wanglab/gogpt-training-data huggingface dataset:
Protein: Trifunctional purine biosynthetic protein adenosine-3 [Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (GARS) (Phosphoribosylglycinamide synthetase); Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase); Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART)] (P21872)
Organism: Gallus gallus (Chicken)
Function: Trifunctional enzyme that catalyzes three distinct reactions as part of the 'de novo' inosine monophosphate biosynthetic pathway.
Interaction partners:
- Bifunctional purine biosynthesis protein ATIC
- Adenylosuccinate lyase
- Multifunctional protein ADE2
- Serine hydroxymethyltransferase
- Uncharacterized protein.
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Amidophosphoribosyltransferase
- Trifunctional purine biosynthetic protein adenosine-3
- Methylenetetrahydrofolate dehydrogenase
- Methylenetetrahydrofolate dehydrogenase
Sequence:
MADRVLVIGSGGREHALAWKLAQSPHVKQVFVAPGNAGTANSGKISNSAVSVSNHAALAQFCRDQEIRLVVVGPEVPLAAGIVDDLTAAGVRCFGPTARAAQLESSKSFTKSFLDRHGIPTARWKSFTDPKAACSFINSANFPALVVKASGLAAGKGVIVASNKEEACKAVNDIMQDKTFGTAGETVVVEELLEGEEVSCLCFTDGVTIAPMPPAQDHKRLKDGDEGPNTGGMGAYSPAPQISKDLLLKIRETVLQKTLDGMRKEGIPYLGVLYAGLMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVMQAVINKKLSSSMPIWYEDSAAVTVVMASEGYPGTYPKGLEITGLSKAKELGLEVFHAGTALKDGKVVTNGGRVLTVTAIKEDLMTALQEANKGVAAINFKGSIYRKDIGYRAIAFLSQSRGLTYKNSGVDIAAGNILVQKIKPLAAATSRSGCNAELGGFAGLFDLKAAGYKDPILVSGTDGVGTKLKIAQVCKKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFACGKLDVEVAQGVIAGIAEACQKAGCALLGGETAEMPGMYPPGEYDLAGFAVGAVERGQMLPQLERIADGDVVIGVASSGVHSNGYSLVRRIVEKSSLDFSSQVGVSGDQTLGDLLLTPTKIYSKTLLPVLRSGHVKAYAHITGGGLLENIPRVLPDSFGVVLDALSWKIPEIFCWLHKEGNLSEEEMARTFNCGIGAVLVVQKELAQQVLKDVQKHEAAWLIGKVVPLQKGSAHVKVHNLLQALQANRSLSVHSHIQGKIQTNKVKVAVLISGTGTNLEALINSTKKPTSFAEIVLVVSNKAGVEGLRKAERAGIPTRVIDHKQYGSRTEFDSAVDRVLEEFSVELICLAGFMRILSGPFVKKWEGKILNIHPSLLPSFKGANAHKLVLEAGVRVTGCTVHFVAEEVDAGAIIFQEAVPVKIGDTVETLSERVKEAEHRAFPAALQLVASGAVQVGEAGKICWK
Protein: Ribosome-inactivating protein lyophyllin (EC 3.2.2.22) (C0HLZ4)
Organism: Lyophyllum shimeji (Hon-shimeji) (Tricholoma shimeji)
Function: N-glycosylase that inhibits protein synthesis by depurinating ribosomal rRNA, and thus acts as a ribosomal inactivating protein (RIP). Has adenine polynucleotide glycosidase activity on the poly(A) substrate A30-ssDNA. Inhibits cell-free translation in rabbit reticulocyte lysate system with an IC(50) of 1 nM. May function in the defense response to pathogens. Displays antifungal activity against C.comatus and P.piricola, but not against R.solani, M.arachidicola and C.gossypii. Inhibits mycelial growth in P.piricola with an IC(50) of 2.5 uM. Has cytotoxic activity against the human cancer cell lines Hela, HepG2, and JAR, with IC(50) of 358.8, 489.8, and 926.9 nM respectively. It also inhibits HIV-1 reverse transcriptase activity (IC(50)=7.9 nM) and disrupts mouse embryonic development.
