wanglab/gogpt-training-data huggingface dataset:
Protein: Exostosin-3 (EC 2.4.1.223) (Protein brother of tout-velu) (Q9XZ08)
Organism: Drosophila melanogaster (Fruit fly)
Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. Plays a central role in diffusion of morphogens hedgehog (hh), wingless (wg) and Decapentaplegic (dpp) via its role in heparan sulfate proteoglycans (HSPGs) biosynthesis, HSPGs being required for movement of Hh, Dpp and wg morphogens.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:23720043}; Single-pass type II membrane protein {ECO:0000269|PubMed:23720043}. Note=Localization to the Golgi may be regulated by sau (PubMed:23720043).
Interaction partners:
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Dally-like, isoform A
Sequence:
MPPAYDLGHSGEAYQPLDTGSGGGNEACAPNSSSAQIRHSMGFRTSWMRQFRRYKLPMVLLMLLFLVSCLAYRILSVEQDAPPLDLHRSSPLLDAYEDFSAMRAGDLKMRIEEMVRIKSTVSVELRELESRRQKLQSDISQYNQKIEELKQELLREQTELERLKISVEQAQVAQREAVQRNTPDLALPRSLLPNTLPRKSNPITGGMAASCEMHNCFNHSRCSLTSGFPVYLYDPDEHSVQRKGYDIDGFLKTTLKQTLGYNAHIVKDPKHACIYLVLVGEALLEQDLLRNNRYAAQEAEHQQPSTPTLENDCPVDMEKLYSLPYWGGDGRNHVLLNLARRDLTSHRTNPLYRQNTMRAIVVQSAFEREQFRPGYDLIVPPILGPPGGDVWQECAEMVPARRKYLLTYQGELRPKQSSLNPLDAFILEHLADMAKGATQDQFVLQFQCVPATEQQEGDSLPDWTLCGSDSSRRQLLKDSTFSLILPPLNGRVSSTLMLARIYEALRSGAVPVILGADELRLPYAETVDWRRTALLLPKARITELHFLLRAVQDADLLLLRRQGRLIWERYLSSVQATVDTVIASLRDRLGIPPRPVPSVIAQSVFNSTFIPLKSDPPVGLDTEPEESLGPIEPPYPSPAFRRNYTILRMQAKEAWNDWLDPFYLYPQLPFDPALPSEAKFMGSHTGFRPIGKGLGGAGKEFGESLGGNYPREQFTIVMLTYEREQVLMDSLGRLYGLPYLHKVVVVWNSPKPPLDDLRWPDIGVPVAVLRAPRNSLNNRFLPFDVIETEAVLSVDDDAHLRHDEILFGFRVWREHRDRVVGFPGRYHAWDLGNPNGQWHYNSNYSCELSMVLTGAAFVHKYYLYLYTYHLPQAIRDKVDEYMNCEDIAMNFLVSHITRKPPVKVTSRWTFRCPGCPVSLSEDDTHFQERHKCINFFSRVFGYTPLLNTQYRADSILFKTRIPHDKQKCFKYI
Protein: AT-rich interactive domain-containing protein 1 (ARID domain-containing protein 1) (ARID and ELM2 domain-containing protein 1) (Q84JT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00512}.
