wanglab/gogpt-training-data huggingface dataset:
Protein: Protease ElaD (EC 3.4.22.-) (Deubiquitinase) (Deubiquitinating enzyme) (DUB) (Deubiquitinating protease) (Q47013)
Organism: Escherichia coli (strain K12)
Function: Protease that can act as an efficient and specific deubiquitinating enzyme in vitro. Does not possess desumoylating and deneddylating activities. The physiological substrate is unknown.
Interaction partners:
- Protease 2
- Evolved beta-galactosidase subunit alpha
Sequence:
MMVTVVSNYCQLSQTQLSQTFAEKFTVTEELLQSLKKTALSGDEESIELLHNIALGYDKFGKEAEDILYHIVRTPTNETLSIIRLIKNACLKLYNLAHIATNSPLKSHDSDDLLFKKLFSPSKLMTIIGDEIPLISEKQSLSKVLLNDENNELSDGTNFWDKNRQLTTDEIACYLQKIAANAKNTQVNYPTGLYVPYSTRTHLEDALNENIKSDPSWPNEVQLFPINTGGHWILVSLQKIVNKKNNKLQIKCVIFNSLRALGYDKENSLKRVINSFNSELMGEMSNNNIKVHLNEPEIIFLHADLQQYLSQSCGAFVCMAAQEVIEQRESNSDSAPYTLLKNHADRFKKYSAEEQYEIDFQHRLANRNCYLDKYGDANINHYYRNLEIKHSQPKNRASGKRVS
Protein: Probable protein phosphatase 2C 73 (AtPP2C73) (EC 3.1.3.16) (AtPPC6;7) (Q0WRB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Microfibrillar-associated protein-like protein
- Microfibril-associated protein-like
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' alpha isoform
- Phosphatidylinositol-3-phosphatase myotubularin-2
- Ankyrin repeat-containing protein ITN1
- Sphingoid long-chain bases kinase 1
- Structural maintenance of chromosomes protein 1
- Clathrin light chain 1
- Sphingosine kinase 1
- Inositol diphosphatase DSP1
Sequence:
MGHFSSMFNGLARSFSIKKVKNNNGNCDAKEAADEMASEAKKKELILKSSGYVNVQGSNNLASLFSKRGEKGVNQDCALVWEGFGCQEDMIFCGIFDGHGPWGHYVAKQVRNSMPLSLLCNWQKILAQATLEPELDLEGSNKKISRFDIWKQSYLKTCATVDQELEHHRKIDSYYSGTTALTIVRQGEVIYVANVGDSRAVLAMESDEGSLVAVQLTLDFKPNLPQEKERIIGCKGRVFCLDDEPGVHRVWQPDAETPGLAMSRAFGDYCIKEYGLVSVPEVTQRHISTKDHFIILASDGIWDVISNQEAIEIVSSTAERPKAAKRLVEQAVRAWKKKRRGYSMDDMSVVCLFLHSSSSSSLSQHHHAMTILK
Protein: Annexin B10 (Annexin X) (Annexin-10) (P22465)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Sperm-specific dynein intermediate chain 1, isoform A
- GH16657p
- Cytoplasmic dynein 1 intermediate chain
- Sperm-specific dynein intermediate chain 2, isoform A
- GEO12096p1
Sequence:
MEYKPVPTVKDAAPFDASQDAQVLRAAMKGFGTDEQEIIDVLVGRSNQQRQTIKAVYEAEFERDLVDDLKDELGGKFEDVIVGLMMPPVEYLCKQLHAAMAGIGTEEATLVEILCTKTNEEMAQIVAVYEERYQRPLAEQMCSETSGFFRRLLTLIVTGVRDGLDTPVDVGQAKEQAAQLYSAGEAKLGTDEEVFNRIMSHASFPQLRLVFEEYKVLSGQTIEQAIKHEMSDELHEAMMAIVECVQSPAAFFANRLYKAMNGAGTDDATLIRIIVSRSEIDLETIKQEFERIYNRTLHSAVVDAETSGDYKRALTALLGSA
Protein: CENP-A histone chaperone scm3 (Q9HDY7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Histone acetyltransferase type B subunit 2
- Histone H4
- Histone H3-like centromeric protein cnp1
- Histone H3.1/H3.2
- NASP-related protein sim3
- CENP-A recruiting complex protein mis19
- CENP-A recruiting complex protein mis20
- Inner kinetochore subunit mis6
- Histone H3.3
- Histone H2A.Z-specific chaperone chz1
Sequence:
MCNRQPKAVDLPPNYSCPHLLSFQSVEFNTNPTACDDVFCKRIESEKKYNDFLESLFKKYGRDTSDIADEVDLATGEIIVNNGHLEALKTKDDIWDPTFNNLEISASNGYEKKLDSSIGNPGEKAVSPVHIEDFQSPQIYKFKNLSLRDEMVSDCVFADEVPLASLFVENVCNETIPSQSCVRLKINDKTRKVDASALEKKSCLLPNSSGTLTDQRGLDTIKHKSIEQNEILHVISDTLSSPRRRNPLLSSPKTPLRRSFSKSKVRNSNSTKRRNFISLISMISPRPNLSTHHFNLGFQPLSQQTSFSGSSTQNPHSSSTCKKAFCFQCISESKKC
Protein: Lupeol synthase (EC 5.4.99.41) (Q8W3Z2)
Organism: Betula platyphylla (Asian white birch)
Function: Oxidosqualene cyclase involved in the biosynthesis of lupeol.
