGISSKQNRNEAKNKDNDPEKADGDSFSVSDFEELQNSVGSPLFDLDEDAKKELDEMLQSAVPSYHHPHPHHGHPHAHPHSHHHASMHHAHAHHAAAAAAAHQRAVQQANYGGGVGVGVGVGVGVGSGTGSAFQRQPAAGGFHHGHHQGRMPRLNRSVSMERLQDFATYFSPIPSMVGGVSDMSPYPHHYPGYSYQASPSNGAPGTPGQHGQYGSGANATLQPPPPPPPPHHAAMLHHPNAALGDICPTGQPHYGHNLGSAVTSSMHLTNSSHEADGAAAAAAAYKVEHDLMYYGNTSSDINQTDGFINSIFTDEDLHLMDMNESFCRMVDNSTSNNSSVLGLPSSGHVSNGSGSSAQLGAGNPHGNQANGASGGVGSMSGSAVGAGATGMTADLLASGGAGAQGGADRLDASSDSAVSSMGSERVPSLSDGEWGEGSDSAQDYHQGKYGGPYDFSYNNNSRLSTATRQPPVAQKKHQLYGKRDPHKQTPSALPPTAPPAAATAVQSQSIKYEYDAGYASSGMASGGISEPGAMGPALSKDYHHHQPYGMGASGSAFSGDYTVRPSPRTSQDLVQLNHTYSLPQGSGSLPRPQARDKKPLVATKTASKGASAGNSSSVGGNSSNLEEEHLTRDEKRARSLNIPISVPDIINLPMDEFNERLSKYDLSENQLSLIRDIRRRGKNKVAAQNCRKRKLDQILTLEDEVNAVVKRKTQLNQDRDHLESERKRISNKFAMLHRHVFQYLRDPEGNPCSPADYSLQQAADGSVYLLPREKSEGNNTATAASNAVSSASGGSLNGHVPTQAPMHSHQSHGMQAQHVVGGMSQQQQQQSRLPPHLQQQHHLQSQQQQPGGQQQQQHRKE
Protein: Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (SMAD family member 2) (SMAD 2) (Smad2) (Q9I9P9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Promotes differentiation of dorsal tissues. May be involved in the mediation of Ndr2 signaling during mesoderm and axis formation during embryogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q15796}. Nucleus {ECO:0000250|UniProtKB:Q15796}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with Smad4. {ECO:0000250|UniProtKB:Q15796}.
Interaction partners:
- Mothers against decapentaplegic homolog.
- Receptor protein serine/threonine kinase
- Forkhead box protein H1
- Mothers against decapentaplegic homolog
- E3 ubiquitin-protein ligase SMURF2
- TGF-beta receptor type-2
- receptor protein serine/threonine kinase
- Receptor protein serine/threonine kinase
- Zinc finger FYVE domain-containing protein 9 isoform X1
- Mitogen-activated protein kinase
Sequence:
MSSILPFTPPVVKRLLGWKKSASGSSGAGGGGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNRNTKCVTIPSNCSEIWGLSTPNTIEQWDTSGLYSYPDQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAIETCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTNSIPENTNFPTGIEPPNNYIPETPPPGYISEDGEASDQQMNQSMDTGSPAELSPSTLSPVNHGMDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS
Protein: Ureidoglycolate lyase (EC 4.3.2.3) (Ureidoglycolatase) (Ureidoglycolate hydrolase) (P77731)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the anaerobic utilization of allantoin as sole nitrogen source. Reinforces the induction of genes involved in the degradation of allantoin and glyoxylate by producing glyoxylate.
Interaction partners:
- Ureidoglycolate dehydrogenase
- Glyoxylate carboligase
- (S)-ureidoglycine aminohydrolase (UGHY) (UGlyAH)
- Allantoinase
- HTH-type transcriptional repressor AllR
- Malate synthase G
- Malate synthase A
- Isocitrate lyase
- Allantoate amidohydrolase
- Glycolate oxidase subunit GlcE
Sequence:
MKLQVLPLSQEAFSAYGDVIETQQRDFFHINNGLVERYHDLALVEILEQDCTLISINRAQPANLPLTIHELERHPLGTQAFIPMKGEVFVVVVALGDDKPDLSTLRAFITNGEQGVNYHRNVWHHPLFAWQRVTDFLTIDRGGSDNCDVESIPEQELCFA
Protein: Auxin-responsive protein (D3K0M2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004549}.
