wanglab/gogpt-training-data huggingface dataset:
Protein: Liquid facets, isoform C (Liquid facets, isoform H) (Liquid facets, isoform K) (Q7KU93)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MQVNVAGLRRNIKNLAHNYSDAQVKVREATSNDPWGPSAAIMSEIAELTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKENIFAIQTLREFVYFEEGKDQGTHVREKAKQLVTLLKDDERLKNERVKAQKAKERFAQNPSGFGSDGYIDGPSQRDLPPGWQEEPPKSVSELEMVRPQTAGEEELQLQLAMAMSREEAEQEEAKRRSDDVRLQLALSQSEQDFKDPNGRPIPAPKKEEQQSHLLDLLDISLGATSISSPPLGAAGGAPTAVVDPWAMPGPRAPSQLSDPWSGTSSPQVDPWNPSAAPRTILGAGVPMTSAPLGAGNDAWGARTQSPSVASGSSNEGWLQSNGNANQNGRGATPAGPPAEGWLIKSTAVGALGAAPINHAANNGSSSSDPWLAEPAASAAGGAAAVGLADPWAPGAASQTGAGALDDPWKALGTGAIKKQSPEFDEFDLITNRNKSEHSNSNASNNNNASLLDDMDPLSANYGNGGINSSMHPSTGATAKKSIKDAHSFLGENSALVNLDNLIKPIAPQTQTGNQPAYNPFSDNVVPPKTNLFQQQQPAVPSINQLKQQAPFSVSMNQDPWAPVMGGVSTTSQPQPNLQVYNNAYQSSSSTNILGKSNIPTNMNSSTSNSTIHSCYASPSPGVDGIRNMDIFTERPYYNSPTAPADDTYMYNSRDNNNINSNYGTPSLYSSFAASYSSALSDSLAETPGISVAPLGFVADTVMSFGPSSSSANCKLEQNNNMPWIKPEAATNPFLS
Protein: Mnd1 HTH domain-containing protein (Q385K1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Homologous-pairing protein 2 winged helix domain-containing protein
- HORMA domain-containing protein
- RAD51/dmc1 protein, putative
Sequence:
MNKSAKKKGLSMEEKVSRIETWFVNNPSPYTLKDLIQILPKATGVIPQSVEECMEILVSENRVRQKKVGVHVLFWRFPQTATQRLAGSMGEKTTTTELAKYLSMSEDELRTELQTLKKTEKDIRQRIKETQASIGDDNAVQKDAEQIRSLQGEVKILEEQLNQLALLDPAFVEKLKAATVVAWESANRWTDNMYLLEQHISRKMGMSARELRAQLQLPLEVEYIEYDELLPSATSGGKSACTSSGNSCASPLICTVDATHGGGNSQEVPAAFHIEEGHTQNINEEAGEALTEGGCDVKPHEDVENETSNTLRKERDGKKRGRGRPPLENAKKDDNMVNAPSVKKKKNEKDRPPAASNTDALTPARQRRCRR
Protein: Proteasome activator protein PA26 (Q38BM8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proteasome regulatory non-ATP-ase subunit
- Proteasome regulatory ATPase subunit 3
- Proteasome regulatory non-ATP-ase subunit 9
- Proteasome regulatory non-ATP-ase subunit 5
- Proteasome regulatory non-ATPase subunit 8
- 26S proteasome regulatory subunit RPN3
- Probable 26S proteasome regulatory subunit rpn-6.2
- Proteasome regulatory non-ATP-ase subunit 7
- Proteasome regulatory ATPase subunit 6
- Proteasome regulatory non-ATPase subunit 11
Sequence:
MPPKRAALIQNLRDSYTETSSFAVIEEWAAGTLQEIEGIAKAAVEAHATIRNSTYGRAQAEKSPEQLLGVLQRYQDLCHNVYCQAETIRTVIAIRIPEHKEEDNLGVAVQHAVLKVIDELEIKTLGSGEKSGSGGAPTPIGMYALREYLSARSTVEDKLLGSVDAESGKTKGGSQSPSLLLELRQIDADFMLKVELATTHLSTMVRAVINAYLLNWKKLIQPRTGSDHMVS
Protein: Tyrosine-protein kinase wzc (EC 2.7.10.-) (P76387)
Organism: Escherichia coli (strain K12)
Function: Required for the extracellular polysaccharide colanic acid synthesis. The autophosphorylated form is inactive. Probably involved in the export of colanic acid from the cell to medium. Phosphorylates udg.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Putative polysaccharide export protein Wza
- Low molecular weight protein-tyrosine-phosphatase Wzb
- UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase
