wanglab/gogpt-training-data huggingface dataset:
Protein: SH3 domain containing 19 (A0A0U1RQE4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEGRRREDEEEELRERRELGGQRRARGRALSGHSAADRNERNKPEHRSSSQGPLSSIRAVIKRSSRTSIQSELHRDRRRPEITIVAAEPLRPASWFPGTPPPGLGFPTSSAAGSWRPNELVPAELPPSYEQVIKEINQVQVNTTNNNNAAATPRHTITSATQTDFSEEIDNDLPQTLQAPLKPLQPFSAVSSGNLPTNVAPLIVFDISEEPNCPENPSATRCPVPKPRSKSNLRPIPRDSHIKEQSQQKISPAAVGEESSPGRPQSLLDNASTSDSQAVMNIMNTEQSQNSIVSRIKVFEGQTNIETSGLPKKPEITPRSLPPKPTVSSGKPSVAPKPAANRASGEWDSGTENRLKVTSKEGLTPYPPLQEAGSIPVTKPELPKKPNPGLIRSVNPEIPGRGPLAESSDSGKKVPTPAPRPLLLKKSVSSENPTYPSAPLKPVTVPPRLAGASQAKAYKSLGEGPPANPPVPVLQSKPLVDIDLISFDDDVLPTPSGNLAEESVGSEMVLDPFQLPAKTEPIKERAVQPAPTRKPTVIRIPAKPGKCLHEDPQSPPPLPAEKPIGNTFSTVSGKLSNVERTRNLESNHPGQTGGFVRVPPRLPPRPVNGKTIPTQQPPTKVPPERPPPPKLSATRRSNKKLPFNRSSSDMDLQKKQSNLATGLSKAKSQVFKNQDPVLPPRPKPGHPLYSKYMRGDVLVMLKQTENNYLECQKGEDTGRVHLSQMKIITPLDEHLRSRPNDPSHAQKPVDSGAPHAVVLHDFPAEQVDDLNLTSGEIVYLLEKIDTDWYRGNCRNQIGIFPANYVKVIIDIPEGGNGKRECVSSHCVKGSRCVARFEYIGEQKDELSFSEGEIIILKEYVNEEWARGEVRGRTGIFPLNFVEPVEDYPTSGANVLSTKVPLKTKKEDSGSNSQVNSLPAEWCEALHSFTAETSDDLSFKRGDRIQILERLDSDWCRGRLQDREGIFPAVFVRPCPAEAKSMLAIVPKGRKAKALYDFRGENEDELSFKAGDIITELESVDDDWMSGELMGKSGIFPKNYIQFLQIS
Protein: Gustatory receptor for bitter taste 93a (Q9VD76)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gustatory receptor required for response to the bitter in taste neurons. Gr93a cells respond to bitter compounds such as caffeine. Flies avoid bitter substances, suggesting that Gr93a neuron activity is sufficient to mediate avoidance behavior.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Gustatory and pheromone receptor 33a
- Gustatory receptor for bitter taste 66a
- Gustatory and pheromone receptor 32a
- Gustatory receptor 8a
- Gustatory and pheromone receptor 39a, isoform C
- Putative gustatory receptor 89a
- Gustatory receptor 5a for trehalose
- Gustatory receptor
- Gustatory receptor for sugar taste 64a
- Gustatory and odorant receptor 21a
Sequence:
MFSSSSAMTGKRAESWSRLLLLWLYRCARGLLVLSSSLDRDKLQLKATKQGSRNRFLHILWRCIVVMIYAGLWPMLTSAVIGKRLESYADVLALAQSMSVSILAVISFVIQARGENQFREVLNRYLALYQRICLTTRLRHLFPTKFVVFFLLKLFFTLCGCFHEIIPLFENSHFDDISQMVGTGFGIYMWLGTLCVLDACFLGFLVSGILYEHMANNIIAMLKRMEPIESQDERYRMTKYRRMQLLCDFADELDECAAIYSELYHVTNSFRRILQWQILFYIYLNFINICLMLYQYILHFLNDDEVVFVSIVMAFVKLANLVLLMMCADYTVRQSEVPKKLPLDIVCSDMDERWDKSVETFLGQLQTQRLEIKVLGFFHLNNEFILLILSAIISYLFILIQFGITGGFEASEDIKNRFD
Protein: Poly [ADP-ribose] polymerase tankyrase (dTNKS) (EC 2.4.2.30) (Poly [ADP-ribose] polymerase) (Protein poly-ADP-ribosyltransferase tankyrase) (EC 2.4.2.-) (Q9VBP3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Stimulates proteasome activity, probably by ADP-ribosylation of PI31. Modulates 26S proteasome assembly.
