wanglab/gogpt-training-data huggingface dataset:
Protein: RNA helicase (EC 3.6.4.13) (X1WET4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mitochondrial antiviral-signaling protein
- WD repeat domain 36
- Cell division cycle 40 homolog
- Pre-mRNA-splicing factor SYF1
- Crooked neck-like protein 1
- Pre-mRNA-splicing factor SLU7
- Cell division cycle 5-like protein
- ATP-dependent RNA helicase
- Si:dkey-251i10.3
- Elongation factor Tu GTP-binding domain-containing 2.
Sequence:
MPHEPDPPPAKRFKPGSPFFRLDKKPGMLLPRAGHAAAGVEAQRRHLPIYQSRTQVISQLRQLHSAVFIGETGSGKTTQIPQYLYEAGIGRQGIIAITQPRRVAAISLAGRVAEEKKVQLGKLVGYTVRFEDVTSPETKLKFMTDGMLLREAIGDPLLLRYTVVILDEAHERTVHTDVLFGVVKAAQRRRLEQNKIPLKVVVMSATMDVDLFSQYFNKSPVLYLEGRQHPIQIYYTKQPQSDYLQAALVSIFQIHQEAPSSHDILVFLTGQEEIEALARTCRDISKHLPDTSGSMTVVPLYASLPPAQQMRVFLPAPKGSRKVILSTNIAETSITISGIKYVIDTGMVKAKRFNPDSGLEVLAVQRVSKAQAWQRAGRAGREDAGSCYRLYTEDEFENLANMTVPEIQRCNLASVVLQLLALGVPDVLNFDFVSKPSPESMRTAVEQLCILGAVDRKDDHVSLTPLGKKMACFPLEPRFSKTLLISPDFSCTEEILTIISLLSVDSVLYNPPARRDEVISVRKKFISSEGDHITLLNIYRAFKKVSGNKDWCRENFVNSRNMGLVGEVRAQLRDICIKMNLKLESSVCDLANVRRCLAHGLFMSAAELQPDGSYVALDTHQPVSIHPSSVLFQARPVCVLFNELLHTSRCYMRDLCLIQTDWLHEAAPEYFRRKLRAIKS
Protein: Cartilage oligomeric matrix protein (COMP) (Q9R0G6)
Organism: Mus musculus (Mouse)
Function: Plays a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP) (By similarity). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:32686688}.
Interaction partners:
- Aggrecan core protein
- Fibronectin
- Integrin beta-3
- Leukocyte surface antigen CD47
- A disintegrin and metalloproteinase with thrombospondin motifs 7
- Platelet glycoprotein 4
- Integrin beta-1
- Syndecan-4
- Integrin alpha-3
- Integrin alpha-V
Sequence:
MGPTACVLVLALAILRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRQQVKEITFLKNTVMECDACGMQPARTPGLSVRPVPLCAPGSCFPGVVCSETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKSNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQTSGCQRRGQHFCPDGSPSPCHEKANCVLERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDSDKWGDACDNCRSKKNDDQKDTDLDGRGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYESHRLQRV
Protein: Protein mab-21-like 3 (Q8N8X9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKYLTVGDLEDCLLNKVDLRRQQISQAVEEVQKVVHHLTTNISNQDIRFQAVPYSDTYNENIKVLAPSQFLVTVPIKGLAGYREAREQHWRYYTLQGTRLPCPLRDPEGLQQWLEVEQFMKSLWQWHETDVNIDGDIVPAKVLLVFRKLVENAVRTCHLSGKVSLLGNRSAVWVAVETSAYQVELELVPAVEIPTTWSKKARWPRCLQRWPSQERVECIKSFGFNLLACSNYHWQLSFLRAEQVLLEQLDEDGGCRRKCFQVMRHLKEDIWCPGNRPVITSHHLQTVLFWTCEKYPHFKDWQVFSKAFLRLVRKLHKCVSQHFLKHYFVRNSNLFQCTNPTELDTVAQKLATFLKNPQIGPP
Protein: Ran GTPase-binding protein (A0A1D8PRQ3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Nucleoporin NSP1
- GTP-binding nuclear protein
- GTPase-activating protein
- Exportin
- Peptidyl-prolyl cis-trans isomerase
- Peptidyl-prolyl cis-trans isomerase
- Nuclear pore protein
- Peptidyl-prolyl cis-trans isomerase
- Ran guanyl-nucleotide exchange factor
- Peptidyl-prolyl cis-trans isomerase
Sequence:
MSAEDTKPKTEESTSIPKPPTSNVFSMFGAKKEKKPEQEDSDNKKESDKKEEKDTSKSTGDDNEVAEEEEADVEFTPVVQLDKKVDVKTNEEDEEVLYKVRAKLFRFHGDSKEWKERGTGDVKFLKHKTTGKVRILMRRDKTLKICANHLISADYELKPNIGSDRSWVYTVTADVSEGEPEAQTLAIRFGNKENADLFKEHFDNAKKEAKKD
Protein: Testis-specific gene 10 protein (Q6NY15)
Organism: Mus musculus (Mouse)
