wanglab/gogpt-training-data huggingface dataset:
Protein: Lysosome membrane protein 2 (85 kDa lysosomal membrane sialoglycoprotein) (LGP85) (CD36 antigen-like 2) (Lysosome membrane protein II) (LIMP II) (Scavenger receptor class B member 2) (CD antigen CD36) (Q14108)
Organism: Homo sapiens (Human)
Function: Acts as a lysosomal receptor for glucosylceramidase (GBA1) targeting.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:7509809}; Multi-pass membrane protein {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:7509809}.
Interaction partners:
- Thrombospondin-1
- Toll-like receptor 4
- Toll-like receptor 2
- Leukocyte surface antigen CD47
- Toll-like receptor 6
- Lysosomal acid glucosylceramidase
- Tyrosine-protein kinase Lyn
- Apolipoprotein B-100
- Thrombospondin-2
- CD63 antigen
Sequence:
MGRCCFYTAGTLSLLLLVTSVTLLVARVFQKAVDQSIEKKIVLRNGTEAFDSWEKPPLPVYTQFYFFNVTNPEEILRGETPRVEEVGPYTYRELRNKANIQFGDNGTTISAVSNKAYVFERDQSVGDPKIDLIRTLNIPVLTVIEWSQVHFLREIIEAMLKAYQQKLFVTHTVDELLWGYKDEILSLIHVFRPDISPYFGLFYEKNGTNDGDYVFLTGEDSYLNFTKIVEWNGKTSLDWWITDKCNMINGTDGDSFHPLITKDEVLYVFPSDFCRSVYITFSDYESVQGLPAFRYKVPAEILANTSDNAGFCIPEGNCLGSGVLNVSICKNGAPIIMSFPHFYQADERFVSAIEGMHPNQEDHETFVDINPLTGIILKAAKRFQINIYVKKLDDFVETGDIRTMVFPVMYLNESVHIDKETASRLKSMINTTLIITNIPYIIMALGVFFGLVFTWLACKGQGSMDEGTADERAPLIRT
Protein: Ewsr1a protein (Q6NUX1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
SAADYNSYGQAGSQQGYGSYPAQPSQPGYGQGTQQSYGQQQGYGSYSQPADSTYSQTSGSSSSYGQQPYGSSYGQQPPASGSYNAASATPQGYTQPVQGYGSSSYDSSTAAASSTSNTQTSYGGQASYGTQSAYPGYGQQPAAAAPPSSYSSGSQQPAGYEQSSYSQQPQQSTYSQQQQGGYQGQQGGYGQQSSYSQQGGYQQTPPQQQQAPPSSYAPPSGSYGQPSASQYGQQGSTGGGYGQSDYKPPNQYGSYRPDHQNGGGYSGPESGGYGGPGEGRGMGGGENRGRGRGGFDRGMMRGGGGMRGGMSRGGMGIAGDRGGFSKPGDGEMGAPEEQDDSENSTIYITGLTENATLEEVADFFKHSGIIRINKRTGLPAVNIYTDKDTGKPKGDATLSYEEPPSAKAAVEWFDGKDFQGKKLKVSMARRKPMMGMMRGGMPMRGDRGGMMGRGGMMGRGGMGRGGDRGGFMPRGGPRGMGRGGPTGGNMQQRAGDWQCPNAGCGNQNFAWRMECNQCKAPKPEGFGPPPFPPGGDRGRGGPGGMRGGRGMDRGGPGGPGGFRGGRGVDRGGFRGRGMDRGGFGGRGRGGPPMDDMGRRGRGMGPPGKMDMKGDHRQDRRERPY
Protein: Glutamyl aminopeptidase (EAP) (EC 3.4.11.7) (Aminopeptidase A) (AP-A) (CD antigen CD249) (P50123)
Organism: Rattus norvegicus (Rat)
Function: Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q07075}; Single-pass type II membrane protein.
