wanglab/gogpt-training-data huggingface dataset:
Protein: THO complex subunit 2 (Q09779)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- THO complex subunit Tho3
- Uncharacterized protein P25A2.03
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- Uncharacterized RNA-binding protein C106.12c
- mRNA export protein mlo3
- THO complex subunit tho5
- THO complex subunit tho7
Sequence:
MTSLPEKDQQGEVSVSENQKKLSEEWEPYIDKLVASNRTRDERVESIQELFQKCVIEEKLPVDIFFSIFSLAFERLEEKNTLASYVIDTLWLFDTEWIKNFHEGSHDKAEKRLVSIGKGLKEFLPEEWLLSRLDCKFLENINVVPNGDFLNRKIVRTNTSLLYRQKKFNLLREESEGFSHLMINFFDALTCLRNKSLNEDYLIVQVNKSIISTIGAFDLDPNKVLDLILLLFSENLLDSWRFFLSILRNSPWGPNKERKFWNQLPDREKETFLNNLSNANGIFNFDERFTNTKSIMSQVLGHNLQYMYKEDDENLESYFMMVALLIKYNFISIDNIWAHLSPSDEELGKELGKYKDKLDEQTFKAKGNALTMAAPLPDDEIEDGETMDGQKAEAVPEIKKAKPSQKLGLLKSLLSIGDLSSSLLILGRYPFLLRAYPELSNLYHKLLHISISSIYANYSPLKLLPNDVRERLKQPKFIPEDSRLREITLRPPKEKNLVFSLDPFADRFNKTESEVFYYFENYDEDIPILRNLTEFYNIAIPWLRLSGLALCHDPVIVTKLCRIGQKCVDNSSESRTLWLDIIRSLLLPLITLIDVNTGLSYELFELLSKFDSSTRYALYGEWSSTSMKKFPELKLQNSITEKETKGILRRLTKTNVKQFGRLLAKVCHSNPCTVFSIALNQIETYDNLVEVVVDSARFITALDFDALTFIILSSFSNEFKKRLKSDGTSIAHWLQGLASFCGRVFRRYSSLDCTSIVEYVIKQFKVNQMFDLVILKELLSQMTGLQPWTNLSDNQIQGAAGGPVLRQLSLSLIYENPDVVRKSSMRLFNTLQKNGLATQLLVLLSQKYSTCIYDVTDENSHLKLISSLQDECSDVLYLLMEFLNMVCSPKSYYKLIPSFEQLIQDFHIQPQVAFYLSRYKNLDHSLTGSNTEDAMDIDYENTSSPNTASNPVWSIDNSVITELLPKQIWDYFSPNFYLTFWKLSLYDVFVPLERYEFERSRAFDQIRQTDAANTFYSRHRHDRQKIMQLSNSLQNELKEHINSLESVRKVLQGDCVKWFIPNGVFPNGTRLEHARFNCARYLWTLCIAPRLKMSPHDALYCAKFVKLLHSLGTPNFSTMSFLEILFNSQLPSFIFSMTQREADNFGRFLYEVLYDITSWYRDKILYERECLANGALPGFRLYWSDEQNDPDLSAVLPYNKFVLLFSKWHKYLTSYFESCLLSTEYMHIYNSVIILEKILPCFPLIIESGSALKRAAERLKDEEKREDLKVLALGYFAKLSKKQPEWVSFNSFSGTVRPSNSEKLQRPQQLSVAATSAVDSKTASISEEQAKIDKQKVALNPSAPEFVPDSTPSDAVASETDNKNLVENKAVEKRVEARSSANERKQEERRRKTTPEGNRRALRTRTPTNEDIQRSDSKLREDQSRDRTPQSRSFTNENNDNLRSVSRHTRREPQQAQNLNARREHESQKSDRWRQNGNVNRNPRVSNNNSTNVSRERSSEANHRTSNDNKRDEVTEGKDKNKRQDISGESNSRQNNAISRAGRSNGSNRGNDSRDADGRRSTHYASNKRPRSSDSQSPSNLREEDERENSRRRARQDDRRDRDSRQQRDRPRDRTSRSAREEKRRKIQ
Protein: Oocyte-expressed protein homolog (Factor located in oocytes permitting embryonic development) (Floped) (Oocyte- and embryo-specific protein 19) (mOEP19) (STAT3 downstream gene and differentiation regulator) (Q9CWE6)
Organism: Mus musculus (Mouse)
Function: As part of the OOEP-KHDC3 scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart. Positively regulates the homologous recombination-mediated DNA double-strand break (DSB) repair pathway by regulating ATM activation and RAD51 recruitment to DSBs in oocytes. Thereby contributes to oocyte survival and the resumption and completion of meiosis. As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics. Required for the formation of F-actin cytoplasmic lattices in oocytes which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18804437}. Nucleus {ECO:0000269|PubMed:29125140}. Note=In the subcortical cytoplasm of early embryos from the 1-cell to the blastocyst stages (PubMed:18804437, PubMed:25208553). From the 2-cell stage, still detected in the subcortex, but excluded from cell-cell contact regions (PubMed:18804437). Expression largely disappears in blastocysts (PubMed:25208553). {ECO:0000269|PubMed:18804437, ECO:0000269|PubMed:25208553}.
