wanglab/gogpt-training-data huggingface dataset:
Protein: Atlastin-2 (EC 3.6.5.-) (ADP-ribosylation factor-like protein 6-interacting protein 2) (ARL-6-interacting protein 2) (Aip-2) (Q8NHH9)
Organism: Homo sapiens (Human)
Function: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:27619977}; Multi-pass membrane protein {ECO:0000269|PubMed:18270207}. Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions (PubMed:27619977). {ECO:0000269|PubMed:27619977}.
Interaction partners:
- Spastin
- Receptor expression-enhancing protein 1
- Reticulon-1
- Spartin
- Receptor expression-enhancing protein 5
- Microtubule nucleation factor SSNA1
- ADP-ribosylation factor-like protein 6-interacting protein 1
- Charged multivesicular body protein 1b
Sequence:
MAEGDEAARGQQPHQGLWRRRRTSDPSAAVNHVSSTTSLGENYEDDDLVNSDEVMKKPCPVQIVLAHEDDHNFELDEEALEQILLQEHIRDLNIVVVSVAGAFRKGKSFLLDFMLRYMYNKDSQSWIGGNNEPLTGFTWRGGCERETTGIQVWNEVFVIDRPNGTKVAVLLMDTQGAFDSQSTIKDCATVFALSTMTSSVQVYNLSQNIQEDDLQHLQLFTEYGRLAMEEIYQKPFQTLMFLIRDWSYPYEHSYGLEGGKQFLEKRLQVKQNQHEELQNVRKHIHNCFSNLGCFLLPHPGLKVATNPSFDGRLKDIDEDFKRELRNLVPLLLAPENLVEKEISGSKVTCRDLVEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVAGARDTYCKSMEQVCGGDKPYIAPSDLERKHLDLKEVAIKQFRSVKKMGGDEFCRRYQDQLEAEIEETYANFIKHNDGKNIFYAARTPATLFAVMFAMYIISGLTGFIGLNSIAVLCNLVMGLALIFLCTWAYVKYSGEFREIGTVIDQIAETLWEQVLKPLGDNLMEENIRQSVTNSIKAGLTDQVSHHARLKTD
Protein: Triacylglycerol lipase (EC 3.1.1.3) (Extracellular lipase) (Triacylglycerol ester hydrolase) (P26876)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the hydrolysis of triacylglycerol. It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity. It shows a marked specificity for the 1,3-oleyl residues of triolein.
Subcellular location: Secreted {ECO:0000269|PubMed:1576157}. Note=During early stationary growth phase about 10% of the enzyme molecules remain cell-bound while about 90% are released into the growth medium. {ECO:0000269|PubMed:1576157}.
Interaction partners:
- Lipase chaperone
- Lipase LipC
- Diacylglycerol kinase
- Long-chain-fatty-acid--CoA ligase
- Long-chain-fatty-acid--CoA ligase
- Esterase EstA
- Uncharacterized AAA domain-containing protein ycf46
Sequence:
MKKKSLLPLGLAIGLASLAASPLIQASTYTQTKYPIVLAHGMLGFDNILGVDYWFGIPSALRRDGAQVYVTEVSQLDTSEVRGEQLLQQVEEIVALSGQPKVNLIGHSHGGPTIRYVAAVRPDLIASATSVGAPHKGSDTADFLRQIPPGSAGEAVLSGLVNSLGALISFLSSGSTGTQNSLGSLESLNSEGAARFNAKYPQGIPTSACGEGAYKVNGVSYYSWSGSSPLTNFLDPSDAFLGASSLTFKNGTANDGLVGTCSSHLGMVIRDNYRMNHLDEVNQVFGLTSLFETSPVSVYRQHANRLKNASL
Protein: Protein arginine N-methyltransferase 5 (EC 2.1.1.320) (A0A8I6ANJ2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR015894}. Nucleus {ECO:0000256|PIRNR:PIRNR015894}.
