wanglab/gogpt-training-data huggingface dataset:
Protein: Dyslexia-associated protein KIAA0319-like protein (Adeno-associated virus receptor) (AAVR) (Q8K135)
Organism: Mus musculus (Mouse)
Function: Possible role in axon guidance through interaction with RTN4R.
Subcellular location: Cytoplasmic granule membrane {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IZA0}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IZA0}. Cell membrane {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IZA0}. Note=Traffics from the plasma membrane to the trans-Golgi network. {ECO:0000250|UniProtKB:Q8IZA0}.
Interaction partners:
Sequence:
MEKRLGVKPSPASWVLPGYCWQTSVKLPRSLYLLYSFFCFSVLWLSTDADESRCQQGKTLYGAGLRTEGENHLRLLAGSLPFHACRAACCRDSACHALWWLEGMCFQADCSKPQSCQPFRTDSSNSMLIIFQKSQTTDDLGLLPEDDEPHLLRLGWGRTSWRRQSLLGAPLTLSVPSSHHQSLLRDRQKRDLSVVPTHGAMQHSKVNHSEEAGALSPTSAEVRKTITVAGSFTSNHTTQTPEWPKNVSIHPEPSEHSSPVSGTPQVKSTEHSPTDAPLPVAPSYSYATPTPQASSQSTSAPHPVVKELVVSAGKSVQITLPKNEVQLNAFVLPEAEPGETYTYDWQLITHPTDYSGEVERKHSQSLQLSKLTPGLYEFKVTVDGQNAHGEGYVNVTVKPEPRKNRPPVAVVSPQFQEISLPTTSTIIDGSQSTDDDKIVQYHWEELKGPLREEKISEDTAILKLSKLVPGNYTFSLTVVDSDGATNSTTASLTVNKAVDYPPVANAGPNQVITLPQNSITLFGNQSTDDHGITSYEWSLSPSSKGKVVEMQGVRTPALQLSAMQEGDYTYQLTVTDTAGQQATAQVTVIVQPENNKPPQADAGPDKELTLPVDSTTLDGSKSTDDQRVVSYLWEQSRGPDGVQLENANSSVATVTGLQVGTYVFTLTVKDERNLQSQSSVNVIVKEEINKPPVAKIAGNVVVTLPTSTAELDGSRSSDDKGIVSYLWTRDETSPAAGEVLNHSDHHPVLFLSNLVEGTYTFHLKVTDAKGESDTDRTTVEVKPDPRKSNLVEIILDVNVSQLTERLKGMLIRQIGVLLGVLDSDIIVQKIQPYTEQSTKMLFFVQNDPPHQLFKGHEVAAMLKSELQKQKADFLIFRALEISTVTCQLNCSDHGHCDSFTKRCVCDPFWMENFIKVQLRDGDSNCEWSVLYVIIASFVIVVALGILSWTTICCCKRQKGKPKRKSRYKILDATDQESLELKPTSRAGSKQKGPTLSSSLMHSESELDSDDAIFTWPDREKGKLLYGQNGSVPNGQTPLKSRSAREEIL
Protein: Heat-labile enterotoxin B chain (P01558)
Organism: Clostridium perfringens
Function: This enterotoxin is responsible for many cases of a mild type of food poisoning.
Interaction partners:
Sequence:
MLSNNLNPMVFENAKEVFLISEDLKTPINITNSNSNLSDGLYVIDKGDGWILGEPSVVSSQILNPNETGTFSQSLTKSKEVSINVNFSVGFTSEFIQASVEYGFGITIGEQNTIERSVSTTAGPNEYVYYKVYATYRKYQAIRISHGNISDDGSIYKLTGIWLSKTSADSLGNIDQGSLIETGERCVLTVPSTDIEKEILDLAAATERLNLTDALNSNPAGNLYDWRSSNSYPWTQKLNLHLTITATGQKYRILASKIVDFNIYSNNFNNLVKLEQSLGDGVKDHYVDISLDAGQYVLVMKANSSYSGNYPYSILFQKF
Protein: Dynein light chain 1, cytoplasmic (Q02647)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex where it may contribute to the stable association of the Nup82 subcomplex with the NPC.
