wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 106 (Zfp-106) (Zinc finger protein 474) (Q9H2Y7)
Organism: Homo sapiens (Human)
Function: RNA-binding protein. Specifically binds to 5'-GGGGCC-3' sequence repeats in RNA. Essential for maintenance of peripheral motor neuron and skeletal muscle function. Required for normal expression and/or alternative splicing of a number of genes in spinal cord and skeletal muscle, including the neurite outgrowth inhibitor RTN4. Also contributes to normal mitochondrial respiratory function in motor neurons, via an unknown mechanism.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:O88466}. Nucleus speckle {ECO:0000250|UniProtKB:O88466}. Note=Colocalizes with RBM39 in nuclear speckles. Inhibition of RNA synthesis, or overexpression of KNOP1, induces translocation from nuclear speckles to the nucleolus. {ECO:0000250|UniProtKB:O88466}.
Interaction partners:
- Zinc finger protein 91
- Lysine-rich nucleolar protein 1
Sequence:
MPVGRIECPSSPSFPRDISHECRVCGVTEVGLSAYAKHISGQLHKDNVDAQEREDDGKGEEEEEDYFDKELIQLIKQRKEQSRQDEPSNSNQEINSDDRRPQWRREDRIPYQDRESYSQPAWHHRGPPQRDWKWEKDGFNNTRKNSFPHSLRNGGGPRGRSGWHKGVAGGSSTWFHNHSNSGGGWLSNSGAVDWNHNGTGRNSSWLSEGTGGFSSWHMNNSNGNWKSSVRSTNNWNYSGPGDKFQPGRNRNSNCQMEDMTMLWNKKSNKSNKYSHDRYNWQRQENDKLGTVATYRGPSEGFTSDKFPSEGLLDFNFEQLESQTTKQADTATSKVSGKNGSAAREKPRRWTPYPSQKTLDLQSGLKDITGNKSEMIEKPLFDFSLITTGIQEPQTDETRNSPTQKTQKEIHTGSLNHKASSDSAASFEVVRQCPTAEKPEQEHTPNKMPSLKSPLLPCPATKSLSQKQDPKNISKNTKTNFFSPGEHSNPSNKPTVEDNHGPYISKLRSSCPHVLKGNKSTFGSQKQSGDNLNDTLRKAKEVLQCHESLQNPLLSTSKSTRNYAKASRNVEESEKGSLKIEFQVHALEDESDGETSDTEKHGTKIGTLGSATTELLSGSTRTADEKEEDDRILKTSRELSTSPCNPIVRQKESELQMTSAASPHPGLLLDLKTSLEDAQVDDSIKSHVSYETEGFESASLDAELQKSDISQPSGPLLPELSKLGFPASLQRDLTRHISLKSKTGVHLPEPNLNSARRIRNISGHRKSETEKESGLKPTLRQILNASRRNVNWEQVIQQVTKKKQELGKGLPRFGIEMVPLVQNEQEALDLDGEPDLSSLEGFQWEGVSISSSPGLARKRSLSESSVIMDRAPSVYSFFSEEGTGKENEPQQMVSPSNSLRAGQSQKATMHLKQEVTPRAASLRTGERAENVATQRRHSAQLSSDHIIPLMHLAKDLNSQERSIPPSENQNSQESNGEGNCLSSSASSALAISSLADAATDSSCTSGAEQNDGQSIRKKRRATGDGSSPELPSLERKNKRRKIKGKKERSQVDQLLNISLREEELSKSLQCMDNNLLQARAALQTAYVEVQRLLMLKQQITMEMSALRTHRIQILQGLQETYEPSEHPDQVPCSLTRERRNSRSQTSIDAALLPTPFFPLFLEPPSSHVSPSPTGASLQITTSPTFQTHGSVPAPDSSVQIKQEPMSPEQDENVNAVPPSSACNVSKELLEANREISDSCPVYPVITARLSLPESTESFHEPSQELKFSVEQRNTRNRENSPSSQSAGLSSINKEGEEPTKGNSGSEACTSSFLRLSFASETPLEKEPHSPADQPEQQAESTLTSAETRGSKKKKKLRKKKSLRAAHVPENSDTEQDVLTVKPVRKVKAGKLIKGGKVTTSTWEDSRTGREQESVRDEPDSDSSLEVLEIPNPQLEVVAIDSSESGEEKPDSPSKKDIWNSTEQNPLETSRSGCDEVSSTSEIGTRYKDGIPVSVAETQTVISSIKGSKNSSEISSEPGDDDEPTEGSFEGHQAAVNAIQIFGNLLYTCSADKTVRVYNLVSRKCIGVFEGHTSKVNCLLVTQTSGKNAALYTGSSDHTIRCYNVKSRECVEQLQLEDRVLCLHSRWRILYAGLANGTVVTFNIKNNKRLEIFECHGPRAVSCLATAQEGARKLLVVGSYDCTISVRDARNGLLLRTLEGHSKTILCMKVVNDLVFSGSSDQSVHAHNIHTGELVRIYKGHNHAVTVVNILGKVMVTACLDKFVRVYELQSHDRLQVYGGHKDMIMCMTIHKSMIYTGCYDGSIQAVRLNLMQNYRCWWHGCSLIFGVVDHLKQHLLTDHTNPNFQTLKCRWKNCDAFFTARKGSKQDAAGHIERHAEDDSKIDS
Protein: Inositol 1,4,5-trisphosphate receptor-interacting protein (Q3TNL8)
Organism: Mus musculus (Mouse)
Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8IWB1}; Single-pass type I membrane protein {ECO:0000255}. Nucleus outer membrane {ECO:0000269|PubMed:31142202}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Ubiquinone biosynthesis protein COQ9
Sequence:
MAMELFRVCLVVVTAIINHPLLFPRENATIPENEEEIIRKMQEHQEKLRLEQLRLEEEVSRLEAEKEALRQVEEEQQQLEAHTAWDLWTTLCMVLFLIIEVLRQNHQEGTFPECLGGDEDELSGLGGTLLQGLPLPNRATLDHFYEHCIRSTTGDATRTQEFVEGFVDDLLEALRSTYNGKTDMELEDFIGVGSMYENWQVERPLRCHLFIPFIPPEPYSFHPEFWCSSLSTPLERQGYGQIKVTLADGNPLGCVCGKAKLEEDMLCLLYGKNRGAWPSSAGCGEMEGLLCSRESSYLDVMQVMKWFQMALTRAWHRIAHKYEFDLAFGELDTPGSLKIKFRSGKSMPFILTPVIQCNDSDLYFILQLPKEPCGGGPASSAHWLLSFAVYEREFLRMTGKALPEGACHLSCLQIASFLLSKQTRLTGPSGLSDYHLKTALLHLLLSRQASDWKASKLDVRLQDLFCFLERSLLEKKLYHFFMGNHKVPEALGLPEVVRRAEPLNLFRPFVLQRTLYRNTVDSFYEMLKNAPALISEYSLHVPSVRASPPPKAVVS
Protein: EF-hand domain-containing protein (Q384L3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQPIERAEELLAHEREKIGLFRMPFRTLQLSCAYCVKTVTSYVVKCIKSSAFMFVLPVILLVVGVSTFLIDSPAGRAFRFLDADGDGYVSVAEVEGYFRDKLNRKLGAGRGANSIFPSGTARLDKSKFTSWWVEGYGDAVRQNAFFNQGPWREAEYMLADALWWLGLGILSSIGLGTGMHSGLLFLFPYIYQLCAAVDSCGNTNFWTYPVNPIYGPRDRVFACLNPQKKDVPTSVLTRVLMLLPACFIWGVGTAIGEIPPYLLSYTAARQGKRNSELDEASRYDILNKMKAWMLEKIQRYGFVAVLLLAAWPNMAFDLCGMACGQFLMPFWTFFGATLIGKAFCKITLQAVFFVHLFSGDNVERLIHRVGDVIAAVVVIPSSVYSGGTQGLVKKAVEAVVRARQSIALRARGEATVGEGMQSASLLATIFGWVVVAAIAFFAKSVVETFAQNEQQQYDKIVLEYIGKALARGRSKKSVTDEELLQLIEESQRLCVEPEHLMSFNHETLVTYVCVVVAGFVMVHYSAVAGLSLLFHMFVCMVHNNESLHPVTLWLLRLLFASAALYTLCGLETL