Interaction partners:
Sequence:
MAAMAVGGAGGSRVSSGRDLNWPDFLQRSREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIHPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDVIENAPTAHTEEYSGEEKTWLWWHNFRTLCDYSKRIAVALEIGADLPSSHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMQQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKETNVQVLMVLGAGRGPLVNASLRAAKQAERRIRLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYRDITLSIRPETHSPGMFSWFPIFFPIKQPITVHEGQNICVRFWRCSNSKKVWYEWAVTAPVCSSIHNPTGRSYTIGL
Protein: DNA-(apurinic or apyrimidinic site) endonuclease 2 (EC 3.1.11.2) (AP endonuclease 2) (Apurinic-apyrimidinic endonuclease 2) (P38207)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA.
Subcellular location: Nucleus.
Interaction partners:
- Apurinic-apyrimidinic endonuclease 1
- Tyrosyl-DNA phosphodiesterase 1
- Endonuclease III homolog 2 lyase 2)
- DNA repair protein RAD1
- Uracil-DNA glycosylase
- Endonuclease III homolog 1 lyase 1)
- Aminopeptidase 2, mitochondrial
- N-glycosylase/DNA lyase
- Polynucleotide 3'-phosphatase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
Sequence:
MSSSENTLLDGKSENTIRFLTFNVNGIRTFFHYQPFSQMNQSLRSVFDFFRADIITFQELKTEKLSISKWGRVDGFYSFISIPQTRKGYSGVGCWIRIPEKNHPLYHALQVVKAEEGITGYLTIKNGKHSAISYRNDVNQGIGGYDSLDPDLDEKSALELDSEGRCVMVELACGIVIISVYCPANSNSSEEGEMFRLRFLKVLLRRVRNLDKIGKKIVLMGDVNVCRDLIDSADTLEQFSIPITDPMGGTKLEAQYRDKAIQFIINPDTPHRRIFNQILADSLLPDASKRGILIDTTRLIQTRNRLKMYTVWNMLKNLRPSNYGSRIDFILVSLKLERCIKAADILPDILGSDHCPVYSDLDILDDRIEPGTTQVPIPKFEARYKYNLRNHNVLEMFAKKDTNKESNKQKYCVSKVMNTKKNSNIKNKSLDSFFQKVNGEKDDRIKESSEIPQQAKKRISTPKLNFKDVFGKPPLCRHGEESMLKTSKTSANPGRKFWICKRSRGDSNNTESSCGFFQWV
Protein: Epididymis secretory sperm binding protein (Speedy homolog 1 (Drosophila)) (A0A384MTT5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRHNQMCCETPPTVTVYVKSGSNRSHQPKKPITLKRPICKDNWQAFEKNTHNNNKSKRPKGPCLVIQRQDMTAFFKLFDDDLIQDFLWMDCCCKIADKYLLAMTFVYFKRAKFTISEHTRINFFIALYLANTVEEDEEETKYEIFPWALGKNWRKLFPNFLKLRDQLWDRIDYRAIVSRRCCEEVMAIAPTHYIWQRERSVHHSGAVRNYNRDEVQLPRGPSATPVDCSLCGKKRRYVRLGLSSSSSLSSHTAGVTEKHSQDSYNSLSMDIIGDPSQAYTGSEVVNDHQSNKGKKTNFLKKDKSMEWFTGSEE
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (Q56IA0)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
- receptor protein serine/threonine kinase
- E3 ubiquitin-protein ligase.
- Activin receptor type-1
- Bone morphogenetic protein receptor type-1B
- Mothers against decapentaplegic homolog 6
- Mothers against decapentaplegic homolog.
- Mothers against decapentaplegic homolog 5
- Mothers against decapentaplegic homolog.
- Mothers against decapentaplegic homolog
- Mitogen-activated protein kinase.
Sequence:
MNVTSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSCPGQPSNCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEYNPQHSLLAQFRNLGQNEPHMPHNATFPDSFQQPNSHPFPHSPNSSYPNSPGSSSSTYPHSPASSDPGSPFQMPADTPPPAYLPPEDQMTHDTSQPMDTNMMAPGIHPDIHRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSILVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTLRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
Protein: POM121 and ZP3 fusion protein (POM-ZP3) (Q6PJE2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVCSPVTLRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKKKKRTVEEEDQIFLDGQENKRSCLVDGLTDASSAFKVPRPGPDTLQFTVDVFHFANDSRNMIYITCHLKVTLAEQDPDELNKACSFSKPSNSWFPVEGLADICQCCNKGDCGTPSHSRRQPRVVSQWSTSASL
Protein: Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cdc2-related kinase, arginine/serine-rich) (CrkRS) (Cell division cycle 2-related protein kinase 7) (CDC2-related protein kinase 7) (Cell division protein kinase 12) (hCDK12) (Q9NYV4)
Organism: Homo sapiens (Human)
Function: Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors.
