wanglab/gogpt-training-data huggingface dataset:
Protein: Capsid protein (Gene product 6) (gp6) (D3WAC5)
Organism: Lactococcus phage p2 (Lactococcus lactis bacteriophage p2)
Function: Capsid protein self-assembles to form an icosahedral capsid with a T=7 symmetry, about 69 nm in diameter, and consisting of 60 capsid proteins hexamers and 11 pentamers. The capsid encapsulates the genomic DNA.
Subcellular location: Virion {ECO:0000269|PubMed:22820334, ECO:0000269|PubMed:24027307}. Note=Main component of the capsid. {ECO:0000269|PubMed:22820334, ECO:0000269|PubMed:24027307}.
Interaction partners:
Sequence:
MNKPDLIEKQNRLAELKENNVSLKSQISGFEVKNAIEDLPKVQELEKTLSENSIEIIKIENELNAQEEKPKGKDKMTNFIESQNAVTEFFDVLKKNSGKSEIKNAWSAKLAENGVTITDTTFQLPRKLVESINTALLNTNPVFKVFHVTNVGALLVSRSFDSANEAQVHKDGQTKTEQAATLTIDTLEPVMVYKLQSLAERVKRLQMSYSELYNLIVAELTQAIVNKIVDLALVEGDGTNGFKSIDKEADVKKIKKITTKAKSAGKTPFADAIEEAVDFVRPTAGRRYLIVKTEDRKALLDELRQATANANVRIKNDDTEIASEVGVDEIIVYTGSKALKPTVLVDQKYHIDMQDLTKVDAFEWKTNSNMILVETLTSGHVETYNAGAVITVS
Protein: Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) (6-O-methylguanine-DNA methyltransferase) (MGMT) (O-6-methylguanine-DNA-alkyltransferase) (P26187)
Organism: Mus musculus (Mouse)
Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA-3-methyladenine glycosylase
- Isocitrate dehydrogenase cytoplasmic
- N-glycosylase/DNA lyase
- Epidermal growth factor receptor
- Isocitrate dehydrogenase, mitochondrial
- DNA mismatch repair protein Msh6
- Ras association domain-containing protein 1
- Cellular tumor antigen p53
- DNA mismatch repair protein Mlh1
- Mismatch repair endonuclease PMS2
Sequence:
MAETCKMKYSVLDSPLGKMELSGCERGLHGIRLLSGKTPNTDPTEAPATPEVLGGPEGVPEPLVQCTAWLEAYFREPAATEGLPLPALHHPVFQQDSFTRQVLWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVVRSDGAIGHYSGGGQAVKEWLLAHEGIPTGQPASKGLGLTGTWLKSSFESTSSEPSGRN
Protein: Ribonuclease (EC 3.1.26.4) (Q38B94)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribonuclease H2 subunit B wHTH domain-containing protein
- Proliferating cell nuclear antigen
- DNA polymerase epsilon catalytic subunit
- ribonuclease H
- Bifunctional dihydrofolate reductase-thymidylate synthase
- DNA primase
- DNA helicase
- Acyl carrier protein
- DNA primase large subunit
- DNA replication licensing factor MCM5
Sequence:
MAEPRSSSSKMPSGAKSNRAGIEFDVSEFMQSMECSENHLVMGIDEAGRGPVVGPMVYTGAMIALHEHDRLVDYCGANDSKVLNEDQRKSVVSKLHELATFRTFTVVVTPDEIAAAMTGAHGTNLNTLSHQTAISIISKLTLEGMGMLTAAYVDTVGPPESYQQKLSGRFPHLRVTVAKKAEIKFPIVAAASVVAKVERDSHIERLGIDVGSGYPSDPKVMMWVRSHVHRFFVMPRECNFVRLSWAPVTQLANDPETCIPIVFEEDTTPKKERKQSKCSGDGKKQKLLSFVKPAPRRHFVYTHLLKLRTIAGIRDTHHTALSREVP
Protein: Nucleosome assembly protein (Q8I608)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Histone H2A
- PH domain-containing protein, putative
- Histone H2A
- 40S ribosomal protein S6