Interaction partners:
- Axin
- E3 ubiquitin-protein ligase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Proteasome inhibitor PI31 subunit
Sequence:
MANSSRSRAILSVNLDAVMANDPLRELFEACKTGEIAKVKKLITPQTVNARDTAGRKSTPLHFAAGYGRREVVEFLLNSGASIQACDEGGLHPLHNCCSFGHAEVVRLLLKAGASPNTTDNWNYTPLHEAASKGKVDVCLALLQHGANHTIRNSEQKTPLELADEATRPVLTGEYRKDELLEAARSGAEDRLLALLTPLNVNCHASDGRRSTPLHLAAGYNRIGIVEILLANGADVHAKDKGGLVPLHNACSYGHFDVTKLLIQAGANVNANDLWAFTPLHEAASKSRVEVCSLLLSRGADPTLLNCHSKSAIDAAPTRELRERIAFEYKGHCLLDACRKCDVSRAKKLVCAEIVNFVHPYTGDTPLHLAVVSPDGKRKQLMELLTRKGSLLNEKNKAFLTPLHLAAELLHYDAMEVLLKQGAKVNALDSLGQTPLHRCARDEQAVRLLLSYAADTNIVSLEGLTAAQLASDSVLKLLKNPPDSETHLLEAAKAGDLDTVRRIVLNNPISVNCRDLDGRHSTPLHFAAGFNRVPVVQFLLEHGAEVYAADKGGLVPLHNACSYGHYEVTELLVKHGANVNVSDLWKFTPLHEAAAKGKYDICKLLLKHGADPMKKNRDGATPADLVKESDHDVAELLRGPSALLDAAKKGNLARVQRLVTPESINCRDAQGRNSTPLHLAAGYNNFECAEYLLENGADVNAQDKGGLIPLHNASSYGHLDIAALLIKHKTVVNATDKWGFTPLHEAAQKGRTQLCSLLLAHGADAYMKNQEGQTPIELATADDVKCLLQDAMATSLSQQALSASTQSLTSSSPAPDATAAAAPGTSSSSSSAILSPTTETVLLPTGASMILSVPVPLPLSSSTRISPAQGAEANGAEGSSSDDLLPDADTITNVSGFLSSQQLHHLIELFEREQITLDILAEMGHDDLKQVGVSAYGFRHKILKGIAQLRSTTGIGNNVNLCTLLVDLLPDDKEFVAVEEEMQATIREHRDNGQAGGYFTRYNIIRVQKVQNRKLWERYAHRRQEIAEENFLQSNERMLFHGSPFINAIVQRGFDERHAYIGGMFGAGIYFAEHSSKSNQYVYGIGGGIGCPSHKDKSCYVCPRQLLLCRVALGKSFLQYSAMKMAHAPPGHHSVVGRPSAGGLHFAEYVVYRGEQSYPEYLITYQIVKPDDSSSGTEDTR
Protein: Flavonol-3-O-rhamnosyltransferase (EC 2.4.1.-) (UDP-glycosyltransferase 78D1) (UDP-rhamnose:flavonol 3-O-glucoside rhamnosyltransferase) (Q9S9P6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Flavonol 3-O-rhamnosyltransferase that catalyzes the transfer of rhamnose from UDP-rhamnose to the 3-OH position of kaempferol and quercetin. Possesses low quercetin 3-O-glucosyltransferase activity in vitro.
