wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein kinase Fer (EC 2.7.10.2) (Proto-oncogene c-Fer) (Tyrosine-protein kinase FLK) (p94-Fer) (P09760)
Organism: Rattus norvegicus (Rat)
Function: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this clearly depends on cell type and stimulus (By similarity). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}. Cell junction {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Note=Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts (By similarity). {ECO:0000250}.
Interaction partners:
- Catenin beta-1
- Catenin delta 1
- Tyrosine-protein kinase Yes
Sequence:
MGFGSDLKNSQEAVLKLQDWELRLLETVKKFMALRIKSDKEYAYTLQNLCNQVDKDSTVQVNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYVGIHQQIEAEMIKVTKTELEKLKSSYRQLIKEMNSAKEKYKEALAKGKETEKAKERCDKATMKLHMLHNQYVLALKGAQLHQSQYYDTTLPLLLDSVQKMQEEMIKALKGIFDEYSEITSLVTEEIVNVHKEIQMSVDQIDPSTEYNDFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTADSLQVMLKTLAEELTQTQQMLLHKEAAVLELEKRIEESSETCAKKSDIVLLLGQKQALEELKQSVQQLRCTEAKCAAQKELLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIKSPKSVLGSSTQLSDVISVGEKPLAEHDWYHGAIPRIEAQELLKQQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQFVDNLYRFEGTGFSNIPQLIDHHFNTKQVITKKSGVVLLNPIPKDKKWVLNHEDVSLGELLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVPGGDFLSFLRKRKDELKLKQLVRFSLDVAAGMLYLEGKNCIHRDLAARNCLVGENNTLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQNCPEEIFTIMMKCWDYKPENRPKFSDLHKELTAIKKKIT
Protein: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 3, mitochondrial (EC 1.3.5.1) (Iron-sulfur subunit of complex II) (Ip) (Q9FJP9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate--CoA ligase subunit alpha-2, mitochondrial
- Succinate--CoA ligase subunit alpha-1, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Fumarate hydratase 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- Fumarate hydratase 2
- L-aspartate oxidase, chloroplastic
- Cytochrome b-c1 complex subunit Rieske-2, mitochondrial
Sequence:
MSSVLRLLGRRICNPAAEKVRLSSSLSGGGDFPILNGHKAAQDLSKDTLKSQDITKEKEGQHKEVKKEFKIYRWNPDKPNSKPFLQSFFVDLSSCGPMVLDVLQKIKAEDDASLSYRRSCREGICGSCSMNIDGTNTVACLKPINPNTSKPTIITPLPHMYVIKDLVVDLTNFYQQYKSMEPWLKTRKPPKDGREHRQSPKDRKKLDGLYECILCACCTTSCPSYWWNPEEFPGPAALLQAYRWISDSRDEYREERLQAITESETKVYRCRAIKNCTATCPKGLNPASAILKMKSKHLLSDPLVRTESV
Protein: Phospholipid scramblase (Q9VZW1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Putative lipoyltransferase 2, mitochondrial
Sequence:
MMQMSEYKVLPQNAPQDENGAVVLQPQAANVGNNANGPENWMSIPVGMPNCPQGLEYLTALDQLLVSQKIEKLELLTGFETKNRFKVKNSLGQNVYFAYEESDCCTRNMLGRSRPFEMKILDNFQNEVLHLYRPFKCDILCCFPSCMNAVEVSAPPGQVIGSVEQVCTFMRPKFNIKNTCGDTVLQIEGPVCPCKCFSDTNFKVLSANNEEIGKISKQWSGLGRELFTDADYFSVTFPLNLDVRMKALIFAALFLIDAVYYEQ
Protein: Nitrogen assimilation transcription factor nirA (P28348)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Pathway-specific regulatory gene of nitrate assimilation; it activates the transcription of the genes for nitrate and nitrite reductases (niaD and niiA).
Subcellular location: Nucleus.