Interaction partners:
Sequence:
MWKLKIAEGGPGLVSGNDFIGRQHWEFDPDAGTPQERAEVEKVREEFTKNRFQMKQSADLLMRMQLRKENPCQPIPPPVKVKETEVITEEAVITTLRRSLSFYSSIQAHDGHWPGESAGPLFFLQPFVMALYITGDLNTIFSPAHQKEIIRYLYNHQNEDGGWGFHIEGHSTMFGSALSYIALRILGEGLEDGEDGAMAKSRKWILDHGGLVAIPSWGKFWVTVLGLYEWSGCNPLPPEFWFLPDIFPIHPGKMLCYCRLVYMPMSYLYGKRFVGPITGLIQSLRQELYNEPYHQINWNKARSTVAKEDLYYPHPLIQDLLWGFLHHVAEPVLTRWPFSMLREKALKAAIGHVHYEDENSKYLCIGSVEKVLCLIACWAEDPNGEAYKLHLGRIPDNYWVAEDGLKIQSFGCQMWDAGFAIQAILSCNLNEEYWPTLRKAHEFVKASQVPENPSGDFKAMYRHINKGAWTFSMQDHGWQVSDCTAEGLKVAILFSQMPPDLVGEKIEKERLYDAVNVILSLQSSNGGFPAWEPQRAYGWLEKFNPTEFFEDTLIEREYVECTSPAVHGLALFRKFYPRHRGTEIDSSIYRGIQYIEDVQEPDGSWYGHWGICYTYGTWFAVGALAACGRNYKNCPALRKSCEFLLSKQLPNGGWGESYLSSQNKVWTNIEGNRANLVQTAWALLSLIDARQAEIDPTPIHRGVRVLINSQMEDGDFPQQEITGVFMRNCTLNYSSYRNIFPIWALGEYRRRVLFA
Protein: Ly6/PLAUR domain-containing protein 3 (GPI-anchored metastasis-associated protein C4.4A) (O55162)
Organism: Rattus norvegicus (Rat)
Function: Supports cell migration. May be involved in tumor progression.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Anterior gradient 2, protein disulphide isomerase family member
Sequence:
MDAARRGDTQPVMWTTRWLLLLPLLLCEGAQALECYSCVQKADDGCSPHKMKTVKCGPGVDVCTEAVGAVESIHGQFSVAVRGCGSGIPGKNDRGLDLHGLLAFIQLQQCTEDRCNAKLNLTLRGLNPAGNESAYEHNGAECYSCMGLSREKCQGAMPPVVNCYNASGRVYKGCFDGNVTLTAANVTVSLPVRGCVQDEACTRDGVTGPGFTLSGSCCQGPRCNSDLRNKTYFSPRIPPLVLLPPPTTPAPSTRTQNSSSTTSTTAPTTATTTIKPTTVQASHTSSTHETEHEVIQEEGSHLSGGATGHQDRSNMGKFPEKGGAQIPSKGGSDALGSWLSAILLTVVAGAML
Protein: Serine/threonine protein kinase UL97 (EC 2.7.11.1) (Q6SW46)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Serine/threonine protein kinase that plays important roles in several processes including nuclear viral egress, viral replication or regulation of host cell cycle progression. Participates in the acquisition of tegument during virion morphogenesis in the nucleus. Redistributes the host nuclear lamina by phosphorylating cellular Lamins-A/C. Plays a role in viral DNA synthesis by phosphorylating the DNA polymerase processivity factor UL44. Stimulates host cell cycle to support viral DNA synthesis by phosphorylating host retinoblastoma/RB1 protein. Additional substrates have been identified including host EF1D or H2B. Phosphorylates also host SAMHD1 and thereby counteracts its antiviral effect by reducing its dNTP hydrolase activity.
Subcellular location: Virion {ECO:0000250}.
Interaction partners:
Sequence:
MSSALRSRARSASLGTTTQGWDPPPLRRPSRARRRQWMREAAQAAAQAAVQAAQAAAAQVAQAHVDEDEVVDLMTDEAGGGVTTLTTLSSVSTTTVLGHATFSACVRSDVMRDGEKEDAASDKENQRRPVVPSTSSRGSAASGDGYHGLRCRETSAMWSFEYDRDGDVTSVRRALFTGGSDPSDSVSGVRGGRKRPLRPPLVSLARTPLCRRRVGGVDAVLEENDVELRAESQDSAVASGPGRVPQPLSGSSGEESATAVEADSTSHDDVHCTCSNDQIITTSIRGLTCDPRMFLRLTHPELCELSISYLLVYVPKEDDFCHKICYAVDMSDESYRLGQGSFGEVWPLDRYRVVKVARKHSETVLTVWMSGLIRTRAAGEQQQPPSLVGTGVHRGLLTATGCCLLHNVTVHRRFHTDMFHHDQWKLACIDSYRRAFCTLADAIKFLNHQCRVCHFDITPMNVLIDVNPHNPSEIVRAALCDYSLSEPYPDYNERCVAVFQETGTARRIPNCSHRLRECYHPAFRPMPLQKLLICDPHARFPVAGLRRYCMSELSALGNVLGFCLMRLLDRRGLDEVRMGTEALLFKHAGAACRALENGKLTHCSDACLLILAAQMSYGACLLGEHGAALVSHTLRFVEAKMSSCRVRAFRRFYHECSQTMLHEYVRKNVERLLATSDGLYLYNAFRRTTSIICEEDLDGDCRQLFPE
Protein: Astacin-like metalloendopeptidase (EC 3.4.-.-) (Oocyte astacin) (Ovastacin) (Sperm acrosomal SLLP1-binding protein) (Q6HA09)
Organism: Mus musculus (Mouse)
Function: Oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization. Plays a role in the polyspermy inhibition. Probably acts as a protease for the post-fertilization cleavage of ZP2. Cleaves the sperm-binding ZP2 at the surface of the zona pellucida after fertilization and cortical granule exocytosis, rendering the zona pellucida unable to support further sperm binding.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22206759, ECO:0000269|PubMed:22472438}. Cell membrane {ECO:0000269|PubMed:22206759}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000269|PubMed:22472438}. Note=Probably exocytosed from cortical granules during post-fertilization. Detected throughout the ooplasm of germinal vesicle stage oocytes in early bilaminar secondary follicles at postnatal (PN) day 3. Detected in the microvillar domain of the oolemma in arrested ovulated secondary oocytes and in the first polar body prior to fertilization. Upon fertilization, detected in the perivitelline space (PVS) and occasionally on the oolemma in 2-cell through morulae stages. Colocalizes with SPACA3 at the microvillar domain of the oolemma and in the perivitelline space (PVS). {ECO:0000269|PubMed:22472438}.
