wanglab/gogpt-training-data huggingface dataset:
Protein: Snaclec alboluxin subunit beta (P0DJL1)
Organism: Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops albolabris)
Function: Potent platelet activator that aggregates platelets via both GPIb (GP1BA/GP1BB) and GPVI (GP6). Alboluxin induces a tyrosine phosphorylation profile in platelets that resembles those produced by collagen and convulxin, involving the time dependent tyrosine phosphorylation of Fc receptor gamma chain (FCGR1A), phospholipase Cgamma2 (PLCG2), LAT and p72SYK. Inhibition of alpha-IIb/beta-3 reduces the aggregation response to alboluxin, as well as tyrosine phosphorylation of platelet proteins, showing that activation of alpha-IIb/beta-3 and binding of fibrinogen are involved in alboluxin-induced platelet aggregation and it is not simply agglutination.
Subcellular location: Secreted.
Interaction partners:
Sequence:
NFSCPPDWYAYD
Protein: ATP synthase subunit beta-2, mitochondrial (EC 7.1.2.2) (P83484)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022}. Mitochondrion inner membrane {ECO:0000305}. Note=Peripheral membrane protein. {ECO:0000305}.
Interaction partners:
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit delta', mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit 9
- ATP synthase subunit O, mitochondrial
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit alpha, chloroplastic
- ATP synthase subunit alpha
- ATP synthase subunit b, chloroplastic
Sequence:
MASRRVLSSLLRSSSGRSAAKLVNRNPRLPSPSPARHAAPCSYLLGRVAEYATSSPASSAAPSSAPAKDEGKKTYDYGGKGAIGRVCQVIGAIVDVRFEDQEGLPPIMTSLEVQDHPTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLGEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDEVVAKAEKIAKESAA
Protein: Y-box-binding protein 2-A (Cytoplasmic RNA-binding protein p56) (Frog Y-box protein 2) (FRG Y2) (Frog Y-box protein 2-A) (FRGY2a) (Messenger ribonucleoprotein particle 4) (mRNP4) (P21574)
Organism: Xenopus laevis (African clawed frog)
Function: Has a dual function in oocytes: as a DNA-binding protein, binds to the Y-box sequence (CTGATTGGCCAA) in the promoters of target genes to stimulate transcription. May also function at CCAAT-containing promoters that lack the consensus Y-box sequence. Also binds mRNA to promote accumulation of the transcripts it contributes to produce.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1729676}. Note=Either free or associated with ribonucleoprotein particles.
Interaction partners:
Sequence:
MSEAEAQEPEPVPQPESEPEIQKPGIAAARNQANKKVLATQVQGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKFLRSVGDGETVEFDVVEGEKGAEAANVTGPGGVPVKGSRFAPNRRRFRRRFYRPRADTAGESGGEGVSPEQMSEGERGEETSPQQRPQRRRPPPFFYRRRFRRGPRPNNQQNQGAEVTEQSENKDPVAPTSEALASGDDPQRPPPRRFRQRFRRPFRPRPAPQQTPEGGDGETKAESGEDPRPEPQRQRNRPYVQRRRRQGATQVAATAQGEGKAEPTQHPASEEGTPSDSPTDDGAPVQSSAPDPGIADTPAPE
Protein: Ankyrin repeat and SOCS box protein 6 (ASB-6) (Q9NWX5)
Organism: Homo sapiens (Human)
Function: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Cullin-5
- E3 ubiquitin-protein ligase NRDP1
- RING-box protein 2
- Elongin-B
- Elongin-C
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MPFLHGFRRIIFEYQPLVDAILGSLGIQDPERQESLDRPSYVASEESRILVLTELLERKAHSPFYQEGVSNALLKMAELGLTRAADVLLRHGANLNFEDPVTYYTALHIAVLRNQPDMVELLVHHGADVNRRDRIHESSPLDLASEEPERLPCLQRLLDLGADVNAADKHGKTALLHALASSDGVQIHNTENIRLLLEGGADVKATTKDGDTVFTCIIFLLGETVGGDKEEAQMINRFCFQVTRLLLAHGADPSECPAHESLTHICLKSFKLHFPLLRFLLESGAAYNCSLHGASCWSGFHIIFERLCSHPGCTEDESHADLLRKAETVLDLMVTNSQKLQLPENFDIHPVGSLAEKIQALHFSLRQLESYPPPLKHLCRVAIRLYLQPWPVDVKVKALPLPDRLKWYLLSEHSGSVEDDI
Protein: Large ribosomal subunit protein uL16m (54S ribosomal protein L16, mitochondrial) (Q9Y822)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P38064}.