Interaction partners:
- Nitrate reductase
- Nitrite reductase [NAD
- Nitrate transporter
- Mediator of RNA polymerase II transcription subunit 13
- RNA polymerase II holoenzyme cyclin-like subunit
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 31
Sequence:
MGEKLDPELSSDGPHTKSSSKGQGTSTDNAPASKRRCVSTACIACRRRKSKCDGNLPSCAACSSVYHTTCVYDPNSDHRRKGVYKKDTDTLRTKNSTLLTLIQALLNYEEEDAFDLVRQIRSCDNLEDVAQSLVNQEKKSSGWLSNAVIHEENDIAQTDQFESELAGKMSNLVLDGSRKFIGGTSNLIFLPPGSELNEFKPGLATNGDLEGSVTRWTTVTDDQQLISHLLTMYFSWHYPFFTTLSKELFYRDYSRGVPSQYCSSLLVNTMLALGCHFSSWPGAREDPDNSATAGDHFFKEAKRLILDNDELVNSKLCTVQALALMSVREAGCGREGKGWVYSGMSFRMAFDLGLNLESSSLRDLSEEEIDARRITFWGCFLFDKCWSNYLGRQPQFTTANTSVSAVDILPNEESTLWSPYSDMGPSREYAQPSRTRAVADQISQLCKISGDLVVFFYDLAPKEKPSSKQLELKKLSEIHTRLEAWKKGLPKELEPREGQLPQALLMHMFYQLLLIHLYRPFLKYTKSTSPLPQHVSPRKLCTQAAAAISKLLRLYKRTYGFKQICNIAVYIAHTALTIHLLNLPEKNAQRDVIHGLRHLEEMGESWLCARRTLRILDISASKWQVQLPREAVIVFEQTHARWGSWGPWDQAASPSTTSDSPPSVSSQSVVATTDLSQPVSQSAGNQPANPSMGTSPNLTQPVASQYSSTPSGPVSVSAMRAVQRSFSAQLAHNEARQPEPTYLRPVSTSYGPVPSTQSAQEQWYSPTEAQFRAFTAAHSMPTTSAQSPLTTFDTPENLVEESQDWWSRDVNALQLGAEDWTQNWNNGLPTTSADWRYVDNVPNIPSTSAPDADYKPPQPPPNMARPNQYPTDPVANVNSNQTNMIFPGSFQR
Protein: Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.1) (EC 3.1.2.11) (EC 3.1.2.2) (EC 3.1.2.3) (EC 3.1.2.5) (Choloyl-coenzyme A thioesterase) (EC 3.1.2.27) (HIV-Nef-associated acyl-CoA thioesterase) (Peroxisomal acyl-CoA thioesterase 2) (PTE-2) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1) (Thioesterase II) (hACTE-III) (hACTEIII) (hTE) (O14734)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT) (By similarity). Is also able to hydrolyze CoA esters of dicarboxylic acids (By similarity). It is involved in the metabolic regulation of peroxisome proliferation.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:15194431}. Note=Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded. {ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:15194431}.
Interaction partners:
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Acyl-coenzyme A thioesterase 1
- Sterol carrier protein 2
- Bile acid-CoA:amino acid N-acyltransferase
- Long-chain fatty acid transport protein 5
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Peroxisomal targeting signal 1 receptor
- Lambda-crystallin homolog
- Peroxisomal multifunctional enzyme type 2
- Peroxisome proliferator-activated receptor alpha
Sequence:
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAAQEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTALLPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVKPQVSESKL
Protein: T-complex protein 1 subunit alpha (TCP-1-alpha) (CCT-alpha) (DdTcp-1) (Q55BM4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MSNKVLMIDGDRISGNEVRAQNVLAVTAIANIVKTSFGPIGLDKMLIDNIGSIVVTNDGATILQKIDIEHPAAKILVQLSELQDQEVGDGTTTVVILAAELLKRANELVARKVHPTVIISGFRLACTEAIKYINETLAVKVETLPKDFIVNIAKTSMSSKTINDDSDFFSKIVIEAITRVKTIDYKGDVKYPINAINILKAHGKSAKESTLVEGYALNCTVASEGMPKRIQGAKIAFLDFNLAKTKMKLGQKVVVTNVNDLEAIRDRENDIVKERISLIIKSGANVVLTTKGIDDLCLKYFVEAGCMAVRRCKKEDLKRIAKSCGGTVLITLANLEGEESFDTTALGIADEVVQDRLADDELIIVKNSNKKSASIILRGANELMLDEMERSIHDSLCIVKRTLESGTIVPGGGAVESALSIYLDNIAATMGSRKQLAISEFAESLLVVPKQLAVNAALDASDLVSKLKAYHHAAQTDPSKKSYAYSGLDLFNNKVRNNLEAGVLEPAIAKIKCIKFATESAITILRIDDKITLNPREQQGGDHEGHGH
