wanglab/gogpt-training-data huggingface dataset:
Protein: Xylosyltransferase 2 (EC 2.4.2.26) (Peptide O-xylosyltransferase 1) (Xylosyltransferase II) (XT-II) (XylT-II) (Q9H1B5)
Organism: Homo sapiens (Human)
Function: Catalyzes the first step in the biosynthesis of chondroitin sulfate, heparan sulfate and dermatan sulfate proteoglycans, such as DCN. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:17189265, ECO:0000269|PubMed:25748573}.
Interaction partners:
- Beta-1,4-galactosyltransferase 7
- Xylosyltransferase 1
- Sodium- and chloride-dependent transporter XTRP3
- Growth factor receptor-bound protein 2
- Beta-1,3-galactosyltransferase 6
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Exostosin-like 3
- ATP-binding cassette sub-family C member 6
Sequence:
MVASARVQKLVRRYKLAIATALAILLLQGLVVWSFSGLEEDEAGEKGRQRKPRPLDPGEGSKDTDSSAGRRGSTGRRHGRWRGRAESPGVPVAKVVRAVTSRQRASRRVPPAPPPEAPGRQNLSGAAAGEALVGAAGFPPHGDTGSVEGAPQPTDNGFTPKCEIVGKDALSALARASTKQCQQEIANVVCLHQAGSLMPKAVPRHCQLTGKMSPGIQWDESQAQQPMDGPPVRIAYMLVVHGRAIRQLKRLLKAVYHEQHFFYIHVDKRSDYLHREVVELAQGYDNVRVTPWRMVTIWGGASLLRMYLRSMRDLLEVPGWAWDFFINLSATDYPTRTNEELVAFLSKNRDKNFLKSHGRDNSRFIKKQGLDRLFHECDSHMWRLGERQIPAGIVVDGGSDWFVLTRSFVEYVVYTDDPLVAQLRQFYTYTLLPAESFFHTVLENSLACETLVDNNLRVTNWNRKLGCKCQYKHIVDWCGCSPNDFKPQDFLRLQQVSRPTFFARKFESTVNQEVLEILDFHLYGSYPPGTPALKAYWENTYDAADGPSGLSDVMLTAYTAFARLSLHHAATAAPPMGTPLCRFEPRGLPSSVHLYFYDDHFQGYLVTQAVQPSAQGPAETLEMWLMPQGSLKLLGRSDQASRLQSLEVGTDWDPKERLFRNFGGLLGPLDEPVAVQRWARGPNLTATVVWIDPTYVVATSYDITVDTETEVTQYKPPLSRPLRPGPWTVRLLQFWEPLGETRFLVLPLTFNRKLPLRKDDASWLHAGPPHNEYMEQSFQGLSSILNLPQPELAEEAAQRHTQLTGPALEAWTDRELSSFWSVAGLCAIGPSPCPSLEPCRLTSWSSLSPDPKSELGPVKADGRLR
Protein: Hexosyltransferase (EC 2.4.1.-) (Q587E7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}.
Interaction partners:
Sequence:
MVSKGLQMVGSTRRKRIVLVVFLVFAVLFIAWINKQPKRKELTFQQRRQQMHLTEVDNDEYLTLVPEKTIKIWESSKYLVAAGIPSIDNKERFRRRGLQRSTCWTYGGVATRRNDFAGDLIPLYLLSPHERNDFILSDSVRAEAQKNHDIIVLPTFDVPSTNGKVIGELQSWGNEVELVMSKKTYLWLKFASNFFGTATYIMKADDDLFIRVPYYLSSLKLMPKYRLYMGWYGLTPEVFVDRWVPFIAGYCVTLSRDVADGVVNYSPLERLVNTPYSESNIEDFREMAMFNEDVMVAVTLGEKVGYSDLVTADIGRCHYISHLRRRLSKVVTEKTMVVHHIKEKDYGYLMKLFPNNSETPPPVVLQWKDKNFARGKC
Protein: High-affinity nitrate transporter 2.3 (OsNRT2.3) (Q94JG1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in nitrate transport, but does not seem to be able to mediate transport by its own. Acts as a dual component transporter with NAR2.1. Imports nitrate with high affinity when expressed with NAR2.1 in a heterologous system (Xenopus oocytes). Plays a key role in long-distance nitrate transport from root to shoot particularly at low external nitrate supply.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23093362}; Multi-pass membrane protein {ECO:0000269|PubMed:23093362}.
