wanglab/gogpt-training-data huggingface dataset:
Protein: Protein CHAPERONE-LIKE PROTEIN OF POR1, chloroplastic (NbCPP1) (G5DBJ0)
Organism: Nicotiana benthamiana
Function: Exhibits holdase chaperone activity involved in the stabilization of POR proteins against photooxidative stress in chloroplasts. Required for chloroplast development.
Subcellular location: Plastid, chloroplast envelope {ECO:0000269|PubMed:24151298}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:24151298}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MATTLISKLTLSSAFLGQQFSSRGNSMRSAPAGLFLRGPRCAATDTPYGGNIPQFPRVNVWDPYKRLGISRDASEEEVWSSRNFLLNQYYNHERSAESIEAAFEKILMASFINRKKTKINLKTRLKKKVEESPPWVQNLLSFVELPPPVIILRRLFLFGFMACWSVMNSTEAGPAFQVAISFGACVYFLNDKTKSLGRAALIGFGALVAGWFCGSLLVPMIPPNLLHPTWSLELLTSLFIYVSLFLGCTFLK
Protein: Trehalose-6-phosphate phosphatase (Trehalose-phosphatase) (Q059G6)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Interaction partners:
Sequence:
MDSMHPDPTPEVPPSLPDLKAQVARLEASHKEKGLPLSGRIIHVMHHLPVEIVRIVPADALESAGTGFLSPPMTPEFKPEDAETTVESADAKWRIHARTAHPALVSGIKSLSETHDQLLVAWTGEVLIQPDNTQSPQQPSQATFSSIASNLLAPFSAGDATPQPQPPPQQGSLMVFGGEFNEADQKEIASELDRFAEAEAKFDPTDRLKYIPVFLPPDVSKGHYEGFCKKTLWPLFHYLLWLDSTATVPSPDPSWLAYQKTNQMFAQRVAQIYKPGDLIICHDYHLLLAPKMIRESLGQVFHPNAGWGTAHPSPSLHHAQRKGFDWESNQQTPTPEKAKGEKIGAFMNHVGTALGNHLGTMEHGLQNEIMIGMFMHTPWPSSEIFRCLPKRREILDGMLGANLVSFQTYSYSRHFVSTCIRVCGYESTPGGVDANGQVTAVGYCPIGIDIKRVVHDRDQPGVLPKMQALRDLYKDKKIIVGREKLDVAKGVYNKLQAFEKFLQVYPEWRGKVVLIQVTTPALSESPKLERMTAELVSHINGTYGSLDFTPVHHYHQALEKDEYFGLLSCADLALITSLRDGMNTTSMEFILCQDKTSKSPLVLSEFMGTAPSFASALQINPHDLLGVAQAINKGLTMRKEEKAERHANLLEGVLAHTSHTWAATILKQLLENVGGEHTAHHTPALDTAQFTDAYKKANKRLLLFDYDGTLTPIVKVPSHAVPTERTRNAIAALCKDPKNVVYLISGRDGDFLEEHWGHLDRLGLSAEHGSFVKQPGEEDFINMTEALDMSWMSEVEEIFKYYTERTTGSTIEVKKASITWHYRNSDPDFGEFQCKQALDLLESSLAPRRPIEVLVGKKNLEVRPLAVNKGEIVRRLMYENPDVDLIFCAGDDKTDEDMFRALRTIFPPGGVVDNNPVVMKPPVAVTSALEPEEVAELPDVELTIRSKGVFATTVGPPAKRTLAGWHVTCPEEVVEAFESLLEEIQVV
Protein: E12/E47 (Q80Z31)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMNQSQRMAPVGSDKELSDLLDFSMMFPLPVANGKSRPASLGGTQFAGSGLEDRPSSGSWGSSDQNSSSFDPSRTYSEGAHFSDSHSSLPPSTFLGAGLG
Protein: Enoyl-[acyl-carrier-protein] reductase [NADH] (ENR) (EC 1.3.1.9) (Q8Z9U1)
Organism: Yersinia pestis
Function: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP).
