wanglab/gogpt-training-data huggingface dataset:
Protein: Artemisinic aldehyde Delta(11(13)) reductase (EC 1.3.1.92) (C5H429)
Organism: Artemisia annua (Sweet wormwood)
Function: Involved in the biosynthesis of the antimalarial endoperoxide artemisinin. Catalyzes the double bond reduction of artemisinic aldehyde to produce (11R)-dihydroartemisinic aldehyde. Also able to reduce 2-cyclohexen-1-one into cyclohexanone to a lesser extent.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18495659}.
Interaction partners:
- OPC-8:0 CoA ligase1
- allene-oxide cyclase
- allene-oxide cyclase
- allene-oxide cyclase
- allene-oxide cyclase
- AMP-dependent synthetase/ligase, AMP-binding enzyme C-terminal domain protein
- AMP-binding, conserved site-containing protein
- AMP-binding, conserved site-containing protein
- AMP-binding, conserved site-containing protein
- AMP-binding, conserved site-containing protein
Sequence:
MSENPPTLFSAYKMGNFNLSHRVVLAPMTRCRAINAIPNEALVEYYRQRSTAGGFLITEGTMISPSSAGFPHVPGIFTKEQVEGWKKVVDAAHKEGAVIFCQLWHVGRASHQVYQPGGAAPISSTSKPISKKWEILLPDATYGTYPEPRPLAANEILEVVEDYRVAAINAIEAGFDGIEIHGAHGYLLDQFMKDGINDRTDEYGGSLENRCKFILQVVQAVSAAIATDRVLIRISPAIDHTDAMDSDPRSLGLAVIERLNKLQFKLGSRLAYLHVTQPRYTADGHGQTEAGANGSEEEVAQLMKTWRGAYVGTFICCGGYTRELGLQAVAQGDADLVAFGRYFVSNPDLVLRLKLNAPLNRYDRATFYTHDPVVGYTDYPSLDKGSLL
Protein: RING-type domain-containing protein (O01481)
Organism: Caenorhabditis elegans
Interaction partners:
- RING-type domain-containing protein
- General receptor for phosphoinositides 1-associated scaffold protein 1 homolog
- B30.2/SPRY domain-containing protein
- Kinesin 1 cargo adaptor alternative variant a
- Ubiquitin-conjugating enzyme E2 W
- E2 ubiquitin-conjugating enzyme
- STI1 domain-containing protein
- TPR_REGION domain-containing protein
Sequence:
MSATKSEMPADVASVTDSSAASPAFPLIGDFLEEFLKCQVCCTNYNETTKLARGLHCGHTFCTECIKTMQKYGNSAYLECPSCRAETKCDIAAVSTNFAIMELIRKCGFLGPEKPEEPPMKQAAQPQLEQTIDELIDEGYRLLIADVKADLMAKFEQLRDVSKTSTIEATKADLEVLCDSVKEAVYEADLEYSYDEEESDEDEEENEDEEDVEEEEEKPCAEKKSPAQPERSSSLVRGFQIGLSRLFRNRRIHTEHLQVDHGAIATKLETRAACTEKSDNVKK
Protein: SLP-76 adaptor protein (Q9DG07)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MDLRNIPYRSEVITWNPDDLAEYFKTLKYKDCEKVVRKHSINGQRFLNMSENDIQKFPKLRVPIVSKLSQEINRNEGRISFFPKWGQTQKCPENSGYSQEDDGWSSFDEDDDYESPDDDQEKEDEADYESPTEETEEAEHDSDGYEPPPSNNDEAHHNVIFPAKSLANNTDYIDRPPTSRSSHQPPVPPQRPGPSPAPASFGGRGASLPAFPPLPGNNDRNVKPSKPPAPSIDRSTKPPLDRLGPPFERENPVPGRKPGHPEKLLTPQLRALGEQLAMMPKPPVPPSDRYERGNPSPLRKQIPVKQGWAQQKRPEEEEDHIPQRAVPQISLPPYSSNTFPSKSIKAPPKPGSNSIPGAESARSLSASGSLPPRFPLGNNSRSPSRGTADLRPPLPIPSRQTAHQTNTEEDEDSLNDEWYVAYISRPEAEAALRKINKDGTFLVRDSSRKTTTHPYVLMVLYKDKVYNIQIRYQEQDQTYLLGTGLKGKEDFSSVAHIIDYFQRTPLLLIDGKDRGSRNQCVLKYAAGNIK
Protein: Non-specific lipid-transfer protein (LTP) (NsLTP) (A0A7G2A2Z3)
Organism: Macadamia integrifolia (Macadamia nut)
Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
Interaction partners:
Sequence:
MANSGVMKLVCLVLACMVVAAPLAEAAITCGQVVSKLAPCLTYLRSGGAVPGTCCNAVKNLNNSAKTTPDRQTACGCLKNAYNSISGINAAYAGGLPAKCGVNLPYKISPSINCATYTLSLYNF