Interaction partners:
- Flavonoid 3'-monooxygenase
- UDP-glycosyltransferase 73C6
- Flavonol synthase/flavanone 3-hydroxylase
- Flavonol 3-O-glucosyltransferase
- Flavonol synthase 3
- Probable flavonol synthase 4
- Probable flavonol synthase 6
- Probable flavonol synthase 5
- Probable long-chain-alcohol O-fatty-acyltransferase 3
- Chalcone--flavanone isomerase 1
Sequence:
MTKFSEPIRDSHVAVLAFFPVGAHAGPLLAVTRRLAAASPSTIFSFFNTARSNASLFSSDHPENIKVHDVSDGVPEGTMLGNPLEMVELFLEAAPRIFRSEIAAAEIEVGKKVTCMLTDAFFWFAADIAAELNATWVAFWAGGANSLCAHLYTDLIRETIGLKDVSMEETLGFIPGMENYRVKDIPEEVVFEDLDSVFPKALYQMSLALPRASAVFISSFEELEPTLNYNLRSKLKRFLNIAPLTLLSSTSEKEMRDPHGCFAWMGKRSAASVAYISFGTVMEPPPEELVAIAQGLESSKVPFVWSLKEKNMVHLPKGFLDRTREQGIVVPWAPQVELLKHEAMGVNVTHCGWNSVLESVSAGVPMIGRPILADNRLNGRAVEVVWKVGVMMDNGVFTKEGFEKCLNDVFVHDDGKTMKANAKKLKEKLQEDFSMKGSSLENFKILLDEIVKV
Protein: Transcription factor SOX-5 (F1M8W4)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor involved in chondrocytes differentiation and cartilage formation (By similarity). Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes, such as COL2A1 and AGC1 (By similarity). Required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on active enhancers and super-enhancers associated with cartilage-specific genes, and thereby potentiate SOX9's ability to transactivate. Not involved in precartilaginous condensation, the first step in chondrogenesis, during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX6, required to form and maintain a pool of highly proliferating chondroblasts between epiphyses and metaphyses, to form columnar chondroblasts, delay chondrocyte prehypertrophy but promote hypertrophy, and to delay terminal differentiation of chondrocytes on contact with ossification fronts (By similarity). Binds to the proximal promoter region of the myelin protein MPZ gene (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P35710}.
Interaction partners:
- Transcription factor SOX-6
- Transcription factor SOX-9
- DNA-binding protein SATB
- Catenin beta-1
- Zinc finger protein 312
- Aggrecan core protein
Sequence:
MLTDPDLPQEFERMSSKRPASPYGETDGEVAMVTSRQKVEEEESERLPAFHLPLHVSFPNKPHSEEFQPVSLLTQEACGPRTPAAQHSTMEVDGNKVMSSLAPYNSSTSPQKAEEGGRQSGESVSSAALGTPERRKGSLADVVDTLKQRKMEELIKNEPEDTPSIEKLLSKDWKDKLLAMGSGNFGEIKGTPESLAEKERQLMGMINQLTSLREQLLAAHDEQKKLAASQIEKQRQQMELAKQQQEQIARQQQQLLQQQHKINLLQQQIQVQGQLPPLMIPVFPPDQRTLAAAAQQGFLLPPGFSYKAGCSDPYPVQLIPTTMAAAAAATPGLGPLQLQQFYAAQLAAMQVSPGGKLLGLPQGNLGAAVSPTSIHTDKSTNSPPPKSKDEVAQPLNLSAKPKTSDGKSPASPTSPHMPALRINSGAGPLKASVPAALASPSARVSTIGYLNDHDAVTKAIQEARQMKEQLRREQQALDGKVAVVNSIGISNCRTEKEKTTLESLTQQLAVKQNEEGKFSHGMMDFNMSGDSDGSAGVSESRIYRESRGRGSNEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKAMTNLEKQPYYEEQARLSKQHLEKYPDYKYKPRPKRTCLVDGKKLRIGEYKAIMRNRRQEMRQYFNVGQQAQIPIATAGVVYPGAIAMAGMPSPHLPSEHSSVSSSPEPGMPVIQSTYGVKGEEPHIKEEIQAEDINGEIYEEYEEEEEDPDVDYGSDSENHIAGQAN
Protein: 3-oxo-glucose-6-phosphate:glutamate aminotransferase (EC 2.6.1.104) (3-dehydro-glucose-6-phosphate--glutamate transaminase) (Kanosamine 6-phosphate transaminase) (O07566)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the reversible pyridoxal phosphate-dependent transamination of 3-dehydro-alpha-D-glucose 6-phosphate to form alpha-D-kanosamine-6-phosphate. It can only use alpha-anomer and glutamate is the only amino donor.