Protein: Uncharacterized protein (Q57WU9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNEAVVSVGGVRKVLNTLQRKHQWLINDARLFYIGGQWHGTVQSLIVEHLSRCRELKRPLVQHEHVGNVLHPLRLEDEYSRKERFLQSLFDEADFNVSADPLFYLFSGSCCNIGVQEPVGNNFSKACELPLTVNEAAAHVRRHTAHQSMSDRFPSSVEPHLLEGGLSDKSAVVCTPVVFLRELFHSCAADVVALDFSGPHEMGMFPQNSVSTVSVLQDVRDAMTLSSYLLKPSGALLLRFPLCMVSREKGSFLRLMKCLTWGFQVSRRCVDGEYIYCLGCRKVAEYPAAVEHRLRPSRRAGGAEKGTGRRNFRNNVKRSYFAALMPSFTNAAFVKEPMEGSAPRDSGPARNAKMDEEAFFAVSVEMMEKGLYNHKPDE
Protein: Phospholipid scramblase (I3L161)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEVQAPPGTTIGHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQWGGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIVSWLPLPPPPACPLLSFEALCISWPLARGKSGIGVVGVEVLELACDSQAGLAQPDLPLTVAS
Protein: Alkaline ceramidase TOD1 (EC 3.5.1.23) (Protein TURGOR REGULATION DEFECT 1) (Q6DBD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Endoplasmic reticulum ceramidase that catalyzes the hydrolysis of ceramides into sphingosine and free fatty acids at alkaline pH (e.g. pH 9.5). Inactive on phytoceramide. Involved in the regulation of turgor pressure in guard cells and pollen tubes.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:25591940}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Alkaline ceramidase
- Probable galacturonosyltransferase 13
- Aminopeptidase M1
- O-fucosyltransferase 1
Sequence:
MGKFITTTLSPPLYARSKLLCFSLLYLFSTIFLFLYVSLSRNQCIFRYSPFDPIQAKLFSYPSSYGEHKYALPTHRSSCSSPIFFSDYWTVLKEIQSILSGSSPKENLRYINGKSESFGGNFSTQKRFSYFNHSNIDVEVPCGFFRDFPVSNSDRVEMEKCGLVVASAIFNDHDKIRQPVGLGVKTLETVCFYMFIDDKTLNSLFHHNVILKNNPSDYRVGAWRIIKISKSENLYLNPAMNGVIPKYLIHRLFPNSKFSIWVDAKIQLMIDPLLLIHSMLVVPEVDMAISKHPFFVNTMEEAMATARWKKWGDVDGLRIQMETYCEHGLKPWSSSKLPYPTDVPDTALILRRHGIRSNLFSCFMFNELEAFNPRDQLAFAFVRDHINPKVKMNMFEVEVFEQVVVEYRHNLKKIESSTYEEQEEEQKQESLRTIQKRRKWLDHESWSLNRSSCKNYLTDMWG
Protein: Nuclear transmembrane protein (Q38BN5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEGFRYFTQRVPQSLWNPVAMKHAFIIALVVAPLWAFLLKPLLEKYHQQSEPLHLFLWALLRGVVMQFPILTSVKLRAQAEPKPSRGRERPSGHTPELGSAKRYATGGKPITAKALDDLFRSPDFEVWYGQHRQSLLEKVRIRCSQQLWASIATLAVLVFGAFALPLFSFSNEEKTLYAVLRPFLTVPTFKVSIFTSGKDKKEIMYSVIAQLTALGHAVVVLVAAFALFTTSFMPVGLKQTAAAALVAFLALVAEATRVEQMAVGAGFVLLFAPVAWRIASVFV
