wanglab/gogpt-training-data huggingface dataset:
Protein: TNR protein (A1L306)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MGQTSDHESQVTFTHRINFPKKACPCASSAQVLQELLSRIEMLEREVSVLRDQCNANCCQESAATGQLDYIPHCSGHGNFSFESCGCICNEGWFGKNCSEPYCPLGCSSRGVCVDGQCICDSEYSGDDCSELRCPTDCSSRGLCVDGECVCEEPYTGEDCRELRCPGDCSGKGRCANGTCLCEEGYVGEDCGQRQCLNACSGRGQCEEGLCVCEEGYQGPDCSAVAPPEDLRVAGISDRSIELEWDGPMAVTEYVISYQPTALGGLQLQQRVPGDWSGVTITELEPGLTYNISVYAVISNILSLPITAKVATHLSTPQGLQFKTITETTVEVQWEPFSFSFDGWEISFIPKNNEGGVIAQVPSDVTSFNQTGLKPGEEYIVNVVALKEQARSPPTSASVSTVIDGPTQILVRDVSDTVAFVEWIPPRAKVDFILLKYGLVGGEGGRTTFRLQPPLSQYSVQALRPGSRYEVSVSAVRGTNESDSATTQFTTEIDAPKNLRVGSRTATSLDLEWDNSEAEVQEYKVVYSTLAGEQYHEVLVPRGIGPTTRATLTDLVPGTEYGVGISAVMNSQQSVPATMNARTELDSPRDLMVTASSETSISLIWTKASGPIDHYRITFTPSSGIASEVTVPKDRTSYTLTDLEPGAEYIISVTAERGRQQSLESTVDAFTGFRPISHLHFSHVTSSSVNITWSDPSPPADRLILNYSPRDEEEEMMEVSLDATKRHAVLMGLQPATEYIVNLVAVHGTVTSEPIVGSITTGIDPPKDITISNVTKDSVMVSWSPPVASFDYYRVSYRPTQVGRLDSSVVPNTVTEFTITRLNPATEYEISLNSVRGREESERICTLVHTAMDNPVDLIATNITPTEALLQWKAPVGEVENYVIVLTHFAVAGETILVDGVSEEFRLVDLLPSTHYTATMYATNGPLTSGTISTNFSTLLDPPANLTASEVTRQSALISWQPPRAEIENYVLTYKSTDGSRKELIVDAEDTWIRLEGLLENTDYTVLLQAAQDTTWSSITSTAFTTGGRVFPHPQDCAQHLMNGDTLSGVYPIFLNGELSQKLQVYCDMTTDGGGWIVFQRRQNGQTDFFRKWADYRVGFGNVEDEFWLGLDNIHRITSQGRYELRVDMRDGQEAAFASYDRFSVEDSRNLYKLRIGSYNGTAGDSLSYHQGRPFSTEDRDNDVAVTNCAMSYKGAWWYKNCHRTNLNGKYGESRHSQGINWYHWKGHEFSIPFVEMKMRPYNHRLMAGRKRQSLQF
Protein: Ammonium transporter Amt2 (Q58739)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nitrogen regulatory protein GlnK1
- Nitrogen regulatory protein GlnK2
Sequence:
MWGENIATADLFANATDIHSIVQALTTLANASDVFFLVVMGVLVFMMQWGFAMLEGGQVRKKNVNNVMMKNMVDWLIGCVAWLFIGGILCSKGFDLSAFIDWWKQILGTNWPNNGLDLASWFFGLVFCATAATIVSGGVAERIKFSAYVLISLIITGLLYPLFVYLGPWGASIVPWHDYAGSLVVHGLGGFLALGAIAALGPRIGRFVDGRPVPILGHNIPMAVFGAFALAIGWYGFNVGSSLALGDISGLVCATTTMAMAGGGIGALIASRNDVLFTANGIVAGLVAICSGTDVVSPIGGLIIGLIAGLQVPIVYKLVEKAGLDDVCGVVPVHGTAGVIGAILTGILGLKIFGGAGGVSLIDQIIGAVFCIIYGTGLGYILAKIVGIALGGLRVSEEEEKMGLDMAEHKMPAYPEETVI
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Q69Z13)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPSSEEWKTSTKLEALGSMEGELAHLLSTCKPETLNHNKTELSGFRNLFARFLRAKPTVDWSKIEPLPEGAIRPYKSLGHVVDKELIASQLRKLVVVKLNGGLGTSMGCKGPKSVISVRNDLTFLDLTMQQIQTLNKTYGVDVPLVLMNSFNTNEDTQKVLKKYANVKVSVHTFSQSQYPRINRETLLPIVKSLEADDNECWYPPGHGNFYEAFHNSGLLDKFLADGKEYCFLSNIDNMGATVDLSILNFVLNPSPDQTAPEFLMEVTDKTRADVKGGTLIQYEGRLMLLEIAQVPKDYVDEFKSISKFRIFNTNNLWAKLDAMRKIVVENKLEMEVIVNPKHLDRGLDVIQLETAAGAAIKSFSGAVGVNVPRSRFLPVKKTSDLLLLMSNLYDIDNGSLTLSHQRSFPTTPLVKLGSSFDKVKDYLGRFNGIPDLLELDHLTVSGDVWFGKDVSLKGTVIIIANHGDRIDIPPGSILENKIVSGNLRILEH