Protein: Putative transcription factor bHLH086 (Basic helix-loop-helix protein 86) (AtbHLH86) (bHLH 86) (Protein ROOT HAIR DEFECTIVE 6-LIKE 1) (AtRSL1) (Protein RHD SIX-LIKE 1) (Transcription factor EN 113) (bHLH transcription factor bHLH086) (Q9FJ00)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that is specifically required for the development of root hairs. Acts with RHD6 to positively regulate root hair development. Acts downstream of genes that regulate epidermal pattern formation, such as GL2. Acts with RHD6 as transcription factor that integrates a jasmonate (JA) signaling pathway that stimulates root hair growth.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17556585, ECO:0000269|PubMed:31988260}.
Interaction partners:
- Transcription factor bHLH120
- Transcription factor MAMYB
Sequence:
MSLINEHCNERNYISTPNSSEDLSSPQNCGLDEGASASSSSTINSDHQNNQGFVFYPSGETIEDHNSLMDFNASSFFTFDNHRSLISPVTNGGAFPVVDGNMSYSYDGWSHHQVDSISPRVIKTPNSFETTSSFGLTSNSMSKPATNHGNGDWLYSGSTIVNIGSRHESTSPKLAGNKRPFTGENTQLSKKPSSGTNGKIKPKATTSPKDPQSLAAKNRRERISERLKVLQELVPNGTKVDLVTMLEKAIGYVKFLQVQVKVLAADEFWPAQGGKAPDISQVKEAIDAILSSSQRDSNSTRETSIAE
Protein: Lysosomal-associated transmembrane protein 5 (Lysosomal-associated multitransmembrane protein 5) (Retinoic acid-inducible E3 protein) (Q61168)
Organism: Mus musculus (Mouse)
Function: May have a special functional role during embryogenesis and in adult hematopoietic cells.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:8661146}; Multi-pass membrane protein {ECO:0000269|PubMed:8661146}.
Interaction partners:
- Lysosomal-associated transmembrane protein 4B
- Lysosomal-associated transmembrane protein 4A
- Nck-associated protein 1-like
- Leukocyte surface antigen CD53
- E3 ubiquitin-protein ligase NEDD4
- Integrin beta-2
- SAM and SH3 domain-containing protein 3
- Coronin-1A
- TYRO protein tyrosine kinase-binding protein
Sequence:
MASRAAPVRQTCCCFNIRVATIALAIYHIVMSVLLFIEHVVEVARGKVSCRFFKMPYLRMADLLSSFLLIGVLFIISISLLFGVVKNREKYLIPFLSLQIMDFLLCLLTLLGSYIELPAYLKLARPRPGPSKVPLMTLQLLDFCLSILTLCSSYMEVPTYLNFKSMNHMNYLPSQEGVPHSQFINMMLIFSVAFITVLILKVYMFKCVYTCYKFLKHMNSAMEDSSSKMFLKVALPSYEEALSLPPKTPEGDPAPPPYSEV
Protein: Sorting nexin (Q9NCC3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26
- Sorting nexin 6, isoform B
- Activated Cdc42 kinase Ack
- Dynamin
- FI18122p1
- Sorting nexin-3
- RE12101p
- FI21262p1
Sequence:
MTSYVRAMYDFTGEPGSSELSIATGDVLSVTRSDVGEGWWEGKNARGQIGLFPAAYVEVMSAAEAQKLSASGATSVPQVPDPFASPPLPRYDQTADDDGSNWDDEDDWSDDNDTYSEIGPGGQKSAGQSARAGGLSHSTSDYDNKHLPIAPNDDTQSLASVAGGTGAAGTVKKGMFAKSSDSYILGLSSTKEKIPECEMAYITQVEDSIYQWTQNHSPYSVVVASPKKESKFKGMKTFIAYQLTPSFNNISVSRRYKHFDWLHERLVDKFCLIPVPPLPDKQISGRYEEQFVEHRRVQLQEFVDWVCRHPVISKCEVWYHFLTCRDEKIWKSGKRKAERDPYMGVNYCLAISPPDKNLLHSKVDAQVELGTQFIHSMDVAVRNLNNISNDMAKRSMSQSKKEFQRIGDGLSDLAKALAIDERRAPTRNAVPLSESVGRIGGIFIGIGQAFGDQPKHDWIPLSDRLHIYRGVLNCFPDIFSTHKGAIQKRKDCEKLAGEGRMNNPQLHDVNRRTDVVSYTVLAELTHFKSERDTHLKHTLKNFIAEQIKFYQGVVARLQEASRQIE
Protein: Putative ATP-dependent RNA helicase PB1A10.06c (EC 3.6.4.13) (Q9HDY4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Uncharacterized protein C57A7.06
- Probable nucleolar complex protein 14
- U3 small nucleolar ribonucleoprotein protein mpp10
- Periodic tryptophan protein 2 homolog
- U3 small nucleolar RNA-associated protein 22
- Uncharacterized protein C3B8.09
- Uncharacterized protein C1604.06c
- U3 small nucleolar RNA-associated protein 6
- U3 small nucleolar RNA-associated protein 4
- Nucleolar protein 58
Sequence:
MGRLRKRFNEKGRQSGIQKMLNLKRARLHRSVREQESSSEVHANPEPDNQDSNAEILIDVPKEERQKRKQELKDQLLKENEGSISSKKKKRLDKYIENKLKKEEVASLIAKLAEERIDTSLLSSSKNLGKQATAKEKLKKSLLEEKLGLPLSDADSRLYKVVDVETTTTKSSTAETNAPEKYSTRSGFGFGFSTGTNESEITPNIKVLPPKKKKNASWGKMLNEDPEYDSAEEDYLSTDSEEFSEDSDNSSEENKDTNEPSTKDAEKTVPEDVVNLRSEQKLQPSFGHPEFENEDFDLETSEDDSSDDATERASRFKSWANKQILGADVGEKSHDVAPDNKIDNPDADMVRAQRMPRKLKMREEDVEPTADDIEIKGRKTTYTIINRPPEIQESRLALPIVAEEQRIMEQIFANDVVIICGATGSGKTTQLPQFLFEAGFSSPESENPGMIAITQPRRVAAVSIAKRVSEELTGFSSKVSYQIRFDSTINPDTAIKFMTDGILLRELSSDFLLTAYSAVIVDEAHERSVNTDILLGLLSRIVRLRREMSKSDQKVKPLKLIIMSATLRVTDFSENKLLFSVPPPIIKIDARQYPVSIHFNRTTKPDYLQDAFDKVCLIHKRLPAGSILVFLTGQQEVEQLCQMLRKRFVRSFRPLKSRARIVVSRKTMSVENEDLQSETEDIDQVPTSSSSSVTYDDESEPMYVLPLYSLLTTEDQMKVFDSSPEGHRMCIVATNVAETSITIPNIRYVVDCGKAKERVYNEKTSVQKFEVRWISKANADQRAGRAGRTGPGHCYRLYSSAVFDSSFPLHSLPEILRTPVESIVLQMKNMNIDNIANFPFPTSPGRSRLEKSLKLLSNLGAIDSEGVLTKLGEQMSLFPLSPRFSKMLIIGQQHGCLPYVIALVSALSINQLFVSKQSLLYDAHDKNSRSEETDLIDDDEIKQKEEYKNRMRGYFNAISRFQAIDPDAPALSLLSAVCAYDYASDKRKFCKENYLREKALEEVTNLRKQIIGLLKRYMVRVEKEFFKLQLKPPTSVQIKALRQFIASAYIDQVALYDKEKRGYVTLFPSGSEVVQFVPDRTYNIDSEYVVYLSLHESRSGRVYMSPLTEISPEHLARLAKNTTLLSYSKPLSYPPIRYLDNATKRECWVIPILSANIGTGSPSWNLPAVQIIQKRINGRWVNC
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (F1LP57)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 7
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 8
- Beta-arrestin-2
- mitogen-activated protein kinase kinase kinase
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase kinase kinase 1
- C-Jun-amino-terminal kinase-interacting protein 3
- Mitogen-activated protein kinase 14
- Filamin-C
Sequence:
AYFFLNFKIFGKRKALKLNFANPPVKSTARFTLNPNTTGVQNPHIERLRTHSIESSGKLKISPEQHWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERTVEVACYVCKILDQMPATPSSPMYVD
Protein: Thymidylate kinase (EC 2.7.4.9) (dTMP kinase) (P23919)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of thymidine monophosphate (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the DNA building block dTTP, with ATP as the preferred phosphoryl donor in the presence of Mg(2+).