- Protein SDA1, putative
- 60S ribosomal protein L39
- Histone H2B
- Histone H2B
- SNF1-related serine/threonine protein kinase KIN
- Calcium/calmodulin-dependent protein kinase, putative
Sequence:
MAANEGNQPIPPEEEKEISSLLESIKIDDDKMTDLTEEQKETLKKLKLYQKEYYDYESKFEYELFLLRQKYHDLYGPIYDKRREALVGNGEAKIGTPNLPEFWLRALRNNNTVSHVIEDHDEEILVYLNDIRCDYIKKNKEKKEGFILSFYFATNPFFSNSVLTKTYHMKCVDCDNEPVLLHTEATVIDWYDNKNILKKNVVKKQHNKNSREVKTVQQTVNRDSFFHFFTSHKVPNSNVIKQLSKHEVAQLEMIIEGDYEVALTIKERIIPYAVDYYLGIIIESESNSIVSDVDSSYSSSENNSNYNSYESNNSAYNDENSNVDTNEYDDNEEEEEGAKSNEDPLTS
Protein: Dual serine/threonine and tyrosine protein kinase (EC 2.7.12.1) (Dusty protein kinase) (Dusty PK) (Receptor-interacting serine/threonine-protein kinase 5) (Q4VSN1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May act as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death (By similarity). Plays a role in the embryonic development.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6XUX1}. Cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Cell junction {ECO:0000250|UniProtKB:Q6XUX1}.
Interaction partners:
- Calymmin
- Glutamine and serine-rich 1
- Bystin-like.
- Myb/SANT-like DNA-binding domain-containing protein 2
- Mediator of RNA polymerase II transcription subunit 20
- Tenascin XBa.
- Proton-associated sugar transporter A
- FMR1-interacting protein NUFIP2
Sequence:
MENPQKPRELTRAFNHYNKHSGFLKKNLKETILFFREIRQNHSNTCAAAEPGQLSCISFPRQDEEYLQNVVSSAPYILILGQDCSARYQLLNCLLGERLLPLGPEAGGACGAEGGACRRRKLCFTHGRQTRLSLALPGQYELVHQLAAHCGRWDTVPRQDLEIQECEDPAQRLAELEITLHHTLLQEVKIMVLPCRNVQPLEEALEDCKRGILPIVLYAVSRESLSAQQLEDLQTLRESLPFPVCFIRVSDGGGGGALFTQLASLQLISASAGNCACGAPAAQSAGRMQGVLCDSLERLQRVLVPFTRQVLQNQQVEAATLLNTIHCRCLDLFIIQAFDMQRDLQITPRRLEYTREKEGELFCSLMAIANRKQEEMKEMIVETLSSMKEQLLEDAQNLDFTDIIMSSNGEPVSSKDIKVCISQIQDLIVNRLNQAVANKLTNSVDYLRESFVGTLERCLGSLEKSTPESCAHNVTSNHLKQILNAAYHVEVTFHSGSSVTRLFWEQIKQIIHRITWVNPPAITAEWKRKVAQDAIESLSAAKLAKSICSQFRTRLNSSHEAFAASLRQLEEGHTGRLERTEDLWLRVRKDHAPRLARLSLESRSLRDILLHGKPKLGRELGRGQYGVVYLCDSWAGRHPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERLVNLHGSVIDHSYSGGSSIAVLLIMERLHRDLYTGLKAGLSLKERLLIALDVVEGIRFLHSQGLLHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGILFWYLCSGSVKLPEAFEKCASKDQLWTNVKKGCRPERLPVFDEECWQLMEACWNGDPSQRPLLGIVQPGLQSIMERLCGEKSLEDSN
Protein: Cell division cycle protein 20 homolog (p55CDC) (Q5H7C0)
Organism: Sus scrofa (Pig)
Function: Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q12834}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q12834}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q12834}.
Interaction partners:
- Cyclin B2
- Securin
- Serine/threonine-protein kinase PLK
- G2/mitotic-specific cyclin-B1
- BUB1 mitotic checkpoint serine/threonine kinase.
- BUB3 mitotic checkpoint protein.
- BUB1 N-terminal domain-containing protein.
