wanglab/gogpt-training-data huggingface dataset:
Protein: Insulin [Cleaved into: Insulin B chain; Insulin A chain] (O73727)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Subcellular location: Secreted.
Interaction partners:
- Glucagon b
- Insulin receptor substrate 1
- Tyrosine-protein kinase receptor
- Tyrosine-protein kinase receptor.
- Appetite-regulating hormone isoform X1
- Tyrosine-protein kinase receptor.
- Tyrosine-protein kinase receptor.
- Insulin receptor substrate 2
- Insulin-degrading enzyme
- Insulin-like growth factor 1
Sequence:
MAVWLQAGALLVLLVVSSVSTNPGTPQHLCGSHLVDALYLVCGPTGFFYNPKRDVEPLLGFLPPKSAQETEVADFAFKDHAELIRKRGIVEQCCHKPCSIFELQNYCN
Protein: Translation initiation factor IF-2, chloroplastic (Q9SHI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity).
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Class I peptide chain release factor
- Small ribosomal subunit protein uS14m
- At1g64880
- Small ribosomal subunit protein uS14c
- Small ribosomal subunit protein mS29
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Large ribosomal subunit protein uL15c
- Large ribosomal subunit protein uL24c
- Peroxidase 7
- Ribosomal protein L18e/L15 superfamily protein
Sequence:
MPSMLVLVGTMPSLASLVSLGGACASVSGTSSSDASYALVKRVSLSRRSVKGTKKWLCRYSVSSSTTTTTADFIADQNNNSVSIDSNSFRGSKDGDDSEVVLKQTPKPVLKPPVARVERGLGVNTAPWSKDLSNGGKFDGEEERNKVIESLGEVLDKAEKLEIPKPGNKEGGEAVKPSQPSANSSNSRNGSYANASDGGTRKTKTMKSVWRKGDAVAAVQKVVKESPKIFNRGVQTEPRTREEGEVNAKAGTPLAPPQPPFRPQPPVRPQPMLQGKPMVAPPVKKSPILKDLGMAAKPLVSEEVDSSVKSKERKPILVDKFASKKKGVDPAASQAVLAPTKPGKGPPSNKFRVEHRNKKNASASPRRRIVAEDDGDDDASISRSGRKGRKWSKASRKAVRLQAAKDAAPVKAEILEVEEEGMSIEDLAYNLAIGEGDILGYLYSKGIRPDGVHTLDREMVKMICRDYDVEVLDADSVKVEEMAKKRQTFDEEDLDKLEDRPPVITIMGHVDHGKTTLLDYIRKSKVAASEAGGITQGIGAYKVSVPVDGKLQSCVFLDTPGHEAFGAMRARGARVTDIAIIVVAADDGIRPQTNEAIAHAKAAAVPIVIAINKIDKEGASPDRVMQELSSIGLMPEDWGGDVPMVQISALKGENVDDLLETVMLVAELQELKANPHRNAKGIVIEAGLDKAKGPFATFIVQKGTLKRGDVVVCGEAFGKVRALFDHSGERVDEAGPSIPVQVIGLNNVPIAGDEFEIVSSLDVAREMAEARAVSLRDERISAKAGDGKVTLSSLASAVSAKKMSGLDLHQLNIILKVDVQGSIEAVRQALQVLPQENVTLKFLLQATGDVSNSDVDLASASEAIVFGFNVKASGSVKKAAENKGVEIRLYRVIYELIDDVRNAMEGLLESVEEQIPIGSAEVRATFSSGSGRVAGCMVNEGKFVKDCGIRVVRKGKTVHVGVLDSLKRVKENVKEVSAGLECGIGMDDYDDWIEGDIIEAFNAVQKRRTLEEASASMSAAIEEAGV
Protein: Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide S-acetyltransferase component 2 of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2 2) (PDC-E2 2) (PDCE2 2) (Q8RWN9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Succinate--CoA ligase subunit alpha-1, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