Interaction partners:
- Angiotensinogen
- Angiotensin-converting enzyme 2
- Aspartyl aminopeptidase
- Angiotensin-converting enzyme
- Renin
- Angiotensin-converting enzyme
- Neprilysin
- Type-2 angiotensin II receptor
Sequence:
MNFAEEEPSKKYCIKGKHVAIICATVVAVGLIVGLSVGLTRSCEPGTTPAPSNPPPHTSTALPPQDQNVCPDSDDESGEWKNFRLPDFIQPVHYDLEVKVLMEEDRYTGIVSISVNLSKDTRDLWLHIRETRITKLPELRRPSGEQVPIRRCFEYKKQEYVVIQAEEDLAATSGDSVYRLTIEFEGWLNGSLVGFYRTTYTEDGQTKSIAATDHEPTDARKSFPCFDEPNKKATYNISLIHPKEYSALSNMPVEKKETLDNDWKKTTFMKSVPMSTYLVCFAVHQFTSIQRTSRSGKPLTVYVQPNQKQTAEYAANITKAVFDFFEDYFAMEYSLPKLDKIAIPDFGTGAMENWGLVTYRETNLLYDPLLSASSNQQRVASVVAHELVHQWFGNIVTMDWWDDLWLNEGFASFFEFLGVNHAEADWQMLSQVLLEDVLPVQEDDSLMSSHPVVVTVSTPAEITSVFDGISYSKGASILRMLQDWITPEKFQKGCQIYLENFKFKNAKTSDFWDSLEKASNQPVKEVMDTWTSQMGYPVVTVSGKQNVTQKRFLLDYKADPSQPPSALGYTWNIPIKWTENGNSNITVYYRSNREGITLNANLSGDGFLKINPDHIGFYRVNYEAETWDWIAETLSSNHMNFSSADRSSFIDDAFALARAQLLDYEKALNLTRYLTSEKDFLPWERVISAVSYIISMFEDDRELYPLIETYFRSQVKPIADSLGWQDTGSHITKLLRASVLGFACKMGAGEALGNASQLFEAWLKGNESIPVNLRLLVYRYGMQNSGNEAAWNYTLEQYQKTSLAQEKEKLLYGLASVKDVTLLARYLEMLKDPNIIKTQDVFTVIRYISYNSYGKSMAWNWIQLNWDYLVNRFTINDRYLGRIVTIAEPFNTELQLWQMQSFFAKYPNAGAGAKPREQVLETVKNNIEWLKLNRKSISEWFTSMP
Protein: Alk8p (Q59K96)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- NADPH--cytochrome P450 reductase
- NADPH-dependent diflavin oxidoreductase 1
Sequence:
MLEEISFESWYLYLIICGVLYFCTNYLYIQYLNKKLGAKSPGSCKSDGCFGFRSGFEMLKAKKIGRQVDLLHERFNDLSNPEVNDTFTSYNFGFPMIITKDPENIKALLATQFNDFSLGRRYDFFKPLLGKGIFTLDGEGWKHSRSMLRPQFAREQIAHVKALEPHFQLLKKHITKNKGQFFDIQELFFRFTVDSATEFLFGESVSSLKDESIGYNQDEFDFAGRKDFPEAFNKSQIYLSTRSLLQNLYWLVNPKDFQNCNAIVHKFSDYYVNKALNATPEELEKNSGYVFLYELVKQTRDPQVLRDQALNILLAGRDTTAGLLSFAVFELARNPQVWKKLREEIIERYADGATEISFETLKQCEYLKAVINETLRLYPSVPRNGRFANKNTTLPRGGGPDGMSPILIKQGQAVMYSIYSTQRDPKYYGKDADVFRPERWFEPETRKLGWAFLPFNGGPRICLGQQFALTEASYVLVRLAQCCENLQLTEGIEYPPAKLTHLTMCMFDGVPIKVD
Protein: Death domain-associated protein 6 (Daxx) (Q1LUU4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
- DNA helicase
- Tumor necrosis factor receptor superfamily member 6
- Small ubiquitin-related modifier 1
- Ubiquitin carboxyl-terminal hydrolase 7
- mitogen-activated protein kinase kinase kinase
- Si:ch211-1i11.3.
