wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein (Q38C85)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MALSLSASKRVAYHDLFMDLHGRRPSGRIRLVSEAAPEASAAWATSWSAFASGGAQDAGMGRSKKRKLAGEHVAVAFNRTKGQASTELFFHVAVFRCDTWALQWVARASSADPAARVLDVCCLSANIVAFLVECKDESETRAELCIATRFSIPSSENLSNVRWRSFISEARVVDTGFTAEGIRSIQALSATSLLVLTGSGRLVRATVSRMETMETTCEQVASLSVMIRRTRGTHTTPALVVSRNCCGKGGAETKTKDRTYAAVLNDNGSKCYVLDLMAPCASRKLQHITFPKDTIAERVEFAGSYMLVVTLRLKESSLYVLQFTCLVPQDSPSEGSFTMTSFDLIHLTARRTPLATMYDSEKETHIVVSQWQDTAEDSSTSEVVETEQWWRRMEFAEVSLASGPYTTDVLRGATWLPLPEPFRSDVPALRTVVGSGVDGDDGEAAEVEYHQELSLLNKERVTGSWLPLYLHYALATPLSRMGDGVREVKTVLVTVFAIETAPFVHTRLAKQWHNAVQGLLFLLGVGWNVGEHRGKMKQIADGVPAFAVPWNPGHMRRALRLFGQRALRRLFSSVACALRHSAEPSAAQQLFYGVATTSLTDVAMQIITLSRRVGAHLRAEDVETVVLLLRASRDLGHAIVNHTTRSQVLLECIVKGRMAGRVLGGFDGRTKGDAGRGAEGDDEKNDEVKERRQESVGFLSGASEMRVERMLHNRYTTNDWSQQLLLKRSQHADVVAQARLYLNDVLPFVQHKQEQPICEEQKQQRQHQGREEEDEEVSEEEHNQKGRKTAMNDALLPDWVFMGRRPHADAGFTEYEGILLRPGGASN
Protein: Uncharacterized motility-related protein HVO_2248 (D4GVW4)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: May be involved in swimming motility.
Interaction partners:
Sequence:
MSEQRVTFNGDTRVLYRQAVRTPLPNEDAERLFHENMMNIADAQERKADMLADPDISLLEAYETQLEGIAKSYKRRCRHIAGDDYEEIAMAYNRGARDDRVGALTAYYFEGLWRMQQRITVTDMLFFPIILRYPDCFTVNIRFASGHTTTESVLYESPEHSTEELDDEYAERYYNESLYSQKEAAEYIRDTAEIIREEFPSPDESTFEERQYGGITSAGGRKGPVFSSMLKRVEPDPNRFSEPVDQPTLVEEGKEARRTERELLPEGAIVL
Protein: Protein kinase domain-containing protein ppk38 (Q9UU85)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MNETNNTSLLPVSSLPSGLLPVGFSCTVEKFSVTVKRYLAEGGFSHVYLVQLVFPGKPPFEAVLKRIFATDAMALRAVHEEVRTMKLVSNQKRCVSYYGSEFFRTSKNQFEVLVLLEYCPCGGLIDFLNTRLQVRLSEQEILKIASDVTEAVAVMHYLKPPLIHRDLKIENVLLAAPNSYKLCDFGSACHPIPGAKTAAEAKQLEYDIEKFTTWQYRCPEMINVHKGFGIDEKSDIWALGVLFYKLCYYTTPFEHQGLAAIMNVSYAFPTFPPYSDRLKRLISTLLQQYPWQRPNIYQTFCEICKMRNVPIHIYDIYNGKNVSSCNPSGSEYLQHASKLENSGIHQSKSSVFPQPASAMKPMASPMLPNVNSMPYLSNGDHNNNGNTSSPVSRFSYGQHTSNVPSTQKLPSNFRVTQGAPPSHTYGPPPPVQPKPKISPTTPRLSTLALADDMFSSTAKETVPTNEAVFTGDVKSFDSQESNIIESEPLSASNASGKPRTSVNRLVDRYNHTSSLNKVAAAPAPVPKPVNLKSVENPQNNISAPTPSSLQSSNAPVGLGEVESKSVPPTNMATERGVVGRRASMSIAVNARRVSKPEKEHTNPNAEQGDVIPEKPMSIKERMNMLMTKTDYEKPKVEGYGRYTDVQQTKK
Protein: Keratin-associated protein 9-2 (Keratin-associated protein 9.2) (Ultrahigh sulfur keratin-associated protein 9.2) (Q9BYQ4)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