Subcellular location: Nucleus {ECO:0000269|PubMed:11683387}. Nucleus speckle {ECO:0000269|PubMed:11683387}. Note=Colocalized with nuclear speckles throughout interphase. {ECO:0000269|PubMed:11683387}.
Interaction partners:
- Cyclin-K
- DNA damage-binding protein 1
- DNA-directed RNA polymerase II subunit RPB1
- Cyclin-dependent kinase 13
- Cyclin-T1
- Cyclin-T2
- Cyclin-H
- Transcription elongation factor SPT5
- Cyclin-dependent kinase 9
- Transcription elongation factor SPT6
Sequence:
MPNSERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLVSKHKRHKSKHSKDMGLVTPEAASLGTVIKPLVEYDDISSDSDTFSDDMAFKLDRRENDERRGSDRSDRLHKHRHHQHRRSRDLLKAKQTEKEKSQEVSSKSGSMKDRISGSSKRSNEETDDYGKAQVAKSSSKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSSKQDDSPSGASYGQDYDLSPSRSHTSSNYDSYKKSPGSTSRRQSVSPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYSGRSPSPYGRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSPAYSRHSSSHSKKKRSSSRSRHSSISPVRLPLNSSLGAELSRKKKERAAAAAAAKMDGKESKGSPVFLPRKENSSVEAKDSGLESKKLPRSVKLEKSAPDTELVNVTHLNTEVKNSSDTGKVKLDENSEKHLVKDLKAQGTRDSKPIALKEEIVTPKETETSEKETPPPLPTIASPPPPLPTTTPPPQTPPLPPLPPIPALPQQPPLPPSQPAFSQVPASSTSTLPPSTHSKTSAVSSQANSQPPVQVSVKTQVSVTAAIPHLKTSTLPPLPLPPLLPGDDDMDSPKETLPSKPVKKEKEQRTRHLLTDLPLPPELPGGDLSPPDSPEPKAITPPQQPYKKRPKICCPRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLIHRSVVNMKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLEYCHKKNFLHRDIKCSNILLNNSGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMAPPDLPHWQDCHELWSKKRRRQRQSGVVVEEPPPSKTSRKETTSGTSTEPVKNSSPAPPQPAPGKVESGAGDAIGLADITQQLNQSELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTEATSQQQDSETMAPEESLKEAPSAPVILPSAEQTTLEASSTPADMQNILAVLLSQLMKTQEPAGSLEENNSDKNSGPQGPRRTPTMPQEEAAACPPHILPPEKRPPEPPGPPPPPPPPPLVEGDLSSAPQELNPAVTAALLQLLSQPEAEPPGHLPHEHQALRPMEYSTRPRPNRTYGNTDGPETGFSAIDTDERNSGPALTESLVQTLVKNRTFSGSLSHLGESSSYQGTGSVQFPGDQDLRFARVPLALHPVVGQPFLKAEGSSNSVVHAETKLQNYGELGPGTTGASSSGAGLHWGGPTQSSAYGKLYRGPTRVPPRGGRGRGVPY
Protein: Laccase (Q5BEX9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MGFLRRRSMMQALLLTIIFSAYAYGANVKTTGQMVSFQVNLTWSDYQPAGIPRKMILANGQFPAPALRLKQGDDVEFLVNNEMPFSTTVHFHGIEQQGTPWSDGVPGLSQRPIPPGESFLYKWRATNYGSYFYHAHSRGQQEDGLYGAIHILADDSIERPFALISEDEQEIQSMRRAESESIPIMLSDVRSLTSAEIWDAEKAMGRDALCANALLVNGKGSVTCLGQQTIDEYTSVAQRGVLGNQSLTDIGCLPPDNLLAQGPWSHNLSAIPPTVFSDCIPSHGLTERFYPDATNRYASFDLVSAALVSTITFSIDEHPMYVYAIDGSYINPIEADGITITNGARYSVLVKLDKPRGDYTIRVVNTGLNQILHGNALMTYHNGIGPIQQHPSTPSIDLVGTPTSNHTLLNESMIIPFAAQDVSRVDVAQTLTLTLERYNASYTWTMGDSSFPLQLEEESPLLFYPQTASKNFTATSKNGTWVDVVFDVANAIQPPHPIHKHSNKFYVLGGGNGKWNYTSVAEAAKHMPESFNFETPQIRDTFATLPAATGPTWLALRYHVVNPGPFLLHCHIQIHQSGGMALALLDGIDEWPEIPEEYQLA
Protein: Flotillin (B5X3E3)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU366054}. Endosome {ECO:0000256|RuleBase:RU366054}.
