wanglab/gogpt-training-data huggingface dataset:
Protein: RecBCD enzyme subunit RecB (EC 3.1.11.5) (EC 5.6.2.4) (DNA 3'-5' helicase subunit RecB) (Exodeoxyribonuclease V 135 kDa polypeptide) (Exodeoxyribonuclease V beta chain) (Exonuclease V subunit RecB) (ExoV subunit RecB) (Helicase/nuclease RecBCD subunit RecB) (P08394)
Organism: Escherichia coli (strain K12)
Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA. The RecBC complex requires the RecD subunit for nuclease activity, but can translocate along ssDNA in both directions. Probably interacts with a component of retron Ec48 which moniters RecBCD stability; when RecB is missing or impaired the retron is activated and becomes toxic (Probable).
Interaction partners:
- RecBCD enzyme subunit RecC
- RecBCD enzyme subunit RecD
- Protease 3
- Protein RecA
- DNA polymerase I
- Exodeoxyribonuclease I
- DNA replication and repair protein RecF
- Single-stranded-DNA-specific exonuclease RecJ
- ATP-dependent DNA helicase RecG
- Crossover junction endodeoxyribonuclease RuvC
Sequence:
MSDVAETLDPLRLPLQGERLIEASAGTGKTFTIAALYLRLLLGLGGSAAFPRPLTVEELLVVTFTEAATAELRGRIRSNIHELRIACLRETTDNPLYERLLEEIDDKAQAAQWLLLAERQMDEAAVFTIHGFCQRMLNLNAFESGMLFEQQLIEDESLLRYQACADFWRRHCYPLPREIAQVVFETWKGPQALLRDINRYLQGEAPVIKAPPPDDETLASRHAQIVARIDTVKQQWRDAVGELDALIESSGIDRRKFNRSNQAKWIDKISAWAEEETNSYQLPESLEKFSQRFLEDRTKAGGETPRHPLFEAIDQLLAEPLSIRDLVITRALAEIRETVAREKRRRGELGFDDMLSRLDSALRSESGEVLAAAIRTRFPVAMIDEFQDTDPQQYRIFRRIWHHQPETALLLIGDPKQAIYAFRGADIFTYMKARSEVHAHYTLDTNWRSAPGMVNSVNKLFSQTDDAFMFREIPFIPVKSAGKNQALRFVFKGETQPAMKMWLMEGESCGVGDYQSTMAQVCAAQIRDWLQAGQRGEALLMNGDDARPVRASDISVLVRSRQEAAQVRDALTLLEIPSVYLSNRDSVFETLEAQEMLWLLQAVMTPERENTLRSALATSMMGLNALDIETLNNDEHAWDVVVEEFDGYRQIWRKRGVMPMLRALMSARNIAENLLATAGGERRLTDILHISELLQEAGTQLESEHALVRWLSQHILEPDSNASSQQMRLESDKHLVQIVTIHKSKGLEYPLVWLPFITNFRVQEQAFYHDRHSFEAVLDLNAAPESVDLAEAERLAEDLRLLYVALTRSVWHCSLGVAPLVRRRGDKKGDTDVHQSALGRLLQKGEPQDAAGLRTCIEALCDDDIAWQTAQTGDNQPWQVNDVSTAELNAKTLQRLPGDNWRVTSYSGLQQRGHGIAQDLMPRLDVDAAGVASVVEEPTLTPHQFPRGASPGTFLHSLFEDLDFTQPVDPNWVREKLELGGFESQWEPVLTEWITAVLQAPLNETGVSLSQLSARNKQVEMEFYLPISEPLIASQLDTLIRQFDPLSAGCPPLEFMQVRGMLKGFIDLVFRHEGRYYLLDYKSNWLGEDSSAYTQQAMAAAMQAHRYDLQYQLYTLALHRYLRHRIADYDYEHHFGGVIYLFLRGVDKEHPQQGIYTTRPNAGLIALMDEMFAGMTLEEA
Protein: Tubby-related protein 4 (Tubby superfamily protein) (Tubby-like protein 4) (Q9NRJ4)
Organism: Homo sapiens (Human)
Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Cytoplasm.
