wanglab/gogpt-training-data huggingface dataset:
Protein: Protein SQS1 (Squelch of splicing suppression protein 1) (P53866)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in splicing since overexpression antagonizes the suppression of splicing defects by SPP382 mutants.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Nucleolar protein 19
- rRNA biogenesis protein RRP36
- U3 small nucleolar RNA-associated protein 22
- Ribosome biogenesis protein SLX9
- U3 small nucleolar ribonucleoprotein protein IMP3
- U3 small nucleolar RNA-associated protein 6
- Essential nuclear protein 1
- ATP-dependent RNA helicase HAS1
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43
- Nucleolar complex protein 14
Sequence:
MAKRHSHYQGSRRRHARGSNSKKAGRGNAKGIQGRKIKKKPTPTNSWHNSSIPLGEGDLDDVGADFNPGRAFISPKTIEDYYFGRDAKSRSMKMGGLRPGNRYDSSTDLQAGRAAFRKRPMQFVKAKEVYDPSHNMIQKLRAKNETKNSEEIVEREADVFEEPGKMTSDVEYINNEDSENEDDDSQNSPSTDHSLSSNESKVEDGDLFFVDEEAQQSPDLTKIKRVCIEEIARPREVAIEFDPILTIGKVELSVSEGNESKEISVDVPNKGNKTYHPFAGYISNVLHGMHTSDSDNDELDYEIETENNSEPLYESSASSEVDQGFNYVGQRHNSRADNNLLPSPSPQLTEDIKCLSINGTKTFEGNNDNLPSPASEELEFGFKEEDFVINTNDIVVSNIRMGGVDNSYYLRCYRLLGDYDFHWIDQDLLTDFVVDELGLPEDRLPAYLNFIKNSLIPKIEPAEPTYSDIPISDSSDEGDSYEGDSYEDDEDMASSVVHSDIEEGLDDLIAYTLKHDTERFKTFETKSLETKGKGKKKKLLIDDALALDTETLETLQSKFSKRIETKAKKRKAKEDFIDQENRNSNDMLKKYPYGLHIQNIKDEFESFLSRNNDRLTFPPLDPHGNKTVMKIAKHYNMKSSKIGKANHTSVVVEKIKKTKWSSPNYSLIDQLMRQRPVFMRIDIRRPREEQAAFERTKTIRGKFHVKEGEIVGQNAPEIGNENIGRRMLEKLGWKSGEGLGIQGNKGISEPIFAKIKKNRSGLRHSES
Protein: NAC domain-containing protein 71 (ANAC071) (O49697)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in tissue reunion of wounded inflorescence stems. Required for the division of pith cells in the reunion process, which is dependent on polar-transported auxin and the wound-inducible hormones ethylene and jasmonate. Binds to the promoters of XTH19 and XTH20 to induce their expression via auxin signaling. XTH19 and XTH20 are involved in cell proliferation in the tissue reunion process of incised stems. Involved in hypocotyl graft union formation. Required for the auxin- mediated promotion of vascular tissue proliferation during hypocotyl graft attachment.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
- Ethylene-responsive transcription factor ERF113
- At4g10470
- Xyloglucan endotransglucosylase/hydrolase protein 20
- Aberrant root formation protein 4
- Xyloglucan endotransglucosylase/hydrolase protein 19
- Dof zinc finger protein DOF5.6
- Auxin-responsive protein IAA5
- WUSCHEL-related homeobox 4
Sequence:
MGSSCLPPGFRFHPTDEELIGYYLSRKIEGLEIELEVIPVIDLYKFDPWELPGKSFLPNRDLEWFFFCPRDKKYANGSRTNRATKAGYWKATGKDRKITCKSSHVIAGYRKTLVFYEGRAPLGDRTNWFMHEYRLCDIDDHSQKSPNFKGAFALCRVVKKNELKKNSKSLKNKNEQDIGSCYSSLATSPCRDEASQIQSFKPSSTTNDSSSIWISPDFILDSSKDYPQIKEVASECFPNYHFPVTTANHHVEFPLQEMLVRS
Protein: Lethal(3)malignant brain tumor-like protein 1 (H-l(3)mbt) (H-l(3)mbt protein) (L(3)mbt-like) (L(3)mbt protein homolog) (L3MBTL1) (Q9Y468)
Organism: Homo sapiens (Human)
Function: Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/H1-4 at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10445843}. Note=Excluded from the nucleolus. Does not colocalize with the PcG protein BMI1, suggesting that these two proteins do not belong to the same complex.