Protein: Helix-loop-helix DNA-binding domain containing protein (Q8H8H9)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MEQWAAAAAADQAAASAGAGQMPFLALLHGAMEADGGGGGDGRKRHAAAAAFASCCPCPPVADLDLLESCVTQAAAPPVTAPATRAERRRKRPRPRPRAAPPPEKRKKPEEAENQRMTHIAVERNRRRLMNDHLASLRSLIPSNYIPRGDQATVVGGAIDYVKQLEQQLVALQAAAAERSGVGVVAAAATAASDGVFVSPQYTSYSEARGGSGVDVEATAAVGGHVRVRVAGRRWTGRLVRAVAAMEDLRLTVLHLAVTSVGHDAVVYCFNLKVKTTTTLHHLLLHVPSFF
Protein: Beta-hexosaminidase subunit alpha (EC 3.2.1.52) (Beta-N-acetylhexosaminidase subunit alpha) (Hexosaminidase subunit A) (N-acetyl-beta-glucosaminidase subunit alpha) (P29416)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme S is as active as the isozyme A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A.
Subcellular location: Lysosome.
Interaction partners:
- Beta-hexosaminidase subunit beta
- Alpha-N-acetylgalactosaminidase
- Alpha-galactosidase A
- N-acetylglucosamine-6-sulfatase
- Ganglioside GM2 activator
- Hexosaminidase D
- Beta-galactosidase
- Beta-1,3-galactosyltransferase 4
- Lactosylceramide alpha-2,3-sialyltransferase
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
Sequence:
MAGCRLWVSLLLAAALACLATALWPWPQYIQTYHRRYTLYPNNFQFRYHVSSAAQAGCVVLDEAFRRYRNLLFGSGSWPRPSFSNKQQTLGKNILVVSVVTAECNEFPNLESVENYTLTINDDQCLLASETVWGALRGLETFSQLVWKSAEGTFFINKTKIKDFPRFPHRGVLLDTSRHYLPLSSILDTLDVMAYNKFNVFHWHLVDDSSFPYESFTFPELTRKGSFNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGAPGLLTPCYSGSHLSGTFGPVNPSLNSTYDFMSTLFLEISSVFPDFYLHLGGDEVDFTCWKSNPNIQAFMKKKGFTDFKQLESFYIQTLLDIVSDYDKGYVVWQEVFDNKVKVRPDTIIQVWREEMPVEYMLEMQDITRAGFRALLSAPWYLNRVKYGPDWKDMYKVEPLAFHGTPEQKALVIGGEACMWGEYVDSTNLVPRLWPRAGAVAERLWSSNLTTNIDFAFKRLSHFRCELVRRGIQAQPISVGYCEQEFEQT
Protein: Probable LRR receptor-like serine/threonine-protein kinase At1g53440 (EC 2.7.11.1) (C0LGG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Sequence:
MGFFFSTRKGLLLIIFICLDIFGSNAQLLPEDEVQTLRTIFRKLQNQTVNIERTSCLDRKWNFVAESTSKLPTSNITCDCTFNASSVCRVTNIQLRGFNLRGIIPPEFGNLTRLTEIDLVLNFLSGTIPTTLSQIPLEILAVTGNRLSGPFPPQLGQITTLTDVIMESNLFTGQLPPNLGNLRSLKRLLISSNNITGRIPESLSNLKNLTNFRIDGNSLSGKIPDFIGNWTRLVRLDLQGTSMEGPIPASISNLKNLTELRITDLRGPTSPFPDLQNMTNMERLVLRNCLIREPIPEYIGTSMTMLKLLDLSSNMLNGTIPDTFRSLNAFNFMYLNNNSLTGPVPQFILDSKQNIDLSYNNFTQPPTLSCNQLDVNLISSYPSVTNNSVQWCLRKDLPCPGDAHHSSLFINCGGNRLKVDKDEYADDLNKRGASTFSSVSERWGYSSSGAWLGNDGATYLATDTFNLINESTPEYYKTARLASQSLKYYGLCMRRGSYKVQLYFAEIMFSNDQTYSSLGRRLFDIYVQGILLERDFNIAQRAGGVGKPFLRQVDEVQVNGSTLEIHLKWTGKGTNVIPTRGVYGPLISAITVTPNFKVDTGKPLSNGVVAGIVIAACVAFGLLVLVILRLTGYLGGKEVDENEELRGLDLQTGSFTLKQIKRATNNFDPENKIGEGGFGPVYKGVLADGMTIAVKQLSSKSKQGNREFVTEIGMISALQHPNLVKLYGCCIEGKELLLVYEYLENNSLARALFGTEKQRLHLDWSTRNKVCIGIAKGLAYLHEESRLKIVHRDIKATNVLLDLSLNAKISDFGLAKLDEEENTHISTRIAGTIGYMAPEYAMRGYLTDKADVYSFGVVCLEIVSGKSNTNYRPKEEFIYLLDWAYVLQEQGSLLELVDPDLGTSFSKKEAMRMLNIALLCTNPSPTLRPPMSSVVSMLQGKIKVQPPLVKREADPSGSAAMRFKALEHLSQDSESQVSTYTRNKEHKSSSSMDGPWVDSSFSDPSKDVSLLQQEEGNSSSSSRRLLDDLTDVEIE
Protein: Photosystem I reaction center subunit V, chloroplastic (PSI-G) (Q9S7N7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Not yet known.
