wanglab/gogpt-training-data huggingface dataset:
Protein: Envelope glycoprotein B (UL55) (A8T7D5)
Organism: Human cytomegalovirus (HHV-5) (Human herpesvirus 5)
Interaction partners:
Sequence:
MESRIWCLVVCVNLCIVRLGAAVSSSSTRGTSATHSHHSSRTTSAAHSRSGSVSQRVTSSQTVSHGVNETIYNTTLKYGDVVGVNTTKYPYRVCSMAQGTDLIRFERNIVCTSMKPINEDLDEGIMVVYKRNIVAHTFKVRVYQKVLTFRRSYAYIHTTYLLGSNTEYVAPPMWEIHHINSHSQCYSSYSRVIAGTVFVAYHRDSYENKTMQLMPDDYSNTHSTRYVTVKDQWHSRGSTWLYRETCNLNCMVTITTARSKYPYHFFATSTGNVVDISPFYNGTNRNASYFGENADKFFIFPNYTIVSDFGRPNSALETHRLVAFLERADSVISWDIQDEKNVTCQLTFWEASERTIRSEAEDSYHFSSAKMTATFLSKKQEVNMSDSALDCVRDEAINKLQQIFNTSYNQTYEKYGNVSVFETTGGLVVFWQGIKQKSLVELERLANRSSLNLTHNRTKRSTDGNNATHLSNMESVHNLVYAQLQFTYDTLRGYINRALAQIAEAWCVDQRRTLEVFKELSKINPSAILSAIYNKPIAARFMGDVLGLASCVTINQTSVKVLRDMNVKESPGRCYSRPVVIFNFANSSYVQYGQLGEDNEILLGNHRTEECQLPSLKIFIAGNSAYEYVDYLFKRMIDLSSISTVDSMIALDIDPLENTDFRVLELYSQKELRSSNVFDLEEIMREFNSYKQRVKYVEDKVVDPLPPYLKGLDDLMSGLGAAGKAVGVAIGAVGGAVASVVEGVATFLKNPFGAFTIILVAIAVVIITYLIYTRQRRLCTQPLQNLFPYLVSADGTTVTSGSTKDTSLQAPPSYEESVYNSGRKGPGPPSSDASTAAPPYTNEQAYQMLLALARLDAEQRAQQNGTDSLDGQTGTQDKGQKPNLLDRLRHRKNGYRHLKDSDEEENV
Protein: CGG triplet repeat binding protein 1 (C9JUJ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MERFVVTAPPARNRSKTALYVTPLDRVTEFGGELHEDGGKLFCTSCNVVLNHVRKSAISDHLKSKTHTKRKAEFEEQNVRKKQRPLTASLQCNSTAQTEKVSVIQD
Protein: Guanine nucleotide-binding protein subunit gamma 1 (Ggamma-subunit 1) (Heterotrimeric G protein gamma-subunit 1) (Q75WU1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15078334}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
Sequence:
MQAGGGGDAGDTRGRHRIQAELKKLEQEARFLEEELEELDKTDKVSAALQELMVTAESKADPLLPVTTGPACQSWDRWFEGPQDLRRCKCWFL
Protein: Growth hormone (H6ULX0)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MAPGSWFSPLLIAVVTLGLPQEAAATFPAMPLSNLFANAVLRAQHLHLLAAETYKEFERTYIPEDQWYTNKNSQAAFCYSETIPAPTGKDDAQQKSDMEVVRFSLVFIQSWLTPVQYLSKVFTNKLVFGTSDRVFEKLKDLEEGIQALMRELEDRSPRGPQLLRPTYDKFDIHLRHGDALLNNYGLLSCFKKDLHKVETYLKVMKCRRFGESNCTI
Protein: Isochorismate synthase 2, chloroplastic (AtIcs2) (EC 5.4.4.2) (Isochorismate mutase 2) (menF-like protein 2) (Q9M9V6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Isochorismate synthase involved in the synthesis of salicylic acid (SA) required for both local and systemic acquired resistance (LAR and SAR) while SA synthesized through the phenylalanine ammonium lyase (PAL) pathway seems to potentiate plant cell death. Also involved in phylloquinone (vitamin K1) synthesis. Has no isochorismate pyruvate lyase (IPL) activity.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18451262}.
