wanglab/gogpt-training-data huggingface dataset:
Protein: Auxin-responsive protein SAUR27 (Protein SMALL AUXIN UP RNA 27) (Q9SRW1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as positive effectors of cell expansion through modulation of auxin transport (By similarity). Involved in thermo-responsiveness of plant architecture. Enhances plasma membrane H(+)-ATPase.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FJG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9FJG1}.
Interaction partners:
- TORTIFOLIA1-like protein 4
- Chaperone DnaJ-domain superfamily protein
- non-specific serine/threonine protein kinase
- Auxin-responsive protein SAUR62
- Putative zinc finger protein At1g68190
Sequence:
MALVRSLFVSNKILGGSLAGMRKSTSAPKGFLAVYVGESQKKQRYLVLVSYLSQPLFQDLLSKSEEEFGFDHPMGGLTIPCPEDTFLTVTSRIQG
Protein: Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta) (Q00005)
Organism: Homo sapiens (Human)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity (By similarity). Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance (By similarity).
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Note=Under basal conditions, localizes to both cytosolic and mitochondrial compartments. Relocalizes from the cytosolic to the mitochondrial compartment during apoptosis. Its targeting to the outer mitochondrial membrane (OMM) involves an association with import receptors of the TOM complex and is required to promote proapoptotic activity (By similarity). {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Ataxin-7
Sequence:
MEEDIDTRKINNSFLRDHSYATEADIISTVEFNHTGELLATGDKGGRVVIFQREQESKNQVHRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNAAYFLLSTNDKTVKLWKVSERDKRPEGYNLKDEEGRLRDPATITTLRVPVLRPMDLMVEATPRRVFANAHTYHINSISVNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALCDRHTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCIFDKFECVWNGSDSVIMTGSYNNFFRMFDRNTKRDVTLEASRENSKPRAILKPRKVCVGGKRRKDEISVDSLDFSKKILHTAWHPSENIIAVAATNNLYIFQDKVN
Protein: Checkpoint signal transducer rad25 (P42657)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts in cell cycle and stress checkpoint signaling by sequestering signal transducers regulated by the checkpoints (By similarity). Required for the DNA damage checkpoint that ensures that DNA damage is repaired before mitosis is attempted. Sequesters byr2 in the cytoplasm to prevent its translocation to the plasma membrane.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:12242289}.
Interaction partners:
- Checkpoint signal transducer rad24
- Cell division control protein 42 homolog
- Serine/threonine-protein kinase shk1/pak1
- M-phase inducer phosphatase
- Uncharacterized bHLH domain-containing protein C3F10.12c
- Double-strand-specific pac1 ribonuclease
- Phosphatidylinositol 4-kinase pik1
Sequence:
MSNSRENSVYLAKLAEQAERYEEMVENMKKVACSNDKLSVEERNLLSVAYKNIIGARRASWRIISSIEQKEESRGNTRQAALIKEYRKKIEDELSDICHDVLSVLEKHLIPAATTGESKVFYYKMKGDYYRYLAEFTVGEVCKEAADSSLEAYKAASDIAVAELPPTDPMRLGLALNFSVFYYEILDSPESACHLAKQVFDEAISELDSLSEESYKDSTLIMQLLRDNLTLWTSDAEYNQSAKEEAPAAAAASENEHPEPKESTTDTVKA
Protein: UPF3 domain-containing protein (Q8WQF3)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- MIF4G domain-containing protein
- Regulator of nonsense transcripts 1
- Nonsense-mediated mRNA decay protein
- PIN domain-containing protein
- Protein mago nashi homolog
- RRM domain-containing protein
- PWI domain-containing protein
- Serine/threonine-protein kinase smg-1
- RNA-binding protein rnp-4
- RNA helicase
Sequence:
MTDSKDGHVKVVLRRLPKYMTEHEVLEQISPLPEEVIGTYFHPANFSFDRCAYATLTVNFSEYCDSMMEFERRFDGYIFVDSRGNDSAAVVEAASNQNFAKCDRNRMKEDTRVGAILTDKYYLDFCKKLEEERAIPILTLEQQIRKLNQPDDARTQIDKMETPLVKYFFEKETGKRRDYDARRQRRDEKRAEKRDKVDKFEKHKNVLDILMKPSVPMASTSATTSKKDLKKEKPMTEKEKERWEKQDAKRKERNMIRKQKFLDEKKKKHEEREQDGPRVPRDKKKERLAKPPRPSPAKTVGEQQGEDWIKKLTDPKSAPMKKKHDLSVTTKLNKETDTRPRTAPSSTKLPTRATTSNHPKRPSTAPNH
Protein: NAD-dependent histone deacetylase HST4 (EC 2.3.1.286) (Homologous to SIR2 protein 4) (Regulatory protein SIR2 homolog 4) (P53688)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: NAD-dependent histone deacetylase, which contributes together with HST3 to histone H3 'Lys-56' deacetylation, regulation of telomeric silencing, proper cell cycle progression, DNA damage control, DNA recombination, and genomic maintenance.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17106263}.