Interaction partners:
- Nitrate reductase 1
- Nitrate reductase
- Nitrate reductase
- Os11g0242400 protein
- Ferredoxin--nitrite reductase, chloroplastic
- Os02g0765900 protein
- High-affinity nitrate transporter 2.1
- High-affinity nitrate transporter 2.2
- Plastocyanin
- High-affinity nitrate transporter-activating protein 2.1
Sequence:
MEAKPVAMEVEGVEAAGGKPRFRMPVDSDLKATEFWLFSFARPHMASFHMAWFSFFCCFVSTFAAPPLLPLIRDTLGLTATDIGNAGIASVSGAVFARLAMGTACDLVGPRLASASLILLTTPAVYCSSIIQSPSGYLLVRFFTGISLASFVSAQFWMSSMFSAPKVGLANGVAGGWGNLGGGAVQLLMPLVYEAIHKIGSTPFTAWRIAFFIPGLMQTFSAIAVLAFGQDMPGGNYGKLHKTGDMHKDSFGNVLRHALTNYRGWILALTYGYSFGVELTIDNVVHQYFYDRFDVNLQTAGLIAASFGMANIISRPGGGLLSDWLSSRYGMRGRLWGLWTVQTIGGVLCVVLGIVDFSFAASVAVMVLFSFFVQAACGLTFGIVPFVSRRSLGLISGMTGGGGNVGAVLTQYIFFHGTKYKTETGIKYMGLMIIACTLPVMLIYFPQWGGMLVGPRKGATAEEYYSREWSDHEREKGFNAASVRFAENSVREGGRSSANGGQPRHTVPVDASPAGV
Protein: Intraflagellar transport protein 172 homolog (Q9UG01)
Organism: Homo sapiens (Human)
Function: Required for the maintenance and formation of cilia. Plays an indirect role in hedgehog (Hh) signaling, cilia being required for all activity of the hedgehog pathway (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:24140113}. Note=Localized to the axoneme and around the base of the cilium.
Interaction partners:
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 57 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 81 homolog
- Clusterin-associated protein 1
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 27 homolog
Sequence:
MHLKHLRTLLSPQDGAAKVTCMAWSQNNAKFAVCTVDRVVLLYDEHGERRDKFSTKPADMKYGRKSYMVKGMAFSPDSTKIAIGQTDNIIYVYKIGEDWGDKKVICNKFIQTSAVTCLQWPAEYIIVFGLAEGKVRLANTKTNKSSTIYGTESYVVSLTTNCSGKGILSGHADGTIVRYFFDDEGSGESQGKLVNHPCPPYALAWATNSIVAAGCDRKIVAYGKEGHMLQTFDYSRDPQEREFTTAVSSPGGQSVVLGSYDRLRVFNWIPRRSIWEEAKPKEITNLYTITALAWKRDGSRLCVGTLCGGVEQFDCCLRRSIYKNKFELTYVGPSQVIVKNLSSGTRVVLKSHYGYEVEEVKILGKERYLVAHTSETLLLGDLNTNRLSEIAWQGSGGNEKYFFENENVCMIFNAGELTLVEYGNNDTLGSVRTEFMNPHLISVRINERCQRGTEDNKKLAYLIDIKTIAIVDLIGGYNIGTVSHESRVDWLELNETGHKLLFRDRKLRLHLYDIESCSKTMILNFCSYMQWVPGSDVLVAQNRNSLCVWYNIEAPERVTMFTIRGDVIGLERGGGKTEVMVMEGVTTVAYTLDEGLIEFGTAIDDGNYIRATAFLETLEMTPETEAMWKTLSKLALEARQLHIAERCFSALGQVAKARFLHETNEIADQVSREYGGEGTDFYQVRARLAMLEKNYKLAEMIFLEQNAVEEAMGMYQELHRWDECIAVAEAKGHPALEKLRRSYYQWLMDTQQEERAGELQESQGDGLAAISLYLKAGLPAKAARLVLTREELLANTELVEHITAALIKGELYERAGDLFEKIHNPQKALECYRKGNAFMKAVELARLAFPVEVVKLEEAWGDHLVQQKQLDAAINHYIEARCSIKAIEAALGARQWKKAIYILDLQDRNTASKYYPLVAQHYASLQEYEIAEELYTKGDRTKDAIDMYTQAGRWEQAHKLAMKCMRPEDVSVLYITQAQEMEKQGKYREAERLYVTVQEPDLAITMYKKHKLYDDMIRLVGKHHPDLLSDTHLHLGKELEAEGRLQEAEYHYLEAQEWKATVNMYRASGLWEEAYRVARTQGGANAHKHVAYLWAKSLGGEAAVRLLNKLGLLEAAVDHAADNCSFEFAFELSRLALKHKTPEVHLKYAMFLEDEGKFEEAEAEFIRAGKPKEAVLMFVHNQDWEAAQRVAEAHDPDSVAEVLVGQARGALEEKDFQKAEGLLLRAQRPGLALNYYKEAGLWSDALRICKDYVPSQLEALQEEYEREATKKGARGVEGFVEQARHWEQAGEYSRAVDCYLKVRDSGNSGLAEKCWMKAAELSIKFLPPQRNMEVVLAVGPQLIGIGKHSAAAELYLNLDLVKEAIDAFIEGEEWNKAKRVAKELDPRYEDYVDQHYKEFLKNQGKVDSLVGVDVIAALDLYVEQGQWDKCIETATKQNYKILHKYVALYATHLIREGSSAQALALYVQHGAPANPQNFNIYKRIFTDMVSSPGTNCAEAYHSWADLRDVLFNLCENLVKSSEANSPAHEEFKTMLLIAHYYATRSAAQSVKQLETVAARLSVSLLRHTQLLPVDKAFYEAGIAAKAVGWDNMAFIFLNRFLDLTDAIEEGTLDGLDHSDFQDTDIPFEVPLPAKQHVPEAEREEVRDWVLTVSMDQRLEQVLPRDERGAYEASLVAASTGVRALPCLITGYPILRNKIEFKRPGKAANKDNWNKFLMAIKTSHSPVCQDVLKFISQWCGGLPSTSFSFQ
Protein: Cold-regulated 413 inner membrane protein 1, chloroplastic (AtCOR413-IM1) (Cold-regulated 413 thylakoid membrane 1) (AtCOR413-TM1) (Q94AL8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:18643950}; Multi-pass membrane protein {ECO:0000269|PubMed:18643950}.
Interaction partners:
- Protein COLD-REGULATED 15B, chloroplastic
- Copper transport protein family
- Low-temperature-induced protein
- Protein COLD-REGULATED 15A, chloroplastic
Sequence:
MASLCLSSSRIVSLHHQKPFLSLKLRSRPSDLSGLGRHTSPVCFNPLRLSGDRQRTATVSTRVEKRRKRGSSVVCYAAPISANSLQWISTISCLALMLARGTGIHKSVVVPLFALHAPSSIVAWIKGEYGVWAAFLALIARLFFTFPGELELPFIALLLVIVAPYQVMNIRGKQEGAIIAIAISGFLAFQHFSRAGSLEKAYEKGSVLATVAIIGVTVVSLLLLL
Protein: Heat shock protein 90-3 (AtHSP90.3) (AtHsp90-3) (HSP81.2) (Heat shock protein 81-3) (Hsp81-3) (Protein MUTANT SNC1-ENHANCING 10) (P51818)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as a holding molecular chaperone (holdase) which stabilizes unfolding protein intermediates and rapidly releases them in an active form once stress has abated. Functions as a folding molecular chaperone (foldase) that assists the non-covalent folding of proteins in an ATP-dependent manner. Regulates RPP4-mediated temperature-dependent cell death and defense responses. May assist SGT1B in the formation of SCF E3 ubiquitin ligase complexes that target the immune receptors SNC1, RPS2 and RPS4 for degradation, to regulate receptor levels and avoid autoimmunity.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Protein SGT1 homolog A
- Protein SGT1 homolog B
- Cysteine and histidine-rich domain-containing protein RAR1
- Heat shock 70 kDa protein 4