- Kinesin-like protein
- Ubiquitin conjugating enzyme E2 C
- Mitotic spindle assembly checkpoint protein MAD2A
Sequence:
MAQFVFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSNSKMQTTPSKPGGDRYIPHRSASQMEVASFLLSKENQPDNSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGDYVSSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLCWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTARVLSLTMSPDGATVASAAADETLRLWRCFELDPARRREREKASAAKSSLIHQGIR
Protein: Small ribosomal subunit protein uS5 (40S ribosomal protein S2) (40S ribosomal protein S4) (Protein LLRep3) (P15880)
Organism: Homo sapiens (Human)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Plays a role in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:30530495}. Nucleus, nucleolus {ECO:0000269|PubMed:30530495}. Note=Probably localized to nucleolus and cytoplasm in complex with ZNF277. {ECO:0000269|PubMed:30530495}.
Interaction partners:
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL21
- Elongation factor 2
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein eL37
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL3
Sequence:
MADDAGAAGGPGGPGGPGMGNRGGFRGGFGSGIRGRGRGRGRGRGRGRGARGGKAEDKEWMPVTKLGRLVKDMKIKSLEEIYLFSLPIKESEIIDFFLGASLKDEVLKIMPVQKQTRAGQRTRFKAFVAIGDYNGHVGLGVKCSKEVATAIRGAIILAKLSIVPVRRGYWGNKIGKPHTVPCKVTGRCGSVLVRLIPAPRGTGIVSAPVPKKLLMMAGIDDCYTSARGCTATLGNFAKATFDAISKTYSYLTPDLWKETVFTKSPYQEFTDHLVKTHTRVSVQRTQAPAVATT
Protein: Cold shock-induced protein TIR2 (Serine-rich protein 2) (TIP1-related protein 2) (P33890)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cell wall.
Subcellular location: Secreted, cell wall {ECO:0000250}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Seripauperin-23
Sequence:
MAYIKIALLAAIAALASAQTQEEIDELNVILNDVKSNLQEYISLAEDSSSGFSLSSLPSGVLDIGLALASATDDSYTTLYSEVDFAAVSKMLTMVPWYSSRLLPELESLLGTSTTAASSTEASSAATSSAVASSSETTSSAVASSSEATSSAVASSSEASSSAATSSAVASSSEATSSTVASSTKAASSTKASSSAVSSAVASSTKASAISQISDGQVQATSTVSEQTENGAAKAVIGMGAGVMAAAAMLL
Protein: Uncharacterized protein C36.11 (O59708)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Note=Localizes to the cell tip and the barrier septum.
Interaction partners:
- UPS-like protein C36.10
Sequence:
MSISNDSLASTVPGDELPSSYPVFSSDFSYIKPSHVLDVVTVTSTAGPEATDDPSYSGFYSTVISTQNPEPTSASTPPSASASSLPNGAQKHNHTGVIAGPIVGVLGGLIVLVIIFYCLRHFKRKKFLAEQQEFERQFEEEKSRLAAVRKNTEQEKMGYRGGYQMHSTPWASSPRNSTIPQRSQSFYNDTRRSSDLGANAADFVTPPGNVANSDNIRILKRNSIATIGNYRSPSALEKRRSISYGAVQSVQGRPLAPIPGRRPLSISSDLYNDSNSGSHSNDDSDETKLKQSSTESSSELLDEKDKFDKNSLNDPFVTIRKSSYEHEISEEHKKHSKKRSEHF
Protein: PKHD-type hydroxylase PiuC (EC 1.14.11.-) (Iron-uptake factor PiuC) (Q9HVQ7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable TonB-dependent siderophore receptor PiuA
- Sel1 repeat family protein
- Probable TonB-dependent receptor
- Probable dihydrodipicolinate synthetase
- Protein TonB
