wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidate cytidylyltransferase 1 (EC 2.7.7.41) (CDP-DAG synthase 1) (CDP-DG synthase 1) (CDP-diacylglycerol synthase 1) (CDS1) (CDP-diglyceride pyrophosphorylase 1) (CDP-diglyceride synthase 1) (CTP:phosphatidate cytidylyltransferase 1) (O04928)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the synthesis of minor phospholipids and in modulation of IP3-mediated signal transduction.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- Cardiolipin synthase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 1, chloroplastic/mitochondrial
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- Phosphatidate phosphatase PAH1
- Diacylglycerol kinase 5
- Triacylglycerol lipase SDP1
- Choline/ethanolaminephosphotransferase 1
Sequence:
MEEENVTSSPSTPVHRLRHRRRSNEVVTDGDKVNASPLLVNDRNKYKSFMVRTYSTLWMIGGFVLVVYMGHLYITAMVVVIQIFMAKELFNLLRKAPEDKCLPYIKQLNWHFFFTAMLFVYGRILSQRLANTMTADQFFYRLVSGLIKYHMAICYLLYIIGFMWFILTLKKKMYKYQFGQYAWTHMILIVVFTQSSFTVANIFEGIFWFLLPASLIIINDIFAYIFGFFFGRTPLIKLSPKKTWEGFIGASVTTIISAFVLANILGRFPWLTCPRQDLSTGWLQCDADPLFKPEPFALPAWIPEWFPWKEMTILPVQWHALCLGLFASIIAPFGGFFASGFKRAFKIKDFGDSIPGHGGITDRMDCQMVMAVFAYIYLQSFIVSQSVSVDKILDQILTNLTFEEQQALFVKLGQMLKDKLS
Protein: Photosystem II reaction center proteins PsbY, chloroplastic (L-arginine-metabolizing enzyme) (L-AME) [Cleaved into: Photosystem II reaction center protein PsbY-1, chloroplastic (PsbY-A1); Photosystem II reaction center protein PsbY-2, chloroplastic (PsbY-A2)] (O49347)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PSBY-1 and -2 are manganese-binding polypeptides with L-arginine metabolizing enzyme activity. They are a component of the core of photosystem II.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:9829828}; Multi-pass membrane protein. Note=Imports into spinach thylakoid membranes. {ECO:0000269|PubMed:9829828}.
Interaction partners:
- Photosystem II reaction center W protein, chloroplastic
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Expressed protein
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I reaction center subunit III, chloroplastic
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I subunit O
- Chlorophyll a-b binding protein
- Chlorophyll a-b binding protein CP26, chloroplastic
- Oxygen-evolving enhancer protein 2-1, chloroplastic
Sequence:
MAAAMATATKCMSLNPSPPKLQNQTKSKPFISLPTPPKPNVSLAVTSTALAGAVFSSLSYSEPALAIQQIAQLAAANASSDNRGLALLLPIVPAIAWVLYNILQPAINQVNKMRESKGIVVGLGIGGGLAASGLLTPPPEAYAAAEAAAASSDSRGQLLLIVVTPALLWVLYNILQPALNQINKMRSGD
Protein: Neutrophil cytosol factor 2 (NCF-2) (67 kDa neutrophil oxidase factor) (NADPH oxidase activator 2) (Neutrophil NADPH oxidase factor 2) (p67-phox) (P19878)
Organism: Homo sapiens (Human)
Function: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Neutrophil cytosol factor 4
- Ras-related C3 botulinum toxin substrate 1
- NADPH oxidase 1
- NADPH oxidase 2
- Ras-related C3 botulinum toxin substrate 2
- Neutrophil cytosol factor 1