Interaction partners:
- Nicotinamidase
- Histone acetyltransferase RTT109
- Glutamine-dependent NAD
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- NAD-dependent histone deacetylase HST3
- NAD
- NAD-capped RNA hydrolase NPY1
- Purine nucleoside phosphorylase
- Uridine nucleosidase
Sequence:
MKQKFVLPITPPSTAEKKPQTENRCNENLKPRRLLPQLKKSVRNRKPRLSYRPELNSVFDLDAYVDSTHLSKSQRHHMDRDAGFISYALNYSKRMVVVSGAGISVAAGIPDFRSSEGIFSTVNGGSGKDLFDYNRVYGDESMSLKFNQLMVSLFRLSKNCQPTKFHEMLNEFARDGRLLRLYTQNIDGLDTQLPHLSTNVPLAKPIPSTVQLHGSIKHMECNKCLNIKPFDPELFKCDDKFDSRTEIIPSCPQCEEYETVRKMAGLRSTGVGKLRPRVILYNEVHPEGDFIGEIANNDLKKRIDCLIIVGTSLKIPGVKNICRQFAAKVHANRGIVLYLNTSMPPKNVLDSLKFVDLVVLGDCQHVTSLL
Protein: Leucine-, isoleucine-, valine-, threonine-, and alanine-binding protein (LIVAT-BP) (Leu/Ile/Val/Thr/Ala-binding protein) (P21175)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Component of the high-affinity leucine, isoleucine, valine transport system I (LIV-I), which is operative without Na(+) and is specific for alanine and threonine, in addition to branched-chain amino acids. Binds L-leucine, L-isoleucine, L-valine, L-threonine and L-alanine with nanomolar affinities. Can also bind L-homoserine with high affinity.
Subcellular location: Periplasm {ECO:0000250}.
Interaction partners:
- High-affinity branched-chain amino acid transport system permease protein BraE
- High-affinity branched-chain amino acid transport system permease protein BraD
- High-affinity branched-chain amino acid transport ATP-binding protein BraF
- High-affinity branched-chain amino acid transport ATP-binding protein BraG
- Probable permease of ABC branched-chain amino acid transporter
- Branched chain amino acid ABC transporter membrane protein
- Branched chain amino acid ABC transporter ATP binding protein
- High-affinity branched-chain amino acid transport ATP-binding protein
- Amino acid binding protein
- Aliphatic amidase expression-regulating protein
Sequence:
MKKGTQRLSRLFAAMAIAGFASYSMAADTIKIALAGPVTGPVAQYGDMQRAGALMAIEQINKAGGVNGAQLEGVIYDDACDPKQAVAVANKVVNDGVKFVVGHVCSSSTQPATDIYEDEGVLMITPSATAPEITSRGYKLIFRTIGLDNMQGPVAGKFIAERYKDKTIAVLHDKQQYGEGIATEVKKTVEDAGIKVAVFEGLNAGDKDFNALISKLKKAGVQFVYFGGYHPEMGLLLRQAKQAGLDARFMGPEGVGNSEITAIAGDASEGMLATLPRAFEQDPKNKALIDAFKAKNQDPSGIFVLPAYSAVTVIAKGIEKAGEADPEKVAEALRANTFETPTGNLGFDEKGDLKNFDFTVYEWHKDATRTEVK
Protein: Uricase (EC 1.7.3.3) (Urate oxidase) (P33282)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Subcellular location: Peroxisome.
