wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein eL22x (Putative 60S ribosomal protein L22-1) (Q9SRX7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein eL42z/eL42y
- Small ribosomal subunit protein eS8y
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL24z
- Large ribosomal subunit protein uL24y
- Large ribosomal subunit protein eL8z
- Large ribosomal subunit protein eL21z/eL21y
Sequence:
MARVGAKSSGAGAKKKGVSFVIDCSKPVDDTILEIATLEKFLQERIKVRGKAGALGNSVSITRYNGKINVNANSNFSKRYLKYLTKKYLKKYNLRDWLRVIASNKDKNVYEVRYFRIDDEVASYEED
Protein: Alpha-1,3/1,6-mannosyltransferase ALG2 (EC 2.4.1.132) (EC 2.4.1.257) (GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase) (Q95SA2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU367136}; Single-pass membrane protein {ECO:0000256|RuleBase:RU367136}.
Interaction partners:
Sequence:
MVRVLFLHPDLGIGGAERLVVDAALALKERGHQVSFLTNHHDSTHCFKETADGTFPVHVVGDWLPRGLFGRFYAICAYLRMLYAAIYASFFMPQREQVDVVVCDLISVCIPVLRFAPHRPKVLFYCHFPDQLLSSREGLLKRLYRLPINWLEEHTIGLADKVLVNSKFTLRVFQDTFRRLSTVPDVLYPSLHTQYFDQMQKKLEQRSALLDEPVHPRVPLNAFIYLDINRYERKKNHALALHSLRLLGDMLPATEFKRCRLIIAGGYDTRCMENVEHFAELEHLTEELKLQDHVVLLRSPTDEEKCRLLFAAHCLLYTPENEHFGIVPLEGMYCSKPVVALNSGGPTETVVNTSTGFLCEKTEKSFGGAMLQLFRDEQLRVKMGDQGHKRVQQKFSFQAFADRLNGIIRDLVPISRESSAKKNK
Protein: Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 (EC 3.6.4.13) (ATP-dependent RNA helicase DHX38) (DEAH box protein 38) (Q92620)
Organism: Homo sapiens (Human)
Function: Probable ATP-binding RNA helicase (Probable). Involved in pre-mRNA splicing as component of the spliceosome.
Subcellular location: Nucleus {ECO:0000269|PubMed:29301961}.
Interaction partners:
- Pre-mRNA-processing factor 17
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-splicing factor CWC25 homolog
- Pre-mRNA-splicing factor SLU7
- G-patch domain and KOW motifs-containing protein
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-processing-splicing factor 8
- Splicing factor YJU2
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
Sequence:
MGDTSEDASIHRLEGTDLDCQVGGLICKSKSAASEQHVFKAPAPRPSLLGLDLLASLKRREREEKDDGEDKKKSKVSSYKDWEESKDDQKDAEEEGGDQAGQNIRKDRHYRSARVETPSHPGGVSEEFWERSRQRERERREHGVYASSKEEKDWKKEKSRDRDYDRKRDRDERDRSRHSSRSERDGGSERSSRRNEPESPRHRPKDAATPSRSTWEEEDSGYGSSRRSQWESPSPTPSYRDSERSHRLSTRDRDRSVRGKYSDDTPLPTPSYKYNEWADDRRHLGSTPRLSRGRGRREEGEEGISFDTEEERQQWEDDQRQADRDWYMMDEGYDEFHNPLAYSSEDYVRRREQHLHKQKQKRISAQRRQINEDNERWETNRMLTSGVVHRLEVDEDFEEDNAAKVHLMVHNLVPPFLDGRIVFTKQPEPVIPVKDATSDLAIIARKGSQTVRKHREQKERKKAQHKHWELAGTKLGDIMGVKKEEEPDKAVTEDGKVDYRTEQKFADHMKRKSEASSEFAKKKSILEQRQYLPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMDAEKFAAFFGNVPIFHIPGRTFPVDILFSKTPQEDYVEAAVKQSLQVHLSGAPGDILIFMPGQEDIEVTSDQIVEHLEELENAPALAVLPIYSQLPSDLQAKIFQKAPDGVRKCIVATNIAETSLTVDGIMFVIDSGYCKLKVFNPRIGMDALQIYPISQANANQRSGRAGRTGPGQCFRLYTQSAYKNELLTTTVPEIQRTNLANVVLLLKSLGVQDLLQFHFMDPPPEDNMLNSMYQLWILGALDNTGGLTSTGRLMVEFPLDPALSKMLIVSCDMGCSSEILLIVSMLSVPAIFYRPKGREEESDQIREKFAVPESDHLTYLNVYLQWKNNNYSTIWCNDHFIHAKAMRKVREVRAQLKDIMVQQRMSLASCGTDWDIVRKCICAAYFHQAAKLKGIGEYVNIRTGMPCHLHPTSSLFGMGYTPDYIVYHELVMTTKEYMQCVTAVDGEWLAELGPMFYSVKQAGKSRQENRRRAKEEASAMEEEMALAEEQLRARRQEQEKRSPLGSVRSTKIYTPGRKEQGEPMTPRRTPARFGL
Protein: Transmembrane O-methyltransferase (EC 2.1.1.6) (Catechol O-methyltransferase 2) (Protein LRTOMT2) (Q8WZ04)
Organism: Homo sapiens (Human)
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (By similarity). Required for auditory function. Component of the cochlear hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity (By similarity).