Interaction partners:
Sequence:
ITFQGCSPARQTVITNAITRARADVRAAVSALPTKAPVSTFSTWFGVYND
Protein: Tumor necrosis factor alpha-induced protein 8-like protein 1 (TIPE1) (TNF alpha-induced protein 8-like protein 1) (TNFAIP8-like protein 1) (Oxidative stress regulated gene-beta) (Oxy-beta) (Q8K288)
Organism: Mus musculus (Mouse)
Function: Acts as a negative regulator of mTOR activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21600655}.
Interaction partners:
Sequence:
MDTFSTKSLALQAQKKVLSKMASKAMVAVFVDNTSSEVLDELYQATKEFTRSRKEAQRVVKNLVKVAVKLAVLLRADQLDSNELAQLQRFRGRVRSLAMTALSFHQVDFTFDRRVLATGLLECRDLLHQAIGPHLTAKSHGRINHIFSHFANGDFLAALYSPAEPYRSHLCRICDGLGRMLDEGGI
Protein: Probable methyltransferase PMT28 (EC 2.1.1.-) (Q9LN50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MMERKREMGIAYFARRIKQPRGIWVKMTFIVVLGLCFVFFWSFLSSSASTFNVQRESFDDIAEPVSSRTKSAHEVSESSKLHERGKVESGSKSKEGKKVGGSSVHKHETKKKKEHAVSHPHKKKDVPKPVVEEVVVKEDQEHEEAESDDSDQSNKEDGEEGTESDGNEGESDGNGDGSVDDSSASVDEEVEEKNEEVTVNEISKKRKRKGPVFDPKAEYSWRLCNTRSKHNYMPCIDNDGLIGRLQSYRHRERSCPKKPVMCLVPLPHDGYDPPVSWPESKSKILYKNVAHPKLAAYIKKHNWVNETGEYLSFPQNQTTFNGNVLQYLEFIQEMVPDIEWGKNVRIVLDIGCSDSSFVAALLDKDVLTVSLGLKDDLVDLAQVALERGFPTFVSSLASRRLPFPSGVFDTIHCAACGVHWHSHGGKLLLEMNRILRPNGYFILSSNNDKIEDDEAMTALTASICWNILAHKTEEASEMGVRIYQKPESNDIYELRRKKNPPLCEDNENPDAAWYVPMKTCIYEIPSAIEQHGAEWPEEWPKRLETYPEWLTSKEKAMEDTNHWNAMVNKSYLTGLGIDWLHIRNVMDMTAIYGGFGASLVKQNVWVMNVVPVHSPDTLPFIYERGLLGIYHDWCEPFGTYPRSYDLLHADHLFSRLKNRCKQPASIVVEMDRLTRPGGWVVVRDKVEILEPLEEILRSLHWEIRMTYAQDKEGMLCAQKTLWRP
Protein: Dynein regulatory complex subunit 4 (Growth arrest-specific protein 8) (GAS-8) (F1QNW4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker (By similarity). Plays dual roles at both the primary (or non-motile) cilia to regulate hedgehog signaling and in motile cilia to coordinate cilia movement. Required for proper slow muscle development and positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway. Required for tether cilia motility which is essential for normal otolith formation and localization in the developing inner ear.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O95995}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:O95995}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q60779}. Golgi apparatus {ECO:0000250|UniProtKB:O95995}. Cell projection, cilium {ECO:0000250|UniProtKB:O95995}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q7XJ96}.
Interaction partners:
- Dynein regulatory complex subunit 2
- Axonemal dynein light intermediate polypeptide 1
- Dynein regulatory complex protein 1
- Dynein regulatory complex subunit 3.
- Radial spoke head component 4A.
- Dynein regulatory complex protein 9
- Protein smoothened
- Coiled-coil domain-containing protein 39
- Radial spoke head 1 homolog
- Dynein, axonemal, heavy chain 5.