Interaction partners:
- Zona pellucida sperm-binding protein 2
- Zona pellucida sperm-binding protein 1
Sequence:
MGIMGSLWPWILTMLSLLGLSMGAPSASRCSGVCSTSVPEGFTPEGSPVFQDKDIPAINQGLISEETPESSFLVEGDIIRPSPFRLLSVTNNKWPKGVGGFVEIPFLLSRKYDELSRRVIMDAFAEFERFTCIRFVAYHGQRDFVSILPMAGCFSGVGRSGGMQVVSLAPTCLRKGRGIVLHELMHVLGFWHEHSRADRDRYIQVNWNEILPGFEINFIKSRSTNMLVPYDYSSVMHYGRFAFSWRGQPTIIPLWTSSVHIGQRWNLSTSDITRVCRLYNCSRSVPDSHGRGFEAQSDGSSLTPASISRLQRLLEALSEESGSSAPSGSRTGGQSIAGLGNSQQGWEHPPQSTFSVGALARPPQMLADASKSGPGAGADSLSLEQFQLAQAPTVPLALFPEARDKPAPIQDAFERLAPLPGGCAPGSHIREVPRD
Protein: Thymopoietin a (Q5RGX4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Emerin
- Barrier-to-autointegration factor-like protein
- Lamin B receptor.
- Lamin A
- Lamin-B2
- Barrier-to-autointegration factor
Sequence:
MSEFLEDPSVLTKDKLKSALLANNVALPNGDQRKDVYVQLYLKNLTVQNKKSSGSPDVFSSDEELPPAPVVSNRSRSGRKATRKTDKVRPDDVDVTELSNEGLKDLLLKYGLNAGPIVASTRKVYEKRLQKLLDQGPPVAVALPSETSQTDGNQNGNNDSDQYSDREEEPVAPAPVTVPEPEVEAELIPVVERPVRSRGKTPVTSRTRSGQHTREDVEEEDWPVLNVKRKLKRSSHRPDQMVPASDDTENSELSSAECFAVSEDRRRTGPGAGRRETRPLLSDRTSKLSSKSESLRRRSAPVRSVLNEASSSDKDFSEPSIVKEVSVSLMRMKVQPLTVPKDPKPSKRYSMSATESTKRPVSSLNNKHDENTADIPSPPHRQSSREPLVSLINTACVEVDDQGMQDVLSCRSANGGLLAQGVRSAAVSKLSKPVLSQSKPSKPLVDMMCCLSPSSDRQKEVFPSHSLPYKNFCLVSEDSLTVSCELSQESCGSPQTHPKSRHSKITPFLSQITPVRGLDNKLMDMKETMMVEKVSAIDQTPRAVERDVLKEIFPTENLNTPTGISATCRRPIRGAAGRPLIDTWLNESRQRLSDLKQTTSSSSFSSTSSYTESRSVPRVSSIPLSASKSTAPPTVKSRSRRSLPVWVQLVLLSAVAGFLFFIYQAMETNDVGLFKQSGTDDSTSK
Protein: Condensin-1 complex subunit CAP-D2 (Protein CHROMOSOME-ASSOCIATED POLYPEPTIDE D-2) (AtCap-D2) (A0A1I9LM04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes (By similarity). The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity). Required for fertility, growth and euchromatin organization, but not for sister chromatid cohesion. Necessary to maintain normal structural integrity of the meiotic chromosomes during the two nuclear divisions of gametogenesis, especially to maintain compaction of the centromeric repeats and 45S rDNA. Seems also involved in crossover formation during meiotic prophase I. Prevents centromeric and pericentromeric heterochromatin repeats association. Contributes to the induction of stress-responsive genes in response to stress treatment.
Subcellular location: Chromosome {ECO:0000269|PubMed:25065716}. Nucleus {ECO:0000250|UniProtKB:Q15021}. Note=Associates with the chromosomes throughout meiosis. {ECO:0000269|PubMed:25065716}.