Interaction partners:
- Kanosamine-6-phosphate phosphatase
- Glucose-6-phosphate 3-dehydrogenase
- Probable polysaccharide biosynthesis protein EpsC
- UDP-N-acetylbacillosamine N-acetyltransferase
- Spore coat polysaccharide biosynthesis protein SpsE
- dTDP-glucose 4,6-dehydratase
Sequence:
MQKQVKISGKSKENMSLLKHLKGDVQGKELVIEDSIVNERWKQVLKEKIDIEHDLFNYQKNREISKVPFLPVDRLITNDEVEDILNTLTEVLPTGKFTSGPYLEQFEKVLSTYLHKRYVIATSSGTDAIMIGLLALGLNPGDEVIMPANSFSATENAVLASGGVPIYVDINPQTFCIDPDKIEEAITPYTKFILPVHLYGKHSDMQHIRQIANRYKLKVIEDACQGIGLTDLGKYADITTLSFNPYKNFGVCGKAGAIATDNEELAKKCIQFSYHGFEVNVKNKKVINFGFNSKMDNLQAAIGLERMKYLSLNNFKRLFLADRYITQLAELQNKGYIELPELSEDHVWHLFPIKVRTEDRADIMTKLNEDFGVQTDVYYPILSHMQKTPLVQDKYAGLQLVHTEKAHSQVLHLPLYPSFTLEEQDRVMEGLFHVIKQEIGV
Protein: Monocarboxylate transporter 2 (MCT 2) (Solute carrier family 16 member 7) (O70451)
Organism: Mus musculus (Mouse)
Function: Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is functionally required and both subunits work cooperatively in transporting substrate (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O60669}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60669}. Cytoplasm {ECO:0000269|PubMed:21792931}. Basolateral cell membrane {ECO:0000250|UniProtKB:P53988}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60669}. Note=Requires the ancillary protein, EMB for plasma membrane localization (By similarity). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (PubMed:21792931). {ECO:0000250|UniProtKB:Q63344, ECO:0000269|PubMed:21792931}.
Interaction partners:
- Embigin
Sequence:
MPSEPSAPLPQPLPPDGGWGWVVVCASFISIGFSYAFPKAVTVFFKDIQEIFNTTSSQIAWISSIMLAVMYAGGPISSVLVNNYGSRPVVIVGGLLCCIGMILASYSNSVIELYLTVGFIGGLGLAFNLQPALTIIGKYFYRRRPLANGCAMAGSPVFLSTLAPFNQYLFNNYGWKGSFLILGGIFLHSCVAGCLMRPVGPSPNTKKSKSKVGSRHDSTLKKASKVSTAQKVNRFLDFSLFMHRGFLIYLSGNVILFLGIFAPIIFLAQYAKHIGVDDYNSAFLLSVMAFIDMFARPSVGLIANTSLIRPRIQYLFSSAIIFTGICHLLCPLATTYSALVVYVVFFGLGFGSISSLLFECLMDIVGATRFSSAVGLTTIVECCPVLFGPPLAGKLLDITGEYKYLYIASGTVVLVSGTYLLIGNAINYRLLDKERKREKAKKKKSASHASREMEALNRSKQDEVTVKASNAHNPPSDRDKESNI
Protein: Protein HEAT-STRESS-ASSOCIATED 32 (Heat-stress-associated 32-kDa protein) (Q8GWL1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transactivator required, together with HSP101, for long-term acquired thermotolerance (LAT) maintenance, probably by regulating heat-inducible genes expression, thus being a cellular component of thermomemory.
Interaction partners:
- Chaperone protein ClpB1
- Heat stress transcription factor A-2
- S-formylglutathione hydrolase
- Heat shock protein 21, chloroplastic
- 22.0 kDa heat shock protein
- 18.1 kDa class I heat shock protein
- Heat shock 70 kDa protein 8
- Heat shock protein 90-1
- Peptidyl-prolyl cis-trans isomerase FKBP62
- Heat shock 70 kDa protein 4
Sequence:
MAAYYRWKSFEENEDRPEKPRRYGVTEMRGPHYSVLSQNLLQEIFESMGQFVDGLKFSGGSNSLIPKSFIKQAIEMAHEHGVYVSTGDWAEHMLRSGPSAFKDYVEECKQLGFDTIELNANLLEVPEETLLRYVRLIKNGGLRAKPMFAVKFNKSDIPGRNRAFGSYVVPEPRSSEFVEDIDLLIRKAERCLEAGADTIMIDADDVCKYADSLRADIIAKVIGRLGIEKTMFEASDAKLVEWFIKRYGPNVNLYVDHSQIMDLECLRGRHLGKDHQSVLSSSYFLF
Protein: Co-chaperone protein p23-1 (Bnp23-1) (Q9FR62)
Organism: Brassica napus (Rape)
Function: Acts as a co-chaperone for HSP90.