Interaction partners:
- Histone H4
- Cellular tumor antigen p53
- Chromobox protein homolog 3
- N-lysine methyltransferase KMT5A
- Lethal
- Histone H1.4
- E3 SUMO-protein ligase CBX4
- Large ribosomal subunit protein uL3m
- Histone H1.5
- Histone H4-like protein type G
Sequence:
MHLVAGDSPGSGPHLPATAFIIPASSATLGLPSSALDVSCFPREPIHVGAPEQVAGCEPVSATVLPQLSAGPASSSTSTVRLLEWTEAAAPPPGGGLRFRISEYKPLNMAGVEQPPSPELRQEGVTEYEDGGAPAGDGEAGPQQAEDHPQNPPEDPNQDPPEDDSTCQCQACGPHQAAGPDLGSSNDGCPQLFQERSVIVENSSGSTSASELLKPMKKRKRREYQSPSEEESEPEAMEKQEEGKDPEGQPTASTPESEEWSSSQPATGEKKECWSWESYLEEQKAITAPVSLFQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQPPKGYKEEEFSWSQYLRSTRAQAAPKHLFVSQSHSPPPLGFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDNFCWEKYLEETGASAVPTWAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLGPREPSSASPGGCPPLSYRSLPHTRTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSEASARKKNLSGFSPRKKPRHHGRIGRPPKYRKIPQEDFQTLTPDVVHQSLFMSALSAHPDRSLSVCWEQHCKLLPGVAGISASTVAKWTIDEVFGFVQTLTGCEDQARLFKDEARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGKGILETGVHSLLCSLPTHLLAKLSFASDSQY
Protein: Exocyst complex component 1 (Exocyst complex component Sec3) (Q9VVG4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Interaction partners:
- Exocyst complex component 5
- Exocyst complex component 8
- Exocyst complex component 2
- Exocyst complex component 4
- Exocyst complex component 3
- Exocyst complex component 7
- Exocyst complex component 6
- Ras-like GTP-binding protein Rho1
- Cdc42 homolog
- Rab11
Sequence:
MLSIGAMANIKHTLQKELFLASGERLLSVVTVVKKKDKKPCYLCVVTTAPPVPVVTLCLIKQSEQREGEYKRKRSWQLDEIKWVDGRNEQFETHEFDLQLEKLYKWYALNPHERQNFLAVLNRQIQKSVRGQRAEFRNVPAAWLSEKSPEKVALGRAVQKTQHMDDEEDEEEEAQEFTALTDKEANELGKLFSECDFAIKDAEQFIEQLSRELHDLDGANMQSVLASEQKVLKMMEHIDNAISEADKFENRLDSYEDILGHVKETMEKIGGKNAMIEIANNNNIKLMKELNKVISQLDLPHSQQQALDEPDLKTANGRKAAIAAAQCLQQAMNSDIDPALLRLEAVQDQRKRFEKWKQKFSATVSRFMNNLFIHLGNEIGDMQVTSTELTLPNHSNVHRELTPYTELMHWTKAMDRKTYDGLMRVYTASLSKIYDRDVRNFFNLAKIQVTEKLRNSREDLDMSTSSRKSAVSTIPYGTLGINRDQWGPGVETADRMRFDALLEKVLAELEPIALQEQLFCINFFQMDVISPTTKNTQTTLEMEKAVDMTQSIISGAVSPSGDGVPQKRIDRQINEDVRKLMMGLFGCLEPELVSFIQSFERVDSFYSLYVFVRLTQHVMSAQDTHSFLSMTFASALVQVKRSFDRFMQNQLLSIREAKLHKRSKAILPYVENFENFAQTAEGIFRKSDRRTDMEKWYLQLVNAIFEGIQLHSQEHPKTPVQVVRMENYHHMYALLAQLKVPGLDALKKEAKKCYNDALKAYVTQYFGRPLEKLNQFFEGVQLKVAQGVKETEISYQMAFSKQELRKVIAQYPAREVKKGLENLYKKVEKHLSEEENLLQVVWHAMQEEFIAQYNYLEERIQKCYAGAMINLEFNIQDILAFFSDIARSH
Protein: Testis-specific serine/threonine-protein kinase 6 (TSK-6) (TSSK-6) (Testis-specific kinase 6) (EC 2.7.11.1) (Serine/threonine-protein kinase SSTK) (Small serine/threonine kinase) (Q925K9)
Organism: Mus musculus (Mouse)
Function: Required for sperm production and function. Plays a role in DNA condensation during postmeiotic chromatin remodeling.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37295417}. Nucleus {ECO:0000269|PubMed:28389581}. Note=Component of the sperm flagellar doublet microtubules (PubMed:37295417). Also localizes in the nucleus of elongating spermatids (PubMed:28389581). {ECO:0000269|PubMed:28389581, ECO:0000269|PubMed:37295417}.