Protein: Tumor necrosis factor alpha-induced protein 8 (D6RCM8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSKQPRLLLLCKVATDVFNSKNLAVQAQKKILGKMVSKSIATTLIDDTSSEVLDELYRVTREYTQNKKEAEKIIKNLIKTVIKLAILYRNNQFNQDELALMEKFKKKVHQLAMTVVSFHQVDYTFDRNVLSRLLNECREMLHQIIQRHLTAKSHGRVNNVFDHFSDCEFLAALYNPFGNFKPHLQKLCDGINKMLDEENI
Protein: dTTP/UTP pyrophosphatase (dTTPase/UTPase) (EC 3.6.1.9) (Maf-like protein C3G6.03c) (Nucleoside triphosphate pyrophosphatase) (Nucleotide pyrophosphatase) (Nucleotide PPase) (O14141)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ENTH domain-containing protein C794.11c
- Probable threonine--tRNA ligase, mitochondrial
Sequence:
MSNEKMDTSPPSYDSHFTLETSMHRQLKDKRIILASGSPRRKQLFEQMGFPNVETCVSGFPEDLNKSMYITPWEYAADTSVQKAIAVYEKLAAEEDSPDIVVSADTILILDSEIMEKPNDPKHHLAMLKKLRNSKTPHKVFTAVSVIVPMEVPIHPGYVMKTHLEETQVKFDPSITDEFLEAYVRCGEGSDKAGGYAIQGHGALLIESIIGDFSNVVGLPIRATFKLMEEALEQGDADNYD
Protein: LON peptidase N-terminal domain and RING finger protein 1 (RING finger protein 191) (Q17RB8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSPAVARTSPGGSREMAPAPQGRGRFWEVGGGSGHRLERAAAESERWELLLRRGELLALGGHLKGALEAFAAALRRGAPARPECLGALVDCLVFNYRLRHGLGWSAAPVAGADGGAGGLLRCLGCRGFLSEPVTVPCGHSYCRRCLRRELRARCRLCRDRLPPATASATDAEGTAPRPPPLAAAIAASDFRTSVVLNHLAEKWFPGQRERARAAGRLGELLHQGRYREALAAACEALRAEPSDLIVKIYRAESYAGLQEFKAAIEDLNAVLFQLPDWPEVYFRKGKVLCDAGFLGDALQLFLQCLALDEDFAPAKLQVQKILCDLLLPENLKEGLKESSWSSLPCTKNRPFDFHSVMEESQSLNEPSPKQSEEIPEVTSEPVKGSLNRAQSAQSINSTEMPAREDCLKRVSSEPVLSVQEKGVLLKRKLSLLEQDVIVNEDGRNKLKKQGETPNEVCMFSLAYGDIPEELIDVSDFECSLCMRLFFEPVTTPCGHSFCKNCLERCLDHAPYCPLCKESLKEYLADRRYCVTQLLEELIVKYLPDELSERKKIYDEETAELSHLTKNVPIFVCTMAYPTVPCPLHVFEPRYRLMIRRSIQTGTKQFGMCVSDTQNSFADYGCMLQIRNVHFLPDGRSVVDTVGGKRFRVLKRGMKDGYCTADIEYLEDVKVENEDEIKNLRELHDLVYSQACSWFQNLRDRFRSQILQHFGSMPEREENLQAAPNGPAWCWWLLAVLPVDPRYQLSVLSMKSLKERLTKIQHILTYFSRDQSK
Protein: Glucose-1-phosphate thymidylyltransferase (EC 2.7.7.24) (dTDP-glucose pyrophosphorylase) (Ep) (dTDP-glucose synthase) (P26393)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is the first of four enzymes commited to biosynthesis of dTDP-L-rhamnose in S.typhimurium LT2. Is also able to convert non natural substrates such as a wide array of alpha-D-hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy-alpha-D-hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars.