Sequence:
MASRIINHSKKLKHVSALLRRDHAVAVRCFSNSTHPSLVGREDIFKARLNYSSVERISKCGTGNVTMLSGISTTSTKLSSPMAGPKLFKEFISSQMRSVRGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVAPGEVLCEVETDKATVEMECMEEGFLAKIVKEEGAKEIQVGEVIAITVEDEDDIQKFKDYTPSSDTGPAAPEAKPAPSLPKEEKVEKPASAPEAKISKPSSAPSEDRIFASPLARKLAEDNNVPLSSIKGTGPEGRIVKADVEDFLASGSKETTAKPSKQVDSKVPALDYVDIPHTQIRKVTASRLAFSKQTIPHYYLTVDTCVDKMMGLRSQLNSFQEASGGKRISVNDLVIKAAALALRKVPQCNSSWTDEYIRQFKNVNINVAVQTENGLYVPVVKDADKKGLSTIGEEVRFLAQKAKENSLKPEDYEGGTFTVSNLGGPFGIKQFCAVINPPQAAILAIGSAEKRVVPGTGPDQYNVASYMSVTLSCDHRVIDGAIGAEWLKAFKGYIETPESMLL
Protein: Estrogen receptor beta (Nuclear receptor subfamily 3 group A member 2) (F1D8N3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHARAEKASQTLTSFGMKMETLLPEATMEQ
Protein: p44-2b outer membrane protein (Q2GIP2)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MMSMAIVMAGNDVRAHDDVSALETGGAGYFYVGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDKLTAALAKTSGKDIVQFANAVKISSSAIDGKVCTGSHADLAPGTNAGKKFVVNPEASGSTDGDTSQCSGLGHSSGVTQNPKLFSTFVDTVKIAEDKNWPTGRAKSNTSLKTGDTNSNAKAVATDLVQELTPEEKTIVAGLLAKTIEGGEVVEIRAVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGHITPKLAYRLKAGLSYQLSPVISAFAGGFYHRVVGDGVYDDLPAQRLVDDTSPAGRTKDTAIANFSMAYVGGEFGVRFAF
Protein: 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58) (Transplantation antigen P91A) (Tum-P91A antigen) (P14685)
Organism: Mus musculus (Mouse)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Interaction partners:
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 6A
Sequence:
MKQEGSARRRGADKAKPPPGGEQEPPPPAPQDVEMKEEAAAGSGSTGEGDGKAAATEHSQRELDTVTLEDIKEHVRQLEKAVSGKEPRFVLRALRMLPSTSRRLNHYVLYKAVHGFFTSNNATRDFLLPFLEEPMDTEADLQFRPRTGKAASAPLLPEVEAYLQLLMVIFLMNSKRYKEAQKISDDLMQKISTQNRRALDLVAAKCYYYHARVYEFLDKLDVVRSFLHARLRTATLRHDADGQATLLNLLLRNYLHYSLYDQAEKLVSKSVFPEQANNNEWARYLYYTGRIKAIQLEYSEARRTMTNALRKAPQHTAVGFKQTVHKLLIVVELLLGEIPDRLQFRQPSLKRSLMPYFLLTQAVRTGNLAKFNQVLDQFGEKFQTDGTYTLIIRLRHNVIKTGVRMISLSYSRISLADIAQKLQLDSPEDAEFIVAKAIRDGVIEASINHEKGYVQSKEMIDIYSTREPQLAFHQRISFCLDIHNMSVKAMRFPPKSYNKDLESAEERREREQQDLEFAKEMAEDDDDSFP
Protein: Retinol dehydrogenase 10 (EC 1.1.1.300) (Short chain dehydrogenase/reductase family 16C member 4) (Q8IZV5)
Organism: Homo sapiens (Human)
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.