Interaction partners:
- Izumo sperm-egg fusion protein 1
Sequence:
MSGDKLLSELGYKLGRTIGEGSYSKVKVATSKKYKGTVAIKVVDRRRAPPDFVNKFLPRELSILRGVRHPHIVHVFEFIEVCNGKLYIVMEAAATDLLQAVQRNGRIPGSQARELFSQIAGAVRYLHDHHLVHRDLKCENVLLSPDERRVKITDFGFGRQAHGYPDLSTTYCGSAAYASPEVLLGIPYDPKKYDVWSLGVVLYVMVTGCMPFDDSDIAGLPRRQKRGVLYPDGLELSERCKSLIAELLQFSPSARPSAGQVARNGWLRAGDSG
Protein: Serine and arginine rich splicing factor 11 (Q5T760)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSNTTVVPSTAGPGPSGGPGGGGGGGGGGGGTEVIQVTNVSPSASSEQMRTLFGFLGKIDELRLFPPDDSPLPVSSRVCFVKFHDPDSAVVAQHLTNTVFVDRALIVVPYAEGVIPDEAKALSLLAPANAVAGLLPGGGLLPTPNPLTQIGAVPLAALGAPTLDPALAALGLPGANLNSQSLAADQLLKLMSTVDPKLNHVAAGLVSPSLKSDTSSKEIEEAMKRVREAQSLISAAIEPDKKEEKRRHSRSRSRSRRRRTPSSSRHRRSRSRSRRRSHSKSRSRRRSKSPRRRRSHSRERGRRSRSTSKTRDKKKEDKEKKRSKTPPKSYSTARRSRSASSLHICDSRERRRRRSRSGTRSPKKPRSPKRKLSRSPSPRRHKKEKKKDKDKERSRDERERSTSKKKKSKDKEKDRERKSESDKDVKQVTRDYDEEEQGYDSEKEKKEEKKPIETGSPKTKECSVEKGTGDSLRESKVNGDDHHEEDMDMSD
Protein: Histone-lysine N-methyltransferase ASHR3 (EC 2.1.1.-) (ASH1-related protein 3) (Protein SET DOMAIN GROUP 4) (Protein stamen loss) (Q949T8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase (By similarity). Involved in stamen development.
Subcellular location: Nucleus {ECO:0000269|PubMed:17978851}. Chromosome {ECO:0000305|PubMed:17978851}. Note=Associated to the euchromatin.
