wanglab/gogpt-training-data huggingface dataset:
Protein: Tigger transposable element-derived protein 4 (Q8IY51)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAEASVDASTLPVTVKKKKSLSIEEKIDIINAVESGKKKAEIAAEYGIKKNSLSSIMKNKDKVLEAFESLRFDPKRKRLRTAFYTDLEEALMRWYRIAQCLNVPVNGPMLRLKANDFAQKLGHNDFKCSNGWLDRFKSRYGLVFRAQPVEATGVPVDPSTVWYQNVLPYYLNDYHPKNVFNIKETGLLYRMLPTNTFAFKGETCSVGKLCKDRITLVVGTNMDGSEKLPLLVIGKKRTPHCFKGLKSLPVCYEANRMAWMTSDVFEQWMRKLDEEFQAQQRRVVIFVESFPAHPEVKNLKSIELAFFPSCLSSKCIAMKQGVIKSLKIKYRHCLIKKFLSSVEGSKEFTFSLLDAVDTLHLCWRAVTPETIVKSYEEAGFKSQKGESDITNAEKDTGLDLVADALGAGVEFPEGLSIEEYAALDDDLETCEAAPNGDSICTKESKSDETGFYTSDEEDDDGSPGTELPLPSKSEAITALDTLKKFLRSQDMNDGLQNSLADLENFINSLSPK
Protein: p-hydroxybenzoic acid efflux pump subunit AaeB (pHBA efflux pump protein B) (P46481)
Organism: Escherichia coli (strain K12)
Function: Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell. Substrates are p-hydroxybenzoic acid (pHBA), 6-hydroxy-2-naphthoic and 2-hydroxycinnamate.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- p-hydroxybenzoic acid efflux pump subunit AaeA
- Protein AaeX
- HTH-type transcriptional activator AaeR
- Nucleoside-specific channel-forming protein Tsx
- Translocation and assembly module subunit TamB
- Protein TsgA
- Outer membrane protein assembly factor BamC
Sequence:
MGIFSIANQHIRFAVKLATAIVLALFVGFHFQLETPRWAVLTAAIVAAGTAFAAGGEPYSGAIRYRGFLRIIGTFIGCIAGLVIIIAMIRAPLLMILVCCIWAGFCTWISSLVRIENSYAWGLAGYTALIIVITIQPEPLLTPQFAVERCSEIVIGIVCAIMADLLFSPRSIKQEVDRELESLLVAQYQLMQLCIKHGDGEVVDKAWGDLVRRTTALQGMRSNLNMESSRWARANRRLKAINTLSLTLITQSCETYLIQNTRPELITDTFREFFDTPVETAQDVHKQLKRLRRVIAWTGERETPVTIYSWVAAATRYQLLKRGVISNTKINATEEEILQGEPEVKVESAERHHAMVNFWRTTLSCILGTLFWLWTGWTSGSGAMVMIAVVTSLAMRLPNPRMVAIDFIYGTLAALPLGLLYFLVIIPNTQQSMLLLCISLAVLGFFLGIEVQKRRLGSMGALASTINIIVLDNPMTFHFSQFLDSALGQIVGCVLAFTVILLVRDKSRDRTGRVLLNQFVSAAVSAMTTNVARRKENHLPALYQQLFLLMNKFPGDLPKFRLALTMIIAHQRLRDAPIPVNEDLSAFHRQMRRTADHVISARSDDKRRRYFGQLLEELEIYQEKLRIWQAPPQVTEPVNRLAGMLHKYQHALTDS
Protein: Polycomb complex protein BMI-1 (Polycomb group RING finger protein 4) (RING finger protein 51) (P35226)
Organism: Homo sapiens (Human)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2.
Subcellular location: Nucleus {ECO:0000269|PubMed:16882984, ECO:0000269|PubMed:9199346}. Cytoplasm {ECO:0000269|PubMed:16882984}.
