wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-18 (IL-18) (B3VHV0)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR015162}.
Interaction partners:
Sequence:
MSCEVMAVCAVRLRENLCLYFEDDELECDAFCKDKTIKRFFRNVNSQLLVVRPDLNVAAFEDVTDQEVKSGSGMYFDIHCYKTTAPSAGMPVAFSVQVEDKSYYMCCEKEHGKMIVRFREGEVPKDIPGESNIIFFKKTFTSCSSKAFKFEYSLEQGMFLAFEEEDSLRKLILKKLPREDEVDETTKFVTSRNERHNL
Protein: Ribonuclease Z 2, mitochondrial (RNase Z 2) (EC 3.1.26.11) (tRNA 3 endonuclease 2) (tRNase Z 2) (P87168)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. May be involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21208191}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribonuclease Z 1
- Small ribosomal subunit protein eS25B
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein bS6m
- Nuclease 1, mitochondrial
- Uncharacterized protein PB1E7.11c
- Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- ATP synthase subunit a
Sequence:
MKASLLVPRRALLFGQLLPPKYSWYSVKRWQSQLTFRNKSKRNTNRIMLSVVSSLNPDSLIAPLLCVSLDNRKYLIGSMGELTQMKFRSQASNYGGKSVSVFLMPPSLQSLNAWGITAGLFGYLQSSGIQNTWGLHAPKPVISIIKKSHHLFSGSPLRLDLNSFSSEDNADATNSFYLDEPEFCTIKGNIYSNWSFLSFNSKEAAGVFNADKALALGVPFGPSNGKLCAGEAVLSKDGTTWIYPHQVVGPPRKRQYFYVLGCSSLSALNQMSKHVDSFSDVYPTCIIHILEKGIWGPEYIKFLSHPKFSRAQHFISCIELASNNPVFQRNKGRNVLPACRDFAAFDIKPSTLDTQTQLPENTYVLKEETSMVLYDEQCKISESPSYSPVKLAKKFSSFNPLPFENEGYTLDVLGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFFRQYGTNTEPMLRKLKAIFITHLHSDHYLGLLNVLQAWNKANTNNSMHINIIGPKFLWQWLQRLKSPANLQALLNRIIFIIAKETVTTPLQLTSDLSISSVPSIHINDSYSCIISHTKYGKLVYSGDTRPNEKLVKAGIGASLLLHESTFEDDLKHEAIQRQHSTASEALSVAQSMKAKALILTHFSQRSYDADFLPPDWTIYPKSKTIYANDGLQWQQFQSKQRETI
Protein: Mitochondrial RNA binding protein 1 (Q386Y3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Guide RNA binding protein
Sequence:
MIRLACLRGPAMRSAWSRGASTFSGVQSLPKFEIHDVRDDPALGTMTRVAVDGKLLLISQYPQLGPRKVDPNDLSPQFDADRRISVRLRHVDLAYLVGVCKERVPRHRMETKAYTLDFEKSAQGYHLHGKVHRVASQRMEDWSVKFDNHFAVTLEHFLESALDESFGFRQHYATRAAEGGEKIAATSSAEGGARRKRSVSDTSRYH
Protein: Activated macrophage/microglia WAP domain protein (OTTMUSG00000000971 protein) (WAP four-disulfide core domain 17) (Q5SSJ1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKTATVLFLVALITVGMNTTYVVSCPKEFEKPGACPKPSPESVGICVDQCSGDGSCPGNMKCCSNSCGHVCKTPVF
Protein: Urease subunit alpha (EC 3.5.1.5) (Urea amidohydrolase subunit alpha) (Q93PJ5)
Organism: Helicobacter hepaticus (strain ATCC 51449 / 3B1)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01955}.