Sequence:
MPPKRKSSPKGKTPTVVDGLSTEEMSKEQLEEHIMRLREELDREREERNYFQLERDKIHTFWEITRRHLEENKCELRNRERELEEVEERHQVEIKVYKQKVKHLLYEQQNMLSELKAESIISTKLLQDEHADLEKEQWKDMRSLKLELKQQELSSENVLKRIHLKHDEETTDLRNDFARQVQEIGSKYEKRMQKLRQEEELRRKTEIHEIEERKNTHINMLMKNHEKAFRDIRNYFSDIVYKNLDLITSLKEELKEMKKNEEKRNKEMAEVLEQNKELKESSQKAKEQVAELQKQLANYEKDKSILTRSRARLKMSDREMKELKWELEVLEQRFSKVQLERDELYMKFTKAILEVQQKSGFKNLLLECKLNTLNDTLEKKEAQLSEVLSASNLDPTTLSVVTHKLEEVLESKNHTIKDLQYEVARVCKAHNDLLKTSEAKLRAFGIPVEELCFEPLKSNGQSVGQGPAMFVSSSN
Protein: Ubiquitin-conjugating enzyme E2 L3 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme L3) (UbcM4) (Ubiquitin carrier protein L3) (Ubiquitin-protein ligase L3) (P68037)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P68036}. Cytoplasm {ECO:0000250|UniProtKB:P68036}.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- Polyubiquitin-C
- E3 ubiquitin-protein ligase RNF213
- E3 ubiquitin-protein ligase ARIH1
- Ubiquitin/ISG15-conjugating enzyme E2 L6
- Ubiquitin-conjugating enzyme E2 variant 1
- GDP-L-fucose synthase
Sequence:
MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD
Protein: Stabilizer of axonemal microtubules 5 (Testis-expressed protein 45) (Q8NA69)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATGALLPCSRPCPMSRLDFLKASHFSLGPDLRLHEGTMRTTSHRDFAYPAATREPPSLQPPPALLFPMDPRWDREERVSEAHRAFPPPSTPPWELLQAQARERTLAMQAGNLHLHEDAHAGIGLSNAHAAYGWPELPARTRERIRGARLIFDRDSLPPGDRDKLRIPPTTHQALFPPHDARPQPRAPSCHLGGPNTLKWDYTRQDGTSYQRQFQALPGPPALRCKRASSGVELGDCKISYGSTCSEQKQAYRPQDLPEDRYDKAQATAHIHCVNIRPGDGLFRDRTTKAEHFYAREPEPFVLHHDQTPESHILKGNWCPGPGSLDTFMQYFYGQPPPPTQPPSRHVPHEKLQSHVTLGEPKLLKRFFKTTMGSDYCPSEWRQVQKAPNLHLQQSYLPRGTGEFDFLTMNQKMLKPHRTPPAPVTEEMLQRCKYSHMEPPLGGLRFFSTQYKDEFPFKYQGPAALRLKNPQEGFVPLGTPHQRGCREKIDPLVPQPPMYLCPSQQ
Protein: Short stop/Kakapo isoform C (Q9U479)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHSSSQSTLKRTQQLVRQTNGGRGDVLSSGSEVVHSSRGPAITTNIDDSNLRYRHETKRERTVEAVITDYPGVSPLGSVPHERTNFERTVTFQDPTGNSRRLSETGALVPAGAIPTSSTHYQQVTRNKRISTEVLGSSVESTKTSQRAPNGHRRVTTHIVRKVTTLSRAEENAQPAEDLLPPAKMIRSSELEYRRALPPAIESSSTQRREISDIVVGKEDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPEDVDTNEPDEKSLITYISSLYDVFPEPPSIHPLFDMESQRRVHEYRDLAQQFIYWCREKTAYLQERSFPPTLIEMKRLLSDLQRFRSDEVSARKGEKSKLIQIYKELERYFETVGEVDVEAELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRLADKVQREIKHVDQKLTDLEARIGEEGRRIERLHPVDAKSIVEALETEIRHLEEPIQDMNQDCHVLNEGRYPHVSELHKKVNKLHQRWAQLRTNFHTNLVQKLSGLKYPVHETTVTRQTRMVVESRQIDTNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIID
Protein: Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75) (P0AF03)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor.