- Putative colanic acid biosynthesis glycosyl transferase WcaA
- Lipopolysaccharide biosynthesis protein WzxC
- Low molecular weight protein-tyrosine-phosphatase Etp
- GDP-mannose 4,6-dehydratase
- Putative colanic acid biosynthesis glycosyl transferase WcaI
- Putative O-antigen transporter
- Tyrosine-protein kinase etk
Sequence:
MTEKVKQHAAPVTGSDEIDIGRLVGTVIEARWWVIGITTVFALCAVVYTFFATPIYSADALVQIEQNSGNSLVQDIGSALANKPPASDAEIQLIRSRLVLGKTVDDLDLDIAVSKNTFPIFGAGWDRLMGRQNETVKVTTFNRPKEMADQVFTLNVLDNKNYTLSSDGGFSARGQAGQMLKKEGVTLMVEAIHASPGSEFTVTKYSTLGMINQLQNSLTVTENGKDAGVLSLTYTGEDREQIRDILNSIARNYQEQNIERKSAEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSVDLPLEAKAVLDSMVNIDAQLNELTFKEAEISKLYTKVHPAYRTLLEKRQALEDEKAKLNGRVTAMPKTQQEIVRLTRDVESGQQVYMQLLNKEQELKITEASTVGDVRIVDPAITQPGVLKPKKGLIILGAIILGLMLSIVGVLLRSLFNRGIESPQVLEEHGISVYASIPLSEWQKARDSVKTIKGIKRYKQSQLLAVGNPTDLAIEAIRSLRTSLHFAMMQAQNNVLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGTNNVNGLSEILIGQGDITTAAKPTSIAKFDLIPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMVARYAVNTLKEVETSLSRFEQNGIPVKGVILNSIFRRASAYQDYGYYEYEYKSDAK
Protein: Tumor protein p53 binding protein 1 (A6NNK5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPGEQMDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEDDSGSHFSMLSRHLPNLQTHKENPVLDVVSNPEQTAGEERGDGNSGFNEHLKENKVADPVDSSNLDTCGSISQVIEQLPQPNRTSSVLGMSVESAPAVEEEKGEELEQKEKEKEEDTSGNTTHSLGAEDTASSQLGFGVLELSQSQDVEENTVPYEVDKEQLQSVTTNSGYTRLSDVDANTAIKHEEQSNEDIPIAEQSSKDIPVTAQPSKDVHVVKEQNPPPARSEDMPFSPKASVAAMEAKEQLSAQELMESGLQIQKSPEPEVLSTQEDLFDQSNKTVSSDGCSTPSREEGGCSLASTPATTLHLLQLSGQRSLVQDSLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQEGRQDKPMDTSVLSEEGGEPFQKKLQSGEPVELENPPLLPESTVSPQASTPISQSTPVFPPGSLPIPSQPQFSHDIFIPSPSLEEQSNDGKKDGDMHSSSLTVECSKTSEIEPKNSPEDLGLSLTGDSCKLMLSTSEYSQSPKMESLSSHRIDEDGENTQIEDTEPMSPVLNSKFVPAENDSILMNPAQDGEVQLSQNDDKTKGDDTDTRDDISILATGCKGREETVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEGSSGSEVEEIPETPCESQGEELKEENMESVPLHLSLTETQSQGLCLQKEMPKKECSEAMEVETSVISIDSPQKLAILDQELEHKEQEAWEEATSEDSSVVIVDVKEPSPRVDVSCEPLEGVEKCSDSQSWEDIAPEIEPCAENRLDTKEEKSVEYEGDLKSGTAETEPVEQDSSQPSLPLVRADDPLRLDQELQQPQTQEKTSNSLTEDSKMANAKQLSSDAEAQKLGKPSAHASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVETHDPILGSGKGDSGAAPDVDDKLCLRMKLVSPETEASEESLQFNLEKPATGERKNGSTAVAESVASPQKTMSVLSCICEARQENEARSEDPPTTPIRGNLLHFPSSQGEEEKEKLEGDHTIRQSQQPMKPISPVKDPVSPASQKMVIQGPSSPQGEAMVTDVLEDQKEGRSTNKENPSKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEFDMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSLHRTSSGTSLSAMHSSGSSGKGAGPLRGKTSGTEPADFALPSSRGGPGKLRETAVPGPLGIEDISPNLSPDDKSFSRVVPRVPDSTRRTDVGAGALRRSDSPEIPFQAAAGPSDGLDASSPGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNVSSPATPTASSSSSTTPTRKITESPRASMGVLSGKRKLITSEEERSPAKRGRKSATVKPGAVGAGEFVSPCESGDNTGEPSALEEQRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH
Protein: WAT1-related protein At3g02690, chloroplastic (Q93V85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:18431481}; Multi-pass membrane protein {ECO:0000269|PubMed:18431481}.