Interaction partners:
Sequence:
MFYTCGPNEAMVVSGFGRSPPLMIAGGRVFVLPCIQQIQRITLNTLTLNVKSDKVYTRHGVPISVTGIAQVKIQGQNKEMLATACQMFMGKSEAEVSNIALETLEGHQRAIIAHLTVEEIYQDRKKFSEQVFKVASSDLVNMGIGVVSYTLKDVHDDQDYLTSLGKARTAQVQKDARIGEAQYKRDAVIREAQAMQEKVSAQYLNEIEMAKAQRDYELKKASYDYEVNTKKAESEMAYQLQVAKTKQRIEEETMQVKVVERSQQIMLQEQEITRKEMELEAKVKKPAEAERYRLERLAEAERAQLIMEAEAEAESIRMRGDAEAFALEAKGRAEAEQMAKKAEAFKQYGEGAMVDMLLEKLPLIAEEISRPLSMAQKVTMVSNGGGEVGAAKLTGEVLDIMTRLPAAVEKLTGINISQVGLSTRMG
Protein: Alpha-1,3-glucanase (Mutanase) (Q96VT3)
Organism: Emericella nidulans (Aspergillus nidulans)
Interaction partners:
Sequence:
MKIFHRCCAALTLLANALPALSLPGANSLTIRKDSNKYVTAHFMVGIVENYTVDDWKHDMELAKETGIDAFALNCASIDSYTDKQLAYAYEAAEEVDFKVFISFDFAYWSNGDTARITSIMQTYADHPGQFQYNGAALVSTFVGDSFDWGPVKRAVDHPIFAVPNLQDPNWAGHATTSIDGAFSWYAWPTDGGNSIIKGPMTTIWDDRFRNNLKDKVYMAPVSPWFSTHFNTKNWVFICEDLPHLRWQQMLEMQPELIEIISWNDYGESHYIGPYSEAHSDDGSAQWTKDFPHDAWRIIAKPYIAAYKAGEREPTVESDQLVYWYRPTPKAVTCSKDPLGPPNGINLLEDSVFVTTLLTEPATLTVGSGSLEFSVDVDAGIVTNSFPMGVGSQAFSVTRDGEEILGGDGGLDVQDRCDYYNFNVYVGSFSA
Protein: Cypemycin (E5KIB6)
Organism: Streptomyces sp
Function: Antibiotic peptide structurally related to lantibiotics. Active against M.luteus (MIC=0.2 ug/ml). Has cytotoxic activity against mouse P388 leukemia cells (IC(50)=1.3 ug/ml).
Subcellular location: Secreted {ECO:0000269|PubMed:7802859}.
Interaction partners:
Sequence:
MRSEMTLTSTNSAEALAAQDFANTVLSAAAPGFHADCETPAMATPATPTVAQFVIQGSTICLVC
Protein: Hexosyltransferase (EC 2.4.1.-) (A0A0S2Z5K4)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004447, ECO:0000256|RuleBase:RU364016}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004447, ECO:0000256|RuleBase:RU364016}.