Sequence:
MTHCCSPCCQPTCCRTTCCRTTCWKPTTVTTCSSTPCCQPACCVSSCCQPCCRPTCCQNTCCRTTCCQPTCVTSCCQPSCCSTPCCQPTCCGSSCCGQTSCGSSCGQSSSCAPVYCRRTCYYPTTVCLPGCLNQSCGSNCCQPCCRPACCETTCCRTTCFQPTCVSSCCQPSCC
Protein: Zinc finger transcription factor YRR1 (Pleiotropic drug-resistance protein 2) (Q12172)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor involved in the regulation of multidrug resistance genes. Acts in concert with YRR1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcription factor PDR3
- Transcription factor PDR1
- Protein SNQ2
- Fluconazole resistance protein 1
- Oligomycin resistance ATP-dependent permease YOR1
- Nitrosoguanidine resistance protein SNG1
- Protein STB5
- Pleiotropic ABC efflux transporter of multiple drugs
- AP-1-like transcription factor YAP1
- Uncharacterized protein YLL056C
Sequence:
MKRRSDALLGSFQATNVTPPSDNSNSTAGGANGSNSGTPTSTSGKKRNKLIKSCGFCRRRKLRCDQQKPMCSTCISRNLTTCQYAEEFNKNIEKKATYGPYPNADLLKKVEELENKIRILEAEKNTNSSASSMYTSPNFPPLGTSVGRGSTETSSPLPDGVINPYADRYYLQSKHSGRSTLYGPTSMRTQIANSNWGFIEKYKQLWAKVKVERNKWKQNNQKTMCRELGLLDESDWQPDPLIKQICRFLPSYNKALSILDDFFNDGACNEINVILDKAKVRRDFLDYFMPEKEVKAEGDRSIVYILSNPKKNYYKAAVILLILCLKYFHTDVPTPIEKFFTLLKGASTAKVFYIERAQMLILFYYHRETYSFGGDGSDLVNINECLVTTVTTIGLHLNIRETFKEHEVFMGSIESLENVWLMAIFIDYNISCNVGRPLLINKFYLDENQDHCILNSKSKTYEGKLKRYLKLTRPMLLTLYDRDKFPDLKAYSKRIINFVEEELGPLGHYTGENISEEVPLRESRILSMAVGLLLSFYALIHSVLKVRNIESKNNTFQLVLINFSIIVNTTIRCYRIDKALYPEKFEASNPHLPPHMALSMSLTAGLFSKTLVFFCSLIYFKLTLFENGLCLSNDMEVGWSDLTKLTVPLDKDLSLGTAMSLYSSIFDRLFTVGNKELIRTMHRSSQFVIELAIERTYRTILGNVIEFRKLTEETWLAQIKQELDPQSDNPSSEAKIVSDRQRDLSLAVPTPTPSIIPMLPSPGETKNHAKSQSEIIQMLTDEFWANYNSGWEELINQSEFSTLFDDYKDN
Protein: Sesquipedalian-2 (Ses2) (27 kDa inositol polyphosphate phosphatase interacting protein B) (IPIP27B) (PH domain-containing endocytic trafficking adaptor 2) (Q6ICB4)
Organism: Homo sapiens (Human)
Function: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane.
Subcellular location: Early endosome {ECO:0000269|PubMed:21233288}. Recycling endosome {ECO:0000269|PubMed:21233288}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21233288}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:21233288}. Note=Also found on macropinosomes. Not detected in late endosomes, nor in lysosomes. {ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:21233288}.