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
- Retinal dehydrogenase 2
- Retinaldehyde dehydrogenase 3
- RPE-retinal G protein-coupled receptor
- Aldehyde dehydrogenase 1A1
- Lecithin retinol acyltransferase
- Retinoid isomerohydrolase
- Retinol dehydrogenase 11
- Beta,beta-carotene 15,15'-dioxygenase
- Retinol dehydrogenase 5
Sequence:
MNIVVEFFVVTFKVLWAFVLAAARWLVRPKEKSVAGQVCLITGAGSGLGRLFALEFARRRALLVLWDINTQSNEETAGMVRHIYRDLEAADAAALQAGNGEEEILPHCNLQVFTYTCDVGKRENVYLTAERVRKEVGEVSVLVNNAGVVSGHHLLECPDELIERTMMVNCHAHFWTTKAFLPTMLEINHGHIVTVASSLGLFSTAGVEDYCASKFGVVGFHESLSHELKAAEKDGIKTTLVCPYLVDTGMFRGCRIRKEIEPFLPPLKPDYCVKQAMKAILTDQPMICTPRLMYIVTFMKSILPFEAVVCMYRFLGADKCMYPFIAQRKQATNNNEAKNGI
Protein: Transcription factor bHLH95 (Basic helix-loop-helix protein 95) (AtbHLH95) (bHLH 95) (Protein RETARDED GROWTH OF EMBRYO 1) (Protein ZHOUPI) (Transcription factor EN 21) (bHLH transcription factor bHLH095) (Q9FXA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that controls embryo growth. Regulates endosperm breakdown and embryonic epidermal development. Regulates the expression of SBT2.4/ALE1. Involved in embryonic cuticle formation upstream of SBT2.4/ALE1. Does not seem to be a general regulator of endosperm patterning. May control specific signaling pathways that coordinate embryo invasion and breakdown of surrounding endosperm tissues. Required for the production the embryo sheath, an extracuticular endosperm-derived structure at the surface of the embryo. Acts upstream of KRS.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:18567831}.
Interaction partners:
- Subtilisin-like protease SBT2.4
- Transcription factor ICE1
- Transmembrane protein
- GDSL esterase/lipase At5g03820
- LRR receptor-like serine/threonine-protein kinase GSO2
- LRR receptor-like serine/threonine-protein kinase GSO1
- F16L1.2 protein
- C2H2 and C2HC zinc fingers superfamily protein
- C2H2 and C2HC zinc fingers superfamily protein
Sequence:
MTNAQELGQEGFMWGISNSDDSGGGCKRIEKEPLPSHPSHPSPEIQTTTVKKGKKRTKRNDKNHEEESPDHEIHIWTERERRKKMRDMFSKLHALLPQLPPKADKSTIVDEAVSSIKSLEQTLQKLEMQKLEKLQYSSASTNTTPTTTFAYAPSSSSSPTALLTPISNHPIDATATDSYPRAAFLADQVSSSSAAAANLPYPCNDPIVNFDTWSSRNVVLTICGNEAFFNLCVPKHKPGVFTSVCYLFEKYNMEVLFANVSSNVFWSTYVIQAQVNPSCENQLLGNGLGVVDVFKQVSQELVLYFSSL