- Cellular tumor antigen p53
- E3 ubiquitin-protein ligase Mdm2
- TGF-beta receptor type-2
- TGF-beta receptor type-2
Sequence:
MAGAGMESIVILDDDDEEAASTSASCSQATAQHLKTPVKSQPVPAPTHITQSPFASAKKDTHVLKVENEKLFNEFVEHCSKHSQEHPEVMTYLQTRYSKALPTFLTSVEFRNTLGRCLTRAQANAGKTFVYINELCTVLKQHTPRKRSSIQSLSVKAKPEEKSNGVNVKEDTQGEQDGGKDVKQQEEESKKTKRASRRQIAYLENLLKVYNEEIRRLQEGDLSLDDLEKEDSSYIQEHKLKRKMMKIYEKLCELKGCNTLTGRVIEQKIPYSGTRYPEINKKVERFINSSEALLNPPDYSDILKIVQRANERYNLQLSRKQQAQISQEAFRETGNKLQERRHLDMVYNFGSHLTDPYKPTLDPALMDPALHRKLRSNRDVAISSLEEVINKYANKQEDMEVEETKKRQDRERLKKEAVNGQQSESKEKEKEEQEEKEKEDEEEEEEDEEEDDSSDPDIEDEIQASEQQAGPEDDEEDVEEEPANISDNDQPINESSPLSIKSSVQDTEEDEEQSPLSSTHEGSAETNTNTNGPAKQSLESTEIKPESIKPESIKPESIKPETIKPESIKPENTDSLAEVKTEQVSSNHVEAVSASTETVSIVSEESSTAVTRSANCSPLLPTSPLLIDETGNYRKRKRRSTENHTSAHNGNCTEDSDIPLDMGVICCSEQEDLTCLKTPPRKTARNSQATPPPKKNKVNVATQCDPEEVIVLSDSE
Protein: Uncharacterized protein YqcC (Q46919)
Organism: Escherichia coli (strain K12)
Interaction partners:
- tRNA pseudouridine synthase C
- Flavodoxin YqcA
Sequence:
MTTHDRVRLQLQALEALLREHQHWRNDEPQPHQFNSTQPFFMDTMEPLEWLQWVLIPRMHDLLDNKQPLPGAFAVAPYYEMALATDHPQRALILAELEKLDALFADDAS
Protein: Tumor protein p73 (p53-like transcription factor) (p53-related protein) (O15350)
Organism: Homo sapiens (Human)
Function: Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein. Is an activator of FOXJ1 expression (By similarity). It is an essential factor for the positive regulation of lung ciliated cell differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:24314664}. Cytoplasm. Note=Accumulates in the nucleus in response to DNA damage.
Interaction partners:
- E3 ubiquitin-protein ligase Mdm2
- Tumor protein 63
- Transcriptional coactivator YAP1
- Cellular tumor antigen p53
- Apoptosis-stimulating of p53 protein 2
- Bcl-2-like protein 1
- Histone acetyltransferase p300
- Protein Mdm4
- Tyrosine-protein kinase ABL1
- E3 ubiquitin-protein ligase Itchy homolog
Sequence:
MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH
Protein: Protein csx2 (Q9UUE2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Oxysterol-binding protein-like protein 1
- Pre-rRNA-processing protein crb3/ipi3
- Acetyl-CoA carboxylase
Sequence:
MTGHVDPVHFERLKIQSVTFGSANDNASLQVHNVSKSPEYSKYSYSRKNNEPIEFIQLREEEGPIVKVEEEDGLTLRFQLEFHAQEGKRDVTNLTCVYGTSPQQLDRLITREFSSDANFQNNHQVFLIGNIEFHSNENSKKIEWTWSNQSLHTLYFRNGGSPIYLCFAEYDKRLNCLVPLKTFQFYVTESDQDSTPATPFPMPMHLAEETATSPEISDAPPLSGNVDPLPINSPPLTNPVARDIDQTEPEDGPLFRATILNYERTTHDMRMVLKKLIKRIEHVAHSHGLLYMSYKELMSAFERVATINPPAFKPFLDHYYAAAAQSFDSFNIDRARLLRNFLIEPLRKIYDTDIKNVSTKKKDFEETSRDYYTSLSRYLSKSEKETSSDKTKESKFAAKKRDFELSRFDYYSYMQDINGGRKGQEVLSVLTSFAANDYNLIHSSLTDIDALRPSIIQLQDIVTEANKEFQLLRAEREERRRYIETSSRELEDKDAEIAAQAYKAKVDQDTSAKQGLLLAFSKSTSDLQVVGKSGWHKYWVVLDHGKICEYANWKQSLELHTEPIDLLMATVRPAQSVSRKFCFEVITPQTKRTYQATSKAEMHSWIEAIQYSISESIVQKGKGTSMNSEETSVKHGPTSTIGKALQRVASVTSPSRHNSDSKEKKQTKSPSLVKTLKEMHSSDQSCADCNTTARVEWCAINFPVVLCIDCSGIHRSLGTHITKIRSLTLDKFNPETVDLLYATGNSFVNEIYEGGITDWKIKNFENQERRVQFVKDKYLYKRFIKSSFSHDPNTGLLESIEHSNLKEAVLCLALGADVNYQRAVVKALLKNNYLIAELLTLNGASLNVDEVTMETLSARAQAFVMNRATP
Protein: Pre-B-cell leukemia transcription factor 1 (Xpbx1) (Homeobox protein pbx1) (Pre-B-cell leukemia transcription factor 1b) (Xpbx1b) (Q8QGC4)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as a transcriptional activator in complex with isoform 2 of meis1, to induce posterior neural and neural crest gene expression, and thereby specify hindbrain and neural crest cell fate. Binds to a highly conserved region in the promoter of the neural crest gene zic3. Required for the nuclear transport or retention of isoform 2 of meis1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P40424}.
