wanglab/gogpt-training-data huggingface dataset:
Protein: Lipase EstA (Lipase A) (EC 3.1.1.3) (Triacylglycerol lipase) (P37957)
Organism: Bacillus subtilis (strain 168)
Function: Active toward triacylglycerides with a preference for esters with C8:0 acyl groups; barely active on C18:1 or C18:4 substrates. Active against p-nitrophenylesters with fatty acid chain lengths from C6 to C18.
Subcellular location: Secreted {ECO:0000269|PubMed:11583117, ECO:0000269|PubMed:8396026}.
Interaction partners:
- Putative hydrolase YdeN
- Extracellular esterase EstB
- Diacylglycerol kinase
- Processive diacylglycerol beta-glucosyltransferase
- Uncharacterized carboxylesterase nap
- Biofilm-surface layer protein A
- Carboxylesterase
- Uncharacterized acyl--CoA ligase YhfT
- Long-chain-fatty-acid--CoA ligase
- Long-chain-fatty-acid--CoA ligase
Sequence:
MKFVKRRIIALVTILMLSVTSLFALQPSAKAAEHNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDKTGTNYNNGPVLSRFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVTLGGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQIHGVGHIGLLYSSQVNSLIKEGLNGGGQNTN
Protein: Transcription initiation factor IIA subunit 1 (General transcription factor IIA subunit 1) (dTFIIA-L) [Cleaved into: Transcription initiation factor IIA alpha chain (TFIIA p30 subunit); Transcription initiation factor IIA beta chain (TFIIA p20 subunit)] (P52654)
Organism: Drosophila melanogaster (Fruit fly)
Function: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor IIA subunit 2
- Maternal gene required for meiosis, isoform H
- Protein tramtrack, alpha isoform
- Transcription initiation factor IIA subunit 2-2
- TATA-box-binding protein
- General transcription factor IIE subunit 1
- Transcription initiation factor IIB
- General transcription factor IIF subunit 2
- Transcription initiation factor IIE subunit beta
- Moonshiner
Sequence:
MALCQTSVLKVYHAVIEDVITNVRDAFLDEGVDEQVLQEMKQVWRNKLLASKAVELSPDSGDGSHPPPIVANNPKSHKAANAKAKKAAAATAVTSHQHIGGNSSMSSLVGLKSSAGMAAGSGIRNGLVPIKQEVNSQNPPPLHPTSAASMMQKQQQAASSGQGSIPIVATLDPNRIMPVNITLPSPAGSASSESRVLTIQVPASALQENQLTQILTAHLISSIMSLPTTLASSVLQQHVNAALSSANHQKTLAAAKQLDGALDSSDEDESEESDDNIDNDDDDDLDKDDDEDAEHEDAAEEEPLNSEDDVTDEDSAEMFDTDNVIVCQYDKITRSRNKWKFYLKDGIMNMRGKDYVFQKSNGDAEW
Protein: SEC7 domain-containing protein (Q584G7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Coatomer subunit gamma
- Vesicle tethering protein Uso1/P115-like head domain-containing protein
- Coatomer subunit alpha
- ADP-ribosylation factor GTPase activating protein 1, putative