Subcellular location: Cytoplasm, cytoskeleton. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17546040, ECO:0000269|PubMed:23223634, ECO:0000269|PubMed:25646085}.
Interaction partners:
- WD repeat-containing protein PAC11
- Dynein heavy chain, cytoplasmic
- Nucleoporin NUP159
- Peroxisomal membrane protein PEX14
- Cytoplasmic dynein intermediate light chain DYN3
- Peroxisomal membrane protein PMP27
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX17
- Peroxisomal biogenesis factor 8
- Nucleoporin NSP1
Sequence:
MSDENKSTPIVKASDITDKLKEDILTISKDALDKYQLERDIAGTVKKQLDVKYGNTWHVIVGKNFGSYVTHEKGHFVYFYIGPLAFLVFKTA
Protein: Kinesin heavy chain 73, isoform A (EC 3.6.1.3) (A1ZA18)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MASDKIKVAVRVRPFNRREIELDTKCIVEMEKQQTILQNPPPLEKIERKQPKTFAFDHCFYSLNPEDENFASQETVFDCVGRGILDNAFQGYNACIFAYGQTGSGKSYTMMGTQESKGIIPRLCDQLFSAIANKSTPELMYKVEVSYMEIYNEKVHDLLDPKPNKQSLKVREHNVMGPYVDGLSQLAVTSYQDIDNLMTEGNKSRTVAATNMNAESSRSHAVFSVVLTQILTDQATGVSGEKVSRMSLVDLAGSERAVKTGAVGDRLKEGSNINKSLTTLGLVISKLADQSNGKKSGNDKFVPYRDSVLTWLLKDNLGGNSRTVMVATISPSADNYEETLSTLRYADRAKRIVNHAVVNEDPNARIIRELRHEVETLRSMLKHATGSPVGDVQDKLAESENLMKQISQTWEEKLVKTERIQNERQQALEKMGISVQASGIKVEKNKYYLVNLNADPSLNELLVYYLKDRTLIGGRTISGQQPDIQLSGLGIQPEHCVITIEDSGLYMEPVQGARCFVNGSAAVEKTPLQNGDRILWGNHHFFRVNSPKSNNTSMCASEPQTPAQLIDYNFARDEIMQNELSNDPIQTAIARLERQHEEDKQVALEKQRQEYERQFQQLRNILSPSTPYAPYAPYDPLRMGKITPNTPTSQMRVEKWAQERDEMFRRSLGQLKTDIMRANSLVQEANFLAEEMEKKTKFSVTLQIPPANLSPNRRRGAFVSEPAILVKRTNSGSQIWTMEKLENKLIDMREMYQEHKERVLNGLPLIEPFSEDEFDDKDEDNAKPQDPFYESQENHNLIGVANIFLEVLFHDVKLDYHTPIISQQGEVAGRLQVEIERIAGQMPQDRMCESVSESSGDSRDEYDDPVDPTSNQITCRVTIKCASGLPLSLSNFVFCQYTFWGHQEMVVPVINAESTAHDQNMVFKFEHTQDFTVTINEEFLEHCIEGALSIEVWGHRSAGFSKTKGWEVEQQQAKARSLVDRWAELSRKIELWVEIHELNDNGEYSPVEVTNRNEVLTGGIYQLRQGQQRRVNVRVKPVQNSGTLPIICQSIVNVAIGSVTVRSRLQRPLDSYQEEDLTVLREKWSEALGRRRQYLDQQIQMLIKKEEKNEQERERELSLVHQWVSLTEERNAVLVPAPGSGIPGAPASWEPPSGMEPHVPVLFLNLNGDDLSAQNTNDELSVAGINSILSKEHGHKFYTLQILQHLDKDVCCVASWDSSMHDSQALNRVTEANERVYLILRTTVRLSHPAPMDLVLRKRLSINIKKGQTLTDRLKKFRLVRGENAIWQSGVTYEVVSNIPKASEELEDRESLAQLAASGDDCSASDGETYIEKYTRGVSAVESILTLDRLRQNVAVKELETAHGQPLSMRKTVSVPNFSQQLINKLTQIMRFDASMESLLNVGRSESFADLNNSALGNKFTPAGHSPAGAGGVIRSRHSFGGKGSSDDSPGKAFGIASPATSKLLGMRMTTLHEEPLGGHRSLDEEPEDSYSDSEYAAEYEQERQQNKSMATRSRLTASKTMDSFMDVSSHSNQSYLSYTSSANANMKHLTGLATLSMSSSTSSGYGSQAVSCNNLSNEDIASMRSMSIDETPDFDRVNSNSPPNRQARVNPFLKDMPKAKIQEQPEQQAKKLQEAFTHPLEQLESSQNAQSDDDECAQLPKNNNNNLDLVNEPKPLSSQTDLEESMSQPKSKTEFATDNQNGNRSSDELSHSSEDLLEGDGIVREELPAGKVVRRKKSNTQPPSNGNSINNNNNGTTQAPRINHRASVAKMEGLAAYLDSSIMTSSTEVDEESKDVELVLPEWIVVGESVLIRPYNTSGVIRFVGTTEFQPGAWIGVELDTPTGKNDGSVKGVQYFQCKPKHGMFVRSDKLMLDKRGKAMRAYKAAEKSNSISKEMSTSMTGSMTRSKSRGDSLNLSARK
Protein: FMR1 autosomal homolog 1 (H7C4S4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTNSELSNPSETESERKDELSDWSLAGEDDRDSRHQRDSRRRPGGRGRSVSGGRGRGGPRGGKSSISSVLKDPDSNPYSLLDNTESDQTADTDASESHHSTNRRRRSRRRRTDEDAVLMDGMTESDTASVNENGLDDSEKKPQRRNRSRRRRFRGQAEDRQPVTVADYISRAESQSRQRNLPRETLAKNKKEMAKDVIEEHGPSEKAINGPTSASGDDISKLQRTPGEEKINTLKEENTQEAAVLN
Protein: Folylpolyglutamate synthase (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (FPGS) (Tetrahydrofolylpolyglutamate synthase) (Tetrahydrofolate synthase) (Q08645)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Required for methionine synthesis and maintenance of intact mitochondrial DNA. Involved in telomere maintenance.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10775416}. Mitochondrion inner membrane {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:10775416}.
Interaction partners:
- Folic acid synthesis protein FOL1
- Dihydrofolate reductase
- Probable folylpolyglutamate synthase
- Dihydrofolate synthetase
- Thymidylate synthase
- C-1-tetrahydrofolate synthase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- GTP cyclohydrolase 1
- Methylenetetrahydrofolate dehydrogenase [NAD
- Tryptophan synthase
Sequence:
MHKGKKNYPNLITSFRMNLKKIILNHDRFSHPERWKTNALLRFTFVYIKFLFDLMIIKNPLRMVGKTYRDAVTALNSLQSNYANIMAIRQTGDRKNTMTLLEMHEWSRRIGYSASDFNKLNIVHITGTKGKGSTAAFTSSILGQYKEQLPRIGLYTSPHLKSVRERIRINGEPISEEKFAKYFFEVWDRLDSTTSSLDKFPHMIPGSKPGYFKFLTLLSFHTFIQEDCKSCVYEVGVGGELDSTNIIEKPIVCGVTLLGIDHTFMLGDTIEEIAWNKGGIFKSGAPAFTVEKQPPQGLTILKERAEERKTTLTEVPPFKQLENVKLGIAGEFQKSNASLAVMLASEILHTSNILEEKIKCSSNASIPEKFIIGLQNTKWEGRCQVLEKGKNVWYIDGAHTKDSMVAASTWFRDMVRLSKRKKILLFNQQSRDANALVNNLYSSVSPEITFDDVIFTTNVTWKSGSYSADLVSMNTSQEDVEKLKVQESLVKNWNKIDDNRAKTHVTASIEEANELIETLYDEPADIFVTGSLHLVGGLLVVFDRIDVK
Protein: Origin of replication complex subunit 3 (OsORC3) (Q0IY07)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UBD5}.