Interaction partners:
Sequence:
MEVSNSCSSFSSSSVDSTKPSPSESSVNLSLSLTFPSTSPQREARQDWPPIKSRLRDTLKGRRLLRRGDDTSLFVKVYMEGVPIGRKLDLCVFSGYESLLENLSHMFDTSIICGNRDRKHHVLTYEDKDGDWMMVGDIPWDMFLETVRRLKITRPERY
Protein: Glycerol-3-phosphate dehydrogenase [NAD(P)+] 2 (EC 1.1.1.94) (NAD(P)(+)-dependent glycerol-3-phosphate dehydrogenase 2) (NAD(P)H-dependent dihydroxyacetone-phosphate reductase 2) (P9WN77)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase 1
- Glycerol-3-phosphate dehydrogenase 2
- Putative acyltransferase plsB1
- 1-acylglycerol-3-phosphate O-acyltransferase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate acyltransferase
- Conserved protein
- GTPase Der
- Diacylglycerol kinase
- D-alanine--D-alanine ligase
Sequence:
MAGIASTVAVMGAGAWGTALAKVLADAGGEVTLWARRAEVADQINTTRYNPDYLPGALLPPSIHATADAEEALGGASTVLLGVPAQTMRANLERWAPLLPEGATLVSLAKGIELGTLMRMSQVIISVTGAEPPQVAVISGPNLASEIAECQPAATVVACSDSGRAVALQRALNSGYFRPYTNADVVGTEIGGACKNIIALACGMAVGIGLGENTAAAIITRGLAEIIRLGTALGANGATLAGLAGVGDLVATCTSPRSRNRSFGERLGRGETLQSAGKACHVVEGVTSCESVLALASSYDVEMPLTDAVHRVCHKGLSVDEAITLLLGRRTKPE
Protein: Uncharacterized protein Rv1324 (P9WG61)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Thioredoxin reductase
- Uncharacterized protein Rv1836c
- Probable uroporphyrin-III C-methyltransferase HemD
- Probable acetyl-CoA acetyltransferase
Sequence:
MTRPRPPLGPAMAGAVDLSGIKQRAQQNAAASTDADRALSTPSGVTEITEANFEDEVIVRSDEVPVVVLLWSPRSEVCVDLLDTLSGLAAAAKGKWSLASVNVDVAPRVAQIFGVQAVPTVVALAAGQPISSFQGLQPADQLSRWVDSLLSATAGKLKGAASSEESTEVDPAVAQARQQLEDGDFVAARKSYQAILDANPGSVEAKAAIRQIEFLIRATAQRPDAVSVADSLSDDIDAAFAAADVQVLNQDVSAAFERLIALVRRTSGEERTRVRTRLIELFELFDPADPEVVAGRRNLANALY
Protein: Pyruvate dehydrogenase E1 component subunit alpha (EC 1.2.4.1) (Q9ZQY0)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MAAAALLRRLPAARAQAQAPAFMAARPISDSTAALTIETSVPFTSHLVDPPSRDVTTTPAELVTFFRDMSLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITRSDSIITAYRDHCTYLARGGDLVSAFSELMGREAGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGCGLAFAQKYKKEDTATFALYGDGAANQGQLFEALNISALWKLPAILVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQACKFAKDHAVANGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLTHDLANAAELKNMEKEIRKQVDDAIAKAKESSMPDTSELFTNVYKKGFGVESFGPDRKEMRASLP
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (A0A0G2JUS4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATPTDPAAMPHPGPSPGPGPSPGPILGPSPGPGPSPGSVHSMMGPSPGPPSVSHPMSTMGSADFPQEGLHQLHKPMDGIHDKGIVEDVHCGSMKGTSMRPPHPGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPISGGGPTPPQMPPSQPGTLIPGDLQAMNQPNRGPSPFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQGKRTLPGMQQQQQQQQQQQQQQQQQQPQQPQQPQQQTQAQPQQQQQQQQQPPALVSYNRPSGPGQELLMTAQNTQQKLSAPAPSGRPSPAPPAATQPTATAVPGPSVQQPAPGQPSPVLQLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRIQELESLPGSLPPDLRTKATVELKALRLLNFQRQLRQEVVACMRRDTTLETALNSKAYKRSKRQTLREARMTEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRRLAYLLQQTDEYVANLTNLVWEHKQAQAAKEKKKRRRRRKKAEENAEGGEPALGPDGEPIDESSQMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPRSDSEESESDYEEEDEEEESSRQETEEKILLDPNSEEVSEKDAKQIIETAKQDVDDEYSMQYSARGSQSYYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHKVLRPFLLRRLKKEVESQLPEKVEYVIKCDMSALQKILYRHMQAKGILLTDGSEKDKKGKGGAKTLMNTIMQLRKICNHPYMFQHIEESFAEHLGYSNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEENEEEDEVPDDETLNQMIARREEEFDLFMRMDMDRRREDARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWLRAIEDGNLEEMEEEVRLKKRKRRRNVDKDPVKEDVEKAKKRRGRPPAEKLSPNPPKLTKQMNAIIDTVINYKDRKESVIISTEAWETWRKMSCFSVTMHRHSTWKDPRSTKTPLSSSQCLRVLGRKLPKKKRVRRKAMRRRRKRMKRSQRQRVSL
Protein: General transcription factor IIH subunit 3 (General transcription factor IIH polypeptide 3) (F5GXG6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368090}.