- p-hydroxybenzoate hydroxylase
Sequence:
MLLHIPAIFTAEEVSRIRAALEQAEWADGKATAGYQSAKAKHNLQLPQDHPLAREIGEAMLQRLWNHPLFMSAALPLKVFPPLFNCYTGGGSFDFHIDNAVRDVHGGRERVRTDLSSTLFFSDPEDYDGGELVIQDTYGLQQVKLPAGDLVLYPGTSLHKVNPVTRGARYASFFWTQSLVREDSQRTLLFEMDQSIQRLTRDVPDHPSLIRLTGTYHNLLRRWSEL
Protein: Transcription initiation factor IIF subunit alpha (TFIIF-alpha) (TFIIF large subunit) (O94416)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription initiation factor IIF subunit beta
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit RPB2
- Transcription initiation factor IIE subunit beta
- Transcription initiation factor IIE subunit alpha
- RNA polymerase II subunit A C-terminal domain phosphatase
- DNA-directed RNA polymerase II subunit RPB3
- Transcription initiation factor IIB
- DNA-directed RNA polymerase II subunit rpb7
- Transcription initiation factor TFIID subunit 14
Sequence:
MDSQETKVFENVKQENPDEKKPKVEEPDSQNNASTQSQQKFLDFQLSWCPESERKTTKYHLLKFHSNKAIDPSKSFVPPIKMQRRDPNAPSSSNGEQNAEQGSSSNVNIASIAPYGGAQNMKQNAFKRKTRQVVKVDPQARRLQEEELSPWIMEDFEGKNTWVSTMEGGQSSAYVLFMFSENGFKVIPTDRFYRFNQRNNFQTLSIDEAEAKMNKKTPIPRWFMKKESEENLAEAGSASPMYKLKTVPNARPVTGPRASGSDDELDYDEEFADDEEAPIMEGNEEDNKKLKDKIKKEMLTANLFGEADQDVDLEEENDRQMSREGKKLQRYLKLLEKNLAYESDEEDEDPYASSHDASSEEEVLQEEEELQKREEKLKSRFSANASKTNTPRPLERTPSSVSPVKASSQLQSPNTSIQIRPQEQLINKPGYIILRLSSEKLSRFANDFPRMVPSMGSTETSVGDQVEVVGDTTNVPIDDSNLITEAEVMKALRAGPISIKDLVHLFQRKIRADNRNRLGIQKIIRKVARFENKLLVLKNY
Protein: Costunolide synthase (TpCOS) (EC 1.14.14.150) (Cytochrome P450 71BL2) (X2JE85)
Organism: Tanacetum parthenium (Feverfew) (Matricaria parthenium)
Function: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Component of the parthenolide biosynthetic pathway; parthenolide and conjugates are promising anti-cancer drugs highly active against colon cancer cells. Hydroxylates germacrene A acid to 6-alpha-hydroxy-germacrene A acid, a precursor of sesquiterpene lactones that spontaneously undergoes a lactonization which yields costunolide.
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEPFTIFSLVVASLVFFACWALVAPNTSKNLPPGPPKLPIIGNIHQLKSPTPHRVLKDLAKKYGPIMHLQLGQVSTVVVSTPRLAQEIMKTNDISFADRPTTTTSQIFFYKAQDIGWAPYGEYWRQMKKICTLELLSAKKVRSFSSIREEELTRIRKILEFKAGTPINYTEMTIEMVNNVICKATLGDCCKDQALLIELLYDVLKTLSAFNLASYYPRLQFLNVISGKKAKWLKMQKRLDDIMEDILKEHRAKGRAKNSDQEDLVDVLLRIKDTGGLDINVTDEHVKAVVLDMLTAGTDTSSTTLEWAMTELMRNPDMMKRAQEEVRSVVKGEHVTETDLQSLHYLKLIVKETMRLHAPTPLLVPRECRQDCNVDGYDIPAKTKVLVNAWACGVDPGSWENPDSFIPERFENSSINFMGADFQYIPFGAGRRICPGLTFGLSMVEYPLAHFLYHFDWKLPYGMKPHELDITEITTISTSLKHHLKIVPFPKSSLAK
Protein: ArfGAP with dual PH domains 1 (A0A3B3ISA7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKERRRAVLELLQRPGNARCADCGAPDPDWASYTLGVFICLSCSGIHRNIPQVSKVKSVRLDAWEEAQVEFMASHGNDAARARFESKVPSFYYRPTPSDCQLLREQWIRAKYERQEFIYPEKQEPYSAGYREGFLWKRGRDNGQFLSRKFVLTEREGALKYFNRNDAKEPKAVMKIEHLNATFQPAKIGHPHGLQVTYLKDNSTRNIFIYHEDGKIVDWFNALRAARFHYLQVAFPGAGDADLVPKLSRNYLKEGYMEKTGPKQTEGFRKRWFTMDDRRLMYFKDPLDAFARGEVFIGSKESGYTVLHGFPPSTQGHHWPHGITIVTPDRKFLFACETESDQREWVAAFQKAVDRPMLPQEYAVEAHFKHKP