Function: Plays a role in spermatogenesis. When overexpressed, prevents nuclear localization of HIF1A.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Z220}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9BZW7}. Note=In mature spermatozoa, localizes to the centriole and midpiece (By similarity). The 27-kDa peptide associates with the fibrous sheath in mature spermatozoa and localizes to the principal piece of sperm tail, while the 55-kDa peptide localizes to the midpiece (PubMed:16643851, PubMed:16777103). Detected in the cytoplasm of almost all spermatogonial cells within the seminiferous tubules (By similarity). {ECO:0000250|UniProtKB:Q9BZW7, ECO:0000250|UniProtKB:Q9Z220, ECO:0000269|PubMed:16643851, ECO:0000269|PubMed:16777103}.
Interaction partners:
- Intersectin-2
- Polyamine-modulated factor 1-binding protein 1
- Intersectin-1
Sequence:
MMRNRSKSPRRPSPTSRAANCDVELLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMMKSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNAYNLGPMKPNTKCHSPERAHHRSPDRGLDRSLEENLCYRDF
Protein: Clathrin interactor EPSIN 1 (EPSIN-related 1) (Q8VY07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity). Does not seem to bind to phospholipids. Plays an important role in the vacuolar trafficking of soluble cargo proteins at the trans-Golgi network.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16905657}. Prevacuolar compartment {ECO:0000269|PubMed:16905657}. Cytoplasm {ECO:0000269|PubMed:16905657}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16905657}. Note=Associated with actin filaments.
Interaction partners:
- Clathrin heavy chain 1
- Clathrin heavy chain 2
- AP-2 complex subunit alpha-1
- Clathrin coat assembly protein AP180
- AP-1 complex subunit gamma-1
- Protein MODIFIED TRANSPORT TO THE VACUOLE 1
- Vesicle transport v-SNARE 11
- Vacuolar-sorting receptor 1
- Putative clathrin assembly protein At2g25430
- Calcium-binding EF hand family protein
Sequence:
MDFMKVFDQTVREIKREVNLKVLKVPEMEQKVLDATDNEPWGPHGTALAEIAQATKKFSECQMVMSVLWTRLSETGKDWRYVYKALAVIDYLISNGSERAVDEIIEHTYQISSLTSFEYVEPNGKDVGINVRKKAENIVALLNNKEKISEIRDKAVANRNKYVGLSSTGITYKSGSSASFGGSFQSGSSNFDSYKDRDSREDKNDYESFQKSRRGVKTEEQSYTSKKSFSRYGSTDHDNLSSGKKSPDSAKHRSYVSAAPSNNDDDFDDFDPRGTSSNKPSTGSANQVDLFGGDLIGDFLDSGPTETSSTNNNENFQEADLFADAAFVSASAQGAEFGSQTQKQVDLFSASEPSVTVSSAPPTVDLFASSESVVSPEAKISIPESMATPNIVDPFAAVPMDNFDGSDPFGAFTSHSASVSTGPQAPSVHGSATNTTSPLSFADSKPQHLQKKDPFQVKSGIWADSLSRGLIDLNITAPKKASLADVGVVGDLSNEDGNKASAASYYSGWSMGAGSGLGKTGLYSTQQQQQQQQQQQAPDISDDFFSSLSNQRYQSGGFKQ
Protein: Uncharacterized protein (Q38BB5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSGMQAPFQGGVSNIFSTPTAPFSARQLFHIAGRPAESTVSGGGSFTQEDRLMLQLLYQQQQAFQIQLQSMALSLQQLYMAISALPHLNASTTKHDSEDASQSAPVHTALSASVGAPLTAVDAPVTSSSVRGRAGEHREDAVVTERQPSTAQHQGEVSRSCTPPPGDSDVSRQSMMNRSSESAAPWDPSAGSRHSSATRGVRGENPLLSSLRGKLPTPNRSAITSTSVATGHSASMNVSVNQDDPKPTARPTARSSTSSASRLDYGARHVTSSLFSSAPSEEKHHHQRARKRIVPSSRKVDASHVTRREEEFIPPHTGTSGSGPVVGSSVTGGVSCGEELQSVKGWNSSRGWNQPDKDEFGETSASVTGYDSQSDGYGSYETRQYLKTVGLI
Protein: Serum response factor (SRF) (P11831)
Organism: Homo sapiens (Human)
Function: SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration. The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. Required for cardiac differentiation and maturation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:19350017}.