Subcellular location: Plastid, chloroplast membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosystem I reaction center subunit VIII
- Photosystem I iron-sulfur center
- Chlorophyll a-b binding protein 6, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I chlorophyll a/b-binding protein 5, chloroplastic
- Photosystem I reaction center subunit XI, chloroplastic
- Chlorophyll a-b binding protein 4, chloroplastic
- Photosystem I reaction center subunit III, chloroplastic
- Photosystem I reaction center subunit IX
- Photosystem I subunit O
Sequence:
MATSASALLSPTTFSTAISHKNPNSISFHGLRPLRLGGSSSALPKLSTTGRKSSSAVVRAELSPSIVISLSTGLSLFLGRFVFFNFQRENVAKQGLPEQNGKTHFEAGDDRAKEYVSLLKSNDPIGFNIVDVLAWGSIGHIVAYYILATSSNGYDPSFFG
Protein: Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3B (Q9SYB5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dol-P-Glc:Glc
- Lipid phosphate phosphatase gamma
Sequence:
MALKSKLVSLLFLIATLSSTFAASFSDSDSDSDLLNELVSLRSTSESGVIHLDDHGISKFLTSASTPRPYSLLVFFDATQLHSKNELRLQELRREFGIVSASFLANNNGSEGTKLFFCEIEFSKSQSSFQLFGVNALPHIRLVSPSISNLRDESGQMDQSDYSRLAESMAEFVEQRTKLKVGPIQRPPLLSKPQIGIIVALIVIATPFIIKRVLKGETILHDTRLWLSGAIFIYFFSVAGTMHNIIRKMPMFLQDRNDPNKLVFFYQGSGMQLGAEGFAVGFLYTVVGLLLAFVTNVLVRVKNITAQRLIMLLALFISFWAVKKVVYLDNWKTGYGIHPYWPSSWR
Protein: DNA helicase (EC 3.6.4.12) (Q8BR71)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRRRTKREYSGAGPGHDRSRDRHSPPSCHLFPPPPPPLPPPPPPDKDDIRLLPSALGVKKRKRGPKKQKENKPGKPRKRKKLDSEEEFGSERDEYREKSESGGSEYGTGPGRKRRRKHREKKEKKTKRRKRGEGDGGHKQVEQKSSATLLLTWGLEDVEHVFSEEDYHTLTNYKAFSQFMRPLIAKKNPKIPMSKMMTILGAKWREFSANNPFKGSAAAVAAAAAAAAAAVAEQVSAAVSSATPIAPSGPPPALPPPPAPEIQPPPIRRAKTKEGKGPGHKRRNKSPRVPDGRKKLRGKKMAPLKIKLGLLGGKRKKAGSCAFQSEEGHEPEAEESDLDSGSVHSASGWPDGPVRAKKLKRGRPGRKKKKVLGCPAVTGEEEVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELDRAPEGKWSCPHCEKEGVQWEAKEEEEEYEEEGEEGEKEEEDDHMEYCRVCKDGGELLCCDACISSYHIHCLNPPLPDIPNGEWLCPRCTCPVLKGRVQKILHWRWGEPPVAVPAPQQADGNPDVPPPRPLQGRSEREFFVKWVGLSYWHCSWAKELQLEIFHLVMYRNYQRKNDMDEPPPLDYGSGEDDGKSDKRKVKDPHYAEMEEKYYRFGIKPEWMTVHRIINHSMDKKGNYHYLVKWKDLPYDQSTWEEDEMNIPEYDDHKQSYWRHRELIMGEDPAQPRK
Protein: Natural resistance-associated macrophage protein 2 (NRAMP 2) (Divalent cation transporter 1) (Divalent metal transporter 1) (DMT-1) (Solute carrier family 11 member 2) (P49282)
Organism: Mus musculus (Mouse)
Function: Proton-coupled metal ion symporter operating with a proton to metal ion stoichiometry of 1:1. Selectively transports various divalent metal cations, in decreasing affinity: Cd(2+) > Fe(2+) > Co(2+), Mn(2+) >> Zn(2+), Ni(2+), VO(2+) (By similarity). Essential for maintenance of iron homeostasis by modulating intestinal absorption of dietary Fe(2+) and TF-associated endosomal Fe(2+) transport in erythroid precursors and other cells. Enables Fe(2+) and Mn(2+) ion entry into mitochondria, and is thus expected to promote mitochondrial heme synthesis, iron-sulfur cluster biogenesis and antioxidant defense (By similarity). Can mediate uncoupled fluxes of either protons or metal ions.
