wanglab/gogpt-training-data huggingface dataset:
Protein: 7-dehydrocholesterol reductase (7-DHC reductase) (EC 1.3.1.21) (Cholesterol-5,6-epoxide hydrolase subunit DHCR7) (EC 3.3.2.11) (Delta7-sterol reductase) (Sterol Delta(7)-reductase) (Sterol reductase SR-2) (Q9UBM7)
Organism: Homo sapiens (Human)
Function: 7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-3beta-ol, two intermediates in that pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9878250}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lathosterol oxidase
- Delta
- Squalene monooxygenase
- Lanosterol 14-alpha demethylase
- 3-beta-hydroxysteroid-Delta
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- Cholesterol 25-hydroxylase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Sterol O-acyltransferase 1
Sequence:
MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF
Protein: Granulin a (Granulin a isoform X6) (E9QI45)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Oogenesis-related
- Aldehyde dehydrogenase 1 family, member A2
- TAR DNA-binding protein 43
- Guanine nucleotide exchange C9orf72 homolog
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Glyceraldehyde-3-phosphate dehydrogenase
- Sortilin
Sequence:
MLRLTVCLAVVTLVICSQCPNNEVCEAGQSCCQDPTGGFSCCPFHHGECCEDHLHCCPEGMLCSVKDLTCTNATHTQPLADRTLAKKPDLPKSFRMIFSMPASESDITCPDGSSCPAEFSCLLMSTSYGCCPVAQGLACSDGKHCCPNDHECSTDSSLCVKRKVKVQTVLCGNGTSECPADTTCCQADDGQWGCCPMPKAVCCDDKIHCCPEDTVCDVKALKCVSSTNQELPMWDKFPARLRAEWEDHKQKRPETQRTTARPTGTTSTTTAANQMTTLPAEHQGVSSDVACNDTAACPDGSTCCKTKDGGWACCPLPEAVCCEDFIHCCPHGKKCDVAAGSCEDPSGSVSWVEKVPVRPIRKQKVAVTQVSSVSSDVPCNDTAACADGTTCCKTKEGDWACCPLPEAVCCEDFVHCCPKGKKCNIAAMKCEDPLCTEEPLVKQTPVQSTTTPNVIGTQKSDVPCNDTAACPDGSTCCKTKDGGWACCPLPEAVCCEDFIHCCPHGKKCDVAAGSCEDPSGSVPWVEKVPVRPIRKQKVAVTTVSPVSSDIACNDTVACPDGSTCCKDKDGEWGCCPLPEAVCCEDFIHCCPHGKKCNVAAGSCDDPSGSVPWMDKVPVRPIKKQKVAVTQASSASSDVPCNDTAACPDGSTCCKTKDGGWACCPLPEAVCCEDFIHCCPHGKKCDVAAGSCEDSSGSVPWVEKVPVRPIRKQKVANTKVSPVSSDVACNDTVACPDGSTCCKDKDGDWGCCPLPEAVCCEDFIHCCPHGKKCNVAAGSCDDPSGSVPWVEKVPVHLRAGQRPSGKVKCNATHGCPESSTCCKNIAGEWGCCPFSQAVCCTDGEHCCPAHYKCNLSSVSCIKGDVVIPWYNKIAAESTPAPKLDLGVVKCDEQSSCSADSTCCLLSKDETGCCPFPEAVCCPDQKHCCPEGYRCDLRRRSCVKTTRLYVEITQLTHIRSNKPQPSVVVKDVQCGGGFSCHDGETCCLTSQTTWGCCPSPKAVCCDDMQHCCPAGYKCGPGGTCISAGDLDWSNWVNWKLFFSKKKRALTL
Protein: Reticulon-4 receptor-like 1 (Nogo receptor-like 2) (Nogo-66 receptor homolog 2) (Nogo-66 receptor-related protein 3) (NgR3) (Q80WD0)
Organism: Rattus norvegicus (Rat)
Function: Cell surface receptor. Plays a functionally redundant role in postnatal brain development and in regulating axon regeneration in the adult central nervous system. Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum. Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG. Plays a role in inhibiting neurite outgrowth and axon regeneration via its binding to neuronal chondroitin sulfate proteoglycans. Binds heparin (By similarity). Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development. Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15673660}; Lipid-anchor, GPI-anchor {ECO:0000305}. Membrane raft {ECO:0000250|UniProtKB:Q86UN2}. Perikaryon {ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:15673660}. Cell projection {ECO:0000269|PubMed:15673660}. Note=Localized to the surface of neurons, including axons. {ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:15673660}.