- Peptidyl-prolyl cis-trans isomerase CYP40
- Heat shock 70 kDa protein 3
- Co-chaperone protein p23-1
- Co-chaperone protein p23-2
- Heat shock 70 kDa protein 16
- Heat shock 70 kDa protein 14
Sequence:
MADAETFAFQAEINQLLSLIINTFYSNKEIFLRELISNSSDALDKIRFESLTDKSKLDGQPELFIHIIPDKTNNTLTIIDSGIGMTKADLVNNLGTIARSGTKEFMEALAAGADVSMIGQFGVGFYSAYLVADKVVVTTKHNDDEQYVWESQAGGSFTVTRDTSGEALGRGTKMVLYLKEDQMEYIEERRLKDLVKKHSEFISYPISLWIEKTIEKEISDDEEEEEKKDEEGKVEEVDEEKEKEEKKKKKIKEVSHEWDLVNKQKPIWMRKPEEINKEEYAAFYKSLSNDWEEHLAVKHFSVEGQLEFKAILFVPKRAPFDLFDTKKKPNNIKLYVRRVFIMDNCEDIIPEYLGFVKGIVDSEDLPLNISRETLQQNKILKVIRKNLVKKCLELFFEIAENKEDYNKFYEAFSKNLKLGIHEDSQNRTKIAELLRYHSTKSGDELTSLKDYVTRMKEGQNDIFYITGESKKAVENSPFLEKLKKKGIEVLYMVDAIDEYAIGQLKEFEGKKLVSATKEGLKLDETEDEKKKKEELKEKFEGLCKVIKDVLGDKVEKVIVSDRVVDSPCCLVTGEYGWTANMERIMKAQALRDSSMGGYMSSKKTMEINPENSIMDELRKRADADKNDKSVKDLVLLLFETALLTSGFSLDEPNTFGSRIHRMLKLGLSIDDDDVVEADADMPPLEDDADAEGSKMEEVD
Protein: 2-hydroxyacylsphingosine 1-beta-galactosyltransferase (EC 2.4.1.47) (Ceramide UDP-galactosyltransferase) (Cerebroside synthase) (UDP-galactose-ceramide galactosyltransferase) (Q64676)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. Galactosylates both hydroxy- and non-hydroxy fatty acid-containing ceramides and diglycerides.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q09426}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q09426}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q09426}.
Interaction partners:
- Galactosylceramide sulfotransferase
- Galactocerebrosidase
- Ceramide glucosyltransferase
- Ceramide kinase
- Ceramide synthase 2
- Arylsulfatase A
- Acid ceramidase
- Non-lysosomal glucosylceramidase
- Sphingomyelin phosphodiesterase 2
- Sphingosine-1-phosphate phosphatase 2
Sequence:
MKSYTPYFMLLWSAVGIARAAKIIIVPPIMFESHLYIFKTLASALHERGHHTVLLLSEGRDIAPSNHYSLQRYPGIFNSTTSDAFLQSKMRNIFSGRLTAVELVDILDHYTKNCDMMVGNQALIQGLKKEKFDLLLVDPNDMCGFVIAHLLGVKYAVFSTGLWYPAEVGAPAPLAYVPEFNSLLTDRMNFLERMKNTGVYLISRIGVSFLVLPKYERIMQKYNLLPAKSMYDLVHGSSLWMLCTDVALEFPRPTLPNVVYVGGILTKPASPLPEDLQRWVSGAQEHGFVLVSFGAGVKYLSEDIANKLAGALGRLPQKVIWRFSGTKPKNLGNNTKLIEWLPQNDLLGHSNIRAFLSHGGLNSIFETMYHGVPVVGIPLFGDHYDTMTRVQAKGMGILLEWNTVTEGELYDALVKVINNPSYRQRAQKLSEIHKDQPGHPVNRTTYWIDYILRHDGARHLRSAVHQISFCQYFLLDIAFVLLLGAVLLYFILSYVTKFIYRKIKSLWSKNEHSTVNGHYQNGIRNGKYKGNGRVKHEKKVR
Protein: Protein Tat (Transactivating regulatory protein) (P04326)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate PCV12) (HIV-1)
Function: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.