Interaction partners:
- Origin of replication complex subunit 1
- Origin of replication complex subunit 2
- Cell division control protein 6 homolog
- Origin of replication complex subunit 1
- Origin of replication complex subunit 6
- Origin of replication complex subunit 4
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM4
- Os05g0121200 protein
Sequence:
MAAPPGEAPLTAATNIEPFYVLHKGGAAASSSSSSAPSLPSSGRARRRIDVSGLASPNPKPGKRSRDDDAAEDDDDDELYERLRLDAFHRVWSKIQSTINEVLRGISLKLFDQVLRWVQESFSAVRSIARPSAAEVRQPYPLLTDVICRKIPTAFVLTKNAEFVDDITTFRDLAEYLESNGCHLAKLSATELSEKNGVGCCFRSLLRQLLSDVPDVADIFALASWYSAAENYDQPIVVVIDDLEQCSGDVLGELVMMLSEWVIKIPIFFVMGIATTLDAPRKLLSSEDLQRLEPCKLTLGSPSDRMNALVEAILVKPCAGFCISHEVAVFLRNYFFKHDGTITSFISALKLACSKHFSVEPLSFLCMGMLEEDRENFWHDKFNALPQELRKYASGLPSCTREKDSTKSGDNMVDGLSELMNIQKDWSSVLLCLYEAGKHGKVQLLDIFCEAVNPDLHTQKAPNLPNEKSGTSRRFIDQVMDTIRYLPVETLFCLLEVWSIHLNGMDKITNKVKELQSTTISTDSVRITKDKWPRRSTNSTGNSTVALNDKVAMLLDDVTRKFLVSVECLPFHEIVCFKNVSILQSALIGNPRRMVQLDLVKSHKHLKCSCCRKNGIAVLASMHDTSIMCNLAQEYGDVINLHDWYISFDGIINSVHSKIKRKPHTSPSKKKSKPVAAESEAMIQARFCRAVTELQITGLLRMPSKRRPDLVQRIAFGL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q4GZ66)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVSKEENANIKKGEESDAYLQERGINNIIENLLHDITKCRPDDHLEFMKEWLATRETGKKEFSDGNEAKQMIESPLEREATVGETSEFISETVPEFAFFQPVKKPSTVSWALGARGVDSSRALFTSSRKSPQPIDSVNTTSSSSGSSALQNNLSVAAQGVSMWVPSAAPLKASPAIPSNPLPLSPTTSEGLVSCGELPSSVKKIIEGVRGLSPADHTAVIAFIDGLANRAATTRLGRRKLSNTRGSFGVNFNVDSCGPTMSEGAVPPCISLLVDDDGNVGGERKLSSVQLQQLVGDALTTSMIATGEIFMEEERAGQLSASTTQGASTLGRRVKKGSNLQLARFTDCFSMSDQILPGSNGGVGSGSGPNDGATDLSQMFSSVDEFAAVPVSFIQQYMQHSRLSSTVSRVDSEYSSGATVSSEDEVSVLRKAFRACKRFSDYSETEIEVLARNAQRLELLAGHTCNFKDSIFYVHSGLLRVENNEGVLRELPAGTFLDAQSCEQLNDAREPLEVRAVSDALVLMLKDEALGTIQENEKKLKKRMFVRCLQKSPLFATVPLKLLKNIANYMHVRTVVQGKVLLRKGEHVDWLSVVISGTVSRVVAGGNGNHEVLPQNKQKGGPSSCAAPYILPPESQSGFEFGELELLFNSPMLTDVVATTPVTLARVCTAFVHSLLPHQIINDMKYAVATNPSAGPLLTIAPDAVRHSVKMFMEHYCQSKRLGGSRLRKRISVSSTGTNSTRGFADSVRCGVLASGAKASGGANNLKVSSAGEIVYAGKCNYYRFPIAALGLGNTVVVAVVSDGTIIRWNDSAERITGFSRQQVLGHSVFSSLTTDSARRSMREQLKLVRNVAGNWNQYVSAGLSSPQVYRFRQASGTHSVGLLLSVIPSSAGSNEDVLLLVGREADNNAMTSYVEDTTRWLNDVLRPQLSAFRKRVCEYEERKWNITLEEGAKLHGYVEACNQLMDRYMRLANLNKHSVDALWKPVRMQNVLRQFLQEVTPHVQRAGNKLTTDVVAGPKGEVFLHVEYVLDVLRGMVLDANKNRPNYHMHIVVEAVLPTTMHQDSTTMPCQGEKSTSCDLAFHSVLDQSRVSLDTPHCTTSQITASEDSIRQRSAHSPRQLSKWPSYMQLIRFIFTISESESGLSMANDNTSGGAATTPSGEVPRSSKIHHSFYAGKECGDLVAAMGGEVFSEQRGMNGSGHCVTVELPLLPTPWEEEDDEDEAPTSSTTGPPFAVILADKNEKERNSVCKLLWARRHPVFSVSSLSEVMMRIESPDIGLLIIDPCHLDMTEGESKTFAKAPYPFNMEHGGNHFVVLIYTEDFDDWRVQKMKKCSHVIELPKPATTSLLHSTLYEAERMVIRVREYEERVAQMRSAFREFQAERYEMGKVLGRGSYGEVYEVVDRLTGGKLAVKRMTLSDGLLAADVAEEFLSVTSMRHKNMIHYFYCEQESETVLRLYMELASGGTLKDKIRQHGGPLPLPTVVQYLEDLCDGLAYIHSNLFVHGDIKTANALVDQYGRVKIGDFGTAKRLKRKSEKLYKFVGTPRFMAPELINADATQGHGYDQKGDIWSLGCVALELATGKPPFWHIEEAQGIGIFNFLINLKETPDLSIIEHSDPDFYAFVRRCLHVDPKERPTAQELLTSNLFQRAGTSVRDMRLAQQIQAATKLHEYAALKEDNSDDENDDDDDDEDDDDDDMFVECDFPLVFSGVGTFPNGDQNVATSNRGNIDNEKKGTAKLSG
Protein: Tyrosine 3-monooxygenase (EC 1.14.16.2) (Tyrosine 3-hydroxylase) (TH) (P04177)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan but with lower specificity. Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000269|PubMed:21392500, ECO:0000269|PubMed:32778969}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000269|PubMed:15496595, ECO:0000269|PubMed:21392500, ECO:0000269|PubMed:32778969}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:15496595}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phosphorylated at Ser-31 as well as at Ser-40 shows a cytosolic distribution (PubMed:21392500, PubMed:32778969). Expressed in dopaminergic axons and axon terminals (By similarity). {ECO:0000250|UniProtKB:P07101, ECO:0000269|PubMed:21392500}.