Interaction partners:
- Urease subunit beta
- Urease accessory protein UreG
- Urease accessory protein UreF
- Urease accessory protein UreH
- Urease accessory protein UreE
- Hydrogenase/urease maturation factor HypB
- Arginase
- Bifunctional enzyme IspD/IspF
- Urease accessory protein UreI
Sequence:
MRLTPKELDKLMLHYAGALAKSRKERGIKLNYVESIALISMEIMELAREGNKSVAELMQQGREILKADEVMEGVASMVNEVQVEVSFPDGTKLVTIHNPIEDNGKLTPGEYILKDEDITLNANKESISIKVTHKGDRPIQVGSHFHFFEVNALLEFDRAQAFGKRLDIASGTSVRFEPGEEKNVNLIDFGGKQKIIGFNDLTNAHINKENKEQCLANAAQKHFIH
Protein: Exo-beta-D-glucosaminidase (GlcNase) (EC 3.2.1.165) (Exochitinase) (Q56F26)
Organism: Amycolatopsis orientalis (Nocardia orientalis)
Function: Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide.
Subcellular location: Secreted {ECO:0000269|PubMed:16316314, ECO:0000269|PubMed:2351651}.
Interaction partners:
- Chitosanase
- N-acetylglucosamine kinase
Sequence:
MSFRQKRTRIPLLAMTVTALAAAVCGVTTAPAATGAEVAVPLSVGAAAGNATPIPGYVIQSSAQVSDDSAVSKPGFPTSGWYPVSSRSTVYAGLLQNGKYADPFYSTNMQNVPAAQFSVPWWYRTDLNVDDTSSRTYLDFSGVLSKADVWVNGTKVATKDQVNGAYTRHDLDITAQVHTGVNSVAFKVYPNDPNRDLSMGWIDWAQTPPDQNMGIVRDVLVRRSGAVALRSAHVIQKLNSALDHADLTVKADVRNDSANAVQTTVAGTVAGKPISQTVSLAAKERKTVTFPLVGLDRPNVWWPAGMGGQHRYDLDLTASVGGTPSDAAKSKFGVRDVKATLNSSGGRQYSVNGKPLLIRGGGYTPDLFLRWNETAAADKLKYVLNLGLNTVRLEGHIEPDEFFDIADDLGVLTMPGWECCDKWEGQVNGEEKGEPWVESDYPIAKASMFSEAERLRDHPSVISFHIGSDFAPDRRIEQGYLDAMKAADFLLPVIPAASARPSPITGASGMKMNGPYDYVPPVYWYDKSQKDRGGAWSFNSETSAGVDIPTMDTLKRMMSASELDTMWKNPSAKQYHRSSSDTFGNLKLFGDALTKRYGASANLNDFVRKAQLSQYENVRAEFESHSRNYTDSTNPSTGLIYWMLNSPWTSLHWQLFDAYMDQNGAYYGAKKANEPLHIQYSHDNRSVVVINQTSNAVSGLTATTKLYNLDGTEKYSNTKTGLSVGALGAKATAVTVPAVSGLSTTYLAKWVLTDSSGKEVSRNVYWLSTKADTLNWGGSDWYYTPQSAFADLSGLNNLGQSAVGATANSVAGADGTTTTTVTLKNTSGGRLPAFYVDSKVVDSAGKPVLPVEWNDNAVSLWPGETTTLTAKYRTADLKGSKPSVRISGWNTGTQTVPADGSGPGPSDPVDYQAEDATIVQGAVESNHAGYTGTGFVNYDNVAGSSVEWTVTVPSAGTYDVVVRYANGTTTSRPLDFSVNGSISASGVAFGSTGTWPAWTTKTVRVTLAAGVNKIKAVATTANGGPNVDKITL
Protein: Protein timeless (P49021)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the production of circadian rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition.
Subcellular location: Nucleus {ECO:0000269|PubMed:8625406}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8625406}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with per is required for nuclear localization. {ECO:0000269|PubMed:8625406}.