Protein: GPI-anchored wall transfer protein 1 (EC 2.3.-.-) (Q873N1)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- N-acetylglucosaminylphosphatidylinositol deacetylase
- GPI mannosyltransferase 1
Sequence:
MDPDYKARKEAFVSGLAGGSILEINAVTLVASVSVFLWSILQSRLSFFTPYSAAALLVDFLLNVLAILFATTLYSSAPLLLNLLLISPALLILLSTKRPRTPVKAKPPRQSARAGKDDSKHATALPESLPIHPFLTTYRAAMMVITCIAILAVDFRIFPRRFAKVENWGTSLMDLGVGSFVFSGGVVSARSLLKSRINGSKRLPLAKRLIASTRHSIPLLVLGLIRLYSVKGLDYAEHVTEYGVHWNFFFTLGLLPPFVEVFDALATIIPSYEVLSVGIAVLYQVALESTDLKSYILVSPRGPSLLSKNREGVFSFSGYLAIFLAGRAIGIRIIPRGTSFSRSPEQARRRVLISLGVQALVWTTLFVLNSTYAMGYGANIPVSRRLANMPYVLWVSAFNTAQLFVFCLIETLCFPAVHRTTTQESESERVDFATSRIMSAFNKNSLAIFLLANLLTGAVNLSISTIDANTAQAIAVLIGYSSIITGVALALHHANIKVLPF
Protein: Sphingosine kinase 2 (M0R344)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPPPPPLAASTPLLHGEFGSYPARGPRFALTLTSQALHIQRLRPKPEARPRGGLVPLAEVSGCCTLRSRSPSDSAAYFCIYTYPRGRRGARRRATRTFRADGAATYEENRAEAQRWATALTCLLRGLPLPGDGEITPDLLPRPPRLLLLVNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDWEEAVKMPVGILPCGSGNALAGAVNQHGGFEPALGLDLLLNCSLLLCRGGGHPLDLLSVTLASGSRCFSFLSVAWGFVSDVDIQSERFRALGSARFTLGTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPMAHSPLHRSVSDLPLPLPQPALASPGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKAALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCGPPDHLLPPLGTPLPPDWVTLEGDFVLMLAISPSHLGADLVAAPHARFDDGLVHLCWVRSGISRAALLRLFLAMERGSHFSLGCPQLGYAAARAFRLEPLTPRGVLTVDGEQVEYGPLQAQMHPGIARGRTQTPALPAAPALYGRQPGAAHGLQPVCQGAALFFHNSWLWGSQDLFRIVLTEAVGG
Protein: Interleukin enhancer-binding factor 3-B (Double-stranded RNA-binding protein 4F.2) (DsRNA-binding protein 4F.2) (Q6DD04)
Organism: Xenopus laevis (African clawed frog)
Function: RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. Plays thereby a role in the back-splicing of a subset of circRNAs. As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response. Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs. Has a cytoplasmic role early in development as part of a ribonucleoprotein (mRNP) complex which may regulate mRNA transport and/or translation. Following nuclear localization at the mid-blastula transition, acts as a transcription factor and binds the 5'-CCAAT-3' promoter sequence to regulate transcription of the gata2 gene as a subunit of the CCAAT box transcription factor (CBTF). Its role as an mRNP component negatively regulates its activity as a transcription factor by precluding its nuclear localization.