Protein: HCG1991317, isoform CRA_b (TWEAK) (Tumor necrosis factor (Ligand) superfamily, member 12) (Q4ACW9)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAARRSQRRRGRRGEPGTALLVPLALGLGLALACLGLLLAVVSLGSRASLSAQEPAQEELVAEEDQDPSELNPQTEESQDPAPFLNRLVRPRRSAPKGRKTRARRAIAAHYEVHPRPGQDGAQAGVDGTVSGWEEARINSSSPLRYNRQIGEFIVTRAGLYYLYCQVHFDEGKAVYLKLDLLVDGVLALRCLEEFSATAASSLGPQLRLCQVSGLLALRPGSSLRIRTLPWAHLKAAPFLTYFGLFQVH
Protein: DNL-type zinc finger protein (Hsp70-escort protein 1) (HEP1) (mtHsp70-escort protein) (Q5SXM8)
Organism: Homo sapiens (Human)
Function: May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23462535}.
Interaction partners:
- Stress-70 protein, mitochondrial
Sequence:
MLRTALRGAPRLLSRVQPRAPCLRRLWGRGARPEVAGRRRAWAWGWRRSSSEQGPGPAAALGRVEAAHYQLVYTCKVCGTRSSKRISKLAYHQGVVIVTCPGCQNHHIIADNLGWFSDLNGKRNIEEILTARGEQVHRVAGEGALELVLEAAGAPTSTAAPEAGEDEGPPSPGKTEPS
Protein: Odorant receptor 33b (P81915)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to pentyl acetate and pyrazines.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 74a
- Odorant receptor 30a
- Odorant receptor 22c
- Odorant receptor 47a
- Odorant receptor 45a
- Odorant receptor 35a
- Odorant receptor 13a
Sequence:
MDLKPRVIRSEDIYRTYWLYWHLLGLESNFFLNRLLDLVITIFVTIWYPIHLILGLFMERSLGDVCKGLPITAACFFASFKFICFRFKLSEIKEIEILFKELDQRALSREECEFFNQNTRREANFIWKSFIVAYGLSNISAIASVLFGGGHKLLYPAWFPYDVQATELIFWLSVTYQIAGVSLAILQNLANDSYPPMTFCVVAGHVRLLAMRLSRIGQGPEETIYLTGKQLIESIEDHRKLMKIVELLRSTMNISQLGQFISSGVNISITLVNILFFADNNFAITYYGVYFLSMVLELFPCCYYGTLISVEMNQLTYAIYSSNWMSMNRSYSRILLIFMQLTLAEVQIKAGGMIGIGMNAFFATVRLAYSFFTLAMSLR
Protein: Mitotic-spindle organizing protein 1A (GCP3-interacting protein 2) (AtGIP2) (Mitotic-spindle organizing protein associated with a ring of gamma-tubulin 1A) (AtGIP1A) (Q9C9T3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for gamma-tubulin complex recruitment to the microtubule organizing centers (MTOCs) (By similarity). During mitosis, modulates gamma-tubulin complex localization, spindle stability and chromosomal segregation. Necessary for gametophyte development and embryogenesis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q08AG7}. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, phragmoplast. Nucleus envelope. Note=Reorganized from the nucleus to the prospindle and the preprophase band in late G2. After nuclear envelope breakdown, localized on spindle and phragmoplast microtubules (MTs) and on the reforming nuclear envelope of daughter cells. Present in mitotic microtubule arrays. In interphase cortical arrays, gamma-tubulin complexes are preferentially recruited to existing microtubules, from which new microtubules are efficiently nucleated.