Interaction partners:
- dTDP-glucose 4,6-dehydratase
- dTDP-4-dehydrorhamnose reductase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- dTDP-glucose 4,6-dehydratase
- Glucose-1-phosphate cytidylyltransferase
- CDP-glucose 4,6-dehydratase
- Protein RfbI
- Lipopolysaccharide biosynthesis protein RfbH
- UTP--glucose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFIGHDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQKGTAVSLEEKPLQPKSNYAVTGLYFYDNSVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKVSCPEEIAFRKNFINAQQVIELAGPLSKNDYGKYLLKMVKGL
Protein: Heterogeneous nuclear ribonucleoprotein Q (hnRNP Q) (Glycine- and tyrosine-rich RNA-binding protein) (GRY-RBP) (NS1-associated protein 1) (Synaptotagmin-binding, cytoplasmic RNA-interacting protein) (pp68) (Q7TMK9)
Organism: Mus musculus (Mouse)
Function: Heterogeneous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1 and isoform 2 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences (By similarity). Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself (By similarity). May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity). Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 2 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins.
Subcellular location: Nucleus {ECO:0000269|PubMed:10734137, ECO:0000269|PubMed:11994298}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O43390}. Microsome {ECO:0000269|PubMed:11994298}. Cytoplasm {ECO:0000269|PubMed:10734137}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). Isoforms 1 and 2 are expressed predominantly in the nucleoplasm. According to PubMed:10734137, isoform 2 is predominantly found in cytoplasm. The tyrosine phosphorylated form bound to RNA is found in microsomes. {ECO:0000250|UniProtKB:O43390, ECO:0000269|PubMed:10734137}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Large ribosomal subunit protein uL13
- Glyceraldehyde-3-phosphate dehydrogenase
- Y-box-binding protein 1
- Heterogeneous nuclear ribonucleoprotein U
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- ATP-dependent RNA helicase A
- Polyadenylate-binding protein-interacting protein 1
- Heterogeneous nuclear ribonucleoprotein D0
Sequence:
MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKSFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPDQKRKERKAQRQAAKNQMYDDYYYYGPPHMPPPTRGRGRGGRGGYGYPPDYYGYEDYYDYYGYDYHNYRGGYEDPYYGYEDFQVGARGRGGRGARGAAPSRGRGAAPPRGRAGYSQRGGPGSARGVRGARGGAQQQRGRGVRGARGGRGGNVGGKRKADGYNQPDTKRRQTNNQNWGSQPIAQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK
Protein: N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 1 (NGalNAc-T1) (EC 2.4.1.244) (Beta-1,4-N-acetylgalactosaminyltransferase IV) (Beta4GalNAc-T4) (Beta4GalNAcT4) (Q76KP1)
Organism: Homo sapiens (Human)
Function: Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Carbohydrate sulfotransferase 9
- Carbohydrate sulfotransferase 8
- Alpha-