Interaction partners:
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- 3-oxoacyl-[acyl-carrier-protein] synthase II
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Similar to Escherichia coli 3-oxoacyl-[acyl-carrier-protein] synthase I FabB SW:FABB_ECOLI
- Fatty acid oxidation complex subunit alpha
- Fatty acid oxidation complex subunit alpha
- Acyl-coenzyme A dehydrogenase
- Similar to Escherichia coli aldehyde-alcohol dehydrogenase AdhE SW:ADHE_ECOLI
- Irp1 protein
Sequence:
MIIKPRVRGFICVTAHPTGCEANVKKQIDYVTTEGPIANGPKRVLVIGASTGYGLAARITAAFGCGADTLGVFFERPGEEGKPGTSGWYNSAAFHKFAAQKGLYAKSINGDAFSDEIKQLTIDAIKQDLGQVDQVIYSLASPRRTHPKTGEVFNSALKPIGNAVNLRGLDTDKEVIKESVLQPATQSEIDSTVAVMGGEDWQMWIDALLDAGVLAEGAQTTAFTYLGEKITHDIYWNGSIGAAKKDLDQKVLAIRESLAAHGGGDARVSVLKAVVTQASSAIPMMPLYLSLLFKVMKEKGTHEGCIEQVYSLYKDSLCGDSPHMDQEGRLRADYKELDPEVQNQVQQLWDQVTNDNIYQLTDFVGYKSEFLNLFGFGIDGVDYDADVNPDVKIPNLIQG
Protein: Ubiquitin-conjugating enzyme E2 6 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 6) (Ubiquitin carrier protein 6) (Ubiquitin-conjugating enzyme E2-21 kDa 3) (Ubiquitin-protein ligase 6) (P42750)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 32
- Probable ubiquitin-conjugating enzyme E2 33
- Ubiquitin-conjugating enzyme E2 34
- Ubiquitin-conjugating enzyme E2 5
- Ubiquitin-conjugating enzyme E2 4
- Derlin-1
- Protein OS-9 homolog
- Probable ubiquitin-conjugating enzyme E2 26
- NEDD8-activating enzyme E1 catalytic subunit
- ERAD-associated E3 ubiquitin-protein ligase HRD1B
Sequence:
MASPSKRREMDMMKLMMSDYKVDTVNDDLQMFYVTFHGPTDSLYQGGVWKIKVELPEAYPYKSPSVGFVNKIYHPNVDESSGAVCLDVINQTWSPMFDLINVFESFLPQLLLYPNPSDPFNGEAASLLMRDRAAYELKVKEYCEKYAKPEEILSDDDDDDSMSEDGSDSDDDDDDEIVGKADP
Protein: Double-strand break repair protein MRE11 (EC 3.1.-.-) (P32829)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing.
Subcellular location: Nucleus {ECO:0000269|PubMed:9845372}. Chromosome, telomere {ECO:0000250|UniProtKB:P49959}. Chromosome {ECO:0000250|UniProtKB:P49959}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. {ECO:0000250|UniProtKB:P49959}.