Protein: alpha-mannosidase (EC 3.2.1.24) (Q4WX47)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- mannan endo-1,4-beta-mannosidase
Sequence:
MGGDVPLRAPSSLPRAPEHPVGQRIKSIYTDRLRQFTDSGQYREQSLISKLYEATTSDEDHVKLSVYSPPDLQRPTFEEATSHEFTPTHIGASFGPSWSTHWFRIRLTVPRDMLDKERLEFHWDANNEGLVWTDDGRPVQGLTGGGERIEWVIPDAWRDGKEHTFYIEMACNAMFGNAPGGDSIQPPAPDKYYTLHTARITAVNVEARALFYDFWIIGDAAREFPGDSWEAHEANMVANAIMDAFIAGHGSRDSIKEARRIAQKYLGDKVDSSDVYETDTQPIVYAIGHCHIDSCWLWPWAETKRKVARSWSNQCDLMDRYPEHRFTCSQAQQFKWLEQYYPSVFDRVKRWVKKGHFQPIGGSWVEHDTNLPSGESLVRQFIYGQRFFESRFGERCSTFWLPDTFGYSSQIPQICRLAGMSRFFTQKLSWNNINNFPHTTFKWVALDGSQVMCHMAPSETYTAEAHFGDVKRSVTQHKSLDHDNTSLLVFGKGDGGGGPTFEHLEKLRRCRGLSDKVGLLPRVKMGDSVDDFFTRLEQKVANGTEFVTWYGELYFELHRGTYTTQANNKRNNRKSEFLLRELEYLSTLASLTKTNGEYKYPKNDIDDMWEGVLLCQFHDCLPGSSIEMCYDDSDKLYAQIFETGERARQQALEALGFPENSAGKSLVAINTLPWFRSEIVKIPDEFVALTGSRYALARGDPGLIQCQVLDAKRKPTVTVAEIRPGIFRLDNGKLRVDVQDGVITSLYDLEAEREVIAKGGKAGQLVVFDDKPLYWQAWDVEVYHLDSRKELQAGKTSIAEEGPHRVSVATTIQISDQSWVKTTISLAAAVDDQPSYVEFESEVEWQETMKFLKVEFPVDITNTEASYETQYGITRRPTHYNTSWDMAKFEVCCHKWADLSEYGYGVSILNDSKYGFATCGNLMRLSLLRAPKAPDAHADMGRHHIRYAILPHAGPLDARTVRAGYNFNSPLILRRCSGMQSADVFRSIAVRGSQSLILDVVKRGEDDEDVSRGELPKRPGKSIILRIYESLGGRSRGTIHAKFPVKEAWKCNVLEDNEERLEVCKGEDDVAVKIELRAFEVATYRLQL
Protein: Kakapo (O77291)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTSHSYYKDRLGFDPNEQQPGSNNSMKRSSSRQTTHHHQSYHHATTSSSQSPARISVSPGGNNGTLEYQQVQREQRDRELYSNNGSLHHHQHHHHHHRHSTTGSASSPLYENSSSPAAPKKAKHSSTQAQPQGGYEDALTQFKDERDAIQKKTFTKWVNKHLKKANRRVVDLFEDLRDGHNLLSLLEVLSGEHLPREKGKMRFHMLQNAQMALDFLRYKKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQISDIVVGKEDNVSAREALLRWARRSTARYPGVRVNDFTSSWRDGLAFSALVHRNRPDLLDWRKARNDRPRERLETAFHIVEKEYGVTRLLDPEDVDTNEPDEKSLITYISSLYDVFPEPPSIHPLFDMESQRRVHEYRDLAQQFIYWCHEKTAYLQERSFPPTLIEMKRLLSDLQRFRSDEVSARKREKSKLIQIYKELERYFETVGEVDVEAELRPDAIEKAWYRMNTALQDREVILQQEIERLERLQRLADKVQREIKHVDQKLTDLEARIGEEGRRIERLHPVDAKSIVEALETEIRHLEEPIQDMNQDCHVLNEGRYPHVSELHKKVNKLHQRWAQLRTNFHTNLVQKLSGLKYPVHETTVTRQTRMVVESRQIDTNPHFRDLQEHIEWCQNKLKQLLAADYGSDLPSVKEELDRQQHEHKIIDQFHTKILNDERQQTKFSGDELALYQQRLNQLQKVYAELLSTSTKRLSDLDSLQHFLGQASAELQWLNEKEQVEITRDWADKQLDLPSVHRYYENLMSELEKREMHFATILDRGEALLNQQHPASKCIEAHLTALQQQWAWLLQLTLCLEVHLKHATEYHQFFGEIKDAEQWLAKRDEILNSKFSQSDFGLDQGETLLRGMQDLREELNAFGETVATLQRRAQTVVPLNKRRQPVNRQGPVQAICAYKQQGQLQIEKGETVTLLDNSGRVKWRVRTAKGQEGPIPGACLLLPPPDQEAIDAAERLKRLFDRSVALWQKKHLRLRQNMIFATIRVVKGWDFDQFLAMGPEQRTAIRRALNDDADKLLSEGDPNDPQLRRLRREMDEVNRLFDEFEKRARAEEESKQASRIFTEECLSIKSKLEDMARELDQIILAPLPRDLDSLEHVLEIHSDYERRLHLLEPELKHLQETFRTIALKTPVLKKSLDNLMELWKELNTQSGLHKDRLKLLEASLAGLEDNEHVISELENELARHQDLPSTAEGLQQVFKQLNHMQDIITQQQPQMDKMNDAADQLGRMGVPTKVLGDLKRLHSNVERLNTRWSAVCNQLGERMRSCETAIGLMKNLQSSVQVEESWVDGTTERLSAMPTATSAYELDKLLGAAIERKPKIENVNVAGGRLIREAKIYDSKCLRFVDWLVEARPSFSPPRRDLRPADSDPGATQYYSQRLDNLNTKYDRLLEQLSQRLKTAIEVNGSDGLQYAESLQKPLKTFRVDFSAGSLPTGDGYAARQEDLYTTTYSTTQISSTKTTKSSTKSVYSSDGLDAASQDVSTASLPQSQIQFNEIRTLKRSQQLGGHSVLDIAGIRDPRTGRVLTIGEAIQLRILDVRTGEMLVGDRRITLEQAADQGLIDLQLAKQLLEPGAGRDASGRELSLLEVIQREISEAESGYETAEKRIKQAVFEKFNMCEENVNDLLKWVTTVEQKISSVGGPREKIDELRNQINALKQIKDEIESQQRPVATCLEQIRQIVLTGGDVLSAPEVTTLENSGRELRSRVDRVNDRTVRLLRRLEAGRDELTKLRSELDVFSDWLQVARRTLEDKERSLSDLTRLPSQADSVREFVSDVIGHQADLRFITMAAQKFVDESKEFLAILNDFRTSLPERLPHVEPLSSAESPIRQEVSLVSAQYKDLLNRVNALQDRVSGLGGRQREYQDALDKANEWLRSVHPRVSRIISEPIAGDPKGVQDQMNEAKALHNELLSSGRLVDNAQQALDNLLRSLGGQLSPMEINQLELPIADLKNNYQQLLDNLGEHCKTLDKTLVQSQGVQDALDSLVGWVNQAEDKFKMNLRPASLIKERLQEQIREHKVLLADLQSHQASIDSVQVSAKHLLASASNARIAKKVESNLNDVTGKFEKLYEKANKRGEFLDDVYNRLSRYLDEISTVEQRMASLQEALDSRETSLLSTEELARRMNELSRDKDQLAPQFEDCVRSGKDLISLRDVTDTGVLRDRIKALESQWRNINISIDERAKLSKQKAEQQLAYEGLKDQVLSWLASTEARVNGLPPVAIDLDRIKQQHDELKPICKDYRDYAPTIDKINDIGAQYDALIRPESPARKRSTYSPIKRTSPLRRMSGDARSPSPTKGGILSPLSTGSSGFGSRRSSQDGFQLSELSPVQQQLSEINNRYGLIGVRLNDRQHELDNLNEELRKQYENLKGL
Protein: Tethering factor for nuclear proteasome cut8 (Cell untimely torn protein 8) (P38937)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Together with nucleoporin alm1, tethers the proteasome to the nuclear envelope. Involved in ubiquitin-mediated protein degradation and facilitates the degradation of nuclear proteins like mitotic cyclin and cut2. Required for normal progression of anaphase.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:11084332, ECO:0000269|PubMed:28974540}.