Interaction partners:
- Histone deacetylase 8
- Methyltransferase-like protein 2
- DEAD-box ATP-dependent RNA helicase 36
- SNF2 domain-containing protein / helicase domain-containing protein / HNH endonuclease domain-containing protein
- Inactive RHOMBOID-like protein 8
- Plant intracellular Ras-group-related LRR protein 1
- Homeodomain-like superfamily protein
- Transcription factor DUO1
Sequence:
MAGWSMVADEDAVDYSKTPKSLDANRSPESVNPESTGFEKKIKELISLFRPLLDSFLAEFCSADGFLPLPAMTGEGRTVDLFNLFLNVTHKGGFDAVSENGSWDEVVQESGLESYDSASAKLIYVKYLDAFGRWLNRVVAGDTDVSSVELSGISDALVARLNGFLSEVKKKYELRKGRPAKELGAELKWFISKTKRRYDKHHVGKESASNDAVKEFQGSKLAERRLEQIMILESVTQECSSPGKRKRECPLETLKWLSDVAKDPCDPSLGIVPDRSEWVSYGSEEPWKQLLLFRASRTNNDSACEKTWQKVQKMHPCLYDDSAGASYNLRERLSYEDYKRGKTGNGSDIGSSDEEDRPCALVGSKFQAKVPEWTGITPESDSKWLGTRIWPLTKEQTKANLLIERDRIGKGRQDPCGCHNPGSIECVKFHITAKRDKLKLELGPAFYMWCFDVMGECTLQYWTDLELKKIKSLMSSPPSLSPAFIHQAKMILPSKSRGKIVSYFYNVTLLQYRASQSRITPHDIDSDTDQIFLRATENENPAPEANTFQKPALLSPNKKRCR
Protein: Eukaryotic translation initiation factor 2A (eIF-2A) (Q9CAT3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- eIF-2-alpha kinase GCN2
- Eukaryotic translation initiation factor 5B
- Eukaryotic translation initiation factor 5B
- Eukaryotic translation initiation factor 5B
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit B
- DPP6 N-terminal domain-like protein
- D-aminoacyl-tRNA deacylase
- Eukaryotic translation initiation factor 5B
- aspartyl aminopeptidase
Sequence:
MSSSPSLEILVREAEGFTVWNGPPFTNGQPTLKLERVSCSNTKFSVDGSKLMAMKSDGVISIYDATSLTEVRSFTIANVTAAELSPCGTYLQTFQKPTTPQEKNVSIWNTETGDLAHSHYQKSITKASWPSIRFCPDESSACRLATNEVQFFDPKDFSKGITSRIRVPGIAAFELSKTPASHVAVFVPESKGSPGSVQIFGCGEELQSQPSARRSFFRCSSVQFSWNHGSTGLLVVVQSDVDKTNQSYYGETKLHYLTIDGTHEGLVPLRKEGPVHDVQWSFSGSEFAVVYGFMPACVTIFDKNCKPLMELGEGPYNTLRWNPKGRVLCVAGFGNLPGDMAFWDVVNKKQLGSNKAEWSVTSEWSPDGRYFLTASTAPRRQIDNGMKIFNYDGKRYYKKMFERLYQAEWKPESPERFGDISELIKSVESLKLGEGKSQGQGSAQKKTIAPNPIAQKPAAYRPPHAKHAAAVQAELLGISTTGEMSKNALKNKKKRENKKAAAAAAAASGSNNA
Protein: Actin, alpha skeletal muscle (EC 3.6.4.-) (Alpha-actin-1) [Cleaved into: Actin, alpha skeletal muscle, intermediate form] (P68133)
Organism: Homo sapiens (Human)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Vasodilator-stimulated phosphoprotein
- Tropomyosin alpha-3 chain
- Gelsolin
- Troponin C, skeletal muscle
- Cofilin-1
- Tropomyosin alpha-1 chain
- Profilin-1
- Actin-related protein 2
- Plastin-2
- Cofilin-2
Sequence:
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF
Protein: TATA box-binding protein-like 1 (TBP-like factor) (Q07DP5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 1
- TBP-associated factor 3
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor IIB
- IP01149p
- Transcription initiation factor TFIID subunit 4
Sequence:
MGSAVKKGDGSPTRILEEYQVARDLRNEDLFPEHPVEHPDEDSDKENQSPNQSPNPRAIGDCEQGPDIGKDTLNPNEADQFSSEEVEKNEANSSCNESGGDARNSRDRLSSSHSEDEQLNQEYSTSSSGSTIGNREQGSDVGKDTSSRNEADQFSNEEVEKNEANSSGNESYGDACNSSDRLSSSNSEDEQLHQEYSTSSRGRTREYAQSDLNPGYQDLNIGNQDLNQVNREYQESNNEYQVSNQEYQHLNTEYQELNHGDQDSNDEYQELNHGNQDSNDEYQESNHGNQDSNDEYQELNHSNQDSNDEYQELNHGDQDSSDEYQDLNHVNQDSNHEYQAWNHEYQDSNHEYQALNREYQYPESDEEEAARKRNIYTRLRSYACQVHLPRLGESEVDSDDRRHNPINQPFNQPINRPNQKSDSSLESSSPERQDSESESRQASDEESSSGDSDYLIDPVTGWLSRRRETSTEREEKSDQSQQESSEEITDEQKEESDDVEQQSPAEHTSSDRRDHSPDKQQNKRKSLGTGNSSYSKKPLLDGDKGDPRSHLSSLGSRRSLKRKWPFDCTDSKKFKPNLQSEEDKSEEEKREDTESECSDEEDSDSSSFDTDSNSDSDSNLDLDSDSDSHSDFESSSSSEESAQDPAPEGETDQDPAPEGEADQDPAPEGGVDQDPAPEGGVDQDPAPEGEVDQDPAPEGESDQDLAPEGGVDQDPAPEFGTDQDPHPYYNDQDPAPYYDDQDPASYYDDHICDSEEDYKPFIFSKERKFLKFVTNPLGDDKSSLDLSIQLYKVFGAYKLEDVYSSIDEEGQPEQDLQLKQQQKHLKKYQKLQLVVFWHQEKFFSKEQLLLYEYLKLLLQKFFPQEQQEKRLQQEKLLQQEKLLQQEKRLQQEKRLQQEKRLQQEKRLQQEKRLQQQKLLQQQKLLQQEKLLQQQKLLQQEKLLQQEKLLQQEKQLQQEKHLPQERQLQQDKVFLQLRQLQQKKELEEQRERKRHLFEQQKQFVLEKLRQQKEQHRRQQNRVKRERKLRQKKEKQRLEYERFLKEYREDCKRQLRLQREHYLIKIKQLEKASQRSLKGNRKHKLMQNDMVSIPVANLNGGLKAASSGSGVGVVTSGGVVSSAVLANAPRVYLTPSSTFMTNRQMAGVASTGRMSGQVVGGSSGTASTAGTVRYFSQFSKMQTAGGPSLQRKLANGDTIVLATGSKNMFLTSSENKANLPTVASNGNGLITAKMDLLEEEVMQSITVIDDDDEEKKEVAEDEEESSNNAKPIDLHQPIADNEHELDIVINNVVCSFSVGCHLKLREIALQGSNVEYRRENGMVTMKLRHPYTTASIWSSGRITCTGATSESMAKVAARRYARCLGKLGFPTRFLNFRIVNVLGTCSMPWAIKIVNFSERHRENASYEPELHPGVTYKMRDPDPKATLKIFSTGSVTVTAASVNHVESAIQHIYPLVFDFRKQRSAEELQHLRQKQRLQAGGDPHELEKNVLADNKTASLDNIFVNTTAAHSKSSSNDQTSAPATILSSTVDSMPRLKQMVNYHQMMKQTQEERRHIMFNGEKANPASTSSAAAAPSTSSSSSSSGDNICANARRRATECWATKLQNKRPRYNDPGTTGTINAASSTASAATSSLASQATHLRNPLKTAALANARMLGAKVTTCTRNSIIVQQPQRIQMQQQQQQLQPQQQQTSFSPSEFDVDDLIEEEENNELDMPF
Protein: Phosphoglycerate mutase-like protein 1 (Q9FGF0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in carbohydrates metabolism.
Interaction partners:
- Uncharacterized protein At4g15545
- Uncharacterized protein
- Serine carboxypeptidase-like 50
- ACT domain-containing protein ACR11
- Cofactor-independent phosphoglycerate mutase
- Phosphoglycerate mutase-like protein 4
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
- Metal-independent phosphoserine phosphatase
- G-type lectin S-receptor-like serine/threonine-protein kinase At4g27290
- Nucleobase-ascorbate transporter 7
Sequence:
METGAGIGLYPLHRCKTIYLVRHAQGIHNVDGEKNYKAYMSHDYFDAELTQLGWKQVDSLRKHVHSSGLHKKIELVISSPLMRTLQTAVGVFGGEGYTDMSDVLPLMVANAGNSSRAAISSLNCPPVITEESCREHLGVHPCDQRRSISDYQFLFPAVDFSLIESEEDKLWKADVRETIEELAARGKKFLNWLWTRKEKEIAIVTHSGFLFHTLNALQNECHPDVKKEICGHFANCELRSMVIVDRSMLGSDSSVTDYPGKIPKGIDLPSDAVVDDNNIKVE
Protein: POU domain, class 5, transcription factor 3 (A7Y7W2)
Organism: Gallus gallus (Chicken)
Function: Required for the maintenance of pluripotency and self-renewal of embryonic stem cells. Transcriptional activator that binds the DNA consensus sequence 5'-ATGCAAAT-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:25846318}.
Interaction partners:
- Homeobox protein NANOG
- Transcription factor SOX-2
- Homeobox domain-containing protein.