Interaction partners:
- Chromobox protein homolog 8
- Polyhomeotic-like protein 2
- Polyhomeotic-like protein 1
- E3 SUMO-protein ligase CBX4
- Polycomb group RING finger protein 2
- E3 ubiquitin-protein ligase RING1
- E3 ubiquitin-protein ligase RING2
- Histone-lysine N-methyltransferase EZH2
- Chromobox protein homolog 2
- Chromobox protein homolog 7
Sequence:
MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSGNHQSSFANRPRKSSVNGSSATSSG
Protein: DNA oxidative demethylase ALKBH2 (EC 1.14.11.33) (Alkylated DNA repair protein alkB homolog 2) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2) (Q6P6J4)
Organism: Mus musculus (Mouse)
Function: Dioxygenase that repairs alkylated nucleic acid bases by direct reversal oxidative dealkylation. Can process both double-stranded (ds) and single-stranded (ss) DNA substrates, with a strong preference for dsDNA. Uses molecular oxygen, 2-oxoglutarate and iron as cofactors to oxidize the alkyl groups that are subsequently released as aldehydes, regenerating the undamaged bases. Probes the base pair stability, locates a weakened base pair and flips the damaged base to accommodate the lesion in its active site for efficient catalysis (By similarity). Repairs monoalkylated bases, specifically N1-methyladenine and N3-methylcytosine, as well as higher order alkyl adducts such as bases modified with exocyclic bridged adducts known as etheno adducts including 1,N6-ethenoadenine, 3,N4-ethenocytosine and 1,N2-ethenoguanine (By similarity). Acts as a gatekeeper of genomic integrity under alkylation stress. Efficiently repairs alkylated lesions in ribosomal DNA (rDNA). These lesions can cause ss- and dsDNA strand breaks that severely impair rDNA transcription (By similarity). In a response mechanism to DNA damage, associates with PCNA at replication forks to repair alkylated adducts prior to replication (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16642038, ECO:0000269|PubMed:18519673}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6NS38}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6NS38}. Note=Relocates to the replication foci during S-phase. {ECO:0000250|UniProtKB:Q6NS38}.
Interaction partners:
- Nucleic acid dioxygenase ALKBH1
- tRNA
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4
- Probable RNA/DNA demethylase ALKBH6
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial
Sequence:
MDKFLVRPDLRDLQGGGEEPAPTGGASGDLKSPDWRHLRAEGLSCDYTVLFGKAEADKIFRELEQEVEYFTGALAKVQVFGKWHSVPRKQATYGDAGLTYTFSGLTLTPKPWVPVLERVRDRVCEVTGQTFNFVLVNRYKDGCDHIGEHRDDERELAPGSPIASVSFGACRDFIFRHKDSRGKRPRRTVEVVRLQLAHGSLLMMNPPTNTHWYHSLPIRKRVLAPRVNLTFRKILPTKK
Protein: Probable proteasome subunit alpha type-7 (Macropain subunit C1) (Multicatalytic endopeptidase complex subunit C1) (Proteasome component C1) (Proteinase YSCE subunit 1) (P21242)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- 26S proteasome regulatory subunit RPN6