Interaction partners:
- Xanthine dehydrogenase
- Transthyretin domain protein
- Nicotinate hydroxylase hnxS
- allantoicase
- Alpha-ketoglutarate-dependent xanthine dioxygenase xanA
- Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase domain-containing protein
- allantoinase
- Uric acid-xanthine permease
- Adenine deaminase
- 3-hydroxybutyryl-CoA dehydrogenase, putative
Sequence:
MSTVAAARYGKDNVRVYKVHKDPKTGVQTVTEMTVCVLLEGEIDTSYTKADNSVIVATDSIKNTIFILAKQNPVTPPELFGSILGTHFINKYKHIHVAHTNIITHRWTRLNIDGKPHSHSFVRDSEETRNVQVDVTEGVGIDIKSSINKLTVLKSTGSQFWGFVRDEYTTLPEVWDRILSTDVEATWAWKRFSGLDEVRGNVPKFDETWEAARNITLKTFAEEESASVQATMYKMGEQILAYQPLLETVEYSLPNKHYFEIDLSWHKGLKNTGKDAEVFVPQTNPNGLIKCTVGRKSKAKL
Protein: HTH cro/C1-type domain-containing protein (Q9X2H8)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Interaction partners:
Sequence:
MSEKWKELGETFRKKREERRITLLDASLFTNINPSKLKRIEEGDLKGLDAEVYIKSYIKRYSEFLELSPDEMLKLYEEGKEEVAEEVEEKKPRKKKEKEKTRDLVMFFFLIAGLVFLLFSAVENLKLRQTPPAYLVAPEETIVNGKSVSGEIPLQEGEYIVESRSDVVLKTASEEWTVKIRKFEVSVSWEK
Protein: Uncharacterized protein, isoform M (M9PCJ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNKVEFKNKNKDQGPCARVRKIRPINMGGNVEQRPWTPTVRIGKIAAETTNPGPATVQLPTLIGSKVPDSKKKAAPSYSFGHKLGGKYDTSGPGPAQYNVTGMRAKGRDYPRAATLQSRPKELTRFSNPGPGEYDVVPAAKAVIDATPKYTFGQRPVALKTFQIPAPGAYCPEKVKLNKTPEFSFGIKHHEQRPDYTPAPGTYKPEQVVLEHIPAYSFGLKTKHIQVSDTPAPGAYSPEKSRLHSAPAYSIAGKASQDVVDCTPAPGAYEPEKCVLSRTPAFSFGHRAELAKSSDTPAPGTYNPEKVRLDHTPAFTLSGRPETRSVSETPAPGSYAPEKYRNDRTPAFTFGGKHEQRLESSTPAPGDYCPEKVRHDHNPAFSFAGRHDLHKPSDTPAPGAYDTEKVRQDHNPAFSFAGRHDLHKPSETPAPGAYSPEKVRQDHNPAFSMAGKHSQKVTSDSPAPGDYCPEKVRLDHTPAYSFGVKSDPKVENNTPAPGDYHPEKVRQDHNPAYSFAGRHDLQKPDNTPAPGAYFPEKVRLDHNPAFSMAGKYDAKVTNDTPAPGDYSPEKVRQDTNPAYSFAGRHDLHKPSETPAPGAYSPEKVRLDHNPAFTMAGKHDQKILNGTPAPGDYSPEKCRLDHTPAYSFGGKNDPKVENNTPAPGDYHPEKVRLDHNPAYSFAGRHDLQKPSDTPAPGAYSPEKVRQDHNPAFSMAGKPVEKLTNGTPAPGDYSPEKVRLNHTPAYTFGGKNDPKVENNTPAPGDYHPEKVRQDHNPAFSFAGRHDLHKPNDTPAPGAYCPEKVRQDHNPAFSMAGKYTQKVANDTPAPGDYSPEKVRLDHTPAYTFGGKNDPKVESNTPAPGDYHPEKVRQDHNPAFSFAGRHNLQKPSDTPAPGAYSPEKVRQDHNPAFTMAGKHDPKVSNDTPAPGDYSPEKVRLDYTPSFTFAGKNNPKVENDTPAPGDYHPEKVRQDHNPAFSFAGRHDLHKPSDTPAPGAYSPEKVRQDHNPAFSMAGKYIEKITNGTPAPGDYCPEKVRLDHTPAFTFGGKNDPKVENNTPAPGDYHPEKVRQDHVPAFSFAGRHDLHKPNETPAPGAYSPEKVRQDHNPAFTMAGKHDPKVTHDTPAPGDYHPEKVRLDHNPAFSFAGRHDLHKPSETPAPGDYFPEKVRQDFNPAFTFAGKHDPRSLSESPAPGDYSPEKVRLDHAPAFSFGGKHDPKTEHLHPAPCDYAPEKVRLDHTPAYTIAGRPAADHVSQTPAPCDYHPEQCQVDSTPAFTFGMRLGRERISDTPAPSAYEPEKHSLHSTPAYSFGTKSDIRVTTDAPAPGHYHPEQCKLDSSPAYSFGLKTVPTASLPVRNNAECTTTTTNHTNNNAGSSTTTTTTTTTTTKTFINGVEQPELQKKETTKQVNGTHKELKSAPQAPLSNGNIVSNGNHSKMVSTTTRIQEVAHGQKESGNLKVVASGKSDASATKAAAVSHQTVVQADGAIVTSGQSSRMQTVKYAVEASSVQEKIISS