Interaction partners:
- Reticulon-4
- Receptor-type tyrosine-protein phosphatase S
- Receptor-type tyrosine-protein phosphatase F
- Myelin-associated glycoprotein
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L2
Sequence:
MLRKGCCVELLLLLLAGELPLSGGCPRDCVCYPSPMTVSCQAHNFAAIPEGIPEDSERIFLQNNHITFLQQGHFSPAMVTLWIYSNNITFIAPNTFEGFVHLEELDLGDNRQLRTLAPETFQGLVKLHALYLYKCGLSSLPAGIFGGLHSLQYLYLQDNHIEYLQDDIFVDLVNLSHLFLHGNKLWSLGQGIFRGLVNLDRLLLHENQLQWVHHKAFHDLHRLTTLFLFNNSLTELQGDCLAPLVALEFLRLNGNAWDCGCRARSLWEWLRRFRGSSSVVPCATPELRQGQDLKSLRVEDFRNCTGPASPHQIKSHTLSTSDRAARKEHHPSHGASRDKGHPHGHLPGSRSGSKKPGKNCTSHRNRNQISKGSAGKELPELQDYAPDYQHKFSFDIMPTARPKRKGKCARRTPIRAPSGVQQASSGTALGVSLLAWILGLVVSLR
Protein: T3SS secreted effector NleH (Q8X831)
Organism: Escherichia coli O157:H7
Interaction partners:
- T3SS secreted effector NleH
- T3SS secreted effector NleH
- T3SS secreted effector NleD
Sequence:
MLSPYSVNLGCSWNSLTRNLTSPDNRVLSSVRDAAVHSDNGAQVKVGNRTYRVVATDNKFCVTRESHSGCFTNLLHRLGWPKGEISRKIEVMLNASPVSAAMERGIVHSNRPDLPPVDYAPPELPSVDYNRLSVPGNVIGKGGNAVVYEDAEDATKVLKMFTTSQSNEEVTSEVRCFNQYYGAGSAEKIYGNNGDIIGIRMDKINGESLLNISSLPAQAEHAIYDMFDRLEQKGILFVDTTETNVLYDRAKNEFNPIDISSYNVSDRSWSESQIMQSYHGGKQDLISVVLSKI
Protein: Protein trichome birefringence-like 39 (Q9SIN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Allergen-like protein BRSn20
- CBS domain-containing protein
Sequence:
MGFTSRGNPSFLFFFFFFLCLSTVSAYINSTSSNNDEVRRELASGRCNWFRGNWVYDVKYPLYDPYKCPFIDPQFNCKKYGRPDNAYLKYRWQPSSCSLPRFNGLYFLRRMRGKKIMFVGDSLSTNMWQSLACLIHSWVPNTRYTLIRQKGLASLTFEEYGVTLLLYRTQFLVDLNVEKVGRVLKLDSIKQGNMWRGMDVLIFNSWHWWTHTEHIQPWDYMEDGNRLYKDMNRLVAFYKGMTTWARWVNAYVDPSKTKVFFNGVSPTHYEGKDWGEPMNSCRSQTQPFYGRKYPGGTPMAWVILNKVMRRLKKPVHWLDITGLSQLRKDAHPSAFSGNHPGNDCSHWCLPGLPDTWNLLFYSTLFSS
Protein: Alpha-glucuronidase A (EC 3.2.1.139) (Alpha-glucosiduronase A) (Q5AQZ4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases 4-O-methylglucuronic acid from xylan.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Xylanolytic transcriptional activator xlnR
- Endo-1,4-beta-xylanase B
- Exo-1,4-beta-xylosidase xlnD
- DNA-binding protein creA
- Endo-1,4-beta-xylanase C
- Endo-1,4-beta-xylanase A
Sequence:
MRSFLLLTALLGVAAVAEDGLAAWLRYAPIPHAKSYHKNLPSVIVPLNATAGRPIDTAAYELVDGIKGIFGKRVTLKNETRDDPNLPAVTVGTVEAYAEAGGDVSSVPELIDDGYYLSVAGPSVLILGQNERGALYGTFQYLERLAQGKVSDTSFASNPSAPIRWVNQWDNLQDGGTHGSVERGYGGDSIFFWDGRVRDDLTRASQYARLLASIGLNAVIVNNVNANETILTQENMDGVARIADAFRPYGIQLGLSLNFASPQSLGGLDTFDPFDERVISWWGEITDELYERIPDMAGYLVKANSEGQPGPFTYNRTLADGANLFARALQPHGGIVLFRAFVYDHENLNETLDWKADRANAAVEFFDGLDPQFEDNVVIQIKNGPIDFQVREPVSPLFAHLSQTASAVELQVTQEYLGQQCHLVYLAPMWKEVLDFDLRVDGKDSVVSDIVSGRRFNNTLGGYAGVVNVGLNTTWLGSHLAMSNLYAYGRLAWDPSADSVELLQEWIKMTFSHDQEVVDVITKMSMESWPAYENYSGNLGIQTLTDILLGHYGPNPASQDGNPWGQWTRADADSIGMDRTVWNGTGNAGQYPEEVYQMYENIDTTPDNLLLWFHHVPYTQRLKSGKTVIQHFYDAHYRGSATAQTFVSLWKTIKGKIDKERYEHVLFRLVYQAGHALVWRDSITNFYYNKSGIPDEAGRVGNHPYRIEAEDMELDGYEPYLVSPFEAASGSHCIVTSNNSTEGRASTPLKVKNGKYDIAVNYFDQAIGNSTWRLFLDDDLVGEWKGDLEYILGRAPSPYIDGQTAARITFKHVHIKSRSTLSIVGIPDGMEPAPIDYVSILPEGVID
Protein: Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) (O14023)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongator complex protein 2
- Elongator complex protein 1
- Elongator complex protein 4
- Elongator complex protein 5
- Elongator complex protein 6 homolog
- Cytoplasmic tRNA 2-thiolation protein 1
- Diphthamide biosynthesis protein 3
- Protein kti12
- Cytoplasmic tRNA 2-thiolation protein 2
- Ubiquitin-related modifier 1
Sequence:
MSTSSLAFLKAKACAEIVAELIASENQNKVINLNALKMRISKKHQLSESPRLTDIIAAIPPDAYLKESLMRKLRAKPVRTASGIAVVAVMCKPHRCPHIAMTGNVCVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPYEQARGRVEQLRSLGHTVDKVEYIIMGGTFMSLPESYRHTFIANLHNALSGATTEDLDEAVKFSEQSETKCVGITIETRPDYCLDQHLDEMLRYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCETFQLAKDTGYKVVTHMMPDLPNVGMERDIFQFQEYFENPAFRTDGLKLYPTLVIRGTGLYELWKTGRYKNYTPNALVDLIARILALVPPWTRIYRIQRDIPMPLVSSGVETGNLRELALNRMRDLGTKCRDIRAREVGMQEVHHKIHPEQVELLRRDYTANGGWETFLSYEDPKQDILIGLLRLRQCSDKTYRPEFTSQPTSLVRELHVYGSAVPVHSRDPKKFQHQGFGTLLLEEAERIAKYEHGSKKISVISGVGVRKYYQKLGYTLDGPYMSKWL
Protein: Tachykinin-related peptide 5 (TKRP-5) (P86561)
Organism: Acrosternum hilare (Green stink bug) (Nezara hilaris)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
APLMGFQGVR
Protein: Dystroglycan 1 (C9JEN1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004135}.
Interaction partners:
Sequence:
MRMSVGLSLLLPLSGRTFLLLLSVVMAQSHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVS
Protein: Cytochrome b-c1 complex subunit 7-2, mitochondrial (Complex III subunit 7-2) (Complex III subunit VII) (Ubiquinol-cytochrome c oxidoreductase subunit 7-2) (F4JWS8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18189341}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00128}; Matrix side {ECO:0000250|UniProtKB:P00128}.