Interaction partners:
- Histone-lysine N-methyltransferase ATXR6
- Histone H3-like 2
- Histone-lysine N-methyltransferase ASHR1
- Histone H3.1
- Histone-lysine N-methyltransferase ATXR5
- Histone H3-like 4
- Histone H3-like centromeric protein CENH3
- Histone H3-like 5
- Histone H3-like 3
- Histone H3-like 1
Sequence:
MLDLGNMSMSASVALTCCPSFLPAASGPELAKSINSPENLAGECNGKHLPMIPPEEEVKDIKIANGVTAFTRKQNPSDRVKKGFVLDDHVKDWVKRRVASGVSESTCFLPFLVGAKKMVDCLVCHKPVYPGEDLSCSVRGCQGAYHSLCAKESLGFSKSSKFKCPQHECFVCKQRTQWRCVKCPMAAHDKHSPWSKEILHLKDQPGRAVCWRHPTDWRLDTKHAVAQSEIEEVFCQLPLPYVEEEFKIDLAWKDSVVKEDPPSYVHIRRNIYLVKKKRDNANDGVGCTNCGPNCDRSCVCRVQCISCSKGCSCPESCGNRPFRKEKKIKIVKTEHCGWGVEAAESINKEDFIVEYIGEVISDAQCEQRLWDMKHKGMKDFYMCEIQKDFTIDATFKGNASRFLNHSCNPNCVLEKWQVEGETRVGVFAARQIEAGEPLTYDYRFVQFGPEVKCNCGSENCQGYLGTKRKEPNCLVVSWGAKRRRLFHRPIARKPQQD
Protein: Pumilio domain-containing protein P35G2.14 (Q9P789)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pumilio homology domain family member 6
Sequence:
MHQDAMQGSIYEGSRRNTISKPSNNNPPLDMSSLNNDFGQQLDSLATGVGSGSLNGTTNPSSNFNDSNRSNISSSLRSEMEMSNNLLKNTQNDTWTSTVGLSVPENQEAMNFNEGPTGISSIASKNNSSITSKLQNNSNLSVTSSANRGRTSSVSSSYDPSFPWGPRMSSVSSGKQHLSSLSLHTHFNPSSSSTVSSDSLESSQQKAPSSSSTATPASAASEIISNKDPVVEPTHSASNAANSGSNTIRARQTTRTRSNTLPWSPRVFGPTLGYNTPPFGYPPTTSSALPNASGSSSSFFGLPTAVSASAGTSFSDISPAAPKASLENNIASNASSLLNPVGLDHFSAASGWSRDFNHLPASSLATARSSLTGNAKSGIDSSVTGMPSDNYARVVESSTAEFFDPSLASSFGLTNYRTKPLTTGFNHPRPQGHGLNTSLFNTSSGGSLKSPTFEVSNRLGDVDTVPDLPPLGSLSSRPKPSSSSRRRSQSLSAMLKTSNPYMPSPSLLSGSLANSSEHSSSPRLRGSPIHNQPVSSSKSTASLNTNNNGLRASTPEMANISTRSSSESNNTNSWPTVGDATIENLTQHEPTHALWVGNLPSGVSATTVATTFSAYGTVSSIRMLSHKHSAFLNFDSVETAKHVLEELNGKRIFFGSDPVCISFAKVASSSSESSHSAVDGLNKAFSNVSFVPSLREVYDDLINVVQSFGFKDLSKIYQILNAACELTDFAAQIPSISKAFSSRRLNAPKLRQVRKRIDNGLCTQEEVEDIAINWLDEVSDLSSDHLGNTVVQKLFDYCSDPVKEMMLERIAPHLAQIGIHKNGTWAAQKIVDVASTEAQMRLIAKHLQPYIPLLFADQFGNYVVQTCLKFGAPMNDFVFEAILNQFWVIAQSRYGSRAVRACLESPDVTEEQRVLVAAAITVYSVHLAMNGNGTLLLTYLVENMNYPHIPILLTRRFVQDIVRVCTHRLAYNSLLKIISISQGDTACGDLVVDAILDTQNDLNPNSLEKILFEQTYGPSFICKLLTHENISASHRQQLQSAVRNVLGTMEDRGSSELKKLAEVCA
Protein: maleylacetoacetate isomerase (EC 5.2.1.2) (X1WD04)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQQVPAVSIDGITLSQSLAIIQYIEETRPEPRLLPADPMQRAHVRIICDIIASGIQPLQNLYVLQKIGEDKVQWAQHFINRGFQALEPVLKETAGKYCVGDEISMADICLVPQVYNADRFKVDMTQYPTIRRLNQTLVEIEAFKASHPSRQPDTPDDLRL
Protein: Mitochondrial inner membrane protease subunit 1 (EC 3.4.21.-) (P28627)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the mitochondrial inner membrane peptidase (IMP) complex. IMP catalyzes the removal of signal peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. The two catalytic IMP subunits seem to have non-overlapping substrate specificities. IMP1 substrates include nuclear encoded CYB2, mitochondrially encoded COX2, NADH-cytochrome b5 reductase and GUT2.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}.