Interaction partners:
- Thymidylate synthase
- Thymidine kinase 2, mitochondrial
- Deoxycytidylate deaminase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
- Nucleoside diphosphate kinase, mitochondrial
- Ribonucleoside-diphosphate reductase large subunit
- Thymidine kinase, cytosolic
- 5'
- Nucleoside diphosphate kinase 6
- Nucleoside diphosphate kinase A
Sequence:
MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKKSDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQPDVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDASKSIEAVHEDIRVLSEDAIRTATEKPLGELWK
Protein: G-protein coupled receptor daf-37 (Abnormal dauer formation protein 37) (Q18321)
Organism: Caenorhabditis elegans
Function: G-protein coupled receptor (GPCR) that forms a heterodimer with daf-38 to control dauer formation and behavior. Receptor for the ascaroside pheromone ascr#2. Required for the response to dauer inducing pheromones, specifically the ascaroside ascr#2. May serve neuronal specific roles in response to ascr#2 with expression in ASI neurons controlling dauer formation in larvae, and expression in ASK neurons playing a role in longevity and hermaphrodite repulsion. May function upstream of the daf-11, daf-7 and daf-2 signaling pathways.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22665789}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium {ECO:0000269|PubMed:22665789}. Golgi apparatus {ECO:0000269|PubMed:22665789}. Note=Localizes to the cell membrane in the presence of daf-38, but localizes to the Golgi apparatus in the absence of daf-38. {ECO:0000269|PubMed:22665789}.
Interaction partners:
- G-protein coupled receptor daf-38
- SRBC-64)
- Serpentine Receptor, class BC
- Serpentine receptor class gamma
- Serpentine receptor class gamma
- Guanine nucleotide-binding protein alpha-3 subunit
- Serpentine receptor class X-43
- Guanine nucleotide-binding protein alpha-2 subunit
Sequence:
MDVIGNITDLSPTVSGIPDECGLEPHDFLEVKFFLISVVGTLIGLFGLFGNATTALILTRPSMRNPNNLFLTALAVFDSCLLITAFFIYAMEYIIEYTAAFDLYVAWLTYLRFAFALSHISQTGSVYITVAVTIERYLAVCHPKSSKNMCGPGGAAWTILGVTTFAVVFNCTKFFELQVTVNPSCPDGSNWQSYILLPSAMASNPIYQQVYSLWVTNFVMVFFPFLTLLLFNAIIAYTIRQSLEKYDFHNQKSVVAALSASVNLPRNIAGISSRNELKEKSREATLVLVIIVFIFLGCNFWGFVLTLLERIMGQETLMVEHHIFYTFSREAINFLAIINSSINFVIYLLFGKDFRKELVVVYGCGIRGISLRLPVQDKFVIWRHWKRTKSRISMNTTNRTRHKISLPQTLVEHANLERLEETRFLAHHEDGVQTQVSPIHALRNGSTPKIDTLQDLTSNGRPCKTSIIDDNGTVVCTVTEFP
Protein: Phosphate transport system permease protein PstA (P07654)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15919996}.