Interaction partners:
- Cytochrome c1 2, heme protein, mitochondrial
- Cytochrome c1 1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 6-1, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Probable mitochondrial-processing peptidase subunit beta, mitochondrial
- Cytochrome b-c1 complex subunit 6-2, mitochondrial
- Probable mitochondrial-processing peptidase subunit alpha-1, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-2, mitochondrial
- Cytochrome c oxidase subunit 6a, mitochondrial
Sequence:
MASFLQRLVDPRKNFLARMHMKSVSNRLRRYGLRYDDLYDPLYDLDIKEALNRLPREIVDARNQRLMRAMDLSMKHEYLPDNLQAVQTPFRSYLQDMLALVKRERAEREALGALPLYQRTIP
Protein: Protein BIIDXI (Q8LAR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:29238286, ECO:0000269|PubMed:30253266}. Note=Accumulates at the cell wall upon root-knot nematode Meloidogyne incognita infection (PubMed:29238286). Observed in epidermal cells of both hypocotyls and primary roots (PubMed:30253266). {ECO:0000269|PubMed:29238286, ECO:0000269|PubMed:30253266}.
Interaction partners:
- Proline-tRNA ligase
- Protein RALF-like 22
- Helicase and polymerase-containing protein TEBICHI
- Putative beta-glucosidase 41
- Signal peptide peptidase
- At4g12520
Sequence:
MKEMGVIVLLLLHSFFYVAFCFNDGLLPNGDFELGPRHSDMKGTQVINITAIPNWELSGFVEYIPSGHKQGDMILVVPKGAFAVRLGNEASIKQKISVKKGSYYSITFSAARTCAQDERLNVSVAPHHAVMPIQTVYSSSGWDLYSWAFKAQSDYADIVIHNPGVEEDPACGPLIDGVAMRALFPPRPTNKNILKNGGFEEGPWVLPNISSGVLIPPNSIDDHSPLPGWMVESLKAVKYIDSDHFSVPQGRRAVELVAGKESAVAQVVRTIPGKTYVLSFSVGDASNACAGSMIVEAFAGKDTIKVPYESKGKGGFKRSSLRFVAVSSRTRVMFYSTFYAMRNDDFSSLCGPVIDDVKLLSARRP
Protein: Kallikrein 4 (Kallikrein b1) (Kallikrein-related peptidase 4) (Q6IE12)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Enamelin
- Ameloblastin
- Amelogenin, X isoform
- Amelotin
- Matrix metallopeptidase 20
- Odontogenic ameloblast-associated protein
- Family with sequence similarity 83, member H
- WD repeat domain 72
- Solute carrier family 24 member 4
Sequence:
MMVTARTPWGWFLGYLILEVTGSSASSISSRIIQGQDCLPHSQPWQAALFSEDNAFFCSGVLVHPQWVLSAAHCIQDSYTVGLGLHNLEGSQEPGSRMLEAHLSIQHPNYNDPSFANDLMLIKLNESVMESNTIRRIPVASQCPTPGDTCLVSGWGRLKNGKLPSLLQCVNLSVASEETCRLLYDPVYHLSMFCAGGGPDRKDTCNGDSGGPIVCNRSLQGLVSMGQGECGQPGIPSVYTNLCKFTNWIWTTIQTR
Protein: S-arrestin (48 kDa protein) (Retinal S-antigen) (S-AG) (Rod photoreceptor arrestin) [Cleaved into: S-arrestin short form] (P08168)
Organism: Bos taurus (Bovine)
Function: Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO. May play a role in preventing light-dependent degeneration of retinal photoreceptor cells (By similarity).
Subcellular location: [Isoform A]: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:7515057}. Membrane {ECO:0000250|UniProtKB:P20443}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20443}. Note=Highly expressed in photoreceptor outer segments in light-exposed retina (PubMed:7515057). Evenly distributed throughout rod photoreceptor cells in dark-adapted retina (PubMed:7515057). Predominantly dectected at the proximal region of photoreceptor outer segments, near disk membranes (By similarity). {ECO:0000250|UniProtKB:P10523, ECO:0000269|PubMed:7515057}.; SUBCELLULAR LOCATION: [Isoform B]: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:7515057, ECO:0000269|PubMed:8003967}. Membrane {ECO:0000269|PubMed:8003967}; Peripheral membrane protein {ECO:0000269|PubMed:8003967}.