Interaction partners:
- Nitrogen permease regulator 2
- Restriction of telomere capping protein 1
- Maintenance of telomere capping protein 5
- Vacuolar membrane-associated protein IML1
- Protein PET111
- Mitochondrial inner membrane protease subunit 2
- Protein SOM1, mitochondrial
Sequence:
MTVGTLPIWSKTFSYAIRSLCFLHIIHMYAYEFTETRGESMLPTLSATNDYVHVLKNFQNGRGIKMGDCIVALKPTDPNHRICKRVTGMPGDLVLVDPSTIVNYVGDVLVDEERFGTYIKVPEGHVWVTGDNLSHSLDSRTYNALPMGLIMGKIVAANNFDKPFWDGSIRNIWGFKWINNTFLDVQAKSN
Protein: Dihydropyrimidinase-related protein 4 (DRP-4) (Collapsin response mediator protein 3) (CRMP-3) (UNC33-like phosphoprotein 4) (ULIP-4) (Q62951)
Organism: Rattus norvegicus (Rat)
Function: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Uridine monophosphate synthetase, isoform CRA_a.
- Carbamoyl-phosphate synthase, mitochondrial
- Dihydropyrimidinase-related protein 5
- Rho guanine nucleotide exchange factor 10-like protein
Sequence:
IPRITSDRLLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVLGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRWHESTKEELEALVRDKGVNSFLVFMAYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYITKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTSPPINPDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNFTLIPEGINGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGMPTVVISQGRVVLEDGNLLVTPGAGRFIPRKTFPDFVYKRIKARNRLAEIHGVPRGLYDGPVHEVMLPAKPGSGTQARASCPGKISVPPVRNLHQSGFSLSGSQADDHIARRTAQKIMAPPGGRSNITSLS
Protein: acetyl-CoA carboxylase (EC 6.4.1.2) (A0A2R8QJA0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAEQDSTEKKLPAVAALHSHFIVGSVSEENSEDETAGKLDLQLEDNPRSLSPSSVSSDSTYEMGFDSLDGPLHNMRPSMSGLHLVKQGRDRRRIDLQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGTNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGTGLTVEWTENDQKKGIINVPTELYEQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVPGSPIFVMQLAKHARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLHRIKDIRVLYGMQPWGDSPIDFDGLSTTPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQHNSIDTGWLDRLISEKMQAERPDTMLGVVSGALHVADVNFRNSVSNFLHSLERGQVLPAHTLLNTVDVELIYEGTKYVLKVTRQSPNSYVVIMNCSSVEVDVHRLSDGGMLLSYDGSSYTTYMKEEVDRYRIIIGNKTCVFEKENDPSVLRSPSAGKLIQYTVEDGGHVFAGQCYAEIEVMKMVMTLTASESGCIHYVKRAGAVLEPGCIIGKLQLDDPSRVQQAELYTGTLPSIQSVALRGEKLHRVFHSTLGHLVHIMNGYCLPEPFFSAKLKEWVERLMKTLRDPSLPLLELQDIMTSVSGRIPPAVEKAIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQKYRSGIRGHMKAVVMDLLRQYLRVEVQFQHGHYDKCVFALREENKVDMANVLNYIFSHAQVTKKNCLVTMLIDQLCGRDPTLTDELMAILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCIVEFQFMLPTSHPNRGNIPTLNRKLSAPLQDYKPPANTANTSGATEAASDSAESEDRMSFSSNLNHYGMVHVASVSDVLLDTSFTPPCQRMGAMVSFRSFQEFTRNIKDVLSCFSDSPPSTPTFPEGGNPVLYREEDSKSIQDEPIHILNVAIKTDSDIDDDGLAAMFREFTQSKKSLLFDHGIRRLTFLVAQKREFPKFFTFRARDKFEEDRIYRHLEPALAFQLELNRMRNFALTAIPCANHKMHLYLGAARVEVGTEVTDYRFFVRAIIRHSDLVTKEASFEYLHNEAERLLLEAMDELEVAFNNTTVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTPTGKQIPIRLFLTNESGYYLDISLYKEVTDSRTGQVGHKDRQIMFQAYGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYVYDFPEMFRQALRKLWQSMDAHANLPKCPLPSELLTFTELVLDSQGQLVQMNRLPGGNEIGMVAWRMTLRTPEYPAGREIIVISNDITHKIGSFGPQEDVLFQQASEMARESGIPRIYIAANSGARIGLAEEIRHMFHVAWQDPVDPYKGFKYLYLTPQDYKKVSALNSVHCEHVEDEGESRYKITDIIGKEEGLGVENLRGSGMIAGESSLAYEDIITMNLVTCRAIGIGAYLVRLGQRTIQVENSHIILTGAGALNKVLGREVYTSNNQLGGVQIMHNNGVTHTNVCDDFEGVYTLLHWLSYMPKNMSSPVPILSAKDPIDRAIEFVPTKAPYDPRWMLAGRPNQNIKGAWVSGFFDQGSFLEIMQPWAQSVVVGRARLGGIPTGVVAVETRSVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTAQAIKDFNREGLPLIVFANWRGFSGGMKDMYDQVLKFGAYIVDGLREYRQPVLVYIPPQAELRGGSWVVIDPTINPRHMEMYADKDSRGGVLEPEGTVEIKFRKKDLVKTMRRVDPVYMGLAERLGTPELSVSERKELESKLKEREEFLLPIYHQVAVQFADLHDTPGRMQEKGVITDILEWSTSRQFFYWRLRRLLLEETVKRKIQCANSELTDGQVQAMLRRWFVEAEGAVKAYLWDSNEDVVEWLERQLAEEEGARSVIDENIKYIRRDHILKQIRSLVQANPEVAMDSIVHMTQHISPTQRAEVVRILSTMDTPASS
Protein: Calpain-like protease palB/RIM13 (EC 3.4.22.-) (Cysteine protease RIM13) (Q5AK25)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH.
Interaction partners:
- pH-response transcription factor pacC/RIM101
- pH-response regulator protein palA/RIM20
- pH-response regulator protein palF/RIM8
- Vacuolar-sorting protein SNF7
- pH-response regulator protein palH/RIM21
- EF-hand domain-containing protein
- pH-response regulator protein palI/RIM9
- Dfg16p
Sequence:
MPTPCLEQFLHHLEKSHLYLSIDNTKQAKKECLESIKILNSIAKTTPLPEIKVLSQYTLNHYESLDKPRTISDKLEWISSKLTQETFFPPVIQFNENFTSHNELFVDTISPIQDNDNKIFEKLPNKLAKFEYIEISNWDNDITHLKNLYQDILPNCSFVSSFLAIIDANIPIIDTITPQKSSQKYKVSLRFNGALRNVIVDSKFPIMPNSRNLIIKSYSDTELYWPALIEKAYLTIMGNGYNFSGSNMANDAYVLSGWLPQIIKLSNGQLPSNIDDLWRLRTQGKVTMGIGTGTLSKQLSSQLHLVSGHDYVIDNIKDGVITVKNPWLDPKDRVVEIKNFNHFKYLYVNWKPDHKPYQHYFLYQAKPNTYNQPQFTIKCMEETWILLERHLSETSSSPSPHWMDMNVFETEYKIITPSQYKKYLSVETNNRLQLIKLKPGVFTIVISSNKPCRFTLSSFNAMFSKSKYKYDYTETVNGEWNSDINGGNWAMSTYINNPQYDIIAKQTTELIMGMHGQGQINFHLFHSSSDSMGERIQNFDKTKLINYQNYNASYQSSSYRLTPGHYKLVVSEYYRSIGTYQLVLNSSEPITITKIPPFLGLYNISKSFNWDNTNRFKLKFETTGYNSKVKIKIAYFNGESDFELQTSYRPAMRASLFNSQTKQPIQINEQFNDSLYGVFLHEILPSPEEYILLIERFEIGYGRCVVEIGCNNKVILK
Protein: Purine nucleoside phosphorylase (PNP) (EC 2.4.2.1) (Inosine phosphorylase) (Inosine-guanosine phosphorylase) (P00491)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22509282}.