Interaction partners:
Sequence:
MSRHPTVKWAQRSDWVYITVELPDAEDVKLKLEPEGKFFFSATSGASKTLYEVDLDLLDSVDVNESKASVSSRSVFYLVKKAESKWWNRLTKPEGKHPLYLKVDWDKWVDEDDEDKGGEGDMDFGDFDFNGLNMGDTDEIGEEVAEEDGDGEGETAAETKEKKIDGEKDEEGVNAKKD
Protein: Autophagy-related protein 101 (Q95XH2)
Organism: Caenorhabditis elegans
Interaction partners:
- Autophagy-related protein 13 homolog
- Serine/threonine-protein kinase unc-51
- Autophagy-related protein 11 C-terminal domain-containing protein
- DAF-15
- Target of rapamycin homolog
- Beclin homolog
- MRG domain-containing protein
- Autophagy-related protein 2
- Target of rapamycin complex subunit lst8
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MNIRQNELRLTVELRQVTDAVECIFHSLLLHRTLGRFQYNDEKTFSMGSIGIKEVSCEQIDMTYVRVNSTELAMCVDEDIRQFKCEVEEATCSGSIPRRTPTVGSPTDSAIPLLSAQIGLQFYTKSKKPNSVIGTAVTWFGGAAATATGATVADDGTSWEEWKLILDVFRVESIDELQKMRQRVADDIGEKVLDICEHINHNHYTPKMPTKTEIPEIFETKFSDCQPYLFKIRRQAVPQMEHKQSLAQVALSRWKDILAV
Protein: Protein KOKOPELLI (Q9FFP2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates positively reproductive function by facilitating male gametophyte formation and double fertilization.
Interaction partners:
- Probable E3 ubiquitin-protein ligase ARI14
- Probable E3 ubiquitin-protein ligase ARI13
- Probable E3 ubiquitin-protein ligase ARI15
- Protein HAPLESS 2
- Protein TRANSPARENT TESTA 16
- KIN17-like protein KLP
- Probable E3 ubiquitin-protein ligase ARI16
- Protein GAMETE EXPRESSED 2
- Agamous-like MADS-box protein AGL62
Sequence:
MEPNNVERNLQSLRRLYSLLVANARNEYIPEAYKLDDNTQFLLKRLLDFASHEHFVTQSNLLATQLRVFPKTVLHGAKPSNVADSSETTPPAMLSQINGSHITRVSKPLEAKGTLQRDLRVDQIRSNPSKDVLTEEVVDAIEQIDTQLSALSFVSSRVDSDERTRSVKSFVTPPTEECRQNSQASMPCLRSNYMTVSQKSVISGAEVTFPYNDQLVRVTSPPQPLPPRAVSGFKKPNQSNRASQKMPIMKPTLMDQETETFDDDSSETEADQTPSATGSESEDEEVSTSQEYSGETGSSSGSEWETQAENDTESKSESSYPPQNDDSVSEVSTSPPHTDRDTSREPGKQRRNVMGRFKRIKNKIGQIFHHHHHHHHHHHHHDKEKPSAWNKLQSKFHHKHQEKSKERKRPMSESKGLTTHKQQHQGGHFHALVEGLVRHRKHSKKQKHQLKSDAKKTEWWKLLKKRQGGGVKIPKRGRVKLGKKKHYLSKNV
Protein: Peroxisomal testis-specific protein 1 (Small testis-specific peroxisomal protein) (Q8K459)
Organism: Mus musculus (Mouse)
Subcellular location: Peroxisome {ECO:0000269|PubMed:18160785}.