- Deleted in azoospermia-like
- Homeotic protein spalt-major
- RNA helicase
- Protein lin-28 homolog A
Sequence:
MFSPDGGLPAAPFGLLPDGGPPFPRGGYDGAAAQQLFFPFASEPDGARDAATARAWLPPPAGPPAKAEARPARPCRQGSPEPRAAPPATPCCGPAWAAPPWPGPAPPAATAVPGPPFPGPAAAAFPAAPGHALCPAALQPSSGGLANLGSSGSSSGAASEGGHSSDSGDEDAPTSEELEQFAKDLKHKRIMLGFTQADVGLALGTLYGKMFSQTTICRFEALQLSFKNMCKLKPLLQRWLNEAENTDNMQEMCNAEQVLAQARKRKRRTSIETNVKGTLESFFRKCVKPSPQEISQIAEDLNLDKDVVRVWFCNRRQKGKRLLLPFGNESEGVMYDMNQSLVPPGLPIPVTSQGYSLAPSPPVYMPPFHKAEMFPPPLQPGISMNNSSH
Protein: Voltage-gated inwardly rectifying potassium channel KCNH7 (Ether-a-go-go-related gene potassium channel 3) (ERG-3) (Eag-related protein 3) (Ether-a-go-go-related protein 3) (hERG-3) (Potassium voltage-gated channel subfamily H member 7) (Voltage-gated potassium channel subunit Kv11.3) (Q9NS40)
Organism: Homo sapiens (Human)
Function: Pore-forming (alpha) subunit of voltage-gated potassium channel. Channel properties may be modulated by cAMP and subunit assembly.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q12809}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12809}.
Interaction partners:
- Grancalcin
- Interferon-induced helicase C domain-containing protein 1
Sequence:
MPVRRGHVAPQNTFLGTIIRKFEGQNKKFIIANARVQNCAIIYCNDGFCEMTGFSRPDVMQKPCTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEGVAMMFIINFEYVTDNENAATPERVNPILPIKTVNRKFFGFKFPGLRVLTYRKQSLPQEDPDVVVIDSSKHSDDSVAMKHFKSPTKESCSPSEADDTKALIQPSKCSPLVNISGPLDHSSPKRQWDRLYPDMLQSSSQLSHSRSRESLCSIRRASSVHDIEGFGVHPKNIFRDRHASEDNGRNVKGPFNHIKSSLLGSTSDSNLNKYSTINKIPQLTLNFSEVKTEKKNSSPPSSDKTIIAPKVKDRTHNVTEKVTQVLSLGADVLPEYKLQTPRINKFTILHYSPFKAVWDWLILLLVIYTAIFTPYSAAFLLNDREEQKRRECGYSCSPLNVVDLIVDIMFIIDILINFRTTYVNQNEEVVSDPAKIAIHYFKGWFLIDMVAAIPFDLLIFGSGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLMLLMCIFALIAHWLACIWYAIGNVERPYLTDKIGWLDSLGQQIGKRYNDSDSSSGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHMQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWTYTNGIDMNMVLKGFPECLQADICLHLNQTLLQNCKAFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILKDDIVVAILGKNDIFGEMVHLYAKPGKSNADVRALTYCDLHKIQREDLLEVLDMYPEFSDHFLTNLELTFNLRHESAKADLLRSQSMNDSEGDNCKLRRRKLSFESEGEKENSTNDPEDSADTIRHYQSSKRHFEEKKSRSSSFISSIDDEQKPLFSGIVDSSPGIGKASGLDFEETVPTSGRMHIDKRSHSCKDITDMRSWERENAHPQPEDSSPSALQRAAWGISETESDLTYGEVEQRLDLLQEQLNRLESQMTTDIQTILQLLQKQTTVVPPAYSMVTAGSEYQRPIIQLMRTSQPEASIKTDRSFSPSSQCPEFLDLEKSKLKSKESLSSGVHLNTASEDNLTSLLKQDSDLSLELHLRQRKTYVHPIRHPSLPDSSLSTVGIVGLHRHVSDPGLPGK
Protein: Fructosyl amine: oxygen oxidoreductase (EC 1.5.3.-) (Q4WMF9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- N,N-dimethylglycine oxidase, putative
- Glycine cleavage system P protein
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase, cytosolic
- alanine--glyoxylate transaminase
- Alanine racemase
- Threonine aldolase, putative
- FAD dependent oxidoreductase superfamily
- D-amino-acid oxidase
- 5-aminolevulinate synthase
Sequence:
MAVTKSSSLLIVGAGTWGTSTALHLARRGYTNVTVLDPYPVPSAISAGNDVNKVISSGQYSNNKDEIEVNEILAEEAFNGWKNDPLFKPYYHDTGLLMSACSQEGLDRLGVRVRPGEDPNLVELTRPEQFRKLAPEGVLQGDFPGWKGYFARSGAGWAHARNALVAAAREAQRMGVKFVTGTPQGRVVTLIFENNDVKGAVTADGKIWRAERTFLCAGASAGQFLDFKNQLRPTAWTLVHIALKPEERALYKNIPVIFNIERGFFFEPDEERGEIKICDEHPGYTNMVQSADGTMMSIPFEKTQIPKEAETRVRALLKETMPQLADRPFSFARICWCADTANREFLIDRHPQYHSLVLGCGASGRGFKYLPSIGNLIVDAMEGKVPQKIHELIKWNPEIAANRNWRDTLGRFGGPNRVMDFHDVKEWTNVQYRDISKL