Interaction partners:
- KH domain-containing protein 3
- Transducin-like enhancer protein 6
- NACHT, LRR and PYD domains-containing protein 5
- Inactive protein-arginine deiminase type-6
- Zinc finger BED domain-containing protein 3
- NACHT
Sequence:
MASHTADADAKPDSDSQKLLNVLPVSLRLRTRPWWFPIQEVSNPLVLYMEAWVAERVIGTDQAEISEIEWMCQALLTVDSVNSGNLAEITIFGQPSAQTRMKNILLNMAAWHKENELQRAVKVKEVEEFLKIRASSILSKLSKKGLKLAGFPLPLEGRETQMES
Protein: Retroelement silencing factor 1 (Q5DTW7)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of imprinted gene expression, regulates repressive epigenetic modifications associated with SETDB1. Required for the recruitment or accumulation of SETDB1 to the endogenous retroviruses (ERVs) and maintenance of repressive chromatin configuration, contributing to a subset of the SETDB1-dependent ERV silencing in embryonic stem cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:29728365}. Note=Localizes around gamma-tubulin during M phase. {ECO:0000269|PubMed:29728365}.
Interaction partners:
Sequence:
MNWNTKQENVPKPPPYSKTQSSILQHFLMTSTTSQSSFNYSPHNQEASQTSFNYSLHNQEACMYSGNSNSVSQPLLSGRNYITPQTQISVSNMPTRTIVASQSSMERVVSTNGKGPQQPNHNLQTVSSGIMQNVWLPSHTEATISHNPDGGTNMPYMHPPQNQLVTSDTYSMQLQMAPLHSGKVPMTHQGSQGLNHFIPDQLVDWTQYTSNELSYPEYRPPPKQYSYILPATTSLQVKNNQLPTYTQSLQSKHSVPLSSHQYAAEASKRLSALPYSCRYENQHVQNAQPVSKHLPMEVPQSSEVHSSEKKKDTYRGFKQQWQNPNEKVSIGQFSEVKINIKQPYSESVRPSGDGVQALVQNNQEKRKYTYNPNTNQVIDTNATKEKLVRDIKSLVEIKKKFSELARKIKINKSLLMAAGCSKTANTSYTEPIQHSEFSAKEMSAKNGNDCSMELLATCLSLWKNQPSKTTEENVPKPLEEKQCNTSRISTTVVGSANPTNEVHVKSLCSGVGNSQKMMSSSQTVLPVLIPSCESSGVAVGKGTELQIAVVSPLVLSDTNTLPGKDSVPEVLPETLYPVVKEGSVCSLQTQPTETVALPFDVIGAVASNNISAEIPLPVDKEKQHKPIQGDPDIADSSLGKHSPLGTEVLPKPMDSTIVSGPMLQIESICSLAEGDVSYNSQIAEIFNSVQTEPQKPSPNQVIDSQQEQVYDTTENKDFSLQKDKCVQCTDVPHEVPEQPEPLQPEEPASSEYVEANREATEESCREYTGRKESTAKDVCLPAAIQQDPHPRETDMFSKSDHSLPAINEINDESEPISYLHDQLSELLKEFPYGIETFNRHEVSLDQQKTHKIVENQTGGKTSNVSGDSTDQIKITVLNSEQIKELFPEDDQPCDKLAEPENKEIVAEVKSPCDSQIPREESHDLGMLDPEKDKIHCCALGWLSMVYEGVPQCHCSSTEKKEKDQCLDINSSKQGEQPCNSGITIFEINPVSNNSKTPLTQATEEGHFSAVHGEKTKASKTKDNREGQELACHFSAKCYKKDKKGNFKIRHDTSLKMEQKLKNISSKCDIPNPSKCNKIAAPEILHVTTSNSAKNMPFSKQASQESLQKKHTSQDLGPVKAPIELSSNTDPCRSNTSSVQSVSPEKKKLKFKAGGSRLKYFEKRKTDHVIIPDVEIKKKKYEKQEQNKNAGDTLKLCSILTESNERASVQEKTVPSPESSDPKGSSSKSTRVITVQEYLQRQKDKQITGNNASRNICVETVLCDSGHTKTSKHSAAVSWGKLVEGQSISAETAKELEHNSSSHGKDFKIHHSEASRTHSVSNNNKGKFDGKQPDKMFKNKTSMNNESNQMPLQVKEQRKQYLNRVAFKCTERESICLTKLDSASKKLSIEKKSGEYTSKTKDTDKPSMLEFKLCPDVLLKNTSTVDKQDCPGPGPEKEQAPVQVSGIKSTKEDWLKCIPTRTKMPESSQRDSADSRLSKRSLSADEFEILQNPVKESNIMFRTYKKMYLEKRSRSLGSSPVK
Protein: T. brucei spp.-specific protein (Q38BX9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRDTNNHNGSACAFHEGSSQMVDTSFHSTGDGSGAPTQNVQQQEQLPHRTGTGKRRVGGFSPSVAPFALDTQDPTPQQRRTLLGRGGVEAMRRNRQDQMNLSCNEYPDPPPVGVRAPLRHVVRPGSAKHQEQSTTCIDEDTLRRAKARCPQSAQQRMPSFIFGEDPQGPRRTGRAMHAQSYKPTSLW
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A4GW50)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- MOB kinase activator 1A
- MOB kinase activator 2
- Dual specificity protein phosphatase CDC14A
- Cell division cycle 14B
- MOB kinase activator 1B
- Protein S100-B
Sequence:
MAMTAGATTTFPMSSHTRERVTVAKLTLENFYSNLILQHEERETRQKKLEVAMEEEGLADEEKKLRRSQHARKETEFLRLKRTRLGLDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYISETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYRNLTHNPPSDFSFQNMNSKRKAETWKKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGFPPFCSETPQETYRKVMSWKETLAFPPEVPVSEKAKDLILRFCTDSENRIGNGGVEEIKGHPFFEGVDWGHIRERPAAIPIEIRSIDDTSNFDDFPESDILQPVPNTTEPDYKSKDWVFLNYTYKRFEGLTQRGSIPTYMKAGKL
Protein: Bifunctional L-3-cyanoalanine synthase/cysteine synthase (CAS) (EC 2.5.1.47) (EC 4.4.1.9) (O-acetylserine (thiol)-lyase 2) (OAS-TL) (O45679)
Organism: Caenorhabditis elegans
Function: Primarily catalyzes the formation of cyanoalanine and hydrogen sulfide from cysteine and hydrogen cyanide. Can also catalyze, although less efficiently, the formation of cyanoalanine and hydrogen sulfide from either S-sulfocysteine or O-acetylserine and hydrogen cyanide and the formation of cysteine from either S-sulfocysteine or O-acetylserine and hydrogen sulfide. By catalyzing the assimilation of cyanide produced by P.aeruginosa, mediates resistance to infection. Involved in fertility, growth and aging. Does not mediate survival in high levels of hydrogen sulfide.