Interaction partners:
- DNA repair protein RAD50
- DNA repair protein XRS2
- Exodeoxyribonuclease 1
- Serine/threonine-protein kinase TEL1
- DNA endonuclease SAE2
- ATP-dependent DNA helicase II subunit 1
- ATP-dependent helicase SGS1
- Serine/threonine-protein kinase MEC1
- ATP-dependent DNA helicase II subunit 2
- DNA repair protein RAD51
Sequence:
MDYPDPDTIRILITTDNHVGYNENDPITGDDSWKTFHEVMMLAKNNNVDMVVQSGDLFHVNKPSKKSLYQVLKTLRLCCMGDKPCELELLSDPSQVFHYDEFTNVNYEDPNFNISIPVFGISGNHDDASGDSLLCPMDILHATGLINHFGKVIESDKIKVVPLLFQKGSTKLALYGLAAVRDERLFRTFKDGGVTFEVPTMREGEWFNLMCVHQNHTGHTNTAFLPEQFLPDFLDMVIWGHEHECIPNLVHNPIKNFDVLQPGSSVATSLCEAEAQPKYVFILDIKYGEAPKMTPIPLETIRTFKMKSISLQDVPHLRPHDKDATSKYLIEQVEEMIRDANEETKQKLADDGEGDMVAELPKPLIRLRVDYSAPSNTQSPIDYQVENPRRFSNRFVGRVANGNNVVQFYKKRSPVTRSKKSGINGTSISDRDVEKLFSESGGELEVQTLVNDLLNKMQLSLLPEVGLNEAVKKFVDKDEKTALKEFISHEISNEVGILSTNEEFLRTDDAEEMKALIKQVKRANSVRPTPPKENDETNFAFNGNGLDSFRSSNREVRTGSPDITQSHVDNESRITHISQAESSKPTSKPKRVRTATKKKIPAFSDSTVISDAENELGDNNDAQDDVDIDENDIIMVSTDEEDASYGLLNGRKTKTKTRPAASTKTASRRGKGRASRTPKTDILGSLLAKKRK
Protein: Large ribosomal subunit protein bL28c (C0H4C3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Ribosomal protein L27, putative
- 40S ribosomal protein S5, putative
- 50S ribosomal protein L19
- Ribosomal protein S16, mitochondrial, putative
- 40S ribosomal protein S11
- 40S ribosomal protein S11, putative
- Mitochondrial ribosomal protein L20, putative
- 40S ribosomal protein S19
- 40S ribosomal protein S18, putative
- 60S ribosomal protein L6, putative
Sequence:
MQITNKIYKLIKYVYILYIIIHSNFIFPKVILTQINKNKTNNILKYPNYFYVISLYRKNVRFKNNNVLNKSVTKFALNTKKRHKEALAIRKYRMTGPSSIKKHYGFGAHKRINKVTMLPHKEIKLPIRRCAILGKMDNWNARKISKSGVRTHRIQRLNLINKRIFFEEENRFIKMKVSAKGLKTIKKYGLAYCIKKFNLDFSKKKYDAGYSSRRRKKKTQELNQTNSERTNVTNENTQQSVEEVDKIMDKLNLDDKKIHKDL
Protein: Proteasome chaperone 3 (Increased recombination centers protein 25) (Q07951)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in 20S proteasome assembly, facilitating the alpha-ring formation.
Interaction partners:
- Proteasome chaperone 4
- Proteasome subunit alpha type-5
- Proteasome chaperone 1
- Proteasome assembly chaperone 2
- Proteasome maturation factor UMP1
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-3
- Proteasome activator BLM10
Sequence:
MISYEFQTHLPKGKDSSLNASSENKELYVQATHFNNTILLQIRLNGEMDSTYEVSSKGLNPILDINVPLAGNLGNTGGDYDDEEEEFVRDHLSDYQVVTKLGDSADPKVPVVCVQIAELYRRVILPEVSGTMAQDNMQFSLLISMSSKIWRATKEQSADDNDFGKLVFVLKCIKDMYAK
Protein: Probable transcriptional regulator (Q9HZ15)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable hydrolase
- Peptidyl-prolyl cis-trans isomerase A
- Probable ATP-binding/permease fusion ABC transporter
- Probable transcriptional regulator
- GbuR
Sequence:
MKAPRVTLDQWRTLQAVVDHGGFAQAAEALHRSQSSISYTVARMQEQLGVPLLRIDGRKAVLTEAGEVLLRRSRQLVKQAGQLEELAHHMEQGWEPEVRLVVDAAYPTARIVRSLSAFMPQSRGCRVLLREEVLSGVEEALIQGAADLAISGLIIPGHLGADLSVVEFVAVAHPDHPLHRLQRELTHQDLETQMQVVIRDSGRLQPRDHGWLGAEQRWTVGSLATAATFVGNGLGFAWLPRHIIERELQSGQLKPLPLSQGGVRQSRFYLYTNKEKPLGPASQILMEMLKSFANVPLNAPFAAPEPAAE
Protein: C-X-C chemokine receptor type 2 (CXC-R2) (CXCR-2) (GRO/MGSA receptor) (High affinity interleukin-8 receptor B) (IL-8R B) (CD antigen CD182) (P35343)
Organism: Mus musculus (Mouse)
Function: Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-X-C motif chemokine 2
- Growth-regulated alpha protein
- Chemokine subfamily B Cys-X-Cys
- C-X-C motif chemokine 5
- Stromal cell-derived factor 1
- C-X-C motif chemokine 3
- C-X-C motif chemokine 15
- C-X-C motif chemokine 13
- C-C motif chemokine 2
- C-C motif chemokine 5
Sequence:
MGEFKVDKFNIEDFFSGDLDIFNYSSGMPSILPDAVPCHSENLEINSYAVVVIYVLVTLLSLVGNSLVMLVILYNRSTCSVTDVYLLNLAIADLFFALTLPVWAASKVNGWTFGSTLCKIFSYVKEVTFYSSVLLLACISMDRYLAIVHATSTLIQKRHLVKFVCIAMWLLSVILALPILILRNPVKVNLSTLVCYEDVGNNTSRLRVVLRILPQTFGFLVPLLIMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLVFLLCWLPYNLVLFTDTLMRTKLIKETCERRDDIDKALNATEILGFLHSCLNPIIYAFIGQKFRHGLLKIMATYGLVSKEFLAKEGRPSFVSSSSANTSTTL
Protein: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A, B subunit, B' delta isoform) (Protein RTS1) (Protein SCS1) (P38903)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7565713}. Nucleus {ECO:0000269|PubMed:7565713}.
Interaction partners:
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Protein phosphatase PP2A regulatory subunit A
- Shugoshin
- Spindle assembly checkpoint serine/threonine-protein kinase BUB1
- Protein phosphatase methylesterase 1
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase PP1-1
- Spindle assembly checkpoint component MAD3
Sequence:
MMRGFKQRLIKKTTGSSSSSSSKKKDKEKEKEKSSTTSSTSKKPASASSSSHGTTHSSASSTGSKSTTEKGKQSGSVPSQGKHHSSSTSKTKTATTPSSSSSSSRSSSVSRSGSSSTKKTSSRKGQEQSKQSQQPSQSQKQGSSSSSAAIMNPTPVLTVTKDDKSTSGEDHAHPTLLGAVSAVPSSPISNASGTAVSSDVENGNSNNNNMNINTSNTQDANHASSQSIDIPRSSHSFERLPTPTKLNPDTDLELIKTPQRHSSSRFEPSRYTPLTKLPNFNEVSPEERIPLFIAKVDQCNTMFDFNDPSFDIQGKEIKRSTLDELIEFLVTNRFTYTNEMYAHVVNMFKINLFRPIPPPVNPVGDIYDPDEDEPVNELAWPHMQAVYEFFLRFVESPDFNHQIAKQYIDQDFILKLLELFDSEDIRERDCLKTTLHRIYGKFLSLRSFIRRSMNNIFLQFIYETEKFNGVAELLEILGSIINGFALPLKEEHKVFLVRILIPLHKVRCLSLYHPQLAYCIVQFLEKDPLLTEEVVMGLLRYWPKINSTKEIMFLNEIEDIFEVIEPLEFIKVEVPLFVQLAKCISSPHFQVAEKVLSYWNNEYFLNLCIENAEVILPIIFPALYELTSQLELDTANGEDSISDPYMLVEQAINSGSWNRAIHAMAFKALKIFLETNPVLYENCNALYLSSVKETQQRKVQREENWSKLEEYVKNLRINNDKDQYTIKNPELRNSFNTASENNTLNEENENDCDSEIQ
Protein: Uncharacterized protein (Q553N9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Probable mitochondrial Rho GTPase gemA