- Cytochrome b-245 light chain
- NADPH oxidase organizer 1
- NADPH oxidase 4
- NADPH oxidase activator 1
Sequence:
MSLVEAISLWNEGVLAADKKDWKGALDAFSAVQDPHSRICFNIGCMYTILKNMTEAEKAFTRSINRDKHLAVAYFQRGMLYYQTEKYDLAIKDLKEALIQLRGNQLIDYKILGLQFKLFACEVLYNIAFMYAKKEEWKKAEEQLALATSMKSEPRHSKIDKAMECVWKQKLYEPVVIPVGKLFRPNERQVAQLAKKDYLGKATVVASVVDQDSFSGFAPLQPQAAEPPPRPKTPEIFRALEGEAHRVLFGFVPETKEELQVMPGNIVFVLKKGNDNWATVMFNGQKGLVPCNYLEPVELRIHPQQQPQEESSPQSDIPAPPSSKAPGRPQLSPGQKQKEEPKEVKLSVPMPYTLKVHYKYTVVMKTQPGLPYSQVRDMVSKKLELRLEHTKLSYRPRDSNELVPLSEDSMKDAWGQVKNYCLTLWCENTVGDQGFPDEPKESEKADANNQTTEPQLKKGSQVEALFSYEATQPEDLEFQEGDIILVLSKVNEEWLEGECKGKVGIFPKVFVEDCATTDLESTRREV
Protein: Uncharacterized protein (Q38CJ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSVGFPCDMNTSSSLTFLANFYFHTKNGVDKNVRTTDRSRMEFWVQRLPTVILQEIFMEVIRSDGFCFAWVGILSSVCRSWYCACQHPVMWAFMAKKVFVAYPLVLRAQAVPEDKTNLRMRSVSNPIIDDADDFGTVSNSRDAMELPTLMTNQSLRRAIEDVRLFDERRSYHTYVRQIRVLVLGMMLSGTLLLFSMFLFVTVCVLEGIKLGGVFTTYAALSFLWATYWGIFTIIIANIVMEAHFEPTPLFPRLRKNKPLILTSTAILLIGLFTLVLPTLLVHINLTREEKFSWMWCGATPLLFLLSWQLYVVLSCFSPSKWGELLRSPHVVLRPMKVVMSLILNIPHAFPFCCAVALYSLLQYIQYGGRTYLLVAVFPLLASLPILSTLLLLDFYMKRQMRDLLTGVSLLLASIFPLSLFWTDFRGFSLLPLAAASLLLFITHFRQVAQQSMLELVEEIQRNRRPARWRRSHSVRM
Protein: Myb-related transcription factor, partner of profilin (Myb-related protein p42POP) (Partner of profilin) (Q8R4U1)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor; DNA-binding protein that specifically recognizes the core sequence 5'-YAAC[GT]G-3'. Dimerization with PFN1 reduces its DNA-binding capacity.
Subcellular location: Nucleus {ECO:0000269|PubMed:15615774}.
Interaction partners:
- Profilin-1
Sequence:
MASATAAAAPGEAEETTRLRKPRFSFEENQILIREVRAHYPQLYGAQSRRVSVAERRRVWDSIATKINGITSWKRTGQEVQKRWNDFKRRTKEKLARVPHSTQGAGPAAEDAFSAEEETIFAILGPGVAGPGAGSGAEESRAAASSQPQASTASTQRYVLSEDRRQDRRADTPAQSKGGSSSPESWARPSCNPQEAKERESTSPAAMQPVQLPRLALSPPLPAPPPPPTALAQVAPSSPSPTPPRPTSAPEQSLDFLRAQQETANAIRELAGTLRQGLAKLSEALSALLPLLPGTPADPLPPPPPPPPPPPPKPVLPPSAPKVELAPEPVSVVAAVVDGAVVAARGVIISPRSEEGVPKPLPPAPPLPLHDSPPHKRRKGFPTRKRRGRWKSP
Protein: Gluconolactonase (Q8P3F8)
Organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Interaction partners:
- Gluconolactonase
- Glucose dehydrogenase
- Glucose dehydrogenase
- 2-hydroxyacid dehydrogenase
- Gluconokinase
- Glucose-fructose oxidoreductase
- Ribonuclease G
Sequence:
MRLSLLMLLVIPLLALLSACTKSNAPPSRYPAIGHLESFHASFSDVVATDARIEKLTEGFTWSEGPTWVRQGGYLLFTDVPENKLYRWSDDSGLSVFLSPSGYAGTDVAALREAGANGLFAEPGGTVLLADSGTRIVARLDPATRTKTPLATSFDGKRFNSPNDVVRRKDGVVFFTDPPYGLKGMNDSPVKELRFNGVYRLDTDGSVHLLDDSLSFPNGIALSPDQRTLYVANSDPARPIWMAYALDAQGAVTGKRVFADATDLVNKDTPGLPDGMAVSADGRLFATGPGGVIVFDPDGRRLGRIETGAAISNCAFGNDGHTLYMTSHALLARVKVTSLGLEFAR
Protein: Phosphoenolpyruvate carboxylase family protein (Putative carboxyphosphonoenolpyruvate mutase) (Q8GYI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Malate synthase
- Acetolactate synthase, chloroplastic
- 2-hydroxyacyl-CoA lyase
Sequence:
MAALSFCSSSPPRILHKQSKSSFFPSSASSSFTQTVGELFANPFSVSRRFRGAVNSTVVSDESGNAKLPSSPAKKLRNIMQSPGVLQGPCCFDALSAKLIERAGFPYCITSGFSISASRLGLPDKGLISYGEMVDQGQQITQSVSIPVIGDGGNGYGNAMNVKRTVKGYIKAGFAGIIINDEVCCENTKSERRVVSREEAVMRVKAAVDARRECDSDIVIVAQTDSREAISLEESLIRARAFTDAGADVLSVDSLVSREEMKAFCNVYPLVPKLANMLESGGKIPILNPLELEEIGYKLVAYPISLIGVSIQAMQDALLAIKGGRIPPPGSMASLEEIGEILGFDTYEEEEKRYATSSSDREVSSSSVYRNQRVAKDDPEQREDLIVEVITPEVYNEPRNPFSRIWSRSLRIKIIGRDGFEKLDVRIPAGFLEGVTNIVPALGGVNLKQLMDDAADEVGGKILLDFKDTAGDRIQVFLE
Protein: Coatomer subunit delta (Q9W555)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Cytoplasmic side {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Cytoplasmic side {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}.
Interaction partners:
- Coatomer subunit alpha
- Coatomer subunit beta
- Coatomer subunit zeta
- Coatomer subunit gamma
- Coatomer subunit epsilon
- Coatomer subunit beta'
- ADP-ribosylation factor GTPase activating protein 3, isoform H
- Transmembrane emp24 domain-containing protein bai
- Centromere/kinetochore protein zw10
- Protein transport protein Sec31A
Sequence:
MVLIAAAVCTKNGKVILSRQFVEMTKARIEGLLAAFPKLMTAGKQHTYVETDSVRYVYQPMEKLYMLLITTKASNILEDLETLRLFSKVIPEYSHSLDEKEIVENAFNLIFAFDEIVALGYRESVNLAQIKTFVEMDSHEEKVYQAVRQTQERDARQKMREKAKELQRQRMEASKRGGPSLGGIGSRSGGFSADGIGSSGVSSSSGASSANTGITSIDVDTKSKAAASKPASRNALKLGGKSKDVDSFVDQLKNEGEKIANLAPAAPAGGSSAAASASAAAKAAIASDIHKESVHLKIEDKLVVRLGRDGGVQQFENSGLLTLRITDEAYGRILLKLSPNHTQGLQLQTHPNVDKELFKSRTTIGLKNLGKPFPLNTDVGVLKWRFVSQDESAVPLTINCWPSDNGEGGCDVNIEYELEAQQLELQDVAIVIPLPMNVQPSVAEYDGTYNYDSRKHVLQWHIPIIDAANKSGSMEFSCSASIPGDFFPLQVSFVSKTPYAGVVAQDVVQVDSEAAVKYSSESILFVEKYEIV
Protein: deoxyribonuclease II (EC 3.1.22.1) (Q2XP49)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MTASSVWCSPTLLLLLLFSPALWAAEISCRNEDGEAVDWFVLYKLPKHTKGGGTGLGLEYLYMDSLAQQWQLGRYLVNMTQGALGQTLGQLYKAYESKRNNTVYAIYNDEVPHSGSINGKRGHTKGFLLLDKSQGFWVIHSVPLFPPFPEDGYGYPASGESYGQTAICITFSYEQFIEIDQQMLSSNPEIYSCSLPDTFQADLPNLQKLCSGSRLPSGPLRRLSKLQSAHGEAFLHFAKSRSFVDDIYVAWVAQELKTDLLAESWQHSGQKLPSNCSLQYYVYNINLIGTPLNSTFHSILDHSKWSVSMKEEVQWTCIGDLNRAVEQAWRSGGFICTQNKHIYSAFRRLVINYESCNDASTWI
Protein: RBR-type E3 ubiquitin transferase (EC 2.3.2.31) (Q6IBL8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEARVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVGVSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQEPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKCNICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQAREALKKYLFYFERWENHNKSLQLEAQTYQRIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKCRYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAEQRRRTLLKDFHDT
Protein: BAR/IMD domain-containing adapter protein 2 (Brain-specific angiogenesis inhibitor 1-associated protein 2) (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase substrate protein p53) (Q6GMN2)
Organism: Rattus norvegicus (Rat)
Function: Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membrane ruffles. Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites (By similarity). {ECO:0000250}.