Interaction partners:
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL2m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS12m
Sequence:
MALQQYNKFPFFFSGILGPTRLNGLQMPPIQTMVRWGHQYAPRSIRNQKAQKGRVPIPIGGSLRGTQLEWGEYGMRLKDRSIRFHAKQLETAEQILKRILKPIKAARVYTRFCCNVPVCVKGNETRMGKGKGAFEYWAARIPIGRVLFEIGGDGMRKELAEHALKQAAFHLPGKYEIIVKQTPKRLGTTLIHETPITTETSKMNYQEITSTTTAV
Protein: Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) (P49843)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (By similarity). Affects inflammatory responses, cellular proliferation and differentiation in target tissues (By similarity). Involved in chromatin remodeling (By similarity). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). Mediates glucocorticoid-induced apoptosis (By similarity). Promotes accurate chromosome segregation during mitosis (By similarity). May act as a tumor suppressor (By similarity). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Note=After ligand activation, translocates from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:P04150}.
Interaction partners:
Sequence:
MDPGGLKHSKDKGLAFGKLSESSVEGSFSGDTGGSKSTTSTSLMHLPGSRPQPPARDSANGLNVTTTQMELSTGGLTIEEAEVKVMEKAIRMQQPQKPQQNQQLFENFALLEASIADLNRSNTPGSSVLGRPHDLFSLKTENFSPMDKDRLDMGSVSFGQSQKDLDVNERLLGDNTMDILQDLDLPGSLSDLNEFYVSDEAAFLSSLSVEDVLLEDGNMETKPIDCSNGGNCTNVDSADQQKQLLEAGVSMPVIKTEEDADTSFIQLCTPGVIKQENDRRSFCQISSLDLPSTHNSAGSISGPSYPYGANTSTAVSLQQDQKPVFGLYPPLPSVSDSWNRGNGYATGSGMSSSSFPVGFSSPKARPEASGSASSAPAKPSGPTHKICLVCSDEASGCHYGVLTCGSCKVFFKRAVEGWRARQNTDGQHNYLCAGRNDCIIDKIRRKNCPACRFRKCLQAGMNLEARKNKKLIRLKGQQTTMEPNPPPPDERACALIPKSMPQLVPTMLSLLKAIEPEAIYSGYDSTIPDTSTRLMTTLNRLGGQQVVSAVKWAKSLPGFRNLHLDDQMTLLQCSWLFLMSFGLGWRSYQQCNGGMLCFAPDLVINDERMKLPYMTDQCEQMLKISTEFVRLQVSYDEYLCMKVLLLLSTVPKDGLKSQAVFDEIRMTYIKELGKAIVKREENSSQNWQRFYQLTKLLDSMQEMVGGLLQICFYTFVNKSLSVEFPEMLAEIISNQLPKFKDGSVKPLLFHALNHDTMP
Protein: Phosphatidylinositol-binding clathrin assembly protein LAP (Like-AP180) (Q9VI75)
Organism: Drosophila melanogaster (Fruit fly)
Function: Assembly protein recruiting clathrin and adaptor protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction.
Subcellular location: Membrane, clathrin-coated pit {ECO:0000269|PubMed:9883738}. Golgi apparatus {ECO:0000269|PubMed:9883738}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:9883738}. Note=Colocalized with clathrin in the Golgi area.