Subcellular location: [Isoform 1]: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18776082}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:16475818, ECO:0000269|PubMed:18776082}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:16475818}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:16475818}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18776082}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:18776082}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:16475818}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:16475818}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:16475818}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Extracellular vesicle membrane {ECO:0000269|PubMed:27462458}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Metal cation symporter ZIP14
- Ferroportin
- Cytoplasmic aconitate hydratase
- Natural resistance-associated macrophage protein 1
- Plasma membrane ascorbate-dependent reductase CYBRD1
- Hepcidin
- Transferrin receptor protein 1
- Hepcidin-2
- Poly
- Iron-responsive element-binding protein 2
Sequence:
MVLDPKEKMPDDGASGDHGDSASLGAINPAYSNSSLPHSTGDSEEPFTTYFDEKIPIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWVLLLATIVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRIILWLMVELAIIGSDMQEVIGSAIAINLLSAGRVPLWGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYITVKPSQSQVLRGMFVPSCPGCRTPQVEQAVGIVGAVIMPHNMYLHSALVKSRQVNRANKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFEKTNKQVVEVCKNNSSPHADLFPSDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVILTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSEFSNGIGWRIAGGILVLIVCSINMYFVVVYVQELGHVALYVVAAVVSVAYLTFVFYLGWQCLIALGLSFLDCGRSYRLGLTAQPELYLLNTVDADSVVSR
Protein: DNA ligase, putative (EC 6.5.1.1) (Q57VQ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- KU80 protein
- KU70 protein
- DNA ligase
- DNA ligase, putative
- Proliferating cell nuclear antigen
- Protein artemis
- Chromosomal passenger protein
- Inhibitor of apoptosis-promoting Bax1
- Mitochondrial inner membrane signal peptidase, putative
- Exonuclease, putative
Sequence:
MRFSRPCLSSLFATTVPFLSRSSRSASLAKNLAQFHPTIAQTWITAACNKLLQPQHVLPSSRKLAWWRCPYCEHQHPKRIDLHVAAGGACPKCSRMPTLTCSRKRSASSSRTSDNTLAATVKHRCRPDNSLAILDAPNASRVKNSIADNGYLRVSETRNLLPMLARNYDKEVKRISNDEQLFVSPKLDGVRCVVAWNLRDRCLSFFSRSGMLFDCCDHIEPQLRPLFEKDNMLVLDGELYNHDASDFEQLTSAIRTTRQHRTAGIEKVQQQLQYHVFDLLYAKEFPHMTVVPFGQRYKHLCDLMQKINSGKGQGRRKVVKLVPVMSAKKSDIDRLLRLNVDRGYEGIMIRRNGIEDNKCMTSVSSSGGASAAVPGYAYGARSPNLLKYKLMQDSEYIIVDGVEGKGKWRGCLGAFVCQTRAGHRFTVAPATTEERKREMWHRLNVYKGKMLTVQYQELSTNGVPRFPIGKCVRGTKTGSDWV
Protein: Selenium-binding protein 1 (AtSBP1) (O23264)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds cadmium and mediates lower sensitivity to stress requiring glutathione (GSH) for tolerance (e.g. cadmium, selenate, and hydrogen peroxide excess). Probably helps to detoxify cadmium potentially through direct binding. Binds selenium, cadmium, zinc and nickel in vitro.