Interaction partners:
Sequence:
MQLRHIGDSVNHRVIQEHLAQEVGDVLAPFVALVFVRGQVLLRFFWNNHLL
Protein: Paraflagellar rod component (Q57TU7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- EF-hand domain-containing protein
Sequence:
MTTMQRVDAMLGRFDRKSPRASYAQICEEMGINRQRHVSLLLSDAPRDWDKHRVIDCSKCVLGAKGCLAVLPLVLCSRSLRRVSFSGCHVTDEFVSELAEILQDHQSIRSIDVSNNPLVTVCSASPIIRMLRANKNVVRFCVEDTHIGTNVMNIIDDLCDKNQNEVANYYADDYFRMKYLFNYLDGDASGWVSMRSLVLNAPFPVLQEQLIERIAAKRPKKRSNGTISVNTFLELVYFNYKTDVEIARRMAETDVEYRNIILNWKHLLDAMDSPEGEPEGKKQNDDEEDEEEFAELEDPEEENEKVPLPGKLPIVPPADFHRLRIRSVELTPAEARGIIALAVKLQIDADARNEEEESTTEPRKEIKLTYQCLRRAYRTISQPQPLPRRFRFLKEHGEDYVPPMMRAGSRLISISKLSFLDSHSSNASFDANETMEESVLDGDENRTRWWALPPAMVRLISKFFNDRAAELPKRRQTTLAISPRTQRDLAMEKTTIPVPLFLSAEFTTDLETLKPRLLTDRFLQYGIPIEESTITLQEMVNCLNEYYLEASVDKRLSVKAIRMMTMPDADGAADSNKGSLDTGSVPKITLDKSQISKASTDTAAFAP
Protein: DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (O15922)
Organism: Leishmania major
Interaction partners:
- Endonuclease III homolog lyase)
- Flap endonuclease 1
- Proliferating cell nuclear antigen
- Tyrosyl-DNA phosphodiesterase 1
- Adenine DNA glycosylase
- DNA-
- Mevalonate kinase
- DNA ligase
- Uracil-DNA glycosylase
- Sm protein F
Sequence:
MASKRCRQCSGDSASSSTSSLSPSELPPSKKAAGGQRVTAEVEVAPITTDATSATVTAAGGAKKKATTGSPARRTSSAAKITNGDAGELIRTAEALAALNAKKSEKEIWSDVVPFVRRTTDSDFDPSRMYKFITWNVAGLRGLLKKNASALRAFMEAEKPDVLCLQETKLNVDEADANATLGVVDGYSFVDHPCAFKRGYSGTRTYMKNSTTVKGLHARCTRGFALPSEPQADAAAGSRVLVEGAGDEEGRVLTTFLSPDPDSASSSSRIALVNTYVANSGMGLTRLPYRVQSFDPSMREYLHRLDTWATENAAVPSAAAMGSGSSPHGFIWAGDLNVAERDYDRYYAGTFKSMQECSGFAPEERMSFRETMQRTNSVDIFRQLYPQAGPVYSFWSQRINGRPRNLGWRLDYFVVSSRLASYVVDCFPMPTVMGSDHCPFQMWMRHP
Protein: Acetyl hydrolase MbtJ (Q79FE8)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Salicyl-AMP ligase / salicyl-S-ArCP synthetase
- Salicylate synthase
- Phenyloxazoline synthase MbtB
- Protein MbtH
- Peptide synthetase MbtE
- Polyketide synthetase MbtD
- Polyketide synthetase MbtC
- L-lysine N6-monooxygenase MbtG
- Protein Rv3402c
- Esterase LipI
Sequence:
MVLRPITGAIPPDGPWGIWASRRIIAGLMGTFGPSLAGTRVEQVNSVLPDGRRVVGEWVYGPHNNAINAGPGGGAIYYVHGSGYTMCSPRTHRRLTSWLSSLTGLPVFSVDYRLAPRYRFPTAATDVRAAWDWLAHVCGLAAEHMVIAADSAGGHLTVDMLLQPEVAARPPAAVVLFSPLIDLTFRLGASRELQRPDPVVRADRAARSVALYYTGVDPAHHRLALDVAGGPPLPPTLIQVGGAEILEADARQLDADIRAAGGICELQVWPDQMHVFQALPRMTPEAAKAMTYVAQFIRSTTARGDL
Protein: Ribonucleoside-diphosphate reductase small chain 2 (EC 1.17.4.1) (Ribonucleotide reductase R2 subunit 2) (Ribonucleotide reductase small subunit 2) (P49723)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR4 is required for proper folding of RNR2 and assembly with the large subunits.
Subcellular location: Nucleus {ECO:0000269|PubMed:12732713, ECO:0000269|PubMed:18851834}. Note=Found predominantly in the nucleus under normal growth conditions and is redistributed to the cytoplasm in damaged cells in a DNA replication and damage checkpoint-dependent manner. Nuclear localization is mediated by DIF1.