Interaction partners:
- Inositol polyphosphate 5-phosphatase OCRL
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- Pleckstrin homology domain-containing family J member 1
- Sesquipedalian-1
Sequence:
MKLNERSVAHYALSDSPADHMGFLRTWGGPGTPPTPSGTGRRCWFVLKGNLLFSFESREGRAPLSLVVLEGCTVELAEAPVPEEFAFAICFDAPGVRPHLLAAEGPAAQEAWVKVLSRASFGYMRLVVRELESQLQDARQSLALQRRSSWKSVASRCKPQAPNHRAAGLENGHCLSKDSSPVGLVEEAGSRSAGWGLAEWELQGPASLLLGKGQSPVSPETSCFSTLHDWYGQEIVELRQCWQKRAQGSHSKCEEQDRP
Protein: Histone acetyltransferase type B catalytic subunit (EC 2.3.1.48) (Histone acetyltransferase 1) (O14929)
Organism: Homo sapiens (Human)
Function: Histone acetyltransferase that plays a role in different biological processes including cell cycle progression, glucose metabolism, histone production or DNA damage repair. Coordinates histone production and acetylation via H4 promoter binding. Acetylates histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, histone H2A at 'Lys-5' (H2AK5ac). Drives H4 production by chromatin binding to support chromatin replication and acetylation. Since transcription of H4 genes is tightly coupled to S-phase, plays an important role in S-phase entry and progression. Promotes homologous recombination in DNA repair by facilitating histone turnover and incorporation of acetylated H3.3 at sites of double-strand breaks. In addition, acetylates other substrates such as chromatin-related proteins. Acetylates also RSAD2 which mediates the interaction of ubiquitin ligase UBE4A with RSAD2 leading to RSAD2 ubiquitination and subsequent degradation.
Subcellular location: [Isoform A]: Nucleus matrix {ECO:0000269|PubMed:20148353, ECO:0000269|PubMed:23653357}. Mitochondrion {ECO:0000269|PubMed:32081014}.; SUBCELLULAR LOCATION: [Isoform B]: Cytoplasm {ECO:0000269|PubMed:20148353}. Nucleus {ECO:0000269|PubMed:20148353}. Nucleus matrix {ECO:0000269|PubMed:20148353}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20148353}. Note=Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redistribution of existing protein. {ECO:0000269|PubMed:20148353}.
Interaction partners:
- Histone-binding protein RBBP7
- Histone H4
- Nuclear autoantigenic sperm protein
- Histone H3.1
- Histone H4-like protein type G
- Histone-binding protein RBBP4
- Histone H3.3
- Histone H3.1t
- Origin recognition complex subunit 3
- Origin recognition complex subunit 5
Sequence:
MAGFGAMEKFLVEYKSAVEKKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGFCTNTNDFLSLLEKEVDFKPFGTLLHTYSVLSPTGGENFTFQIYKADMTCRGFREYHERLQTFLMWFIETASFIDVDDERWHYFLVFEKYNKDGATLFATVGYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLETVHRYYTEFPTVLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMVIEAQQKFKINKQHARRVYEILRLLVTDMSDAEQYRSYRLDIKRRLISPYKKKQRDLAKMRKCLRPEELTNQMNQIEISMQHEQLEESFQELVEDYRRVIERLAQE
Protein: Vacuolar protein sorting-associated protein 29 (Vesicle protein sorting 29) (A0A384MR19)
Organism: Homo sapiens (Human)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}.