Interaction partners:
- Gamma-tubulin complex component 3
- NAI2-like protein
- Gamma-tubulin complex component 4
- Protein NEDD1
- TSK-associating protein 1
- Probable transmembrane ascorbate ferrireductase 4
- Probable transmembrane ascorbate ferrireductase 3
- Gamma-tubulin complex component 2
- SUN domain-containing protein 1
- Transmembrane ascorbate ferrireductase 2
Sequence:
MNQEAAETARESLELVFRMSNILETGLDRHTLSVLIALCDIGLNPEALATLVKELRRDSATTTTTVD
Protein: Linalool synthase Tps-5042L13, chloroplastic (PfTps-5042L) (EC 4.2.3.-) (C0KWV7)
Organism: Perilla frutescens (Beefsteak mint) (Perilla ocymoides)
Function: Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into linalool.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSSMRIYVAIMKKPSVKHVDNVDKKASKPSWRVSSSATAGLRASSSLQLDVKKPADEILTARRSGNYQPSLWDFNYLQPLNTTHYKEERHLKREAELIEQVKMLLEEEMEAVQQLELVDDLKNLGLSYFFEDQIKQILTFIYNEHKCFRSNVEAEERDLYFTALGFRLLRQHGFQVSQEVFDCFKNEEGSDFKASLGDDTKGLVQLYEASFLLREGEDTLELARQYATKFLQKKVDHELIDDDNNLLSWIRHSLEIPLHWRIQRLEARWFLDAYATRHDVNPIILELAKLDFNIIQATQQEELKDLSRWWNSTCLAEKLPFVRDRLVESYFWAIALFEPHQYGYHRKIAAKIITLITSLDDVYDIYGTLDELQLFTDAIQRWDTESISRLPYYMQLFYMVLYNFVSELAYDGLKEKGFITIPYLQRSWADLVEAYLKEAKWFYNGYTPSMEEYLNNAYISIGATPVISQVFFTLATSIDKPVIESLYEYHRILRLSGMLVRLPDDLGTSPFEMKRGDVPKAILLYMKERNATEIEAQEHVRFLIREAWKEMNTATAAADCPLTDDLVAAAANLGRAAQFMYLDGDGNHSQLHQRIASLLFEPYA
Protein: SWI/SNF and RSC complexes subunit ssr2 (O14470)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
Interaction partners:
- SWI/SNF and RSC complexes subunit ssr3
- Chromatin structure-remodeling complex subunit sfh1
- Chromatin structure-remodeling complex subunit rsc7
- Chromatin structure-remodeling complex subunit rsc58
- SWI/SNF chromatin-remodeling complex subunit snf5
- Chromatin structure-remodeling complex subunit rsc9
- Chromatin structure-remodeling complex subunit snf21
- SWI/SNF and RSC complexes subunit arp9
- Chromatin structure-remodeling complex subunit rsc1
- SWI/SNF and RSC complexes subunit arp42
Sequence:
MTLDQVRIPFLVEQTYPIIVPSYAGWFDMSKIHDIERRSNPEFFNGKSPLKTPSIYKDYRDFMINSYRLEPNEYLTVTACRRNLVGDVCAIIRVHAFLEQWGLINYQIDPETRPAFRLPPISGHVQAISNTPIVTQEMLAQHPPPSTVGGSSSQEFVKLEEKHYSPSLNAMEQTSPKEEDEKSDKVPRVDKVCFTCGVNCSQTWYHNLKNKKYDICPNCYKQGRFSSSFNSSDFLCMDAIDFNHDEEKPWSNQETLLLLEAIETYGDDWNQIALHVGSRTKEQCLIHFLQIPIEDPYRQKLQGDFSPFKKGFLPFDENENPVLSTLTYLASIVQQGMKERKQNESVKQGETSFGNSEFKNPLERVAYYALKSAAQKAKLIAAFENRQLRRLVFSLIQAQLEKLQLKMKVLEQLEKMCSLELSELDLRGKNLLLSRLSTKKMLLAFNKKLEEAVNLGGEDGLKIIDDLMSTEHAEALLTFEMPTATTVSPLSKQYPDKFRTIAL
Protein: Packaging protein UL32 (Q4JQU9)
Organism: Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3)
Subcellular location: Host cytoplasm {ECO:0000256|RuleBase:RU364029}. Host nucleus {ECO:0000256|RuleBase:RU364029}.