- Translocase of outer mitochondrial membrane
- Mitofilin
- Glutathione S-transferase domain-containing protein
- Translocase of outer mitochondrial membrane
- SMP-LTD domain-containing protein
- Uncharacterized transmembrane protein DDB_G0283573
- Bacterial surface antigen
Sequence:
MSDSSEFLEKHQQDILNQLNNLKEKIENLENKMETIEDTQVQQPTEEITQIKDDIIVVDDAQKTIEQEEIKKEEPENDESSEEITQQQQQVEEQEEVKQEEPVVEQQQKEDEIKQEEPIVEEPIVEEPIVEQQQEEEVKQEEPIVEEPIVEEPIVEQQVEEIKQDEPIVKEPIVEQQEEKEEEEVKQTQEETTTVTESVVVTETVITEEEKNETTITTATTTTTTTEQPTIEQQQQEEEESRPVIESEPIVVVEATEQPTVEEESDEEDKKETNENDKSSSNDNNNNNNDKQEEQKEQTNGKNEKDEEEEKEKDNKKDKEEEEVEKEDENILSQAELANFYKLEGNEYFKHNIYFDAIESYSKAISIKPSHLLYSNRSISYYKFGLFAESLQDALESIKLEANWVKGYHRAGQALEKLNQKDEAIKYYEKGLLIEPDHQPMRDALDSILNVGKEDQKGENTSSDSESDSESDSEEESESDSESDSDSDDSDDDDDNTSNQNKSIVPYGPVAKVAIATSIVGAIALGFYLITKLKK
Protein: Uncharacterized protein (Q57Z69)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAQHSEASDPGSSLRWVLYEDVYYAAIVVPAEEAPVDVPADNQFVYFLGSESGSVVPLTAVEPFDMNNQERMNHPAAAAGVAVAKQLIMGTGSGENESADGDNEWTARPSREKRTKKGKERKATGKKRDGAAVPLKKTRKNARIMDNEDDYTASSSDERNSGTSEGSEESSFSREDEEEEEGVGLGHWREIEKSLGFTPTSKGKKGSNATKNTSRRGFSSPSERRPGDYVGFFDSCAGSPVAPFVAEINYYHRKAVDEAKASDCALNLQQSALIRAVEARLVALRAEVLHLRRLIRDAESENEEQLETEELKNIRNRIKFLEDSFSVEEIVKQELHMEKITPPQHERKRRRAATQLFSFVDTSFGYLLDAASATALPRESAAALLDVYGSQKRERERFVASKQGLGKLGLRAPKASVMENWRRSREMIVLDPMSDKRPVSRRFSQTLRKVDQRARECYNAASHKTNDIIPRQRRPTTIYNFNDLRFENERHSESCMEDGVDLVGYNALGLGFNVTTDTAVAIDADADIPVLSPLKTSFDPRATFIIDASATAPDSLAAQQHGYYSAQCSQTLRLPSQESLWGRSEVPDAAGCDATMASQHMRSISRTGRSLSRAGSMSRASSRASSVMWDATSGTSRKHGRSNASSVARGSRNAGDWRSSAKRVILEQLTLYLRGLRGKPAVLNKEDFSHTAKELLGRALKAESKRKGISLSLQATNLRATLEKDVETRLRKSVDNYVLRHFVNNQVPNRHKSVDIDSGSHASKHRSETRRREDDGEENRTTIINEDRETDSPVYDQ
Protein: Ceramide synthase 1 (CerS1) (LAG1 longevity assurance homolog 1) (Longevity assurance gene 1 protein homolog 1) (Protein UOG-1) (Sphingoid base N-stearoyltransferase CERS1) (EC 2.3.1.299) (P27544)
Organism: Homo sapiens (Human)
Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward stearoyl-CoA (octadecanoyl-CoA; C18:0-CoA). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively. Plays a predominant role in skeletal muscle in regulating C18 ceramide and dihydroceramide levels with an impact on whole-body glucose metabolism and insulin sensitivity. Protects from diet-induced obesity by suppressing the uptake of glucose in multiple organs in a FGF21-dependent way (By similarity). Generates C18 ceramides in the brain, playing a critical role in cerebellar development and Purkinje cell function (By similarity). In response to cellular stress mediates mitophagy, a known defense mechanism against cell transformation and aging. Upon mitochondria fission, generates C18 ceramides that