Interaction partners:
- Molybdopterin molybdenumtransferase
- Molybdopterin synthase catalytic subunit
- Cyclic pyranopterin monophosphate synthase
- GTP 3',8-cyclase
- Molybdenum cofactor guanylyltransferase
- Molybdenum cofactor biosynthesis protein B
- DNA-binding transcriptional dual regulator ModE
- Molybdopterin-guanine dinucleotide biosynthesis adapter protein
- Molybdopterin synthase sulfur carrier subunit
- Transaldolase B
Sequence:
MNTLRIGLVSISDRASSGVYQDKGIPALEEWLTSALTTPFELETRLIPDEQAIIEQTLCELVDEMSCHLVLTTGGTGPARRDVTPDATLAVADREMPGFGEQMRQISLHFVPTAILSRQVGVIRKQALILNLPGQPKSIKETLEGVKDAEGNVVVHGIFASVPYCIQLLEGPYVETAPEVVAAFRPKSARRDVSE
Protein: AUGMIN subunit 8 (QWRF motif-containing protein 8) (ROP1 enhancer 2) (Q9SUH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to the assembly of the acentrosomal spindle and phragmoplast microtubule arrays as part of the augmin complex.
Interaction partners:
- AUGMIN subunit 6
- AUGMIN subunit 7
- AT4g30750/T10C21_100
- Uncharacterized protein AT4g30730
- AUGMIN subunit 4
- Serine/Threonine-kinase ULK4-like protein
- Uncharacterized protein At1g01500
- AUGMIN subunit 1
- B3 domain-containing protein REM2
- FAD/NAD
Sequence:
MDVATDTTRRRLLPSDKNNAVVATRRPRTMEVSSRYRSPTPTKNGRCPSPSVTRPTVSSSSQSVAAKRAVSAERKRPSTPPSPTSPSTPIRDLSIDLPASSRRLSTGRLPESLWPSTMRSLSVSFQSDSVSVPVSKKERPVSSSSGDRTLRPSSNIAQKHKAETTSVSRKPTPERKRSPLKGKNNVSDLSENSKPVDGPHSRLIEQHRWPSRIGGKITSNSLNRSLDLGDKASRGIPTSGPGMGPSLRRMSLPLSSSSRPLHKTSSNTSSYGGLVSPTKSEDNNIARTSGAQRLLSAGSLDRATLATAVARLHPLPAPGSRPASPSRTSFLSSSSISRGMSTSRGVSPSRGLSPSRGLSPTRGLSPSRGLSPSRGTNTSCFARPSTPPSRGISPSRIRQTTTSTQSSTTTSVLSFITDVKKGKKASYIEDVHQLRLLHNRYLQWRFAIARAESVMYIQRLTSEETLFNVWHAISELQDHVTRQRIGLQQLKLEIKLNSLLNDQMVSLEDWATLERDHVSSLVGAISDLEANTLRLPATGGTKADTESLKAAMSSALDVMQAMGSSIWSLLSKVEEMNIMVTELAVVVTKESSMQGKCEDLLASTAIMQIEECSLRTHLIQTRREEGEDAETPPPLLPLSKFPWP
Protein: Diphthine methyl ester synthase (EC 2.1.1.314) (Diphthamide biosynthesis methyltransferase) (O74898)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Diphthine--ammonia ligase
- 2-
- Elongation factor 2
- Diphthamide biosynthesis protein 4
- Diphthamide biosynthesis protein 3
- Diphthine methyltransferase
- 2-
- GPI mannosyltransferase 1
Sequence:
MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILLVQKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAMLVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLHTLVLLDIKVKEQSWENLARGRKVYEPPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAEHDIGPPLHSVVLVGRDVHDLELEFLRAYAVNLENFDRVAKTYLEK
Protein: Pebble, isoform D (Q8IQ95)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MESGEKTAKGRWKLILGPPALKYAAEMKQTLGQNSRPIYNYAMRGVVTCFTGIRKKDELTKLVNLIHSMGGCIKKDLNTKTTHLICNHSGGEKYQYAKTFRLTVVRPAWVFAAWADRNSLEFDATQENFTKTHRLKAFEGQKICFFGFPVEEHQHMVDVLLENGGVCAELDDPECSHVVMPNTGAVFTSTSTSTDTNPSTLINPPESQVPGSSSASQAGEEEQRKAEHLEQAEIKKMEYSHAETDNGMSLDIDQEQKENQGIEDEDDIHFDERLFVEAADIINHGEDQLPESDEEDLEEEQKPKVEEVLKEQEVEEDVQASTPKTSKIRTSLKAATPLSSPEMDGIALDFESTTQNISPILKAIDECDLETDDLPPSENDLKRKRESFDNVSLMSVDSFALPASTKKPKLIRTGSISRTLRRSVSFVAEPLMKTLRPRRSSVADASSFVGSEAADNSICSLASSINLTLNDSIRKPVKEKLRSFCGRITRSSSRRHDRGVDGTPECTTLLDSGFKTPKAPKLRSTATPKTAKRLFGPVSGVVSALTLTNPSTPTPNPNPNTNCTATLDVNDTSIHTFAFCAAAVTPAMPPSSSSSSSSPILSTSIAVHSSVQVIKSPEESTTRRNSPAPIEEPMAMVVDEHTTLTKPEPKNNHTHILKSDWFWYTIQNGYANEMDYLFGDYLDSITNTPNTDRRDSLPISFNKRKRKRFSQRIQLEGTPLGSGKRRSSVSDAGLLSVSNSLFDCTTSPDKLESDKLLHAEPEASDATPAKKSMRFNHFMDFYTTESNYVGILDTILNLFKNKLEELAETNDPLLNKSEIKTIFGNFLPIHEVHQSMLEHLRKLHANWREDCLIGDIIIQHRDELIKAYPPYVNFFEQMKEQLQYCDREYPRFHAFLKINQTKPECGRQGLQDLMIRPVQRLPSISLLLNDILKHTTSGNADHGRLEEALKAIKQVTLHINEDKRRTESRMAIFDIFNDIEGCPAHLVSSNRSFILKCEVNELSDSLSGRGDSLVLYLFSDSIELCKRRSKGFNTAKSPSTAKTHKHLKLISLNTIRLVIDISDSPRAFGLLLRGDKEKLYTFTISDEETDKSVYVKKLCNQIAAHTCRTDADKLLICRTSQELEVDISDVNVSTLSKAFKLAAKTRLKVGRAFSFNKTPNKLKRAVSTMMTSPFGSTNSLTPASQLAQMRLASCTNINEVDDEDCASMRSSSPSTQSEMLVVPPLSVQPTRKNKAVVGRI
Protein: Tumor necrosis factor ligand 7C (A0A0U5J797)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTLSSLGGLDPDSPITSHLGQPSPKQQPLEPGEAALHSDSQDGHQMALLNFFFPDEKPYSEEESRRVRRNKRSKSNEGADGPVKNKKKGKKAGPPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKAGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVYYINFTDFASYEVVVDEKPFLQCTRSIETGKTNYNTCYTAGVCLLKARQKIAVKMVHADISINMSKHTTFFGAIRLGEAPAS
Protein: DNA polymerase epsilon catalytic subunit A (Q93WK6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein unannotated coding sequence from BAC F9L11
- Proline-rich extensin-like family protein
- AT3g10020/T22K18_16
- Proline-rich extensin-like family protein
- Proline-rich extensin-like family protein