Interaction partners:
- WAT1-related protein At2g37450
- WAT1-related protein At5g07050
- WAT1-related protein At1g21890
- Gibberellin-regulated protein 10
- Ethylene-responsive transcription factor ERF070
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- E3 ubiquitin-protein ligase At3g02290
- Pentatricopeptide repeat-containing protein At3g29290
- Pentatricopeptide repeat-containing protein At5g39350
- Pentatricopeptide repeat-containing protein At2g01740
Sequence:
MEWPWSAIAASSSSSSSCFFASPNSCLSITRRTNLSCVNTSVKSLRHSRFDSKHNLVKRRINGDSVVRRSTTSNNSTEETESSSSSSSVDCVGMGSDVECVNNGEDEENRSSGILSGGEGTFLEWTVLISPFFFWGTAMVAMKEVLPITGPFFVAAFRLIPAGLLLVAFAVYKGRPLPEGINAWFSIALFALVDATCFQGFLAQGLQRTSAGLGSVIIDSQPLTVAVLASFLFGESIGIVRAGGLLLGVAGLLLLEVPSVTSDGNNFSLWGSGEWWMLLAAQSMAIGTVMVRWVSKYSDPIMATGWHMVIGGLPLLAISVINHDPVFNGSLQDLSTNDVIALLYTSIFGSAVSYGVYFYSATKGSLTKLSSLTFLTPMFASIFGYLYLNETFSSLQLVGAAVTLVAIYLVNFPEGND
Protein: Glycine-rich RNA-binding protein RZ1A (AtRZ-1a) (Q9LIN3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds RNA and DNA sequences with a preference to single-stranded nucleic acids. Displays strong affinity to poly(G) and poly(U) sequences. May be involved in tolerance to cold stress.
Subcellular location: Nucleus {ECO:0000269|PubMed:20850334}. Cytoplasm {ECO:0000269|PubMed:20850334}.