Interaction partners:
- Cryptochrome-1
- Period circadian protein
- Circadian locomoter output cycles protein kaput
- Jetlag, isoform A
- Protein cycle
- 
- Claspin
- Protein kinase shaggy
- Protein TIPIN homolog
- Discs overgrown protein kinase
Sequence:
MDWLLATPQLYSAFSSLGCLEGDTYVVNPNALAILEEINYKLTYEDQTLRTFRRAIGFGQNVRSDLIPLLENAKDDAVLESVIRILVNLTVPVECLFSVDVMYRTDVGRHTIFELNKLLYTSKEAFTEARSTKSVVEYMKHILESDPKLSPHKCDQINNCLLLLRNILHIPETHAHCVMPMMQSMPHGISMQNTILWNLFIQSIDKLLLYLMTCPQRAFWGVTMVQLIALIYKDQHVSTLQKLLSLWFEASLSESSEDNESNTSPPKQGSGDSSPMLTSDPTSDSSDNGSNGRGMGGGMREGTAATLQEVSRKGQEYQNAMARVPADKPDGSEEASDMTGNDSEQPGSPEQSQPAGESMDDGDYEDQRHRQLNEHGEEDEDEDEVEEEEYLQLGPASEPLNLTQQPADKVNNTTNPTSSAPQGCLGNEPFKPPPPLPVRASTSAHAQMQKFNESSYASHVSAVKLGQKSPHAGQLQLTKGKCCPQKRECPSSQSELSDCGYGTQVENQESISTSSNDDDGPQGKPQHQKPPCNTKPRNKPRTIMSPMDKKELRRKKLVKRSKSSLINMKGLVQHTPTDDDISNLLKEFTVDFLLKGYSYLVEELHMQLLSNAKVPIDTSHFFWLVTYFLKFAAQLELDMEHIDTILTYDVLSYLTYEGVSLCEQLELNARQEGSDLKPYLRRMHLVVTAIREFLQAIDTYNKVTHLNEDDKAHLRQLQLQISEMSDLRCLFVLLLRRFNPSIHSKQYLQDLVVTNHILLLILDSSAKLGGCQTIRLSEHITQFATLEVMHYYGILLEDFNNNGEFVNDCIFTMMHHIGGDLGQIGVLFQPIILKTYSRIWEADYELCDDWSDLIEYVIHKFMNTPPKSPLTIPTTSLTEMTKEHNQEHTVCSWSQEEMDTLYWYYVQSKKNNDIVGKIVKLFSNNGNKLKTRISIIQQLLQQDIITLLEYDDLMKFEDAEYQRTLLTTPTSATTESGIEIKECAYGKPSDDVQILLDLIIKENKAQHLLWLQRILIECCFVKLTLRSGLKVPEGDHIMEPVAYHCICKQKSIPVVQWNNEQSTTMLYQPFVLLLHKLGIQLPADAGSIFARIPDYWTPETMYGLAKKLGPLDKLNLKFDASELEDATASSPSRYHHTGPRNSLSSVSSLDVDLGDTEELALIPEVDAAVEKAHAMASTPSPSEIFAVPKTKHCNSIIRYTPDPTPPVPNWLQLVMRSKCNHRTGPSGDPSDCIGSSSTTVDDEGFGKSISAATSQAASTSMSTVNPTTTLSLNMLNTFMGSHNENSSSSGCGGTVSSLSMVALMSTGAAGGGGNTSGLEMDVDASMKSSFERLEVNGSHFSRANNLDQEYSAMVASVYEKEKELNSDNVSLASDLTRMYVSDEDDRLERTEIRVPHYH
Protein: Small ribosomal subunit protein uS17 (40S ribosomal protein S11) (P62281)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62280}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein uS12
Sequence:
MADIQTERAYQKQPTIFQNKKRVLLGETGKEKLPRYYKNIGLGFKTPKEAIEGTYIDKKCPFTGNVSIRGRILSGVVTKMKMQRTIVIRRDYLHYIRKYNRFEKRHKNMSVHLSPCFRDVQIGDIVTVGECRPLSKTVRFNVLKVTKAAGTKKQFQKF
Protein: At1g71950 (Proteinase inhibitor, propeptide) (Q9C8W7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MQTFAPGTRVYHLIIIVFFFFFCLSSFFASIVMADEYTGEATGSSEAKVHIIYTEKPTDEEPKTYHLRTLSSALGSEEAAKDALIYSYKEAASGFSAKLTPEQVAEISKQPGVIQVVPSQTYQLHKPGGGGGFKLT
Protein: Patellin-2 (Q56ZI2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carrier protein that may be involved in membrane-trafficking events associated with cell plate formation during cytokinesis. Binds to some hydrophobic molecules such as phosphoinositides and promotes their transfer between the different cellular sites (By similarity).