Interaction partners:
- Cullin-5
- Mitotic interactor and substrate of PLK1
Sequence:
MYAAVEHGPVLCSDSNILCLSWKGRVPKSEKEKPVCRRRYYEEGWLATGNGRGVVGVTFTSSHCRRDRSTPQRINFNLRGHNSEVVLVRWNEPYQKLATCDADGGIFVWIQYEGRWSVELVNDRGAQVSDFTWSHDGTQALISYRDGFVLVGSVSGQRHWSSEINLESQITCGIWTPDDQQVLFGTADGQVIVMDCHGRMLAHVLLHESDGVLGMSWNYPIFLVEDSSESDTDSDDYAPPQDGPAAYPIPVQNIKPLLTVSFTSGDISLMNNYDDLSPTVIRSGLKEVVAQWCTQGDLLAVAGMERQTQLGELPNGPLLKSAMVKFYNVRGEHIFTLDTLVQRPIISICWGHRDSRLLMASGPALYVVRVEHRVSSLQLLCQQAIASTLREDKDVSKLTLPPRLCSYLSTAFIPTIKPPIPDPNNMRDFVSYPSAGNERLHCTMKRTEDDPEVGGPCYTLYLEYLGGLVPILKGRRISKLRPEFVIMDPRTDSKPDEIYGNSLISTVIDSCNCSDSSDIELSDDWAAKKSPKISRASKSPKLPRISIEARKSPKLPRAAQELSRSPRLPLRKPSVGSPSLTRREFPFEDITQHNYLAQVTSNIWGTKFKIVGLAAFLPTNLGAVIYKTSLLHLQPRQMTIYLPEVRKISMDYINLPVFNPNVFSEDEDDLPVTGASGVPENSPPCTVNIPIAPIHSSAQAMSPTQSIGLVQSLLANQNVQLDVLTNQTTAVGTAEHAGDSATQYPVSNRYSNPGQVIFGSVEMGRIIQNPPPLSLPPPPQGPMQLSTVGHGDRDHEHLQKSAKALRPTPQLAAEGDAVVFSAPQEVQVTKINPPPPYPGTIPAAPTTAAPPPPLPPPQPPVDVCLKKGDFSLYPTSVHYQTPLGYERITTFDSSGNVEEVCRPRTRMLCSQNTYTLPGPGSSATLRLTATEKKVPQPCSSATLNRLTVPRYSIPTGDPPPYPEIASQLAQGRGAAQRSDNSLIHATLRRNNREATLKMAQLADSPRAPLQPLAKSKGGPGGVVTQLPARPPPALYTCSQCSGTGPSSQPGASLAHTASASPLASQSSYSLLSPPDSARDRTDYVNSAFTEDEALSQHCQLEKPLRHPPLPEAAVTLKRPPPYQWDPMLGEDVWVPQERTAQTSGPNPLKLSSLMLSQGQHLDVSRLPFISPKSPASPTATFQTGYGMGVPYPGSYNNPPLPGVQAPCSPKDALSPTQFAQQEPAVVLQPLYPPSLSYCTLPPMYPGSSTCSSLQLPPVALHPWSSYSACPPMQNPQGTLPPKPHLVVEKPLVSPPPADLQSHLGTEVMVETADNFQEVLSLTESPVPQRTEKFGKKNRKRLDSRAEEGSVQAITEGKVKKEARTLSDFNSLISSPHLGREKKKVKSQKDQLKSKKLNKTNEFQDSSESEPELFISGDELMNQSQGSRKGWKSKRSPRAAGELEEAKCRRASEKEDGRLGSQGFVYVMANKQPLWNEATQVYQLDFGGRVTQESAKNFQIELEGRQVMQFGRIDGSAYILDFQYPFSAVQAFAVALANVTQRLK
Protein: ATP synthase subunit epsilon, mitochondrial (ATPase subunit epsilon) (Q96253)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}. Mitochondrion inner membrane {ECO:0000269|PubMed:14671022}.