Interaction partners:
- Cold shock protein 2
- GDSL esterase/lipase At3g26430
- KH domain-containing protein
- F17H15.1/F17H15.1
- KH domain-containing protein
- Pumilio homolog 4
Sequence:
MSEDPEYRCFIGGLAWTTSDRGLRDAFEKYGHLVEAKVVLDKFSGRSRGFGFITFDEKKAMDEAIAAMNGMDLDGRTITVDKAQPHQGGAGRDNDGDRGRDRGYDRDRSRPSGGRGGGDCFKCGKPGHFARECPSESSRDGGGRFSSKDDRYSSKDDRYGAKDDRYGAKEDRYGAKDDRYSSKDDRYSSKDDRYGSRDGGGSRYGPDRSGERAGGRSRDGGSRGAPGGERHSRAPYDRPRAGGFH
Protein: site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) (O33298)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible type I restriction/modification system specificity determinant HsdS.1
- Possible type I restriction/modification system specificity determinant HsdS
- site-specific DNA-methyltransferase
- Ribonuclease VapC21
- Helicase ATP-binding domain-containing protein
- Flavin-dependent thymidylate synthase
- Winged helix-turn-helix domain-containing protein
Sequence:
MPPRKKQAPQAPSTMKELKDTLWKAADKLRGSLSASQYKDVILGLVFLKYVSDAYDERREAIRAELAAEGMEESQIEDLIDDPEQYQGYGVFVVPVSARWKFLAENTKGKPAVGGEPAKNIGQLIDEAMDAVMKANPTLGGTLPRLYNKDNIDQRRLGELIDLFNSARFSRQGEHRARDLMGEVYEYFLGNFARAEGKRGGEFFTPPSVVKVIVEVLEPSSGRVYDPCCGSGGMFVQTEKFIYEHDGDPKDVSIYGQESIEETWRMAKMNLAIHGIDNKGLGARWSDTFARDQHPDVQMDYVMANLPFNIKDWARNEEDPRWRFGVPPANNANYAWIQHILYKLAPGGRAGVVMANGSMSSNSNGEGDIRAQIVEADLVSCMVALPTQLFRSTGIPVCLWFFAKDKAAGKQGSIDRCGQVLFIDARELGDLVDRAERALTNEEIVRIGDTFHAWRGSKSAAVKGIMYEDVPGFCKSATLAEIKATDYALTPGRYVGTPAVEDDGEPIDEKMARLSKALLEAFDESARLERVVREQLGRLR
Protein: Pentamidine resistance factor, mitochondrial (P38969)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probably involved in mitochondrial export. Confers resistance to the anti-pneumocystis carinii drug pentamidine. May act by the removal of pentamidine, or its damage targets, from the matrix by an active-transport mechanism.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823961}; Single-pass membrane protein {ECO:0000269|PubMed:16823961}.
Interaction partners:
- Cytochrome c oxidase assembly protein COX18, mitochondrial
- Protein MSS2
- Inner membrane mitoribosome receptor MBA1, mitochondrial
- Protein transport protein TIP20
- FKBP12-associated protein 1
- DNA primase small subunit
- Histone H4
- Mitochondrial inner membrane protein OXA1
- Enhancer of mRNA-decapping protein 3
- Cardiolipin synthase
Sequence:
MDSRVALVRKYIAPSVIKSDSIQLHGLVKAPLFKALNSRYKLGSLQIVQDVDWNAKTTPSDSPEPLAATLNSNRSLPMTKFPKQEILEQVKLDTKVGKWRKFMTGWFRIGLYLLKSYKTGIQNTLKVFWDTRNEEQKFSIKNGALANLVREIEMHEINTRLSSSSLPTSSSAKAPLRPLSINRKTLVELIRRDQIWKLPVFFTLVFIFEEVSVLIFTFFPRVCPYNCLTPGGYKKLSNSYIKGTTSTQGNYGLGPLEFTKQGTIKYEPPYAVPIENLYNFLTSFPQSMISNWKLYIYKKLKLQKLLCNEIEKIYQYLFIDDWLLLQSILNTDVEKTKIALSDRELVNCILERKLYHMGDDLNEMVNDTLGKEILLKRLFLYWTLRYNDTISLNGKHTFSEKWGVNNISLLKYNSELVATKDIQ
Protein: Circadian clock oscillator protein KaiC 1 (EC 2.7.11.1) (EC 3.6.4.-) (P74646)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Component of the oscillator and circadian clock in this organism, enhances fitness in a rhythmic environment. Autophosphorylates in the presence of KaiA, no activity is seen in its absence.