Interaction partners:
Sequence:
MDDQPRLMHSHPGVGMAGHPSLSQHMQDGTGANEGDVGRKQDIGDILQQIMTITDQSLDEAQARKHALNCHRMKPALFNVLCEIKEKTVLSIRGAQEEEPSDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGAGADNSTEHSDYRAKLSQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVSIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEILNEYFYSHLSNPYPSEEAKEELAKKCAITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAAKTAVNATNVSVHGSQANSPSTPSSAGGYPSPCYQSDRRIQ
Protein: Sulfhydryl oxidase (EC 1.8.3.2) (Q7JQR3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ero1-like protein
Sequence:
MSATHLVILAVALLVDIASAGVPLPRYEALLKQQSPPSDPTLGLYDDGDKVIRLSVDNFNATVLDQNRGALVEFYNTYCGHCRRFAPTYKSVAEHLLPWSEVLIVAAIDCAAEENNGICRNYEVMGYPTLRYLGPGFQPGPQHYGQSLHTQDKNEIREILAGMVAAENLTSSHNNSYWPNFHYLTENDSASSLFEGLSSATEYVAVVHEPENTTLGVEVALFMTQWPAVRVRRVIDPAVAAKFKIDPTNLPLSLVDRKGEITAYAPESTNGESYAKKLWDVLGKKNITPRPVKVHQPSATPASKIKGQNELIDEVHRNKHFVYQADLEQAIRTVLHNEVSKVGEISGEKLLALQRFLAVLQRYNPLGANGHQLVSKLKDYVVQFNDQRLTGSQFEEELKRLEAHLSPVYSSNHFVGCVGSSPRLRGFSCSLWTLFHFMTVQAANNEETQDPLEVLQAMHGYIKNFFGCTECSEHFQAMASRRKIWSVPNKEEAVLWLWAAHNEVNQRLAGDATEDPEFPKKQFPAPESCNECYRTPVSKSENLEIEWNKDAVLGFLKNIHNPQFVSRYGVQREELLHPTADKMRQKRQISSVFTDMDMRMGMLLYAFCIVMMVLAFKLFAFKGYRKKPYGHDLLGKV
Protein: Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (SerRSmt) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) (Q9N0F3)
Organism: Bos taurus (Bovine)
Function: Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:10764807}.
Interaction partners:
- Phosphoseryl-tRNA kinase
- Probable arginine--tRNA ligase, mitochondrial
- Serine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Cysteine--tRNA ligase, mitochondrial
- Alanine--tRNA ligase
- Alanine--tRNA ligase
- leucine--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
Sequence:
MAASIVRRLGPLVAGRGLRLRGGCVCNQSFKRSFATERQDRNLLYEHAREGYSALPLLDMESLCAYPEDAARALDLRKGELRSKDLPGIISTWQELRQLREQIRSLEEEKEAVTEAVRALVVNQDNSQVQQDPQYQSLRARGREIRKQLTLLYPKEAQLEEQFYLRALRLPNQTHPDVPVGDESQARVLHVVGDKPAFSFQPRGHLEIAEKLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTLNKLIHRGFTPMTVPDLLRGVVFEGCGMTPNAKPSQIYNIDPSRFEDLNLAGTAEVGLAGYFMDHSVAFRDLPIRMVCSSTCYRAETDTGKEPWGLYRVHHFTKVEMFGVTGPGLEQSSELLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVTSASNCTDFQSRRLHIMFQTEAGELQFAHTVNATGCAVPRLLIALLESYQQKDGSVLVPPALQPYLGTDRITTPTHVPLQYIGPNQPQKPRLPGQPASS
Protein: Echinoderm microtubule-associated protein-like 3 (EMAP-3) (Q32P44)
Organism: Homo sapiens (Human)
Function: Regulates mitotic spindle assembly, microtubule (MT)-kinetochore attachment and chromosome separation via recruitment of HAUS augmin-like complex and TUBG1 to the existing MTs and promoting MT-based MT nucleation. Required for proper alignnment of chromosomes during metaphase.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18445686, ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:18445686}. Nucleus {ECO:0000269|PubMed:18445686}. Midbody {ECO:0000269|PubMed:18445686}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18445686, ECO:0000269|PubMed:30723163}. Note=Localizes to microtubules throughout all mitotic stages and localizes to the midbody during cytokinesis. {ECO:0000269|PubMed:18445686}.