Interaction partners:
- Myocardin-related transcription factor A
- Myocardin
- ETS domain-containing protein Elk-4
- Transcription factor GATA-4
- Forkhead box protein G1
- ETS domain-containing protein Elk-1
- Homeobox protein Nkx-2.5
- Myocardin-related transcription factor B
- Protein c-Fos
- Nuclear factor of activated T-cells, cytoplasmic 3
Sequence:
MLPTQAGAAAALGRGSALGGSLNRTPTGRPGGGGGTRGANGGRVPGNGAGLGPGRLEREAAAAAATTPAPTAGALYSGSEGDSESGEEEELGAERRGLKRSLSEMEIGMVVGGPEASAAATGGYGPVSGAVSGAKPGKKTRGRVKIKMEFIDNKLRRYTTFSKRKTGIMKKAYELSTLTGTQVLLLVASETGHVYTFATRKLQPMITSETGKALIQTCLNSPDSPPRSDPTTDQRMSATGFEETDLTYQVSESDSSGETKDTLKPAFTVTNLPGTTSTIQTAPSTSTTMQVSSGPSFPITNYLAPVSASVSPSAVSSANGTVLKSTGSGPVSSGGLMQLPTSFTLMPGGAVAQQVPVQAIQVHQAPQQASPSRDSSTDLTQTSSSGTVTLPATIMTSSVPTTVGGHMMYPSPHAVMYAPTSGLGDGSLTVLNAFSQAPSTMQVSHSQVQEPGGVPQVFLTASSGTVQIPVSAVQLHQMAVIGQQAGSSSNLTELQVVNLDTAHSTKSE
Protein: Protein PIP82 (Q9W3E2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the morphological differentiation and maintenance of the rhabdomeric photoreceptor apical domain. Acts as a downstream component of the gl and Pph13 transcriptional pathway which is required for photoreceptor cell development. Likely to function by regulating the trafficking or retention of rhabdomeric proteins including the phototransduction proteins ninaE and didum.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:26481050, ECO:0000269|PubMed:32579558}. Cytoplasm, cytosol {ECO:0000269|PubMed:26481050, ECO:0000269|PubMed:32579558}. Cell projection, rhabdomere {ECO:0000269|PubMed:32579558}. Note=Cortical membrane protein (PubMed:26481050, PubMed:32579558). In photoreceptors, restricted to the rhabdomeric portion of the apical surface (PubMed:32579558). Localizes to the terminal web at the base of the rhabdomere and not to the microvilli (PubMed:32579558). Phosphorylation appears to displace it from the cortex, increasing cytosol levels (PubMed:26481050, PubMed:32579558). {ECO:0000269|PubMed:26481050, ECO:0000269|PubMed:32579558}.