Interaction partners:
Sequence:
MAGHRLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYKKP
Protein: AT-rich interaction domain 2 (F8W108)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XDRFLKMRGMEILGNLCKAEDNGVLICEYVDQDSYREIICHLTLPDVLLVISTLEVLYMLTEMGDVACTKIAKVEKSIAAVKLIEHPSSSHQMLSEIRPQAIEQVQTQTHVASAPASRAVVAQHVAPPPGIVEIDSEKFACQWLNAHFEVNPDCSVSRAEMYSEYLSTCSKLARGGILTSTGFYKCLRTVFPNHTVKRVEDSSSNGQAHIHVVGVKRRAIPLPIQMYYQQQPVSTSVVRVDSVPDVSPAPSPAGIPHGSQTIGNHFQRTPVANQSSNLTATQMSFPVQGVHTVAQTVSRIPQNPSPHTHQQQNAPVTVIQSKAPIPCEVVKATVIQNSIPQTGVPVSIAVGGGPPQSSVVQNHSTGPQPVTVVNSQTLLHHPSVIPQQSPLHTVVPGQIPSGTPVTVIQQAVPQSHMFGRVQNIPACTSTVSQGQQLITTSPQPVQTSSQQTSAGSQSQDTVIIAPPQYVTTSASNIVSATSVQNFQVATGQMVTIAGVPSPQASRVGFQNIAPKPLPSQQVSSTVVQQPIQQPQQPTQQSVVIVSQPAQQGQTYAPAIHQIVLANPAALPAGQTVQLTGQPNITPSSSPSPVPATNNQVPTAMSSSSTPQSQGPPPTVSQMLSVKRQQQQQHSPAPPPQQVQVQVQQPQQVQMQVQPQQSNAGVGQPASGESSLIKQLLLPKRGPSTPGGKLILPAPQIPPPNNARAPSPQVVYQVASNQAAGFGVQGQTPAQQLLVGQQNVQLVPSAMPPSGGVQTVPISNLQILPGPLISNSPATIFQGTSGNQVTITVVPNTSFAPATVSQGNATQLIAPAGITMSGTQTGVGLPVQTLPATQASPAGQSSCTTATPPFKGDKIICQKEEEAKEATGLHVHERKIEVMENPSCRRGATNTSNGDTKENEMHVGSLLNGRKYSDSSLPPSNSGKIQSETNQCSLISNGPSLELGENGASGKQNSEQIDMQDIKSDLRKPLVNGICDFDKGDGSHLSKNIPNHKTSNHVGNGEISPMEPQGTLDITQQDTAKGDQLERISNGPVLTLGGSSVSSIQEASNAATQQFSGTDLLNGPLASSLNSDVPQQRPSVVVSPHSTTSVIQGHQIIAVPDSGSKVSHSPALSSDVRSTNGTAECKTVKRPAEDTDRETVAGIPNKVGVRIVTISDPNNAGCSATMVAVPAGADPSTVAKVAIESAVQQKQQHPPTYVQNVVPQNTPMPPSPAVQVQGQPNSSQPSPFSGSSQPGDPMRKPGQNFMCLWQSCKKWFQTPSQVFYHAATEHGGKDVYPGQCLWEGCEPFQRQRFSFITHLQDKHCSKDALLAGLKQDEPGQAGSQKSSTKQPTVGGTSSTPRAQKAIVNHPSAALMALRRGSRNLVFRDFTDEKEGPITKHIRLTAALILKNIGKYSECGRRLLKRHENNLSVLAISNMEASSTLAKCLYELNFTVQSKEQEKDSEMLQ
Protein: Keratin-associated protein 4-11 (Keratin-associated protein 4-14) (Keratin-associated protein 4.11) (Keratin-associated protein 4.14) (Ultrahigh sulfur keratin-associated protein 4.14) (Q9BYQ6)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
Sequence:
MVNSCCGSVCSHQGCGRDLCQETCCRPSCCETTCCRTTYCRPSCCVSSCCRPQCCQSVCCQPTCCRPRCCISSCCRPSCCVSSCCKPQCCQSMCCQPTCCRPRCCISSCCRPSCCVSSCCRPQCCQSVCCQPTCCHPSCSISSCCRPSCCESSCCRPCCCLRPVCGRVSCHTTCYRPTCVISSCPRPLCCASSCC
Protein: Heat shock transcription factor 1 (A0A8I6ADR2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDLAVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTRLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLSDSSSAHSVPKYGRQYSLEHVHGPGPYSAPSPAYSSSSLYSSDAVTSSGPIISDITELAPTSPLASPGRSIDERPLSSSTLVRVKEEPPSPPHSPRVLEASPGRPASMDTPLSPTAFIDSILRESEPTPAASNTAPMDTTGAQAPAPPAPSTPEKCLSVACLDNLARAPQMSGVARLFPCPSSFLHGRVQPGLALPPLGREEDSARPPPTAMDQFPTRA
Protein: RNA polymerase III subunit D (E5RHT4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTPNIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKKGNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQLPLAHSGWLFKEENDEPDVKPWLAGPKE
Protein: Gallinacin-1 alpha (Gal-1 alpha) (Antimicrobial peptide CHP2) (Chicken heterophil peptide 2) (P46157)
Organism: Gallus gallus (Chicken)
Function: Has bactericidal activity. Potent activity against E.coli ML-35, L.monocytogenes EGD and C.albicans.
