wanglab/gogpt-training-data huggingface dataset:
Protein: Plasmodium RESA N-terminal domain-containing protein (Q8IK27)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MLFSFKYIYFSSTFLLLLVLQSKTKYIQNFVNIQETLNEKCSSKYIRLISEQTSDESTSKSIKNCKCVNKRNNKNEDNHELQSKSRSLKGTELDVTSYNKSKHTQQNNLGDSLKRTKNNITNISSKKNETYLFDENTNEYKLRNTLRLMNERYADSIVDTMDLNDKTKDKFKKFLHLYMAKENPDKQRKLYEQIESDIEKYKKNHVICSIVDFENIYDSFYFLKYEDRYIT
Protein: Holocytochrome c-type synthase (EC 4.4.1.17) (Cytochrome c-type heme lyase) (P53701)
Organism: Homo sapiens (Human)
Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:17033964}. Membrane {ECO:0000269|PubMed:23150584}; Lipid-anchor {ECO:0000305|PubMed:25255805, ECO:0000305|PubMed:25807930}.
Interaction partners:
- Protoheme IX farnesyltransferase, mitochondrial
- Ferrochelatase, mitochondrial
- Rho GTPase-activating protein 6
- Heme oxygenase 2
- Heme oxygenase 1
- Heme A synthase COX15
- Cytochrome c
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MGLSPSAPAVAVQASNASASPPSGCPMHEGKMKGCPVNTEPSGPTCEKKTYSVPAHQERAYEYVECPIRGTAAENKENLDPSNLMPPPNQTPAPDQPFALSTVREESSIPRADSEKKWVYPSEQMFWNAMLKKGWKWKDEDISQKDMYNIIRIHNQNNEQAWKEILKWEALHAAECPCGPSLIRFGGKAKEYSPRARIRSWMGYELPFDRHDWIINRCGTEVRYVIDYYDGGEVNKDYQFTILDVRPALDSLSAVWDRMKVAWWRWTS
Protein: BBX high mobility group box domain containing (C9J8D0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKGSNRNKDHSAEGEGVGKRPKRKCLQWHPLLAKKLLDFSEEEEEEDEEEDIDKVQLLGADGLEQDVGETEDDESPEQRARRPMNAFLLFCKRHRSLVRQEHPRLDNRGATKILADWWAVLDPKEKQKYTDMAKEYKDAFMKANPGYKWCPTTNKPVKSPTPTVNPRKKLWAFPSDSSRDLPSPKKAKTEEMPQLNFGMADPTQMGGLSMLLLAGEHALGTPEVSSGTCRPDVSESPELRQKSPLFQFAEISSSTSHSDASTKQCQTSALFQFAEISSNTSQLGGAEPVKRCGKSALFQLAEMCLASEGMKMEESKLIKAKESDGGRIKELEKGKEEKEIKMEKTDETRLQKEAEFEKSAKENLRDSKELRNFEALQIDDIMAIKMEDPKEIRKEELEEDHKCSHFPDFSYSASSKIIISDVPSRKDHMCHPHGIMIIEDPAALNKPE
Protein: CEA cell adhesion molecule 5 (A0A087WYX0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MESPSAPPHRWCIPWQRLLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNELSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSAGATVGIMIGVLVGVALI
Protein: Regulating synaptic membrane exocytosis protein 4 (RIM4 gamma) (Rab3-interacting molecule 4) (RIM 4) (P60191)
Organism: Mus musculus (Mouse)
Function: Regulates synaptic membrane exocytosis.
Subcellular location: Synapse {ECO:0000250}.