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-N-acetylgalactosaminyltransferase 3
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 3
- Protein-glucosylgalactosylhydroxylysine glucosidase
Sequence:
MPRLPVKKIRKQMKLLLLLLLLSCAAWLTYVHLGLVRQGRALRQRLGYGRDGEKLTSETDGRGVHAAPSTQRAEDSSESREEEQAPEGRDLDMLFPGGAGRLPLNFTHQTPPWREEYKGQVNLHVFEDWCGGAVGHLRRNLHFPLFPHTRTTVKKLAVSPKWKNYGLRIFGFIHPARDGDVQFSVASDDNSEFWLSLDESPAAAQLVAFVGKTGSEWTAPGEFTKFSSQVSKPRRLMASRRYYFELLHKQDDRGSDHVEVGWRAFLPGLKFEVISSAHISLYTDESALKMDHVAHVPQSPASHVGGRPPQEETSADMLRPDPRDTFFLTPRMESSSLENVLEPCAYAPTYVVKDFPIARYQGLQFVYLSFVYPNDYTRLTHMETDNKCFYRESPLYLERFGFYKYMKMDKEEGDEDEEDEVQRRAFLFLNPDDFLDDEDEGELLDSLEPTEAAPPRSGPQSPAPAAPAQPGATLAPPTPPRPRDGGTPRHSRALSWAARAARPLPLFLGRAPPPRPAVEQPPPKVYVTRVRPGQRASPRAPAPRAPWPPFPGVFLHPRPLPRVQLRAPPRPPRPHGRRTGGPQATQPRPPARAQATQGGREGQARTLGPAAPTVDSNLSSEARPVTSFLSLSQVSGPQLPGEGEEEEEGEDDGAPGDEAASEDSEEAAGPALGRWREDAIDWQRTFSVGAVDFELLRSDWNDLRCNVSGNLQLPEAEAVDVTAQYMERLNARHGGRFALLRIVNVEKRRDSARGSRFLLELELQERGGGRLRLSEYVFLRLPGARVGDADGESPEPAPAASVRPDGRPELCRPLRLAWRQDVMVHFIVPVKNQARWVAQFLADMAALHARTGDSRFSVVLVDFESEDMDVERALRAARLPRYQYLRRTGNFERSAGLQAGVDAVEDASSIVFLCDLHIHFPPNILDGIRKHCVEGRLAFAPVVMRLSCGSSPRDPHGYWEVNGFGLFGIYKSDFDRVGGMNTEEFRDQWGGEDWELLDRVLQAGLEVERLRLRNFYHHYHSKRGMWSVRSRKGSRTGAS
Protein: Decorin (Bone proteoglycan II) (Dermatan sulfate proteoglycan-II) (DSPG) (PG-S2) (PG40) (Q01129)
Organism: Rattus norvegicus (Rat)
Function: May affect the rate of fibrils formation (By similarity). May be implicated in the dilatation of the rat cervix.
Subcellular location: Secreted, extracellular space, extracellular matrix. Secreted {ECO:0000250|UniProtKB:P07585}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Receptor protein-tyrosine kinase
- Toll-like receptor 4
- Y-box-binding protein 3
- Y-box-binding protein 1
- Y box binding protein 1, pseudogene 20
- Insulin-like growth factor 1
- Toll-like receptor 2
- Biglycan
- Transforming growth factor beta-2 proprotein
Sequence:
MKATLVLFLLAQVSWAGPFEQRGLFDFMLEDEASGIIPYDPDNPLISMCPYRCQCHLRVVQCSDLGLDKVPWEFPPDTTLLDLQNNKITEIKEGAFKNLKDLHTLILVNNKISKISPEAFKPLVKLERLYLSKNHLKELPEKLPKTLQELRLHDNEITKLKKSVFNGLNRMIVIELGGNPLKNSGIENGALQGMKGLGYIRISDTNITAIPQGLPTSISELHLDGNKIAKVDAASLKGMSNLSKLGLSFNSITVVENGSLANVPHLRELHLDNNKLLRVPAGLAQHKYVQVVYLHNNNISEVGQHDFCLPSYQTRKTSYTAVSLYSNPVRYWQIHPHTFRCVFGRSTIQLGNYK
Protein: Protein BASIC PENTACYSTEINE4 (AtBPC4) (Q8S8C6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that specifically binds to GA-rich elements (GAGA-repeats) present in regulatory sequences of genes involved in developmental processes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- RNA exonuclease 4
Sequence:
MENGGQYDNARFKPDYFKGAQSMWNMIPQHQIKEQHNALVMNKKIMSILAERDAAVHERNQAVSAKKEAVAARDEALQQRDKALSERDKALIERDNAYAALQHHENSLNFALSGGKCVDGDDCFGIGEPHKLEVFPLSTIPPEVTNTKVVNKRKKENKQGLSKVKKVGEDLNRRVPAPGKKSRTDWDSQDVGLNLVTFDETTMPVPMCSCTGSTRQCYKWGNGGWQSSCCTTTLSQYPLPQMPNKRHSRMGGRKMSGNVFSRLLSRLSAEGYDLSCPVDLKDYWARHGTNRYITIK