Interaction partners:
- Circadian clock oscillator protein KaiB1
- Circadian clock oscillator protein KaiA
- Circadian clock protein KaiB3
- Circadian clock protein KaiB2
- Protein RecA
- Amidophosphoribosyltransferase
- Probable transcriptional regulator ycf27
- Adaptive-response sensory kinase SasA
- Replicative DNA helicase DnaB
- Cell division protein FtsZ
Sequence:
MNLPIVNERNRPDVPRKGVQKIRTVIEGFDEITHGGLPIGRTTLVSGTSGTGKTLLAVQFLYQGIHHFDYPGLFITFEESPSDIIENAYSFGWDLQQLIDDGKLFILDASPDPEGQEVVGTFDLSALIERIQYAVRKYKAKLVSIDSVTAVFQQYDAASVVRREIFRLVARLKQLQVTSIMTTERVEEYGPIARFGVEEFVSDNVVVLRNVLEGERRRRTVEILKLRGTTHMKGEYPFTITHDGINIFPLGAMRLTQRSSNARISSGVQTLDEMCGGGFFKDSIILATGATGTGKTLLVSKFLQEGCRQRERAILFAYEESRAQLSRNASSWGIDFEEMEHKGLLKLLCTYPESAGLEDHLQMIKSEISEFKPSRIAIDSLSALARGVTNNAFRQFVIGVTGYAKQEEITGFFTNTTDQFMGAHSITESHISTITDTILMLQYVEIRGEMSRALNVFKMRGSWHDKGIREYSISHDGPDIRDSFRNYERIISGSPTRISVDEKSELSRIVRGVKDKTAE
Protein: L-sulfolactate dehydrogenase (EC 1.1.1.337) ((R)-2-hydroxyacid dehydrogenase) ((R)-sulfolactate dehydrogenase) (L-2-hydroxycarboxylate dehydrogenase (NAD(+))) (Q58820)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate much more efficiently than the reverse reaction. Also catalyzes the reduction of oxaloacetate, alpha-ketoglutarate, and to a much lower extent, KHTCA, but not pyruvate. Involved in the biosynthesis of both coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha-ketoglutarate).
Subcellular location: Cytoplasm.
Interaction partners:
- 2-phosphosulfolactate phosphatase
- L-2-hydroxycarboxylate dehydrogenase
- tRNA-splicing endonuclease
- Phosphosulfolactate synthase
- Uncharacterized protein MJ1426
- Threonine synthase
Sequence:
MILKPENEKKLIIDVLKKFGVPEEDAKITADVFVDADLKGFTSHGIGRFPQYITALKLGNINPKPDIKIVKESPATAVIDGDLGLGQVVGKKAMELAIKKAKNVGVGVVATRNANHFGIAGYYSELAMNQDMIGITITNTEPAMAPFGGKEKILGTNPIAIAFKGNKYKFSLDMATASIARGKILEALRKKIKIPEGCAVDKDGKPTTDPAKALEGCILPFGGPKGYGLALAIEMLSAIGGAEVGTKVKGTANPEERCTKGDLFIAINPEFFMGKEEFKRKVDELLDEIKNSEPAEGFEILIPGEIEERNKMKRKDGFEIDKNLYNQLKEICNELGLNIEDYIE
Protein: 3-mercaptopyruvate sulfurtransferase (MST) (EC 2.8.1.2) (Rhodanese-like protein) (P31142)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of sulfur from 3-mercaptopyruvate to a thiol-containing acceptor to form an intramolecular disulfide releasing hydrogen sulfide and pyruvate (Probable). May be involved in the enhancement of bacterial growth inhibition by serine.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Cysteine desulfurase IscS
- Cystathionine beta-lyase MetC
- Thiosulfate sulfurtransferase GlpE
- Protein MalY
- Sulfite reductase hemoprotein beta-component
- Sulfite reductase flavoprotein alpha-component
- Phosphoadenosine 5'-phosphosulfate reductase
- Aspartate aminotransferase
- Putative cytochrome YdhU
- D-cysteine desulfhydrase
Sequence:
MSTTWFVGADWLAEHIDDPEIQIIDARMASPGQEDRNVAQEYLNGHIPGAVFFDIEALSDHTSPLPHMLPRPETFAVAMRELGVNQDKHLIVYDEGNLFSAPRAWWMLRTFGVEKVSILGGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVKVTDVLLASHENTAQIIDARPAARFNAEVDEPRPGLRRGHIPGALNVPWTELVREGELKTTDELDAIFFGRGVSYDKPIIVSCGSGVTAAVVLLALATLDVPNVKLYDGAWSEWGARADLPVEPVK
Protein: Cell division cycle 20.3, cofactor of APC complex (AtCDC20.3) (Q9S7H3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21687678}.