anchor lipidated MAP1LC3B/LC3B-II autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24782409}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAAAGPAAGPTGPEPMPSYAQLVQRGWGSALAAARGCTDCGWGLARRGLAEHAHLAPPELLLLALGALGWTALRSAATARLFRPLAKRCCLQPRDAAKMPESAWKFLFYLGSWSYSAYLLFGTDYPFFHDPPSVFYDWTPGMAVPRDIAAAYLLQGSFYGHSIYATLYMDTWRKDSVVMLLHHVVTLILIVSSYAFRYHNVGILVLFLHDISDVQLEFTKLNIYFKSRGGSYHRLHALAADLGCLSFGFSWFWFRLYWFPLKVLYATSHCSLRTVPDIPFYFFFNALLLLLTLMNLYWFLYIVAFAAKVLTGQVHELKDLREYDTAEAQSLKPSKAEKPLRNGLVKDKRF
Protein: Large ribosomal subunit protein eL24A (60S ribosomal protein L24-A) (L30) (RP29) (YL21) (P04449)
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:
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein uL30A
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL8B
- Large ribosomal subunit protein uL18
Sequence:
MKVEIDSFSGAKIYPGRGTLFVRGDSKIFRFQNSKSASLFKQRKNPRRIAWTVLFRKHHKKGITEEVAKKRSRKTVKAQRPITGASLDLIKERRSLKPEVRKANREEKLKANKEKKKAEKAARKAEKAKSAGTQSSKFSKQQAKGAFQKVAATSR
Protein: Kinesin-like protein KIF11-B (Kinesin-5) (Kinesin-related motor protein Eg5-1) (XLEg5K1) (XlEg5) (P28025)
Organism: Xenopus laevis (African clawed frog)
Function: Plus end-directed motor protein required for establishing a bipolar spindle. Associates with both interphase and spindle microtubules. May be involved in nuclear divisions taking place during the development of unfertilized eggs. Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface (By similarity).
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Note=Concentrated around the polar ends of both meiotic and mitotic spindles.
Interaction partners:
Sequence:
MSSQNSFMASKKEDKGKNIQVVVRCRPFNQLERKASSHSVLECDSQRKEVYVRTGEVNDKLGKKTYTFDMVFGPAAKQIEVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSSDEEFTWEQDPLAGIIPRTLHQIFEKLSENGTEFSVKVSLLEIYNEELFDLLSPSPDVGERLQMFDDPRNKRGVIIKGLEEISVHNKDEVYHILERGAARRKTASTLMNAYSSRSHSVFSVTIHMKETTVDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHIPYRESKLTRILQDSLGGRTKTSIIATVSPASINLEETVSTLDYANRAKSIMNKPEVNQKLTKKALIKEYTEEIERLKRELAAAREKNGVYLSSENYEQLQGKVLSQEEMITEYTEKITAMEEELKSISELFADNKKELEECTTILQCKEKELEETQNHLQESKEQLAQESFVVSAFETTEKKLHGTANKLLSTVRETTRDVSGLHEKLDRKKAVDQHNFQVHENFAEQMDRRFSVIQRTVDDYSVKQQGMLDFYTNSIDDLLGASSSRLSATASAVAKSFASVQETVTKQVSHSVEEILKQETLSSQAKGDLQQLMAAHRTGLEEALRSDLLPVVTAVLDLNSHLSHCLQNFLIVADKIDSHKEDMNSFFTEHSRSLHKLRLDSSSALSSIQSEYESLKEDIATAQSMHSEGVNNLISSLQNQLNLLGMETQQQFSGFLSKGGKLQKSVGSLQQDLDLVSSEAIECISSHHKKLAEQSQDVAVEIRQLAGSNMSTLEESSKQCEKLTSSINTISQESQQWCESAGQKIDSVLEEQVCYLHSSKKHLQNLHKGVEDSCGSSVVEITDRVNAQRQAEEKALTSLVEQVRDDQEMVGEQRLELQEQVQSGLNKVHSYLKEELRNDVPTGTTPQRRDYAYPSLLVKTKPRDVLLEQFRQQQQEYLESISSVISEAVEPPVEQDSLEDEPPVAVNDSVISERSCIDLSMTCQEKGGIRFFQQKKALRKEKENRGNTTLLERSKIMDEVDQALTKSKLPLRMQN