Interaction partners:
- Protein glass
- FI01102p
Sequence:
MSHQEQQFQHYPHHQHHHHHHHHHIHQVQSETQLEQRSSDLEPNRSRNTDRIGSSMDFRNLCQRIDVDGLKAKLPQLKLPKSLPKLRGRKIFRSSKSGSNAAGGGTAGGSAKDGAGAAQQTHLQVAGQSQQFINRTPQRISTISSLMYEGEQEEIRANLGQSQPGTYRSAGSLDDDYYAPGSGDRASRPISPIKIPVVGALDDSSPSENGNVRTTFTQRLQRGYKSLSELRIKHIFAKQTTVRRDNIEVDRYVEQYERELKSEKLARERRDREIAENYDIKIKTLAGTRQNTFDDDDVEHEQFERGKISHETDESGMEATPPLPSRRKPGIAATRFAKVRKPPLEMEEEQQQAAAEESPQANPPPPPPPRPSSYKQLLINKLPHLPSLPNLPQFSRTKEETTKTAENADENNASRKLSIRQNIKRLRKSIKRPSKIKSKAAAPVPDSDEEEATPDGQKTKDAPTRSSTANLRARLSRFASTEQLQQRWRKSFKVAKEPEELETKAEGSATGGASGVLGGLLVGSQLEKTLAKLNEKVHQLKFFQRNANNQNATTSKQPKPNTVGHEPIEIDDDELEATYHRSDSLEAENGNGNENDDSGEDISAEEAFGQIQEEDNEEDHSQDQTKRGQSSVSGIATAHAARQMAKLAEIQAASKSGAAAWSSESLEEIADEDYPRVLIHQEHSDAYESTLIIAVASKGSSMSPVVRSSGLKSSPAAGPKTSPHPEIRISASGPQKSMSYSPGNPRGEPVTKRSPSPEFKTPAGGNKIVPKSETSAWLPNEQIIAGFKEQTSWPAPALYKPKSIDIFEASAGGSAAFADFDEALRNAPVLRISAGSSIDTSGEEADDSCSRVTRIRVQSPQIGNSRESLMAQEEEDKEAERDSEEEEEERDPSERPPSESPPPPPLPQRRPPTKRPATPPIYDAVPPPLPVSKPPPPPSVETIPSVASLPSPAPVTRSMAQRSASMSRPAKPLVKTSSLRLTYNEQVRPGDVGKVNKLISRFEGGRPRLCPRRMHSEEYERCAQPEDEEPEMEQILELQIIERRAVDSVTPTNRAVVIPQITVNNNNNNERQLEQSDQSDQSAHQEITDTRKTKSMELALDRQNSNCSRSEYGSPLSFPSSRRSSTPTNLNANSNSNPNPSTNPNQNPSQILQHQRRSRRSMTRDDDNFYSFDSDEENSYYSISPSGSSRYVVEI
Protein: Callose synthase 3 (EC 2.4.1.34) (1,3-beta-glucan synthase) (Protein GLUCAN SYNTHASE-LIKE 12) (Q9LXT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in callose synthesis at the forming cell plate during cytokinesis. During plant growth and development, callose is found as a transitory component of the cell plate in dividing cells, is a major component of pollen mother cell walls and pollen tubes, and is found as a structural component of plasmodesmatal canals (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- PLASMODESMATA CALLOSE-BINDING PROTEIN 1
- Glucan endo-1,3-beta-glucosidase 10
- Plasmodesmata-located protein 5
Sequence:
MSATRGGPDQGPSQPQQRRIIRTQTAGNLGESFDSEVVPSSLVEIAPILRVANEVESSNPRVAYLCRFYAFEKAHRLDPTSSGRGVRQFKTALLQRLEREHDPTLMGRVKKSDAREMQSFYQHYYKKYIQALHNAADKADRAQLTKAYQTANVLFEVLKAVNLTQSIEVDREILEAQDKVAEKTQLYVPYNILPLDPDSANQAIMRYPEIQAAVLALRNTRGLPWPEGHKKKKDEDMLDWLQEMFGFQKDNVANQREHLILLLANVHIRQFPKPDQQPKLDDQALTEVMKKLFKNYKKWCKYLGRKSSLWLPTIQQEMQQRKLLYMALYLLIWGEAANLRFMPECLCYIYHHMAFELYGMLAGNVSPMTGENVKPAYGGEEDAFLRKVVTPIYEVIQMEAQRSKKGKSKHSQWRNYDDLNEYFWSVDCFRLGWPMRADADFFCLPVAVPNTEKDGDNSKPIVARDRWVGKVNFVEIRSFWHVFRSFDRMWSFYILCLQAMIIMAWDGGQPSSVFGADVFKKVLSVFITAAIMKLGQAVLDVILNFKAHQSMTLHVKLRYILKVFSAAAWVIILPVTYAYSWKDPPAFARTIKSWFGSAMHSPSLFIIAVVSYLSPNMLAGVMFLFPLLRRFLERSNYRIVMLMMWWSQPRLYVGRGMHESAFSLFKYTMFWVLLIATKLAFSYYIEIRPLVAPTQAIMKARVTNFQWHEFFPRAKNNIGVVIALWAPIILVYFMDSQIWYAIFSTLFGGIYGAFRRLGEIRTLGMLRSRFESLPGAFNDRLIPDGKNQQKKKGIRATLSHNFTEDKVPVNKEKEAARFAQLWNTIISSFREEDLISDREMDLLLVPYWADRDLDLIQWPPFLLASKIPIALDMAKDSNGKDRELKKRIESDTYMKCAVRECYASFKNIIKFVVQGNREKEVIEIIFAEVDKHIDTGDLIQEYKMSALPSLYDHFVKLIKYLLDNKEEDRDHVVILFQDMLEVVTRDIMMEDYNISSLVDSSHGGTWHGGMIPLEQQYQLFASSGAIRFPIEPVTEAWKEKIKRIYLLLTTKESAMDVPSNLEARRRISFFSNSLFMDMPMAPKVRNMLSFSVLTPYYTEEVLFSLRDLETPNEDGVSILFYLQKIFPDEWNNFLERVKCLSEEELKESDELEEELRLWASYRGQTLTRTVRGMMYYRKALELQAFLDMAMHEDLMEGYKAVELNSENNSRGERSLWAQCQAVADMKFTYVVSCQQYGIHKRSGDPRAQDILRLMTRYPSLRVAYIDEVEEPVKDKSKKGNQKVYYSVLVKVPKSTDHSTLAQNLDQVIYRIRLPGPAILGEGKPENQNHAIIFSRGEGLQTIDMNQDNYMEEALKMRNLLQEFLTKHDGVRHPSILGLREHIFTGSVSSLAWFMSNQETSFVTIGQRLLANPLRVRFHYGHPDVFDRLFHLTRGGVSKASKVINLSEDIFAGFNSTLREGNVTHHEYIQVGKGRDVGLNQISMFEAKIANGNGEQTLSRDIYRLGHRFDFFRMMSCYFTTVGFYFSTLITVLTVYIFLYGRLYLVLSGLEQGLSTQKGIRDNTPLQIALASQSFVQIGFLMALPMLMEIGLERGFRTALSEFVLMQLQLAPVFFTFSLGTKTHYYGRTLLHGGAKYRSTGRGFVVFHAKFADNYRLYSRSHFVKGLEMMLLLVVYQIFGSAYRGVLAYLLITISMWFMVGTWLFAPFLFNPSGFEWQKIVDDWTDWNKWINNIGGIGVPAEKSWESWWEEEQEHLRYSGKRGIVVEILLALRFFIYQYGLVYHLTITEKTKNFLVYGVSWLVIFLILFVMKTVSVGRRRFSASFQLMFRLIKGLIFMTFIAIIVILITLAHMTIQDIIVCILAFMPTGWGMLLIAQACKPVVHRAGFWGSVRTLARGYEIVMGLLLFTPVAFLAWFPFVSEFQTRMLFNQAFSRGLQISRILGGHRKDRSSRNKE
Protein: PTS system fructose-specific EIIB'BC component (EIIB'BC-Fru) [Includes: PTS system fructose-specific EIIB component (EC 2.7.1.202) (EIII-Fru) (Fructose-specific phosphotransferase enzyme IIB component); PTS system fructose-specific EIIC component (Fructose permease IIC component)] (P20966)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:3076173}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:3076173, ECO:0000305|PubMed:8626640}.
Interaction partners:
- Multiphosphoryl transfer protein
- 1-phosphofructokinase
- Phosphocarrier protein HPr
- ATP-dependent 6-phosphofructokinase isozyme 2
- Fructokinase
- Phosphoenolpyruvate-protein phosphotransferase
- Xylose isomerase
- PTS system glucose-specific EIICB component
- Fructose-bisphosphate aldolase class 2
- PTS system N-acetylglucosamine-specific EIICBA component
Sequence:
MKTLLIIDANLGQARAYMAKTLLGAAARKAKLEIIDNPNDAEMAIVLGDSIPNDSALNGKNVWLGDISRAVAHPELFLSEAKGHAKPYTAPVAATAPVAASGPKRVVAVTACPTGVAHTFMAAEAIETEAKKRGWWVKVETRGSVGAGNAITPEEVAAADLVIVAADIEVDLAKFAGKPMYRTSTGLALKKTAQELDKAVAEATPYEPAGKAQTATTESKKESAGAYRHLLTGVSYMLPMVVAGGLCIALSFAFGIEAFKEPGTLAAALMQIGGGSAFALMVPVLAGYIAFSIADRPGLTPGLIGGMLAVSTGSGFIGGIIAGFLAGYIAKLISTQLKLPQSMEALKPILIIPLISSLVVGLAMIYLIGKPVAGILEGLTHWLQTMGTANAVLLGAILGGMMCTDMGGPVNKAAYAFGVGLLSTQTYGPMAAIMAAGMVPPLAMGLATMVARRKFDKAQQEGGKAALVLGLCFISEGAIPFAARDPMRVLPCCIVGGALTGAISMAIGAKLMAPHGGLFVLLIPGAITPVLGYLVAIIAGTLVAGLAYAFLKRPEVDAVAKAA
Protein: Transcription repressor KAN1 (Protein KANADI 1) (Q93WJ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional repressor that regulates lateral organ polarity. Promotes lateral organ abaxial identity by repressing the adaxial regulator ASYMMETRIC LEAVES2 (AS2) in abaxial cells. Required for abaxial identity in both leaves and carpels. Functions with KAN2 in the specification of polarity of the ovule outer integument. Regulates cambium activity by repressing the auxin efflux carrier PIN1. Plays a role in lateral root formation and development.