- Coatomer subunit beta
- ADP-ribosylation factor GTPase activating protein, putative
- Coatomer subunit beta'
- Coatomer subunit epsilon
- ER lumen protein-retaining receptor
- Coatomer subunit zeta
Sequence:
MIGSSATTVSCSNDVCSRANERWDEDRLAVATHVQSLLVAIRSNERFGAKARFLGSSDVVEHVLLRRLRALQRKIVTPCLVRPITEEAILLPFCDIWISEEMSYTIIGTAMTSLSNLIDLRCTFITVKGIQRVLELAQRSVGGSEDDLTYEDLLLRKLKLCVSCVKHPCARALPETFFVDVVRLAFVIAMHPDTSLLLRCIAKEAMKDTATAMYGFIIENISSYNLGQGSTDGVENFQAHESCVDFQLTGVPMLRYVCSLIDGTVSEIKEGRFSPGMFGSAADSSLVRKVQLEGLHLAQSILFVVKDHLCMPECGNLLYSVQHNLCRALLVAGVGTEDIGLLSQIFPTVHTVVKVASFHLLPQTYSFLKVLHLDPLVRIGSDLNTNSTSSRVGSVTTSSQRPSPAAQMSVSKMLDLCEKRELILESLVGFCTDANFAVFCYAQYDLSRRFLPLLEHMCSLLVENCFNITNSNVPLEGGKPGHNGLTNDVEVGTPLTRMDALALEAIKGLLWQVSQVAPPQRFHGDSNMAAMINARITEKNMLVELASLFRTNALKSGIPFLLEKAIRLPAGSLKGVETGSIGCDVPMLILEEPAGGREVGACLYRLSGLLDKRALGDYLGELGREPPEPDPDEGEHYQAALAAWMEDRKDDHLKLGTVRYHQEQLKGFLQSFDFRGKSLLSSIRETAYHMCMPGEAQKIDRVMEVFSRTWLEANRGEGKDINPFQSEQGPFILGFSLIMLNTDQHSGKMSKPMTQEDFRRMHRDSDGGGSLPEEYLRAVFEDVKAHPIIMAEMMDVGFSNDVTWRLEMRPSEAVESRKSDPFTRVSMQAVSPNALESCEVEALRPFILRMIWSYCLTAFGNTLVGCTKSVFATQKDSTQETGAEGGDVIPQLATPEYAYNCALDGLCLLAKAARDRGMASVVDRVILTILSQLPLDLENVGSTIPQLSTQPSALLCLEKVFRVLDECVHDVLDAWEKLGRLFSNFFLLGMFSRDVVDSPETVTLRAELYANPCAGAEEIGDTQPDGGWLSTLWGSPNTQNRTKELRLQREQETMERVKALLPTLEELLNMIDGLDVDSHGRFFSVLCEEVRHKLRQKDGGRLSTHLLVLITEIAVRRPAEQTILDRYIKLCQQTASHYFTAHEHLDDADLYRNNISEDGESSSRLYAPTTERFGVSFGAGASPASFDFFEEWLTSTTRVVKAVLRALVCFASNAESRHVFSPLLDLLMAAPPNVFKVAVAADLSLTLLELTQEAPRLVNPPYNLSLNGVLSALSLSFTTCPSPVVQKRVQSALSFVVREALYDSLSESDDIVNVLVTCALQSSRMQEEYPASADTTWPRTNVKPSDVPEQGELVESFIGSLVTVCHRFAINHALRDAPADNAKGPAVWIIALKGLSNLVVMSRHSRDRNMALLCLQRCLLDLEIGSLSADTVVLVYENVIFPLVEQTCASPSDSPATLGERCDQNDGCQGGHATDKVLPQILPKQFSVTSILSSLAPAPPSRRAAQSAAAAAAQRSQGGRDKHREVVDLKCRVVSLLSKVFLHYAKLMGENPVVLRDLWQRVLGTLCALYTSLSEESGTGLPGGEAATLDVPAFNGPRRIGAMAEDNAVLREAIQEAVKNMIYVLASILVGTGSTLEAVEAQQFWTSTKNLLRTFDFAEQLLVFIDNLEGT
Protein: Aspartate aminotransferase 3, chloroplastic (EC 2.6.1.1) (Protein YELLOW-LEAF-SPECIFIC GENE 4) (Transaminase A) (P46644)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Amino acid aminotransferase important for the metabolism of amino acids and Krebs-cycle related organic acids. No activity with D-Asp or D-Ala as amino donors. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:14754918}. Note=accumulates in stromules, which are membrane-bound protrusions of the plastid envelope containing soluble stroma. Stromules are often found connecting plastids within a cell.