Subcellular location: Secreted. Cytoplasmic granule.
Interaction partners:
Sequence:
MRIVYLLLPFILLLAQGAAGSSQALGRKSDCFRKNGFCAFLKCPYLTLISGKCSRFHLCCKRIWG
Protein: Ribosome maturation protein SBDS (Shwachman-Bodian-Diamond syndrome protein) (Q9Y3A5)
Organism: Homo sapiens (Human)
Function: Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation.
Subcellular location: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Note=Primarily detected in the cytoplasm, and at low levels in nucleus and nucleolus (PubMed:17475909, PubMed:19602484). Detected in the nucleolus during G1 and G2 phase of the cell cycle, and diffusely distributed in the nucleus during S phase. Detected at the mitotic spindle. Colocalizes with the microtubule organizing center during interphase (PubMed:19759903). {ECO:0000269|PubMed:19759903}.
Interaction partners:
- Elongation factor-like GTPase 1
- Ubiquitin-ribosomal protein eL40 fusion protein
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein eS19
- Eukaryotic translation initiation factor 6
- Large ribosomal subunit protein uL18
- mRNA turnover protein 4 homolog
- Protein-tyrosine sulfotransferase 1
Sequence:
MSIFTPTNQIRLTNVAVVRMKRAGKRFEIACYKNKVVGWRSGVEKDLDEVLQTHSVFVNVSKGQVAKKEDLISAFGTDDQTEICKQILTKGEVQVSDKERHTQLEQMFRDIATIVADKCVNPETKRPYTVILIERAMKDIHYSVKTNKSTKQQALEVIKQLKEKMKIERAHMRLRFILPVNEGKKLKEKLKPLIKVIESEDYGQQLEIVCLIDPGCFREIDELIKKETKGKGSLEVLNLKDVEEGDEKFE
Protein: Spore coat protein SP70 (Protein Beejin) (P15269)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Spore coat protein SP60
- Extracellular matrix protein A
- Spore coat protein SP85
- Prestalk protein
- Spore coat protein SP96
- Prespore-specific protein A
Sequence:
MRILKLAALSCLLFIAPSLSINCDGLSKDQCEQNFPQCQILTAKSCCGESKSYCAERDSNDCLASKISCKKDPQGNIYEFWSSCTPSSGFTDFIPSNATCSSLNCNAQQMSCKYVQQACHETSCCPDIPQCQIPATGGGPATGSATGQGTSGGTPGSCDKVNCPNGYICTIVNQLAVCVSPSSSSSSSSSTTGSHTTTGGSTTGSHTTTGGSTTGSHTTTGGSTTGSHTTTGGSTTGSHTTTGGSTTGPTCGNVNCPRGYHCEVRGSQAVCVADEFDSCANVDCGSGYHCKNGECIRDKVECDACDQINCPKGHHCISQPKGGWIGSHKKRHWQLHPEHCGGRPNKIKVICVPSPKGTCKTVQCPKGYKCKLYADGPTCVKIEKPKCLTCKDMHCESNGLLCVLTPQKKTDEECCPIIPICINPSTIAASTIATTTASTRHSTASTIASLVTGTTSGGGGMGSFGGRSDEESSDPNAILGLFEDDIFWGDNDEYFSDNYRYVDEEDIDEDFNGNDEFEIDVEGDFQEDDFEEEYAFY
Protein: HSP20-like chaperones superfamily protein (Q8VXX3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g50410
- Universal stress protein PHOS34
- AT3g53990
- Chaperonin CPN60-like 1, mitochondrial
- Protein DA1
- Endoplasmin homolog
- CLIP-associated protein
Sequence:
MAEKLAPEKRHDFIHNGQKVFEWDQTLEEVNMYITLPPNVHPKSFHCKIQSKHIEVGIKGNPPYLNHDLSAPVKTDCSFWTLEDDIMHITLQKREKGQTWASPILGQGQLDPYATDLEQKRLMLQRFQEENPGFDFSQAQFSGNCPDPRSFMGGIRSD
Protein: Pertussis toxin-like subunit ArtA (Pertussis-like toxin subunit (EC 2.4.2.-)) (Typhoid-like toxin S-CDT ADP-ribosylating subunit PltA) (Q8Z6A4)
Organism: Salmonella typhi