Interaction partners:
Sequence:
MDGAAGPGDGPAREALQSLSQRLRVQEQEMELVKAALAEALRLLRLQVPPSSLQGSGTPAPPGDSLAAPPGLPPTCTPSLVSRGTQTETEVELKSSPGPPGLSNGPPAPQGASEEPSGTQSEGGGSSSSGAGSPGPPGILRPLQPPQRADTPRRNSSSSSSPSERPRQKLSRKAISSANLLVRSGSTESRGGKDPLSSPGGPGSRRSNYNLEGISVKMFLRGRPITMYIPSGIRSLEELPSGPPPETLSLDWVYGYRGRDSRSNLFVLRSGEVVYFIACVVVLYRPGGGPGGPGGGGQRHYRGHTDCVRCLAVHPDGVRVASGQTAGVDKDGKPLQPVVHIWDSETLLKLQEIGLGAFERGVGALAFSAADQGAFLCVVDDSNEHMLSVWDCSRGMKLAEIKSTNDSVLAVGFNPRDSSCIVTSGKSHVHFWNWSGGVGVPGNGTLTRKQGVFGKYKKPKFIPCFVFLPDGDILTGDSEGNILTWGRSPSDSKTPGRGGAKETYGIVAQAHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWGPGLVALQEAEIPEHFGAVRAIAEGLGSELLVGTTKNALLRGDLAQGFSPVIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGESHALAWSIDLKETGLCADFHPSGAVVAVGLNTGRWLVLDTETREIVSDVIDGNEQLSVVRYSPDGLYLAIGSHDNVIYIYSVSSDGAKSSRFGRCMGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGCKQLKNRYESRDREWATYTCVLGFHVYGVWPDGSDGTDINSLCRSHNERVVAVADDFCKVHLFQYPCARAKAPSRMYGGHGSHVTSVRFTHDDSHLVSLGGKDASIFQWRVLGAGGAGPAPATPSRTPSLSPASSLDV
Protein: 1,3,6,8-tetrahydroxynaphthalene synthase (THNS) (EC 2.3.1.233) (1,3,6,8-tetrahydroxynaphthalene synthesis polyketide synthase type III) (B0FYK7)
Organism: Streptomyces peucetius subsp. caesius
Function: Involved in the biosynthesis of melanin but also various secondary metabolites containing a naphthoquinone ring. Catalyzes the iterative condensation of five CoA-linked malonyl units to form a pentaketide intermediate. THNS subsequently catalyzes the dual intramolecular Claisen and aldol condensations of this linear intermediate to produce the fused ring of 1,3,6,8-tetrahydroxynaphthalene (THN).