Interaction partners:
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 7
- Anaphase-promoting complex subunit 11
- Mitotic spindle checkpoint protein MAD2
- Cell division cycle protein 27 homolog A
- Cell division cycle protein 27 homolog B
Sequence:
MDSDTCTVPDHFLPRKLSKQNLDRFIPNRSAMDFDFANYALTQGRKRNVDEITSASRKAYMTQLAVVMNQNRTRILAFRNKPKALLSSNHSDSPHQNPKSVKPRRYIPQNSERVLDAPGLMDDFYLNLLDWGSANVLAIALGDTVYLWDASSGSTSELVTIDEDKGPVTSINWTQDGLDLAVGLDNSEVQLWDFVSNRQVRTLIGGHESRVGSLAWNNHILTTGGMDGKIVNNDVRIRSSIVGTYLGHTEEVCGLKWSESGKKLASGGNYNVVHIWDHRSVASSKPTRQWLHRFEEHTAAVRALAWCPFQATLLATGGGVGDGKIKFWNTHTGACLNSVETGSQVCSLLWSQRERELLSSHGFTQNQLTLWKYPSMSKMAELNGHTSRVLFMAQSPNGCTVASAAGDENLRLWNVFGEPPKTTKKAASKNYLELFSHVNSLR
Protein: 23S rRNA (guanine(2535)-N(1))-methyltransferase (EC 2.1.1.209) (Avilamycin resistance protein A) (Q9F5K5)
Organism: Streptomyces viridochromogenes
Function: Specifically methylates the guanine-2535 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic.
Interaction partners:
Sequence:
MSAYRHAVERIDSSDLACGVVLHSAPGYPAFPVRLATEIFQRALARLPGDGPVTLWDPCCGSGYLLTVLGLLHRRSLRQVIASDVDPAPLELAAKNLALLSPAGLTARELERREQSERFGKPSYLEAAQAARRLRERLTAEGGALPCAIRTADVFDPRALSAVLAGSAPDVVLTDLPYGERTHWEGQVPAQPVAGLLRSLASALPAHAVIAVTDRSRKIPVAPVKALERLKIGTRSAVLVRAADVLEAGP
Protein: Transferrin receptor protein 1 (TR) (TfR) (TfR1) (Trfr) (CD antigen CD71) (Q07891)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (By similarity). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). Positively regulates T and B cell proliferation through iron uptake (By similarity). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (By similarity). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (By similarity). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P02786}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P02786}. Melanosome {ECO:0000250|UniProtKB:P02786}.
Interaction partners:
Sequence:
MMDQARSAISNLFGGEPLSYTRFSLARQVDGDNSHVEMKLAVDEEENTDNNMKASVRKHRRLNGRLCFGTIAVVIFFLIGFMIGYLGYCKRTEQKDCVRLAETETGNSEIIQEENIPQSSRLYWADLKKLLSEKLDAIEFTDTIKQLSQTSREAGSQKDENLAYYIENQFRDFKLSKVWRDEHYVKIQVKGSAAQNAVTIINVNGDSDLVENPGGYVAYSKATTVSGKLIHANFGTKKDFEDLKYPVNGSLVIVRAGKITFAEKVANAQSFNAIGVLIYMDQTKFPVVEAELSLFGHAHLGTGDPYTPGFPSFNHTQFPPSQSSGLPSIPVQTISRKAAEKLFQNMETNCPPSWNTDSLCKLESSQGINVNLSVNNVLKETRILNIFGVIKGFEEPDRYIVVGAQRDAWGPGAAKSSVGTGLLLKLAQAFSDMVSRGGFKPSRSIIFASWSAGDFGAVGATEWLEGYLSSLHLKAFTYINLDKVVLGTRNFKVSASPLLYTLIEKTMQDVRHPIDGKPLYRDSNWISKVEDLSLDNAAFPFLAYSGIPAVSFWFCENEDYPYLDTNLDTYEKLIQKVPQLNKMVRAAAEVAGQFIIKLTHDIELNLDYDMYNNKILSFVKELNQFRADIKAMGLSLQWLYSARGDFFRATSRLTTDFHNAEKTNRFVVREINNRIMKVEYHFLSPYVSPRESPFRHIFWGSGSHTLTALVENLKLRQKNSSAFNETLFRNQLALATWTIQGVANALSGDIWDIDNEF
Protein: Kinesin-1 heavy chain (Conventional kinesin heavy chain) (Ubiquitous kinesin heavy chain) (UKHC) (Q61768)
Organism: Mus musculus (Mouse)
Function: Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. May be involved in the mechanisms of growth arrest induced by exposure to DNA-damaging drugs or by cellular senescence. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes. Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). Through binding with PLEKHM2 and ARL8B, directs lysosome movement toward microtubule plus ends. Involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q2PQA9}. Cytolytic granule membrane {ECO:0000250|UniProtKB:P33176}. Lysosome membrane {ECO:0000250|UniProtKB:P33176}; Peripheral membrane protein {ECO:0000250|UniProtKB:P33176}; Cytoplasmic side {ECO:0000250|UniProtKB:P33176}. Note=Uniformly distributed between soma and neurites in hippocampal neurons. {ECO:0000250|UniProtKB:Q2PQA9}.