Interaction partners:
- Pertussis-like toxin subunit
- Cytolethal distending toxin subunit B homolog
- Hypothetical periplasmic protein
- Iron-sulfur cluster assembly scaffold protein IscU
Sequence:
MKKLIFLTLSIVSFNNYAVDFVYRVDSTPPDVIFRDGFSLLGYNRNFQQFISGRSCSGGSSDSRYIATTSSVNQTYAIARAYYSRSTFKGNLYRYQIRADNNFYSLLPSITYLETQGGHFNAYEKTMMRLQREYVSTLSILPENIQKAVALVYDSATGLVKDGVSTMNASYLGLSTTSNPGVIPFLPEPQTYTQQRIDAFGPLISSCFSIGSVCHSHRGQRADVYNMSFYDARPVIELILSK
Protein: Cytoplasmic aconitate hydratase (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Iron regulatory protein 1) (IRP1) (Iron-responsive element-binding protein 1) (IRE-BP 1) (Q63270)
Organism: Rattus norvegicus (Rat)
Function: Bifunctional iron sensor that switches between 2 activities depending on iron availability (By similarity). Iron deprivation, promotes its mRNA binding activity through which it regulates the expression of genes involved in iron uptake, sequestration and utilization. Binds to iron-responsive elements (IRES) in the untranslated region of target mRNAs preventing for instance the translation of ferritin and aminolevulinic acid synthase and stabilizing the transferrin receptor mRNA.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16144863}.
Interaction partners:
- Citrate synthase, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Isocitrate dehydrogenase, mitochondrial
- ATP-citrate synthase
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- Probable isocitrate dehydrogenase gamma 2, mitochondrial
- Aconitate hydratase, mitochondrial
- Fumarate hydratase, mitochondrial
Sequence:
MKNPFAHLAEPLDPAQPGKKFFNLNKLEDSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWSIMQHKSIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVHFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFCNMRIIPPGSGIIHQVNLEYLARVVFDQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDDVSIAYLVQTGREEDKVKHIKRYLQAVGMFRDFSDSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEIEKDFESCLGAKQGFKGFQVAPDHHNDHKTFIYNDSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLNVKPYVKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTVRIDFEKEPLGVNAQGQQVFLKDIWPTRDEIQEVERKYVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPRDFNSYGSRRGNDAIMARGTFANIRLLNKFLNKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERTHCSNLVGMGVIPLEYLPGETADSLGLTGRERYTIHIPEHLKPRMKVQIKLDTGKTFQAVMRFDTDVELTYFHNGGILNYMIRKMAQ
Protein: Ephrin-A5 (AL-1) (EPH-related receptor tyrosine kinase ligand 7) (LERK-7) (P52803)
Organism: Homo sapiens (Human)
Function: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11870224}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11870224}. Membrane, caveola {ECO:0000269|PubMed:11870224}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11870224}. Note=Compartmentalized in discrete caveolae-like membrane microdomains.