Interaction partners:
- Anthranilate synthase beta subunit 1, chloroplastic
- anthranilate synthase
- anthranilate synthase
- Anthranilate synthase beta subunit 2, chloroplastic
- Indole-3-glycerol phosphate synthase, chloroplastic
- indole-3-glycerol-phosphate synthase
- Anthranilate phosphoribosyltransferase, chloroplastic
- Chorismate synthase, chloroplastic
- Protein PHYLLO
- Anthranilate phosphoribosyltransferase
Sequence:
MASLQCSFHFLGTNPKKYNPSSIFQSYSRTSFTKLSSRVSRQRFLRCTLSMNGCEADHKAPLGTVETRTLSTVPSPAAATERLITAVSDLKSQPPPFSSGIVRLQVPIEQKIGAIDWLHAQNEILPRSFFSRRSDSGRPDLLQDFSSDNGSSDHNPVSVAGIGSAVFFRDLDPFSHDDWRSIRRFLSSKSPLIRAYGGLRFDPTGKIAVEWEHFGSFYFTVPQVEFDEFGGSSMLAATVAWDNELSWTLENAIEALQETMLQVSSVIMRLRRESLGVIVVSKNHVPSEGAYYPAVNNALEIIKDKHSPLSKVVLARSSRIITDTDIDPIAWLARLQCEGQDAYQFCLQPPGAPAFIGNTPERLFHRKHLGVCSEALAATRPRGDSKVREMEIERDLLTSPKDDLEFSIVRENIREKLKTICDRVVVKPHKSVRKLARVQHLYSQLAGQLKREDDEFNILTALHPTPAVCGCPVEEARLLIKQIESFDRGMYAGPIGFFGGGESEFSVGIRSALVEKGLGALIYAGTGIVSGSNPSSEWNELELKISQFTKSLEHESALQPIN
Protein: Nickel/cobalt efflux system RcnA (P76425)
Organism: Escherichia coli (strain K12)
Function: Efflux system for nickel and cobalt.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15805538}; Multi-pass membrane protein {ECO:0000269|PubMed:15805538}.
Interaction partners:
- Transcriptional repressor RcnR
- Nickel/cobalt homeostasis protein RcnB
- Nickel-responsive regulator
- Zinc/cadmium/lead-transporting P-type ATPase
- Nickel-binding periplasmic protein
Sequence:
MTEFTTLLQQGNAWFFIPSAILLGALHGLEPGHSKTMMAAFIIAIKGTIKQAVMLGLAATISHTAVVWLIAFGGMVISKRFTAQSAEPWLQLISAVIIISTAFWMFWRTWRGERNWLENMHGHDYEHHHHDHEHHHDHGHHHHHEHGEYQDAHARAHANDIKRRFDGREVTNWQILLFGLTGGLIPCPAAITVLLICIQLKALTLGATLVVSFSIGLALTLVTVGVGAAISVQQVAKRWSGFNTLAKRAPYFSSLLIGLVGVYMGVHGFMGIMR
Protein: BMP and activin membrane-bound inhibitor homolog (Non-metastatic gene A protein) (Putative transmembrane protein NMA) (Q13145)
Organism: Homo sapiens (Human)
Function: Negatively regulates TGF-beta signaling.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- TGF-beta receptor type-1
- Mothers against decapentaplegic homolog 7
- Activin receptor type-1
- Frizzled-5
- Low-density lipoprotein receptor-related protein 6
- Bone morphogenetic protein receptor type-1A
- Bone morphogenetic protein receptor type-1B
- Segment polarity protein dishevelled homolog DVL-2
- Frizzled-4
- Frizzled-9
Sequence:
MDRHSSYIFIWLQLELCAMAVLLTKGEIRCYCDAAHCVATGYMCKSELSACFSRLLDPQNSNSPLTHGCLDSLASTTDICQAKQARNHSGTTIPTLECCHEDMCNYRGLHDVLSPPRGEASGQGNRYQHDGSRNLITKVQELTSSKELWFRAAVIAVPIAGGLILVLLIMLALRMLRSENKRLQDQRQQMLSRLHYSFHGHHSKKGQVAKLDLECMVPVSGHENCCLTCDKMRQADLSNDKILSLVHWGMYSGHGKLEFV