Interaction partners:
- Adenosine deaminase
- Xanthine dehydrogenase/oxidase
- Adenine phosphoribosyltransferase
- Uridine phosphorylase 2
- Uridine phosphorylase 1
- Guanine deaminase
- 5'-nucleotidase
- Hypoxanthine-guanine phosphoribosyltransferase
- Adenosine kinase
- 5'
Sequence:
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Protein: Atonal bHLH transcription factor 1a (Protein atonal homolog 1a) (B0R059)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- POU domain, class 4, transcription factor 3
- Myosin VIIAa
- Neurogenic locus notch homolog protein 1
- Growth factor-independent 1A transcription repressor b.
- Transcription factor Sox-2
- Eyes absent homolog
- Myosin VIIAb
- Homeobox protein six1b
- Paired box protein Pax-2a
- Transcription factor HES-5
Sequence:
MDGMSTDTREVVELDVQHSSLGRGEQSEYPPALALMASSDPRAWLAPVQAGTCAAHAEYLLHSPGSSAEGVSSASNFRKSSKSPVKVRELCRLKGAVGADEGRQRAPSSKSTNVVQKQRRMAANARERRRMHGLNHAFDELRSVIPAFDNDKKLSKYETLQMAQIYINALSDLLQGPGAKADPPNCDLLHANVLETDRSPRGSPGVCRRGTGVGYPYQYEDGTFNSFMEQDLQSPSGTSKSGSEASKDSPRSNRSDGEFSPHSHFSDSDETHLELQSEDELSELKLAKRRAF
Protein: Sad1 and UNC84 domain containing 1 (A0A0G2K016)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004540}.
Interaction partners:
- Emerin
- KASH domain containing 5
- Nesprin-3
- Nesprin-4
- Sad1 and UNC84 domain containing 2
- Prelamin-A/C
- Nuclear pore complex protein Nup153
- Plectin
- Membrane-anchored junction protein
- Telomere repeat binding bouquet formation protein 2
Sequence:
MDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHRLEPVFDSPRMSRRSLRLITTTAAYSSGDGQTVDTHISTSRATPAKGRETRTVKQRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAVHGPTSRVYSRDRTLRPRGASFYLDRTLWLAKYTSSSFASFIVQLFQVVLMKLNFESETYKLKGYESRAYESQSYETKSHESEAHLGHCGRMTAGELSRVDGESLCDDCKGKKHLETHTTTHSQLSQPHRAAGAMGRLCTYTGDLLVRALRRTRAAGWSVAEAMWSVLWLAVTAPGKAASGTFWWLGSGWYQFVTLISWLNVFLLTRCLRNICKVFVLLLPLLLLLGAGFSLWGQGNFFSLLPMLNWTAMQPAQRVDNPKDMHRPGPLSPSPPLKVDPMASQWPQESDMGQKIASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLSLWVKDMVGQHLQEIGSIEPPDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEETKLRAGRDEEQPLLDRVQHLELELNLLKSQLSDWQHLRSSCEQADARIQETVQLMFSEDQPGGSLEWLLQKLSSRFVSKDELQVLLHDLELKLLQNITHHITVTGQAPTSEAIVSAMSQAGISGITEAQAHIIVNNALRLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALLSLFGVPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLSPTGNISSAPRDFAVYGLETEYQEEGQPLGRFTYDQEGDSLQMFHTLERPDQGFQIVELRVLSNWGHPEYTCLYRFRVHGEPIQ
Protein: Defensin (Varisin A1) (Q86QI5)
Organism: Dermacentor variabilis (American dog tick)
Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.