Interaction partners:
- Asparagine synthetase 1
- Asparagine synthetase 2
- 4-hydroxyphenylpyruvate dioxygenase
- Asparagine synthetase 3
- Arogenate dehydrogenase 1, chloroplastic
- Arogenate dehydrogenase 2, chloroplastic
- L-lactate dehydrogenase
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 2
- Thiosulfate/3-mercaptopyruvate sulfurtransferase 1, mitochondrial
- Malate dehydrogenase, chloroplastic
Sequence:
MKTTHFSSSSSSDRRIGALLRHLNSGSDSDNLSSLYASPTSGGTGGSVFSHLVQAPEDPILGVTVAYNKDPSPVKLNLGVGAYRTEEGKPLVLNVVRKAEQQLINDRTRIKEYLPIVGLVEFNKLSAKLILGADSPAIRENRITTVECLSGTGSLRVGGEFLAKHYHQKTIYITQPTWGNHPKIFTLAGLTVKTYRYYDPATRGLNFQGLLEDLGAAAPGSIVLLHACAHNPTGVDPTIQQWEQIRKLMRSKGLMPFFDSAYQGFASGSLDTDAKPIRMFVADGGECLVAQSYAKNMGLYGERVGALSIVCKSADVAGRVESQLKLVIRPMYSSPPIHGASIVAVILRDKNLFNEWTLELKAMADRIISMRKQLFEALRTRGTPGDWSHIIKQIGMFTFTGLNPAQVSFMTKEYHIYMTSDGRISMAGLSSKTVPHLADAIHAVVTKAV
Protein: DNA mismatch repair protein Msh3 (hMSH3) (Divergent upstream protein) (DUP) (Mismatch repair protein 1) (MRP1) (P20585)
Organism: Homo sapiens (Human)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to 13 nucleotides long. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis.
Interaction partners:
- DNA mismatch repair protein Mlh3
- PMS1 protein homolog 1
- Mismatch repair endonuclease PMS2
- DNA mismatch repair protein Msh6
- DNA mismatch repair protein Mlh1
- DNA mismatch repair protein Msh2
- Sorting nexin-8
- Exonuclease 1
- Structure-specific endonuclease subunit SLX4
- Proliferating cell nuclear antigen
Sequence:
MSRRKPASGGLAASSSAPARQAVLSRFFQSTGSLKSTSSSTGAADQVDPGAAAAAAAAAAAAPPAPPAPAFPPQLPPHIATEIDRRKKRPLENDGPVKKKVKKVQQKEGGSDLGMSGNSEPKKCLRTRNVSKSLEKLKEFCCDSALPQSRVQTESLQERFAVLPKCTDFDDISLLHAKNAVSSEDSKRQINQKDTTLFDLSQFGSSNTSHENLQKTASKSANKRSKSIYTPLELQYIEMKQQHKDAVLCVECGYKYRFFGEDAEIAARELNIYCHLDHNFMTASIPTHRLFVHVRRLVAKGYKVGVVKQTETAALKAIGDNRSSLFSRKLTALYTKSTLIGEDVNPLIKLDDAVNVDEIMTDTSTSYLLCISENKENVRDKKKGNIFIGIVGVQPATGEVVFDSFQDSASRSELETRMSSLQPVELLLPSALSEQTEALIHRATSVSVQDDRIRVERMDNIYFEYSHAFQAVTEFYAKDTVDIKGSQIISGIVNLEKPVICSLAAIIKYLKEFNLEKMLSKPENFKQLSSKMEFMTINGTTLRNLEILQNQTDMKTKGSLLWVLDHTKTSFGRRKLKKWVTQPLLKLREINARLDAVSEVLHSESSVFGQIENHLRKLPDIERGLCSIYHKKCSTQEFFLIVKTLYHLKSEFQAIIPAVNSHIQSDLLRTVILEIPELLSPVEHYLKILNEQAAKVGDKTELFKDLSDFPLIKKRKDEIQGVIDEIRMHLQEIRKILKNPSAQYVTVSGQEFMIEIKNSAVSCIPTDWVKVGSTKAVSRFHSPFIVENYRHLNQLREQLVLDCSAEWLDFLEKFSEHYHSLCKAVHHLATVDCIFSLAKVAKQGDYCRPTVQEERKIVIKNGRHPVIDVLLGEQDQYVPNNTDLSEDSERVMIITGPNMGGKSSYIKQVALITIMAQIGSYVPAEEATIGIVDGIFTRMGAADNIYKGQSTFMEELTDTAEIIRKATSQSLVILDELGRGTSTHDGIAIAYATLEYFIRDVKSLTLFVTHYPPVCELEKNYSHQVGNYHMGFLVSEDESKLDPGAAEQVPDFVTFLYQITRGIAARSYGLNVAKLADVPGEILKKAAHKSKELEGLINTKRKRLKYFAKLWTMHNAQDLQKWTEEFNMEETQTSLLH
Protein: Coronatine-insensitive protein homolog 2 (OsCOI2) (Q84QA7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in jasmonate (JA) signaling. Required for jasmonate signaling in plant defense responses (By similarity). Component of SCF(COI1) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including TIFY/JAZ family (By similarity).
Interaction partners:
- Coronatine-insensitive protein homolog 1a
- Coronatine-insensitive protein homolog 1b
- Protein TIFY 3
- Protein TIFY 10b
- Protein TIFY 6b
- Protein TIFY 6a
- Protein TIFY 10a
- Protein TIFY 8
- Protein TIFY 9
- Protein TIFY 11e
Sequence:
MGGEAGERRLGRAMSFGIPDVALGLVMGFVEDPWDRDAISLVCRHWCRVDALSRKHVTVAMAYSTTPDRLFRRFPCLESLKLKAKPRAAMFNLIPEDWGGSASPWIRQLSASFHFLKALHLRRMIVSDDDLDVLVRAKAHMLSSFKLDRCSGFSTSSLALVARTCKKLETLFLEDSIIAEKENDEWIRELATNNSVLETLNFFLTDLRASPAYLTLLVRNCRRLKVLKISECFMLDLVDLFRTAEILQDFAGGSFDDQGQVEESRNYENYYFPPSLLRLSLLYMGTKEMQVLFPYGAALKKLDLQFTFLSTEDHCQLVQRCPNLEILEVRDVIGDRGLEVVAQTCKKLQRLRVERGDDDQGGLEDEHGMVTQVGLMAVAQGCPHLEYWAVHVTDITNAALEAIGTYSSSLNDFRLVLLDREANITESPLDNGVRALLRGCTKLRRFAFYVRPGALSDVGLGYIGEFSKTIRYMLLGNVGESDQGLLQLSTGCPSLQKLELRGCFFSERALAVAVLQLKSLRYLWVQGYKASPNGTDLMAMVRPFWNIEIIAPNQDEVCPDGQAQILAYYSLAGMRSDYPHSVIPLYPSV
Protein: Spermatogenesis-associated protein 33 (Q96N06)
Organism: Homo sapiens (Human)
Function: Plays an important role in sperm motility and male fertility (By similarity). Required for sperm midpiece flexibility and for the localization of sperm calcineurin to the mitochondria (By similarity). Promotes mitophagy as well as acts as an autophagy mediator in male germline cells (By similarity). Links damaged mitochondria to autophagosomes via its binding to the outer mitochondrial membrane protein VDAC2, as well as to key autophagy machinery component ATG16L1 (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8C624}. Nucleus {ECO:0000250|UniProtKB:Q8C624}. Cytoplasm {ECO:0000250|UniProtKB:Q8C624}. Mitochondrion {ECO:0000250|UniProtKB:Q8C624}.