Interaction partners:
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit O, mitochondrial
- ATP synthase subunit delta, chloroplastic
- ATP synthase subunit delta', mitochondrial
- ATP synthase subunit 9
- ATPase, F1 complex, OSCP/delta subunit protein
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit beta-2, mitochondrial
- ATP synthase subunit beta-3, mitochondrial
- ATP synthase epsilon chain, chloroplastic
Sequence:
MASNAAVPFWRAAGMTYISYSNICANIVRNCLKEPHKAEALTREKVHFSLSKWADGKPQKPVLRSDTPEV
Protein: Sll1835 protein (P73111)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Slr1506 protein
- Slr1270 protein
- Slr1908 protein
- Slr0431 protein
Sequence:
MATHNLDRVAAPLISKLFPFFLVLAGMFSGTLAAQAQGKPTISVPEFKNDTNMSWWWWSGNTSRELADALSNELTSTGNFQVVERQNLGSVLSEQELAELGLTRPETSAQRGQLTGAQYIVLGRVTAYEEGVSSESGGNNFGLNLGLFSIGNSERQAKQEAYVAIDLRVVDSSTGEVVYARTVEGRATDTAASSANNVNILGIVNTGQDNQSTSRAPVGKALRAGLVEITDYLSCVMVEQDNCIQEYQDKDRQRRQKTKDTLILE
Protein: Respiratory burst oxidase homolog protein B (EC 1.11.1.-) (EC 1.6.3.-) (NADPH oxidase RBOHB) (OsrbohB) (Q5ZAJ0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Calcium-dependent NADPH oxidase that generates superoxide.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Calcium-dependent protein kinase 4
- Calcium-dependent protein kinase 18
- Calcium-dependent protein kinase 5
- Calcium-dependent protein kinase 9
- Calcium-dependent protein kinase 6
- Calcium-dependent protein kinase 13
- Calcium-dependent protein kinase 7
- Os04g0589400 protein
- Calcium-dependent protein kinase 1
- Calcium-dependent protein kinase 21
Sequence:
MADLEAGMVAAATDQGNSTRSQDDAATLIPNSGNLGSSNRSTKTARFKDDDELVEITLDVQRDSVAIQEVRGVDEGGSGHGTGFDGLPLVSPSSKSGKLTSKLRQVTNGLKMKSSSRKAPSPQAQQSAKRVRKRLDRTKSSAAVALKGLQFVTAKVGNDGWAAVEKRFNQLQVDGVLLRSRFGKCIGMDGSDEFAVQMFDSLARKRGIVKQVLTKDELKDFYEQLTDQGFDNRLRTFFDMVDKNADGRLTAEEVKEIIALSASANKLSKIKERADEYTALIMEELDPTNLGYIEMEDLEALLLQSPSEAAARSTTTHSSKLSKALSMKLASNKEMSPVRHYWQQFMYFLEENWKRSWVMTLWISICIALFIWKFIQYRNRAVFGIMGYCVTTAKGAAETLKFNMALVLLPVCRNTITWIRSKTQVGAVVPFNDNINFHKVIAAGVAVGVALHAGAHLTCDFPRLLHASDAQYELMKPFFGEKRPPNYWWFVKGTEGWTGVVMVVLMAIAFTLAQPWFRRNKLKDSNPLKKMTGFNAFWFTHHLFVIVYTLLFVHGTCLYLSRKWYKKTTWMYLAVPVVLYVSERILRLFRSHDAVGIQKVAVYPGNVLALYMSKPPGFRYRSGQYIFIKCTAVSPYEWHPFSITSAPGDDYLSVHIRTRGDWTSRLRTVFSEACRPPTEGESGLLRADLSKGITDEKARFPKLLVDGPYGAPAQDYREYDVLLLIGLGIGATPLISIVKDVLNHIQGEGSVGTTEPESSSKAKKKPFMTKRAYFYWVTREEGSFEWFRGVMNEVSEKDKDGVIELHNHCSSVYQEGDARSALIVMLQELQHAKKGVDILSGTSVKTHFARPNWRSVFKKVAVSHENQRVGVFYCGEPVLVPQLRQLSADFTHKTNTRFDFHKENF
Protein: Transcriptional activator spt7 (P87152)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SAGA complex subunit Sgf73
- Probable ubiquitin carboxyl-terminal hydrolase 8
- SAGA complex subunit Hfi1
- SAGA complex subunit Sgf29
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex subunit Ngg1
- SAGA complex subunit Spt3
- SAGA complex subunit Sus1
- SAGA complex/transcription factor TFIID complex subunit Taf10