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly membrane-associated. Also cytoplasmic (By similarity). {ECO:0000250}.
Interaction partners:
- Sec14p-like phosphatidylinositol transfer family protein
- At4g36640
- AT1G14820 protein
- F16L1.9 protein
- AT3g10210/F14P13_19
- SEC14 cytosolic factor family protein / phosphoglyceride transfer family protein
- Transmembrane protein
- MD-2-related lipid recognition domain-containing protein / ML domain-containing protein
- Sec14p-like phosphatidylinositol transfer family protein
- KIN17-like protein KLP
Sequence:
MAQEEIQKPTASVPVVKEETPAPVKEVEVPVTTEKAVAAPAPEATEEKVVSEVAVPETEVTAVKEEEVATGKEILQSESFKEEGYLASELQEAEKNALAELKELVREALNKREFTAPPPPPAPVKEEKVEEKKTEETEEKKEEVKTEEKSLEAETKEEEKSAAPATVETKKEEILAAPAPIVAETKKEETPVAPAPVETKPAAPVVAETKKEEILPAAPVTTETKVEEKVVPVETTPAAPVTTETKEEEKAAPVTTETKEEEKAAPGETKKEEKATASTQVKRASKFIKDIFVSVTTSEKKKEEEKPAVVTIEKAFAADQEEETKTVEAVEESIVSITLPETAAYVEPEEVSIWGIPLLEDERSDVILLKFLRARDFKVKEAFTMLKNTVQWRKENKIDDLVSEDLEGSEFEKLVFTHGVDKQGHVVIYSSYGEFQNKEIFSDKEKLSKFLKWRIQFQEKCVRSLDFSPEAKSSFVFVSDFRNAPGLGQRALWQFIKRAVKQFEDNYPEFVAKELFINVPWWYIPYYKTFGSIITSPRTRSKMVLSGPSKSAETIFKYVAPEVVPVKYGGLSKDSPFTVEDGVTEAVVKSTSKYTIDLPATEGSTLSWELRVLGADVSYGAQFEPSNEASYTVIVSKNRKVGLTDEPVITDSFKASEAGKVVITIDNQTFKKKKVLYRSKTQA
Protein: Homoserine O-acetyltransferase (EC 2.3.1.31) (Homoserine O-trans-acetylase) (P08465)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11914276, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Homoserine dehydrogenase
- Cystathionine gamma-synthase
- Homocysteine/cysteine synthase
- Cystathionine beta-synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Homocysteine/cysteine synthase
- Putative cystathionine gamma-synthase YML082W
- Tryptophan synthase
- Cystathionine beta-lyase
- Sulfate permease 2
Sequence:
MSHTLKSKTLQELDIEEIKETNPLLKLVQGQRIVQVPELVLESGVVINNFPIAYKTWGTLNEAGDNVLVICHALTGSADVADWWGPLLGNDLAFDPSRFFIICLNSMGSPYGSFSPLTINEETGVRYGPEFPLCTVRDDVRAHRIVLDSLGVKSIACVIGGSMGGMLSLEWAAMYGKEYVKNMVALATSARHSAWCISWSEAQRQSIYSDPNYLDGYYPVEEQPVAGLSAARMSALLTYRTRNSFENKFSRRSPSIAQQQKAQREETRKPSTVSEHSLQIHNDGYKTKASTAIAGISGQKGQSVVSTASSSDSLNSSTSMTSVSSVTGEVKDIKPAQTYFSAQSYLRYQGTKFINRFDANCYIAITRKLDTHDLARDRVDDITEVLSTIQQPSLIIGIQSDGLFTYSEQEFLAEHIPKSQLEKIESPEGHDAFLLEFKLINKLIVQFLKTNCKAITDAAPRAWGGDVGNDETKTSVFGEAEEVTNW
Protein: Dynactin subunit 6 (Q9N3F1)