Interaction partners:
- Cell division control protein 42 homolog
- Wiskott-Aldrich syndrome protein family member
- Epidermal growth factor receptor kinase substrate 8
- Actin-binding protein WASF1
- small monomeric GTPase
- Ras-related C3 botulinum toxin substrate 1
- Abl interactor 1
- Vasodilator-stimulated phosphoprotein
- Protein diaphanous homolog 3
- Disks large homolog 4
Sequence:
MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTFAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKAFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPNKIPDRAAQLMQQMANSNGSILPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQENVPVMNGVAGADSEDYNPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLALPPPDYGTSSRAFPSQTAGTFKQRPYSVAVPAFSQGLDDYGARSVSRNPFANVHLKPTVTNDRSAPLLS
Protein: Oxygen-dependent coproporphyrinogen-III oxidase (COX) (Coprogen oxidase) (Coproporphyrinogenase) (EC 1.3.3.3) (P11353)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:3516695}.
Interaction partners:
- Uroporphyrinogen decarboxylase
- Protoporphyrinogen oxidase
- Porphobilinogen deaminase
- Uroporphyrinogen-III synthase
- Ferrochelatase, mitochondrial
- Delta-aminolevulinic acid dehydratase
- 5-aminolevulinate synthase, mitochondrial
- Eukaryotic translation initiation factor 5A-2
- Repressor ROX1
- C-4 methylsterol oxidase ERG25
Sequence:
MPAPQDPRNLPIRQQMEALIRRKQAEITQGLESIDTVKFHADTWTRGNDGGGGTSMVIQDGTTFEKGGVNVSVVYGQLSPAAVSAMKADHKNLRLPEDPKTGLPVTDGVKFFACGLSMVIHPVNPHAPTTHLNYRYFETWNQDGTPQTWWFGGGADLTPSYLYEEDGQLFHQLHKDALDKHDTALYPRFKKWCDEYFYITHRKETRGIGGIFFDDYDERDPQEILKMVEDCFDAFLPSYLTIVKRRKDMPYTKEEQQWQAIRRGRYVEFNLIYDRGTQFGLRTPGSRVESILMSLPEHASWLYNHHPAPGSREAKLLEVTTKPREWVK
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial (Complex I-ESSS) (NADH-ubiquinone oxidoreductase ESSS subunit) (Q57UT1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
Sequence:
MTGWNQKMAKMAFRRSKFRRLAWGDGDPYPYTPRATFRYQWDDWPLWEKIWHIGIGIVGVEFAMWAYYSKLNSRMDWAREEALRRMRLRREAQELMILEGEKFDSDIQPDRR
Protein: Non-specific phospholipase C3 (EC 3.1.3.106) (Q9SRQ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses specific phosphatase activity toward lysophosphatidic acid (LPA) in vitro. Does not show phospholipase C activity. May play a role in signal transduction and storage lipid synthesis. May be involved in brassinolide-mediated signaling in root development.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 7
- Glycerol-3-phosphate acyltransferase, chloroplastic
- Glycerol-3-phosphate acyltransferase 9
- Glycerol-3-phosphate acyltransferase 5
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5
- 1-acyl-sn-glycerol-3-phosphate acyltransferase 3
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4
- 1-acyl-sn-glycerol-3-phosphate acyltransferase 2
- Probable glycerol-3-phosphate acyltransferase 8
- Lysophospholipid acyltransferase 2
Sequence:
MVEETSSGGGSSASPIKTIVVLVQENRSFDHMLGWFKELNPEIDGVSESEPRSNPLSTSDPNSAQIFFGKESQNIDPDPGHSFQAIYEQVFGKPFSDESPYPDPKMNGFVQNAEAITKGMSEKVVMQGFPPEKLPVFKELVQEFAVCDRWFSSLPSSTQPNRLYVHAATSNGAFSNDTNTLVRGFPQRTVFESLEESGFTFGIYYQSFPNCLFYRNMRKLKYVDNFHQYHLSFKRHCKEGKLPNYVVIEPRYFKILSAPANDDHPKNDVVEGQNLVKEIYEALRASPQWNEILFVVVYDEHGGYYDHVPTPVIGVPNPDGLVGPEPYNFKFDRLGVRVPALLISPWIEPGTVLHEPNGPEPTSQFEHSSIPATLKKIFNLKSFLTKRDEWAGTLDAVINRTSPRTDCPVTLPELPRARDIDIGTQEEDEDLTDFQIELIQAAAVLKGDHIKDIYPFKLADKMKVLDAARYVEEAFTRFHGESKKAKEEGRDEHEIVDLSKGSTRHSTPKSFVQKLFSCLICDN
Protein: Aspartoacylase (EC 3.5.1.15) (Aminoacylase-2) (ACY-2) (Q9R1T5)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16935940}. Nucleus {ECO:0000269|PubMed:16935940}.