Subcellular location: [Isoform 1]: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:28504928}. Endoplasmic reticulum {ECO:0000250|UniProtKB:A1Y9I9}. Note=Localized to the cell body of the cochlear hair cells, but is not present in the stereocilia (PubMed:28504928). Present but not restricted to the apical cistern, Hensen's body and the subsurface cistern (By similarity). {ECO:0000250|UniProtKB:A1Y9I9, ECO:0000269|PubMed:28504928}.
Interaction partners:
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Aromatic-L-amino-acid decarboxylase
- Cytochrome P450 1B1
- Dopamine beta-hydroxylase
- Phenylethanolamine N-methyltransferase
- Cytochrome P450 1A1
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Aldehyde dehydrogenase family 3 member B2
- Aldehyde dehydrogenase family 3 member B1
Sequence:
MGTPWRKRKGIAGPGLPDLSCALVLQPRAQVGTMSPAIALAFLPLVVTLLVRYRHYFRLLVRTVLLRSLRDCLSGLRIEERAFSYVLTHALPGDPGHILTTLDHWSSRCEYLSHMGPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEHMVELIVGSSEDVIPCLRTQYQLSRADLVLLAHRPRCYLRDLQLLEAHALLPAGATVLADHVLFPGAPRFLQYAKSCGRYRCRLHHTGLPDFPAIKDGIAQLTYAGPG
Protein: Fem-3 mRNA-binding factor 1 (Q9N5M6)
Organism: Caenorhabditis elegans
Function: Involved in the control of stem cells and sex determination in the C.elegans hermaphrodite germline. May also play a role in the hermaphrodite germline proliferation and oogenesis. Binds specifically to the regulatory region of fem-3 3'-UTR and mediates the sperm/oocyte switch. Negatively regulates gld-3 expression, possibly by directly binding to two sites within the 3'-UTR of gld-3 isoform b. In association with the cye-1/cdk-2 complex, negatively regulates gld-1 expression in the distal germline cells of the mitotic zone. By binding to the 3'-UTR, represses phosphatase lip-1 expression in the distal part of the germline mitotic zone. Suppresses germline tumor formation by preventing the dedifferentiation of secondary spermatocytes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9393998}.