- 26S proteasome regulatory subunit RPN12
- Proteasome subunit beta type-6
- Ubiquitin carboxyl-terminal hydrolase RPN11
- Proteasome subunit alpha type-3
- 26S proteasome regulatory subunit RPN10
- 26S proteasome regulatory subunit RPN1
- 26S proteasome regulatory subunit RPN8
- Proteasome subunit alpha type-4
- 26S proteasome subunit RPT4
Sequence:
MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQKNVKIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLVDHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAIDFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE
Protein: Sodium/potassium-transporting ATPase subunit alpha (Q6VYM8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGKGSGAEYGDGKKKKKKEQELDELKKEVSMDDHKISLDDLGRRYGVDLARGLTNAKALEVLAREGPNVLTPPPTTPEWVKFCRQLFGGFSLLLWIGAILCFLAYSIQVATEDEPANDNLYLGVVLSAVVIITGCFSYYQEAKSSRIMDSFKNMVPQQALVIREGEKMTINAELVVRGDLVEIKGGDRIPADLRVVSAAGCKVDNSSLTGESEPQTRTPEFTHENPLETRNIAFFSTNCVEGTAHGVVVGTGDHTVMGRIATLASGLETGQTPINMEIEHFIQLITAVAVFLGVSFFILAIILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMAKKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNMIHEADTTEDQSGATFDKSSATWHALSRVAGLCNRAEFKAGQETLPILKRDTAGDASESALLKCIQLSCGCVRSMRERNAKVGEIPFNSTNKYQLSIHEQEDNENGHLLVMKGAPERILDRCSTILIHGQEVPMDANWNEAFQSAYMELGGLGERVLGFCHLPLSPAQFPRGFSFDCEEVNFPIKGLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAERLNIPLSQVNPRDAKACVVHGGDLKDMSAEYLDDLLRNHTEIVFARTSPQQKLIIVEGCQRTGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEISPFLLFIIASIPLPLGTVTILCIDLGTDMVPAISLAYETAESDIMKRQPRCPKTDKLVNDRLISMAYGQIGMIQALAGFFTYFVILAENGFWPETLLGIRLNWDDRANNEVEDSYGQQWTYEQRKIIEFTCHTSFFVSIVVVQWADVIICKTRRNSVFQQGMKNRILIFGLFAETALAAFLSYCPGMDIALRMYPLKVSWWFCALPYSLLIFIYDEVRKLIIRRYPGGWVELETYY
Protein: Ligand-gated ion channel pHCl-C (Q5D6V9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
FDESSSDKEILDLLLEKKRYDKRLLPPVNGTLTVNVNVLLLSLASPDESSLKYEVEFLLNQQWNDPRLQYGNKSHYDFLNALHHHDSIWTPDTYFIMHGDFKDPIIPMHFALRIFRNGTITYAMRRHLILSCQGSLHIFPFDDPKCSFSMESISYEEAQIKYVWKNDEDTLRKSPSLTTLNAYLIKNQTTACDQNSWRGNYSCLQVELTFTRDRAYYFTTVFIPGIILVTSSFITFWLEWNAVPARVMIGVTTMLNFFTTSNGFRSTLPVVSNLTAMNVWDGVCMCFIYASLLEFVCVNYVGRKRPLHNVVYRPGENPVTQPGEKRQNAGAPNEIVACTTCGGSNSPCTHSANNGCATETCFVQVRKKEPPHPIRVAKTIDVIARITFPTAYAIFLIFFFVHYKGFS
Protein: Small ribosomal subunit protein eS8B (40S ribosomal protein S8-B) (RP19) (S14) (YS9) (P0CX40)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
Sequence:
MGISRDSRHKRSATGAKRAQFRKKRKFELGRQPANTKIGAKRIHSVRTRGGNKKYRALRIETGNFSWASEGISKKTRIAGVVYHPSNNELVRTNTLTKAAIVQIDATPFRQWFEAHYGQTLGKKKNVKEEETVAKSKNAERKWAARAASAKIESSVESQFSAGRLYACISSRPGQSGRCDGYILEGEELAFYLRRLTAKK
Protein: Small and basic intrinsic protein 21 (F4J0V0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGRIGLVVTDLVLSFMWIWAGVLVNILVHGVLGFSRTDPSGEIVRYLFSIISMFIFAYLQQATKGGLYNPLTALAAGVSGGFSSFIFSVFVRIPVEVIGSILAVKHIIHVFPEIGKGPKLNVAIHHGALTEGILTFFIVLLSMGLTRKIPGSFFMKTWIGSLAKLTLHILGSDLTGGCMNPAAVMGWAYARGEHITKEHLLVYWLGPVKATLLAVWFFKVVFKPLTEEQEKPKAKSEFCNVFFFYVANSTVSTSSIKSEI