Interaction partners:
- Ribonucleoside-diphosphate reductase large chain 1
- Transcriptional modulator WTM1
- Ribonucleoside-diphosphate reductase small chain 1
- Ribonucleoside-diphosphate reductase large chain 2
- Nucleoside diphosphate kinase
- Guanylate kinase
- Adenylate kinase
- Uridylate kinase
- GTP:AMP phosphotransferase, mitochondrial
- Thymidylate kinase
Sequence:
MEAHNQFLKTFQKERHDMKEAEKDEILLMENSRRFVMFPIKYHEIWAAYKKVEASFWTAEEIELAKDTEDFQKLTDDQKTYIGNLLALSISSDNLVNKYLIENFSAQLQNPEGKSFYGFQIMMENIYSEVYSMMVDAFFKDPKNIPLFKEIANLPEVKHKAAFIERWISNDDSLYAERLVAFAAKEGIFQAGNYASMFWLTDKKIMPGLAMANRNICRDRGAYTDFSCLLFAHLRTKPNPKIIEKIITEAVEIEKEYYSNSLPVEKFGMDLKSIHTYIEFVADGLLQGFGNEKYYNAVNPFEFMEDVATAGKTTFFEKKVSDYQKASDMSKSATPSKEINFDDDF
Protein: Oleosin G (A0A060L102)
Organism: Pinus massoniana (Chinese red pine)
Subcellular location: Lipid droplet {ECO:0000269|PubMed:24954070}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}.
Interaction partners:
Sequence:
MQKIHDHTPNPTQILGFITLFVSGAVLLFLTGLTLTGTVVGLVVLTPVLIFFSPILIPLATVLFVAVAGFLSAGGFGLAALSAISWLYNYIKGRHPPGADQIDYARMRIADTATHVKDYAREYGGYLQSKIQDAAPGA
Protein: Heat shock protein 90 (65 kDa IgE-binding protein) (Heat shock protein hsp1) (allergen Asp f 12) (P40292)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- SGT1 and CS domain protein
- Heat shock protein
- Peptidyl-prolyl cis-trans isomerase D
- Hsp90 binding co-chaperone
- Hsp90 chaperone protein kinase-targeting subunit
- GTPase activating protein
- Serine/threonine-protein phosphatase
- Transcription factor
- Heat shock transcription factor Hsf1, putative
- non-chaperonin molecular chaperone ATPase
Sequence:
MSSETFEFQAEISQLLSLIINTVYSNKEIFLRELISNASDALDKIRYQSLSDPTKLDTGKDLRIDIIPDKENKTLTIRDTGIGMTKADLINNLGTIARSGTKQFMEALSAGADISMIGQFGVGFYSAYLVADRVTVVSKNNDDEQYIWESAAGGTFTLTQDTEGEQLGRGTKIILHLKDEQTDYLNESRIKEVVRKHSEFISYPIYLHVLKETEKEVPDEEAEETKEEEDEEKKAKIEEVDDEEEEEKKKKKKTKTVKESKIEEEELNKTKPIWTRNPADITQEEYASFYKSLSNDWEDHLAVKHFSVEGQLEFRAILYVPKRAPFDLFETKKTKNNIKLYVRRVFITDDATDLIPEWLGFIKGVVDSEDLPLNLSRETLQQNKIMKVIKKNIVKKTLELFNEIAEDREQFDKFYSAFSKNIKLGIHEDAQNRQTLAKLLRYQSTKSGDEATSLADYVTRMPEHQKQIYYITGESIKAVAKSPFLDSLKQKNFEVLFLVDPIDEYAFTQLKEFDGKKLVDITKDFELEETEEEKAEREKEEKEYENLAKSLKNILGDKVEKVVVSHKLVGSPCAIRTGQFGWSANMERIMKAQALRDTSMSSYMSSKKTFEISPKSSIIKELKKKVEADGENDRTVKSITQLLFETSLLVSGFTIEEPASFAERIHKLVSLGLNIDEEAETTEEKATEEAAPAEATTGESAMEEVD
Protein: Melanoma antigen A 4 (cDNA, FLJ94494, Homo sapiens melanoma antigen, family A, 4 (MAGEA4), mRNA) (Q1RN33)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSEQKSQHCKPEEGVEAQEEALGLVGAQAPTTEEQEAAVSSSSPLVPGTLEEVPAAESAGPPQSPQGASALPTTISFTCWRQPNEGSSSQEEEGPSTSPDAESLFREALSNKVDELAHFLLRKYRAKELVTKAEMLERVIKNYKRCFPVIFGKASESLKMIFGIDVKEVDPTSNTYTLVTCLGLSYDGLLGNNQIFPKTGLLIIVLGTIAMEGDSASEEEIWEELGVMGVYDGREHTVYGEPRKLLTQDWVQENYLEYRQVPGSNPARYEFLWGPRALAETSYVKVLEHVVRVNARVRIAYPSLREAALLEEEEGV
Protein: COX assembly mitochondrial protein 2 homolog (Q9NRP2)
Organism: Homo sapiens (Human)
Function: May be involved in cytochrome c oxidase biogenesis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:20220131}.