Interaction partners:
- Cyclin-G-associated kinase
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
- Clathrin heavy chain
- AP-2 complex subunit alpha
- Huntingtin interacting protein 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Neuronal synaptobrevin, isoform J
- CIN85 and CD2AP related, isoform J
- Synaptobrevin
Sequence:
MTMAGQTINDRLLAARHSLAGQGLAKSVCKATTEECIGPKKKHLDYLVHCTNEPNVSIPHLANLLIERSQNANWVVVYKSLITTHHLMAYGNERFMQYLASSNSTFNLSSFLDKGTVQDGGMGVPGGRMGYDMSPFIRRYAKYLNEKSLSYRAMAFDFCKVKRGKEEGSLRSMNAEKLLKTLPVLQAQLDALLEFDCQSNDLSNGVINMSFMLLFRDLIRLFACYNDGIINLLEKYFDMNKKHARDALDLYKKFLVRMDRVGEFLKVAENVGIDKGDIPDLTKAPSSLLDALEQHLATLEGRKVSAANTPTQSSSSAFGTAAASSKFDTTNGIDEQLKAQVLAEEEAAMNQYKSKVSSPTSSGAAGASAALTNPFLSSPPAAQAGQPIVDLFGAASAQPAAAAAATKASDDLLQLGNPFADMFDASGGGAAAVGATGNAGDGTAKYDGGAGSSPFDWGATDDDGGAAQ
Protein: Probable vacuolar protein sorting-associated protein 16 homolog (Q6FKC4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome D complete sequence
- Vacuolar protein sorting-associated protein 41
- Candida glabrata strain CBS138 chromosome C complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- E3 ubiquitin-protein ligase PEP5
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Vacuolar fusion protein CCZ1
- Candida glabrata strain CBS138 chromosome C complete sequence
Sequence:
MASPSLHWEKLGDKFWRSKEVCQLNWFGGNNSSGDDTLEMSCSATCLSLFAIEVDNSVHVFDRTGHFITKTAIDQKFGKLVKLAFTEDEDLVLVYTNGVEILKDWNVSDKISVPLVVDVDDTIWDYKSGVLILRNSKDIYQLIDNKLVLLHKNTENYEILVKDGWDCKNGDVVILDLDSVWRFDLRSHHFKKIIAGCHYHRLYLSYNGQLCLYNGKGDRLDFYSLKGDDLNRNITLQKAPRDIKWDFEGNLSVLYEDELFLYNSQSQYVSFWYPYGIVLLEIFLDGILVVTTNQLSFVTQVKESTSSIFKIGSVTAGALLLDAFKELETNLPKAIENLRSIDLSTAVVDCLTASLEESDVKVQKQLLGAASFGKESLPYKSFDSSFFVSICNKLKILNFLNSIDFFITNDEYDYYKIEGILDMLLKMGKYYESIKLLELANRPDLKPKVFVQWCIVKIRVSSDLEDIKILDIINKQLSVLNTKNNVPMATIAGYSYSEGRFKLARELCKMEKLTPTKVAMLMKLEDYNIAVQECLHEGSCALTISLLLELKDKLPASQFTKLLILEMRDTQLFPYYEQDNYEFLYDYFRQIDEYKDLAHVLRRSVNKNLSLQSIQPQILELYNTIPHKTEHLKQDISLIQREVKRNQYMTEINNKLGTNFEREPLNDVLAKLIELKQDRVAKDLVKKFDIPERNFHITTLKVLVKQKRFEELSSFMTGIRPAISYQYIFDYIKKRGHKLEASEYISHLHVSYSDKMALYLECKNYRAAVELAGREKDVMGLKDVYAKIPANEPQVKALANQILATL
Protein: Cyclin-dependent kinase inhibitor 2C (Q8R5G4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- cyclin-dependent kinase
- Cyclin-dependent kinase 4
- G1/S-specific cyclin-D3
- G1/S-specific cyclin-D1
- G1/S-specific cyclin-D2
- Cellular tumor antigen p53
- Menin
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinase inhibitor 1
- Tumor suppressor ARF
Sequence:
MAEPWGNELASAAARGDLEQLTSLLQNNVNVNAQNGFGRTALQVMKLGNPEIARRLLLRGANPNLKDRTGFAVIHDAARAGFLDTVQALLEFQADVNIEDNEGNLPLHLAAKEGHLPVVEFLMKHTACNVGHRNHKGDTAFDLARFYGRNEVISLMEANGVGGATSLQ
Protein: Photosystem I reaction center subunit II (Photosystem I 16 kDa polypeptide) (PSI-D) (P19569)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center.