Organism: Caenorhabditis elegans
Function: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Dynactin subunit 5
- Actin-related protein 10
- Dynactin subunit 4
- Probable dynactin subunit 2
- Dynactin subunit 1
- Actin
- F-actin-capping protein subunit beta
- DyNactin Complex component
- F-actin-capping protein subunit alpha
- Protein sumv-1
Sequence:
MTETSTVSIASSAIVCVEADIKGEVIIKEGCVVHPFVVFDATKGPIYVGENNIFEEYAVIRNNSDGQPMIIGDWNIFQVHSKSSAKYVGSRNVIGVHAVLEDGCSVSDDCSVGAKCTVFSHQNLEPSVSVYAATNLSRTTKTPNMTSPHQIEFLRKILPSYHHLYGKKKAVATASASAAQ
Protein: Small ribosomal subunit protein uS7A (40S ribosomal protein S5-A) (O14277)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL5B
- Elongation factor 3
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein eS7
- mRNA export factor elf1
Sequence:
MATSSLTPGVSLDENGSIKLFNKFPFEGVEVKDISLVDYITIGNGQPLPHTAGRFQTKRFRKARCFIVERLTNSLMMNGRNNGKKLLATRIVKHAFEIIALLTDQNPLQVLVDAVAACGPREDSTRIGSAGTVRRQAVDVSPLRRVNQALALITIGAREAAFRNVKSISECLAEEIINAAKGSSNSYAIKKKDELERVAKSNR
Protein: Probable beta-1,4-xylosyltransferase IRX9L (EC 2.4.2.-) (OsGT43F) (Probable glucuronosyltransferase Os01g0675500) (Protein IRREGULAR XYLEM 9 homolog L) (OsIRX9L) (Q5QM25)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable beta-1,4-xylosyltransferase involved in xylan biosynthesis in cell walls.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSRRNAGAMQREGSVKDWEEFDPSPSPKLAYSQSYVAMRGLLTSVASLDLVLMSSSLKSAWAAISSHKHARSLERSRSKGMSLKRAMLQLLVCFMVGIFIGFTPPFSVDLPGKIASENGRLPFDGDAIDRRQMVERQGTKLEPFVAEAESEASSEPQVEEGPPVPAMLDDEADFVEASPIVHSVNDSGIVVRKHLIIITTTSVRPHQAYYLNRLAHVLKDVPPPLLWIVAEWPYQSRETAEILRSSGIMYRHLICNRNTTNIRKIVVCQKNNAIFHIKKHRLDGIVHFADEERAYSADLFEEMRKIRRFGTWPVAIHVGTKYRVVLEGPVCKGNQVTGWHTNQRRGVSRRFPIGFSGFAFNSTILWDPQRWNSPTLESIIVHSGGRGGLQESRFIEKLVEDESQMEGLGDNCTRVMVWNFELEPPQVNYPIGWLLQRNLDAVVPIT
Protein: Secreted beta-glucosidase sun1 (EC 3.2.1.-) (Q4WGL5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Cell surface beta-glucosidase involved in cell wall biosynthesis and septation, and thus required for normal growth and correct hyphal morphogenesis. Has hydrolytic activity on linear (1->3)-beta-D-glucans such as laminaribiose and other laminarioligosaccharides. Has also a minor transferase activity.
Subcellular location: Secreted, cell wall. Secreted.