Interaction partners:
- cystathionine gamma-lyase
- Putative cystathionine gamma-lyase 2
- FAD/NAD
- Adenosylhomocysteinase
- Probable phosphoserine aminotransferase
- Aspartate aminotransferase, cytoplasmic
- Sulfide:quinone oxidoreductase, mitochondrial
- Cysteine dioxygenase 1
- Kynurenine--oxoglutarate transaminase
- Kynurenine--oxoglutarate transaminase
Sequence:
MSRELMVETGGELIGNTPLLKLNKIGKDLGASIAVKVEYMNPACSVKDRIAFNMIDTAEKAGLITPGKTVLIEPTSGNMGIALAYCGKLRGYKVILTMPASMSIERRCLLKAYGAEVILTDPATAVKGAVQRAEELRDVIPNAYILNQFGNPANPEAHYKTTGPEIWRQTQGKVDIVCFGVGSGGTCTGVGRFLKEKNPSVQVFPVEPFESSVINGLPHSPHKIQGMGTGMIPDILDLTLFSEALRVHSDDAIAMAKKLADEESILGGISSGANVCAAVQLAKRPENKGKLIVTTVNSFGERYLSTALYAELRDNAANMKQLNLDDSIKIAKEYLGI
Protein: Bowman-Birk type proteinase inhibitor 1a (LSI-1a) (C0HKB4)
Organism: Lathyrus sativus (White vetchling)
Function: Inhibits trypsin (IC(50)=2.7 nM) and alpha-chymotrypsin (IC(50)=322 nM).
Interaction partners:
Sequence:
GDDVLSACCD
Protein: Myotubularin (EC 3.1.3.95) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Phosphatidylinositol-3-phosphate phosphatase) (Q32PM3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, myofibril, sarcomere {ECO:0000256|ARBA:ARBA00004204}. Late endosome {ECO:0000256|ARBA:ARBA00004603}.
Interaction partners:
Sequence:
MTFRRGSGFHLRLLRENSRLNAALESCRKVNAVMASAPIAPYNSSPLGNSSSQNASRESLKMEPLADVTLLPGEERVIDKDIIYICPYNAAVKGKVFITNYRLYFKNTDSETPVTLNIPLGVISRVEKMGGASSRGENSYGLEITCKDMRNLRFALKQEGHSRRDIFEIIFKYAFPLSHGMQLFAFLSQEKYEENGWNVYEALEEYRRQGLPNNEWRVTFINKNYELCDTYPTILVVPYKATEDDLRKVATFRSRCRIPVMSWFHKENHAVITRCSQPLVGMSGKRNKDDERYLDLIREANGTTKLTIYDARPNVNAVANKATGGGYEGDDAYQNAELVFLDIHNIHVMRESLKKLKDIVYPNVEESHWLSSLESTHWLEHIKLVLSGAIQVADKVSSGSSVMVHCSDGWDRTAQLTSLSMLMLDSYYRTLRGFQVLMEKEWISFGHKFASRIGHGDKNHADQDRSPIFLQFIDCVWQMTKQFPTAFEFNERLLVVILDHLYSCRFGTFLYNCESVRDSNNVRTKTVSLWSYINSDTSLYINPFYTAESSRVLYPVASMRHLELWVTYYIRWNPRIQHQQQSPVEQRYKELLALRDQYLKKLEELQLSDSAPSSTHLTNSSTPNAATPNQHITHLQTPF
Protein: Leucine-rich repeat and fibronectin type-III domain-containing protein 5 (Q96NI6)
Organism: Homo sapiens (Human)
Function: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase delta
- Receptor-type tyrosine-protein phosphatase S
- Disks large homolog 4
- Receptor-type tyrosine-protein phosphatase F
Sequence:
MEKILFYLFLIGIAVKAQICPKRCVCQILSPNLATLCAKKGLLFVPPNIDRRTVELRLADNFVTNIKRKDFANMTSLVDLTLSRNTISFITPHAFADLRNLRALHLNSNRLTKITNDMFSGLSNLHHLILNNNQLTLISSTAFDDVFALEELDLSYNNLETIPWDAVEKMVSLHTLSLDHNMIDNIPKGTFSHLHKMTRLDVTSNKLQKLPPDPLFQRAQVLATSGIISPSTFALSFGGNPLHCNCELLWLRRLSREDDLETCASPPLLTGRYFWSIPEEEFLCEPPLITRHTHEMRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNATRSLVYDNGTLDILITTVKDTGAFTCIASNPAGEATQIVDLHIIKLPHLLNSTNHIHEPDPGSSDISTSTKSGSNTSSSNGDTKLSQDKIVVAEATSSTALLKFNFQRNIPGIRMFQIQYNGTYDDTLVYRMIPPTSKTFLVNNLAAGTMYDLCVLAIYDDGITSLTATRVVGCIQFTTEQDYVRCHFMQSQFLGGTMIIIIGGIIVASVLVFIIILMIRYKVCNNNGQHKVTKVSNVYSQTNGAQIQGCSVTLPQSVSKQAVGHEENAQCCKATSDNVIQSSETCSSQDSSTTTSALPPSWTSSTSVSQKQKRKTGTKPSTEPQNEAVTNVESQNTNRNNSTALQLASRPPDSVTEGPTSKRAHIKPNALLTNVDQIVQETQRLELI
Protein: Initiator protein NS1 (NS1) (EC 3.1.21.-) (EC 3.6.4.12) (NCVP1) (Non-capsid protein NS-1) (Non-structural protein 1) (Non-structural protein NS1) (Q9PZT1)
Organism: Human parvovirus B19 (strain HV) (HPV B19)