Subcellular location: Nucleus.
Interaction partners:
- Axial regulator YABBY 1
- Axial regulator YABBY 3
- Protein ASYMMETRIC LEAVES 2
- Protein ULTRAPETALA 2
- Auxin response factor 3
- Auxin response factor 4
- Putative axial regulator YABBY 2
- Transcription factor AS1
- Axial regulator YABBY 5
- WUSCHEL-related homeobox 1
Sequence:
MSMEGVFLEKTKTNTTTTLPDLSLHISLPDIHQYHHNESSKESSRRSSQLENNNRSSNFELSLSHHNHPTARIFHCPDRRTLNLPHQQHYNNPIINGVHQRVDESEISNLHRPIRGIPVYHNRSFPFHQQNSSLPSLGGGDMDQISILNSSSGYNNAYRSLQSSPRLKGVPLHHHHHHNQYGVVGSSDSSSPHHHNHHHHGMIRSRFLPKMPTKRSMRAPRMRWTSSLHARFVHAVELLGGHERATPKSVLELMDVKDLTLAHVKSHLQMYRTVKTTNKPAASSDGSGEEEMGINGNEVHHQSSTDQRAQSDDTSLHQETDISSTQPRWSNSSRETWPLSNNCSSDIDTMIRTSSTSMISHYQRSSIQNQEQRSNDQAKRCGNLSCENPSLEFTLGRPDWHEK
Protein: Beta-2-glycoprotein 1 (APC inhibitor) (Activated protein C-binding protein) (Anticardiolipin cofactor) (Apolipoprotein H) (Apo-H) (Beta-2-glycoprotein I) (B2GPI) (Beta(2)GPI) (P02749)
Organism: Homo sapiens (Human)
Function: Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein A-II
- Apolipoprotein C-III
- Apolipoprotein B-100
- Apolipoprotein A-I
- Prothrombin
- Apolipoprotein M
- Alpha-2-HS-glycoprotein
- Apolipoprotein C-II
- Antithrombin-III
- Annexin A2
Sequence:
MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTIEVPKCFKEHSSLAFWKTDASDVKPC
Protein: RuvB-like 2 (EC 3.6.4.12) (Reptin) (Q9GZH2)
Organism: Caenorhabditis elegans
Function: Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity suggesting a role in nuclear processes such as recombination and transcription (By similarity). May participate in several chromatin remodeling complexes that mediate the ATP-dependent exchange of histones and remodel chromatin by shifting nucleosomes (By similarity). Involvement in these complexes is likely required for transcriptional activation of selected genes and DNA repair in response to DNA damage (By similarity). Has a role in gonadal development. Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes. Specifically, negatively controls the expression of ER homeostasis regulator ckb-2 in a cdc-48.1/2-dependent manner.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25437307}. Nucleus {ECO:0000269|PubMed:25437307}.