Protein: Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3) (P84025)
Organism: Rattus norvegicus (Rat)
Function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P84022}. Nucleus {ECO:0000269|PubMed:8917532}. Note=Cytoplasmic and nuclear in the absence of TGF-beta (By similarity). On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4 (By similarity). Through the action of the phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1 (By similarity). Co-localizes with LEMD3 at the nucleus inner membrane. MAPK-mediated phosphorylation appears to have no effect on nuclear import (By similarity). PDPK1 prevents its nuclear translocation in response to TGF-beta (By similarity). Localized mainly to the nucleus in the early stages of embryo development with expression becoming evident in the cytoplasm of the inner cell mass at the blastocyst stage (By similarity). {ECO:0000250|UniProtKB:P84022, ECO:0000250|UniProtKB:Q8BUN5}.
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 4
- TGF-beta receptor type-1
- E2F transcription factor 4
- Zinc finger FYVE domain-containing protein
- TGF-beta receptor type-2
- Activin receptor type-2A
- Histone lysine acetyltransferase CREBBP
- NEDD4-like E3 ubiquitin protein ligase.
- Activin receptor type-1B
Sequence:
MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS
Protein: Candida glabrata strain CBS138 chromosome H complete sequence (Q6FSH6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- L15
- Candida glabrata strain CBS138 chromosome M complete sequence
- 40S ribosomal protein S4
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- 60S ribosomal protein L28
- Large ribosomal subunit protein eL24
- Small ribosomal subunit protein uS14
- L33
Sequence:
MSDTEAPVEVQEEFEVVEEFTPVTLATPIPEEVQRGSTEIKLFNKWSFEDVEVKDPSLVDYVQIRQPIFVAHTSGRYANKRFRKAQCPIIERLTNSMMMNGRNNGKKLKAVRIIKHTLEIIHILTEQNPLQVVVDAITNTGPREDTTRVGGGGAARRQAVDVSPLRRVNQAIALLTIGAREAAFRNIKTIAETLAEELINAAKGSSTSYAIKKKDELERVAKSNR
Protein: Intramembrane protease 2 (EC 3.4.23.-) (P49049)
Organism: Caenorhabditis elegans
Function: Acts as intramembrane protease (Probable). In larvae, required for the complete shedding of the cuticle during molting, possibly by regulating cholesterol uptake via lrp-1. Involved in embryonic and larval development.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1-interacting protein
- Derlin-1
- Translocon-associated protein subunit gamma
- Endoplasmin homolog
- Translocon-associated protein subunit beta
Sequence:
MAEAATEIPPTASNVTVFTFEEQATSSLALYGMSILCIIIGSIRSAQYIRTNIDKKRLIEGSITMREARKFPISASLVLFGLYLFFKPAAERFLWVARVFQILRVPEEYVQKINSTIISYTANTTTTGPSEPFLLRLASRIPQERVPEAIQNAATYAYTNLPTIQKAECMQLLTFLICFEGVNAFASLLKPFVTAFLKKMPLVPSFLRFNAPYLFSLKKGNKEMEEGDIEDAKKKETEYLFKIDFDRYDIIALLMCSPILISHLLKRHWITNNIIGVSFSILGIERLHLASFKAGSLLLVGLFFYDIFWVFGTDVMTSVAKGIDAPILLQFPQDIYRNGIMEASKHSMLGLGDIVIPGIFIALLRRFDYRVVQTTAESKAPQGSLKGRYYFVVTVVAYMAGLFITMAVMHHFKAAQPALLYLVPCCLFVPLLLAVIRGELSALWNYDESRHVDNEENRKKVDSGKKNN
Protein: Complement C1s subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s) [Cleaved into: Complement C1s subcomponent heavy chain; Complement C1s subcomponent light chain] (Q6P6T1)
Organism: Rattus norvegicus (Rat)
Function: C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4 (By similarity).