Interaction partners:
- Rhodopsin
- Rhodopsin kinase GRK7
- Retinol-binding protein 3
Sequence:
MKANKPAPNHVIFKKISRDKSVTIYLGKRDYIDHVERVEPVDGVVLVDPELVKGKRVYVSLTCAFRYGQEDIDVMGLSFRRDLYFSQVQVFPPVGASGATTRLQESLIKKLGANTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEIKAFATHSTDVEEDKIPKKSSVRLLIRKVQHAPRDMGPQPRAEASWQFFMSDKPLRLAVSLSKEIYYHGEPIPVTVAVTNSTEKTVKKIKVLVEQVTNVVLYSSDYYIKTVAAEEAQEKVPPNSSLTKTLTLVPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDKTVMGILVSYQIKVKLTVSGLLGELTSSEVATEVPFRLMHPQPEDPDTAKESFQDENFVFEEFARQNLKDAGEYKEEKTDQEAAMDE
Protein: Small ribosomal subunit protein uS10m (37S ribosomal protein S10, mitochondrial) (Q03201)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein mS29
- Ribosome assembly protein RSM22
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL3m
- Small ribosomal subunit protein bS1m
Sequence:
MLRNTIALRSFIRTQSTRPYPVNVEAVYYAPLKLPIKYGDLVADIQLRSYDNENLDFYSDFILRTGYYLGIPLTGPKPLPTRRERWTVIKSPFVHAKSKENFERHTHKRLIRAWDTNPEVLQMLIAYITKHSMAGVGMKCNFFQRSEISLDLGSDANGLEKSLSNIDELYSLRNDDKAQTSAVGQKVLELLDSPDFKKHLEKK
Protein: RNA helicase (EC 3.6.4.13) (Q68FX3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MATDSWALAVDEQEAAVKSMNSLQIKEEKVKADTNGVIKTSTTAEKTEEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPADRHPQCLCLSPTYELALQTGKVIEQMGKFHPELKLAYAVRGNKLERGQKVGEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN
Protein: Ptpn3 protein (Q562B7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
EDELSQLFPEAMFPACPEGGDSLEGSMELLKKGLESGTVLIQFEQLYRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEEGLVQTLDPS
Protein: Polyprenal reductase (EC 1.3.1.94) (3-oxo-5-alpha-steroid 4-dehydrogenase 3) (EC 1.3.1.22) (Steroid 5-alpha-reductase 2-like) (Steroid 5-alpha-reductase 3) (S5AR 3) (SR type 3) (Q9H8P0)
Organism: Homo sapiens (Human)
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism. Also able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:20637498}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Dolichol kinase
- Aldo-keto reductase family 1 member C3
- Aldo-keto reductase family 1 member C4
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Aldo-keto reductase family 1 member C2
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- 17-beta-hydroxysteroid dehydrogenase type 2
- Aldo-keto reductase family 1 member C1
Sequence:
MAPWAEAEHSALNPLRAVWLTLTAAFLLTLLLQLLPPGLLPGCAIFQDLIRYGKTKCGEPSRPAACRAFDVPKRYFSHFYIISVLWNGFLLWCLTQSLFLGAPFPSWLHGLLRILGAAQFQGGELALSAFLVLVFLWLHSLRRLFECLYVSVFSNVMIHVVQYCFGLVYYVLVGLTVLSQVPMDGRNAYITGKNLLMQARWFHILGMMMFIWSSAHQYKCHVILGNLRKNKAGVVIHCNHRIPFGDWFEYVSSPNYLAELMIYVSMAVTFGFHNLTWWLVVTNVFFNQALSAFLSHQFYKSKFVSYPKHRKAFLPFLF
Protein: Upstream stimulatory factor 1 (Major late transcription factor 1) (Q61069)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.
Subcellular location: Nucleus.
Interaction partners:
- Upstream stimulatory factor 2
- Transcription factor Sp1
- Histone acetyltransferase p300
- General transcription factor II-I
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
- Mediator of RNA polymerase II transcription subunit 1
- Estrogen receptor
- Interferon regulatory factor 1
- Catenin beta-1
- Cellular tumor antigen p53
Sequence:
MKGQQKTAETEEGTVQIQEGAVATGEDPTSVAIASIQSAATFPDPNVKYVFRTENGGQVMYRVIQVSEGQLDGQTEGSGAISGYPATQSMTQAVIQGAFTSDDAVDTEGAAAETHYTYFPSTAVGDGSGGTTSGSTTAVVTTQGSEALLGQATPPSTGQFFVMMSPQEVLQGGSQRSIAPRTHPYSPKSEAPRTTRDEKRRAQHNEVERRRRDKINNWIVQLSKIIPDCSMESTKSGQSKGGILSKACDYIQELRQSNHRLSEELQGLDQLQLDNDVLRQQVEDLKNKNLLLRAQLRHHGLEVVIKNDSN
Protein: Cell death protein Grim (Q24570)
Organism: Drosophila melanogaster (Fruit fly)
Function: Activator of apoptosis, independent of rpr and hid, that acts on the effector Dredd.