Interaction partners:
- PITH domain-containing protein P35G2.02
- 26S proteasome regulatory subunit rpn1
- Securin
- 26S proteasome regulatory subunit rpn11
Sequence:
METLSYSQIKKRKADFDEDISKRARQLPVGEQLPLSRLLQYSDKQQLFTILLQCVEKHPDLARDIRGILPAPSMDTCVETLRKLLINLNDSFPYGGDKRGDYAFNRIREKYMAVLHALNDMVPCYLPPYSTCFEKNITFLDAATNVVHELPEFHNPNHNVYKSQAYYELTGAWLVVLRQLEDRPVVPLLPLEELEEHNKTSQNRMEEALNYLKQLQKNEPLVHERSHTFQQTNPQNNFHRHTNSMNIGNDNGMGWHSMHQYI
Protein: Beta-tubulin 2 (A6MUS8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
PELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSTVCDIPPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYT
Protein: HTH-type transcriptional repressor Rv1474c (O53165)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Represses the expression of the aconitase gene acn and its own expression, in an iron-responsive manner. Binds to the inverted repeat element present in the upstream region of acn (Rv1475c)-Rv1474c operon. Preferentially binds to major groove of the DNA.
Interaction partners:
- Aconitate hydratase A
- PaaX domain-containing protein, C-domain protein
Sequence:
MPKVSEDHLAARRRQILDGARRCFAEYGYDKATVRRLEQAIGMSRGAIFHHFRDKDALFFALAREDTERMAAVASREGLIGVMRDMLAAPDQFDWLATRLEIARKLRNDPDFSRGWAERSAELAAATTDRLRRQKQANRVRDDVPSDVLRCYLDLVLDGLLARLASGEDPQRLAAVLDLVENSVRRS
Protein: Cell pattern formation-associated protein stuA (Stunted protein A) (Q5B8H6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MAAVDFSNVYSATYSSVPVYEFKIGTDSVMRRRSDDWINATHILKVAGFDKPARTRILEREVQKGVHEKVQGGYGKYQGTWIPLQEGRQLAERNNILDKLLPIFDYVAGDRSPPPAPKHTSAASKPRAPKINKRVVKEDVFSAVNHHRSMGPPSFHHEHYDVNTGLDEDESIEQATLESSSMIADEDMISMSQNGPYSSRKRKRGINEVAAMSLSEQEHILYGDQLLDYFMTVGDAPEATRIPPPQPPANFQVDRPIDDSGNTALHWACAMGDLEIVKDLLRRGADMKALSIHEETPLVRAVLFTNNYEKRTFPALLDLLLDTISFRDWFGATLFHHIAQTTKSKGKWKSSRYYCEVALEKLRTTFSPEEVDLLLSCQDSVGDTAVLVAARNGVFRLVDLLLSRCPRAGDLVNKRGETASSIMQRAHLAERDIPPPPSSITMGNDHIDGEVGAPTSLEPQSVTLHHESSPATAQLLSQIGAIMAEASRKLTSSYGAAKPSQKDSDDVANPEALYEQLEQDRQKIRRQYDALAAKEAAEESSDAQLGRYEQMRDNYESLLEQIQRARLKERLASTPVPTQTAVIGSSSPEQDRLLTTFQLSRALCSEQKIRRAAVKELAQQRADAGVSTKFDVHRKLVALATGLKEEELDPMAAELAETLEFDRMNGKGVGPESPEADHKDSASLPFPGPVVSVDA