Interaction partners:
- N-acetylaspartate synthetase
- Glutamate carboxypeptidase 2
- Argininosuccinate synthase
- Aspartate aminotransferase, cytoplasmic
- Asparagine synthetase
- Isoaspartyl peptidase/L-asparaginase
- Aspartate aminotransferase, mitochondrial
- Amine oxidase
- Ribosomal modification protein rimK-like family member B.
- Amine oxidase
Sequence:
MTSCVAEEPIKKIAIFGGTHGNELTGVFLVTHWLKNGAEVHRAGLEVKPFITNPRAVEKCTRYIDCDLNRVFDLENLSKEMSEDLPYEVRRAQEINHLFGPKNSDDAYDVVFDLHNTTSNMGCTLILEDSRNDFLIQMFHYIKTCMAPLPCSVYLIEHPSLKYATTRSIAKYPVGIEVGPQPHGVLRADILDQMRRMLKHALDFIQRFNEGKEFPPCAIDVYKIMEKVDYPRNESGDVAAVIHPNLQDQDWKPLHPGDPVFVSLDGKVIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLNAKSIRSTLH
Protein: Opacity protein V28 (P11297)
Organism: Neisseria gonorrhoeae
Function: Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
Subcellular location: Cell outer membrane.
Interaction partners:
Sequence:
AGEDHGRGPYVQADLAYAYEHITHDYPEPTGTKKDKISTVSDYFRNIRTHSIHPRVSVGYDFGGWRIAADYARYRKWNDNKYSVDIKELENKNQNKRDLKTENQENGTFHAVSSLGLSAVYDFKLNDKFKPYIGARVAYGHVRHSIDSTKKTTKFLTSSYGGLNPTVYTEENTQNAHHQSNSIRRVGLGVIAGVGFDITPKLTLDAGYRYHNWGRLENTRFKTHEASLGVRYRF
Protein: Protein decapping 5 (Q9C658)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: As a component of the decapping complex, involved in the degradation of mRNAs. Promotes P-body formation. Translational repressor.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:19855049}.