Interaction partners:
Sequence:
MERSQSRLSLSASFEALAIYFPCMNSFDDEDAADSRRLKGAIQRSTETGLAVEMPSRTLRQASHESIEDSMNSYGSEGNLNYGGVCLASDAQFSDFLGSMGPAQFVGRQTLATTPMGDVEIGLQERNGQLEVDIIQARGLTAKPGSKTLPAAYIKAYLLENGVCIAKKKTKVARKSLDPLYNQVLLFPESPQGKVLQVIVWGNYGRMERKQFMGVARVLLEELDLTTLAVGWYKLFPTSSMVDPATGPLLRQASQLSLESTVGPCGERS
Protein: Endoplasmic reticulum junction formation protein lunapark (ER junction formation factor lunapark) (Protein ulnaless) (Q7TQ95)
Organism: Mus musculus (Mouse)
Function: Endoplasmic reticulum (ER)-shaping membrane protein that plays a role in determining ER morphology. Involved in the stabilization of nascent three-way ER tubular junctions within the ER network. May also play a role as a curvature-stabilizing protein within three-way ER tubular junction network. May be involved in limb and central nervous system development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9C0E8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9C0E8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9C0E8}. Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions, which represent crossing-points at which the tubules build a polygonal network. {ECO:0000250|UniProtKB:Q9C0E8}.
Interaction partners:
- Atlastin-3
- Atlastin-2
- Atlastin-1
- Homeobox even-skipped homolog protein 2
- Metaxin-2
Sequence:
MGGLFSRWRAKPSTVEVLENIDKEIQALEEFREKNQRLQKLWVGRLIIYSSILYLFTCLIVYLWYLPDEFTARLVMTLPFFAFPLIIWTLRTVLIFFFSKRTERNNEALDDLKSQKKKILEEVMEKETYKTAKLILERFDPDSKKAKEFEPPSAGAAVTAKPGQEIRQRTAAQRNLSPAPASSSQGPPPQGPVSPGPAKDASAPGGPPERTVAPALPRRLGSPATSVPGMGLHPPGPPLARPILPRERGALDRIVEYLVGDGPQNRYALICQQCFSHNGMALKEEFEYIAFRCAYCFFLNPARKTRPQAPRLPEFSFEKRQAVEGSSSTGPTLLESVPSAESQLIEDSLEEQDVLDNSTEQRDDKIPVTEQTSQVIEKTSGPEEPAENQEETENEETSTNEAKSPVLRADSVPNLEPSEESLVTK
Protein: Mitochondrial nicotinamide adenine dinucleotide transporter 1 (Mitochondrial NAD(+) transporter 1) (P40556)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial inner membrane carrier protein that mediates the import of NAD(+) into mitochondria. Can transport NAD(+) by unidirectional transport or by exchange with intramitochondrially generated dAMP and dGMP. Also able to transport NAD(+) by exchange with AMP, GMP or deamido-NAD (+) in vitro.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16291748}; Multi-pass membrane protein {ECO:0000269|PubMed:16291748}.
Interaction partners:
Sequence:
MTQTDNPVPNCGLLPEQQYCSADHEEPLLLHEEQLIFPDHSSQLSSADIIEPIKMNSSTESIIGTTLRKKWVPLSSTQITALSGAFAGFLSGVAVCPLDVAKTRLQAQGLQTRFENPYYRGIMGTLSTIVRDEGPRGLYKGLVPIVLGYFPTWMIYFSVYEFSKKFFHGIFPQFDFVAQSCAAITAGAASTTLTNPIWVVKTRLMLQSNLGEHPTHYKGTFDAFRKLFYQEGFKALYAGLVPSLLGLFHVAIHFPIYEDLKVRFHCYSRENNTNSINLQRLIMASSVSKMIASAVTYPHEILRTRMQLKSDIPDSIQRRLFPLIKATYAQEGLKGFYSGFTTNLVRTIPASAITLVSFEYFRNRLENISTMVI
Protein: Prolactin receptor (PRL-R) (F1N4H8)
Organism: Bos taurus (Bovine)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU365035}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU365035}.