Protein: DnaJ heat shock protein family (Hsp40) member C7 (A0A6I8PU89)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAAAECDVVMAATEPELLDDQEAKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQWWDCSSPRLSL
Protein: Glutathione hydrolase 7 (EC 3.4.19.13) (Gamma-glutamyltransferase 7) (GGT 7) (EC 2.3.2.2) (Gamma-glutamyltransferase-like 3) (Gamma-glutamyltransferase-like 5) (Gamma-glutamyltranspeptidase 7) [Cleaved into: Glutathione hydrolase 7 heavy chain; Glutathione hydrolase 7 light chain] (Q9UJ14)
Organism: Homo sapiens (Human)
Function: Hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07314}.
Interaction partners:
- Glutathione synthetase
- Aminopeptidase N
- Glutathione hydrolase 6
- Glutathione hydrolase 5 proenzyme
- Gamma-glutamylcyclotransferase
- 5-oxoprolinase
- Cytosol aminopeptidase
- Glutathione hydrolase 1 proenzyme
- TLC domain-containing protein 3A
- Glutamate--cysteine ligase catalytic subunit
Sequence:
MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDSFLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATGVTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPHSSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLHEAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPLPGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEKPVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALASRLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMGPDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPLSFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLARGRLHPDLQSNLLQVDSEFTEEEIEFLEARGHHVEKVDVLSWVHGSRRTNNFIIAVKDPRSPDAAGATIL
Protein: 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component (EC 1.18.1.3) (P77650)
Organism: Escherichia coli (strain K12)
Function: Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.
Interaction partners:
- 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin subunit
- 3-phenylpropionate/cinnamic acid dioxygenase subunit beta
- 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha
- 3-phenylpropionate-dihydrodiol/cinnamic acid-dihydrodiol dehydrogenasepropanoate dehydrogenase)
- Anaerobic nitric oxide reductase flavorubredoxin
- Formate dehydrogenase H
- Nitrite reductase small subunit
- Periplasmic nitrate reductase
- Carnitine monooxygenase reductase subunit
- 2Fe-2S ferredoxin
Sequence:
MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANEQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFWSDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIALKSL
Protein: Transthyretin (U6C7B8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361269}.