Protein: Nicotinate phosphoribosyltransferase (NAPRTase) (EC 6.3.4.21) (P39683)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Essential for growth under anaerobic conditions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamidase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide riboside kinase
- Purine nucleoside phosphorylase
- Glutamine-dependent NAD
- Uridine nucleosidase
- NAD-capped RNA hydrolase NPY1
- IMP-specific 5'-nucleotidase 1
Sequence:
MSEPVIKSLLDTDMYKITMHAAVFTNFPDVTVTYKYTNRSSQLTFNKEAINWLKEQFSYLGNLRFTEEEIEYLKQEIPYLPSAYIKYISSSNYKLHPEEQISFTSEEIEGKPTHYKLKILVSGSWKDTILYEIPLLSLISEAYFKFVDIDWDYENQLEQAEKKAETLFDNGIRFSEFGTRRRRSLKAQDLIMQGIMKAVNGNPDRNKSLLLGTSNILFAKKYGVKPIGTVAHEWVMGVASISEDYLHANKNAMDCWINTFGAKNAGLALTDTFGTDDFLKSFRPPYSDAYVGVRQDSGDPVEYTKKISHHYHDVLKLPKFSKIICYSDSLNVEKAITYSHAAKENGMLATFGIGTNFTNDFRKKSEPQVKSEPLNIVIKLLEVNGNHAIKISDNLGKNMGDPATVKRVKEELGYTERSWSGDNEAHRWT
Protein: UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8 (BGnT-8) (Beta-1,3-Gn-T8) (Beta-1,3-N-acetylglucosaminyltransferase 8) (Beta3Gn-T8) (EC 2.4.1.-) (Q7Z7M8)
Organism: Homo sapiens (Human)
Function: Beta-1,3-N-acetylglucosaminyltransferase that plays a role in the elongation of specific branch structures of multiantennary N-glycans. Has strong activity towards tetraantennary N-glycans and 2,6 triantennary glycans.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NY97}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NY97}.
Interaction partners:
Sequence:
MRCPKCLLCLSALLTLLGLKVYIEWTSESRLSKAYPSPRGTPPSPTPANPEPTLPANLSTRLGQTIPLPFAYWNQQQWRLGSLPSGDSTETGGCQAWGAAAATEIPDFASYPKDLRRFLLSAACRSFPQWLPGGGGSQVSSCSDTDVPYLLLAVKSEPGRFAERQAVRETWGSPAPGIRLLFLLGSPVGEAGPDLDSLVAWESRRYSDLLLWDFLDVPFNQTLKDLLLLAWLGRHCPTVSFVLRAQDDAFVHTPALLAHLRALPPASARSLYLGEVFTQAMPLRKPGGPFYVPESFFEGGYPAYASGGGYVIAGRLAPWLLRAAARVAPFPFEDVYTGLCIRALGLVPQAHPGFLTAWPADRTADHCAFRNLLLVRPLGPQASIRLWKQLQDPRLQC
Protein: HSPB1 associated protein 1 (EC 1.14.11.-) (Q9VB06)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- 2-oxoglutarate and iron-dependent oxygenase JMJD4 homolog
- Bifunctional peptidase and
- Lysine-specific demethylase 3
- Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66
Sequence:
MELSSKLRDLILNTHVPLVLEQFPLKWECFEGSLHDWCKRFDKEATCLPAFELMALADSSTPQWERKRTKSSQLLNMQQFLRKYGVLDGDSTHWAAYQYKKADEVPLSCRSGIGFSSFGFPDIGNDYRFWLGSEQANTPCHYDTFGVNIVVQVHGCKSWLLFPPETPLQSTRIPYEETSVYCLENFYAPDPAKISSYEHLGRQAYHCNLQPGNVLIVPRHWWHYVEAKSTSLSVNYWVPLKVDMDLILDEFLVMHIVESFVRGESNQVKQYLLNPNQLDNVSTKPSDLFAQFEQAVQNLESGKSTRQLYDTDYISQADWKTLLNSINLSVRPLEVMPHEEYKLLLNANSKRFRVAANPPETTPISSNCELLVSSMCAPRVIAEMKREFFRRLGKSNSL
Protein: Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (SMAD family member 5) (SMAD 5) (Smad5) (Q56I99)
Organism: Gallus gallus (Chicken)
Function: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}.