Interaction partners:
Sequence:
MAPPFVFPQILRALEEDPEDNHRLFAQNPVDVTSLRPSDLEEFVKGVSFDLSDRELFCVEDQDVFDRVYSLVRSFFSLPPSCKCNLVESLRSNLSVLLPNVDSISRSVQDQEDDVPIIDRITSHRNALKIYTFFLLTVVMNEESHISSVETTKVAARGRKKQIIQSWNWEPQRGRMLNLIANSLEINLSLLFGSSDLDENYLSFIVKNSFTLFENATILKDAETKDALCRIIGASATKYHYIVQSCASIMHLIHKYDFAVVHIADAVARAESKYSDGTLAVTIIRDIGRTDPKAYVKDTAGADNVGRFLVELADRLPKLMSTNVGVLVPHFGGESYKIRNALVGVLGKLVAKAFNDVEGDMSSKSLRLRTKQAMLEILLERCRDVSAYTRSRVLQVWAELCEEHSVSIGLWNEVASLSAGRLEDKSAIVRKSALNLLIMMLQHNPFGPQLRIASFEATLEQYKRKLNELEPTEHASKESTSDGESCNGDGEIDDLHLETTTKIHQDSLSDSCQPENGEEISEKDVSVPDIGNVEQTKALIASLEAGLRFSKCMSASMPILVQLMASSSATDVENAILLLMRCKQFQIDGAEACLRKILPLAFSQDKSIYEAVENAFISIYIRKNPVDTAKQLLNLAIDSNIGDQAALEFIVNALVSKGEISSSTTSALWDFFCFNINGTTAEQSRGALSILCMAAKSSPRILGSHIQDIIDIGFGRWAKVEPLLARTACTVIQRFSEEDRKKLLLSSGSRLFGILESLITGNWLPENIYYATADKAISAIYMIHPTPETLASTIIKKSLSTVFDVVEQEEAQTDTENNKVDILTPVQVAKLSRFLFAVSHIAMNQLVYIESCIQKIRRQKTKKDKPAAESQNTEENLEATQENNGINAELGLAASDDALLDTLAERAEREIVSGGSVEKNLIGECATFLSKLCRNFSLLQKHPELQASAMLALCRFMIIDASFCESNLQLLFTVVENAPSEVVRSNCTLSLGDLAVRFPNLLEPWTENMYARLRDASVSVRKNAVLVLSHLILNDMMKVKGYIYEMAICIEDDVERISSLAKLFFHELSKKGSNPIYNLLPDILGQLSNRNLERESFCNVMQFLIGSIKKDKQMEALVEKLCNRFSGVTDGKQWEYISYSLSLLTFTEKGIKKLIESFKSYEHALAEDLVTENFRSIINKGKKFAKPELKACIEEFEEKINKFHMEKKEQEETARNAEVHREKTKTMESLAVLSKVKEEPVEEYDEGEGVSDSEIVDPSMEESGDNLVETESEEEPSDSEEEPDSAQCGTAIPRYLNQKTSGDNLIETEPEEEQSDSEPDSAQCGTTNPRSLNRKTSGDNLIETESEEEQSDSEEEPSDSEEEPDSAQCGTTNPRSLNQKTSGGEEGESESKSTESSSSIRRNLRSGSRS
Protein: Elongation factor 1-alpha (Q3LUM6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWHKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFGPSGLTTEVKSVEMHHEALSEALPGDNVGFNVKNVAVKDLKRGFVASNSKDDPAKEAASFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSELLTKIDRRSGKELEKEPKFLKNGDAGMIKMVPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKSAAKKK
Protein: Transmembrane protein 132A (HSPA5-binding protein 1) (Q24JP5)
Organism: Homo sapiens (Human)
Function: May play a role in embryonic and postnatal development of the brain. Increased resistance to cell death induced by serum starvation in cultured cells. Regulates cAMP-induced GFAP gene expression via STAT3 phosphorylation (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
Sequence:
MCARMAGRTTAAPRGPYGPWLCLLVALALDVVRVDCGQAPLDPVYLPAALELLDAPEHFRVQQVGHYPPANSSLSSRSETFLLLQPWPRAQPLLRASYPPFATQQVVPPRVTEPHQRPVPWDVRAVSVEAAVTPAEPYARVLFHLKGQDWPPGSGSLPCARLHATHPAGTAHQACRFQPSLGACVVELELPSHWFSQASTTRAELAYTLEPAAEGPGGCGSGEENDPGEQALPVGGVELRPADPPQYQEVPLDEAVTLRVPDMPVRPGQLFSATLLLRHNFTASLLTLRIKVKKGLHVTAARPAQPTLWTAKLDRFKGSRHHTTLITCHRAGLTEPDSSPLELSEFLWVDFVVENSTGGGVAVTRPVTWQLEYPGQAPEAEKDKMVWEILVSERDIRALIPLAKAEELVNTAPLTGVPQHVPVRLVTVDGGGALVEVTEHVGCESANTQVLQVSEACDAVFVAGKESRGARGVRVDFWWRRLRASLRLTVWAPLLPLRIELTDTTLEQVRGWRVPGPAEGPAEPAAEASDEAERRARGCHLQYQRAGVRFLAPFAAHPLDGGRRLTHLLGPDWLLDVSHLVAPHARVLDSRVASLEGGRVVVGREPGVTSIEVRSPLSDSILGEQALAVTDDKVSVLELRVQPVMGISLTLSRGTAHPGEVTATCWAQSALPAPKQEVALSLWLSFSDHTVAPAELYDRRDLGLSVSAEEPGAILPAEEQGAQLGVVVSGAGAEGLPLHVALHPPEPCRRGRHRVPLASGTAWLGLPPASTPAPALPSSPAWSPPATEATMGGKRQVAGSVGGNTGVRGKFERAEEEARKEETEAREEEEEEEEEMVPAPQHVTELELGMYALLGVFCVAIFIFLVNGVVFVLRYQRKEPPDSATDPTSPQPHNWVWLGTDQEELSRQLDRQSPGPPKGEGSCPCESGGGGEAPTLAPGPPGGTTSSSSTLARKEAGGRRKRVEFVTFAPAPPAQSPEEPVGAPAVQSILVAGEEDIRWVCEDMGLKDPEELRNYMERIRGSS
Protein: Energy-coupling factor transporter ATP-binding protein EcfA1 (ECF transporter A component EcfA1) (EC 7.-.-.-) (Q9X1Z1)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:23359690}; Peripheral membrane protein {ECO:0000305|PubMed:23359690}.