Subcellular location: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
Interaction partners:
Sequence:
MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAPQGSQTHQVSLSKQPTSQSRGDPTGPKE
Protein: Ribosomal protein S19 (Q2F8W2)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MPRRSIWKGSFVDAFLFRIKKNRESLMSRKIWSRRSSISPEFVDCSVLIYNGKTPVRCKITEGKVGHKFGEFAFTRRRRPYQTNRGKGRKGKK
Protein: 5'-hydroxyaverantin dehydrogenase stcG (HAVN dehydrogenase) (EC 1.1.1.352) (Sterigmatocystin biosynthesis cluster protein G) (A0A1U8QGV2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: 5'-hydroxyaverantin dehydrogenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Interaction partners:
Sequence:
MEPLDLTCDLTSLNGKSAFITGGASGLGLATARKWAEAGVYITIADIQPPTSPVQPGLAHCFHYVYCDVTSWESQVAAFKSALRFSPSGALDIVACFAGTALAPGNQIDHVLAAGVPSLEVDPPRPSSSVRNIEVNLVGSYFTSWLGLYYLRIPGTGTDPELPSNKCLLFCASIAAYMDSPKASTYPASKFGVRGLFRSTRSQTKQLGVRCNLLAPWFFDSPLIAPIKHAMAARGVDMAKVLTFTSIDACVDAATYCVASPEIHGRALAVQPEGTFDLKDDLEDGWGGNQLRPIMQRRRDAGFDV
Protein: Cyclin J (Q24159)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FNFDTMEQKVAAEQNIFVVDRKLKKTCPQADVERLAKTHWLTDYARDIFLTMREQELSRRPLFYLSPQLNERRRMLQLLKLATSAHKLSRLALHLAVYYMDRFVDYYKIRPDKLLLVAITCLHIAAQIENTDAFIPRYSEMNRLVKNAYTAFEYKAVERKILCFLNFELIRPTTASFVELFACSFLTRSDFKNYIEMLDEYERIHHTQPYQRYISFEEMLSILAQLLLRMADYTLYISRFANDLPSLLAAACIAAVRQVSGVRRWSEYLVGLTSYTEAHVEPYMNVLTDYHYYHVIQADYGSPSVQTNQSLASPDSGFEESFTENTNLVVSDEVVTVETYNIITVQLQDPSPHSSTFLPKEQTNLKRSRFEDDTENQHPLKHAKVESVAKD
Protein: Possible integral membrane protein (O53930)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Uncharacterized ABC transporter ATP-binding protein Rv2564
- Probable transposase
- Probable conserved transmembrane protein
Sequence:
MCAHEYAEQRSAVSGIEGLLTWLGGGHWRELGERHERSTHAVAGVIVAVGAALAGLLASLAVSEAAQGPISSPIGAASLALVLGLLVGAVTRGTASGPARGRAGVTGRASVAVAVGFVVGELAALVMFSGAIDRRLDEQAMHSADATPAAVQASASLQQARNARTALDSAVERARGRLDDALVVARCEYHPTPACPQTRITGVPGRGPETRTANQLLADAQRELDNALAARDHQAPALDAKMAHDEQALAEVRQAVVADAGRGLGSRWVAMNDLTLASAGALTARMLAIAFFALLYLLPLILRLWRGDTTHDRHAAARAERERAELEADTAIAIKRAEVRRAAEIMWAEHQLTQTRLAIEAQAEIDREQQRRRVVEALEGPVRASSERTLQPVEDEVYLPIAAETEAASRTVAQLPAGAAHHRPGIAKNLPAQVQPEGAVEPREKRATPVIRSIPDATKAAARWIRPLVPPFVARMLDNTTAPLRTARQVFEEVEEIAFSFKRTHKVTVNAEGSDPNDQPPLESHSPAAPAESNPIASSDSARRSRLATNDDHPPLAQVPPRDLASLSVGSTGELTQREGPHELRSPDGPRQLPPPR
Protein: SMN complex subunit smn1 (Gemin-1) (Survival motor neuron protein) (Q09808)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins smb1, smd1, smd2, smd3, sme1, smf1 and smg1 that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (By similarity). In the cytosol, the Sm proteins smd1, smd2, sme1, smf1 and smg1 (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone saf5 that controls the assembly of the core snRNP (By similarity). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from saf5 forming an intermediate (By similarity). Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of smd3 and smb1 to complete assembly of the core snRNP (By similarity). Within the SMN complex, smn1 acts as a structural backbone and together with yip11/gem2 it gathers the Sm complex subunits.
Subcellular location: Nucleus {ECO:0000269|PubMed:10749974, ECO:0000269|PubMed:10816558}.