- Metal-independent phosphoserine phosphatase
- Adenine phosphoribosyltransferase 5
- Adenine phosphoribosyltransferase 3
- Glutathione S-transferase U27
- Enoyl-CoA delta isomerase 3
Sequence:
MGSLMSGWDSRVRDPKSVRRCKSLTREEIDTFWKTKKKNEEEEHVQAFSKLVTQEGAQSQAKEKKSVDDLFENQSKSSGWWRKTYWAFLNEPREEEGRPNNYVSQFKVAHIAKIAGS
Protein: Pentatricopeptide repeat-containing protein At1g09220, mitochondrial (Q680Z7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At2g28050
- F-box/kelch-repeat protein At4g05080
- Filament-like plant protein 6
- Pentatricopeptide repeat-containing protein At1g02370
- Pentatricopeptide repeat-containing protein At1g06270
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Pentatricopeptide repeat-containing protein At1g10270
Sequence:
MFLFSSRRITSLRSYTIIKHSSCYSTLVSDGNIFSIQHFQSLMQKYESNLKIIHQLHSHFTTSGFLLLHQKQNSGKLFLFNPLLRCYSLGETPLHAYFLYDQLQRLHFLSDHNKSLPPFDSFTYLFLLKASSNPRFPSLLLGIGLHGLTLKLGFESHVYVQTALVGMYLVGGNMIDAHKVFDEMPERNPVTWNVMITGLTNLGDFEKALCFLEKMPNRTVVSWTTIIDGYARVDKPKEAILLFSRMVACDAIKPNEITILAILPAVWNLGDLKMCGSVHAYVGKRGFVPCDIRVTNSLIDAYAKCGCIQSAFKFFIEIPNGRKNLVSWTTMISAFAIHGMGKEAVSMFKDMERLGLKPNRVTMISVLNACSHGGLAEEEFLEFFNTMVNEYKITPDVKHYGCLVDMLRRKGRLEEAEKIALEIPIEEKAVVWRMLLGACSVYDDAELAERVTRKLMELERSHGGDYVLMSNIFCGTGRFLDAQRFRKQMDVRGVAKLPGHSQVT
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IFQ6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MVPPGGRQGGSGEDGIDDKDAKHLLDSIGKIVHEQVKNDAKTYKGELEGKLSLATTIGELNYTKDPCIFDYSKLINGSGSGGVTARDDPCGNGSGKGEDVSRFSDKEGAQCANSKIHGNSKGSNGGACAPLRRLHLCNKNMEKIATSTAKHDLLVDVCMAANYEAQSLIRDHPQHKRTNPDSKICTELARSFADIGDIVRGRDLYRGNKKENKQREKLEENLRKIFENIYEGLSNNGVKARYEGDKENFYQLREDWWALNRDQVWKALTCSDDLKDASYFRPTCSDRKGSCSQAKDNCRCDGSNTDQVPTYFDYVPQFLRWFEEWAEDFCRKKKKKLEKLEQQCRGVYEGKERYCSRNGFDCEKTVNARGKVRMGKGCTDCFFACNPYIDWIEKQKEQFDKQKQKYDEEIKKYTKVASSSSGGRAKRAARGGSNVNGYEKIFYKKLKDSGYESVGEFLDLLSKEEVCKNFKEKEEGKIDFKTVKSSSAKNSDDSNKTFCRTKYCQPCPLCGMKKNNNGEWEHKKKGKCTSGNLYRPIDGAIHTDINFLYSGDRHDDIEKKLNRFCDETNGDTINSVAGVSGTGVVAGSNSRSKELYQEWKCYKGKDVEKVKDGKDEDDEDYEDDYHKEVENAGGLCILENNDGKEKVNKQKTYNDFFYYWVAHMLKDSIHWKKKLEKCLKNGTKTRCKNNKCNRECGCFQKWVEQKKKKEWGKIIEHFYKQEGIPPGTHDITLEGVLKKEVLLTSLQEGYGNAEDIEHIKQLLEEEENEENEGTPGADNKNKNTIDKLLDHEEGIAKECQQKQNECPKKPPKKTPGGPDRALKPEEVDASSEDHYDEEGGEDEEEEEDKEEEGEDGEDVQDDVAEEDTAKEEGSSTTETQLPDACNIVKTLFESTKNFEDACRQKYGPKAPTSWKCVPTTGDKDGATGKSDGSICVPPRRRRLYVGKLHDWASGNTQEDGKAQPQGDTPSQPDPLLKAFVESAAVETFFLWDRYKKLNTKRQGVGAGAPQLQEEDDNDEEEENPQQELEDGTIPDDFLRQMFYTFGDYRDIFFGNNIGSGNDVEKVKPNIDKVFENSEKPTSGGHNSEQQRETWWEEYGPHIWDGMICALSYNTKDKEIIKLAHHNLTSKEIYKYNNVTFIGGFNSDKNSKTETSATKLEEFSRRPTFFRWLEEWGEDFCRKRNDKLKNVKKECRGKYPNGDKQYCSGDGHDCEKTYLKHNDMFADLNCRRCGEQCRNYKQWIEKKLEEFHKQKSIYEKEIPKLKDNYNNHHYKNFYEQIIEKNGYSSFKKFLESFNQRKVCQGNSDQTNNTDFNEPLKTFSLSTYCKTCPLNGLNCGSKECNEVKGKGATWESVLNGKSKDYRRTTGINVEMINRRGKYIEKHTQDSLFKESSLLKSVRDQKWECTFINDKMDICKLNNYNESIDMNKYTTFKVFLENWLQDFLEGYYISKRKIEICTENGENKCIKGCKGKCECVKEWLNKKSTEWKQIKERYKVHHDSKGYDIAHKVRSYFEKNESDVNKSIDNYEVLKKKDEYEDCIDSDTCGPKNNWKKKDMVSILLSELQHNMNKCKTLHDPSGKPEAQCVEPTNPLDDENPDPEDDTSTTSSRPKFCPEIPQPEPEPEPFPEEDTEQEEKEEKLPAAPDNSEQEETSKEVVPEKKMPTPPPKKPEQGPKQRKKQKRQLPTHTSILPEMLSISSFPLTVGVAFAALSYFLLKKKSKSTIDLLRVIDIPKGEYGIPTSKSKNRYIPYASDRYKGKTYIYMEGDESDDYTYIGDISSSDITSSESEYEDIDINNIYPYKSPKYKTLIDVVLEPSKRDTFNTQSDIPSDTSTNKFTDNEWNQLKQDFISNILQSTQMDLPNENIIDDFMDKGIQPNNPVLDVNMAEKPFITSIHDRDLHNGEEVTYNINFDVSKNINEITNTTDDSKYVSNNIYSGIDLINDSLNSDQHVDIYDELLKRKENEIFGTNHTKHTTTNSIAKQTHTDPILNQLDLFHKWLDRHRNMCEQWNKNKKEELLDKLKEEWNKKNNNNSDLTHTSSNIPSGENSIKNVLNTDVSIQIDMDDPKPINEFTYMDNIIDNLEKNSEPYYDIDEDDIIYFDIDDEKTPMYHNNMDNNKSNVPTKVQIEMNVINKQELFQEEFPISDIWNI
Protein: Placenta-expressed transcript 1 protein (Q6UQ28)
Organism: Homo sapiens (Human)
Function: Modulates leading keratinocyte migration and cellular adhesion to matrix proteins during a wound-healing response and promotes wound repair. May play a role during trichilemmal differentiation of the hair follicle (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Localized at the apical membrane of the most differentiated keratinocytes of the outer root sheath (ORS), clustered mainly in planar regions of the plasma membrane at the base of microvilli. {ECO:0000250}.
Interaction partners:
Sequence:
MAVFHDMLLQPLGMFLCLSLQLSSATFIRYSSTCFTFDEYYTITLDIKASSHIYESNAVYSVFVPVNDSVYAVVMKTLDENSDSAGLWQRADKNCYSNSTYYVKDQYMTVLEAQWQAPEPENITEVEIQAFTVQIRALPILSTLKLREKLSTLALAAKIPQSSAFKPFFMITPKSIRLEGLANQVFSSPITEAIYILLAFLTSTLLF
Protein: Netrin receptor UNC5 (A9JR35)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU367033}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU367033}.