Interaction partners:
- Energy-coupling factor transporter transmembrane protein EcfT
- Energy-coupling factor transporter ATP-binding protein EcfA2
- Biotin transporter BioY
- iron
- Conserved hypothetical protein
- Conserved hypothetical protein
- Hypothetical protein
- Peptide deformylase
- 5'-nucleotidase SurE
- Succinyl-diaminopimelate desuccinylase, putative
Sequence:
MKITLNSVSFRYNGDYVLKDVNAEFETGKIYVVVGKNGSGKTTLLKILAGLLEAEGEIFLDGSPADPFLLRKNVGYVFQNPSSQIIGATVEEDVAFSLEIMGLDESEMRKRIKKVLELVGLSGLEKEDPLNLSGGQKQRLAIASMLARDTRFLALDEPVSMLDPPSQREIFQVLESLKNEGKGIILVTHELEYLDDMDFILHISNGTIDFCGSWEEFVEREFDDVEIPFKWKLWKKCGKINLWEDRYENSGNQRRRDTV
Protein: Protein S100-A1 (S-100 protein alpha chain) (S-100 protein subunit alpha) (S100 calcium-binding protein A1) (P23297)
Organism: Homo sapiens (Human)
Function: Small calcium binding protein that plays important roles in several biological processes such as Ca(2+) homeostasis, chondrocyte biology and cardiomyocyte regulation. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers conformational changes. These changes allow interactions with specific target proteins and modulate their activity. Regulates a network in cardiomyocytes controlling sarcoplasmic reticulum Ca(2+) cycling and mitochondrial function through interaction with the ryanodine receptors RYR1 and RYR2, sarcoplasmic reticulum Ca(2+)-ATPase/ATP2A2 and mitochondrial F1-ATPase. Facilitates diastolic Ca(2+) dissociation and myofilament mechanics in order to improve relaxation during diastole.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15171681}. Sarcoplasmic reticulum {ECO:0000269|PubMed:12804600}. Mitochondrion {ECO:0000250|UniProtKB:P56565}.