Interaction partners:
Sequence:
MKFNTVALTLATAGSLVTAQHHHQHRHHQHKREDVVESSATVVQYELDGKPISLKQVCAGLADNTLKFANNDHPTGICDNLSSAAAPASTPEVTSAFAPAQFIELSSVVTSATPTSASSSETVQTPAASSSSASSSSTATGLDADFPDGELDCSTFPSEYGAIPLDYLKLGGWSGIQYVSYAGNFINDIVTAVAGDTCKDGAMCSYACPPGYQKSQWPSTQGATGQSVGGIECRNGKLHLTNPSLSKKLCIPGVGGVHVQNTLGETVAVCRTDYPGTESETIPIGLGGNDLQPLTCPDGETYYKWQGKTTSAQYYVNPKGVTPEKGCQWGDGTQPIGNWAPVNLGVGLNKGKWLSIFQNSPTTSEKLDFNIKIKGDNLSGSCKYENGVFYSETGSSSSGCTVQVMSGDATFVFY
Protein: Membrane-bound lytic murein transglycosylase F (EC 4.2.2.n1) (Murein lyase F) (P0AGC5)
Organism: Escherichia coli (strain K12)
Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_02016, ECO:0000269|PubMed:18234673}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_02016, ECO:0000269|PubMed:18234673}. Note=Attached to the inner leaflet of the outer membrane.
Interaction partners:
- Membrane-bound lytic murein transglycosylase D
- Membrane-bound lytic murein transglycosylase C
- Membrane-bound lytic murein transglycosylase B
- Soluble lytic murein transglycosylase
- Membrane-bound lytic murein transglycosylase A
- Endo-type membrane-bound lytic murein transglycosylase A
- Endolytic peptidoglycan transglycosylase RlpA
- Endolytic murein transglycosylase
- Anhydromuropeptide permease
Sequence:
MKKLKINYLFIGILALLLAVALWPSIPWFGKADNRIAAIQARGELRVSTIHTPLTYNEINGKPFGLDYELAKQFADYLGVKLKVTVRQNISQLFDDLDNGNADLLAAGLVYNSERVKNYQPGPTYYSVSQQLVYKVGQYRPRTLGNLTAEQLTVAPGHVVVNDLQTLKETKFPELSWKVDDKKGSAELMEDVIEGKLDYTIADSVAISLFQRVHPELAVALDITDEQPVTWFSPLDGDNTLSAALLDFFNEMNEDGTLARIEEKYLGHGDDFDYVDTRTFLRAVDAVLPQLKPLFEKYAEEIDWRLLAAIAYQESHWDAQATSPTGVRGMMMLTKNTAQSLGITDRTDAEQSISGGVRYLQDMMSKVPESVPENERIWFALAAYNMGYAHMLDARALTAKTKGNPDSWADVKQRLPLLSQKPYYSKLTYGYARGHEAYAYVENIRKYQISLVGYLQEKEKQATEAAMQLAQDYPAVSPTELGKEKFPFLSFLSQSSSNYLTHSPSLLFSRKGSEEKQN
Protein: Neural/ectodermal development factor IMP-L2 (Q09024)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential developmental role during embryogenesis, in particular the normal development of the nervous system. May be involved in some aspect of cell adhesion.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Insulin-like peptide 5
- Insulin-like peptide 2
- Death-associated inhibitor of apoptosis 2
- Insulin-like peptide 3
- Acid labile subunit
- Insulin-like peptide 6
- Insulin-like receptor
- Interference hedgehog