Interaction partners:
- Plasma protease C1 inhibitor
- Complement C1r subcomponent
- Complement C4
- Complement C1q subcomponent subunit A
- Complement C1q subcomponent subunit B
- Complement C1q subcomponent subunit C
- Complement C4A
- Complement C2
- Complement C1r subcomponent-like protein
- Complement C4A.
Sequence:
MWCFVFFSLLASFSAEPTMYGEILSPNYPQAYPNEVVKTWDIEVPEGFGIHLYFTHLDMELSENCAYDSVQIISGGIEEERLCGQRTSKSPNSPTVEEFQFPYNRLQVVFTSDFSNEERFTGFAAYYSAVDVNECTDFTDVPCSHFCNNFIGGYFCSCPPEYFLHDDMRTCGVNCSGDVFTALIGEIASPNYPNPYPENSRCEYQIRLQEGFRLVLTIRREDFDVEPADSEGNCHDSLTFAAKNQQFGPYCGNGFPGPLTIKTQSNTLDIVFQTDLTGQNKGWKLRYHGDPIPCPKEISANSIWEPEKAKYVFKDVVKITCVDGFEVVEGNVGSTSFYSTCQSNGQWSNSRLECQPVDCGVPEPIENGKVEDPEDTVFGSVIHYTCEEPYYYMEQEEGGEYHCAANGSWVNDQLGVELPKCIPVCGVPTEPFKVQQRIFGGYSTKIQSFPWQVYFESPRGGGALIDEYWVLTAAHVVEGNSDPVMYVGSTLLKIERLRNAQRLITERVIIHPSWKQEDDLNTRTNFDNDIALVQLKDPVKMGPTVAPICLPETSSDYNPSEGDLGLISGWGRTENRTNVIQLRGAKLPITSLEKCQQVKVENPKARSNDYVFTDNMICAGEKGVDSCEGDSGGAFALPVPNVKDPKFYVAGLVSWGKKCGTYGIYTKVKNYVDWILKTMQENSGPKKD
Protein: Cytochrome b (Q8HCN3)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
- Cytochrome c oxidase subunit 3
- Cytochrome b6-f complex subunit 4
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 1
- Cytochrome b6-f complex subunit 5
- Cytochrome c oxidase subunit 2
- Cytochrome f
- NADH-ubiquinone oxidoreductase chain 1
- Cytochrome c oxidase subunit 2
Sequence:
MTIRNQRFSLLKQPIYSTLNQHLIDYPTPSNLSYWWGFGSLAGICLVIQIVTGVFLAMHYTPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFFIVVYLHIFRGLYYASYSSPREFVWCLGVVIFLLMIVTAFIGYVLPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNATLNRFFSLHYLLPFILVGASLLHLAALHQYGSNNPLGVHSEMDKIAFYPYFYVKDLVGWVAFAIFFSIWIFFAPNVLGHPDNYIPANPMSTPPHIVPEWYFLPIYAILRSIPDKAGGVAAIALVFISLLALPFFKEMYVRSSSFRPIYQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQISSFFFFLFFAITPILGRVGRGIPKYYTDETHRTGSVS
Protein: RNA polymerase-associated transcription-specificity factor RAP94 (Protein H4) (RPO-associated protein of 94 kDa) (P68438)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: DNA-directed RNA polymerase-associated factor required for the transcription of viral early genes as well as for transcription termination. Within minutes after virus entry, recruits the core RNA polymerase, the early transcription factor (ETF) and other enzymes needed for transcription initiation, elongation, and termination thereby allowing synthesis of early mRNAs which are extruded through pores in the core particle. Recruits the multifunctional OPG102 protein, with poly(A) polymerase-stimulatory, cap nucleoside-2'-O-methyltransferase, and transcription elongation activities. Interacts with nucleoside triphosphatase I/OPG123, a DNA-dependent ATPase required for the termination of early transcripts. Acts as a transcription termination factor by binding, together with the capping enzyme/VTF, to the termination motif 5'-UUUUUNU-3' in the nascent mRNA. Involved as well in the packaging of RNA polymerase and other components needed for early transcription in assembling virus particles.