Function: Multifunctional protein essential for viral DNA replication, which cooperatively interacts with the viral DNA origin of replication and transactivates several promoters including the viral p6 promoter. Binds the origin of replication and performs an endonucleolytic nick within a conserved sequence in the viral genome, thereby initiating the rolling circle replication (RCR). Participates in the transcriptional regulation the viral p6 promoter that regulates all viral transcripts and the cellular CDN1A or IL6 promoters. Transactivates several host promoters some of which induce the S cell cycle phase for the production of host replicative proteins. Up-regulates the expression of host E2F4 and E2F5 and interacts with both these factors thereby inhibiting the host cell cycle G2/M transition. This arrest promotes apoptosis for viral release.
Subcellular location: Host nucleus {ECO:0000269|PubMed:20890043}.
Interaction partners:
Sequence:
MELFRGVLQVSSNVLDCANDNWWCSLLDLDTSDWEPLTHTNRLMAIYLSSVASKLDFTGGPLAGCLYFFQVECNKFEEGYHIHVVIGGPGLNPRNLTVCVEGLFNNVLYHLVTENVKLKFLPGMTTKGKYFRDGEQFIENYLMKKIPLNVVWCVTNIDGYIDTCISATFRRGACHAKKPRITTAINDTSSDAGESSGTGAEVVPINGKGTKASIKFQTMVNWLCENRVFTEDKWKLVDFNQYTLLSSSHSGSFQIQSALKLAIYKATNLVPTSTFLLHTDFEQVMCIKDNKIVKLLLCQNYDPLLVGQHVLKWIDKKCGKKNTLWFYGPPSTGKTNLAMAIAKSVPVYGMVNWNNENFPFNDVAGKSLVVWDEGIIKSTIVEAAKAILGGQPTRVDQKMRGSVAVPGVPVVITSNGDITFVVSGNTTTTVHAKALKERMVKLNFTVRCSPDMGLLTEADVQQWLTWCNAQSWDHYENWAINYTFDFPGINADALHPDLQTTPIVTDTSISSSGGESSEELSESSFFNLITPGAWNTETPRSSTPIPGTSSGESFVGSSVSSEVVAASWEEAFYTPLADQFRELLVGVDYVWDGVRGLPVCCVQHINNSGGGLGLCPHCINVGAWYNGWKFREFTPDLVRCSCHVGASNPFSVLTCKKCAYLSGLQSFVDYE
Protein: Protein phosphatase 1 regulatory subunit 14A (17 kDa PKC-potentiated inhibitory protein of PP1) (Protein kinase C-potentiated inhibitor protein of 17 kDa) (CPI-17) (O18734)
Organism: Sus scrofa (Pig)
Function: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11517233}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 1 regulatory subunit
- Protein phosphatase 1 regulatory subunit
- Serine/threonine-protein phosphatase
- Ras homolog family member A
- Serine/threonine-protein kinase N1
Sequence:
MAAQRLGKRVLSKLQSPSRARGPGGSPGGLQKRHARVTVKYDRRELQRRLDVEKWIDGRLEELYRGREADMPDEVNIDELLELESEEERSRKIQGLLKSCTNPTENFVQELLVKLRGLHKQPGLRQPSPSGDGSLSPRQDRARTAPP
Protein: Large ribosomal subunit protein bL21m (54S ribosomal protein L49, mitochondrial) (YmL49) (P40858)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL5m
- Small ribosomal subunit protein uS8m
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein uL14m
- Large ribosomal subunit protein bL34m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL30m
- Small ribosomal subunit protein uS15m
Sequence:
MLQLKFIWPVARITPIYRPFTSHPFRNLATSSSISSTKAKTTKTDTTPLKLSNELYAIFKIHNRPYLVTEGDRVILPFKLKQAEVGDILNMTDVTTLGSRNYKLVGHPINTSLYTLKATVVGKTKRAFQTREVTKRRNRRVRHAKSKGDLTILRISELSMN
Protein: Type VI secretion system spike protein VgrG1b (Q9I737)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Part of the H1 type VI secretion system (H1-T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection. Allows the delivery of the Tse7 toxin to target cells where it exerts toxicity through its nuclease domain.