Protein: HCG2043421, isoform CRA_c (RNA binding protein, mRNA processing factor) (cDNA FLJ61582, highly similar to RNA-binding protein with multiple splicing) (B4E3T4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNNGGKAEKENTPSEANLQEEEVRTLFVSGLPLDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVSFDSRSEAEAAKNALNGIRFDPEIPQTLRLEFAKANTKMAKNKLVGTPNPSTPLPNTVPQFIAREPYELTVPALYPSSPEVWAPYPLYPAELAPALPPPAFTYPASLHAQVIDTHRPGLHSLHHQSFQTWFPRAHHTTNTYPANRSTLKRLMIPSKSS
Protein: Ferritin (EC 1.16.3.1) (A0A0B4KI27)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ferritin
- Cytoplasmic aconitate hydratase
- Protein Malvolio
Sequence:
MVKLIASLLLLAVVAQAYGDFKCALSKQESKSFVRELQREREEHQLKEKQNLSHEGQDQECKGSLAVPEITKDWVDMKDACIKGMRNQIQEEINASYQYLAMGAYFSRDTVNRPGFAEHFFKAAKEEREHGSKLVEYLSMRGQLTEGVSDLINVPTVAKQEWTDGAAALSDALDLEIKVTKSIRKLIQTCENKPYNHYHLVDYLTGVYLEEQLHGQRELAGKLTTLKKMMDTNGELGEFLFDKTL
Protein: Calcium permeable stress-gated cation channel 1 (Transmembrane protein 63c) (X1WEM4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as an osmosensitive calcium-permeable cation channel (By similarity). Required for the functional integrity of the kidney glomerular filtration barrier.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8CBX0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transmembrane protein 234
- Si:ch1073-111c8.3.
- R3H domain and coiled-coil-containing 1.
- Uncharacterized protein.
- Striatin-interacting protein 1 homolog
- Golgin A3
Sequence:
MAFESWPAGGVRPVEELDVRSFLMEENSTAERCYRSHSRSSVLQGLPFGGVPTVLAINVVLWLILLLIFSCLRKAAWDYGRLALLMKNDSLTSLFYGEQSEKEKTPSDSSPSDSETKDMGFCSWLTSLYHMKDEEIRSKCGIDAVTYLSFQRHIILLMMVVCLLSLTIILPVNLSGNLLGDNPENFGRTTVVNVPAQNIFLWLHSIFALLYFVITVLCMAHHSSRLEYREDEKVARTLMITSIPREISDPGLITKHLHEAYPSCTVTDIHFCFNVQKLMKLDSERRKAMKGRLYFTTKAQKNGRIMIKTHPCAQIFCCDICGFEKVDAEQYYSELEEKLTDEFNAEKNWISMKRLGIAFVTFRDERMTAVIVKDYSRARCRHKPQQSSITTVVRSHQWDVSYAPAPNDIIWENLSVCGPRWWLRCILLNILLFLLLFFLTTPAIIVNTMDKFNVTRPVESLRNPVITQFFPTLLLWAFSILLPFIVYYSSFFEYHWTRSGENQVTMHKCFLLLVFMVIILPSLGLSSLNLFFRWLFDVRFLDETDVKFQCVFLPDNGAFFVNYVITSSLIGTAMELLRIPALLVYSLRLCFAKSKAECIHVKISQAYEFQFGLEYAWTMCIFSVSMTYSITCPVIVPFGLLYLVLKHMVDRYNIYYAYTPTKLNQRIHAAAISQVVVAPILCMFWLLFFSVLRLGPVQPITLFTFITLLCSIAFSCFGFCMKKLRADRSTSYQMSDQTTEGGFSDAERSTISTTATANLFIASVLLEPELGLTPMPSPAHQSYGTMVNSQSSVRDAEEDEEKDLEETLETELKDDLLMDSPVAFQ
Protein: Gasdermin-E (Non-syndromic hearing impairment protein 5 homolog) [Cleaved into: Gasdermin-E, N-terminal (GSDME-NT); Gasdermin-E, C-terminal (GSDME-CT)] (Q9Z2D3)
Organism: Mus musculus (Mouse)
Function: Precursor of a pore-forming protein that converts non-inflammatory apoptosis to pyroptosis. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-E, N-terminal) binds to membranes and forms pores, triggering pyroptosis.