Interaction partners:
- receptor protein serine/threonine kinase
- Bone morphogenetic protein receptor type-1B
- Activin receptor type-1
- Mothers against decapentaplegic homolog.
- E3 ubiquitin-protein ligase.
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog 6
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog
- Mitogen-activated protein kinase.
Sequence:
MTSMASLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSSPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDICEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEFNPQHSLLVQFRNLSHNEPHMPHNATFPDSFQQPNSTPFSISPNSPYPPSPASSTYPSSPASSGPSSPFQLPADTPPPAYMPPDDQMGQDNSQSMDTSNTMIPQIMPNISTRDVQPVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPLNPISSVS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q4GYR0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAIAPALRDMLERNTIPRRQLLGRRYHVVTDIGKGMFSEAFLVEDKQAGGALAVVKSSRIAQGNAEGMNREQQLRLAISEARIMAMFNDDGVVRLLDFWCEDGIDSICFLMEYCAGGDLEAYLRLRYPLAEGLLLVFFVQCLLAVAHIHTKGVIHRDLKPANILVAEGDSGNTVPTLKLTDFGLSAMNNAGTALEELSLVGTPLYMSPEVIQHGACVFGSDVWSLGVVFYRLITNEQPFNALNQRALHFSIVNTQPPHPCSVAKHYSRELGDLVMVMLEKDIAKRPTARYLIASPLFERVLQRSPWRSRPLRGATCLFVCRTDRTVNILAEPHFSAPIVATLGFGEHVFVSNRLCVRTVLKQCSVTGAVTRAFTWLPPQASNGGNGRSDGGGGSNPHALNPFECSHRPVARPPRTMQVTGEGILLWYRVVGPREGYCAPSECGRNLLWHVHNYTPCGPLPTHPAPVTTNLPRPVSPGSPDKKQTWTIGQIISSLFGAHG
Protein: Bas1p (Q5A683)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Grf10p
Sequence:
MSSPSNEASDTSNSSVRKRVVHIDPLEITQSLGFQTFRKGARKPWTKEEDSKLSSLVATEYPKPIDVEKVNWDSIAETLFPDGFRKGKECRKRWCNSLNPTLRRGKWSKEEDEKLVRAFEKYGASWLKVSQEIEGRTDDQCAKRYMEVLDPSTKNRLKPWSMEEDLRLIQQIKIHGTKWRTISNGFEGRPSLTCRNRWRKLVTDVVRGKADPLIKSQVENVTQKNMDDESNEDNILEVLSKKQQELTESNKETGPKNSKRPKKLKRDPDLSSNTPRPTSVNTPANEQSRTEVEWRYTLTPDGNKQARVGEDGYFSRNNIFGEENGGVIKNQQMVQQLVSYAKKRHLNITVHQHIHHHYASNTQQDTNSRTQPNRFNVEPEDQSSRFQHFNYLPPLIEVPKLNSSQSSPNNSSYEGASGTTPTTTQFHHHHHHHHHHHNNNEKDQRTKPASTNGSVIRSTTPAELDGTRESDLIKLLNNTDELNRRETTPISNPLTPLAQTVEYVEAEENQKLKRRKLGPTVESNADMVSKAQHLNNDKNHDIPSEDEEELDFWETMRNLTELPNNTLNNTTTKPTVTSSKNILSHDTTYHNSTTSSNNSKILTSTQFSQKPVSQHHPLHYYNSNTRENTPKPVLIQSQARKETGNAQGSNNNEGQEEGLDEEDKLLAREVAEVGVDQETLNSYGLFYNVYTREGSTFPELQPQQSSQQQQQQQQQQQQKYSAYDQWGGGFGMIPFNPS
Protein: Vesicular glutamate transporter 3 (VGluT3) (Solute carrier family 17 member 8) (Q8NDX2)
Organism: Homo sapiens (Human)
Function: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter that mediates the uptake of L-glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification (By similarity). At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation (Probable). The symporter activity is electrogenic. Moreover, operates synergistically with SLC18A3/VACHT under a constant H(+) gradient, thereby allowing striatal vesicular acetylcholine uptake (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q7TSF2}. Cell membrane {ECO:0000305|PubMed:33440152}; Multi-pass membrane protein {ECO:0000305}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q7TSF2}.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- Vesicular acetylcholine transporter
- Synaptic vesicular amine transporter
- Otoferlin
- Chromaffin granule amine transporter
- Vesicular glutamate transporter 2
- Vesicular glutamate transporter 1
- Synaptophysin
- Synapsin-1