- SAGA complex subunit Spt8
Sequence:
METNFEDSKSLDEPVLHDIAIALLKNDYWSLYLSPEQKRKYISILNDTLLWNRFINVIEWDKLCDEKDSNGSNDDEEDDLDITTLFRCRCMIFDAKINPALFDLSSTSSGSIEHVDHQNISLEASLAEEEERKKGDAKKSEATGRQLFDDDDFDESDAEDSSKATITLDLQKDKSLRKSIIDLKSVDIDDMDTSGFAAIESNKALSNISFNYVYYTLENDSENINEVKKFEDEEDTSTPNTSSFQNNSSSLDLSDNLSLNSKFGSLTSSFKYLLQYLEGNRSKINATDADVKQLLSDVKKNKSKWANDQRIGQEELYEAAEKVVLELRSYTEHSLAFLTKVSKRDAPDYYTVIKEPMDLGTILRNLKNLHYNSKKEFVHDLMLIWSNCFLYNSHPDHPLRVHAQFMKDKSLELINLIPDIVIQSRKDYDDSLIEAELESDEESTAETSKHVTSKKTSSRGGQTQQAVEVHTDANSPEENNTPVTKKEVETSKPPAVSGSTPPVNEAAVIESSNTLEKEPLSDVATEYWKIKTKDIRESHILNNRRILKSLQFIETELPMIRKPTAMSAFIDREVAYGSIDCLPMDKGDFEPIMKLDTTPLLEYDVGSGVPMTAGSVLETESEEDLYFRDYSLFEINRNTPGVPSLMYKNIAKMQEIRKLCNKIQTVRQLQLPQPFYYEHHKSHVPFANNEPILLDIPQNYDNMSSFKPLAHDVLKKLCTIILFHAGFESFQMGALDALTEIAADYMAKMGAVMDQYLIYGKDKSQQEIVGQTLGELGVDDVNDLISYVYHDVERQSVKLLEIHQRLQRHFVELLRPALSERNDEEAIFNQNGESFVTGNFSYETGDDFFGLRELGLDRELGLDSLSVPLHLLQSRLRSNMSWQPEATIKGDQEYAPPPKYPPITAESISNEIGLIQGFLKKNLEEFGLDELLEDEDIRPRSKPPRPRLPPNGKITTGRKRIASSVFLNQSLRKKRCLKENEQGTEVTTLPEE
Protein: Mitochondrial antiviral signaling protein (Virus-induced signaling adapter) (A0ZVR1)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MTFAEDKTYQYIRNHHRNFCKIHVLEILPYLSCLTASDQDRLRASFERWGNQGTLWDLFDSLRRRSGWVQSFIGALRICELSDLADEVSRVYQNSLLRNSNSPPAPLEPPSTPAEAPGPSRPAVAPSIPHNGYREDEPSYPMPVQDTQSPEAPGESSKTAPQPPNSGAVLKRPGGPLEPSSDVALSPLTSGGHQKQDTELGSAHTAGTVSSPTSPRGPVSPTVSFQPLARSTPRASRLPGPPVSTASSSTGLASAGGAGDQVEATICSGGAGVPTTSVTASMVPSKVPTNSAFASTMPSKLPTSLKPPGAMSTNVSPSVAPSKLPINSTRPGAMSPKVPTGLLPDHRKPTSTVASKVPANTGPTIRSSNRPEKETPASPAPIGTAAGGTSPWPDSNSDRWDSEEPELSKPGRLVSRMDSQPFSGSSEDLAISYSNPLGSGPDNTPEENEYVSVDTIRIQGDPSTPPVGDSPGPLTASEFQAEEELEEGLEEVKTEARAPWVGVAVVGVLLATLLAMLYRRRLPQ
Protein: Zinc finger and BTB domain-containing protein 12 (Protein G10) (Q9Y330)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Phosphatidylserine lipase ABHD16A
Sequence:
MASGVEVLRFQLPGHEAATLRNMNQLRAEERFCDVTIVADSLKFRGHKVILAACSPFLRDQFLLNPSSELQVSLMHSARIVADLLLSCYTGALEFAVRDIVNYLTAASYLQMEHVVEKCRNALSQFIEPKIGLKEDGVSEASLVSSISATKSLLPPARTPKPAPKPPPPPPLPPPLLRPVKLEFPLDEDLELKAEEEDEDEDEDVSDICIVKVESALEVAHRLKPPGGLGGGLGIGGSVGGHLGELAQSSVPPSTVAPPQGVVKACYSLSEDAEGEGLLLIPGGRASVGATSGLVEAAAVAMAARGAGGSLGAGGSRGPLPGGFSGGNPLKNIKCTKCPEVFQGVEKLVFHMRAQHFIFMCPRCGKQFNHSSNLNRHMNVHRGVKSHSCGICGKCFTQKSTLHDHLNLHSGARPYRCSYCDVRFAHKPAIRRHLKEQHGKTTAENVLEASVAEINVLIR
Protein: Lactoperoxidase (LPO) (EC 1.11.1.7) (Salivary peroxidase) (SPO) (P22079)
Organism: Homo sapiens (Human)
Function: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. Shows antibacterial properties against Pseudomonas aeruginosa. The lactoperoxidase-SCN(-)-H2O2 system shows antibacterial properties against Burkholderia cepacia and Haemophilus influenzae in vitro. Present in mammary and salivary gland secretions and may contribute to airway host defense against infection. May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:12626341}. Cytoplasm {ECO:0000250|UniProtKB:Q5SW46}.