Interaction partners:
- Selenium-binding protein 3
- Cystathionine gamma-synthase 1, chloroplastic
- Probable cystathionine gamma-synthase 2
- Selenium-binding protein 2
- Assimilatory sulfite reductase
- Small ribosomal subunit protein uS2y
- Homocysteine S-methyltransferase 3
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 1, mitochondrial
Sequence:
MATETEVVAPVTVSNGGSKGCCKYGGPGYATPLAAMSGPSEKLIYVTAVYTGTGIDKPDYLATVDVDPSSPSYSSVIHRLPMPFVGDELHHSGWNSCSSCHGDASVDRRYLVLPSLISGRIYAIDTKENPRAPSLYKYVDPKEIADKTGLAFPHTAHCLATGEILVSCLGDEEGNAKGNGFLLLDSDFNIKNRWEKPGHSPLYGYDFWYQPRHKTMISTSWGAPKAFSKGFNLQHVADGLYGSHLHVYSWPGGEIKQLIDLGPTGLLPLEIRFLHDPSKDTGFVGSALSSNMIRFFKNSDETWSHEVVISVKPLKVENWILPEMPGLITDFLISLDDRFIYFVNWLHGDIRQYNIEDPKNPVLTGQIWVGGLLQKGSPVKAVGEDGNTFQFEVPQIKGKSLRGGPQMIQLSLDGKRLYATNSLFSAWDRQFYPEIMEKGSHIIQIDVDTEKGGLTINPDFFVDFGDEPDGPSLAHEMRYPGGDCTSDIWI
Protein: Serine/threonine-protein kinase AFC2 (EC 2.7.12.1) (P51567)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Serine/arginine-rich splicing factor RSZ22
- Serine/arginine-rich splicing factor RSZ21
- Serine/arginine-rich SC35-like splicing factor SCL33
- Serine/arginine-rich splicing factor SR45
- THO complex subunit 4A
- Protein SEEDLING LETHAL 1, chloroplastic
- Ribosome biogenesis protein NSA2 homolog
- Vacuolar protein sorting-associated protein 53 B
- FYD
- Sequence-specific DNA binding transcription factor
Sequence:
MEMERVHEFPHTHMDRRPRKRARLGWDVLPQATKAQVGMFCGQEIGNISSFASSGAPSDNSSSLCVKGVARNGSPPWREDDKDGHYIFELGDDLTPRYKIYSKMGEGTFGQVLECWDRERKEMVAVKIVRGVKKYREAAMIEIEMLQQLGKHDKGGNRCVQIRNWFDYRNHICIVFEKLGSSLYDFLRKNNYRSFPIDLVREIGWQLLECVAFMHDLRMIHTDLKPENILLVSSDYVKIPEYKGSRLQRDVCYKRVPKSSAIKVIDFGSTTYERQDQTYIVSTRHYRAPEVILGLGWSYPCDVWSVGCIIVELCTGEALFQTHENLEHLAMMERVLGPFPQQMLKKVDRHSEKYVRRGRLDWPDGATSRDSLKAVLKLPRLQNLIMQHVDHSAGELINMVQGLLRFDPSERITAREALRHPFFARRR
Protein: Inter-alpha-trypsin inhibitor heavy chain H1 (ITI heavy chain H1) (ITI-HC1) (Inter-alpha-inhibitor heavy chain 1) (Q61702)
Organism: Mus musculus (Mouse)
Function: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.
Subcellular location: Secreted.