Interaction partners:
Sequence:
MKENAASRVVFILLLFLSVSLLNGQSPPEKPKLVKCRSPGKETFTCWWEPGADGGLPTNYTLTYHKEGETLIHECPDYKTGGPNSCYFSKKHTSIWKMYVITVNAINQMGISSSDPLYVDVTYIVEPEPPANLTLELKHPEDRKPYLWIKWSPPTMTDVKSGWFIIQYEIRLKPEKATDWETHFTPKQTQLKIFNLYPGQKYLVQIRCKPDHGYWSEWSPESSIQIPNDFPVKDTSMWIFVAILSAVICLIMVWAVALKGYSMVTCILPPVPGPKIKGFDVHLLEKGKSEELLRALESQDFPPTSDCEDLLMEFIEVDDCEDQQLMPRPSKEHTEQGVKPMHLDLDSDSGRGSCDSPSLLSEKCDEPQAHPSKFHTPEGPEKLENPETNLTCLQAPQSTSGEGKIPYFLANGPKSSTWPFPQPPSLYSPRYSYHNIADVCELALGMAGTTATSLDQTDQHALKASKTIETGREGKATKQRESEGCSSKPDQDTVWPRPQDKTPLISAKPLEYVEIHKVSQDGVLALFPKQNEKFGAPEASKEYSKVSRVTDSNILVLVPDPQAQNLTLLEEPAKKAPPALP
Protein: IP01015p (Poils au dos) (Q9VEW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAAAGSNVRCINYYDLCRICTDSSDHKTNIYSPEGRAKNLSQKILECLSLQIDEKDRLPKVVCAQCVQLVEQIHGLRATCRNSQTMLNNCLNIRPAPSSDKLYIRDAVDETGKSLSVAQSAPPVPNGAQQSGNLLNSIIQAVNMQPQQQYTITMDNGVQQQQQQHQAMPEVQIKSERQTALEEFIRLKPDIKITPLGKKEPISPAKPQQQHSLQSQTVTPTINPTQLQLQPQLGDQLQPLWQQIQQLQLQQQLQQLTNQLQATTQYSVAQDDTSSSGDSKKPKLNFVLSSPTAPQFTTSMPQFGGSQPQIQLQLMPGSGGVTSAGTVPAQTQLNAAALLSSLAGPQSTTNLLSPNKCFLPITIRDENSDQQIVAHIDTKNLVLPTTYQVQMKLQPQLATADGQPIMQLTPTSIPATLQLTPQTLGNPGSAFQGTTVTQNQFLAPQQPLTQLPNTAQVTSQQIIRSPHTSTTNSQLVIRNVTNIPPTPTTPTSSKKAPTFKTPSPKQKPMPSPKSKTTVGPSSGGSNGTSTNEFKRLITQTKPQPQVKQQQTAGLSASGAPTATSANQAAMQRLSSNTTITKVPKQPASLPAPAPTSNPAKLPMLNKQNITISRISMQTAPKAQSKPSTTSPTPASQPIPVSVPALSQAQPPPLAAQHKKIVRKPPENQDTSGQKVKAARPPQQILPSPQQEGQNATHSGSEAPTTSGLICPTCKREFKKKEHLTQHVKLHAGLRPFKCSEEGCDKTFSRKEHLSRHLVSHSGQKMYTCEVCKKPFSRKDNLNKHRRIHTQTSTETLYCCDVCNKNFATKLHYEKHREMHKKIRPESAAPGATASPAAAPALTHVRSNGQVPNKAVFEIKQERSAQQTQTQQPPAQVMHVVTTQDLAGNTITITQAPDSNMPGSLANYVQLGFSQFQNPSASVAK
Protein: mRNA-decapping enzyme 1B (EC 3.6.1.62) (Q8IZD4)
Organism: Homo sapiens (Human)
Function: May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15067023}. Nucleus {ECO:0000250|UniProtKB:Q9NPI6}.