Interaction partners:
- Nanos-type domain-containing protein
- Defective in germ line development protein 3
- Female germline-specific tumor suppressor gld-1
- FOG-1 protein
- Fem-3 mRNA-binding factor 2
- Sex-determination protein fem-3
- Centriolar and ciliogenesis-associated protein hyls-1
- Nanos-type domain-containing protein
- Poly
- Protein glp-1
Sequence:
MDQSKMRYTNQFRKTPQKPTSTEVGNHHTPAHSPMAQHETSMWNFNSLNPYFSMLNMNDGMNYARHQQNHIVTSRPPTPLTDLMSLRSFQSFPNVFMPVSRSRTSSFIQSDTDSSRLEPDDFSQNVRYCSTEIDRNNSSSKNDHLKYSRPALSRNSRSFTRSNNVLPTWSLDSNGEMRSRLSLSEVLDSGDLMKFAVDKTGCQFLEKAVKGSLTSYQKFQLFEQVIGRKDDFLKLSTNIFGNYFVQEIIGMSLTTYDDDNIKRQEKLKNFISSQMTDMCLDKFACRVIQSSLQNMDLSLACKLVQALPRDARLIAICVDQNANHVIQKVVAVIPLKNWEFIVDFVATPEHLRQICFDKYGCRVVQTIIEKLTADSINVDLTSAAQHLRERALQRLMTSVTNRCQELATNEYANYIIQHIVSNDDLAVYRECIIEKCLMRNLLSLSQEKFASHVVEKAFLHAPMELLAEMMDEIFDGYMPHPGTGKDALDIMMFHQFGNYVVQCMLTICCDAVSGRRQTKEGSYDHANSFQVWLKKLHSRVTKERHRLSRFSSGKKMIETLAHLRSTHPIYGLQSSGHESFKTDCFSTASEHDGLELEKNGIEEGNLRLMRTFSP
Protein: Tyrosine-protein phosphatase non-receptor type 5 (EC 3.1.3.48) (Neural-specific protein-tyrosine phosphatase) (Striatum-enriched protein-tyrosine phosphatase) (STEP) (P35234)
Organism: Rattus norvegicus (Rat)
Function: May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 7
- Mitogen-activated protein kinase 3
- mitogen-activated protein kinase
- Receptor-type tyrosine-protein phosphatase R
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 10
- Dual specificity protein phosphatase
Sequence:
MEEKVEDDFLDLDAVPETPVFDCVMDIKPEADPTSLTVKSMGLQERRGSNVSLTLDMCTPGCNEEGFGYLVSPREESAHEYLLSASRVLRAEELHEKALDPFLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYIRGYNGEEKVYIATQGPIVSTVVDFWRMVWQERTPIIVMITNIEEMNEKCTEYWPEEQVVHDGVEITVQKVIHTEDYRLRLISLRRGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAMSLYEKQLSLQSSE
Protein: Tyrosine 2,3-aminomutase (EC 5.4.3.6) (Tyrosine ammonia-lyase) (EC 4.3.1.23) (Q0VZ68)
Organism: Chondromyces crocatus
Function: Has aminomutase and, to a lesser extent, ammonia-lyase activity. Primarily, catalyzes the rearrangement of L-tyrosine to R-beta-tyrosine, which is incorporated into secondary metabolites called chondramides. The aminomutase activity mainly produces R-beta-tyrosine but also S-beta tyrosine in smaller amounts. Does not accept D-tyrosine, L-histidine or L-phenylalanine as substrates.
Interaction partners:
- Urocanate hydratase
- Imidazolonepropionase
- Uncharacterized protein
- Amidohydrolase
- Phosphoenolpyruvate synthase
Sequence:
MKITGSNLSIYDVADVCMKRATVELDPSQLERVAVAHERTQAWGEAQHPIYGVNTGFGELVPVMIPRQHKRELQENLIRSHAAGGGEPFADDVVRAIMLARLNCLMKGYSGASVETVKLLAEFINRGIHPVIPQQGSLGASGDLSPLSHIALALIGEGTVSFKGQVRKTGDVLREEGLKPLELGFKGGLTLINGTSAMTGAACVALGRAYHLFRLALLATADFVQCLGGSTGPFEERGHLPKNHSGQVIVAREIRKLLAGSQLTSDHQDLMKEMVARSGVGNDVVDTGVYLQDAYTLRAVPQILGPVLDTLDFARKLIEEELNSTNDNPLIFDVPEQTFHGANFHGQYVAMACDYLNIAVTEIGVLAERQLNRLVDPNINGKLPPFLASAHSGLLCGFEGGQYLATSIASENLDLAAPSSIKSLPSNGSNQDVVSMGTTSARKSLRLCENVGTIVSTLIAACNQAGHILGNERFSPPIRELHGELSRSVPLYQDDSPIFELFQTVRAFVGGDGFRAHLVTHLDLAATTASS
Protein: Protein kinase A anchor protein nuclear localisation signal domain-containing protein (Q382R1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHLTLGVLTEDEDARTALSEAVENQCLPRFENNDGPLLDVWLGERKLFGLVERVAPNNFLQVTSENGGTAKGESTCADDPHDMRVTDNVSFIIRLSSVPHTSLQPGFTAEDAFVNCTRIVMAYSAQLERGASAELVGSDASAEYMRFTEK