Interaction partners:
- mRNA-decapping enzyme subunit 2
- mRNA-decapping enzyme-like protein
- Enhancer of mRNA-decapping protein 4
- DEAD-box ATP-dependent RNA helicase 6
- DEAD-box ATP-dependent RNA helicase 1
- DEAD-box ATP-dependent RNA helicase 12
- Cold shock domain-containing protein 3
- 5'-3' exoribonuclease 4
- Sm-like protein LSM1A
- Sm-like protein LSM1B
Sequence:
MAADNTGSKSSSAADSYVGSLISLTSKSEIRYEGILYNINTDESSIGLQNVRSFGTEGRKKDGPQVPPSDKVYEYILFRGTDIKDLQVKASPPVQPPASTINNDPAIIQSHYPSPMPTSGSLPSTASGSLPDISSHNGQPGQHGMGFQNAMPLYQPGGNLGSWGASPQPPMYWQGFYTPPPNGLPQLHQQSLIRPPHGLPMPNSLQQPLQYPNFNTPPPPTGSSSLQGSSLPEAPSSLFPFSTSSQMLAPSSLPFPGLPPVTLSSSLQSTLQSAPSPSLASEMAPPLLSNKAPITAPPTLPQDTNLLSFSLSTTRATEASTGLPLSNKPSVVTGPISPPQTTPLTSAPVAGVSSSISQDKPKPLLVTPGQLLQSGSSAVSLSPPSTNADKDVEVVQVSSSAGLEQSVPVTSEAQPPILPLPSSARPTQKPNGHSFPNHNGYRGRGRGRGRGAGRSHQVMKFTEDFDFTAMNEKFNKDEVWGHLGKSTTLDGDEDDDSPTVDEAELPKIEAKPVYNKDDFFDSLSSNTIDRESQNSRPRFSEQRKLDTETFGEFSRFRGGRGGRGGYGRNNGYSRGGYGGRGYGGYGGRGGGGGGYGYGGRGQGRGVSNRTT
Protein: LexA repressor (EC 3.4.21.88) (P44858)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
Sequence:
MRPLTARQQEVLDLLKRHLETTGMPPTRAEISRELGFKSANAAEEHLKALSRKGAIEIIPGASRGIRILDNSSNDEFDGLPLVGRVRAGEPILAEQHIEATYRVDADMFKPQADFLLKVYGLSMKNVGILDGDLLAVHSTKDVRNGQIVVARIEDEVTVKRLEKKGSIIYLHAENEEFDPIVVNLEEQKNFEIEGIAVGIIRNNAWM
Protein: Insulin-like growth factor-binding protein 6 (IBP-6) (IGF-binding protein 6) (IGFBP-6) (P35572)
Organism: Rattus norvegicus (Rat)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Activates the MAPK signaling pathway and induces cell migration.
Subcellular location: Secreted.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Insulin-like growth factor-binding protein 1
- Insulin-like growth factor-binding protein 3
- Insulin-like growth factor-binding protein complex acid labile subunit
- Insulin-like growth factor-binding protein 5
- Platelet-derived growth factor subunit A
- Platelet-derived growth factor subunit B
- Insulin-like growth factor 1 receptor
Sequence:
MTWDGLPTQPLLMLLMLLFAAGSESALAGCPGCGPGVQEEDAGSPADGCAETGGCFRREGQPCGVYIPKCAPGLQCQPRENEETPLRALLIGQGRCQRARGPSEETTKESKPHGGASRPRDRDRQKNPRTSAAPIRPSPVQDGEMGPCRRHLDSVLQQLQTEVFRGGANGLYVPNCDLRGFYRKQQCRSSQGNRRGPCWCVDPMGQPLPVSPDGQGSSQCSARSSG
Protein: POZ (BTB) and AT hook-containing zinc finger 1 (BTB/POZ domain zinc finger transcription factor) (Protein kinase A RI subunit alpha-associated protein) (Zinc finger and BTB domain-containing protein 19) (Zinc finger protein 278) (Q5NBY9)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator that plays a role in many biological processes such as embryogenesis, senescence, T-cell development or neurogenesis. Interacts with the TP53 protein to control genes that are important in proliferation and in the DNA-damage response. Mechanistically, the interaction inhibits the DNA binding and transcriptional activity of TP53/p53 (By similarity). Part of the transcriptional network modulating regulatory T-cell development and controls the generation of the regulatory T-cell pool under homeostatic conditions (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18241078}.