Interaction partners:
- m7GpppN-mRNA hydrolase
- Enhancer of mRNA-decapping protein 3
- Probable ATP-dependent RNA helicase DDX6
- 5'-3' exoribonuclease 1
- Enhancer of mRNA-decapping protein 4
- mRNA-decapping enzyme 1A
- Protein LSM14 homolog A
- Serine/threonine-protein kinase pim-1
- Protein PAT1 homolog 1
- Regulator of nonsense transcripts 1
Sequence:
MAAVAAGGLVGKGRDISLAALQRHDPYINRIVDVASQVALYTFGHRANEWEKTDVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQLQDPFLLYRNARLSIYGIWFYDKEECQRIAELMKNLTQYEQLKAHQGTGAGISPVILNSGEGKEVDILRMLIKAKDEYTKCKTCSEPKKITSSSAIYDNPNLIKPIPVKPSENQQQRIPQPNQTLDPEPQHLSLTALFGKQDKATCQETVEPPQTLHQQQQQQQQQQEKLPIRQGVVRSLSYEEPRRHSPPIEKQLCPAIQKLMVRSADLHPLSELPENRPCENGSTHSAGEFFTGPVQPGSPHNIGTSRGVQNASRTQNLFEKLQSTPGAANKCDPSTPAPASSAALNRSRAPTSVTPVAPGKGLAQPPQAYFNGSLPPQTVGHQAHGREQSTLPRQTLPISGSQTGSSGVISPQELLKKLQIVQQEQQLHASNRPALAAKFPVLAQSSGTGKPLESWINKTPNTEQQTPLFQVISPQRIPATAAPSLLMSPMVFAQPTSVPPKERESGLLPVGGQEPPAAATSLLLPIQSPEPSVITSSPLTKLQLQEALLYLIQNDDNFLNIIYEAYLFSMTQAAMKKTM
Protein: Voltage-gated potassium channel KCNC4 (KSHIIIC) (Potassium voltage-gated channel subfamily C member 4) (Voltage-gated potassium channel subunit Kv3.4) (Q03721)
Organism: Homo sapiens (Human)
Function: This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Ubiquitin-like protein FUBI
- Potassium voltage-gated channel subfamily E member 3
- Voltage-gated potassium channel KCNC1
- Voltage-gated potassium channel subunit beta-2
- Potassium voltage-gated channel subfamily E member 4
- Voltage-gated potassium channel subunit beta-1
- Voltage-gated inwardly rectifying potassium channel KCNH2
- Voltage-gated potassium channel subunit beta-3
- Voltage-gated potassium channel KCNC3
- Potassium voltage-gated channel subfamily E member 1
Sequence:
MISSVCVSSYRGRKSGNKPPSKTCLKEEMAKGEASEKIIINVGGTRHETYRSTLRTLPGTRLAWLADPDGGGRPETDGGGVGSSGSSGGGGCEFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELTFWGIDETDVEPCCWMTYRQHRDAEEALDIFESPDGGGSGAGPSDEAGDDERELALQRLGPHEGGAGHGAGSGGCRGWQPRMWALFEDPYSSRAARVVAFASLFFILVSITTFCLETHEAFNIDRNVTEILRVGNITSVHFRREVETEPILTYIEGVCVLWFTLEFLVRIVCCPDTLDFVKNLLNIIDFVAILPFYLEVGLSGLSSKAARDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGARPSDPRGNDHTDFKNIPIGFWWAVVTMTTLGYGDMYPKTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKRKKHVPRPAQLESPMYCKSEETSPRDSTCSDTSPPAREEGMIERKRADSKQNGDANAVLSDEEGAGLTQPLASSPTPEERRALRRSTTRDRNKKAAACFLLSTGDYACADGSVRKGTFVLRDLPLQHSPEAACPPTAGTLFLPH
Protein: FK506-binding protein-like (WAF-1/CIP1 stabilizing protein 39) (WISp39) (Q9UIM3)
Organism: Homo sapiens (Human)
Function: May be involved in response to X-ray. Regulates p21 protein stability by binding to Hsp90 and p21.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Ankyrin repeat domain-containing protein 49
- Cyclin-dependent kinase inhibitor 1
- G2 and S phase-expressed protein 1
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Estrogen receptor
Sequence:
METPPVNTIGEKDTSQPQQEWEKNLRENLDSVIQIRQQPRDPPTETLELEVSPDPASQILEHTQGAEKLVAELEGDSHKSHGSTSQMPEALQASDLWYCPDGSFVKKIVIRGHGLDKPKLGSCCRVLALGFPFGSGPPEGWTELTMGVGPWREETWGELIEKCLESMCQGEEAELQLPGHSGPPVRLTLASFTQGRDSWELETSEKEALAREERARGTELFRAGNPEGAARCYGRALRLLLTLPPPGPPERTVLHANLAACQLLLGQPQLAAQSCDRVLEREPGHLKALYRRGVAQAALGNLEKATADLKKVLAIDPKNRAAQEELGKVVIQGKNQDAGLAQGLRKMFG
Protein: Myosin light chain 1/3, skeletal muscle isoform (MLC1/MLC3) (MLC1F/MLC3F) (Myosin light chain alkali 1/2) (Myosin light chain A1/A2) (P02600)
Organism: Rattus norvegicus (Rat)
Function: Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function.
Interaction partners:
- Myosin regulatory light chain 11
- Troponin I, fast skeletal muscle
- Nebulin
- Troponin T, fast skeletal muscle
- Actin, alpha skeletal muscle
- Myosin-4
- Troponin I, cardiac muscle
- Troponin T, cardiac muscle
- Troponin I, slow skeletal muscle
- Tropomyosin alpha-1 chain
Sequence:
MAPKKDVKKPAAAAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQEEFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMMQAISNNKDQGGYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQEDSNGCINYEAFVKHIMSV
Protein: Secreted frizzled-related protein 1 (sFRP-1) (Q8C4U3)
Organism: Mus musculus (Mouse)
Function: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vascular cells, in vitro and in vivo, and can induce, in vivo, an angiogenic response. In vascular cell cycle, delays the G1 phase and entry into the S phase. In kidney development, inhibits tubule formation and bud growth in metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF-dependent transcription (By similarity).
Subcellular location: Secreted {ECO:0000250}. Note=Cell membrane or extracellular matrix-associated. Released by heparin-binding (By similarity). {ECO:0000250}.
Interaction partners:
- Proto-oncogene Wnt-1
- Protein Wnt-3a
- Protein Wnt-5a
- Protein Wnt-2
- Protein Wnt-4
- Frizzled-2
- Protein Wnt-7b
- Protein Wnt-5b
- Protein Wnt-16
- Protein Wnt-2b
Sequence:
MGVGRSARGRGGAASGVLLALAAALLAAGSASEYDYVSFQSDIGSYQSGRFYTKPPQCVDIPVDLRLCHNVGYKKMVLPNLLEHETMAEVKQQASSWVPLLNKNCHMGTQVFLCSLFAPVCLDRPIYPCRWLCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEGDVCIAMTPPNTTEASKPQGTTVCPPCDNELKSEAIIEHLCASEFALRMKIKEVKKENGDKKIVPKKKKPLKLGPIKKKELKRLVLFLKNGADCPCHQLDNLSHNFLIMGRKVKSQYLLTAIHKWDKKNKEFKNFMKRMKNHECPTFQSVFK
Protein: Serine/threonine-protein kinase STY8 (EC 2.7.11.1) (Serine/threonine/tyrosine-protein kinase 8) (O22558)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine protein kinase that specifically phosphorylates chloroplast precursor proteins in the cytosol within the cleavable presequences (transit peptides). May be part of a cytosolic regulatory network involved in chloroplast protein import. Does not phosphorylate mitochondrion precursor proteins. Specific for ATP and does not utilize other NTPs. Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17090544, ECO:0000269|PubMed:21799034}.