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (C1BH42)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MGVEIETITPGDGQTFPKKGQTCVVHYVGSLTDGTKFDSSRGRGKPFKFKIGKQEVIRGWEEGVGQMSVGQRATLTCTPDFAYGSKGHPGIIPPNSTLIFDVELMGLE
Protein: mRNA interferase toxin MqsR (EC 3.1.-.-) (Endoribonuclease MqsR) (Motility quorum-sensing regulator MqsR) (Toxin MqsR) (Q46865)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Plays a significant role in the control of biofilm formation and induction of persister cells in the presence of antibiotics. An mRNA interferase which has been reported to be translation-independent. It has also been reported to be translation-dependent. Cleavage has been reported to occur on either side of G in the sequence GCU. Also reported to cleave after C in GC(A/U) sequences. There are only 14 genes in E.coli W3110 (and probably also MG1655) that do not have a GCU sequence and thus are resistant to the mRNA interferase activity; among these is the gene for toxin GhoT. Overexpression of MqsR causes cessation of cell growth and inhibits cell proliferation via inhibition of translation as well as increasing persister cell formation; these effects are overcome by concomitant or subsequent expression of antitoxin MqsA. Cross-talk can occur between different TA systems. Ectopic expression of this toxin induces transcription of the relBEF TA system operon with specific cleavage of the relBEF mRNA produced. Regulates the expression of GhoT/GhoS, a type V TA system. Persistence depends on toxin GhoT activity, which MqsR controls at the post-transcriptional level by selectively degrading the antitoxin ghoS segment of the ghoST mRNA. Overexpression leads to a dramatic increase in tolerance to the antibiotic ofloxacin. This TA system mediates cell growth during bile acid deoxycholate stress by degrading mRNA for probable deoxycholate-binding protein YgiS; bile acid detergents such as deoxycholate are important for host defense against bacterial growth in the gall bladder and duodenum.
Interaction partners:
- Antitoxin MqsA
- mRNA interferase toxin RelE
- Antitoxin RelB
- Antitoxin MazE
- Endoribonuclease toxin MazF
- Antitoxin YefM
- Antitoxin DinJ
- Toxin YoeB
- mRNA interferase toxin YafQ
- mRNA interferase toxin HigB
Sequence:
MEKRTPHTRLSQVKKLVNAGQVRTTRSALLNADELGLDFDGMCNVIIGLSESDFYKSMTTYSDHTIWQDVYRPRLVTGQVYLKITVIHDVLIVSFKEK
Protein: Dynein axonemal intermediate chain 2 (Axonemal dynein intermediate chain 2) (A2AC93)
Organism: Mus musculus (Mouse)
Function: Part of the dynein complex of respiratory cilia.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9GZS0}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q4QR00}. Note=Located in the proximal region of respiratory cilia. {ECO:0000250|UniProtKB:Q9GZS0}.
Interaction partners:
- Dynein axonemal heavy chain 5
- Thioredoxin domain-containing protein 3
- Dynein, axonemal, heavy chain 9
- Dynein axonemal heavy chain 11
- Dynein axonemal intermediate chain 1
- Dynein axonemal assembly factor 1
- Outer dynein arm-docking complex subunit 1
- Dynein, axonemal, heavy chain 10
- Dynein axonemal heavy chain 17
- Axonemal dynein light intermediate polypeptide 1
Sequence:
MEIVYVYLKKRSEFGKQCNFSDRQAELNIDILPNPELAALYVERNPVDTGIQCSASMSEHEANTERFEMESCGVNHVEGGWPKDVNPQELEQTIRFRKKVEKDENYINAVMQLGSIMEHCIKQNNAIDIYEEYFDDEEAVEVTEEAPSAKTINVFRDPQEIKRTATHLSWHPDGNRKLAVAYSCLKFQRAPMSMNYDSYIWDLENPNRPEIALKPLSPLVTLEYNPKDSHVLLGGCYNGQIACWDTRKGSLVAELSTIEFSHRDPVYGTIWLQSKTGTECFSASTDGQVMWWDIRKISEPIEVVIMDISRKEQLENALGAISLEFESTLPTKFMVGTEQGIVISCNRKAKTQAEKIVCTFYGHHGPIYALQRNPFYPKNFLTVGDWTARIWSEDSRESSIMWTKYHMAYLSDGAWSPVRPAVFFTTKMDGTLDIWDLVFKQCDPALSLKVCDDPLFCLRVQDNGCLIACGSELGTTTLLEVSSSLSTLQRNEKNIASSIFERETRREKILEARHREMRLKEKGKVEGKEDDQKEEEAALDLDELVGKAEEEFFEVIFSELKRKEAEALKKKPKPRKKSSVKVEAEEEVEENVGEEEEAGGIIGIDAVEDMSEEAGEEQEDVPT
Protein: Large ribosomal subunit protein eL39z/eL39x (60S ribosomal protein L39-1) (P51424)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein eL29z
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein eL29y
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL6z/uL6y
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein eL24y
- Large ribosomal subunit protein eL28z
Sequence:
MPSHKSFMIKKKLGKKMRQNRPIPHWIRLRTDNTIRYNAKRRHWRRTKLGF
Protein: Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) (P9WFU1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phenylalanine--tRNA ligase alpha subunit
- Leucine--tRNA ligase
- Isoleucine--tRNA ligase
- Small ribosomal subunit protein uS2
- GMP synthase
- Alanine--tRNA ligase
- DNA-directed RNA polymerase subunit beta
- Putative methyltransferase Rv1407
- Tyrosine--tRNA ligase
- Threonine--tRNA ligase
Sequence:
MRLPYSWLREVVAVGASGWDVTPGELEQTLLRIGHEVEEVIPLGPVDGPVTVGRVADIEELTGYKKPIRACAVDIGDRQYREIICGATNFAVGDLVVVALPGATLPGGFTISARKAYGRNSDGMICSAAELNLGADHSGILVLPPGAAEPGADGAGVLGLDDVVFHLAITPDRGYCMSVRGLARELACAYDLDFVDPASNSRVPPLPIEGPAWPLTVQPETGVRRFALRPVIGIDPAAVSPWWLQRRLLLCGIRATCPAVDVTNYVMLELGHPMHAHDRNRISGTLGVRFARSGETAVTLDGIERKLDTADVLIVDDAATAAIGGVMGAASTEVRADSTDVLLEAAIWDPAAVSRTQRRLHLPSEAARRYERTVDPAISVAALDRCARLLADIAGGEVSPTLTDWRGDPPCDDWSPPPIRMGVDVPDRIAGVAYPQGTTARRLAQIGAVVTHDGDTLTVTPPSWRPDLRQPADLVEEVLRLEGLEVIPSVLPPAPAGRGLTAGQQRRRTIGRSLALSGYVEILPTPFLPAGVFDLWGLEADDSRRMTTRVLNPLEADRPQLATTLLPALLEALVRNVSRGLVDVALFAIAQVVQPTEQTRGVGLIPVDRRPTDDEIAMLDASLPRQPQHVAAVLAGLREPRGPWGPGRPVEAADAFEAVRIIARASRVDVTLRPAQYLPWHPGRCAQVFVGESSVGHAGQLHPAVIERSGLPKGTCAVELNLDAIPCSAPLPAPRVSPYPAVFQDVSLVVAADIPAQAVADAVRAGAGDLLEDIALFDVFTGPQIGEHRKSLTFALRFRAPDRTLTEDDASAARDAAVQSAAERVGAVLRG
Protein: Leukocyte-associated immunoglobulin-like receptor 2 (LAIR-2) (CD antigen CD306) (Q6ISS4)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
- Pulmonary surfactant-associated protein D
Sequence:
MSPHLTALLGLVLCLAQTIHTQEGALPRPSISAEPGTVISPGSHVTFMCRGPVGVQTFRLEREDRAKYKDSYNVFRLGPSESEARFHIDSVSEGNAGLYRCLYYKPPGWSEHSDFLELLVKESSGGPDSPDTEPGSSAGTVPGTEASGFDAP
Protein: Endonuclease I (EC 3.1.21.2) (Gene product 3) (Gp3) (Junction-resolving enzyme gp3) (P00641)
Organism: Escherichia phage T7 (Bacteriophage T7)
Function: Junction-resolving enzyme that selectively binds and cleaves four-way (Holliday) DNA junctions present after viral genomic replication. These intermediates are created during DNA repair, processing of stalled replication forks and homologous genetic recombination. Introduces two nicks on the two non-crossing strands, at 5' sides of the junction. Participates also together with gp6 in the degradation of host chromosome to provide nucleotides for phage DNA synthesis.