Interaction partners:
- Photosystem I reaction center subunit PsaK 2
- Photosystem I reaction center subunit PsaK 1
- Photosystem I reaction center subunit XI
- Iron stress-induced chlorophyll-binding protein
- Photosystem I reaction center subunit XII
- Photosystem I iron-sulfur center
- Photosystem I reaction center subunit IX
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I reaction center subunit III
Sequence:
MTELSGQPPKFGGSTGGLLSKANREEKYAITWTSASEQVFEMPTGGAAIMNEGENLLYLARKEQCLALGTQLRTKFKPKIQDYKIYRVYPSGEVQYLHPADGVFPEKVNEGREAQGTKTRRIGQNPEPVTIKFSGKAPYEV
Protein: Sec1 family transport protein, putative (Q38FX1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Golgi SNARE protein-like
- Syntaxin 5
- Vesicle-associated membrane protein, putative
- SNARE protein, putative
- Vesicle tethering protein Uso1/P115-like head domain-containing protein
- Longin domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- Synaptobrevin-type vesicle transport protein, putative
- Golgi vesicular membrane trafficking protein, putative
- Vesicle-fusing ATPase
Sequence:
MPPQRKISLRQRQRDVIQAMISSALPLGQGGVPAPQPMTATYGPAAVAPWRLLIYDDIGRDIIAPLLRVGDLRELGITLYMHIKSKRDPVPGAPAIYFCAPTDENINIMASDAVKEFYEWVYINFTSQISRRSMEHLAERLTRGQLQNIEHIRVFDRTLNYVALEDDLFTLMQKDSFVILNSRHAKDEDVEAHLNEIVMGILHVLLSQQVLPVIAHSRTGPAEEVARRLSVSLNDSLNERTLTPASANVLGRPLLLIVDRSSDLATVLHHPFSYRGLLAELGDMHLNKVTVLGDDGVETFFEINPDRDDFYRNNALLDFSAVGGNIEAALKRYREEHANLSESTCDVDGDVGTDSMSKLLANAPKLGEKKRMLDAHTKMAYSLLHRIRQTHLDRFHGVELGIIQQEGLDHEQFENLLLTGCGTAEDRQRLYLIAYLLGTQGEHETVLEQCAPAFEGMPFSALSYLKHLRQWSLGTANPTGGEADGAHGFAWGLAQTLAKNIVNSLGANSKSQLPLTKLVDSLLQDSSTSSGVGVGGSRAAGSSNLRAELLATVVGYDPRSRKQVDLNEAHFSQAIVFTIGGGCVAEYDDLKQWEAAHPRKAVSYGCTAMMTGNEALRQLTVLGEGIS
Protein: Myelin regulatory factor homolog 2 (EC 3.4.-.-) [Cleaved into: Myelin regulatory factor homolog 2, N-terminal; Myelin regulatory factor homolog 2, C-terminal] (D9PTN5)
Organism: Caenorhabditis elegans
Function: Constitutes a precursor of the transcription factor. Mediates the autocatalytic cleavage that releases the Myelin regulatory factor homolog 2, N-terminal component that specifically activates transcription of genes involved in synaptic rewiring during nervous system maturation.