- Vesicle-associated membrane protein 2
Sequence:
MPFKAFDTFKEKILKPGKEGVKNAVGDSLGILQRKIDGTTEEEDNIELNEEGRPVQTSRPSPPLCDCHCCGLPKRYIIAIMSGLGFCISFGIRCNLGVAIVEMVNNSTVYVDGKPEIQTAQFNWDPETVGLIHGSFFWGYIMTQIPGGFISNKFAANRVFGAAIFLTSTLNMFIPSAARVHYGCVMCVRILQGLVEGVTYPACHGMWSKWAPPLERSRLATTSFCGSYAGAVVAMPLAGVLVQYIGWSSVFYIYGMFGIIWYMFWLLQAYECPAAHPTISNEEKTYIETSIGEGANVVSLSKFSTPWKRFFTSLPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFAISKVGLLSAVPHMVMTIVVPIGGQLADYLRSRQILTTTAVRKIMNCGGFGMEATLLLVVGFSHTKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPLIVGAMTRHKTREEWQNVFLIAALVHYSGVIFYGVFASGEKQEWADPENLSEEKCGIIDQDELAEEIELNHESFASPKKKMSYGATSQNCEVQKKEWKGQRGATLDEEELTSYQNEERNFSTIS
Protein: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (BPG-independent PGAM) (Phosphoglyceromutase) (iPGM) (EC 5.4.2.12) (Q81X77)
Organism: Bacillus anthracis
Function: Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Interaction partners:
- Enolase
- Phosphoglycerate kinase
- Triosephosphate isomerase
- MBL fold metallo-hydrolase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- D-3-phosphoglycerate dehydrogenase
- NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
- Histidine phosphatase family protein
- Histidine phosphatase family protein
Sequence:
MRKPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRVNVAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQSYIDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGPTYKSAEECVEDSYANGIYDEFVLPSVIVNEDNTPVATINDDDAVIFYNFRPDRAIQIARVFTNGDFREFDRGEKVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEVVAQAGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFANCDMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSEGEPMTAHTTNPVPFIVTKNDVELREDGILGDIAPTMLTLLGVEQPKEMTGKTIIK
Protein: Progesterone receptor (C9V3N7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDTVNTSPADSTGTVTGMSHLMEKYTDLGFGHGRVSLRNFGDAGTLRGSAPASSSDALDHLSALDLPLGTKPYTEHIDDFLKAETGQWNAKTDCPESSYIKDDKELNLIMEPPNPDFDITVLESCYDSTERKQQCEFIEESSALISSQAIQQVVVDSSSNFQLDMNQTTLVLPPPRTVSASLDRGLLNFDVPSATHMMSKADISKWMSAADSPFWYQSANEEHAGYTPDCLIPRSQTAYTAFSGVPSQRQCVICGDEASGCHYGVLTCGSCKVFFKTAVEGHHNYLCAGRNDCIVDKIRRKNCPACRLRKCYQAGMMLGGRKMKRFAGLKVMGLSPSLMFQSPLSLLTDGQTLSSLPCMSAMRELQLSPQMISILENIEPQVVYSGYDNTQPEVPHLLLNSLNRLCERQLLWIVRWSKSLPGFRNLHINDQMTLIQYSWMGLMLFSLGWRTFQNVTPDYLYFAPDLVLSNDQLRRSPIYDLCLAMQFVPQEFANLQVTKEEFLCMKALMLLNTVPLEGLKSQTQFDEMRQNYICELSKAIQLKEKGVVASSQRFYHLTKLMDNMHEIVKKVNLYCLTTFIQADAMKVEFPEMMTEVIASQLPKVLAGMVKPLMFHHK
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (E5KP27)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPLVSRLSRLWAIMRKPRAAVGSGHRKQAASQEGRQKHAKNNSQAKPSACDGLARQPEEVVLQASVSSYHLFRDVAEVTAFRGSLLSWYDQEKRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLLASGSLSGSPDVEECAPNTGQCHLCLPPSEPWDQTLGVVNFPRKASRKPPREESSATCVLEQPGALGAQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKALLQELQRWAGPLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFRVYQGQQPGTCMGSKRSQVSSPCSRKKPRMGQQVLDNFFRSHISTDAHSLNSAAQ
Protein: N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase (EC 3.1.4.45) (Mannose 6-phosphate-uncovering enzyme) (Phosphodiester alpha-GlcNAcase) (Q8BJ48)
Organism: Mus musculus (Mouse)
Function: Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Cis/medial Golgi.