Interaction partners:
Sequence:
MAGYGAKGIRKVGAFRSGLEDKVSKQLESKGIKFEYEEWKVPYVIPASNHTYTPDFLLPNGIFVETKGLWESDDRKKHLLIREQHPELDIRIVFSSSRTKLYKGSPTSYGEFCEKHGIKFADKLIPAEWIKEPKKEVPFDRLKRKGGKK
Protein: Prolyl endopeptidase (EC 3.4.21.-) (F4I2A0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Acylamino-acid-releasing enzyme
- Probable carboxylesterase 7
- Probable glutamyl endopeptidase, chloroplastic
- Dipeptidyl peptidase IV-like protein
- Probable carboxylesterase 12
- Methylesterase 2
- Methylesterase 3
- Alpha/beta-Hydrolases superfamily protein
- Serine carboxypeptidase-like 50
- Alpha/beta hydrolase domain-containing protein WAV2
Sequence:
MLTAFASHARSHVFAFVTVPTITRRLRINILRQSPLSSSLLLNETFSNRPNSVSRRCYCSSSAIMGSSSVFGEQLQYPATRRDDSVVDDYHGVKIGDPYRWLEDPDAEEVKEFVQSQVKLTDSVLEKCETKEKLRQNITKLIDHPRYDSPFRQGDKYFYFHNTGLQAQSVLYMQDNLDAEPEVLLDPNTLSDDGTVALNTFSVSEDAKYLAYGLSSSGSDWVTIKLMKIEDKKVEPDTLSWVKFTGITWTHDSKGFFYGRYPAPKEGEDIDAGTETNSNLYHELYYHFIGTDQSQDILCWRDNENPKYMFGAEVTDDGKYLIMSIGESCDPVNKLYYCDMTSLSGGLESFRGSSSFLPFIKLVDTFDAQYSVISNDETLFTFLTNKDAPKYKLVRVDLKEPNSWTDVVEEHEKDVLASACAVNGNHLVACYMSDVKHILQIRDLKSGSLLHQLPLDIGSVSDVSARRKDNTFFFSFTSFLTPGVIYKCDLANESPEVKVFREVTVPGFDREAFQAIQVFYPSKDGTKIPMFIVAKKDIKLDGSHPCLLYAYGGFNISITPSFSASRIVLSKHLGVVFCFANIRGGGEYGEEWHKAGSLAKKQNCFDDFISGAEYLVSAGYTQPSKLCIEGGSNGGLLVGACINQRPDLYGCALAHVGVMDMLRFHKFTIGHAWTSDYGCSENEEEFHWLIKYSPLHNVKRPWEQQTDHLVQYPSTMLLTADHDDRVVPLHSLKLLATLQHVLCTSLDNSPQMNPIIGRIEVKAGHGAGRPTQKMIDEAADRYSFMAKMVNASWTE
Protein: Sugar transporter SemiSWEET (F9RBV9)
Organism: Vibrio sp. (strain N418)
Function: The homodimer mediates transmembrane sugar transport down a concentration gradient. Transport is probably effected by rocking-type movements, where a cargo-binding cavity opens first on one and then on the other side of the membrane.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000269|PubMed:25186729}.
Interaction partners:
Sequence:
MALIERIGKALEPLMLVMGLISPLATMPQLYKLYVSHSEHALGLSLTTWLLYSFIALLWTIYGIYHKNPTIWVGNCLGFLMYVAMVVGIIAHTGGTY
Protein: Centrosomal P4.1-associated protein (Centromere protein J) (CENP-J) (Centrosome assembly and centriole elongation protein) (Q569L8)
Organism: Mus musculus (Mouse)
Function: Plays an important role in cell division and centrosome function by participating in centriole duplication. Inhibits microtubule nucleation from the centrosome. Involved in the regulation of slow processive growth of centriolar microtubules. Acts as microtubule plus-end tracking protein that stabilizes centriolar microtubules and inhibits microtubule polymerization and extension from the distal ends of centrioles. Required for centriole elongation and for STIL-mediated centriole amplification. Required for the recruitment of CEP295 to the proximal end of new-born centrioles at the centriolar microtubule wall during early S phase in a PLK4-dependent manner. May be involved in the control of centriolar-microtubule growth by acting as a regulator of tubulin release (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9HC77}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9HC77}. Note=Localized within the center of microtubule asters. During centriole biogenesis, it is concentrated within the proximal lumen of both parental centrioles and procentrioles (By similarity). {ECO:0000250|UniProtKB:Q9HC77}.