Subcellular location: [Myelin regulatory factor homolog 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28441531}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:33950834}. Apical cell membrane {ECO:0000269|PubMed:33950834}; Single-pass membrane protein {ECO:0000255}. Note=In early L1 larvae, localizes to the cell membrane, but then localizes to the nucleus in late L1 larvae (PubMed:33950834). Cell membrane localization is promoted by pan-1 (PubMed:33950834). {ECO:0000269|PubMed:33950834}.; SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 2, N-terminal]: Nucleus {ECO:0000269|PubMed:28441531}. Cytoplasm {ECO:0000269|PubMed:28441531}. Note=Translocates from the cytoplasm to the nucleus upon autocatalytic cleavage. {ECO:0000269|PubMed:28441531}.; SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 2, C-terminal]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28441531}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putative iroquois-class homeodomain protein irx-1
Sequence:
MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTNLSPCQNPNMTNLFYITLLQNKLNKYTQQLLKKNEEGLNDPLANVEQFNIIQFLQNDVDFNLPIEAFEQGNMDQNIRIDPILQRQQMANQPMLMPQHMLQQLHQQQIYEQQLASMPMTPAITDLTRHGSSSSPSTTNSDPPYSPEGLNNFGLGTQRPNHGVIPNDISNVPQHINRQFNPRMGPNTSPNPPSFPQFLNSNHPTPGSYVQSISPDSNGQGFAQSNLYNALNVSSDESINGSDDIPNRKRPRMDQNMDPSFIMHAPVSGKLGAEVTEEGGQPNIRFFKYQEEQWCPMYDANGEELGRLQVHVLADKGFNYSTNDNCFVNQKKNHFQVTVKIEAIDPSPPQCFKINGVCKPIENFQLSFVGAKSESQNSEIPIRQSTTERKPILHTPVLFKIVERRMTIVTVPRLHFSETTLNNQRKNLRPNPDQKYFNLVVRLYATATDGTTVLMQAFASERVIVRATNPGSFEPPEMVDASWNKNGGILSTNGPVVIGKSEPRAQLTVDGDIYSSGRVMYPSDIRLKDNITEKGAKDALENLQKLRIVDYFYKPEVASKWGLTEDQRKRTGVIAQELAAVLPDAVKDLGDYLTVNESRVFYETVLATQELCRLTGDLDQKIDDKVAEISQRLTQYAQKKKMLNSMASGLNSEGRSLNASRTSLDSSASALTLTNTKKNRRSSRKDKKDAPKSKMTHGTVIGLVGVMAFCLLAMSALYILDWHNRNFGYHHFTPSATTSGPKEGPGNVVIPLDHYVPLRQPDAPPLVPFCPMETCRGYCCMEYDKDHAELEITEYDPNTATDNDFGFKADTRSDFTLKGFGNNVKISLPELGMQIDERYCIEKSCVKKRKVYSLFIPMTRYLPNVPLEVQIDVPSSKVVNNCGYIQEFDNRKCDETGSSSTETDAPRSIQLFDNTFQVSAGQWTQSAYRFRVGYSTELCSIDDTHFGGFYEEYNLIFYRACNRTNSTAINVV
Protein: Ent-copalyl diphosphate synthase 2, chloroplastic (Ent-CPP synthase 2) (Ent-CPS 2) (EC 5.5.1.13) (Protein ANTHER EAR 2) (ZmAN2) (A0A1D6K6U5)
Organism: Zea mays (Maize)
Function: Involved in gibberellin biosynthesis. Catalyzes the conversion of geranylgeranyl diphosphate to the gibberellin precursor ent-copalyl diphosphate (ent-CPP). Involved in the production of antifungal dolabralexin phytoalexins in response to biotic and abiotic stresses. In response to fungal infection and in associtation with KSL4, is involved in the production dolabradiene, a type of antifungal phytoalexin.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Kaurene synthase4
- Kaurene synthase3
- Geranylgeranyl diphosphate reductase, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- Ent-copalyl diphosphate synthase AN1, chloroplastic