- Insulin-like peptide 1
- GH12395p
Sequence:
MEAKMNLHVCALALLLFGSIATVRGRAVDLVDDSNDVDNSIEAEEEKPRNRAFEADWLKFTKTPPTKLQQADGATIEIVCEMMGSQVPSIQWVVGHLPRSELDDLDSNQVAEEAPSAIVRVRSSHIIDHVLSEARTYTCVGRTGSKTIYASTVVHPPRSSRLTPEKTYPGAQKPRIIYTEKTHLDLMGSNIQLPCRVHARPRAEITWLNNENKEIVQGHRHRVLANGDLLISEIKWEDMGNYKCIARNVVGKDTADTFVYPVLNEED
Protein: Sporulation-specific chitinase 2 (EC 3.2.1.14) (Q06350)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Endochitinase
- Chitin deacetylase 2
- Chitin deacetylase 1
Sequence:
MVGHSAQHRSKSSLVSHLLILLIFITIIIEMCLYNKIFKNQRSDDIRDNFNNGGHRVPSNVQNHGTHIRDEAFISGVYYSNWSPYKPRFHFPHDINLKQVSHIYYAFFKINSRTGGIENTDSWSDLEMNLYKSLAIKNSELIKESSNNSVQNILPLGCIGELFYLKNTCSDKKFKVIMSIGGWSDSENFKIIIKDDKLLQNFVDSSVETMFRLGFDGIDLDWEFPGNNESEPRGYLKLVRMLRLKLNSLESQIFGKRTEDHFQLSIAAPAFKDKLFYLPITEIDQYVDYWNMMTYDYYGSWSETTGYHSNLFSETELNGNFAMHYMIDRFGVNSRKLVLGMAAYGRSFHIKDNKFEPFNQNTVLINKIFKGVGKPTKEIDKADGKEGIWPYKNLPKIGTIEQYDPKYVSAYCFDEKNSIFISYDNTKSVKTKAEYVTHNNLGGGFWWESCGEAYANESRSLINAFNEGLHFNVSSKPSIFQDVRVKKYYLNKYGDGGFLSPYLKHLDSRKQ
Protein: Poly(A) polymerase alpha (H0YJL4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XVLQKKKKHSTEGVKLTALNDSSLDLSMDSDNSMSVPSPTSATKTSPLNSSGSSQGRNSPAPAVTAASVTNIQATEVSVPQVNSSESSGGTSSESIPQTATQPAISPPPKPTVSRVVSSTRLVNPPPRSSGNAATSGNAATKIPTPIVGVKRTSSPHKEESPKKTKTEEKTSSTDLSDIPA
Protein: Spore wall protein 3 (Q8SWI4)
Organism: Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Function: Spore wall component.
Subcellular location: Spore wall {ECO:0000269|PubMed:16368098, ECO:0000269|PubMed:16368977}. Membrane {ECO:0000269|PubMed:16368098, ECO:0000269|PubMed:16368977}; Lipid-anchor, GPI-anchor. Cytoplasm {ECO:0000269|PubMed:16368977}. Note=Is found in the cytoplasm during the proliferative and early sporogonic stages before localizing to cell surface and spore wall in sporonts and spores. {ECO:0000269|PubMed:16368098}.
Interaction partners:
Sequence:
MVRRSLYFLAVMGVVRSSSGLYIPSVVLQELGIASSQGCLMIAETNNGNFGIVSSGLENPVYITESPQGHREVSWQPVRGEDRAVPIYAPSAEEVRESISSVRGSEPGQYIAPQPTGFVPASTPVFGTIESASTAGAAVPVEGVFVASTENPASTGSSSTSTCPPKGTAGTTDNKGKAGGAAADDKSKSSSSSSSKKKKKGAKSLVALGAVATTALFSIVM
Protein: ADP-ribosylation factor 4 (P61751)
Organism: Rattus norvegicus (Rat)
Function: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:P18085}. Membrane {ECO:0000250|UniProtKB:P18085}; Lipid-anchor {ECO:0000250|UniProtKB:P18085}.