Subcellular location: Secreted {ECO:0000269|PubMed:21325275}.
Interaction partners:
- DNase toxin Tse7
- DUF6484 domain-containing protein
- DUF2169 domain-containing protein
- Immune protein Tsi7
- TIGR02270 family protein
- Protein hcp1
- 3-oxoacyl-ACP synthase
- Type VI secretion system component TssA1
- AAA+ ATPase ClpV1
- OmpA-like domain-containing protein
Sequence:
MALAQQTRLVRVDSPLGAEVLQLQRMEGREELGRPFAYELELISENPDLPLDGLLGKPASLALELHDGSRRHFHGIVAACSQGSGNGQFASYQVTLRPWLWLLTRTSDCRIFQNQKVPDIIKQVFRDLGFSDFEDALSRSYREWEYCVQYRETSFDFVSRLMEQEGIYYWFRHEQSRHILVLSDAYGAHQSPPNYASVPYYPPTLEQRERDHFYDWHMAREVQSGSLSLNDYDFQRPGARLEVRSNIARSHAAADYPLYDYPGEYVQSQDGEQYARTRIEALQARYERVRLRGRARGLGSGHLFKLSGYPREDQNREYLVVGAEYRVVQELYETGGGGVGAQFESELDCIDAGQAYRPLPTTPLPIVRGPQTAVVVGPKGEEIWTDQYGRVKVHFHWDRHDQSNENSSCWIRVSQAWAGKNWGSMQIPRIGQEVIVSFLEGDPDRPIITGRVYNAEQTVPYELPANATQSGMKSRSSKGGTPANFNEIRMEDKKGAEQLFIHAEKNQDIEVENDETHWVGHDRTKTIDHDETVHVKHDRTETVDNNETITIGVDRTEKVGNNEKISIGANRTEDVGSNETISIGVDRTEKVGSNEKISIGANRTEDVGNDETISIGANRSESVGNNETISIGADRSESVGANETIDIGGNQSTSIGKNESRSVGQGRDTSVGKDDSLDVGKSFTLNAGDSITLVTGAASIRMKKDGSIVISGKNITIDGSGAINVKADKNVVVKGRKILQN
Protein: nicotinate phosphoribosyltransferase (EC 6.3.4.21) (Q389I2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cytidyltransferase-like domain-containing protein
- DNA-directed RNA polymerase subunit beta
- Tubulin gamma chain
- nicotinamidase
- NAD+ synthase, putative
Sequence:
MKPIIKSILDTDAYKLHMQQAVFHFYPTIHVVYEFQCRSSENKLGDAADAIREQVDLMRHVALTDDEYAYLSTKRYLKKDYLDWLREYRFKPDQVIIDAVPKTRCNGETNITYRELAITIKGPWVETILWEVPLLAIVCEVVHSKRTQHIGAAEAVEHLNAKLDKLFATYVNGELDMFRVTDFGTRRRYSFDVQEAIVRTLQSHPSFGRNFSGTSNYHLAMKLGLPAVGTQAHEWFQAHQQLSPVLRDFQRVALKQWLLEYPQDLHIALTDCISMDGFLGDFDADLAQAYVGLRHDSGNPYVWGRKAIEHYKRFNIDPKLKTLVFSDSLDLERAAKLHCTFAQESNVMCGIGTQLTCSIPGVQPLSIVIKMTECDGKPVAKISDEPEKTTFRDLDYVQLLGRTFNVELQDMIDAGCGRSAVHHPTQVQ
Protein: Uncharacterized protein YgcP (Q46906)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Ferredoxin-like protein YgcO
- Probable electron transfer flavoprotein-quinone oxidoreductase YgcN
Sequence:
MPLLHLLRQNPVIAAVKDNASLQLAIDSECQFISVLYGNICTISNIVKKIKNAGKYAFIHVDLLEGASNKEVVIQFLKLVTEADGIISTKASMLKAARAEGFFCIHRLFIVDSISFHNIDKQVAQSNPDCIEILPGCMPKVLGWVTEKIRQPLIAGGLVCDEEDARNAINAGVVALSTTNTGVWTLAKKLL