Interaction partners:
- Kinesin light chain 2
- Kinesin light chain 1
- Kinesin light chain 4
- Kinesin light chain 3
- Kinesin heavy chain isoform 5A
- Kinesin heavy chain isoform 5C
- Trafficking kinesin-binding protein 1
- Mitochondrial Rho GTPase 1
- E3 SUMO-protein ligase RanBP2
- Glycogen synthase kinase-3 beta
Sequence:
MADPAECNIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKTLRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTADKDIAITSDKPAAAVGMAGSFTDAERRKCEEELAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPGTVRGGGSFVQNNQPVGLRGGGGKQS
Protein: Earthbound 2, isoform A (Earthbound 2, isoform B) (MIP13624p) (MIP13924p) (Q9VP44)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00320}.
Interaction partners:
Sequence:
MAAIAALPTTTLRRNNNNNTKGIKSRRNERNILTFYEKIAVIRYYDETNISRNSLAKMFHCCATQIRRILDKKKDLLQQLATLSEADASIIIEEMTRKRRKFEMSAISFLLHEWVERCIQMQLNISIRNQKLKETAIRMAAVLNLPSFRPSYRWLSRFRNKYKYEADELGYQGENPLNQDLPVEDIIVEFKHALPNFMQRELDNPGEAISKAAVMADFVNLSSENSIMSDHPEGDNEVELVTCEPTMMSSPSSTPDAAEGEIPLQAHGDQENPDDQINAGTSTLLNGVFPHLAIIHQFALMNSDVQALELISQLGVHMQQQAVSGAYHNLSLATTDGDGQDDPGEIALSELPPGSIYADIDDIELIE
Protein: Retinol dehydrogenase 10 (EC 1.1.1.300) (Q8VCH7)
Organism: Mus musculus (Mouse)
Function: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol (By similarity). Required for normal embryonic development.
Subcellular location: Microsome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 26A1
- Lecithin retinol acyltransferase
- Retinol dehydrogenase 11
- Retinoid isomerohydrolase
- Beta,beta-carotene 15,15'-dioxygenase
- Retinol dehydrogenase 5
- Retinal dehydrogenase 2
- Diacylglycerol O-acyltransferase 1
- All-trans-retinol 13,14-reductase
- Retinaldehyde dehydrogenase 3
Sequence:
MNIVVEFFVVTFKVLWAFVLAAARWLVRPKEKSVAGQVCLITGAGSGLGRLFALEFARRRALLVLWDINTQSNEETAGMVRHIYRDLEAADAAALQAGKGEEEILPPCNLQVFTYTCDVGKRENVYLTAERVRKEVGEVSVLVNNAGVVSGHHLLECPDELIERTMMVNCHAHFWTTKAFLPTMLEINHGHIVTVASSLGLFSTAGVEDYCASKFGVVGFHESLSHELKAAEKDGIKTTLVCPYLVDTGMFRGCRIRKEIEPFLPPLKPDYCVKQAMRAILTDQPMVCTPRLMYIVTFMKSILPFEAVVCMYRFLGADKCMYPFIAQRKQATNNNEAKNGI