Interaction partners:
- Alpha-lactalbumin
- Lactotransferrin
- Albumin
Sequence:
MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAMSSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLEVGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTPGKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSEYSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINALTSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTTARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAFVQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDENYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQPTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGLYGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDSLQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN
Protein: Intercellular adhesion molecule 1 (Q5NKV8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDXLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTREVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP
Protein: Kinesin-like protein (F5H3M2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MIKVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVRPVTKEDGEGPEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSVELGPGLRRAELGSWSSQEHLEWEPACQTPQPSARAHSAPSSGTSSRPGSIRRKLQPSA
Protein: Infection Response protein (P91316)
Organism: Caenorhabditis elegans
Interaction partners:
- ShKT domain-containing protein
Sequence:
MSRFLSFCLLAALVSATSAQFTDQCTTQDYAAITQCYVTYMAGYNISMTTTVPEYWSFHFARRDLLDADGLHIQPYVCQLGNALSNCLAPYSCMGPNAYMQMNAANTTEATDYWIDLAVTEYQCGVGYNLTMTEFYCMAFCRDRYQPNIDQCDAQAAIDMKNGMDPCAAQQKDFNCQAAVYRNCCDWNAGVYICNVDVAGSKAVNPACVNAGLVTCPAPR
Protein: alpha-amylase (EC 3.2.1.1) (G5EAT0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
- Alpha-1,4 glucan phosphorylase
- Glucoamylase
- Glucoamylase
- Zn
- Alpha-glucosidase
- Probable alpha/beta-glucosidase agdC
- Alpha/beta-glucosidase agdC
- Alpha/beta-glucosidase agdC
Sequence:
MRLLALTSALALLGKAVHGLDADGWRSQSIYFLLTDRFARTDGSTTAACDLAQRRYCGGSWQGIINQLDYIQDMGFTAIWITPITEQIPDVTAVGTGFHGYWQKNIYGVDTNLGTADDIRALSEALHDRGMYLMLDVVANHMSYGGPGGSTDFSIFTPFDSASYFHSYCAINNYDNQWQVENCFLGDDTVSLTDLNTQSSEVRDIWYDWIEDIVANYSVDGLRIDTVKHVEKDFWPGYIDAAGVYSVGEIFHGDPAYTCPYQDYMDGVMNYPIYYPLLNAFKSSSGSMSDLYNMINTVASNCRDPTLLGNFIENHDNPRFPNYTPDMSRAKNVLAFLFLTDGIPIVYAGQEQHYSGSNDPYNREPVWWSSYSTSSELYKFIATTNKIRKLAISKDSSYLTSRNTPFYSDSNYIAMRKGSGGSQVLTLLNNIGTSIGSYTFDLYDHGYNSGANLVELYTCSSVQVGSNGAISIPMTSGLPRVLVPAAWVSGSGLCGLTNPTSKTTTATTTSTTTCASATATAITVVFQERVQTAYGENVFLAGSISQLGNWDTTEAVALSAAQYTATDPLWTVAIELPVGTSFEFKFLKKRQDGSIVWESNPNRSAKVNEGCARTTQTISTSWR
Protein: Serine protease inhibitor dipetalogastin (Dipetalin) (O96790)
Organism: Dipetalogaster maximus (Blood-sucking bug)
Function: Thrombin inhibitor. Prevents blood clotting to allow insect to feed on blood. Also functions as an inhibitor of trypsin and plasmin.