Interaction partners:
- Alpha-synuclein
- Aromatic-L-amino-acid decarboxylase
- Pterin-4-alpha-carbinolamine dehydratase
- 4a-hydroxytetrahydrobiopterin dehydratase
- Sepiapterin reductase
- Synaptic vesicular amine transporter
- Dihydropteridine reductase
- Dopamine beta-hydroxylase
- Aspartate aminotransferase, mitochondrial
- Tyrosinase
Sequence:
MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIQRSLEGVQDELHTLAHALSAIS
Protein: RE04485p (Q8IGY7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEATMDTDHANLNDFRDRDLATRMRRCNYEKYKSLVRMHLSFELELNTDEFDLPCHEIVYEDKGKLKKWNRLSKKHRLGHGAAATSCAAGSASKSVGNSPTETLQQQIDPGFLMHLQELKEFLMLEKNLTQEGLFRKAGAVSRQNELRMHIQHDKPLNLELAGFSAHDCATVFKGFLSELPEPLLTDAHYPAHLQIAPLCQALNGQTTATAERQQHLLNSVQLLLLLLPEEHRELLQHIIEMLHAVAKHEKSNKMSADNLATLFTPHLICPRQLPPEVLHYQAKKMSSIVTYMIVRGLDIFEVPGKLSTDIRAYFLERKRKKTMSPEQTLDESISDVSTVNTVYTFVDRAATAAATNTNNTDTELAQLYAHIQSMPESSKKRRLIKQFNKQNGQGKLLYIFNALMPFHSGSYDLNTSASNFKIT
Protein: Alpha N-terminal protein methyltransferase 1 (EC 2.1.1.244) (X-Pro-Lys N-terminal protein methyltransferase 1) (A0A1D8PQL1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ribosome assembly factor mrt4
- Arginine N-methyltransferase 2
Sequence:
MPAKSQQGWEIDFNQSSEPADSQINYDDAIQYWSNTPASVDGVLGGYGEQTSVPKADIVGSSTFLRKLATRMTCPEGVPKTTIDMGAGIGRITRDLLWKVSDSVDLLEPVKPFVAQMHNELTEVKKRGKLGKIYDIGMQDWQPEQSYWLIWCQWCVGQLPDDVLVEFWSRCRSALIENGTMIVKENIAPFEDIFDETDSSVTRTDAKFRELFERAGFKLIASDIQKGLPKELYPVRMYCLKSK
Protein: Type IV pilus inner membrane component PilO (G3XD51)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:19857645}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Type IV pilus inner membrane component PilM
- Type IV pilus inner membrane component PilP
- Type IV pilus inner membrane component PilN
- Fimbrial assembly protein PilQ
- Type IV pilus assembly protein PilF
- Type IV pilus retractation ATPase PilT
- Type IV pilus non-core minor pilin PilE
- Type IV pilus ATPase PilU
- Type IV pilus biogenesis factor PilY1
- Type 4 fimbrial biogenesis protein PilW
Sequence:
MSLASSLESLRKIDINDLDLNNIGSWPAAVKVIVCVLLTAAVLALGYNFHLSDMQAQLEQQAAEEETLKQQFSTKAFQAANLEAYKAQMKEMEESFGALLRQLPSDTEVPGLLEDITRTGLGSGLEFEEIKLLPEVAQQFYIELPIQISVVGGYHDLATFVSGVSSLPRIVTLHDFEIKPVAPGSTSKLRMSILAKTYRYNDKGLKK
Protein: Stabilizer of axonemal microtubules 1 (Q8IYX7)
Organism: Homo sapiens (Human)
Function: May play a role in the regulation of cilium length. Stabilizes microtubules at low temperature.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:25673876}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25673876}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25673876}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25673876}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:25673876}. Note=In multi-ciliated cells, localizes to the basal bodies and in non-ciliated cells, to the centrosome. In spermatozoa, colocalizes with microtubules along the length of the axoneme from its proximal end to its distal tip and with tubulin at the distal end of the flagellum and at the proximal centriole. {ECO:0000269|PubMed:25673876}.
Interaction partners:
Sequence:
MKTKCICELCSCGRHHCPHLPTKIYDKTEKPCLLSEYTENYPFYHSYLPRESFKPRREYQKGPIPMEGLTTSRRDFGPHKVAPVKVHQYDQFVPSEENMDLLTTYKKDYNPYPVCRVDPIKPRDSKYPCSDKMECLPTYKADYLPWNQPRREPLRLEHKYQPASVRFDNRTTHQDDYPIKGLVKTISCKPLAMPKLCNIPLEDVTNYKMSYVAHPVEKRFVHEAEKFRPCEIPFESLTTQKQSYRGLMGEPAKSLKPLARPPGLDMPFCNTTEFRDKYQAWPMPRMFSKAPITYVPPEDRMDLLTTVQAHYTCPKGAPAQSCRPALQIKKCGRFEGSSTTKDDYKQWSSMRTEPVKPVPQLDLPTEPLDCLTTTRAHYVPHLPINTKSCKPHWSGPRGNVPVESQTTYTISFTPKEMGRCLASYPEPPGYTFEEVDALGHRIYKPVSQAGSQQSSHLSVDDSENPNQRELEVLA
Protein: Uncharacterized protein (Q381B5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGVRMFCDFLKLRRWERHVLAQRERQESALAAAFRCIPWSGVAMFFFVMIFFGIDLGAGIKHTARQIQEKKEEAAQSVEVQKMQARQWSVEQVKNFREGEIPKPSWAEGGPRGSNNPL
Protein: Protein K3 (P20639)
Organism: Vaccinia virus (strain Copenhagen) (VACV)
Function: Viral mimic of eIF-2-alpha that acts as a pseudosubstrate for EIF2AK2/PKR kinase. Inhibits therefore eIF-2-alpha phosphorylation by host EIF2AK2/PKR kinase and prevents protein synthesis shutoff (By similarity).