Protein: tRNA (uracil-O(2)-)-methyltransferase (EC 2.1.1.211) (O74516)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- tRNA pseudouridine synthase 4
- tRNA
- tRNA
- tRNA
- tRNA
Sequence:
MKVPAYWKPREPKNALTCDPPVPYDLQSSYQWQSILEHDTCYAAEVFDKMMIELVYHPERTSSVIMRTDIILDSQEDDSILNKQKSVFENLDERYQISRWIDRRIIPRNTNLDATMDQTVVVLHEKLENDRILMYLPHLDKSLEQPYNHLPYYHPAVAGIAFHYKGSSVEVLYLVEKDFQRELSSRLLRTAHMLLLVLHKHCKGAVEGYQKRMLHDTVVERNKFQDTYVILKDKYAKQLVDNWVEKTDPGKHVFEDLAIAAFLIELWKQTYSSNKEFSFVDVGCGNGLLVYLLLMEGYNGYGFDARKRKSWETYPLWVQVKLYEKVLVPYFLHDFETKIPFPQLPAGFTMSAANIHDGRFSENSFLIGNHADELTPYLPILARLNQKCYFMSIPCCVHDLTGAKISWALPKPRNPKHGGRYAMYIEWLMQLSEEVGWNIEVEPLRIPSTRNYALIGRKLLSNDLLHSSLSTDALYDIVEKNHGSQGFFVHAMQVAAANSRSH
Protein: Claudin-22 (Q8N7P3)
Organism: Homo sapiens (Human)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Claudin-23
- Claudin-34
- Tight junction protein ZO-3
- Claudin-16
- Occludin
- Tight junction protein 1
- Claudin-17
- Claudin-20
Sequence:
MALVFRTVAQLAGVSLSLLGWVLSCLTNYLPHWKNLNLDLNEMENWTMGLWQTCVIQEEVGMQCKDFDSFLALPAELRVSRILMFLSNGLGFLGLLVSGFGLDCLRIGESQRDLKRRLLILGGILSWASGVTALVPVSWVAHKTVQEFWDENVPDFVPRWEFGEALFLGWFAGLSLLLGGCLLHCAACSSHAPLASGHYAVAQTQDHHQELETRNTNLKH
Protein: Acrosin-binding protein (Acrosin-binding protein, 60 kDa form) (Proacrosin-binding protein sp32) [Cleaved into: Acrosin-binding protein, mature form (Acrosin-binding protein, 32 kDa form, mature form) (Sp32) (p32)] (Q29016)
Organism: Sus scrofa (Pig)
Function: Acrosomal protein that maintains proacrosin (pro-ACR) as an enzymatically inactive zymogen in the acrosome. Involved also in the acrosome formation (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:15955892, ECO:0000269|PubMed:8144514}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15955892, ECO:0000269|PubMed:8144514}. Note=Appears to be present only in the round spermatids and elongating spermatids. Colocalizes in the acrosome with proacrosin. {ECO:0000269|PubMed:8144514}.
Interaction partners:
- Zona pellucida binding protein 2.
- Acrosin
- Carbohydrate-binding protein AQN-1
Sequence:
MRQLAAGSLLSLLKVLLLPLAPAPAQDANSASTPGSPLSPTEYERFFALLTPTWKAETTCRLRATHGCRNPTLVQLDQYENHGLVPDGAVCSDLPYASWFESFCQFTQYRCSNHVYYAKRVRCSQPVSILSPNSLKEVDTSSEVPITTMTSPVSSHITATGRQVFQPWPERLNNNVEELLQSSLSLGGQEQGQEHKQEHKQEQGQEHKQDEGQEQEEQEEEQEEEGKQEEGQGTEESLEAMSGLQADSEPKFQSEFVSSNPFSFTPRVREVESTPMMMENIQELIRSAQEMDEMGDVYEEENIWRAQSPGSLLQLPHVDALLVLCYSIVENTCVITPTAKAWQYLEDETLGFGKSVCDSLGRRHLAACSLCDFCSLKLEQCHSETNLQRQQCDNSHKTPFISPLLASQSMSIGTQIGTLKSGRFYGLDLYGGLRMDFWCARLATKGCEDNRVASWLQTEFLSFQDGDFPTKICDTEYVQYPNYCAFKSQQCMMRNRDRKVSRMRCLQNETYTVLTQAKSEDLVLRWSQEFSTLTLGQAG
Protein: Putative serine/threonine-protein kinase YPL150W (EC 2.7.11.1) (Q12152)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Putative serine/threonine-protein kinase.