Interaction partners:
Sequence:
SDTHCPLMVKILDAVKGVPAGAVALSVSRRVNGMTWAQVASGVTDLTGEVHNLISDQDFQSGVYRVEFDTKAYWKSQGTTPFHETAEVVFEAHAEGHRHYTLALLLSPFSYTTTAVV
Protein: Tumor necrosis factor ligand superfamily member 10 (Apo-2 ligand) (Apo-2L) (TNF-related apoptosis-inducing ligand) (Protein TRAIL) (CD antigen CD253) (P50591)
Organism: Homo sapiens (Human)
Function: Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14609566}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:14609566}. Note=Exists both as membrane-bound and soluble form. {ECO:0000269|PubMed:14609566}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 10D
- Tumor necrosis factor receptor superfamily member 10A
- Tumor necrosis factor receptor superfamily member 10B
- Tumor necrosis factor receptor superfamily member 10C
- Tumor necrosis factor receptor superfamily member 6
- Caspase-8
- FAS-associated death domain protein
- Tumor necrosis factor receptor superfamily member 1A
- CASP8 and FADD-like apoptosis regulator
- Tumor necrosis factor ligand superfamily member 6
Sequence:
MAMMEVQGGPSLGQTCVLIVIFTVLLQSLCVAVTYVYFTNELKQMQDKYSKSGIACFLKEDDSYWDPNDEESMNSPCWQVKWQLRQLVRKMILRTSEETISTVQEKQQNISPLVRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG
Protein: Cytochrome P450 monooxygenase (D4QC33)
Organism: Aspergillus oryzae (Yellow koji mold)
Interaction partners:
Sequence:
MEWQIYLGIAFALWIVQVLYTAFTSPLRRVPGPLYTVLTRLPLKLASLTGNRIYFVHELHRKYGPIVRIAPDEVDISSLAEFREIHRAGSPFLKSKWYEKFVPSKRSGVFTMRDPKEHAARRKLFARPFSKSELRRTWEPAVREKVQLAVSQIQRELKAVGKSDLLKWWTFLATDVSGQLMFGESFNMLQLGKKNQYINVLESTMMGSGIGAELPLVAWLGRHIPLSSFQNMFRATDYLFQYGQRAVTNSRTTSNASRNIFAGMVYESEKGDGIITDEEVVLEAGNLIVAGSDTTAITLTYLIWAVLSQPKLQRELEEEVNSLSADFDDSALEELPLLNAVIMEALRLYGAAPGALPRETPEGGAKFCGYFIPQGMTVTTQAYSIHRDGDIYPDPERFDVSRWLKTETSASELAKKAFSPFGAGGRICLGIHLAWMELRLATAQFFRECAGVRLAPSATWENMRPVNYFLISPRGHQCEVECNY
Protein: Multiple C2 domain and transmembrane region protein 7 (Q84TJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000269|PubMed:29259105}. Endosome membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in small structures within cells. {ECO:0000269|PubMed:29259105}.
Interaction partners:
- 16 kDa phloem protein 2
Sequence:
MMMSNLKLGVDVIGAHNLFPKDGQGTSNAYVELYFDGQKHRTTIKDRDLNPVWNESFFFNISDPSRLHYLNLEAQAYSHNRSTNGRSFLGKVSLSGTSFVPHSDAVVLHFPMERRGIFSRVRGELGLKVYITDEASLKSSAASNDHPDNLDPALPRAMNVEHRSDKRHVFYNLPNSAQEHQHQHPQGPNQSSSLAAEQDNHNEHHHHYVPKHQVDEMRSEPARPSKLVHAHSIASAQPADFALKETSPHLGGGRVVGGRVIHKDKTATSTYDLVERMYFLYVRVVKARELPIMDITGSVDPFVEVRVGNYKGITRHFEKRQHPEWNQVFAFAKERMQASVLEVVVKDKDLLKDDYVGFVRFDINDVPLRVPPDSPLAPQWYRLEDKKGEKIKGELMLAVWIGTQADEAFSDAWHSDAAMPVDCSPAISAVLRSKVYHAPRLWYVRVNVIEAQDLIPTDKTRFPDVYVKAQLGNQVMKTRPCQARTLGAVWNEDFLFVVAEPFEDHLVLTVEDRVAPGKDEIVGRTYIPLNTVEKRADDHMIHARWYNLERPVIVDVDQLKREKFSMRIHLRVCLEGGYHVLDESTHYSSDLRPSARPLWRQPIGVLELGILNAVGLHPMKTREGRGTSDTFCVGKYGQKWVRTRTMVDNLCPKYNEQYTWEVFDPATVLTVGVFDNGQLGEKGNRDVKIGKIRIRLSTLETGRIYTHSYPLLVLHPTGVKKMGELHMAVRFTCISFANMLYQYSKPLLPKMHYVRPFSVMQQDMLRHQAVNIVAARLGRAEPPLRKEIIEFMSDTDSHLWSMRKSKANFFRMMTVFSGVIAVGKWFSDICSWRNPITTVLVHVLFLMLVCLPELILPTMFLYMFLIGLWNYRFRPRYPPHMNTKISQAEAVHPDELDEEFDTFPTTRNPDMVRLRYDRLRSVAGRIQTVIGDLATQGERFQALLSWRDPRATAIFVILCFIAAIVFFITPIQIVVALAGFFTMRHPRFRHRLPSVPVNFFRRLPARTDSML