Protein: Pentatricopeptide repeat-containing protein GUN1, chloroplastic (Pentatricopeptide repeat-containing protein At2g31400) (Protein GENOMES UNCOUPLED 1) (Q9SIC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in nuclear gene expression via the retrograde plastid-to-nucleus signaling. Plastid signals that depend on GUN1 can affect photomorphogenesis developments, such as cotyledon opening and expansion, anthocyanin biosynthesis, and hypocotyl elongation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17395793}.
Interaction partners:
- Multiple organellar RNA editing factor 2, chloroplastic
- Magnesium-chelatase subunit ChlH, chloroplastic
- Multiple organellar RNA editing factor 1, mitochondrial
- Tetrapyrrole-binding protein, chloroplastic
- Ethylene-responsive transcription factor ABI4
- Heme oxygenase 1, chloroplastic
- Small ribosomal subunit protein bS1c
- Transcription activator GLK1
- Ferrochelatase-1, chloroplastic/mitochondrial
- Chlorophyll a-b binding protein 3, chloroplastic
Sequence:
MASTPPHWVTTTNNHRPWLPQRPRPGRSVTSAPPSSSASVSSAHLSQTTPNFSPLQTPKSDFSGRQSTRFVSPATNNHRQTRQNPNYNHRPYGASSSPRGSAPPPSSVATVAPAQLSQPPNFSPLQTPKSDLSSDFSGRRSTRFVSKMHFGRQKTTMATRHSSAAEDALQNAIDFSGDDEMFHSLMLSFESKLCGSDDCTYIIRELGNRNECDKAVGFYEFAVKRERRKNEQGKLASAMISTLGRYGKVTIAKRIFETAFAGGYGNTVYAFSALISAYGRSGLHEEAISVFNSMKEYGLRPNLVTYNAVIDACGKGGMEFKQVAKFFDEMQRNGVQPDRITFNSLLAVCSRGGLWEAARNLFDEMTNRRIEQDVFSYNTLLDAICKGGQMDLAFEILAQMPVKRIMPNVVSYSTVIDGFAKAGRFDEALNLFGEMRYLGIALDRVSYNTLLSIYTKVGRSEEALDILREMASVGIKKDVVTYNALLGGYGKQGKYDEVKKVFTEMKREHVLPNLLTYSTLIDGYSKGGLYKEAMEIFREFKSAGLRADVVLYSALIDALCKNGLVGSAVSLIDEMTKEGISPNVVTYNSIIDAFGRSATMDRSADYSNGGSLPFSSSALSALTETEGNRVIQLFGQLTTESNNRTTKDCEEGMQELSCILEVFRKMHQLEIKPNVVTFSAILNACSRCNSFEDASMLLEELRLFDNKVYGVVHGLLMGQRENVWLQAQSLFDKVNEMDGSTASAFYNALTDMLWHFGQKRGAELVALEGRSRQVWENVWSDSCLDLHLMSSGAARAMVHAWLLNIRSIVYEGHELPKVLSILTGWGKHSKVVGDGALRRAVEVLLRGMDAPFHLSKCNMGRFTSSGSVVATWLRESATLKLLILHDHITTATATTTTMKSTDQQQRKQTSFALQPLLL