Interaction partners:
- 5'-AMP-activated protein kinase subunit gamma
- SNF1 protein kinase subunit beta-1
- SNF1 protein kinase subunit beta-2
- SNF1 protein kinase subunit beta-3
Sequence:
MVNPVGSSKLEQNNIKSIIGSSYNRLYSQFTSDELTEVGNYKILKQIGEGSFGKVYLALHRPTHRKVCLKTSDKNDPNIVREVFYHRQFDFPYITKLYEVIVTESKVWMALEYCPGKELYDHLLSLRRISLLECGELFAQISGAVYYAHSMHCVHRDLKLENILLDKNGNAKLTDFGFTRECMTKTTLETVCGTTVYMAPELIERRTYDGFKIDIWSLGVILYTLITGYLPFDDDDEAKTKWKIVNEEPKYDAKVIPDDARDLISRLLAKNPGERPSLSQVLRHPFLQPYGSVVLDQTQKILCRQRSGGTQFKSKLERRLLKRLKQSGVDTQAIKQSILKKKCDSLSGLWLLLLAQGKKQENCKYPKRSRSVLSVKKVIESATHNDTNGISEDVLKPSLELSRAASLSKMLNKGSDFVTSMTPVSRKKSKDSAKVLNPTLSKISSQRAYSHSIAGSPRKSNNFLQKVSSFFKSKKSSNSNSNNSIHTNVSESLIASNRGAPSSGSFLKKNSGSIQKSRTDTVANPSRTESIGSLNENVAGAIVPRSANNTTLENKKTSGNEIGLKVAPELLLNEHIRIEEPRLKRFKSSISSEISQTSTGNYDSESAENSRSISFDGKVSPPPIRNRPLSEISQISNDTYISEYSTDGNNSSFKISDTIKPSYIRKGSETTSQYSASSEKMTNGYGRKFVRRDLSIVSTASSTSERSSRTDSFYDITTATPVVTTDNRRNKNNNLKESVLPRFGTQRPWTGKRTYTTSRHGKNARRSSKRGLFKITSSNTDSIIQEVSSSEEEDHNVIYSKGKGLPTPVLQTKGLIENGLNERDEEGDDEYAIHTDGEFSIKPQFSDDVIDKQNHLPSVKAVATKRSLSEGSNWSSSYLDSDNNRRRVSSLLVEDGGNPTA
Protein: Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 subunit 8) (eIF3 p110) (Q99613)
Organism: Homo sapiens (Human)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 1
- Eukaryotic translation initiation factor 3 subunit H
Sequence:
MSRFFTTGSDSESESSLSGEELVTKPVGGNYGKQPLLLSEDEEDTKRVVRSAKDKRFEELTNLIRTIRNAMKIRDVTKCLEEFELLGKAYGKAKSIVDKEGVPRFYIRILADLEDYLNELWEDKEGKKKMNKNNAKALSTLRQKIRKYNRDFESHITSYKQNPEQSADEDAEKNEEDSEGSSDEDEDEDGVSAATFLKKKSEAPSGESRKFLKKMDDEDEDSEDSEDDEDWDTGSTSSDSDSEEEEGKQTALASRFLKKAPTTDEDKKAAEKKREDKAKKKHDRKSKRLDEEEEDNEGGEWERVRGGVPLVKEKPKMFAKGTEITHAVVIKKLNEILQARGKKGTDRAAQIELLQLLVQIAAENNLGEGVIVKIKFNIIASLYDYNPNLATYMKPEMWGKCLDCINELMDILFANPNIFVGENILEESENLHNADQPLRVRGCILTLVERMDEEFTKIMQNTDPHSQEYVEHLKDEAQVCAIIERVQRYLEEKGTTEEVCRIYLLRILHTYYKFDYKAHQRQLTPPEGSSKSEQDQAENEGEDSAVLMERLCKYIYAKDRTDRIRTCAILCHIYHHALHSRWYQARDLMLMSHLQDNIQHADPPVQILYNRTMVQLGICAFRQGLTKDAHNALLDIQSSGRAKELLGQGLLLRSLQERNQEQEKVERRRQVPFHLHINLELLECVYLVSAMLLEIPYMAAHESDARRRMISKQFHHQLRVGERQPLLGPPESMREHVVAASKAMKMGDWKTCHSFIINEKMNGKVWDLFPEADKVRTMLVRKIQEESLRTYLFTYSSVYDSISMETLSDMFELDLPTVHSIISKMIINEELMASLDQPTQTVVMHRTEPTAQQNLALQLAEKLGSLVENNERVFDHKQGTYGGYFRDQKDGYRKNEGYMRRGGYRQQQSQTAY
Protein: Poly(A) polymerase alpha (PAP-alpha) (EC 2.7.7.19) (Polynucleotide adenylyltransferase) (Q61183)
Organism: Mus musculus (Mouse)
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Polyadenylate-binding protein 2
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 2