Interaction partners:
Sequence:
MVSDVDANPIWWGKQALKESQFTLSKCIDAVMVLGNSHLFMNRSNKLAVIASHIQESRFLYPGKNGRLGDFFGDPGNPPEFNPSGSKDGKYELLTSANEVIVEEIKDLMTKSDIKGQHTETLLAGSLAKALCYIHRMNKEVKDNQEMKSRILVIKAAEDSALQYMNFMNVIFAAQKQ
Protein: Voltage-gated potassium channel regulatory subunit KCNG1 (Potassium voltage-gated channel subfamily G member 1) (Voltage-gated potassium channel subunit Kv6.1) (D4AD53)
Organism: Rattus norvegicus (Rat)
Function: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q14721}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Vitamin K-dependent gamma-carboxylase
- Voltage-gated delayed rectifier potassium channel KCNH4
- Ubiquitin-like protein FUBI
- FAU ubiquitin like and ribosomal protein S30 fusion like 2
- Voltage-gated potassium channel subunit beta-1
- Voltage-gated potassium channel subunit beta-3
- Voltage-gated potassium channel subunit beta-2
Sequence:
MTLLPGDNSDYDYSALSCASDTSFHPAFFPQRQAIKGVFYRRAQRLGPQDDLHQSISLGDRRRQIIINVGGIKYSLPWTTLDEFPLTRLGQLKACTNFDDILSVCDDYDVTCNEFFFDRNPGAFGTILTFLRAGKLRLLREMCALSFQEELLYWGIAEDHLDGCCKRRYLQKIEEFAEMMEREDEEEALDSEDQESEGPSTSEGRLSRCMRRLRDMVEKPHSGLPGKVFACLSVLFVTVTAVNLSVSTLPSLREEEEQGQCSQMCHNVFIVESVCVGWFSLEFLLRFIQAPSKFAFLRSPLTLIDLVAILPYYVTLLVDGAASSRRKPSTGNSYLDKVGLVLRVLRALRILYVMRLARHSLGLQTLGLTARRCTREFGLLLLFLCVAIALFAPLLYVIENEMADSPEFTSIPACYWWAVITMTTVGYGDMVPRSTPGQVVALSSILSGILLMAFPVTSIFHTFSRSYLELKQEQERVLIRRAQYLIKTKSQLSGMSQDSDILFGSASSDTRDNN
Protein: Carnosine synthase 1 (EC 6.3.2.11) (ATP-grasp domain-containing protein 1) (D3KCC4)
Organism: Gallus gallus (Chicken)
Function: Catalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine.
Interaction partners:
- Carnosine N-methyltransferase 2
- Glutamate decarboxylase like 1.
- Carnosine dipeptidase 1
- Carnosine N-methyltransferase
- M20_dimer domain-containing protein.
- Uncharacterized protein.
- Beta-ureidopropionase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase 9 family member A1
- Aldehyde dehydrogenase 7 family member A1
Sequence:
MISVDRLSEEQALGMKEQEWAGPEALCPGWQEEEVSDGEGPEDSGHPDPTAHAYEVLQHTLRLEGMPLTIDRTGQPRTGSGPLDMTVCVLGSPTAFLPVLLEGGTRYPGAMVLCLAPAWASRVPSETSPGSWSLLLSRGVSFEAGGCTALEEFVPPRRATYVTGTFGSEGSWEGELARDLDCPTGGSALLTRWLEDPLLSRWLLSARAGLPVPPTLAFITGLWETLPEEPEPPGVHLVRLQDPQGQESLVRDEVGAFLEGSSMQPYDQVAVRLSGWRWRGTDPHSTHRKVEGEAVAQAVAALLKGLREEESILLEALVPTARLPTLPPRSAAPRLPMALRICTVVCRSWGDRPQLCQVACTAGRAEVPVRHGSALPLGLDSSLRQWGLADAAQRQALAGQLREAAEAAMAALLAAEGELSPAQRGGARAHTDVLGVDFLLACVDGTLELVALSANCLRCLETCLLAEGMGHDVGQPAGDVPRLLAECLLHRAQCHLVEGKDILLIGAGGVSKSFVWEAAREYGLRIHLVESDPEHFAAGLVETFLPYDSREHRRDEEHAERVLEMLRARGLRPDACLSYWDDCVVLTALLCQRLGLPGCPPAAVRLAKQKSRTHQHLQRCRRGRPPPAAFSVPCRRLRSHGDVERAAGAVPFPAVAKLEFGAGAVGVRLVENAGQCHAHAAQLWHDLRADADHPGIGLGWGNAMLLMEYVPGTEHDVDLVLFEGRLLGAWVSDNGPTRVPTFLETAATLPSCLPADRQAQLVRAALRCCRACGLRHGVFNVELKLSPAGPRLLEINPRMGGFYLRDWMRAVYGPDLLLAAVLLALGLPPVLPSRPAPRQQLAGVMCLASEHGRALRGGVMAALQGLQRRGLVRLNPLFEEAGGRYEEPCLSVACAGDGPAEACGRLLGLCQALGIDSPQYPVGHFLSHFK