Interaction partners:
Sequence:
MLAFCYSLPNAGDVIKGRVYEKDYALYIYLFDYPHSEAILAESVKMHMDRYVEYRDKLVGKTVKVKVIRVDYTKGYIDVNYKRMCRHQ
Protein: Equilibrative nucleoside transporter 4 (mENT4) (Plasma membrane monoamine transporter) (PMAT) (Solute carrier family 29 member 4) (Q8R139)
Organism: Mus musculus (Mouse)
Function: Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorptprev reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q7RTT9}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:23255610}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the apical blood-cerebrospinal fluid(CSF)-facing membrane of the choroid plexus epithelium. {ECO:0000269|PubMed:23255610}.
Interaction partners:
- Solute carrier family 28 member 3
- Sodium/nucleoside cotransporter 1
- Sodium/nucleoside cotransporter 2
Sequence:
MGSIGSQRLKEPCVAATSDQSVVTSFSFDNFQLETTAEGAQDPGIRVRGVPTFTDSAVEEPVPDDRYHAIYFAMLLAGVGFLLPYNSFITDVDYLHHKYPGTSIVFDMSLTYILVALAAVLLNNVVVERLNLHTRITTGYLLALGPLLFISICDVWLQLFSHDQAYAINLAAVGTVAFGCTVQQSSFYGYTGLLPKRYTQGVMTGESTAGVMISLSRILTKLLLPDERASTIIFFLVSAGLELLCFLLHLLVRRSRFVLYYTTRPRDSRPVQAGYRVHHDVASGDIHFEHQTPALSSSRSPKESPAHEVTHSNSGVYMRFDVPRPRVKRSWPTFRALLLHRYVVARVIWADMLSIAVTYFITLCLFPGLESEIRHCVLGEWLPILVMAVFNLSDFVGKILAALPVEWRGTHLLACSCLRVVFIPLFILCVYPSGMPALRHPAWPCVFSLLMGISNGYFGSVPMILAAGKVSPKQRELAGNTMTVSYMSGLTLGSAVAYCTYSLTRDAHGSCFQTATAAAANDSIPVGP
Protein: Protein TILLER ANGLE CONTROL 1 (PpeTAC1) (U3MMQ4)
Organism: Prunus persica (Peach) (Amygdalus persica)
Function: Involved in the regulation of axillary shoot growth angle. Promotes horizontal shoot growth.