Interaction partners:
Sequence:
MRVPVAVDDLVAPSTMGERHTVIDRGTSVAAVHTALPPHRYAQSDLTELIADLCLEPGADRALLRRLHTSAGVRTRHLALPIEQYAGLGDFGQANAAWLTVGLALAEEALSGALDAAGLTAADIDLLVCTSITGVAAPSLDARLAVRMGMRADVKRVPVFGLGCVGGAAGLGRLHDYLLGHPDDTAVLLSVELCSLTLQRDGSLANLVAGALFGDGAAAVVARGGDAGRRGAGWPMVAATRGHLYPDTEHLLGWRIGASGFRVVVDAGIPDVVRTHLGGDLRNFLATHGLVPDDIGTWICHPGGPKVLAAVGDALELPDGALDSSWRSLAGVGNLSSASVLRVLEDVATRCRPDPGTWGVLLAMGPGFCAEFVLLRW
Protein: Dihydrouridine synthase 2 (I3L4H0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MILNSLSLCYHNKLILAPMVRVGTLPMRLLALDYGADIVYCEELIDLKMIQCKRVVNEVLSTVDFVAPDDRVVFRTCEREQNRVVFQMGTSDAERALAVARLVENDVAGIDVNMGCPKQYSTK
Protein: Ubiquitin fusion degradation protein 1 homolog (Q9U3I6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MFANFFQQQLRRTTRHFDLIVYGPVFLPNATQSKISEINYGGKILLPSSALNLLMQYNIPMPMLFKLTNMAVQRVTHCGVLEFSAPEGQAILPLWMMQQLGLDDGDTIRIESATLPKATFAKLKPMSLEFLNITNPKAVLEVELRKYACLTKNDRIPTSYAGQTLEFLVVDLKPANSVCIIECDVNLDFDPPEGYVEQPRQVTPAVTAKPPAPDASAFIGAGQKAGGSGGTGQNATSVFGGAGRRLDGKKKPSSSVSLSDGTGVSTSNAAPVANDLPAIPPVVVNEDYKPGRVSFLRYDYKRVDVLEKELREKEASKAGQPSNVFRGGNRTLRGAR
Protein: At5g18850 (Low-density receptor-like protein) (Q6NLF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASPSSSPTTRIWFRTVILIALMVVLFYVGRPLYWKISATIHDIRHNKQSVREGISQIVHEAQRSVGWYHDESDSGFREGHNKKSGIAVSRRLLFAGDQ
Protein: Kunitz/Bovine pancreatic trypsin inhibitor domain protein (G3MVG9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MIPRGLITLSHYHEKLKFSQNRQRQRLDDRRCSLDFRISLIILSQLIPLISCRSEVCWDKFDMNYRNQCMNGQWQQRYYFDHASLTCRQFWFDGCRSDSRNIFDDELTCQWLCESQPMYKSRSCLEDFDEGLKKECNGGRWRHQWYFDKGSKKCFSFWYDGCKGANENIFQDELSCLHTCENPAKKDPKKPWHNNDKFKMKEIIGDIYKPNLTDTCLAKNPCKNNGTCIFVWKKDTHYCKCQPGFHGNNCDKVVDYDPCAEKPCLNGATCQIKYNDDDVDEKPTFECFCAAGFGGPKCDQRPCESNPCLNNGTCRTTKGYSTYFCECANGFGGKNCDVSIGNTPPEEKFGKNVEQISSGKEEWIAQMRQRLKETGGGIGGASGSGLKSENGTMGGSSGEKSGEKKSGKNKKSKATQVADEPYKDPATRKREREEREKKEAEIQAAEEEEKQRKEYEEDAQRKKAEEMELEAKKALEAANFGLKTDFSMSLLTILMAFVLREF
Protein: Coatomer subunit delta (Archain) (Delta-coat protein) (Delta-COP) (Q5XJY5)
Organism: Mus musculus (Mouse)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit epsilon
- Coatomer subunit beta'
- Coatomer subunit beta
- Coatomer subunit alpha
- Coatomer subunit gamma-1
- Coatomer subunit zeta-1
- Coatomer subunit gamma-2
- ADP-ribosylation factor GTPase-activating protein 2
- Coatomer subunit zeta-2
- Transmembrane emp24 domain-containing protein 10
Sequence:
MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAAMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGETIMSSNMGKRTSEATKVHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKFGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEKSFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDAKNKSGSLEFSIPGQPNDFFPVQVSFISKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKYEIL
Protein: ECF RNA polymerase sigma factor SigE (ECF sigma factor SigE) (Alternative RNA polymerase sigma factor SigE) (RNA polymerase sigma-E factor) (Sigma-E factor) (P9WGG7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released. Responds to heat shock and surface stress (detergent exposure). When combined with isolated core RNA polymerase from M.smegmatis is able to guide initiation from the sigB promoter. Required for full expression of sigB, and for sigB induction after detergent exposure but not after heat shock. Controls a regulon of about 38 genes in culture and about 16 genes during macrophage infection, most of which have decreased expression in a disruption mutant. Probably down regulates the host immune response to mycobacterial infection.