Subcellular location: [Gasdermin-E, N-terminal]: Cell membrane {ECO:0000250|UniProtKB:O60443}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.; SUBCELLULAR LOCATION: [Gasdermin-E]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O60443}.
Interaction partners:
- Caspase-3
- Gasdermin-C
- Granzyme B
- Cytochrome c, somatic
- High mobility group protein B1
- Gasdermin-C3
- Gasdermin-C2
- Gasdermin-C4
- Gasdermin-A
- Caspase-4
Sequence:
MFAKATRNFLKEVDAGGDLISVSHLNDSDKLQLLSLVTKKKRYWCWQRPKYQILSATLEDVLTEGHCLSPVVVESDFVKYESKCENHKSGAIGTVVGKVKLNVGGKGVVESHSSFGTLRKQEVDVQQLIQDAVKRTVNMDNLVLQQVLESRNEVLCVLTQKIMTTQKCVISEHVQSEETCGGMVGIQTKTIQVSATEDGTVTTDTNVVLEIPAATTIAYGIMELFVKQDGQFEFCLLQGKHGGFEHERKLDSVYLDPLAYREFAFLDMLDGGQGISSQDGPLRVVKQATLHLERSFHPFAVLPAQQQRALFCVLQKILFDEELLRALEQVCDDVAGGLWSSQAVLAMEELTDSQQQDLTAFLQLVGYRIQGEHPGPQDEVSNQKLFATAYFLVSALAEMPDNATVFLGTCCKLHVISSLCCLLHALSDDSVCDFHNPTLAPLRDTERFGIVQRLFASADIALERMQFSAKATILKDSCIFPLILHITLSGLSTLSKEHEEELCQSGHATGQD
Protein: Carbonic anhydrase (EC 4.2.1.1) (Q6R4A1)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MHLFISFFFAIIVKIQGADWCYQSQVTCGGNCIGPDGWPTVAGACGGKAQSPINIVTRRTLPDERLTPFTFTGYQEAFHSLITNNGRTVQVDLPATAKVHGGDLAVPYKAIQLHLHLGKDGGPGSEHTIDGERYPMELHIVNIKKEYNSLDEALKDLAGVGVLGFFTSGFFYEQSGSSNKKYESIINALNSINMPSSNTTLSDVSLDMFIPSQSNMTSYFRYQGSLTTPPCEEAVVWTVFKNTIPLSRQQLDAFSRLQFADGKPMVGTYRPVQPLNGRPVYRSGSQVILVSTLPLSY
Protein: Uncharacterized protein NKAPD1 (NKAP domain containing protein 1) (Q6ZUT1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRIPLGKVLLRNVIRHTDAHNKIQEESDMWKIRELEKQMEDAYRGTKRKMLPSSSSRMRSDGFDEESQRYYWRPKNEISGTLEDDFLKAKSWNKKFYDYEANMPDRWGHSGYKELYPEEFETDSDQQDITNGKKTSPQVKSSTHESRKHKKSKKSHKKKQKKRSHKKQKKSKKEATDITADSSSEFSEETGASGTRKGKQPHKRKKKSRKKSLKKPALFLEAESNTSHSDDSASSSSEESEERDTKKTKRKKREKKAHTSVANNEIQERTNKRTNWKVATDERSAESSEDD
Protein: Myozenin-3 (Calsarcin-3) (FATZ-related protein 3) (Q8R4E4)
Organism: Mus musculus (Mouse)
Function: Myozenins may serve as intracellular binding proteins involved in linking Z line proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11842093}. Note=Localized at the Z-line of skeletal muscle.
Interaction partners:
Sequence:
MIPKEQKEPVMAVPGDLAEPVPSLDLGKKLSVPQDLMIEELSLRNNRGSLLFQKRQRRVQKFTFELSESLQAILASSARGKVAGRAAQATVPNGLEEQNHHSETHVFQGSPGDPGITHLGAAGTGSVRSPSALAPGYAEPLKGVPPEKFNHTAIPKGYRCPWQEFTSYQDYSSGSRSHTPIPRDYRNFNKTPVPFGGPHVREAIFHAGTPFVPESFSGLELLRLRPNFNRVAQGWVRKLPESEEL