Interaction partners:
- N-acetylglucosamine-1-phosphotransferase subunit gamma
- N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
- AP-4 complex subunit epsilon-1
Sequence:
MAAPRGPGLFLIPALLGLLGVAWCSLSFGVSRDDDLLLPYPLARRRPSRDCARVRSGSPEQESWPPPPTNPGASHHAAVRTFVSHFEGRAVAGHLTRVADPLRTFSVLEPGGAGGCAQKRRATVEDTAVPAGCRIAQNGGFFRMSTGECLGNVVSDGRLVSSSGGLQNAQFGIRRDGTIVTGYLSEEEVLDPVNPFVQLLSGVVWLIRNGNIYINESQAIECDETQETGSFSKFVNVMSARTAVGHDREGQLILFHADGQTEQRGLNLWEMAEFLRQQDVVNAINLDGGGSATFVLNGTLASYPSDHCQDNMWRCPRQVSTVVCVHEPRCQPPDCSGHGTCVDGHCECTSHFWRGEACSELDCGPSNCSQHGLCTETGCHCDAGWTGSNCSEECPLGWYGPGCQRPCQCEHQCSCDPQTGNCSISQVRQCLQPTEATPRAGELASFTRTTWLALTLTLIFLLLISTGVNVSLFLGSRAERNRHLDGDYVYHPLQEVNGEALTAEKEHMEETSNPFKD
Protein: Jasmonate-induced oxygenase 2 (EC 1.14.11.-) (2-oxoglutarate-dependent dioxygenase JOX2) (Jasmonic acid oxidase 2) (Q9FFF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 2-oxoglutarate-dependent dioxygenase involved in the oxidation of jasmonate (JA), a stress-induced phytohormone synthesized in response to attack by pathogens and herbivores, which triggers the activation of defense responses via the JA-mediated signaling pathway. Converts JA to 12-hydroxyjasmonate (12OH-JA), an inactive form of JA. Is specific to free JA, and cannot oxidize the bioactive form jasmonoyl-L-isoleucine (JA-Ile) or other JA-amino acid conjugates. Prevents over-accumulation of JA and indirectly its bioactive form JA-Ile under stress response. Acts as negative regulator of JA-mediated defense signaling, by contributing to 12OH-JA accumulation, which represses JA defense responses upon infection by the fungal pathogen Botrytis cinerea. Acts as negative regulator of JA-mediated defense responses upon infestation by the herbivorous caterpillar Mamestra brassicae. May be involved in the catabolism of cytotoxic polycyclic aromatic hydrocarbons (PAHs).
Interaction partners:
- 2-nitropropane dioxygenase-like protein
Sequence:
MNKNKIDVKIETKKGSMDEWPEPIVRVQSLAESNLSSLPDRYIKPASLRPTTTEDAPTATNIPIIDLEGLFSEEGLSDDVIMARISEACRGWGFFQVVNHGVKPELMDAARENWREFFHMPVNAKETYSNSPRTYEGYGSRLGVEKGASLDWSDYYFLHLLPHHLKDFNKWPSFPPTIREVIDEYGEELVKLSGRIMRVLSTNLGLKEDKFQEAFGGENIGACLRVNYYPKCPRPELALGLSPHSDPGGMTILLPDDQVFGLQVRKDDTWITVKPHPHAFIVNIGDQIQILSNSTYKSVEHRVIVNSDKERVSLAFFYNPKSDIPIQPLQELVSTHNPPLYPPMTFDQYRLFIRTQGPQGKSHVESHISPR
Protein: Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7) (F1QUS9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- UV-stimulated scaffold protein A
- E3 ubiquitin-protein ligase Mdm2
- Cellular tumor antigen p53
- Death domain-associated protein 6
- DNA
- GMP synthase
- Ubiquitin-ribosomal protein eS31 fusion protein
- E3 ubiquitin-protein ligase UHRF1
- Forkhead box O3b.