Interaction partners:
Sequence:
MVTHAAGARTFCEEQKKGSTYSVPKSKEKLMEKHSQEARQADRESEKPVDSLHPGAGTAKHPPPAASLEEKPDVKQKSSRKKVVVPQIIITRASNETLVSCSSSGSDQQRTIREPEDWGPYRRHRNPSTADAYNSHLKE
Protein: Possible epoxide hydrolase EphF (Epoxide hydratase) (Arene-oxide hydratase) (P96811)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Epoxide hydrolase EphG
Sequence:
MIALPALEGVEHRHVDVAEGVRIHVADAGPADGPAVMLVHGFPQNWWEWRDLIGPLAADGNRVLCPDLRGAGWSSAPRSRYTKTEMADDLAAVLDGLGVAKVKLVAHDWGGPVAFIMMLRHPEKVTGFFGVNTVAPWVKRDLGMLRNMWRFWYQIPMSLPVIGPRVISDPKGRYFRLLTGWVGGGFRVPDDDVRLYLDCMREPGHAEAGSRWYRTFQTREMLRWLRGEYNDARVDVPVRWLHGTGDPVITPDLLDGYAERASDFEVELVDGVGHWIVEQRPELVLDRVRAFLAAGTEQRD
Protein: Tail assembly protein G (Gene product G) (gpG) (Minor tail protein G) (Tail assembly chaperone) (TAC) (P03734)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Promotes tail assembly by creating a scaffold for the tail tube proteins. Tail assembly proteins G and GT probably wrap the linear tape measure protein to create a tail assembly scaffold. This allows the polymerization of the tail tube protein, during which G and GT are released, therefore they are absent in the mature virion. The tail assembly protein GT is produced by a rare -1 ribosomal frameshift. The ratio of translated G/GT is about 20, and this ratio is important for proper tail assembly.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04134}.
Interaction partners:
Sequence:
MFLKTESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQKTQMPSMNEAVKQIEQEVLTTWPTEAISHAENVVYRLSGMYEFVVNNAPEQTEDAGPAEPVSAGKCSTVS
Protein: Lens epithelium-derived growth factor (Q5XXA9)
Organism: Gallus gallus (Chicken)
Function: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O75475}.
Interaction partners:
- Histone-lysine N-methyltransferase
- Pogo transposable element derived with ZNF domain.
- Serine/arginine-rich splicing factor 1
- Prefoldin subunit 3
- Cleavage and polyadenylation specificity factor subunit 6
Sequence:
MSRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKMPIFFFGTHETAFLGPKDIFPYSENKDKYGKPNKRKGFNEGLWEIDNNPKVKFSHQPSHPAVNTSIKETIQESSPEAAEGSEEKSGAKRRKPSIPKLPPKGDNNSPAEAEAEEKEMHSTKEDEEPSEKNSKEGVVKTNDASIPKVARRGRKRKAEKQAESEEAAVVATAAVVAAAAAPVTVSPKVSPKRGRPAVSEVKVPKPRGRPKLVKPSCLSESDPVNEEEKAKKKGPDEKPKKQGKKDEEGQKEEEKPKKEYDKKDGKKEAEPKRKNAAKLGSASASDSEDEGGEEEGDKKKKGGRSFQSTHRRNIMRGQHEKEVTERKRKQEEQGESELQNKEEGKKTEVKKMEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVSMQQAQKHTEMILTLKKIRKFKVSQVIMEKSTMLYNKFKTMFLVGEGDSVLSQVLNKSLAEQKQHEEANKTKEQWKKGTNKKNEKEKDQTGSKIVNGGSETQDTNQSQHNGENAEEKDKLEVASKKKTCGEESELEKPAKESAFENK
Protein: Putative exopolyphosphatase (ExopolyPase) (EC 3.6.1.11) (Metaphosphatase) (O14094)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Degradation of inorganic polyphosphates.