Protein: Mannose-specific lectin (Agglutinin) (NTL-125) (C0HLU1)
Organism: Narcissus tazetta (Cream narcissus)
Function: Mannose-specific lectin (By similarity). Displays antiviral activity and therefore may contribute to defense against infections. Shows agglutinating activity towards rabbit erythrocytes.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P49329}.
Interaction partners:
Sequence:
DNILYSGETLSPGEFLNNGRYVFIMQEDCNLVLYDLDKPIWATNTGGLDRRCHLSMQSDGNLVVYSPRNNPIWASNTGGENGNYVCVLQKDRNVVIYGTARWATGTNIHGAGIVGVPGSAPQNSTAEMMKLVRKYLITK
Protein: Virulence factor mce family protein (O53542)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MLNRKPSSKHERDPLRTGIFGLVLVICVVLIAFGYSGLPFWPQGKTYDAYFTDAGGITPGNSVYVSGLKVGAVSAVSLAGNSAKVTFSVDRSIVVGDQSLAAIRTDTILGERSIAVSPAGSGKSTTIPLSRTTTPYTLNGVLQDLGRNANDLNRPQFEQALNVFTQALHDATPQVRGAVDGLTSLSRALNRRDEALQGLLAHAKSVTSVLSERAEQVNKLVEDGNQLFAALDARRAALSALISGIDDVAAQISGFVADNRKEFGPALSKLNLVLANLNERRDYITEALKRLPTYATTLGEVVGSGPGFNVNVYSVLPGPLVATVFDLVFQPGKLPDSLADYLRGFIQERWIIRPKSP
Protein: Heat shock factor Hsf2 (Heat shock factor protein 2) (Q90XA8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKHSSNVPAFLTKLWTLVEDSDTNEFICWSQEGNSFLVLDEQRFAKEILPKFFKHNNMASFVRQLNMYGFRKVMHIDSGIVKQERDGPVEFQHPYFKHGQDDLLENIKRKVSNARPEESKIRQDDLSKILTSVQSVHEQQENMDARLATLKRENEALWTELSDLRKVHVQQQQVIKELVQFIFTLVQNNRLLNLKRKRPLALNINGKKSKFIHQLFEEPIDHSKTTVNGLKNNSDISDDVIICDITDEDPEVTDGISVPDEEDAEIVEITYESSPKTVQQDSANGTIVNSTAHQEAEPKTTHDVSTTNSALQLNKPSCLSLEDPMKLMDSILSENGAISQNINLLGKVELMDYLDSIDCSLEDFQAMLYGKQFNIDPDIIEETISETKNNNSKANKENLDSENTDKQLIQYTTCPLMAFLDGCTPLTPSDPQPEDPPDLLDESLEMKTPRSSLIRLEPLTEAEANEATLFYLCELNSDLPNADTPPLDI
Protein: Leucine zipper protein 1 (Filamin mechanobinding actin cross-linking protein) (Fimbacin) (Q86V48)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26638075, ECO:0000269|PubMed:32496561, ECO:0000269|PubMed:32553112}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:32496561}. Midbody {ECO:0000269|PubMed:32496561, ECO:0000269|PubMed:32553112}. Chromosome, centromere {ECO:0000269|PubMed:38009294}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:38009294}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:30990684, ECO:0000269|PubMed:32553112, ECO:0000269|PubMed:38832964}. Nucleus {ECO:0000250|UniProtKB:Q9ESV1}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9ESV1}. Perikaryon {ECO:0000250|UniProtKB:Q9ESV1}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8R4U7}. Note=Localizes to the proximal end of basal bodies (PubMed:32496561). During mitosis, localizes at the inner centromere in metaphase, at the central spindle in anaphase, and at the midbody in telophase (PubMed:38009294). Central spindle localization requires KIF20A while centromere localization requires the kinase activity of the chromosomal passenger complex (PubMed:38009294). {ECO:0000269|PubMed:32496561, ECO:0000269|PubMed:38009294}.