- Ent-kaurene oxidase
- Geranylgeranyl pyrophosphate synthase4
- Geranylgeranyl pyrophosphate synthase1
- Heterodimeric geranylgeranyl pyrophosphate synthase small subunit chloroplastic
- all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]
Sequence:
MVLSSSCTTVPHLSSLAVVQLGPWSSRIKKKTDAVAVPAAAGRWRARARAQDTSESAAVAKGSSLTPIVRTDAESRRTRWPTDDDDAEPLVDEIRAMLTSMSDGDISVSAYDTAWVGLVPRLDGGEGPQFPAAVRWIRNNQLPDGSWGDAALFSAYDRLINTLACVVTLTRWSLEPEMRGRGLSFLGRNMWKLATEDEESMPIGFELAFPSLIELAKSLGVHDFPYDHQALQAIYSSREIKVKRIPKEVMHTVPTSILHSLEGMPGLDWARLLKLQSSDGSFLFSPAATAYALMNTGDDRCFSYIDRTVKKFNGGVPNVYPVDLFEHIWAVDRLERLGISRYFQKEIEQCMDYVNRHWTEDGICWARNSDVKEVDDTAMAFRLLRLHGYSVSPDVFKNFEKDGEFFAFVGQSNQAVTGMYNLNRASQISFPGEDVLHRAGPFSYEFLRRKQAEGALRDKWIISKDLPGEVVYTLDFPWYGNLPRVEARDYLEQYGGGDDVWIGKTLYRMPLVNNDVYLELARMDFNHCQALHQLEWQGLKKWYTENRLMDFGVAQEDALRAYFLAAASVYEPCRAAERLAWARAAILANAVSTHLRNSPSFRERLEHSLRCRPSEETDGSWFNSSSGSDAVLVKAVLRLTDSLAREAQPIHGGDPEDIHKLLRSAWAEWVREKADAADSVCNGSSAVEQEGSRMVHDKQTCLLLARMIEISAGRAAGEAASEDGDRRIIQLTGSICDSLKQKMLVSQDPEKNEEMMSHVDDELKLRIREFVQYLLRLGEKKTGSSETRQTFLSIVKSCYYAAHCPPHVVDRHISRVIFEPVSAAK
Protein: Meiotically up-regulated gene 146 protein (O74848)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in sporulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Meiotically up-regulated gene 168 protein
- Putative uncharacterized protein C32H8.15
- Putative uncharacterized protein SPCC794.16.
- Meiotic drive suppressor wtf25
Sequence:
MICKNTFVDYPTTQVRKERVHTYRTLTSATPSLEFFSNENTNRLSEVQCKLTHFLSSSENSSSVRNTRTHKFKQLLHYIFFSNRSSSVLGKQNVHNSQTLGSVSFCEKHAIDINYSENVNKQLNFESHLDDQTCSKRFYFNEQSGSDRYSLKCDSDTDSSTYFGDSASETCSSASNSLYKQTDLTSLCMFNQNKIQTDWSSIDPMDNDKIVCADFEKNFNILKELLNNTKDNGIDQQIVHKEHISHLEKIWKNINEESSEDPSLLLLRLEFLLTDLQTAIRKYSDTVSTNSVNEAFFDKIKIELQAFGVLV
Protein: Putative lipoprotein LprE (P9WK49)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- ERCC4 domain-containing protein
- TM0106 family RecB-like nuclease
- DNA polymerase I
- Probable transcriptional regulatory protein
- ATP-dependent RNA helicase DeaD
- Decaprenylphosphoryl-5-phosphoribose phosphatase
- Probable conserved integral membrane protein
- Large ribosomal subunit protein uL6
- ATP-dependent helicase DinG
Sequence:
MPGVWSPPCPTTPRVGVVAALVAATLTGCGSGDSTVAKTPEATPSLSTAHPAPPSSEPSPPSATAAPPSNHSAAPVDPCAVNLASPTIAKVVSELPRDPRSEQPWNPEPLAGNYNECAQLSAVVIKANTNAGNPTTRAVMFHLGKYIPQGVPDTYGFTGIDTSQCTGDTVALTYASGIGLNNVVKFRWNGGGVELIGNTTGG
Protein: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59) (Q9SIE3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Beta-ketoacyl-[acyl-carrier-protein] synthase III, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic
- EMBRYO DEFECTIVE 3147
- Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- NADPH-dependent aldehyde reductase-like protein, chloroplastic