Interaction partners:
- Pentatricopeptide repeat-containing protein 1
- ATP synthase subunit e, mitochondrial
- Vacuolar protein sorting-associated protein vps901
Sequence:
MKLGRFLENGREQIRNLLLNASTVSSAPSFSFVSGNESADLDSCASSIVYAYCLQRKQLGRIVVPFFNIPRKELRLRPELSYLLNLASISSDDIVFLDDIVKLPKRIFSNPIYLVDHNSLDRKDLENFNGSIAGIIDHHKDEGGSLHADPRIIEECGSCCTLVCRYFMPVIRSLYDSKVSELHQTATNLAVLALGPILIDTGNLKNEKTTDTDVKIVNDLCSFVPKDWVRDEFFDTLKEKKKSCKGFSFDDLLRRDLKQYFPDGIVVNYASVGKGLDWIKKKRLGWEDELKSFAEVQNSDLVIVGLSLSKNDEFGRQLILYKRTERGAGLADSFLKLSKQNLGLEIIEEKDNGDLSMWNQRNSAASRKKVVPLLMDSVKQVASK
Protein: Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) (Q15181)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Potassium-transporting ATPase alpha chain 1
- Potassium-transporting ATPase alpha chain 2
- Phospholysine phosphohistidine inorganic pyrophosphate phosphatase
- Potassium-transporting ATPase subunit beta
- Inorganic pyrophosphatase 2, mitochondrial
- ATP synthase F
- Adenine phosphoribosyltransferase
- Myosin phosphatase Rho-interacting protein
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
Sequence:
MSGFSTEERAAPFSLEYRVFLKNEKGQYISPFHDIPIYADKDVFHMVVEVPRWSNAKMEIATKDPLNPIKQDVKKGKLRYVANLFPYKGYIWNYGAIPQTWEDPGHNDKHTGCCGDNDPIDVCEIGSKVCARGEIIGVKVLGILAMIDEGETDWKVIAINVDDPDAANYNDINDVKRLKPGYLEATVDWFRRYKVPDGKPENEFAFNAEFKDKDFAIDIIKSTHDHWKALVTKKTNGKGISCMNTTLSESPFKCDPDAARAIVDALPPPCESACTVPTDVDKWFHHQKN
Protein: ATP-dependent DNA helicase DDX31 (EC 5.6.2.-) (DEAD box protein 31) (Helicain) (Probable ATP-dependent RNA helicase DDX31) (EC 3.6.4.13) (Q9H8H2)
Organism: Homo sapiens (Human)
Function: Probable ATP-dependent RNA helicase (By similarity). Plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:23019224}. Note=Colocalized with NPM1 in the nucleoli. {ECO:0000269|PubMed:23019224}.