Interaction partners:
- Anti-sigma-E factor RseA
- RNA polymerase sigma factor SigB
- Conserved protein
- Anti-sigma factor RshA
Sequence:
MELLGGPRVGNTESQLCVADGDDLPTYCSANSEDLNITTITTLSPTSMSHPQQVRDDQWVEPSDQLQGTAVFDATGDKATMPSWDELVRQHADRVYRLAYRLSGNQHDAEDLTQETFIRVFRSVQNYQPGTFEGWLHRITTNLFLDMVRRRARIRMEALPEDYDRVPADEPNPEQIYHDARLGPDLQAALASLPPEFRAAVVLCDIEGLSYEEIGATLGVKLGTVRSRIHRGRQALRDYLAAHPEHGECAVHVNPVR
Protein: ATP-dependent RNA helicase HAS1 (EC 3.6.4.13) (Helicase associated with SET1 protein 1) (Q03532)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:15049817}.
Interaction partners:
- Nucleolar complex-associated protein 3
- Ribosome biogenesis protein NSA2
- Ribosome assembly factor MRT4
- Ribosome biogenesis protein BMS1
- Ribosome biogenesis protein SSF1
- 27S pre-rRNA
- Pumilio homology domain family member 6
- Ribosome production factor 1
- Ribosome biogenesis protein YTM1
- Ribosome biogenesis protein RLP24
Sequence:
MATPSNKRSRDSESTEEPVVDEKSTSKQNNAAPEGEQTTCVEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTGIIVITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFEDEMRQIIKILPNEDRQSMLFSATQTTKVEDLARISLRPGPLFINVVPETDNSTADGLEQGYVVCDSDKRFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKGKGKSLMFLTPNELGFLRYLKASKVPLNEYEFPENKIANVQSQLEKLIKSNYYLHQTAKDGYRSYLQAYASHSLKTVYQIDKLDLAKVAKSYGFPVPPKVNITIGASGKTPNTKRRKTHK
Protein: Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Suppressor of actin mutations 1-like protein) (Q9EP69)
Organism: Mus musculus (Mouse)
Function: Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 3-phosphate (PtdIns(3)P) and has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) (By similarity). Shows a very robust PtdIns(4)P phosphatase activity when it binds PtdIns(4)P in a 'cis' configuration in the cellular environment, with much less activity seen when it binds PtdIns(4)P in 'trans' configuration (By similarity). PtdIns(4)P phosphatase activity (when it binds PtdIns(4)P in 'trans' configuration) is enhanced in the presence of PLEKHA3 (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ES21}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NTJ5}; Multi-pass membrane protein {ECO:0000255}. Note=Trafficking between the ER and Golgi is regulated by nutrient status and by TMEM39A. Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS) in the presence of phosphatidylinositol-4,5-bisphosphate. {ECO:0000250|UniProtKB:Q9NTJ5}.
Interaction partners:
- Inositol polyphosphate 5-phosphatase OCRL
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol 4-kinase type 2-alpha
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Myotubularin
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MAAAAYEHLKLHITPEKFYVEACDDGADDVLIIDRVSTEVTLAVKKDVPPSAVTRPIFGILGTIHLVAGNYLVVITKKMKVGECFNHAVWRATDFDVLSYKKTMLHLTDIQLQDNKTFLAMLNHVLSMDGFYFSTTYDLTHTLQRLSNTSPEFQEMSLLERADQRFVWNGHLLRELSAQPEVHRFALPVLHGFITMHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYSGNRASFVQTRGSIPIFWSQRPNLKYKPHPQISKVANHMDGFQRHFDSQVIIYGKQVIINLVNHKGSEKPLEQTFANMVSSLGSGMIRYIAFDFHKECKNMRWDRLSILLDQVAEMQDELSYFLVDSAGKVVTNQDGVFRSNCMDCLDRTNVIQSLLARRSLQAQLQRLGVLHVGQKLEEQDEFEKTYKNAWADNANACAKQYAGTGALKTDFTRTGKRTQLGLLMDGFNSLLRYYKNNFSDGFRQDSIDLFLGNYSVDELESHSPLSVPRDWKFLALPIIMVVAFSMCIICLLMAGDTWTETLAYVLFWGVASIGTFFIILYNGKDFVDAPRLVQKEKID