Subcellular location: Virion {ECO:0000305}. Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome.
Interaction partners:
Sequence:
MDSKETILIEIIPKIKAYLLDANISPKSYDDFISRNKNIFVINLYNVSTITEEDIRLLYTTIEQNIDADDQTLVAIFSYIGYKFEQAVKEEISTSLSFNDKNTTDEMTYNLYDLFFNTLDMYLRQKKISILVNDDVRGDVIVSYKNSDLVSSFNAELEPEIKKIPFNMKNLLPYLEKNLDQLRFSKKYLDFAYLCRHIGIPISKKKYNVRYVFLYKIDGLSIPIIIKDFLDVKYVYLENTGKIYKNSFSEDHNNSLSDWGKVIIPLLKDRHLYSYIFLSSYHLHSYYTDLIARDEPVFVKRKKLDIIEIDEPEAWKRDVRVEFAPCEHQIRLKEAMKVDANYFTKINNFANEFIYYEDGVAYCRVCGINIPIFNLDAADVIKNTVIVSTFNKTIFLSEPYSYFVHSQRFIFNIIMSFDNIMKSQTWVMKYNINRLILNFLIDINSRRQEYEKKFSSEIKRGLFFLRLSANLFESQVSSTELFYVSKMLNLNYIVALVIILNSSADFIVSYMTSKNKTVEESTLKYAISVVIYDFLVKTRICEKGSLDTIVLFTDVYTSIMPEELDLHFQRITLELRKLVSIQRSALEPNYDVESRGEELPLSALKFFDTSTIIVKTMAPVHTYIEQKIVAPTPSVEPTDASLKNFKELTCDEDIKILIRVHDTNATKLVIFPSHLKIEIERKKLIIPLKSLYITNTLKYYYSNSYLYVFRFGDPMPFEEELIDHEHVQYKINCYNILRYHLLPDSDVFVYFSNSLNREALEYAFYIFLSKYVNVKQWIDENITRIKELYMINFNN
Protein: Tubulin alpha-3 chain (EC 3.6.5.-) (P09734)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta chain
- Dynein heavy chain, cytoplasmic
- Protein BIM1
- WD repeat-containing protein PAC11
- Kinesin-like protein CIN8
- Tubulin alpha-1 chain
- Chromosome instability protein 1
- Transgelin
- Kinesin-like protein KIP1
- Nuclear fusion protein BIK1
Sequence:
MREVISINVGQAGCQIGNACWELYSLEHGIKEDGHLEDGLSKPKGGEEGFSTFFHETGYGKFVPRAIYVDLEPNVIDEVRTGRFKELFHPEQLINGKEDAANNYARGHYTVGREIVDEVEERIRKMADQCDGLQGFLFTHSLGGGTGSGLGSLLLENLSYEYGKKSKLEFAVYPAPQLSTSVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDICKRNLGISRPSFSNLNGLIAQVISSVTASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYAPILSKKRATHESNSVSEITNACFEPGNQMVKCDPTKGKYMANCLLYRGDVVTRDVQRAVEQVKNKKTVQMVDWCPTGFKIGICYEPPSVIPSSELANVDRAVCMLSNTTAIADAWKRIDQKFDLMYAKRAFVHWYVGEGMEEGEFTEAREDLAALERDYIEVGADSYAEEF
Protein: Uncharacterized protein YDR476C (Q03362)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribonuclease MRP protein subunit SNM1
- Uncharacterized protein YDL211C
Sequence:
MWDSLIVSINDTHKLGLEDCLAVFGHVPITKAVKHVRLTEIDTQTSTFTLKFLHTETGQNIEKIIYFIDNDTGNDTRTATGIKQIFNKMFRIAAEKRKLSLIQIDTVEYPCTLVDLLILVGVALPPLCYLYRPALHAIFFLVPNPVGSTLEAWLDSDLVLRLIIVAEFLTHALETLIFVVPRLKYYRVPGEFVPEWLLLGLLEGYGPARRLDTKARTLGEGSVN