Interaction partners:
- Mannose-binding protein A
- Fibrinogen alpha chain
- Plasminogen
- Histidine-rich glycoprotein
- Albumin
Sequence:
MEGATGLRVLLCLLPLLTLQARPALGLATGRPRGSEKRHAVDTSVNGVSIKSLKVNCKVTSRFAHYVITSQVVNNADKAREVAFDVEIPKTAFISDFAITSDGKAFIGDIKDKVTAWKQYRKAAVLGESAGLVRASGRNMEQFTIHITVGAQSKATFRLTYEEVLKRRLMQYDITIKVRPKQLVQHFEIDVDIFEPQGISKLDAQASFLSEELAAQTIKKSFSGKKGHVLFRPTVSQQQSCPTCSTSLLNGEFKVTYDVNRDKLCDLLVANNYFTHFFAPKNLTNMSKNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFSLAGATNLNGGLLRGIEILNKAQGSHPELSSPASILIMLTDGEPTEGETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMSTENNGWAQRIYEDHDATQQLQGFYNQVANPLLTDVELQYPQDAVLALTQHRHKQYYDGSEIVVAGRIANHKLNTFKADVRARGEKQEFRATCLVDEEEMKKLLRERGHVLENHVERLWAYLTIQELLAKRMKTEGEERANLSSQVLKMSLDYHFVTPLTSLTIRGLTDEDGLEPTIDKPLEDSQPLEMVGPRRTFVLSAIQPSPTAHPIDSKLPLRVTGVDTDPHFIIYVPSKEDSLCFNINEEPGVILNLVQDPDTGFTVNGQLIGNKASSPGQHESTYFGRLGISSPTSDFQLEVTPQNITLNPSSSGSMFSWRDQAVLQKDGVVVTINKKRNLVVSVDDGATFEIVLHRTWKGSAVHQDFLGFYVLDSFRMSARTKGLLGQFFSPLDFEVFDLHPGSDPTKTDATMVVKNRQLTVTRGLQKDYSKDPRHGAEVPCWFVHDNGAGLIDGVHTDYVVSDIF
Protein: Ubiquitin conjugating enzyme E2 I (I3LSZ1)
Organism: Sus scrofa (Pig)
Interaction partners:
- E3 SUMO-protein ligase RanBP2
- Ran GTPase-activating protein 1
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier 1.
- Small ubiquitin-related modifier 2
- Uncharacterized protein.
- Ubiquitin conjugating enzyme E2 K
- Small ubiquitin-related modifier 1
- SUMO-activating enzyme subunit 1
- Zinc finger protein 451.
Sequence:
GASALLLPSVGQPRYLLYGVSSLGRFGRRPALSPELANCKEFHGLPRARGCHRAATLRGSLGLNDLCSPAPGPSPKETSRTRARGGARGASGGPLEISASWLPRRTPACPRIDAGPAKGSLQTLPHIRDAAPLRAQVSRAPPDWKAAPGAGLPGLARGAGARRRGTGGGRRTATWTARGVRRQRRGAGQARGGQTPQAPPRPARAGVLERSGCARSGLGREVPRQRSAAAAAAAAASSASLAGPRPPEGLEMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYWLVALRPHLVQPRIGRLESLL
Protein: 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (Q9FVP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Shikimate kinase 1, chloroplastic
- Shikimate kinase 2, chloroplastic
- Chorismate synthase, chloroplastic
- 3-dehydroquinate synthase, chloroplastic
- Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic
- Chorismate mutase 2
- Chorismate mutase 3, chloroplastic
- 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic
- Chorismate mutase 1, chloroplastic
- Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic
Sequence:
MASSLTSKSILGCTKPASSSFLPSELRRLSSPAVQISLHSQTRKNFRQSWGLKKSDLMLNGSEIRPVKVRASVSTAEKASEIVLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVETHSENNRAVVEGCGGVFPASIDSKSDIELYLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVNANGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSAEHSESWDRFFVKGGQKYKSPGNAYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPSRDAFGMRHLRAIDVNMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKLGATVEEGSDYCVITPPKKVKPAEIDTYDDHRMAMAFSLAACADVPITINDPGCTRKTFPDYFQVLERITKH
Protein: Kinesin family member 20A (D6RBN1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
Sequence:
MSQGILSPPAGLLSDDDVVVSPMFESTAADLGSVVRKNLLSDCSVVSTSLEDKQQVPSEDSMEKVKVYLRVRPLLPSELERQEDQGCVRIENVETLVLQAPKDSFALKSNERGIGQATHRFTFSQIFGPEVGQASFFNLTVKEMVKDVLKGQNWLIYTYGVTNSGKTHTIQGTIKDGGILPRSLALIFNSLQGQLHPTPDLKPLLSNEVIWLDSKQIRQEEMKKL
Protein: POU domain protein (H0YLL6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MVHSSMGAPEIRMSKPLEAEKQGLDSPSEHTDTERNGPDTNHQNPQNKTSPFSVSPTGPSTKVGILSGLHLTFWGPGPCLSPPQIKAEDPSGDSAPAAPLPPQPAQPHLPQAQLMLTGSQLAGDIQQLLQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQPPKCLEPPSHPEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAETMSVDSSLPSPNQLSSPSLGFDGLPGRRRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINPCSAAPMLPSPGKPASYSPHMVTPQGGAGTLPLSQASSSLSTTVTTLSSAVGTLHPSRTAGGGGGGGGAAPPLNSIPSVTPPPPATTNSTNPSPQGSHSAIGLSGLNPSTGPGLWWNPAPYQP
Protein: Protein CREBRF homolog (Protein Repressed by Tor) (Q9VC61)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional regulator that acts in the TORC1 signaling pathway to regulate energy homeostasis and promote survival during nutrient deprivation. Interacts with REPTOR to form a transcriptional activator complex that functions downstream of TORC1 to up-regulate the expression of most target genes induced by TORC1 inhibition. In the complex, acts as the transcriptional activator. Under normal conditions TORC1 is active, inhibiting the formation of the REPTOR/REPTOR-BP complex by phosphorylating REPTOR and mediates its cytoplasmic retention by forming a docking site for 14-3-3 proteins. Upon TORC1 inhibition resulting from nutrient stress, REPTOR is recruited into the nucleus where it interacts with REPTOR-BP and together they maintain organismal metabolism by activating the expression of target stress response genes including those involved in glycogenesis and triglyceride biosynthesis. The complex also appears to negatively regulate some aspects of TORC1-dependent larval growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:25920570}. Cytoplasm {ECO:0000269|PubMed:25920570}. Chromosome {ECO:0000269|PubMed:25920570}. Note=Translocation from the cytoplasm to the nucleus is promoted by dephosphorylation and inhibited by phosphorylation. Binds to chromatin. {ECO:0000269|PubMed:25920570}.
Interaction partners:
- REPTOR-binding partner
Sequence:
MTENQLYPMSSEFFDTGSNSSSNTLKYDLYSLGSTVVGAALPTLTINTGYGSSSSNNNNTNNNNNNSSSHSSSSNCSTSTTNTCNVMLSTTAITIPRSSNHNQIHHHPYQQSDLQTPRHHPSPLHTLPSMTHQQNQLQQQQQQQHHNQQQQLQQSHLALGELSDFGLDALDAASLSPTLLQDVSLSAVSPLSTTLYNGNTSGAGSSNGIGSGSGGYFTPDMSHSLSLNVVSEQVLLQEATTPNELLYEMTPNSNAMWSDISSAIIHTKHEPFSLDDDYIFPNDKAEIQAADLSDLNGGDFLDVIGNIEDFLPQTAVTQSVNFLLSPQAQGQDALVAPPMELLQQQQQNHQQLQVGSLPQLQTLLTLSQQQQSNSSSTSPYEIYHSTPQKPQQQQLSASFSPGSQASQSPLTPPPPPHANRPQYQMVKSRNMQELIKKGFPMSSPPERSILSQSAALSPGGSSGFGSSASGNSTTTSNQTSGSAVRKSFGYQSAVENSQLSRLSSSAPTHLGLEHIWMRREPRQHLLSTGSLAEAESFSSLSTGSVLSPDGIDFSQDDEDDNSSENSDNYDDCSSDNGLSEDEDETRTSTPNHLSSSKGKERFFWQYNVQAKGPKGKRLVFQSKLEDPHVLNEVTDPVFSPTCSVRGIKVYKHSGKARKGDGNDLTPNARKLHNIGKELDKLSRTINDMTPVSELPFNVRPKSRKEKNKLASRACRLKKKAQHEANKIKLFGLEIEHSEFNVKAVEISYNPSIFVL