Interaction partners:
- Death-associated inhibitor of apoptosis 1
- Cell death protein rpr
- Caspase Dronc
- Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6
- FI02818p
- Caspase drICE
- Apoptosome protein Dark
- Death-associated inhibitor of apoptosis 2
- Ecdysone receptor
Sequence:
MAIAYFIPDQAQLLARSYQQNGQQTAASPRTTATAAAPSQQQQQSQQQQQQQRHHHQQQRPQFRANISVPLGSQQGSMTMSEFGCWDLLAQIFCYALRIYSYSSSQRQPTVIQISFEISSGGQNNDEDDVTDATSKEN
Protein: Transmembrane protein (DUF2215) (Q0WVK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004575}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004575}; Nucleoplasmic side {ECO:0000256|ARBA:ARBA00004575}.
Interaction partners:
Sequence:
MSDSSSVIVRSSNFIVVILFLNLVTFFSLVSSNELVFAVGETGSLQVTPRTEVIYSPGLKRGITSICERLHIHGLQRRLEHIDRYAHSLKLTLLSNNASNSIDVCFHRNSSRAIGMCPDNQWKRVSKGLPWVGIMSPFDYKILDIRTFGGSSNVSTVELVAKQEFFIYRIVFLIMGIVLLSLASRLSKSVAFYYIGAMSIGIVILVTLIINQGIKRLPTRGKSRFQLFFYSSMIGVGGYFLQYIRGLVQDLLMQIEISEDLYIPLAILLVVFVFMLGAWSGFWTVKKFVVTKDGSVDISTSIFVSWSIRAFAVALILQSSLDPLLAGGALITGILISLILKSISRKLLAQRIYEQDDETESCSPGLIHATSFASPLPRGSNKKLRTVPLSESDIFPSSFHKTPEGRRKLTKEELQKFTKESTENALKELVSSPGFGEWAVKNAKRITVNPIKESSSK
Protein: Spindle assembly checkpoint component MAD3 (Mitotic MAD3 protein) (P47074)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Component of the mitotic checkpoint complex (MCC) which inhibits the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20.
Subcellular location: Nucleus.
Interaction partners:
- Mitotic spindle checkpoint component MAD2
- APC/C activator protein CDC20
- Spindle assembly checkpoint protein BUB3
- Serine/threonine-protein kinase MPS1
- Spindle assembly checkpoint component MAD1
- Anaphase-promoting complex subunit CDC23
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit CDC27
- Anaphase-promoting complex subunit DOC1
- Anaphase-promoting complex subunit CDC16
Sequence:
MKAYAKKRISYMPSSPSQNVINFEEIETQKENILPLKEGRSAAALSKAIHQPLVEINQVKSSFEQRLIDELPALSDPITLYLEYIKWLNNAYPQGGNSKQSGMLTLLERCLSHLKDLERYRNDVRFLKIWFWYIELFTRNSFMESRDIFMYMLRNGIGSELASFYEEFTNLLIQKEKFQYAVKILQLGIKNKARPNKVLEDRLNHLLRELGENNIQLGNEISMDSLESTVLGKTRSEFVNRLELANQNGTSSDVNLTKNNVFVDGEESDVELFETPNRGVYRDGWENFDLKAERNKENNLRISLLEANTNLGELKQHEMLSQKKRPYDEKLPIFRDSIGRSDPVYQMINTKDQKPEKIDCNFKLIYCEDEESKGGRLEFSLEEVLAISRNVYKRVRTNRKHPREANLGQEESANQKEAEAQSKRPKISRKALVSKSLTPSNQGRMFSGEEYINCPMTPKGRSTETSDIISAVKPRQLTPILEMRESNSFSQSKNSEIISDDDKSSSSFISYPPQR