Interaction partners:
Sequence:
MPRRGLILHTRTHWLLLGLALLCSLVLFMYLLECAPQTDGNASLPGVVGENYGKEYYQALLQEQEEHYQTRATSLKRQIAQLKQELQEMSEKMRSLQERRNVGANGIGYQSNKEQAPSDLLEFLHSQIDKAEVSIGAKLPSEYGVIPFESFTLMKVFQLEMGLTRHPEEKPVRKDKRDELVEVIEAGLEVINNPDEDDEQEDEEGPLGEKLIFNENDFVEGYYRTERDKGTQYELFFKKADLTEYRHVTLFRPFGPLMKVKSEMIDITRSIINIIVPLAERTEAFVQFMQNFRDVCIHQDKKIHLTVVYFGKEGLSKVKSILESVTSESNFHNYTLVSLNEEFNRGRGLNVGARAWDKGEVLMFFCDVDIYFSAEFLNSCRLNAEPGSQKGFWLLARFWLWNDLSVSFRFPDHWWI
Protein: ClC family H(+)/Cl(-) exchange transporter (A0A2R7DXN8)
Organism: Limosilactobacillus reuteri (Lactobacillus reuteri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEAVFVKNENTLYHKRARDILGKPFTSIVSRYLGVSIAIGIVTGLVIGVFRWIIDHTLTLLTIIYPFMGKHPLVLIPYVLGTFIVAWLIGKIVKPYEEDVVRSGVTQLKAVLLGRHRIHWWPVLWRKFVASLLTICPGLFLGREGPSIQIGACIGACFNEKFFHLTDKDKYLLMECGVAAGLSAAFSAPLAGTMFLLEEMTHNFNSRIWIPALTSSIVSAFITFLFFGIKPCLYIPITTKLPVASYPWLIIAGVAIGFLAYCFQFAALNLTWWYSKITFIPKEFHSIIPLLLVIPVGLWNPYILGGSHDFIKYVTNMSLSTNWQAMVAILLVYFILRFGGTMIAYGATVPGGIFMPLFVLGTVVGALTGTILIHMGIIPASCYVNVIIISMAAYFGGAEGLPFTAILLVTEMVGSVEQILPMTLITLVAYYVNRLLGGRPSLYDAMLEEK
Protein: Homoisocitrate dehydrogenase (HICDH) (EC 1.1.1.87) (Homo(2)-isocitrate/homo(3)-isocitrate dehydrogenase) (EC 1.1.1.-) (Isohomocitrate dehydrogenase) (IHDH) (NAD-dependent threo-isohomocitrate dehydrogenase) (Q58991)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the NAD-dependent oxidation and decarboxylation of (2R,3S)-homoisocitrate, (2R,3S)-homo(2)-isocitrate and (2R,3S)-homo(3)-isocitrate, into 2-oxoadipate, 2-oxopimelate (2-oxoheptanedioate), and 2-oxosuberate, respectively. All these substrates are intermediates in the biosynthesis of biotin and of 7-mercaptoheptanoate, a moiety of coenzyme B in methanoarchaea. Is also able to produce 2-oxoazelate from (2R,3S)-homo(4)-isocitrate in vitro, but this substrate is probably not physiologically relevant. Is unable to use any isomer of isocitrate or isopropylmalate as a substrate, and NADP as an oxidant.
Interaction partners:
- Methanogen homoaconitase large subunit
- Methanogen homoaconitase small subunit
- Homocitrate synthase AksA
- Isopropylmalate/citramalate isomerase large subunit
- Ketol-acid reductoisomerase
- Isopropylmalate/citramalate isomerase small subunit
- Probable acetolactate synthase small subunit
- Dihydroxy-acid dehydratase
- Succinate--CoA ligase subunit beta
- UPF0104 membrane protein MJ1595
Sequence:
MMKVCVIEGDGIGKEVIPEAIKILNELGEFEIIKGEAGLECLKKYGNALPEDTIEKAKEADIILFGAITSPKPGEVKNYKSPIITLRKMFHLYANVRPINNFGIGQLIGKIADYEFLNAKNIDIVIIRENTEDLYVGRERLENDTAIAERVITRKGSERIIRFAFEYAIKNNRKKVSCIHKANVLRITDGLFLEVFNEIKKHYNIEADDYLVDSTAMNLIKHPEKFDVIVTTNMFGDILSDEASALIGGLGLAPSANIGDDKALFEPVHGSAPDIAGKGIANPMASILSIAMLFDYIGEKEKGDLIREAVKYCLINKKVTPDLGGDLKTKDVGDEILNYIRKKLKGY