Interaction partners:
- SMN complex subunit yip11/gem2
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein G
- Splicing factor saf5
- Small nuclear ribonucleoprotein E
- Uncharacterized protein C16H5.15
- Gem-associated protein 7 homolog
- Uncharacterized protein new12
- Survival of motor neuron protein-interacting protein yip12
Sequence:
MDQSQKEVWDDSELRNAFETALHEFKKYHSIEAKGGVSDPDSRLDGEKLISAARTEESISKLEEGEQMINQQTETTLEGDTHIQQFADNKGLSDEKPETRAAETHQEFMEVPPPIRGLTYDETYKKLIMSWYYAGYYTGLAEGLAKSEQRKD
Protein: NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial (EC 1.14.13.253) (3-demethoxyubiquinone 3-hydroxylase (NADH)) (Clock abnormal protein 1) (Protein clk-1) (Ubiquinone biosynthesis monooxygenase COQ7) (P48376)
Organism: Caenorhabditis elegans
Function: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis (By similarity). Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides (By similarity). Involved in lifespan determination in a ubiquinone-independent manner (By similarity). Plays a role in modulating mitochondrial stress responses, acting in the nucleus, perhaps via regulating gene expression, independent of its characterized mitochondrial function in ubiquinone biosynthesis. Plays a role in modulating polyribosome formation.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03194}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03194}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03194}. Mitochondrion {ECO:0000269|PubMed:25961505}. Nucleus {ECO:0000269|PubMed:25961505}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit
- Neuronal acetylcholine receptor subunit eat-2
- Insulin-like receptor
- Probable NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 4
- Cytochrome b
- Forkhead box protein O
Sequence:
MFRVITRGAHTAASRQALIEKIIRVDHAGELGADRIYAGQLAVLQGSSVGSVIKKMWDEEKEHLDTMERLAAKHNVPHTVFSPVFSVAAYALGVGSALLGKEGAMACTIAVEELIGQHYNDQLKELLADDPETHKELLKILTRLRDEELHHHDTGVEHDGMKAPAYSALKWIIQTGCKGAIAIAEKI
Protein: Extracellular deoxyribonuclease (DNase) (EC 3.1.21.-) (P08038)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Subcellular location: Secreted.
Interaction partners:
Sequence:
MMIFRFVTTLAASLPLLTFAAPISFSHAKNEAVKIYRDHPVSFYCGCEIRWQGKKGIPDLESCGYQVRKNENRASRIEWEHVVPAWQFGHQLQCWQQGGRKNCTRTSPEFNQMEADLHNLTPAIGEVNGDRSNFSFSQWNGVDGVTYGQCEMQVNFKERTAMPPERARGAIARTYLYMSEQYGLRLSKAQSQLMQAWNNQYPVSEWECVRDQRIEKVQGNSNRFVREQCPN
Protein: Mitochondrial fission regulator (H0YBZ4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|RuleBase:RU369053}.
Interaction partners:
Sequence:
XMVFQQVGVSMQSINSHATEWSPSHPGEDAVASFADVGWVAKEEGECSARLRTEVRSRPPLQDDLLFFEKAPSRQISLPDLSQEEPQLKTPALANEEALQKICALENELAALRAQIAKIVTQQEQQNLTAGDLDSTTFGTIPPHPPPPPPPLPPPALGLHQSTSAVDLIKERREKRANAGKTLVKNNPKKPEMPNMLEILKEMNSVKLRSVKRSEQDVKPKPVDATDPAALIAEALKKKFAYRYRSDSQDEVEKGIPKSESEATSERVLFGPHMLKPTGKMKALIENVSDS
Protein: Probable plastid-lipid-associated protein 9, chloroplastic (Fibrillin-7a) (AtPGL34) (Q9M2P7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16414959, ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:17214877, ECO:0000269|PubMed:22274653}.
Interaction partners:
- Probable plastid-lipid-associated protein 10, chloroplastic
- Probable plastid-lipid-associated protein 1, chloroplastic
- Plastid-lipid-associated protein 6, chloroplastic
- Probable plastid-lipid-associated protein 8, chloroplastic
- Fibrillin-5, chloroplastic
- Probable plastid-lipid-associated protein 2, chloroplastic
- Uncharacterized protein At4g13200
- FAM10 family protein At4g22670
- Probable plastid-lipid-associated protein 4, chloroplastic
- 14-3-3-like protein GF14 mu
Sequence:
MALIQHGSVSGTSAVRLSFSSSVSPPSSSPPLSRVSLNFQSEKKSCYRRMICRAMVQDSVQGIPSVYAREMERLSAKESLILAFNDAGGFEALVTGKITDMQKIDVNERITNLERLNPTPRPTTSPYLEGRWSFEWFGVNTPGSLAVRVMFERFPSTLVSLSNMEIFIKDNNTKATANIKLLNSIENKITLSSKLTIEGPLRMKEEYLEGLLESPTVIEEAVPDQLRGLLGQATTTLQQLPEPIKDTLANGLRIPLGGTYQRFFMISYLDDEILIVRDTAGVPEVLTRVETSSPMSSSSVVENLEYNS