Interaction partners:
Sequence:
MERVNDASCGPSGCYTYQVSRHSTEMLHNLNQQRKNGGRFCDVLLRVGDESFPAHRAVLAACSEYFESVFSAQLGDGGAADGGPADVGGAAAAPGGGAGGSRELEMHTISSKVFGDILDFAYTSRIVVRLESFPELMTAAKFLLMRSVIEICQEVIKQSNVQILVPPARADIMLFRPPGTSDLGFPLDMTNGAAMAANSNGIAGSMQPEEEAARATGAAIAGQASLPVLPGVDRLPMVAGPLSPQLLTSPFPNVASSAPPLTSKRGRGRPRKANLLDSMFGSPGGLREAGILPCGLCGKVFTDANRLRQHEAQHGVTSLQLGYIDLPPPRLGENGLPISEDPDGPRKRSRTRKQVACEICGKIFRDVYHLNRHKLSHSGEKPYSCPVCGLRFKRKDRMSYHVRSHDGSVGKPYICQSCGKGFSRPDHLNGHIKQVHTSERPHKCQTCNASFATRDRLRSHLACHEDKVPCQVCGKYLRAAYMADHLKKHSEGPSNFCSICNRGFSSASYLKVHVKTHHGVPLPQVSRHQEPILNGGAAFHCARTYGNKEGQKCSHQDLIESSDSYGDLSDASDLKTPEKQSANGSFSCDVAVPKNKMESDGEKKYPCPECGSFFRSKSYLNKHIQKVHVRALGGPLGDLGPALGSPFSPQQNMSLLESFGFQIVQSAFASSLVDPEVDQQPMGPEGK
Protein: Probable glycosyltransferase STELLO2 (EC 2.4.-.-) (Q9SCN0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable glycosyltransferase regulating the assembly and trafficking of cellulose synthase complexes.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:27277162}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- NEDD8-like protein RUB3
- F12F1.16 protein
- Aconitate hydratase 1
- Aconitate hydratase 3, mitochondrial
- Aconitate hydratase 2, mitochondrial
- Aconitase family protein
- Protein MANNAN SYNTHESIS-RELATED 2
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin carboxyl-terminal hydrolase 3
- Mechanosensitive ion channel protein 1, mitochondrial
Sequence:
MLVQDRVAPKPPKSRIRELPSRDRFAEPKILDFSSWVSDNVYRIVIIFLFIVTVAAFFFLYNTTDTASLLCFQSQSTQSLQSLTRPQINWNSIQIVSDKTSPYASFRTEKWIVVSVTKHPTEELKGLVKIKGWQVLAIGNSLTPKDWNLKGAIFLSLDAQAELNYRILDHLPYDSFVRKSVGYLFAIQHGAKKIFDADDRGEVIDGDLGKHFDVELVGEDARQEPILQYSHENPNRTVVNPYIHFGQRSVWPRGLPLENVGEINHEEYYTEVFGGKQFIQQGISNGLPDVDSVYYSTRKTTFEPFDIRFDEHSPKVALPQGMMVPVNSFNTLYHSSAFWGLMLPVSVSSMASDVIRGYWGQRLLWELGGYVAVYPPTVHRYDRVEAYPFSDEKDLHINVGRLIKFLLAWRSNKHRFFETILDLSFVMAEQGFWTELDVKFTAAWLQDLLMVGYQQPRLMSLELDRPRATIGHGDRKEFVPRKLPSVHLGVEEIGTVSSEIGNLIKWRKNFGNVVLIMFCNGPVERTALEWRLLYGRIFKTVVILSSRKNSDLYVQEAKLDHIYKRLPKIFDRYSSADGFVFVEDDTVLNYWNLLQADKTKLWTTDKVTESWTTVRPAGNSDWYSVQAELVKKIVSTMPVHFQVNYKEATKNSDGTSLTMCSSEVFYVPKRFVSDFTDLVNLVGDMDLHYKVAVPMFFLSMDSPQNFDPVLGSMVYKSEPASLNSSLSLYSAEAPAVHPWSISNEQDFIKLVREMAEGDPLLMELV
Protein: Transcriptional regulator RedD (P16922)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: The RedD protein is probably one of several delicately balanced regulatory factors that contribute to the control of the biosynthesis of the antibiotic undecylprodigiosin (Red) in S.coelicolor.
Interaction partners:
- Response regulator
- Polyketide synthase RedX
- L-prolyl-[peptidyl-carrier protein] dehydrogenase
- Multi-domain regulatory protein
Sequence:
MTGGGVLATMDPVRKLVRSQPKIGRHPVAAGQDGRDRHPIRSWECGERARTARTGRTVGRAADPSDHGPSLYNFGGCVEINILGPVSIDTSHSGGGIRAGKVRTLVATLAIDAGRAVSLADLVDELWGATPPDNVLNALQAHAARARKVLNERACPERAGGILRSVLGGYLLEIDPQCVDGNRFLRLVSQGAALLPADPTRAVELLETGLRLWRGPALIDAGEGRRCRGAAALFEERRLTALEDLISAMFLRGGEAQAIAMLQQLVAQYPLRERFCELLMVGLYRVGRQGDALESYRLARKRLDDELGVQPGALLRRRHAEILAQDPVLKVPSALWREPYAPADTSLLSA