Interaction partners:
- Ras-related protein Rab-11A
- Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
- Ras-related protein Rab-8A
- Coatomer subunit beta
- Rhodopsin
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- Rab11fip3 protein
- Rab-3A-interacting protein
- Polycystin-1
- Coatomer subunit gamma-1
Sequence:
MGLTISSLFSRLFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIQEGAAVLQKMLLEDELQDAVLLLFANKQDLPNAMAISEMTDKLGLQSLRNRTWYVQATCATQGTGLYEGLDWLSNELSKR
Protein: tRNA-splicing endonuclease subunit Sen15 domain-containing protein (Q580R9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIDDVRICHLVLQDVKERLPLYESRLEAVNNSHVVISCWNESVKAFVPVPVAEDVEFTSDVLHEVVSLVDGLRQLGCTDFFVVFVDSGGTLSFYHVDTLRLLQSGRSGSS
Protein: Probable formate transporter (P35839)
Organism: Methanobacterium formicicum
Function: May act as a formate transporter.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable [NiFe]-hydrogenase-type-3 Eha complex membrane subunit A
- Carbonic anhydrase
- F420-dependent formate dehydrogenase subunit alpha
- F420-dependent formate dehydrogenase subunit beta
- Prefoldin subunit beta
- Coenzyme F420 hydrogenase subunit alpha
- Prefoldin subunit alpha
- F420-dependent methylenetetrahydromethanopterin dehydrogenase
Sequence:
MASSFKSPADTAKACVGVAALKEKAPLSNLIVLSFVAGAYIAFGGLLAEVATGGMAAAGWPTGLVKLVFGGVFPVGLMLVVIAGSELFTGNCMYMPMGILQGEASVMGTIKNWVGSWVFNLVGALFVAYVLAYLTGILTAEPWAATAVTIAKTKALGGAQFIAAGKTVTSLSWMQVFWRAIGCNWLVCLAVYLAVASDDVIGKSFGIWFPIMAFVCIGFEHVVANMFFIPVGIFIGGVTWSQFFINNMIPATLGNIVGGAIFVGCIYWFTYLRGTNKAKA
Protein: Protocadherin beta-16 (PCDH-beta-16) (Protocadherin-3X) (Q9NRJ7)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protocadherin beta-7
- Protocadherin beta-14
- Protocadherin beta-6
Sequence:
MEIGWMHNRRQRQVLVFFVLLSLSGAGAELGSYSVVEETERGSFVANLGKDLGLGLTEMSTRKARIISQGNKQHLQLKAQTGDLLINEKLDREELCGPTEPCILHFQVLMENPLEIFQAELRVIDINDHSPMFTEKEMILKIPENSPLGTEFPLNHALDLDVGSNNVQNYKISPSSHFRVLIHEFRDGRKYPELVLDKELDREEEPQLRLTLTALDGGSPPRSGTAQVRIEVVDINDNAPEFEQPIYKVQIPENSPLGSLVATVSARDLDGGANGKISYTLFQPSEDISKTLEVNPMTGEVRLRKQVDFEMVTSYEVRIKATDGGGLSGKCTLLLQVVDVNDNPPQVTMSALTSPIPENSPEIVVAVFSVSDPDSGNNGKTISSIQEDLPFLLKPSVKNFYTLVTERALDREARAEYNITLTVTDMGTPRLKTEHNITVQISDVNDNAPTFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLASLVSINADNGHLFALRSLDYEALQAFEFRVGATDRGSPALSREALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKQRLVVLVKDNGEPPRSATATLHVLLVDGFSQPFLPLPEAAPGQTQANSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCSMPEGPFPGRLVDVSGTGTLSQSYQYEVCLTGGSETSEFKFLKPIIPNFSP
Protein: Protein extra-macrochaetae (P18491)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participates in sensory organ patterning by antagonizing the neurogenic activity of the Achaete-scute complex (AS-C). It lacks a basic DNA-binding domain but is able to form heterodimers with other HLH proteins, thereby inhibiting DNA binding. May sequester proneural proteins in complexes inefficient for DNA interaction. EMC also affects vein differentiation. Inhibits the activity of AS-C proteins by forming an non-DNA binding heterodimer.
Subcellular location: Nucleus.
Interaction partners:
- Protein daughterless
- Achaete-scute complex protein T4
- Achaete-scute complex protein T5
- ETS-like protein pointed
Sequence:
MKSLTAVCQTGASGMPALNASGRIQRHPTHRGDGENAEMKMYLSKLKDLVPFMPKNRKLTKLEIIQHVIDYICDLQTELETHPEMGNFDAAAALTAVNGLHEDEDSDMEDADAEAEAEVDPDILAQRLNAEQPAKVSSPAARLPLTDRQTPNTLVAPAHPQQHQQQQQLQLQQQQLQSQQQLSNSLATPQNAEKDSRQS