Subcellular location: Secreted {ECO:0000269|PubMed:11439245}.
Interaction partners:
Sequence:
MRGLCICLVFLLVCGLVSATAAAPAESEVAHLRVRRGFGCPLNQGACHNHCRSIRRRGGYCSGIIKQTCTCYRN
Protein: Coupling protein TraD (DNA transport protein TraD) (P09130)
Organism: Escherichia coli (strain K12)
Function: Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Couples the transferosome to a type IV secretion system. Probably forms a pore through which single-stranded plasmid DNA is transferred to the secretion system. The last 37 residues are important for determining plasmid specificity and transfer efficiency, with additional specificity conferred by the TraD-TraM pair.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:9324263}; Multi-pass membrane protein {ECO:0000269|PubMed:9324263}.
Interaction partners:
Sequence:
MSFNAKDMTQGGQIASMRIRMFSQIANIMLYCLFIFFWILVGLVLWIKISWQTFVNGCIYWWCTTLEGMRDLIKSQPVYEIQYYGKTFRMNAAQVLHDKYMIWCSEQLWSAFVLAAVVALVICLITFFVVSWILGRQGKQQSENEVTGGRQLTDNPKDVARMLKKDGKDSDIRIGDLPIIRDSEIQNFCLHGTVGAGKSEVIRRLANYARQRGDMVVIYDRSGEFVKSYYDPSIDKILNPLDARCAAWDLWKECLTQPDFDNTANTLIPMGTKEDPFWQGSGRTIFAEAAYLMRNDPNRSYSKLVDTLLSIKIEKLRTYLRNSPAANLVEEKIEKTAISIRAVLTNYVKAIRYLQGIEHNGEPFTIRDWMRGVREDQKNGWLFISSNADTHASLKPVISMWLSIAIRGLLAMGENRNRRVWFFCDELPTLHKLPDLVEILPEARKFGGCYVFGIQSYAQLEDIYGEKAAASLFDVMNTRAFFRSPSHKIAEFAAGEIGEKEHLKASEQYSYGADPVRDGVSTGKDMERQTLVSYSDIQSLPDLTCYVTLPGPYPAVKLSLKYQTRPKVAPEFIPRDINPEMENRLSAVLAAREAEGRQMASLFEPDVPEVVSGEDVTQAEQPQQPVSPAINDKKSDSGVNVPAGGIEQELKMKPEEEMEQQLPPGISESGEVVDMAAYEAWQQENHPDIQQQMQRREEVNINVHRERGEDVEPGDDF
Protein: Citrate synthase, mitochondrial (EC 2.3.3.16) (O00098)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- ATP citrate synthase
- ATP citrate synthase
- Pyruvate carboxylase
- Malate dehydrogenase
- malate dehydrogenase
- Acetyltransferase component of pyruvate dehydrogenase complex
- malate dehydrogenase
- Malate synthase, glyoxysomal
Sequence:
MASTLRLSTSALRSSTLAGKPVVQSVAFNGLRCYSTGKTKSLKETFADKLPGELEKVKKLRKEHGNKVIGELTLDQAYGGARGVKCLVWEGSVLDSEEGIRFRGLTIPECQKLLPKAPGGEEPLPEGLFWLLLTGEVPSEQQVRDLSAEWAARSDLPKFIEELIDRCPSTLHPMAQFSLAVTALEHESAFAKAYAKGINKKEYWHYTFEDSMDLIAKLPTIAAKIYRNVFKDGKVAPIQKDKDYSYNLANQLGFADNKDFVELMRLYLTIHSDHEGGNVSAHTTHLVGSALSSPMLSLAAGLNGLAGPLHGLANQEVLNWLTEMKKVVGNDLSDQSIKDYLWSTLNAGRVVPGYGHAVLRKTDPRYTSQREFALRKLPDDPMFKLVSQVYKIAPGVLTEHGKTKNPYPNVDAHSGVLLQYYGLTEANYYTVLFGVSRALGVLPQLIIDRAFGAPIERPKSFSTEAYAKLVGAKL