Interaction partners:
Sequence:
MDRVESEEPMDGFESPVFSENTSSNSGWCSDAFSDSYIAYNPALLLKNDLLFSELLFASHLINVPRAIENNVTYEASSAVGVDNEMTSSTTEFIEEIGDVLALDRACLVCRTLDLYKRKFGLTPEWVADYAMLCMKSLASPPCAVVTFSAAFEFVYLMDRYYLCRYNVTLVGSFARRTLSLLDIQRHFFLHVCFRTDGGLPGIRPPPGKEMANKVRYSNYSFFVQAVVRAALLSISTSRLDETETRKSFYFNQDGLTGGPQPLAAALANWKDCARMVDCSSSEHRTSGMITCAERALKEDIEFEDILIDKLKKSSYVEAAWGYADLALLLLSGVATWNVDERTNCAIETRVGCVKSYWQANRIENSRDVPKQFSKFTSEDACPEVAFGPILLTTLKNAKCRGRTNTECMLCCLLTIGHYWIALRQFKRDILAYSANNTSLFDCIEPVINAWSLDNPIKLKFPFNDEGRFITIVKAAGSEAVYKHLFCDLLCALSELQTNPKILFAHPTTADKEVLELYKAQLAAQNRFEGRVCAGLWTLAYAFKAYQIFPRKPTANAAFIRDGGLMLRRHAISLVSLEHTLSKYV
Protein: Mucin 3 (Q7TQB7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSTRRWVRQTAALCLLAFILHSLPRHIAAENGTTESGSVWDGGGNSTQDDSQETQFRTVLKTKTTVTGDRDDTGSTYETYNNFRSNKQTTSEVIPTTDVSTIAETTTAEV
Protein: Alpha-fibrinogenase A2 (EC 3.4.21.-) (Snake venom serine protease) (SVSP) (Q9PRW3)
Organism: Crotalus atrox (Western diamondback rattlesnake)
Function: Snake venom serine protease that cleaves fibrinogen Aalpha chain (FGA), partially cleaves Bbeta chain (FGB) and has no activity on gamma chain. Is more potent than A3 alpha-fibrinogenases and less potent than A1.
Subcellular location: Secreted {ECO:0000269|PubMed:8024586}.
Interaction partners:
Sequence:
VPGGDECNINEHRSL
Protein: UTP--glucose-1-phosphate uridylyltransferase 2 (EC 2.7.7.9) (UDP-glucose pyrophosphorylase 2) (AtUGP2) (UDPGP 2) (UGPase 2) (Q9M9P3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts glucose 1-phosphate to UDP-glucose, which is the major glycosyl donor for polysaccharides. Acts redundantly with UGP1 and is essential for the synthesis of sucrose, starch and cell wall, and callose deposition.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable phosphoglucomutase, cytoplasmic 1
- Probable phosphoglucomutase, cytoplasmic 2
- Phosphoglucomutase, chloroplastic
- ADP-glucose phosphorylase
- Alpha-glucan phosphorylase 1
- Alpha-glucan phosphorylase 2, cytosolic
- Sucrose-phosphate synthase 1
- UDP-sugar pyrophosphorylase
- Sucrose-phosphate synthase 4
- Probable sucrose-phosphate synthase 3
Sequence:
MAATTENLPQLKSAVDGLTEMSESEKSGFISLVSRYLSGEAQHIEWSKIQTPTDEIVVPYEKMTPVSQDVAETKNLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTFNQSKYPRVVADEFVPWPSKGKTDKEGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIVDLTILKHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPNPKEVDGVKVLQLETAAGAAIRFFDNAIGVNVPRSRFLPVKASSDLLLVQSDLYTLVDGFVTRNKARTNPSNPSIELGPEFKKVATFLSRFKSIPSIVELDSLKVSGDVWFGSSIVLKGKVTVAAKSGVKLEIPDRAVVENKNINGPEDL