- pre-mRNA 3' end processing protein WDR33
- Cleavage and polyadenylation specificity factor subunit 3
- Pre-mRNA 3'-end-processing factor FIP1
- Splicing factor U2AF 65 kDa subunit
- Cleavage stimulation factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 4
Sequence:
MPFPVTTQGSQQTQPPQRHYGITSPISLAAPKETDCLLTQKLIETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSKLFEAPNFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKESPDREEFRTMWVIGLVFKKTENSENLSVDLTYDIQSFTDTVYRQAINSKMFELDMKIAAMHVKRKQLHQLLPSHVLQKRKKHSTEGVKLTALNDSSLDLSMDSDNSMSVPSPTSAMKTSPLNSSGSSQGRNSPAPAVTAASVTSIQASEVSVPQANSSESPGGPSSESIPQTATQPAISPPPKPTVSRVVSSTRLVNPSPRPSGNTATKVPNPIVGVKRTSSPNKEESPKKTKTEEDETSEDANCLALSGHDKTETKEQVDLETSAVQSETVPASASLLASQKTSSTDLSDIPALPANPIPVIKNSIKLRLNR
Protein: Elongation factor 2 (EF-2) (EC 3.6.5.-) (Eukaryotic elongation factor 2) (eEF2) (Ribosomal translocase) (Translation elongation factor 2) (P32324)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein uS7
Sequence:
MVAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTRKDEQERGITIKSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVSKEDLYQTFARTVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGWAFTIRQFATRYAKKFGVDKAKMMDRLWGDSFFNPKTKKWTNKDTDAEGKPLERAFNMFILDPIFRLFTAIMNFKKDEIPVLLEKLEIVLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGPADDANCIAIKNCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYVPGKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLTTSETAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEICLQDLEHDHAGVPLKISPPVVAYRETVESESSQTALSKSPNKHNRIYLKAEPIDEEVSLAIENGIINPRDDFKARARIMADDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIKDSVVAAFQWATKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLADPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEIVLAARKRHGMKEEVPGWQEYYDKL
Protein: Complement C1q subcomponent subunit B (P14106)
Organism: Mus musculus (Mouse)
Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
Subcellular location: Secreted.
Interaction partners:
- Complement C1q subcomponent subunit A
- Complement C1q subcomponent subunit C
- Plasma protease C1 inhibitor
- Complement C1s-1 subcomponent
- Complement C1r-A subcomponent
- Complement C1s-1 subcomponent
- Complement C1r-B subcomponent
- Complement C4-B
- Complement C2
- Calreticulin
Sequence:
MKTQWGEVWTHLLLLLLGFLHVSWAQSSCTGPPGIPGIPGVPGVPGSDGQPGTPGIKGEKGLPGLAGDLGEFGEKGDPGIPGTPGKVGPKGPVGPKGTPGPSGPRGPKGDSGDYGATQKVAFSALRTINSPLRPNQVIRFEKVITNANENYEPRNGKFTCKVPGLYYFTYHASSRGNLCVNLVRGRDRDSMQKVVTFCDYAQNTFQVTTGGVVLKLEQEEVVHLQATDKNSLLGIEGANSIFTGFLLFPDMDA