Protein: Sialic acid-binding Ig-like lectin 11 (Sialic acid-binding lectin 11) (Siglec-11) (Q96RL6)
Organism: Homo sapiens (Human)
Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,8-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 11
Sequence:
MVPGQAQPQSPEMLLLPLLLPVLGAGSLNKDPSYSLQVQRQVPVPEGLCVIVSCNLSYPRDGWDESTAAYGYWFKGRTSPKTGAPVATNNQSREVEMSTRDRFQLTGDPGKGSCSLVIRDAQREDEAWYFFRVERGSRVRHSFLSNAFFLKVTALTKKPDVYIPETLEPGQPVTVICVFNWAFKKCPAPSFSWTGAALSPRRTRPSTSHFSVLSFTPSPQDHDTDLTCHVDFSRKGVSAQRTVRLRVAYAPKDLIISISHDNTSALELQGNVIYLEVQKGQFLRLLCAADSQPPATLSWVLQDRVLSSSHPWGPRTLGLELRGVRAGDSGRYTCRAENRLGSQQQALDLSVQYPPENLRVMVSQANRTVLENLGNGTSLPVLEGQSLRLVCVTHSSPPARLSWTRWGQTVGPSQPSDPGVLELPPIQMEHEGEFTCHAQHPLGSQHVSLSLSVHYPPQLLGPSCSWEAEGLHCSCSSQASPAPSLRWWLGEELLEGNSSQGSFEVTPSSAGPWANSSLSLHGGLSSGLRLRCKAWNVHGAQSGSVFQLLPGKLEHGGGLGLGAALGAGVAALLAFCSCLVVFRVKICRKEARKRAAAEQDVPSTLGPISQGHQHECSAGSSQDHPPPGAATYTPGKGEEQELHYASLSFQGLRLWEPADQEAPSTTEYSEIKIHTGQPLRGPGFGLQLEREMSGMVPK
Protein: Invasin CotH7 (Spore coat protein homolog 7) (I1BJN3)
Organism: Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Function: Promotes invasion of host epithelial cells by adhering to receptors on the host cell surface to facilitate endocytosis of the pathogen into host cells. Probably binds integrin ITGA3:ITGB1 via ITGB1, on the cell surface of host alveolar epithelial cells.
Subcellular location: Cell membrane {ECO:0000305|PubMed:32487760}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
Sequence:
MKSLSFISLACLTAVHAASVTFKVIAPTAESSVQVNINGQLTQLKAQDEDIPYYTGSAELNDGQSYKYVVDGAAETFERILNGTSTKNEFFNRPITYATNIPELPNILSEGSWTRGETTDPLWDSNYVPSIFVTGKSDEMEDLITNVTKKTYQAKITFIGPENITTIENCTFGLHKPGRKHNDAKQTWVWTLPEGQYVAKRSWFKIRHMEEDPTQLREKLYADIARKMGTYANEANMVRFFINKEGMGTFNMLDDVIMYSYINAMFYNGNPPQQLGALYDGASGAAFNASGDMDSFIPNVESPLDQDALMPFSKAFAAVDFSNDDQVKAISQYFDYDQFLRFMVMEFLTADWDGYWQEQTNDGAYIDVSDNNKVYYLAQDFDATFGVNLDQERDFVNTPYTDFPTKFPGGILINKLLENPTTKATFETYLKTTVQEIFNNATLGAYVTARHNFLAPDLKWDRSIKQRSPGNIFGWTYEQTYQNLFEGVTAPGKEQGGAEWGLLEWVAAKEKAVRSSLKLSETATTSTSATIAAPATSESASQDNTSDDTDSASTSSSTLNQAAADTSSASKSAPTFYCLQLVLYLSLSFKNLYKYI
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8Y4S2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGLSSCYCPEYLKDASKKMKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKMAAQRQKRGK
Protein: LD21067p (Phosphatidic acid phospholipase A1, isoform A (EC 3.1.1.-, EC 3.1.1.32)) (Q9VLS7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein transport protein Sec31A
- Protein transport protein SEC23
- Protein SEC13 homolog
- Secretory 24AB, isoform A
Sequence:
MSERSKGDVSARVNNNANQTRVVKNPLLSASVTGLSFDDFPNKPQLLPAAPPVVHATPPAAPVLIAGILNREPKSLVTVGQPSSIDDSEALDEINLNTSSEDSVGAGGSSPYLGAGDQNANPLLEPPTEAGNDSLLSQAASSFTALPAVASNVFSTFSKRIYAGSRETSEEPKLDIQPSYIQQASYVQPVAPVPAPFYAAPPAAANEVVAPEPPKFYAPTEVPPPNVGVPAPPPTSGNPNTYRFTARKKLYAPIPGLSEQSGQPAQQPQVPQAPQAAPSFQTPPYPPQLTYAANPAPFDISAQPAAIPAEERKSGGGLFSLTSLVPTGVLQNITGIVQSATGRSSEPEHTNVQQAGGYLDITTASAPAPSTNLFGGPNSTFPPGGNYFVPGAPPSLPSTGVVGPPSVGNFFAPAAPLPVAQTAAPPAVGAFFTSAAPSVTPSVFTPGTVPPLAPQPFQSATVNQSALPPNNPPTASAVGELFVPAPTTIAQGTSPAVPFVDTQAVPTIPLTVPPGNPPPTSTLGGFFTTGEVAPVVAPFGTQASPATQSAGFFNPGEVRPNVPLAEPVPTIPITSSGVPPIGLFPPAPAQPGVQTASNPNPLPGAAAPPPAAGQASYRLQKGTRLYKSPLTPQETATSSGFAAPLPPTSVTPAIFNPFGAPAPGSFNSVGHLEGQSSQGVPFFTPPVQNPPGQVAAPTVAVPQSAPIAPPPGTSSTSVAPPLTASIANPPPTSGFASVPLFAAPTISSTPIPFFNPQPTGAEVTTGLSQQENEATASTTLEGLVQGPAPTLSASQFFDTPLPTGTQPENQVASVSSERENLVQEPISNQGIPFFAPPQTNIFTPQLQQEFIAPAEDSKRSEIQEEFLSAPPQESNLSTELREDTHTGPPVIEPVLEETPASSSESSVPPASKVDQEDIVYPEPSAPVEQEIPLFVPVPGLPGLSQDIPLYPPPPTGSTTASSIFAAPPVASSAPLFVPVPGPPSVSSLFSPSQVDSTSSLFAPPPTSANTTILTPAPDTTSTLFANNIPTTTPSIPDIVPTTSAELVDAPPGFQGSSDDTATNLFQGNTETQTVFSPFAQTKATPLVQETKPELVPPPIGFFAPKSESEVLSQPPLAPSPLQSFFSTAPETATTTDFNFFGSPAPGSVFPDLPVQQGIAPPPLALESPPQNSVSNIATSAIGFDLLNQTQQASSLVENSNQNSSVNSFDGYFGGPSASAAQTFANETTNALVAPAINCDPVNFFDQVPQTQSQIQQANEDQRIQNFFNNPPLQDQPAVPGELKYDIVHSGVAVKQLQERSQTPVSNLVEPPSSACSEFSTLAPAPTQTDRQSGDDLLQQHLGELPEDILRELRMASASSEKGQVATPPVAIPYSPVVAHWFYKRSVDTKFIWTPFSHYDSALLETSLNLDDSTLIIPVEGGRYDVNIKERTKTPVYWEGKAIEVRRCSWFYKGVDSKYVPYTEDTAALLEAEYKRSAETGEWHQKIMLANGEQVVFHGPTVIVHFLPQQNADTWGASTQGSMRPRVVKRDLDDFTIEQGESQRVDHLLFMVHGIGSACDLKMRSVEEVVDDFRVIAQQLVQSHYKNSTDMGLVGRVEVLPISWHGHLHSEELGIDEKLKSITLESIPRLRNFTNDTLLDVLFYTSPKYCQKIMNTVADALNDVYLKYRMRHPEFNGGVSLAGHSLGSLILFDLLCHQEPLKESEEENKENPDQLPQKQSSQKVQLPTSDPLPKQVSYAMGPEGTGQPVITYTQLIFHPKKFFALGSPIGMFVTIRGIDKLGLDFHLPTCPGFYNIFHPFDPVAYRIEALVNPDMNGIRPVLIPHHKGRKRMHLELKETMTRVGADIKQRFMDTFKTTLDSVNFLTTVTKVKKEAEESLEKETSQTSSQAFQKQTEDQDESSVASSSCKLRNRTDSNSTTASDPEFIELDFPLGKLNDSKRVDYVLQEAPLEFINEYIFALSSHVCYWGSEDTILFVMKEIYASLGISTDSQVPQSSMTIERPVSHESSVSHSLLPM
Protein: 3-oxo-Delta(4,5)-steroid 5-beta-reductase (EC 1.3.1.3) (Delta(4)-3-oxosteroid 5-beta-reductase) (Delta-4,5-steroid 5-beta-reductase) (At5beta-StR) (Progesterone 5-beta-reductase) (5beta-POR) (Protein VEIN PATTERNING 1) (Q9STX2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in vascular strand development. Catalyzes the stereospecific conversion of progesterone to 5-beta-pregnane-3,20-dione. Can use progesterone, testosterone, 21-acetyl cortexone, 2-cyclohexenone, but-1-en-3-one, ethyl acrylate, ethylmethacrylate, cortisone and canarigenone as substrates, lower activity with 3-methyl-2-cyclohexenone and 3,5,5-trimethyl-2-cyclohexenone as substrate, and no activity with canarigenin, canarigenin digitoxoside and pregnenolone. May be involved in the formation of 5-beta phytoecdysteroids.