Protein: Coiled-coil domain containing 14 (J3QT39)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVRSGARPGQVLSSGRHTGPAKLTNGKKATYLRKIPRFNADSGYSIHSDSESQAETVHGLDGCASLLRDILRNEDSGSETAYLENRSNSRPLESKRYGSKKKRHEKHTIPLVVQKETSSSDNKKQIPNEASARSERDTSDLEQNWSLQDHYRMYSPIIYQALCEHVQTQMSLMNDLTSKNIPNGIPAVPCHAPSHSESQATPHSSYGLCTSTPVWSLQRPPCPPKVHSEVQTDGNSQFASQGKTVSATCTDVLRNSFNTSPGVPCSLPKTDISAIPTLQQLGLVNGILPQQGIHKETDLLKCIQTYLSLFRSHGKETHLDSQTHRSPTQSQPAFLATNEEKCAREQIREATSERKDLNIHVRDTKTVKDVQKAKNVNKTAEKVRIIKYLLGELKALVAEQEDSEIQRLITEMEACISVLPTVSGNTDIQVEIALAMQPLRSENAQLRRQLRILNQQLREQQKTQKPSGAVDCNLELFSLQSLNMSLQNQLEESLKSQELLQSKNEELLKVIENQKDENKKFSSIFKDKDQTILENKQQYDIEITRIKIELEEALVNVKSSQFKLETAEKENQILGITLRQRDAEVTRLRELTRTLQTSMAKLLSDLSVDSARCKPGNNLTKSLLNIHDKQLQHDPAPAHTSIMSYLNKLETNYSFTHSEPLSTIKNEETIEPDKTYENVLSSRGPQNSNTRGMEEASAPGIISALSKQDSDEGSETMALIEDEHNLDNTIYIPFARSTPEKKSPLSKRLSPQPQIRAATTQLVSNSGLAVSGKENKLCTPVICSSSTKEAEDAPEKLSRASDMKDTQLLKKIKEAIGKIPAATKEPEEQTACHGPSGCLSNSLQVKGNTVCDGSVFTSDLMSDWSISSFSTFTSRDEQDFRNGLAALDANIARLQKSLRTGLLEK
Protein: Cd209f protein (Q8CHZ4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
PEFHQSKNHEEEVTSGEQGFAEHDPEGLICSSKSLQGHLTQVPWLLLLLISLGLFLLMLATLVQVSRIRAYSQGQTQDQQGSSSLDKVAVPREQTHSGLEQIQQIQQQLTQFNASLAGLCRPCPWDWELFSRTLGSWETSASSCEDLGAHLVIVNSVSEQSASRLECRVKLCARLRRVGSRESQTFLCAEIHEILECEEKPTLLDRPQ
Protein: Protein shq1 (O43076)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the early biogenesis steps of box H/ACA snoRNP assembly.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit cbf5
- H/ACA ribonucleoprotein complex subunit nop10
- H/ACA ribonucleoprotein complex subunit nhp2
- H/ACA ribonucleoprotein complex subunit gar1
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- tRNA pseudouridine synthase 4
- RuvB-like helicase 1
- RuvB-like helicase 2
- Nucleolar protein 58
- Heat shock protein 90 homolog
Sequence:
MITPKFELRQDEEFVYLDVHTPYIKAKNVEIDAFNNEVNFCIAPYFLKLELPGNVLDDDRANASYDISSGFVHIKFPKETPGEVFPDLDLLTTLLVNQNKEPVKKPLIEEVEDTPSPSTSQNASKDEEKEVKIDWQNIHFDDPDFDWGLLQRLDDEKMQYTSTSQYGFNNQYSGLLKYNALVGNEINQIPEPERTPPSTRSEIRVQLEDEKFDAEHYMADFYDREMIDEILHYIPDYIGEFLLVQQGKSDRLLEFTSEEKEALAKLPKRSYLIDNPKNVYLCLVPLIFAYAYDNRTTLGDPTIESCWNIGTLSSTISCLDTNFLAIKDIFIACIRRSLAYPLYRNWDLALTCWKDTHAILSLGKRWILRVLLRIRNLFEHHDVYYIYNAIVLNDYAYWIQTANDNVLAALAYQVSECTITKEETNWPLEEIEANVQETIIASDEESESIEK
Protein: Signiferin-4.2 (P86134)
Organism: Crinia signifera (Common eastern froglet)
Function: Inhibits the formation of NO by neuronal nitric oxide synthase with an IC(50) of 26.4 uM.
Subcellular location: Secreted {ECO:0000269|PubMed:15317042}.