Interaction partners:
- Protein S100-B
- Annexin A2
- Ryanodine receptor 2
- Protein S100-P
- Toll-like receptor 4
- Protein S100-A2
- Ryanodine receptor 1
- Protein S100-A7
- Protein S100-A4
- Advanced glycosylation end product-specific receptor
Sequence:
MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
Protein: SH3 domain-containing protein 21 (A4FU49)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVQSELQLQPRAGGRAEAASWGDRGNDKGGLGNPDMPSVSPGPQRPPKLSSLAYDSPPDYLQTVSHPEVYRVLFDYQPEAPDELALRRGDVVKVLSKTTEDKGWWEGECQGRRGVFPDNFVLPPPPIKKLVPRKVVSRESAPIKEPKKLMPKTSLPTVKKLATATTGPSKAKTSRTPSRDSQKLTSRDSGPNGGFQSGGSYHPGRKRSKTQTPQQRSVSSQEEEHSSPVKAPSVKRTPMPDKTATPERPPAPENAPSSKKIPAPDKVPSPEKTLTLGDKASIPGNSTSGKIPAPDKVPTPEKMVTPEDKASIPENSIIPEETLTVDKPSTPERVFSVEESPALEAPPMDKVPNPKMAPLGDEAPTLEKVLTPELSEEEVSTRDDIQFHHFSSEEALQKVKYFVAKEDPSSQEEAHTPEAPPPQPPSSERCLGEMKCTLVRGDSSPRQAELKSGPASRPALEKPHPHEEATTLPEEAPSNDERTPEEEAPPNEQRPLREEVLPKEGVASKEEVTLKEELPPKEEVAPKEEVPPIERAFAQKTRPIKPPPDSQETLALPSLVPQNYTENKNEGVDVTSLRGEVESLRRALELMEVQLERKLTDIWEELKSEKEQRRRLEVQVMQGTQKSQTPRVIHTQTQTY
Protein: Serine/Arginine-related protein 53 (SRrp53) (Arginine/serine-rich coiled-coil protein 1) (Q9DBU6)
Organism: Mus musculus (Mouse)
Function: Plays a role in pre-mRNA splicing. Involved in both constitutive and alternative pre-mRNA splicing. May have a role in the recognition of the 3' splice site during the second step of splicing (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15798186}. Nucleus speckle {ECO:0000269|PubMed:15798186}. Cytoplasm {ECO:0000269|PubMed:15798186}. Note=Shuttles between the nucleus and cytoplasm.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein eL24
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL30
Sequence:
MGRRSSDTEEESRSKRKKKHRRRSSSSSSSDSRTYSRKKGGRRPRSDSRSWSRDRQLRSHSYERRRRRRSSSSSSYGSRRKRSRSRSRGRGKPYRVQRSRSKSRTRRSRSRPRPRSHSRSSERSSHRRTRSRSRDRDRRKVRDKEKREKEKDKGKDKEVHSIKRGDSGNIKAGLEHLPPAEQAKARLQLVLEAAAKADEALKAKERSEEEAKRRKEEDQATLVEQVKRVKEIEAIESDSFVQQTFRSSKDVKKAVEPSEVQHVTAASGPASAAAEPPSTGKEIDPDSIPTAIKYQDDNSLAHPNLFIEKAEAEEKWFKRLIALRQERLMGSPVA
Protein: Non-reducing polyketide synthase aptA (NRPKS) (EC 2.3.1.-) (Asperthecin synthesis protein A) (Q5B0D0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Non-reducing polyketide synthase (NRPKS); part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Through its product template (PT) domain, catalyzes the cyclization of the polyketide backbone via C6-C11 aldolcondensation. Polyketide is subsequently hydrolyzed from the NRPKS by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster. Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin.
Interaction partners:
Sequence:
MKDNTHSTTLIFFGNEFPNDDLKGLFRCLLRLSKDRRFRQLAAFLEESTLVLKKEVAALPQPLRDLVPHFHTVLPLAELGDFRQGPLGAAMESALLTVLELGMFIGHYEAEGRDWNLLEHNTTLAGLSIGLLAAAGVALSTNLAEVAQNGAECVRVSFRLGVYVSEISRKLEAPQADGTLLSWAHVVTGETKSAIQDELSKYNSESGTPELLKVFISAADKTSVSVSGPPSRMKACFSSSHLLRYSKSFALPVYDGLCHASHLYNEDSINTVINSAESVIPVSRPVQLSLHSSNTGQPFPAATAHELFQAIGKELLTGTIYLDNIIDGIIKRIEGFNPSDLQVETFRTSIVFKSVRAALEGEFPDLEIKITDLIPWAFRDYGPRLPRSFAHSKLAVVGMACRMPGGGNDTELFWEILEQGRDVHTTVPADRFDLSTHYDPSGKTDNAATTPYGNFVDKPGLFDAGFFNMSPKEAEQTDPMQRLALVTAYEALEMAGVVPGRTASSNPKRIGTYYGQASDDWRELNASQNIGTYAVTGGVRAFGNGRINYYFKFPGPSFNVDTACSSGLAAVQVACSALWAGEADTVLAGGLNIITDPDNYAGLGCGHFLSKTGQCKVWDETADGYCRADGIGSVVIKRLEDAEADNDNIIAVVLSAATNHSAEAISITHPHAGNQKDNYRQVIDMAAVNPLDVSYIELHGTGTQAGDAVESESVLDVFAPRSPPRRPDQLLQLGAVKSNIGHGEAAAGIASFLKVLLMYQKNMIPAHIGIHTVINPTIPKDLEQRRVRLTQTNTPWPRLPGKKRIAMVNSFGAHGGNTTVLLEDAPERNKDVARENRSTHTVVISAKSKKSLQANIANLALHLEENPDIDLGDLSYTTCARRIHYTLRVGFAVSSIAGLKEALRKAGEKEALAEVRPTPGDVPPVVFAFTGQGAFYQGIARELFESFSYFRDEVLQLDHIVQRLGFQSIVPVIDGSIGENPSATVSQLSIVVIEIALAHLWTLLLGMQPSAVIGHSLGEYAALVVAGVLSTADGIFLAGRRAQLIEKCCTAGSHAMLSVRASVSEISKLLGNAKYEISCQNTLNDTVIGGTKANLDAARQVLESSSIKCVPVDVPFAFHTEQVDPVLDQLTRVAETVHFKAPSIPIISPLLRSVVFDGKTINSSYLIRATREPVHFAGAIEAAQDLGMVNDKTVWVDVGPHPICASFVRSLIPKARVASSCRRNEDNYATMAKNLVALHLAGCTPVWDEYFRANEKAYNLLTLPKYAWNDVNYWIQYIGTWTLDKAHLKYTGTNGPPQVKPSSSALRTSLIHEIIEETIGEETATLKTVSDLQHPEFLEAVHGHRMNNCGVATSSIWTDMSLTVGEYLYNKLAPGSKVHMNVGELEVLHATVANPAKNCTQNLYLDAHLDLRTQKMSLAWFNVDPATGSKAAESYATGSVRFEADAEKWKSEWERLTHLVLGRIETLESMAKDGQASQLSKALSYALFKNVVDYADHYRGMERVVMHDYEAFCDIKLTPERRGMFHTPPHWIDSVSHLAGLIMNGSDASNTRDYFFVTPGYESFRLLAKLDPDVKYQSYVRMFPLPEANMYGGDLYILQDNQIIGMVGHFKFRRVPRLLMDRFFSAEAASKQSVAASASSAPKTATKHAPLPASKPAQAPAEPTPSSLPTVQAQNTSPPQQVTPSKPAMNGVKTPEEEKPGKADAEGPNGTTSQPEATGVVGQCLQLIANETGQSVNELTPDATFVQLGVDSLMSLVLSEKFRAELGLEVKSSLFLECPTVGDMMDWLEQYC
Protein: Heat shock protein 105 kDa (Antigen NY-CO-25) (Heat shock 110 kDa protein) (Heat shock protein family H member 1) (Q92598)
Organism: Homo sapiens (Human)
Function: Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9931472}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- BAG family molecular chaperone regulator 2
- DnaJ homolog subfamily B member 1
- Small glutamine-rich tetratricopeptide repeat-containing protein alpha
- DnaJ homolog subfamily B member 4
- Hsp70-binding protein 1
- BAG family molecular chaperone regulator 1
- Heat shock 70 kDa protein 1A
- DnaJ homolog subfamily A member 1
- Heat shock protein HSP 90-alpha
Sequence:
MSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVPFPISLIWNHDSEDTEGVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVPYPEAKIGRFVVQNVSAQKDGEKSRVKVKVRVNTHGIFTISTASMVEKVPTEENEMSSEADMECLNQRPPENPDTDKNVQQDNSEAGTQPQVQTDAQQTSQSPPSPELTSEENKIPDADKANEKKVDQPPEAKKPKIKVVNVELPIEANLVWQLGKDLLNMYIETEGKMIMQDKLEKERNDAKNAVEEYVYEFRDKLCGPYEKFICEQDHQNFLRLLTETEDWLYEEGEDQAKQAYVDKLEELMKIGTPVKVRFQEAEERPKMFEELGQRLQHYAKIAADFRNKDEKYNHIDESEMKKVEKSVNEVMEWMNNVMNAQAKKSLDQDPVVRAQEIKTKIKELNNTCEPVVTQPKPKIESPKLERTPNGPNIDKKEEDLEDKNNFGAEPPHQNGECYPNEKNSVNMDLD