Interaction partners:
- AT5g22320/MWD9_11
- AT4g30010/F6G3_40
- AT5g25280/F18G18_20
Sequence:
MTIKDESESCGSRAVVASPSQENPRHYRMKLDVYSEVLQRLQESNYEEATLPDFEDQLWLHFNRLPARYALDVKVERAEDVLTHQRLLKLAADPATRPVFEVRSVQVSPRISADSDPAVEEDAQSSHQPSGPGVLAPPTFGSSPNFEAITQGSKIVEDVDSVVNATLSTRPMHEITFSTIDKPKLLSQLTSLLGELGLNIQEAHAFSTVDGFSLDVFVVDGWSQEETDGLRDALSKEILKLKDQPGSKQKSISFFEHDKSSNELIPACIEIPTDGTDEWEIDVTQLKIEKKVASGSYGDLHRGTYCSQEVAIKFLKPDRVNNEMLREFSQEVFIMRKVRHKNVVQFLGACTRSPTLCIVTEFMARGSIYDFLHKQKCAFKLQTLLKVALDVAKGMSYLHQNNIIHRDLKTANLLMDEHGLVKVADFGVARVQIESGVMTAETGTYRWMAPEVIEHKPYNHKADVFSYAIVLWELLTGDIPYAFLTPLQAAVGVVQKGLRPKIPKKTHPKVKGLLERCWHQDPEQRPLFEEIIEMLQQIMKEVNVVV
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (Q8DTS9)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). Binds plasminogen and human salivary mucin MG2 when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity that may help the dissemination through oral tissues and entrance into the blood stream.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15501816}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15501816}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15501816}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface (PubMed:15501816). Once secreted, it remains attached to the cell surface (PubMed:15501816). {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15501816}.
Interaction partners:
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Pyruvate kinase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Fructose-bisphosphate aldolase
- ATP-dependent 6-phosphofructokinase
- phosphoenolpyruvate carboxykinase
- Transketolase
Sequence:
MSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGASTGEHEAVELRDGDKSRYGGLGTQKAVDNVNNIIAEALIGYDVRDQQAIDKAMIALDGTPNKGKLGANAILGVSIAVARAAADFLEIPLYSYLGGFNTKVLPTPMMNIINGGSHSDAPIAFQEFMIVPAGAPTFKEALRWGAEIFHALKKILKERGLETAVGDEGGFAPKFDGTEDAVETIIKAIETAGYKPGEEVFLGFDCASSEFYDNGVYDYTKFEGEKGAKRSAAEQIDYIEELVNKYPIITIEDAMDENDWDGWKALTARLGDRVQLVGDDFFVTNTDYLARGIKEGAANSILIKVNQIGTLTETFEAIEMAKEAGYTAVVSHRSGETEDSTIADISVATNAGQIKTGSLSRTDRIAKYNQLLRIEDQLGEVAEYRGLKSFYNLKK
Protein: Insulin-like growth factor 2 (Q2F6J2)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGITAGKSVLVLLAFLAFASCCYAAYRPSETLCGGELVDTLQFVCGDRGFYF
Protein: Versicolorin B desaturase stcL (EC 1.14.19.n5) (Cytochrome P450 60B) (Cytochrome P450 monooxygenase stcL) (Sterigmatocystin biosynthesis cluster protein L) (Q00707)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Norsolorinic acid synthase stcA
- FAD-binding monooxygenase stcW
- Versicolorin reductase stcU
- Glutathione S-transferase stcT
- Oxidoreductase stcQ
Sequence:
MAFLSLPILTALGAVVYVLFQLVYNLYFHPLRDYPGPLLWRASSLPWKLTLLRGTMHHDLMRHHQTYGDTVRIKPDEISYANGQAWRDIHAHVPGRPEFLKDPVRLPLAPNGVMSILVSDTRNHARFRSLFGHAFSDKGLRAQEPTIARYADLLVEVLREVADTGKSVEMVRYFNMAIFDSIGALSFGESFDSLRNRELHPWVDTIHKNLKSVAISHVLRSMGVEFLAPYLMPAELRGKRQENYTYAIEKLKKRMQKTGDQGDFWDRVIVKSADGNQSGDGMSYGEMINNAAVMVVAGSETTSSALCGCTYLLCKFDKMDKAVAEVRGAFAAADQIDLVSVSRLPYLTAVIDETLRMYPSVPGQPPRVVPEGGAIVCGRFVPAETRVGVSHLGAYYAPYNFSHADKFIPERHLAGAKLEEPFRHDNYAAYQPWSVGVRNCIGRNLAYAEVRLTLAKLLWHFDISLDEERTGNFLDQKIWSIWAKRELYLEIRTREF
Protein: 14-3-3 protein homolog (O42766)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Transcription factor SKN7
- Cell division control protein 42 homolog
- M-phase inducer phosphatase
- Serine/threonine-protein kinase CST20
- Phosphatase
- Serine/threonine-protein kinase TOR
- Phosphatidylinositol 4-kinase PIK1a
- Tsc2p
- Rab GDP dissociation inhibitor
- Glyceraldehyde-3-phosphate dehydrogenase
Sequence:
MPASREDSVYLAKLAEQAERYEEMVENMKAVASSGQELSVEERNLLSVAYKNVIGARRASWRIVSSIEQKEEAKGNESQVALIRDYRAKIEAELSKICEDILSVLSDHLITSAQTGESKVFYYKMKGDYHRYLAEFAIAEKRKEAADLSLEAYKAASDVAVTELPPTHPIRLGLALNFSVFYYEILNSPDRACHLAKQAFDDAVADLETLSEDSYKDSTLIMQLLRDNLTLWTDLSEAPAATEEQQQSSQAPAAQPTEGKADQE
Protein: TANK binding kinase 1 (A0A494C167)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGLIYEKISLPKVHPRYDLDGDASMAKAITGVVCYACRIASTLLLYQELMRKGIRWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEKLMKINLEAAELGEISDIHTKLLRLSSSQGTIETSLQDIDSRLSPGGSLADAWAHQEGTHPKDRNVEKLQVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMTHFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNELQETLPQKMFTASSGIKHTMTPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL
Protein: Probable FAD-dependent monooxygenase kojA (EC 1.14.13.-) (Kojic acid biosynthesis cluster protein A) (Q2U5I0)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Probable FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of 5-hydroxy-2-hydroxymethyl-1,4-pyrone, also know as kojic acid, a by-product in the fermentation process of malting rice that acts as a chelation agent. Glucose might be converted to kojic acid by a combination of dehydrogenase and dehydratase reactions involving kojA and probably additional enzymes.
Interaction partners:
- Transcription factor kojR
- MFS-type transporter kojT
Sequence:
MRVATQLRVGIVGGGWNGCHLALELKKQGHRVSLFEQKPDIFQGVSGNFGIRLHKGPHYPRSKATRDSCREALVKFCETYPELVVHHESAIYAHGEADALGNPSKVSDEAFRDVCYESPECTAVDPKANGFQGLISAYNLDEPSVAIGDRLRNTFKEKLGRAGIYVHLNATVDRIIHTEDTNRIQTGDGQYVFDVVINATGYTSLLPQNIADALPVDIGITYQTCIALVYEDQQPQEKPLSFIVMDGWFPCVMPAIDTNEPLQKKYILTHGSYTILGSFDRHEEGQELLDSLDEEAIAARIKPHCEREITRFWPGFLDRFQYRGWKGSVLAKLKTTSEFRSSLTFEKDGVIHIFPGKVSNVVTAAEEVVPLINDIARRRHGVVREWNGVRFTVSSAFHTHSKEIGDKPGLGEHHTSNLQTYVSLVTAN