Sequence:
MATTSNSVLFLSSDSLIHHHHHQPLHLSSSRSHSVSLPPNKRSNSLTLRCSTNGDSTSTEKETPIELKFPAFPTVMDINQIREILPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQPEVGGSQDNFFFAGIDKVRFRKPVIAGDTLVMRMTLLKFQKRFGLAKMEGKAYVGGALVCEGEFMMVSAGSS
Protein: Trifunctional (S)-stylopine synthase 2/(S)-nandinine synthase/(S)-canadine synthase (STS) (EC 1.14.19.64) (EC 1.14.19.68) (EC 1.14.19.73) (Cytochrome P450 719A3) (EcCYP719A3) (EcCYPA) (Q50LH4)
Organism: Eschscholzia californica (California poppy)
Function: Methylenedioxy bridge-forming cytochrome P450 involved in the biosynthesis of isoquinoline alkaloids. Converts (S)-cheilanthifoline to (S)-stylopine, (S)-scoulerine to (S)-nandinine and (S)-tetrahydrocolumbamine to (S)-canadine, but only the ring A (2,3-position) of the substrates is converted. Catalyzes an oxidative reaction that does not incorporate oxygen into the product.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEEMKFLIMNNPWVLFATSATLLISIFLFFRRKSPNMAWPEGPKTLPIIGNMHLLGGTALQVVLYNLAKVHGRVMTIWIGSWRPVIVVSDIEQAWEVLVNKSSDYSARDMPDITKIVTADWRTISTSDSGPHWSNLRKGLQNIAISPNNLAAQFQFQEKDIIKMIQILEQEAKDNNGIVKPLDHLKKATIRLISRLVFGRDFEEDKYVEDMHHAIEELIRISGYARLAEAFYYAKYLPSHRKAVRYVEELKQIVKNLIRPFLSVNPPTNTYLHFLRSQNYDEEVVIFAIFETYLLGVDSTSSTTAWALAYLVREPSVQDRLHQELDHFAKQNDRKILKVEDMNKLQYLQAVIKETMRMKPIAPLAIPHKACKDTSLMGNKINKGTRVMVNLYALHHNKNVFNDPFKFMPERFLKVDNQDAKGKAMEQSLLPFSAGMRICAGMELGKLQFSFALANLIFAFKWSCVDDGVLPDMSDELGFVLLMKTPLKARINPRN
Protein: Pseudouridine synthase family protein (Q9C5K6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pseudouridine synthase family protein
- Periodic tryptophan protein 2
- Ribosome production factor 2 homolog
- Bystin
- tRNA
- Putative U3 small nucleolar ribonucleoprotein
- AT1G07840 protein
Sequence:
MTISDAKSDPGGDDRDSEIAKETELVFLRNRVKELEVENAKLLSQVSSCQCQQMEVKHDRSLSDSSSLVRRRRVRKGDKNSIPSHLISKRYVALKIMYFGKRFYGFSAEAQMEPSIESEVFKALERTRLLVGDKKDSCYSRCGRTDKGVSSTGQVIALFLRSRLKSPPGDSKAQVNGRTGERPEYDYVRVLNRALPDDIRVIGWSPAPIDFHARFSCYAREYKYFFWRQNLNLSAMDFAGKKFIGEHDFRNFCKMDVANVHCYTRRVTFFEVSPCQNSHEGDQLCTFTMRGSAFLWHQIRCMVAVLFMIGQGVESVDVIDTLLDTKKTPRKPQYLLASEIPLVLRTCEFENVDFICSPGAAESLRSHFKNESLTYQLESVIYQEALRNCLPLSNNVSTEESSCNGVEKKKKRAEHVPLLSRPTEPSYEERTAKLKPRKEETLACVV
Protein: DNA-directed RNA polymerase III subunit RPC3 (RNA polymerase III subunit C3) (Q9BT08)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367076}.
Interaction partners:
Sequence:
MTQAEIKLCSLLLQEHFGEIVEKIGVHLIRTGSQPLRVIAHDTGTSLDQVKKALCVLVQHNLVSYQVHKRGVVEYEAQCSRVLRMLRYPRYIYTTKTLYSDTGELIVEELLLNGKLTMSAVVKKVADRLTETMEDGKTMDYAEVSNTFVRLADTHFVQRCPSVPTTENSDPGPPPPAPTLVINEKDMYLVPKLSLIGKGKRRRSSDEDAAGEPKAKRPKYTTDNKEPIPDDGIYWQANLDRFHQHFRDQAIVSAVANRMDQTSSEIVRTMLRMSEITTSSSAPFTQPLSSNEIFRSLPVGYNISKQVLDQYLTLLADDPLEFVGKSGDSGGGMYVINLHKALASLATATLKSVVQERFGSRCARIFRLVLQKKHIEQKQVEDFAMIPAKEAKDMLYKMLSENFMSLQVGCQ