Interaction partners:
- RuvB-like 1
- Helicase ssl-1
- Actin-related protein 4
- Non-specific serine/threonine protein kinase
- HIT-type domain-containing protein
- DNA methyltransferase 1-associated protein 1
- Actin-like protein C08B11.6
- Nop domain-containing protein
- Putative H/ACA ribonucleoprotein complex subunit 4
- Vacuolar protein sorting-associated protein 72 homolog
Sequence:
MATLDGINVKDIVKVERTSVHSHITGLGLNDRLEAEYVSGGMVGQVAARQAAGLIVKMIQEGKIAGRALLVTGEPGAGKTAIAIAISKELGEDTPFVSIVASEIYSNEINKTEALTQAFRRALGIQIKEETEVLEGEVISLEVDRSANGMGPKVGKLTMRTTDMETIYDLGSKMVDACLKEKVMPGDVIQVDKASGRVTRLGRSFNRSHDYDAMGPKVKLVQCPDGEIQKRRETVHTVCLHDIDVINSRTQGYVALFSGDTGEIKAEVRDQINKKVLEWREEGKAKFVPGVLFIDEAHMLDIECFSFLNRAIEGELSPLIIMATNRLIEKVRGTDVESAHGIPSDFLDRMLIINAIPYTKEDTAKILSIRCDEEGVKLQPTALDLLVKLQEATSLRYCIHLIAASEVIRIRSKAEIVTTDHIGSAYRLFFDTKRSEKILTEESAGFLQ
Protein: Glycerate 2-kinase (GCK) (EC 2.7.1.165) (2-phosphoglycerate forming glycerate kinase) (Q96YZ3)
Organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
Function: Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate. It can also utilize GTP, CTP, UTP, ADP, AMP or pyrophosphate as phosphate donor.
Interaction partners:
- Enolase
- Indolepyruvate--methylviologen oxidoreductase subunit b
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Indolepyruvate--methylviologen oxidoreductase subunit a
- Indolepyruvate--methylviologen oxidoreductase subunit c
- Pyruvate kinase
- D-glucosamine-6-phosphate 4-epimerase
- Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
- Fructose-1,6-bisphosphate aldolase
Sequence:
MDKIIEKILTFSDPYIALDERVVIKKNEIIVDGNHFPYTKPAIIAVGKASYKMAKFFIDKLKDVKGLVILPKGSYISLPKVEVIESTHPDISELSFKAGTEVIKFLKNEDYDLLIFLLSGGASALMEYSNVPYEILRDINEKLVKSGLSVNEINIVRKHLSLIKGGKLTEFSKAPILTLIVSDVPGGDLSAVGSGPTLPDSSTVDDAKLILNKVGLGEYSKYLIETKKEVHNSFNFLILDINIVLRKLRDIVQNPIILSSEIRGDAYSFGQNLAGIVNTSFSNLGLKPPYTLLAGGEPDVKIEGKAGKGGRNGEVCLGFLKWVKRNSNHRFKLYAIATDGIDGNSEYAGCIVDENTIVDNIEYYIYSHSSYEALEKVGRVIKTGYTFTNVNNVYVLEVT
Protein: Asparagine--tRNA ligase, cytoplasmic (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) (P38707)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn).
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:9605503}.
Interaction partners:
- Glutamyl-tRNA
- Putative proline--tRNA ligase YHR020W
- Glutamate--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, mitochondrial
- Glutamine--tRNA ligase
- DNA repair protein RAD1
- Histidine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
Sequence:
MSSLYIKEATGVDELTTAGSQDHPFKTPAYALFASQQKSDATEPKLFVFKTEDNEYQEISASALKKARKGCDGLKKKAVKQKEQELKKQQKEAENAAKQLSALNITIKEDESLPAAIKTRIYDSYSKVGQRVKVSGWIHRLRSNKKVIFVVLRDGSGFIQCVLSGDLALAQQTLDLTLESTVTLYGTIVKLPEGKTAPGGVELNVDYYEVVGLAPGGEDSFTNKIAEGSDPSLLLDQRHLALRGDALSAVMKVRAALLKSVRRVYDEEHLTEVTPPCMVQTQVEGGSTLFKMNYYGEEAYLTQSSQLYLETCLASLGDVYTIQESFRAEKSHTRRHLSEYTHIEAELAFLTFDDLLQHIETLIVKSVQYVLEDPIAGPLVKQLNPNFKAPKAPFMRLQYKDAITWLNEHDIKNEEGEDFKFGDDIAEAAERKMTDTIGVPIFLTRFPVEIKSFYMKRCSDDPRVTESVDVLMPNVGEITGGSMRIDDMDELMAGFKREGIDTDAYYWFIDQRKYGTCPHGGYGIGTERILAWLCDRFTVRDCSLYPRFSGRCKP