Subcellular location: Secreted.
Interaction partners:
Sequence:
LIKELVNMVIQHAEEEEVKELKNPCECPRALHRVCGSDGNTYSNPCMLNCAKHEGNPDLVQVHKGPCDEHDHDFEDPCKCDNKFEPVCGDDQITYLNLCHLECATFTTSPGVEVAYEGECHAETTNAMEVLFQGNPCECPRALHRVCGSDGNTYSNPCMLTCAKHEGNPDLVQVHEGPCDEHDHDFEDTCQCDDTFQPVCGDDEITYRNLCHLECATFTTSPGVEVKHEGECHPETKVNQLILKSCMCPKIYKPVCGTDGRTYPNICVLKCHISSNPGLGLAHLGECKVAVLAKETGEVRNPCNCFRNFNPVCGTDGKTYGNLCMLGCAAETKVPGLKLLHNGRCLPKEQL
Protein: Serine protease 59 (D3Z4W5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKTFFIFTLLSLAVANTPKAVLKEYNNSEEYLPENFNVPYMVYLQSSPEPCVGTLIDPQWVLTAAHCSLPTKIRLGVYRPNIKNEKEQICNYSFTVVHPNFDAKLLKNDLMLIKLSYPATINMYVGTIAIAMEPMAFNESCFIPTWTWNNYKNLSDPDILTWINEYSLSPSDCLDT
Protein: RNA annealing protein YRA2 (P36036)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in export of poly(A) mRNAs from the nucleus. Recruited to the coding sequences as well as poly-A sites of active genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:11390651}.
Interaction partners:
- RNA annealing protein YRA1
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein complex subunit 1
- ATP-dependent RNA helicase SUB2
- THO complex subunit THP2
Sequence:
MDKAFDEIIGNSHTDSSSNHKVTRYRRRDLRNELGPRLGFAPSDAASRSKDRLYREREEPPLPKRIRISKIPLDVSDYTLDDMIKEFGSPIFSKIFDNKEDRTCIYEFEDPEVLEKIVERYNGHELHNAKIEVEIYQPQRKHSRMNAHNRRKQTAQEHGRGRPGSHYRQKPNRVSKKNKGREKNNTPTSVEALDAELDAYMKG
Protein: Transcription factor IIIA (AtTFIIIA) (Q84MZ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Isoform 1 is a transcription activator the binds both 5S rDNA and 5S rRNA and stimulates the transcription of 5S rRNA gene. Isoform 1 regulates 5S rRNA levels during development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:12711688}. Nucleus, nucleolus {ECO:0000269|PubMed:12711688}. Note=Accumulates in several nuclear foci including the nucleolus. {ECO:0000269|PubMed:12711688}.
Interaction partners:
- Large ribosomal subunit protein uL18z
- RING-H2 finger protein ATL7
- AT-hook motif nuclear-localized protein 8
- B-block binding subunit of TFIIIC
- GATA transcription factor 1
- F14D16.11
- Zinc finger protein AZF1
- Protein EPIDERMAL PATTERNING FACTOR 1
Sequence:
MAEEAKVDVKTSAKKDIRNYLCQYCGISRSKNYLITKHIQSHHQMELEEERDDEACEVDEESSSNHTCQECGAEFKKPAHLKQHMQSHSLERSFTCYVDDCAASYRRKDHLNRHLLTHKGKLFKCPKENCKSEFSVQGNVGRHVKKYHSNDNRDKDNTGLGDGDKDNTCKGDDDKEKSGSGGCEKENEGNGGSGKDNNGNGDSQPAECSTGQKQVVCKEIGCGKAFKYPSQLQKHQDSHVKLDSVEAFCSEPGCMKYFTNEECLKSHIRSCHQHINCEICGSKHLKKNIKRHLRTHDEDSSPGEIKCEVEGCSSTFSKASNLQKHMKAVHDDIRPFVCGFPGCGMRFAYKHVRNKHENSGYHVYTCGDFVETDEDFTSRPRGGLKRKQVTAEMLVRKRVMPPRFDAEEHETC
Protein: Ataxin-2 homolog (Pab1-binding protein 1) (Poly(A)-binding protein-binding protein) (Q9USW1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in post-transcriptional regulation of gene expression, probably by association with mkt1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum.