Interaction partners:
- Cytochrome P450 71B34
- Phloem protein 2-A10
- Germin-like protein subfamily 2 member 3
Sequence:
MSWWWAGAIGAAKKKLDEDEPSQSFESVALIIGVTGIVGNSLAEILPLSDTPGGPWKVYGVARRPRPTWNADHPIDYIQCDVSDAEDTRSKLSPLTDVTHVFYVTWTNRESESENCEANGSMLRNVLQAIIPYAPNLRHVCLQTGTKHYLGPFTNVDGPRHDPPFTEDMPRLQIQNFYYTQEDILFEEIKKIETVTWSIHRPNMIFGFSPYSLMNIVGTLCVYAAICKHEGSPLLFPGSKKAWEGFMTASDADLIAEQQIWAAVDPYAKNEAFNCNNADIFKWKHLWKILAEQFGIEEYGFEEGKNLGLVEMMKGKERVWEEMVKENQLQEKKLEEVGVWWFADVILGVEGMIDSMNKSKEYGFLGFRNSNNSFISWIDKYKAFKIVP
Protein: Probable eukaryotic initiation factor 4A (EC 3.6.4.13) (ATP-dependent RNA helicase eIF4A) (Q38DF6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- PRP1 splicing factor N-terminal domain-containing protein
- U5 small nuclear ribonucleoprotein component, putative
- ATP-dependent DEAD/H RNA helicase, putative
- TOG domain-containing protein
- Cell division control protein, putative
- ATP synthase alpha chain
- ATP synthase subunit beta
- ATP synthase F1 subunit gamma protein, putative
Sequence:
MSLSRTENNGTTSDTPAREFNNNERNAPVNNGGAGRGGRWAFRGDFRSDEGGERKGKPWGRFPQGDGERGNRGYGGGYRGRGGRGRGGGGGGGFREGSFGFENRAQQQPPREGLMNDQAPQEERQPTEESEPVQRGRFDVDFYDRPRRRGRGRQYGGRGDNDGERGFFGGDNNERQPQKQRQQNPKPFGQQQQLEPQQEDEQEAVASPQQQYNQQQRQPERRPDTAPTMDPISTNPNRTQRAPRFRKNCRDEREIEKLFESHHQQKGISLENYASIPVDIVPRDIDAVESFEDLFVEPALALNIAKCGYKEPTPVQRYGIPVCLNGNDLMACAQTGSGKTAAFLVPVVHYILKNGVSPAKDRISHPIAVIMAPTRELALQIYDEVRKLTFRTDIFYDVVYGGTPYPTRFENDILVACPGRLKDIFDRNIVSFSCVKFLILDEADRMLEMGFEEQIEYLVASRYSDMPSSEERQTLMFSATFPQRILNLAKRYLRPKYYLLTVGRVGSTTKNITQKLERVPEAEKKDKLFDIIYKQKQTDLVLIFVETKRSAEQLHSALKSSGIPSTTIHGDRRQSDREIALKDFKSGITPILVATDVASRGLDIPNVAHVIQYDLPKEMDDYTHRIGRTGRAGNKGVATSFYDRNNRNLAVELYHYLREHEQEVPMWLENEKDAVEGERFVGGTRGGNRRGGGESRAAAPLGNSTWGEAATGRGGRQGGQQQQERKESNVDDGGF