Interaction partners:
Sequence:
GFADLFGKAVDFIKS
Protein: Cytochrome c oxidase assembly factor, putative electron transport protein SCO1/2, putative (Q4GZ61)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cytochrome oxidase assembly protein, putative
Sequence:
MSLRRHVITRSISVHNRFISSSGEQKTGGSRGGFFSVLRYGPRNRAELFGLCLGCAMCPLSIYLINWCEGCSNRNNNTQPELVLGNETFVTHGVAAPDKGSKYPLGGPFRLRESRTGNYITDKELFQDHWTLLYFGFSKCAEVCPSTLRFITDVMKACDEKLAGDKNLSTEAARLQAVFLSVDSRRDTPEVLEGFVSKYDPRVRGLTGTSKEIEQAARAWRVYYSSIDETDEEKSAREAKGVPMVGADDDTYQLDHSSAIYLVGVDGKLKDFFFKEMGVADAVGRLEVHLQDVYGFKDTRG
Protein: Proline-rich protein 27 (Q6MZM9)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKLLLWACIVCVAFARKRRFPFIGEDDNDDGHPLHPSLNIPYGIRNLPPPLYYRPVNTVPSYPGNTYTDTGLPSYPWILTSPGFPYVYHIRGFPLATQLNVPPLPPRGFPFVPPSRFFSAAAAPAAPPIAAEPAAAAPLTATPVAAEPAAGAPVAAEPAAEAPVGAEPAAEAPVAAEPAAEAPVGVEPAAEEPSPAEPATAKPAAPEPHPSPSLEQANQ
Protein: Pre-mRNA-splicing factor SLU7 (hSlu7) (O95391)
Organism: Homo sapiens (Human)
Function: Required for pre-mRNA splicing as component of the spliceosome. Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:10197984, ECO:0000269|PubMed:15728250, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:30705154}. Nucleus speckle {ECO:0000269|PubMed:15181151}. Cytoplasm {ECO:0000269|PubMed:15728250}. Note=Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. Upon UV-C stress stimulus, the nuclear concentration of the protein decreases, affecting alternative splicing. Translocates from the nucleus to the cytoplasm after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules. {ECO:0000269|PubMed:15728250}.
Interaction partners:
- ATP-dependent RNA helicase DHX8
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-splicing factor 18
- Pre-mRNA-processing factor 17
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Splicing factor 3B subunit 2
- Cell division cycle 5-like protein
- U4/U6 small nuclear ribonucleoprotein Prp3
Sequence:
MSATVVDAVNAAPLSGSKEMSLEEPKKMTREDWRKKKELEEQRKLGNAPAEVDEEGKDINPHIPQYISSVPWYIDPSKRPTLKHQRPQPEKQKQFSSSGEWYKRGVKENSIITKYRKGACENCGAMTHKKKDCFERPRRVGAKFTGTNIAPDEHVQPQLMFDYDGKRDRWNGYNPEEHMKIVEEYAKVDLAKRTLKAQKLQEELASGKLVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDMPGQNFDSKRRITVRNLRIREDIAKYLRNLDPNSAYYDPKTRAMRENPYANAGKNPDEVSYAGDNFVRYTGDTISMAQTQLFAWEAYDKGSEVHLQADPTKLELLYKSFKVKKEDFKEQQKESILEKYGGQEHLDAPPAELLLAQTEDYVEYSRHGTVIKGQERAVACSKYEEDVKIHNHTHIWGSYWKEGRWGYKCCHSFFKYSYCTGEAGKEIVNSEECIINEITGEESVKKPQTLMELHQEKLKEEKKKKKKKKKKHRKSSSDSDDEEKKHEKLKKALNAEEARLLHVKETMQIDERKRPYNSMYETREPTEEEMEAYRMKRQRPDDPMASFLGQ
Protein: Large ribosomal subunit protein bL20 (50S ribosomal protein L20) (P0A7L3)
Organism: Escherichia coli (strain K12)
Function: One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.
Interaction partners:
- Large ribosomal subunit protein uL13
- Elongation factor G
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS10
- Alternative ribosome-rescue factor A
- Large ribosomal subunit protein uL14
- GTP pyrophosphokinase
- Large ribosomal subunit protein bL35
- Large ribosomal subunit protein bL21
Sequence:
MARVKRGVIARARHKKILKQAKGYYGARSRVYRVAFQAVIKAGQYAYRDRRQRKRQFRQLWIARINAAARQNGISYSKFINGLKKASVEIDRKILADIAVFDKVAFTALVEKAKAALA