Protein: Transcriptional regulatory protein ComA (Competence protein A) (P14204)
Organism: Bacillus subtilis (strain 168)
Function: Response regulator in the two-component regulatory system ComP/ComA involved in a major quorum response pathway that regulates the development of genetic competence. Regulates directly the expression of over 20 genes, including genes of the srfA operon, degQ, rapA, rapC, rapE, rapF, etc. Regulates indirectly, through the regulation of comK transcription, the expression of late competence genes.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Regulatory protein RapF
- Sensor histidine kinase ComP
- Regulatory protein RapC
- Regulatory protein RapG
- Response regulator aspartate phosphatase H
- Regulatory protein RapK
- Sensor histidine kinase YhcY
- Putative esterase ComA2
- Tryptophan prenyltransferase ComQ
- Sensor histidine kinase LiaS
Sequence:
MKKILVIDDHPAVMEGTKTILETDSNLSVDCLSPEPSEQFIKQHDFSSYDLILMDLNLGGEVNGMELSKQILQENPHCKIIVYTGYEVEDYFEEAIRAGLHGAISKTESKEKITQYIYHVLNGEILVDFAYFKQLMTQQKTKPAPSSQKEQDVLTPRECLILQEVEKGFTNQEIADALHLSKRSIEYSLTSIFNKLNVGSRTEAVLIAKSDGVL
Protein: Azurin (Q9F646)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Transfers electrons from cytochrome c551 to cytochrome oxidase.
Subcellular location: Periplasm {ECO:0000250|UniProtKB:P34097}.
Interaction partners:
Sequence:
MFAKAVAVSLLTLASAQVFAADCKVTVDSTDQMSFNTKAIEIDKSCKTFTVELTHSGNLPKNVMGHNLVISKEADMQPIATDGLSAGIDKDYLKEGDDRVIAHTKVIGAGEKDSVTFDVSKLKADEKYGFFCSFPGHISMMKGTVTLK
Protein: Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (Digs into agar protein 4) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser) synthetase) (P38705)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the attachment of serine to tRNA(Ser) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Arginine--tRNA ligase, mitochondrial
- Arginine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, mitochondrial
- Tryptophan--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Cysteine--tRNA ligase
- Tryptophan--tRNA ligase, cytoplasmic
- Peroxisomal protein PEX21
- Tyrosine--tRNA ligase, mitochondrial
Sequence:
MIIRRLFSISNRSFFLKKPQFDVKKIIEMIPQYQTSIQNRELIEADSIIRSLQLLGERYQNIKEIDKVIADIQIQRKSIEAQIKKDKTKITEYSAALKALKEQYNDQNSKSSELKKKILETCKSLPNTLDPTVPLDAPQIEQWINPLKTHKTSEAQAHVDIMLKKNMLDLQTASNVTGMSWYYLLNDGARLEQALVAYALKKANENGFSSCVPPSITKKELIDACGFNPRDMNNERQIYALQDTNLGLVATAEIPLAGLGANKVLELNSGECSKKLVGVSRCYRAEAGARGKDTKGLYRVHEFTKVELFCWSKPETSAKVLEEIKQFQISVVEELGIPAKVLNMPSNDLGNPAFKKYDIEAWMPGRGKFGEISSASNCTDFQSRRLNTKYRDDNTGKLEYVHTLNGTAMAIPRVIVALVENFYDPSTGKISVPECLREFMNGQRYI
Protein: GH22837p (Neyo, isoform A) (Neyo, isoform B) (Q9VAG2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 20-hydroxyecdysone protein
Sequence:
MAKINLLRHLFLALMLYSAATAKEHLRIRRQAAESVTAAAPNASKVMASEEIKDKTEWPGAKETSTEINRTERPVENVETRNSGFDLPAASDLSSSLGSEEDSIYYDNAPVDCNPELVGFEIVTGYVFSAPEKLMDSQPGTLMLTDCLDTCRKNKTCQSVNYETGLCVLFSAHADQLPGALTKSQFPVFTIYAQKSCLAVKPCSRAWYVDRVQNYKLKTEVKRTVSVASRRECFELCLGENDFTCRSANYDRTSGACELSELDRLTLAGSQAFQVNDGSDYLENHCVDEPNKLCEFKRLPGRILKTVDSVYQEVSSIDECRELCLNSPYRCHSYDYNDTGDMVCRLSHHSRATLADVQEPFLEVPEASTYELTSCYNVTIECGGGDMLARIRTSKLFNGKVYAKGSPKSCSVDVKSALDFELRMNYHDLECNVRQSTAGRYVNDIIIQHHDMIVTSSDLGLALACQYDLTNKSVSNGVDLDVRGDIMPALSEEVIVESPNVIMRITSRDGSDMMRSAEVGDPLALKFEIVDEQSPYEIFIRELVAMDGVDNSEITLIDSNGCPTDHFIMGPIYKGSVSGKMLLSNFDAFKFPSSEVVQFRALVTPCMPSCEPVQCEQEDTSGEFRSLLSYGRKRRSLNTTDDHPRPRRDIDTSKKSAPSDMLLVQSIQITDKFGFKQDKQESGDFYDGNETTFTANEEGHGFCVNAIGLITAATIFLLTQLAVIAIWTYCYQRRQKLQPYQHSY
Protein: LIM domain-containing protein unc-95 (Q9NEZ5)
Organism: Caenorhabditis elegans
Function: Required for the assembly and integrity of muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix. Decreased localization of unc-95 to dense bodies and their subsequent dissociation plays an important role in ecdysis during molting. Involved in the organization of the muscle sarcomeric structure and thereby required for locomotion.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}. Nucleus {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}. Cell membrane {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:15210732}. Cell junction {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}. Cell junction, focal adhesion {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}. Note=Localized in the cytoplasm in comma stage embryos, and gradually becomes more localized at the membrane in the 1.5- and 2-fold stage embryos. In the threefold embryo, associated with dense bodies at the cell membrane, but also present in the cytoplasm. Nuclear localization from the threefold stage embryo as well. In adult animals, localized in dense bodies, M-lines, muscle-muscle cell boundaries, cytoplasm and nucleus (PubMed:15210732). Decreased localization to dense bodies during the L2/L3 molt (PubMed:20385102). {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}.
Interaction partners:
- Zinc finger protein unc-98
- Paralyzed arrest at two-fold protein 6
- LIM domain-containing protein unc-97
- CRE-UNC-96 protein
- Vinculin
- Protein unc-112
- Protein vav
- Muscle M-line assembly protein unc-89
- Zyxin
- Myosin-3
Sequence:
MTISPQPSHQQFESYQWTTESRSSQQRHGTGTPSQDGRLSAIPDPVERHVARWRSESRNSNKDKVFRNDEEFSQQDEIVNGTLTALKNDVEQTTEIIRRKQEQMRMERRQFQTEMEVNGRISIDPTDDWLAARLKAVSSDDMNQQLVKLKQDQRQNAVTDTLAALVYDVNATTEVLRRGQRGRDGEDGNKKKKEEIEYTLRLTPAPEEQIPQRPKIPEDDNMETDDYSRQYGVQMSEETDSLRRRRARSTTPRRTLHISGSPPPPAAAVCAYCSEEIDGAILTALAPNSERAQKFHTYHFMCTYCQKALNMHGTYREHDLKPYCHDCFYKLYNGLQYAPDDHQASIEKLI
Protein: DNA replication complex GINS protein PSF3 (A0A0S2Z5L4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367161}.
Interaction partners:
Sequence:
MSEAYFRVESGALGPEENFLSLDDILMSHEKLPVRTETAMPRLGAFFLERSAGAETDNAVPQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLFQTGQKGLNDFQCWEKGQASQITASNLVQNYKKRKFTDMED