Interaction partners:
Sequence:
MLSTCIHRDQSPASLLGLLLLSSTLVIHADGSDYSEVLPDSFPSAPAEPLPEFQSEPEDAFIVKNRPVKLSCKAAPATQIYFKCNGEWVNQNDHVTKESLDHITGLVVREVDISVSRTQVEELFGLEDYWCQCVAWSSAGTTKSRRAYVRIAYLRKNFEQEPLGREVRLEQEVLLQCRPPEGSPPAEVDWLKNEELIDPALDSNFLITIEHDLIIKQARLSDTANYTCVARNVVAKRRSSTATLIVYVSGGWSSWTEWSECNAQCGRGWQRRTRSCTNPAPLNGGAFCDGPPFQRVTCTTLCPVDGGWTEWAKWSACGTECTHWRSRECQAPPPRNGGRHCSGSMMESKNCTEGLCARNKKVSVEHTSHPLGSGTGVAVYAGLVGALLLCVILVLCVGILVYRRSCRHLHGEITDSSSALTAAFHPGNYKPPRQDNPHLLHPTAPPDLTASAGTFRGPLFSLQQATLDSHHKIPMTTSPLLDPLPSLKIKVYNSSTMSSLELPTGLGSVDGEIMSLKTVGSGPKDHHGHTLPREPSHSASATLGSLGGRLTIPNTGVGLLVPPGTIPQGKFYEMYLIINKWEKTTLPSDGSQTVLSPVVSCGPSGMLLSRPVVLTLPHCAQLEPPDWTLTLKMQNHQGAWEEVLTVGEESLSSPCYLQVEEQSCHILMEQLGTYGLVGQSAPPRPACKRLQLALFAPRAPCLSLDYSLRVYCIQDTPHALKEVLEVERSLGGVLLEDPKPLLFKDSYHNLRLSIHDIPHSHWRSKLLAKYQEIPFYHIWSGSQRPLHCTFSLERGSLVVSQLTCKICVRQVEGEGQIFQLNTDIQETLPPHSPLPAGGSCLPSSQVGPYAFRLPVSIRQKICASLDAPSARGCDWRMLARSLAFDRYLNYFATKPSPTGVLLDLWEACHQGDADLVSLATALEEMGKSEVLVVMTTDGDC
Protein: Leucine-rich repeat protein (LRRP), putative (Q57TQ8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- adenylate cyclase
Sequence:
MVKISWVTECPVREEVGCPQCLMKCAVPIEVLPCEHVLCSTCYRDLSVCPLCDISVCSRRPAFRYELDNTRFARCRRRSSVATTFIGSEDCSGSVDPVKLTKRMGGKVPSKIYEQVLKAEESNWTVMDLENCVDLSRIRALSGVPTLEEVNLSGYSKLKTDLEHIMTLSNLRKLTLDNTELDDECVVEISSNRILLHLSCNNCHHITDISPVAEIKTLEELSLSGCKNIKKGLEHICALPNVRKLSLRGTAANDACILSLSGSTHLADLDCSECMNISDIKALGKISPLEVLSLEKCINMKEGLEELAAIPNLRELNLASTCIDDECVIKVSTFKQLVHLNCENCLAVTDIQPLAKMKTLEYLSIGGSRNIEVGVRQVCGNPKLTGLNLGGVVVRDVDVMFLREFEGFVTLNLSGCARMKGLYALDGCTRLRTLILRGCKNVKDITLLRECKDITTLDFTGCISLSDLRPLRNCGSLKMLNLSECARLKHLTGVEECKKLATVEMIDCKTLEDISALRGCTNLETLNLCNCGGNPDLSVLGACKNLKTLRLTGSSKIDDFSMLSGCSNLMTVELNDCVSLREVWLNGCECRNLTNLYLSNCENITDLWLDGCGNLRTLDLRNCTRLWYIHGQRDCRGLLTLDLRNCGTIRNGIVEFMNLPRLCVLYIDDNNADRNLVEGLMDRGVDVEVTDETHACYVKRMDDEYM