Interaction partners:
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- Pumilio homolog 3
- Nucleolar complex protein 2 homolog
- Probable RNA-binding protein 19
- Probable ATP-dependent RNA helicase DDX56
- ATP-dependent RNA helicase DDX24
- RNA-binding protein 34
- Probable ATP-dependent RNA helicase DDX10
- Ribosome biogenesis protein BOP1
- Probable ATP-dependent RNA helicase DDX52
Sequence:
MAPDLASQRHSESFPSVNSRPNVILPGREGRREGLPPGGGTRGSLVPTRPVPPSPAPLGTSPYSWSRSGPGRGGGAGSSRVPRGVPGPAVCAPGSLLHHASPTQTMAAADGSLFDNPRTFSRRPPAQASRQAKATKRKYQASSEAPPAKRRNETSFLPAKKTSVKETQRTFKGNAQKMFSPKKHSVSTSDRNQEERQCIKTSSLFKNNPDIPELHRPVVKQVQEKVFTSAAFHELGLHPHLISTINTVLKMSSMTSVQKQSIPVLLEGRDALVRSQTGSGKTLAYCIPVVQSLQAMESKIQRSDGPYALVLVPTRELALQSFDTVQKLLKPFTWIVPGVLMGGEKRKSEKARLRKGINILISTPGRLVDHIKSTKNIHFSRLRWLVFDEADRILDLGFEKDITVILNAVNAECQKRQNVLLSATLTEGVTRLADISLHDPVSISVLDKSHDQLNPKDKAVQEVCPPPAGDKLDSFAIPESLKQHVTVVPSKLRLVCLAAFILQKCKFEEDQKMVVFFSSCELVEFHYSLFLQTLLSSSGAPASGQLPSASMRLKFLRLHGGMEQEERTAVFQEFSHSRRGVLLCTDVAARGLDLPQVTWIVQYNAPSSPAEYIHRIGRTARIGCHGSSLLILAPSEAEYVNSLASHKINVSEIKMEDILCVLTRDDCFKGKRWGAQKSHAVGPQEIRERATVLQTVFEDYVHSSERRVSWAKKALQSFIQAYATYPRELKHIFHVRSLHLGHVAKSFGLRDAPRNLSALTRKKRKAHVKRPDLHKKTQSKHSLAEILRSEYSSGMEADIAKVKKQNAPGEPGGRPLQHSLQPTPCFGRGKTLKWRKTQKGVQRDSKTSQKV
Protein: Protein PPP1R35 homolog (Protein Rcd4) (Reduction in Cnn dots 4 protein) (Q9VLM6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participates in the later stages of centriole assembly through the interaction with Ana3 leading to the centriole to centrosome conversion in somatic cells.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:32543652}. Note=Localizes to the more distal part of the lumen of the centriole. Recruited into zone I during interphase after the formation of the cartwheel at the end of mitosis (PubMed:32543652). The Rcd4 recruitment to the daughter centriole is dependent on Ana3 (PubMed:32543652). {ECO:0000269|PubMed:32543652}.
Interaction partners:
- Protein rotatin homolog
Sequence:
MPHKRRNRVHANQRNFTARRVSVAKLSSAPPNVLVESCNGSHADNSSPDSPKAKEGAMTNGKNPEIKLAVPKCNTTVRKQNEAHIISNIKLDMNLNKDSNFIAPQITKKMNFAPNRVVFGVLVPLNVNDSVLVPHNRKPDALKHTSKESESCKAISEPQLADYAEKVDPMIMAVKEPVLHLDWEPGPFDFFGAYRRTYN
Protein: Elongator complex protein 4 (A0A1W2PNW2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XSSTLKVEPCSLTPGYTKLLQFIQNIIYEEGFDGSNPQKKQRNILRIGIQNLGSPLWGDDICCAENGGNSHSLTKFLYVLRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESFIGSERETNPLYKDYHGLIHIRQIPRLNNLICDESDVKDLAFKLKRKLFTIEAEVQKGVSTATFLLDGPRKKLFPCLFQLLEVACIPWLMASSSVFKASNIGIGGRVCGLFQT
Protein: SSD domain-containing protein (O61894)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- O-acyltransferase
- Sulfotransferase domain-containing protein
Sequence:
MKLRIRNPSGILQEYLAHLFYQYGLFIYDRPRFFTLGPLILTIIFSFGILNMRTEDDLRFLYSPEHSLSREEYQVHKDFSGDSKNNSFVSITIQTSSEDKNLLKKDLAQKLIQLNKYVLEKMEIQVDGKIINFGKEVCSRMKQCELSNTIATIFLDTFWSEKLRKDPRIKIEYPTMKFFDNKFFLPTHFYGVQPGGPLGIESIDMVHFVYQIPAYNEHTSEEMSKIFEQSLTALLENQTTFDTSMFSLSILKDEMQKNSTYTMPFISLTILLLLCFTVASCMTDNWVTSKPIEAMIGILVSSMAIVSAGGLLFALGVPFINQVTVMPFIALAIGVDDVYVMLGAWQDTRRTLDAKKRMGLALEEAGSAITVTSLTSVLSFGIGTYSTTPAIAIFCKFIALAIMFDWFYQLTFFAAVMAMGAKREAAGYHCVFVWKRCDREEIAKAKNENAISPTRYFFENIFAPFICRPSVRFCMLNLYVVYIAIAFYGCSQLTPNLTPSQLVVDDSPLVPYLNLAEKKIWAEGLIGRIYVNNAPDFSKNPEMVDRMLQMVNELESTPYSMGPNSTNFWLNEFNNYRQFFFQEDAKFYETLKSFLKVSFNSHWETDLVWDTPDKSSKGGTKVEKFVFTTAFKISNWNIRTSLLLTWRNITSSYPEFDALVFDENNFYSDQMLELQSTILSSLGTAIILLSAICIMFIAESYIVFWVVCTLISMDIGTAGLLSLWGADLDPMTVVNILMSIGQCIDFATHVGIRIYRSEYSDPDERIRDAMGAIGWPVVQAGTSTLLAIVVMLMVPSSAVRMFARTSVLVVGTGFFHGLIILPIIVRSFATNAKALAPSNH
Protein: Altered inheritance of mitochondria protein 19, mitochondrial (P40502)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Protein FUN14
- Mitochondrial hydrolase YKR070W
Sequence:
MSAKPATDDAKDELLSPFRRLYALTRTPYPALANAALLASTPVLSPSFKVPPTQSPALSIPMSRVFSKSSTARIGITTKTALFFSTMQAIGAYMIYDNDLENGAGFIATWSALYLIVGGKKSFSALRYGRTWPLVLSSVSLANAVLYGQRFLATGFQ
Protein: 10 kDa heat shock protein, mitochondrial (Hsp10) (10 kDa chaperonin) (Chaperonin 10) (CPN10) (P26772)
Organism: Rattus norvegicus (Rat)
Function: Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P61604}.
Interaction partners:
- 60 kDa heat shock protein, mitochondrial
- Stress-70 protein, mitochondrial
- ATP-dependent Clp protease proteolytic subunit
- Uncharacterized protein.
- Heat shock 70 kDa protein 4
- GrpE protein homolog
- GrpE protein homolog 1, mitochondrial
- Mitochondrial disaggregase
- Lon protease homolog, mitochondrial
- T-complex protein 1 subunit alpha
Sequence:
MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD
Protein: PTS system, IIA component (A0A0H2US90)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MDRRNKMTEEMEYICFQLIANSGAAKSSFIEAIQLAKAGNLKEAKIKVEEAEDSLVEAHKIHSNLIQKEATGEKIGFSLLFMHAEDQMASTEIIQLLSKEFIDLYQNK
Protein: Keratin-associated protein 10-8 (High sulfur keratin-associated protein 10.8) (Keratin-associated protein 10.8) (Keratin-associated protein 18-8) (Keratin-associated protein 18.8) (P60410)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 10-9
- Keratin-associated protein 10-5
- Keratin-associated protein 12-3
- Keratin-associated protein 10-4
- Keratin-associated protein 10-11
- Keratin-associated protein 10-7
Sequence:
MADACCTRTYVIAASTMSVCSSDVGHVSRVSSPSTCTGSSWQVDNCQESCCEPRSCASSCCTPSCCAPAPCLALVCAPVSCEPSPCQSGCTDSCTPSCCQQSSCQPACCTSSPCQQACCVPVCCKSNCCKPVCCVSICSGASSPCCQQSSCQSACCTFSPCQQACCVPICCKPICCVPVCSGASSLCCQKSSCQPACCTTSCCRPSSSVSLLCRPVCRPACCVPVPSCCVPASSCQPSCCHPASCLSFLCRPACSRLAC