Interaction partners:
- Putative ATP-dependent RNA helicase ste13
- Small nuclear ribonucleoprotein-associated protein B
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Post-transcriptional regulator mkt1
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- Cytosolic neutral trehalase
- Inheritance of peroxisomes protein 2
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 1 isoform
Sequence:
MATRSVSMKQTSQRAASPNKTQGAKKWSAVAARGSKIAQSATNDHRNVESIKVVPENRVRGGVAAKATDSSSNVTSLASSEENVSSVSGSAKSNNSQQRVWKTDVAISAEKRTETRQRELRRWMPDPEDAGVPLAGLEESTDNVEWDQFATNEKLFGVKSHFDEDLYTSRIDRSHPKYKEKEQEADRIAKEIEGTVTNNIHIAEERGLKVDDSGLDEEDLYSGVHRSIDVVRNYTRSNAYNKNNKDQKPKNHEAPHQHPQQKVVPPDDPAIVSHRHLALPRAPGPDSRAAERFFNARRKAGPLSRREKEGQIKEFMQFSQSLKIGSLDSKQPSSTKSVAEVKVADEKQLPDASSQATPADSKEPRKEEAEKPVTSATEVSSEKVEKVDGNTSSPSKEEEKPSTEPEKPSVVTQRKETTGTKLGTKLNAKAISFKPNVAAPVFTPGKFTIPSKPAPVNASRPMMPQQSNNSEASIPSTTPQSPSVVSNGENKPSSSPVFFNGPVSSEKEPILDNFNVFKNVGEEHQGAEQIDKPFSCPPTWNTGPNSLQQTIANSRPEGNSGSAKKAAAANPMIPSIVLPNSAMPSAMPMYPTPTMPYIPVGYPVPGYTPYMRNPSQHTSVAPSPNGTPTSGNSSTVGSPMIGYMAPQFIPPYAMPQFPPSGNGRGASAPATYFVPQMGGMMAYTMNGVPPMYGQYAPNNGMMNMHYPMYGDSRRSNSQRSFNSSNGKRSNVHKNNNASNTFSHSNASTSSSLNAAPNTTAKSSSQTAPPVSKGDATEKTEKDASANQEAKP
Protein: Muscle-derived protein 62 (Q9I8F3)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MSSFQEVPSSANALQTSNFAHVIFQNVAKSYLPNTHLECHYTLTQFIHPHQKDWVGIFKVGWSTARDYYTFLWSPMPENYVEGPTVNCVLNFQGYYLPNDDGEFYQFCYVTHKGEIRGASTPFQFRTSSPVEELLTMEDEGNSDMLVVTTKAGLLEFKIEKIVKEKEELLKVTSVLEKETAQLRDQVERLEKELNLEKQRCDQLQTEQKTNIQASESLKTENDDLKKKHDEVASKVLQLEEDIMTVTQKAIAKETELDSMKDKLKKVMLEKEQLECVLKTEKDEKELYKIHLKNTEIENTKLVKEIETFKNLDANKENMISYYKEEVGRLQLFIAEKENMKKAFLLTSSNKEDAAILKEQLRKAEDQIQASKQEAVLMSKELSDAVNVRDKTMADLHSARLENEKLKKQLADALAELKKITALKNEQETSNTTEQELRREVEDLKLRLQMAADHYKEKFKECQKLQKQVNKFTEQAKIVGNQQKLTDASNTVTATAIVTDKKLPASPVSPISSDVVSEFMVKEQVREMNKEIAEKTEEK
Protein: Uncharacterized protein (Q5AK01)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase PP2A-like PPG1
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase 2A activator 1
- Serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase
- Transcription elongation factor SPT5
- Protein phosphatase 2A structural subunit
- Serine/threonine-protein phosphatase SIT4
Sequence:
MAFELPQLDSELRTELEVIIQNKTFDESKSQLQWNDGILPKLITRLNELAALSKDGDRFGNPKGIDFIAEIEATNETITHHLAEQMSSSPPFTIHRLAELIVDPNSQGYTITNNDQLFKYFNSLKKVCIVSSRISEFPPVRIGNETNGHDKKESIGLVAENVSLVEIPWLKTSKKDEVTHATINDSPPLKRKGEEEDCIVPKKGKS