Interaction partners:
- Death-associated protein kinase 3
Sequence:
MAEFTSYKETASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGEVEGEDAFLSSKGRHERTKFRGHGSEASVSKHTARELSPQHKRERLRNREFALNNENYSLSNRQVSSPSFTNRRAAKASHMGVSTDSGTQETKKTEDRFVPGSSQSEGKKSREQPSVLSRYPPAAQEHSKAWKGTSKPGTESGLKGKVEKTTRTFSDTTHGSVPSDPLGRADKASDTSSETVFGKRGHVLGNGSQVTQAANSGCSKAIGALASSRRSSSEGLSKGKKAANGLEADNSCPNSKAPVLSKYPYSCRSQENILQGFSTSHKEGVNQPAAVVMEDSSPHEALRCRVIKSSGREKPDSDDDLDIASLVTAKLVNTTITPEPEPKPQPNSREKAKTRGAPRTSLFENDKDAGMENESVKSVRASTNTMELPDTNGAGVKSQRPFSPREALRSRAIIKPVIVDKDVKKIMGGSGTETTLEKQKPVSKPGPNKVTSSITIYPSDSSSPRAAPGEALRERHTSTSNIQVGLAELTSVSNHVSSPFELSIHKHDITLQLAEAERMADGPLKDRPETVVSRSSIIIKPSDPVERNSHAPPAETIRWKSHSAPSEVGFSDARHVTVRNAWKSRRDLKSLEDPPTRIGKNVESTNSNAYTQRSSTDFSELEQPRSCLFEQGTRRVGPSSGDAPEPSSRRTQSSLTVSEVLTRRNRVGDTITVAAWNHSASMEEEGEDCTLSVYRQLHNSLDPSELPGKQGLPESGRVRAEERLRPTRPCAEEN
Protein: Protein LURE 1.1 (AtLURE1.1) (Cysteine-Rich Peptide 810_1.1) (CRP810_1.1) (Defensin-like protein 217) (Q4VP09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pollen tube attractants guiding pollen tubes to the ovular micropyle.
Subcellular location: Secreted {ECO:0000269|PubMed:23271953}. Note=found at the micropylar end of the female gametophyte, possibly at the filiform apparatus of the synergid cell. Difuses to the surface of the funiculus of the ovule through the micropyle. {ECO:0000269|PubMed:23271953}.
Interaction partners:
- Uncharacterized protein
- Pollen receptor-like kinase 6
- Pollen receptor-like kinase 3
- Defensin-like protein 308
- Protein MALE DISCOVERER 1
- F-box/kelch-repeat protein At5g43190
- MDIS1-interacting receptor like kinase 1
- Cysteine rich peptide
- Cysteine rich peptide
- Transmembrane protein
Sequence:
MKLIFIFLTLLIFVSSCTSILIKESSEEERIYPFNPVASPFDPRSLNQILKIGKIGYCFDCARACMRRDRYIRTCSFERKLCRCSYSHIHHTHG