- Forkhead box protein O1-B
Sequence:
MNHHHTQQQQQKAGEQQLSEPEDMEMEAGDPDDPPRIPQNPVINGNVAMADGHNNTEEDMEDDTSWRSEATFPFVVERFSRLSESVLSPPCFVRNLPWKIMVMPRFYPDRPHQKSVGFFLQCNAESDSTSWSCHAQAMLKIINYKDDEKSFSRRISHLFFHKENDWGFSNFMSWSDVTDPERGFVEDDKVTFEVYVQADAPHGVAWDSKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRRAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKHVDYRSERIEDYYDIQLSIKGKKNIFESFKDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTFPPILHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKPDVKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKVSVTAPIWCKFDDDVVSRCTKEEATEHNYGGHDDDLSVRHCTNAYMLVYIRESKLSEVLQPVTDMDIPQQLVERLQEEKRVEAQKRKERQEAHLYMQVQMVTEDQFCGHQGNDMYDEEKVKYTVFKVLKSSTLAEFVQNLSQTMGFPQDQMRLWPMQARSNGTKRPAMLDYEADCNKSMIDLSDNENPWTIFLETVDPEMAASGATLPKFDKDHDVMLFLKMYDPKTRSLNYCGHIYTPISCKIRDLLPVMCERAGFQQGTSLILYEEVKPNLTERIQDYDVSLDKALDELMDGDIIVFQKDDPENDTSELPTAKDYFRDLYHRVDVIFCDKTIHNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRHNYEGTLRDLLQFFKPRQPKKLYYQQLKMKITDFENRRSFKAIWLNSMFREEEITLYPDKHGCVRDLLEECKKAVELSDKGSEKLRLLEIVSYKIIGVHQEDELLECLSPAASRTFRIEEIPLDQVDLDKENEMLIPVAHFHKEVFGTFGIPFLLKIRQGEPFREVMKRIQSMLDIQEKEFEKFKFAIVMMGRHQYINEEDYEVNLKDFEPQPGNMSHPRPWLGLDHFNKAPKRGRYTYLEKAIKIHN
Protein: Patatin-like protein 3 (AtPLP3) (EC 3.1.1.-) (Patatin-related phospholipase A IIbeta) (pPLAIIb) (Phospholipase A IVC) (AtPLAIVC) (O23181)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12226489}.
Interaction partners:
- Thioredoxin domain-containing protein PLP3A
- Thioredoxin domain-containing protein 9 homolog
- UPF0540 protein At1g62060
- Thioredoxin domain-containing protein PLP3B
- Hyperosmolality-gated Ca2+ permeable channel 1.7
- Pentatricopeptide repeat-containing protein At3g53170
- Geranylgeranyl transferase type-1 subunit beta
- Glutamate receptor 2.3
- Patatin
- Subtilisin-like protease SBT3.7
Sequence:
MDTERGSISSSEISRTAHLQDRTVACLPPSYGQLVTILSIDGGGIRGIIPGTILAYLESQLQELDGEEARLVDYFDVISGTSTGGLIVAMLTAQDQSGGHSRNSNRPLFEAKEIVPFYLKHSPKIFPQPRGIFCGWGETIVRLVGGPKFNGKYLHDLVEGFLGDTKLTQSLTNVVIPCFDIKKLQPVIFSSYQAVNNQAMNAKLSDICISTSAAPTFFPAHRFTNEDSEGIKHEFNLIDGGIAANNPTLCAIAEVTKQIIKKNPVMGDISPLDFTRFLVISIGTGSIRNQEKYNAKMASKWGLMCWVFESGSTPILDCYSEAIHDMVDYQSSVVFQALRSEKNYLRIDDDSLKGDLGSVDISTEKNMEGLVEVGEALLKKRVSRVNLESGHYQPISENVTNEEALKRFAKVLSEERKLRESRSPKLKI