Interaction partners:
- Spindle assembly abnormal protein 6 homolog
- SCL-interrupting locus protein homolog
- Serine/threonine-protein kinase PLK4
- Serine/threonine-protein kinase PLK1
- Centrosomal protein of 135 kDa
- Centrosomal protein of 152 kDa
- Centrosomal protein 192
- Serine/threonine-protein kinase PLK2
- Pericentrin
- Abnormal spindle-like microcephaly-associated protein homolog
Sequence:
MFLMPTSSELNSGQNFLTQWMTSPSRAGVILNRGFPILEADDKQAATNVSTSFPAKATHFSNSFSISSEEDSFHEEQKLEAGGPYKPWSENPEAPPVFPSVRKEPIASRQDAPGCQEDNNNDLTPHLESEFKEVANKNPLFKKLEQLKEIQQKKQEQLKRQQLEQLQRLMEEQEKLLTMVSAQHAFPGTLLPDDQSQKHRSPGDLTLPPHSYSNPTQENSCASNVLPDEQSNFCRATQDSVLTSKNASDLFYESQYQEAHVKRNDLKEESPAHPSGEGALPRWEKKMGRSQEGKDVNLQKCGDSSEVVNIDERPIKAAVREKQQTFEDYLEEQIQLEERELRQKQLQEAEGPLLAKTKPKQPFLKRGEGLARFTNAKSKFQKGKESKLASTQSPSEDQPGSKVDRQHLQRKTALINKDLCAETPTVKKDSKARPKAGFASLRQKPKVTKTNMRESLSPPGLKVQTGKKRDGQFRHQVKGERNAHASNKENVPACIKPWDAGCKMWSKTQGRERLPLSTGPVGCVVSRSPIRETDRETESSLDFSLQKKLEIWEREKEKENLELDEFLFLERAADEISFSSNSSFVLRILERDQQICDGHRLSSTPVKAVQQREAQQADPRGQSNCSEIPRYGVAHENESECEAMLLSWGSGSPDGLRELSCKRSMKAFQTSTSEIQSQWDARDDGVANSDSSTESEEQHDITIKPSTEVGDRVFSNREDSPQVCDAKGPIRDTGAQEDKWRDADLDLSDKECSSDESVIVESLNNKVLEPLRLPSSQAGSKIDFDDERSWTDLEENPYEHGVIHREEAIYGTPQTQCHSKSEGCVLDKTIKRKIAPVKKGEDFKCDRRISPPPPSDLMVKFFPSLKPKPKLDSHLENESKLNLSQDQPPEFMVCFIGDSVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYTAAARTFPDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVMERFRLDAWKRAEAMENSPKACQYMMATKKDESMNSSFQFQKSHVSSGVQVEKYKKKYLPAQGNLSRRIKSAPPRDLGSSDKGQAALPREPLQQVNFPDLEYKNKEEKEEEIQGEISHPDGKVEKIYKNGRRVVLFPNGTRKEVSADGKSVTVTFFNGDVKQVMPDERVVYYYAAAQTTHTTYPEGLEVLHFSSGQIEKHFPDGRKEITFPDQTIKTLFADGQEESIFPDGTIVRVQRDGNKIIEFNNGQRELHTAQFKRREYPDGTVKTVYANGHQETKYTSGRVRVKDKDGNVLMDTEM
Protein: Ribosome maturation factor RimM (21K) (P0A7X6)
Organism: Escherichia coli (strain K12)
Function: One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late assembly stage of the 30S ribosomal subunit. An accessory protein needed during the final step in assembly of the 30S ribosomal subunit, for assembly of the head region (the 16S rRNA 3' domain). It may act while Era is associated and before RimP in 30S subunit assembly. Interacts with S19. Essential for efficient processing of 16S rRNA; a deletion mutant accumulates 17S rRNA. Deletions also do not assemble the head-associated ribosomal proteins correctly. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11514519, ECO:0000269|PubMed:9226267}. Note=Binds 30S subunit, but not 70S ribosomes (PubMed:9226267). {ECO:0000269|PubMed:9226267}.
Interaction partners:
- tRNA
- Small ribosomal subunit protein bS16
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein bS6
- Ribosome maturation factor RimP
- Small ribosomal subunit protein uS2
Sequence:
MSKQLTAQAPVDPIVLGKMGSSYGIRGWLRVFSSTEDAESIFDYQPWFIQKAGQWQQVQLESWKHHNQDMIIKLKGVDDRDAANLLTNCEIVVDSSQLPQLEEGDYYWKDLMGCQVVTTEGYDLGKVVDMMETGSNDVLVIKANLKDAFGIKERLVPFLDGQVIKKVDLTTRSIEVDWDPGF