Protein: Nuclear factor I A (Nuclear factor I/A, isoform CRA_b) (A0A590UK38)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSPGAMRRSLPSTSSTSSTKRLKSVEDEMDSPGEEPFYTGQGRSPGSGSQSSGWHEVEPGMPSPTTLKKSEKSGFSSPSPSQTSSLGTAFTQHHRPVITGPRASPHATPSTLHFPTSPIIQQPGPYFSHPAIRYHPQETLKEFVQLVCPDAGQQAGQVGFLNPNGSSQGKVHNPFLPTPMLPPPPPPPMARPVPLPVPDTKPPTTSTEGGAASPTSPTYSTPSTSPANRFVSVGPRDPSFVNIPQQTQSWYLG
Protein: Glycosylphosphatidylinositol anchor attachment 1 (Q9W464)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Putative GPI-anchor transamidase
- Phosphatidylinositol glycan anchor biosynthesis class T
- LD37974p
- Phosphatidylinositol glycan anchor biosynthesis class S
- GPI ethanolamine phosphate transferase 3
- GPI inositol-deacylase
- Prolyl 3-hydroxylase sudestada1
- GPI mannosyltransferase 2
- Phosphatidylinositol glycan anchor biosynthesis class F
- Peptidoglycan-recognition protein SA
Sequence:
MGLLSDPSISTQSKLVDGLARHVRKVCYALYVAGVAWFFCLALPEFNHGTYLSENALSPGLVYPEIRIDANRLAIQLLEELQRERKDHLSTTPHAWIAAKMNEFGLETHTHNYTLRYPFGGGKEYHGKNIYGILRAPRIASTEGIVFAAPYRAASSVHTDISASVPLLLAFADFARRKNYWAKDLIFLITEQEQLGMQAWLEAYHDGDRELDLSKAYLRPGNLPARAGSLQAALNIEVQDLEIDHVDVRIEGLNGKLPNLDMFNLVQRIMAREGIASGYKQAPRKKRRHSQSHFEQNFRQMLTMLASQSSGVPTGNHGLFHRYRIDALTIAANRRATHATLKGSPGSAAVPLLKAIEGIARSLNNLLERFHQSFFFYVIVSNDRYISIGDYMPALVALVACAFLKAYLTWSTLPATNAELEKAAGWLREHEQEAELEENLEPDKFELPYGSVLIYLTATLLIGFLCNVLPLQQYFLEIPMGAAPLTTSVLSFLSLIGFVLPFVVVLPPGGLELLHVAFLLIYGCALIVIGLLNFALGLFAAVLTVPLVIALETKEENSRSTLRNTIRLATLVMNPMMVVYVIVLAMTFYQFPELPVQKIMLRAATAAMDASAYGLIDSVIYGNWLYFVICTIFLPLWIICWTLSLSKRRDYADYLDFDESPSTSPQPQSKVKTN
Protein: Amino acid transporter (A0A3Q1M3C0)
Organism: Bos taurus (Bovine)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}.
Interaction partners:
Sequence:
MPKQVEVRMHDSHLSAEEPKPRHLGLRLCDKLGKNLLLTLTVFGVILGAVCGGLLRLASPIHPDVVMLIAFPGDILMRMLKMLILPLIISSLITGLSGLDAKASGRLGTRAMVYYMSTTIIAAVLGVILVLAIHPGNPKLKKQLGPGKKNDEVSSLDAFLDLIRNLFPENLVQACFQQIQTVTKKVLVAPPSDEDGNATNAVLSLLNETVTEVPEETQVVIKKGLEFKDGMNVLGLIGFFIAFGIAMGKMGEQAKLMVEFFNILNEIVMKLVIMIMWYSPLGIACLICGKIIAIKDLEVVARQLGMYMITVIVGLIIHGGIFLPLIYFLVTRKNPFSFFAGIFQAWITALGTASSAGTLPVTFRCLEENLGIDKRVTRFVLPVGATINMDGTALYEAVAAIFIAQMNGVVLDGGQIVTVSLTATLASVGAASIPSAGLVTMLLILTAVGLPTEDISLLVAVDWLLDRMRTSVNVVGDSFGAGIVYHLSKSELDTIDSQHRVHEDIEMTKTQSIYDDLKNHRESNSNQCVYAAHNSVIVDECKVPFPFMDIETCI