Interaction partners:
- Endoglucanase
Sequence:
MKIFNWVHKRLHQRVVKDGFAGNVKKSELETNDKDTQAFLKQVGLVNVDGLDGWRDGILTIGTFGFDPLKPSTHQNEYFVLESEEDDQESHGFSHSGNDDDDDDDEHYDHSVEDEELNPLMFTTFEHSFEDIGSNFDAIVQKPADVILTVDGVPLTPFEGSSEISTKPDQSANDQSKNKKGQRITLADLFQADVPDVGQLKLDSGKVQPEMEKKMNARTRSGLAFAKKLIPRVKDDSSPIKNMQRLMRRMLKRKIHPAELEVKIHKSDGQKQPSAVELISNVENDAYESVSLLPIQGAPCVH
Protein: Plakophilin-3 (Q9QY23)
Organism: Mus musculus (Mouse)
Function: May play a role in junctional plaques.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y446}. Cell junction, desmosome {ECO:0000269|PubMed:18079750, ECO:0000269|PubMed:26173741, ECO:0000269|PubMed:27033150, ECO:0000269|PubMed:27375112, ECO:0000269|PubMed:29678907, ECO:0000269|PubMed:38395410}. Cytoplasm {ECO:0000269|PubMed:27033150, ECO:0000269|PubMed:29678907}. Cell membrane {ECO:0000250|UniProtKB:Q9Y446}; Peripheral membrane protein {ECO:0000305}. Cell junction, adherens junction {ECO:0000269|PubMed:27375112}. Note=Translocates to the nucleus following canonical WNT signaling activation by WNT3A (By similarity). Maintains a cytoplasmic pool which can then be translocated to the desmosome, the cytoplasmic pool is maintained through PKP3 interaction with SFN (By similarity). Aberrant increases in translocation to the desmosome result in cell junction instability and therefore decreased cell adhesion (By similarity). Partially colocalizes at cell junctions in a zipper-like pattern with DSP, CDH1, CTNNB1 and CTNND1 in the early stages of keratinocyte differentiation (PubMed:27375112). Moves to cell junctions at tricellular contacts as differentiation progresses and as epithelial sheet formation completes (PubMed:27375112). {ECO:0000250|UniProtKB:Q9Y446, ECO:0000269|PubMed:27375112}.
Interaction partners:
- Desmoglein-3
- Polyadenylate-binding protein 1
- Junction plakoglobin
- Desmoplakin
- Plakophilin-1
- Desmoglein-2
- Desmocollin-2
- Desmoglein-1-alpha
- RNA-binding protein FXR1
- Desmocollin-1
Sequence:
MQEGNFLLSALQPETGVCSLALPSDLQLDRRGAEGPEADRLRAARVQEQVRARLLQLGQQSRHNGSAELDGSAESARGMPRGQYHTMQTGFSSRSQGMSGDKTSTFRPIAKPAYSPASWSSRSAVDLTCSRRLSSAHNGGSAFGAVGYGGTQPTPPMPTRPVSFHERGGAASRADYDTLSLRSLRLGPGGLDDRYSVVSEQLEPAAASTYRAYAYERQASSGSSRAGGLDWPEATEGPPSRTIRAPAMRTLQRFQSSHRSRGGTGSVSGAGLEPVARAPSVRSLSLSLADSGHLPDVRGLDSYTGHRTLQRLSSGFDDIDLPSAVKYLMASDPNLQVLGAAYIQHRCYSDAAAKKQARSLQAVPRLVKLFNHANQEVQRHATGAMRNLIYDNVDNKLALVEENGIFELLRTLREQDDELRKNVTGILWNLSSSDHLKDRLARDTLEQLTDLVLSPLSGAGGPPLIQQNASEAEIFYNATGFLRNLSSASQATRQKMRECHGLVDALVTYINHALDVGKCEDKSVENAVCVLRNLSYRLYDEMPPSALQRLEGRGRRDMAGAPPGEMVGCFTPQSRRLRELPLTADALTFAEVSKDPKGLEWLWSPQIVGLYNRLLQRCELNRHTTEAAAGALQNITAGDRRWAGVLSRLALEQERILNPLLDRVRTADHNQLRSLTGLIRNLSRNARNKDEMSTKVVSHLIEKLPGSVGEKCPPAEVLVNIIAVLNNLVVASPIAARDLLYFDGLRKLVFIKKKRDSPDSEKSSRAASSLLANLWQYSKLHRDFRAKGYRKEDFLGP
Protein: XPC complex subunit, DNA damage recognition and repair factor (E7EUB5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARKRAAGGEPRGRELRSQKSKAKSKARHAFEDEKPPKKSLLSKVSQGKRKRGCSHPGGSADGPAKKKVAKVTVKSENLKVIKDEALSDGDDLRDFPSDLKKAHHLKRGATMNEDSNEEEEESENDWEEVEELSEPVLGDVRESTAFSRSLLPVKPVEIEIETPEQAK