Interaction partners:
- Ephrin type-A receptor 4
- Ephrin type-A receptor 3
- Ephrin type-A receptor 5
- Ephrin type-A receptor 2
- Ephrin type-B receptor 2
- Ephrin type-A receptor 7
- Ephrin type-A receptor 1
- Ephrin type-A receptor 8
- Regulatory-associated protein of mTOR
- BDNF/NT-3 growth factors receptor
Sequence:
MLHVEMLTLVFLVLWMCVFSQDPGSKAVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGENAAQTPRIPSRLLAILLFLLAMLLTL
Protein: Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1 (Protein ABNORMAL INFLORESCENCE MERISTEM 1) (AtAIM1) [Includes: Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] (Q9ZPI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in peroxisomal fatty acid beta-oxidation. Required for wound-induced jasmonate biosynthesis. Possesses enoyl-CoA hydratase activity against short chain substrates (C4-C6) and 3-hydroxyacyl-CoA dehydrogenase activity against chains of variable sizes (C6-C16). Possesses cinnamoyl-CoA hydratase activity and is involved in the peroxisomal beta-oxidation pathway for the biosynthesis of benzoic acid (BA). Required for the accumulation in seeds of benzoylated glucosinolates (BGs) and substituted hydroxybenzoylated choline esters, which are BA-containing secondary metabolites. Required for salicylic acid (SA) in seeds.
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- Peroxisomal acyl-coenzyme A oxidase 1
- 3-ketoacyl-CoA thiolase 5, peroxisomal
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Acyl-coenzyme A oxidase 3, peroxisomal
- Acyl-coenzyme A oxidase 4, peroxisomal
- Acyl-coenzyme A oxidase 2, peroxisomal
- Probable enoyl-CoA hydratase 1, peroxisomal
- Probable acyl-CoA dehydrogenase IBR3
Sequence:
MAKKIGVTMEVGNDGVAVITISNPPVNSLASPIISGLKEKFRDANQRNDVKAIVLIGNNGRFSGGFDINVFQQVHKTGDLSLMPEVSVELVCNLMEDSRKPVVAAVEGLALGGGLELAMACHARVAAPKAQLGLPELTLGVIPGFGGTQRLPRLVGLAKATDMILLSKSISSEEGHKLGLIDALVPPGDVLSTSRKWALDIAEGRKPFLQSLHRTDKIGSLSEARAILKNSRQLAKKIAPNMPQHHACIEVIEEGIIHGGYSGVLKEAEVFKQLVLSDTAKGLVHVFFAQRATSKVPNVTDVGLKPRPIKKVAVIGGGLMGSGIATALLLSNIRVVLKEINSEFLMKGIKSVEANMKSLVSRGKLTQDKAGKALSLFKGVLDYTEFNDVDMVIEAVIENIQLKQNIFKEIEKVCSPHCILASNTSTIDLDVIGEKTNSKDRIVGAHFFSPAHLMPLLEIVRSKNTSAQVILDLMAVGKAIKKVPVVVGNCIGFAVNRTFFPYSQAAHMLANLGVDLFRIDSVITSFGLPLGPFQLGDLAGHGIGLAVGPIYAKVYGDRMFRSPMTELLLKSGRNGKINGRGYYIYEKGSKPKPDPSVLSIVEKSRKLTNIMPGGKPISVTDKEIVEMILFPVVNEACRVLDEGVVIRASDLDIASVLGMSFPSYRGGIVFWADTVGPKYIYERLKKLSETYGSFFKPSRYLEERAMNGMLLSESKSSRSKL
Protein: Ig-like domain-containing protein (A0A060ZZG4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Interleukin 1 receptor accessory protein
- Interleukin-1
- Interleukin-1
- Death domain-containing protein
- Interleukin-1
- Interleukin-1
- Interleukin-18
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MCSFTFRLVDGGLMFLLLSLTRISAQREMSLNTTTISHYTESPCQLFDKYETTVTEGEALSLPAYRDLSELVWASVTEFTWYRNRTQELPSSEEERVHHHGPVLFFLPLLINDSDQYYTYWRKGADTCLIFVTEVIVVKAQPFDHSVLFNDISESAENIAIPCPDPVEKLCQDGKENLVWYKNFSLIPNESERNLWVYGASKADEGIYTCVCTWEHNGTVLNTSASRRLKIQGM
Protein: Thymosin beta-10 (P63313)
Organism: Homo sapiens (Human)
Function: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity).
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Protein S100-A6
- Transmembrane glycoprotein NMB
- BMP and activin membrane-bound inhibitor homolog
- Melanocyte protein PMEL
Sequence:
MADKPDMGEIASFDKAKLKKTETQEKNTLPTKETIEQEKRSEIS