Interaction partners:
- Endothelial protein C receptor
- Kinetochore-associated protein NSL1 homolog
- Cx9C motif-containing protein 4
- Intercellular adhesion molecule 1
- Cytochrome c oxidase assembly factor 4 homolog, mitochondrial
- Coiled-coil-helix-coiled-coil-helix domain-containing protein 7
- Cytochrome c oxidase assembly protein COX19
- Cytochrome c oxidase assembly factor 6 homolog
Sequence:
MHPDLSPHLHTEECNVLINLLKECHKNHNILKFFGYCNDVDRELRKCLKNEYVENRTKSREHGIAMRKKLFNPPEESEK
Protein: Hemocyanin subunit A (Q95P08)
Organism: Scutigera coleoptrata (House centipede)
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:12823556}.
Interaction partners:
Sequence:
MWSLALATLFVLGTVIRADQCPPVPADTKDKLEKILELIGHVNRPLTPETPEPAGYDETKLKGLGILPQHEIFSLFDERTWPEATKAAEFLMEATDFEHFIQRADVLRHRINEDMFMYALNVAVLHRKDTRGVQVPRIHKIYPDKFLKQDILVEVREKVNHGEEKPVVDATELHQNQLDPNYRLSYFLEDIGMNSHHYHWHVVHPAVWLPKHGPRKDRKGELFYYMHHQMVARYDSERLSNNLPRTEPFENWDDPLEEGYAPHLTIHKTGYNYMFRPEGLIVRDLPELNKNKMRQWKSRILHGIHLNVLYAENGTKISLDNEHGIDLLGDAIESSLLSVNRAFYGNIHCYAHVMAARIADPDGRYGEDNGVMHDVATSARDPLFYRWHKFIDNIFLEYKDNLDPYTQYELTWPDVVLNDVTVKPHKGDYDDEVHTYWEVDNYELGKGFDYTRKTTATVKVRHLQHEDYHYEIDIDNNAGKAKKAVFRIFLAPKYNEKGELFPVNEQRQLLVELDKFVATLEPGHNVIERQSKESSVTMSKDHVFGEIRNLADDHQCSCGWPDYLLLPKGKYEGMTYQLFVVATDYEEDHVEDAGEECQCRDSMSYCGSVEHKLPDNKPLGYPFDRRIDGTGFEEFKTQNMYYGDVVIQFTGETVTH
Protein: Large ribosomal subunit protein eL30 (60S ribosomal protein L30) (P62888)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS12
Sequence:
MVAAKKTKKSLESINSRLQLVMKSGKYVLGYKQTLKMIRQGKAKLVILANNCPALRKSEIEYYAMLAKTGVHHYSGNNIELGTACGKYYRVCTLAIIDPGDSDIIRSMPEQTGEK
Protein: Probable protein phosphatase 2C 60 (AtPP2C60) (EC 3.1.3.16) (Q9SZ53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGIYLSTPKTDKFSEDGENHKLRYGLSSMQGWRASMEDAHAAILDLDDNTSFLGVYDGHGGKVVSKFCAKYLHQQVLSDEAYAAGDVGTSLQKAFFRMDEMMQGQRGWRELAVLGDKINKFSGMIEGLIWSPRSGDSANKPDAWAFEEGPHSDFAGPNSGSTACVAVVRDKQLFVANAGDSRCVISRKNQAYNLSRDHKPDLEAEKERILKAGGFIHAGRVNGSLNLSRAIGDMEFKQNKFLPSEKQIVTASPDVNTVELCDDDDFLVLACDGIWDCMTSQQLVDFIHEQLNSETKLSVVCEKVLDRCLAPNTSGGEGCDNMTMILVRFKNPTPSETELKPEASQAEGNHDEPSSSN