Interaction partners:
- Phosphate-binding protein PstS
- Phosphate import ATP-binding protein PstB
- Phosphate transport system permease protein PstC
- Phosphate-specific transport system accessory protein PhoU
- Phosphate regulon sensor protein PhoR
- Phosphonates-binding periplasmic protein
- Phosphate regulon transcriptional regulatory protein PhoB
- Low-affinity inorganic phosphate transporter PitB
- Phosphonates import ATP-binding protein PhnC
- sn-glycerol-3-phosphate transport system permease protein UgpE
Sequence:
MAMVEMQTTAALAESRRKMQARRRLKNRIALTLSMATMAFGLFWLIWILMSTITRGIDGMSLALFTEMTPPPNTEGGGLANALAGSGLLILWATVFGTPLGIMAGIYLAEYGRKSWLAEVIRFINDILLSAPSIVVGLFVYTIVVAQMEHFSGWAGVIALALLQVPIVIRTTENMLKLVPYSLREAAYALGTPKWKMISAITLKASVSGIMTGILLAIARIAGETAPLLFTALSNQFWSTDMMQPIANLPVTIFKFAMSPFAEWQQLAWAGVLIITLCVLLLNILARVVFAKNKHG
Protein: AP-1 complex-associated regulatory protein (2c18) (Adaptor-related protein complex 1-associated regulatory protein) (Gamma-1-adaptin brefeldin A resistance protein) (GBAR) (Gamma-BAR) (Gamma-A1-adaptin and kinesin interactor) (Gadkin) (Q63HQ0)
Organism: Homo sapiens (Human)
Function: Necessary for adaptor protein complex 1 (AP-1)-dependent transport between the trans-Golgi network and endosomes. Regulates the membrane association of AP1G1/gamma1-adaptin, one of the subunits of the AP-1 adaptor complex. The direct interaction with AP1G1/gamma1-adaptin attenuates the release of the AP-1 complex from membranes. Regulates endosomal membrane traffic via association with AP-1 and KIF5B thus linking kinesin-based plus-end-directed microtubular transport to AP-1-dependent membrane traffic. May act as effector of AP-1 in calcium-induced endo-lysosome secretion. Inhibits Arp2/3 complex function; negatively regulates cell spreading, size and motility via intracellular sequestration of the Arp2/3 complex.
Subcellular location: Golgi apparatus, trans-Golgi network. Late endosome. Early endosome. Note=Localizes to the juxta-nuclear Golgi region and to tubular structures throughout the cytoplasm, which are highly mobile and cycle between the juxta-nuclear area and the cell periphery.
Interaction partners:
- Cytochrome P450 2C18
- E3 ubiquitin-protein ligase TRIM23
- AP-1 complex subunit gamma-1
Sequence:
MGNCCWTQCFGLLRKEAGRLQRVGGGGGSKYFRTCSRGEHLTIEFENLVESDEGESPGSSHRPLTEEEIVDLRERHYDSIAEKQKDLDKKIQKELALQEEKLRLEEEALYAAQREAARAAKQRKLLEQERQRIVQQYHPSNNGEYQSSGPEDDFESCLRNMKSQYEVFRSSRLSSDATVLTPNTESSCDLMTKTKSTSGNDDSTSLDLEWEDEEGMNRMLPMRERSKTEEDILRAALKYSNKKTGSNPTSASDDSNGLEWENDFVSAEMDDNGNSEYSGFVNPVLELSDSGIRHSDTDQQTR
Protein: RHS1a (Q8T9M8)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MSRANSPAAPQGNNENQQVADNFEGPMRRPRDENVPPPPPPAAAAAAQPPQIRQRTEGGPNWTMDSKVRDVLLDDYAGLRNLTLHDFLLKKFLNTYNTENVAMDVFVQSPGDYILDAGILERIQRLYQFEEYKELYDQFSEMKRKARYLDEKEIYYLSQWEEKGTVEIREFVGPVARGRLDGAVTAAKRAEKRAAQTADGSELKGVYDSIYNATWSYVESGHDTEPLGMKVFNGRPPHMWTKEEVDVSHTPETMNEPLPRHGNLEIAVLTSQMGWPYTSFEKNPNDYDINHEKGVEYVFKSDVYIRREALRVWYKVENVLNRWLMDEVIVDDASNVLIGTPGIGKSFSVGSLLLYKLLHYEASQLQIIIYVVRGKAYVFHKPIGGRAGYVTFYNDYGNAFTVVEQIIGGSRSGEDIKGYVIFDVDKDHPAPTKPPAGCAGIALSSPNVKQFHEWSKQNTASDIYMNCDTLKDLEAIHISRWGKIAPAYKWSPPVAKEKIESEWQEIQARIRIVGPLLRHIGRLSSYNRQEGKVQEAIGKMKDDDMNDYAKYFQNAAMWQTDEVSHKLVGVVRVKEEKLLCEMYRCRPLSSYTGQAILDFLIPWLTDKYAAMSALLSNRAIAAYMFEKSGIEALSHENTLTELARELQGLSFARNQIPQSVLQVLQEPRLIGPSIVVPEDVPIVAGAEIQYMKLYKPQSRSFPVVDAFFFVESPKTFVGLQYTVSGRHPCSTGGLFKMKRYLRSYFQGWDNFSNDMVWEIIYVQRVDSEKITKPQCCERTDRDEGQNNEVEERFWKREVRQFAVSLYKHIIALYVELKTRGENNNGVNNRGGNNA
Protein: Endo-1,4-beta-xylanase 1 (AtXyn1) (Xylan endohydrolase 1) (Xylanase 1) (EC 3.2.1.8) (A0A1P8AWH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to and hydrolyzes insoluble and soluble xylan substrates (By similarity). Exhibits xylanase activity.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:12154138}.
Interaction partners:
- At5g48430
- Probable thionin-2.4
Sequence:
MKRFTVCCFSNKIHKNGDRNPDKKSRESMEVSRKDNEEPEKQNNNNVASIIGSDRTNVIVNHDFSSGMHSWHPNCCEAFVVTAESNVSHGVLDPSKCGSYVVVKNRKETWQGLEQDITNRVKPCSLYKVSATVAVSGPVHGLVEVMATLKLESQQSQTNYQFIAKTCVFKEKWVRLEGMFSLPSLPEKVVFYLEGPSPGIDLLIQSVTIHRESEPELERVTAEDETIVVNPNFEDGLNNWSGRSCKIVLHDSMADGKIVPESGKVFASATERTQNWNGIQQEITGKVQRKRVYEATAVVRIYGNNVTTATVQATLWVQNPNQRDQYIGISTVQATDKEWIHLKGKFLLNGSASRVVIYIEGPPPGTDILLNSLTVKHAEKIPPSPPPSIENPAFGVNILTNSHLSDDTTNGWFSLGNCTLSVAEGSPRILPPMARDSLGAHERLSGRYILVTNRTQTWMGPAQMITDKLKLFLTYQISVWVKVGSGINSPQNVNVALGIDSQWVNGGQVEINDDRWHEIGGSFRIEKNPSKALVYVQGPSSGIDLMVAGLQIFPVDRLARIKHLKRQCDKIRKRDVILKFAGVDSSKFSGASVRVRQIRNSFPVGTCISRSNIDNEDFVDFFLKNFNWAVFANELKWYWTEPEQGKLNYQDADDMLNLCSSNNIETRGHCIFWEVQATVQQWIQNMNQTDLNNAVQNRLTDLLNRYKGKFKHYDVNNEMLHGSFYQDKLGKDIRVNMFKTAHQLDPSATLFVNDYHIEDGCDPKSCPEKYTEQILDLQEKGAPVGGIGIQGHIDSPVGPIVCSALDKLGILGLPIWFTELDVSSVNEHIRADDLEVMMWEAFGHPAVEGIMLWGFWELFMSRDNSHLVNAEGDVNEAGKRFLAVKKDWLSHANGHIDQNGAFPFRGYSGNYAVEVITTSSSKVLKTFGVDKEDSSQVITVDLQGL