Subcellular location: Nucleus {ECO:0000269|PubMed:7922339}. Cytoplasm {ECO:0000250|UniProtKB:Q91550}. Note=Cytoplasmic in fertilized eggs, then translocates to the nucleus prior to gastrulation. RNA-binding is required for cytoplasmic retention during early development, and nuclear translocation at the mid-blastula transition (MBT) is probably coupled to the degradation of maternal mRNA that occurs at that stage (By similarity). {ECO:0000250|UniProtKB:Q91550, ECO:0000269|PubMed:7922339}.
Interaction partners:
Sequence:
MRPMRIFLNDDRHVMAKHSVVYPTQEELEAVQNMVSHTERALKAVSDWIDQQEKDSGIEQENPEPEETETTEEGKDSEAKTGENPTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCRDKPTISLLKRVADNLVLQFETVSEDKYEVVQNIREASIVIKNTKEPPLTLHIRLTSPLVREEVEKLSAGETLTVSDPPDVLDRHKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWEPLRGWPLELLCEKAIGTANRPMGAGEALRRVLECLSSGILMPDGPGLYDPCEKDASDALEHLERQQREDITQSAQHALRLAAFGQLHKVLGMDPLPTKMPKKTKIEIPIIDYTVQIPPSTTYAMPALKRPIEEDGEDKSPSKKKKKIQKKDEKSEPPQAMNALMRLNQLKPGLQYKLISQTGPVHAPIFTMSVEVDDKTFEASGPSKKTAKLHVAVKVLQDMGLPTGIDEKEESVDESEEKPVLQTPSQTADSEQADSSAGDQSESGKQQGPILTRHGKNPVMELNEKRRGLKYELISETGGSHDKRFIMEVEVDGVKFQGNGSNKKVAKAYAALSALEKLFPDYTTYTEAPKKKRPPMMPRGGPKFAGKHNQGFGMMYNEVPPPQVMRGRGRGGMNRGRGRGRGGFGGGNYGGYMNSGGYGGGYGGNNYQTSATAGYSQFYSNGGASGNAGGGGAGSGGYSSYYQGEGYNAPTPPKPFVKKPPPPQQQQQPPPQHASNPPKPSYNQGYQGHQGGQQQQQPQQQQQQTYNQNQYSNYGPPQKQKGGYNQGTQGAASAGSYNYSNSYTGGTACRVRQWRGCRRARRPALTQRQALVTTQGRTPAMVQPAVPHRTKVTHSRTTIKVPPDRTTAALQIITSPLREEQEVMAGIQITT
Protein: Large ribosomal subunit protein eL14 (60S ribosomal protein L14) (P55841)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL21
- 60S ribosomal protein L27
- Small ribosomal subunit protein uS14
- 40S ribosomal protein S27
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein eS7
Sequence:
MPFERFVQTGRIAKASAGPLKGRLVAIVDVIDQNRVLVDGPLTGVPRQEYRLNNLHLTKYRIKFPYTAPTRIVRKAWTESDLKAQWKVSPWSVKAQNICKRSSLNDFDRFKLRYAKRQRNKLLTIAFNTLKKRTKADGTPRVLKKDRRERLRAEKAKGGKKAAAKK
Protein: Nuclear pore complex protein Nup85 (Q5ANL4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567, ECO:0000256|RuleBase:RU365073}.
Interaction partners:
- Nucleoporin
- Nuclear pore protein
- Nucleoporin NSP1
- Uncharacterized protein
- Seh1p
- Uncharacterized protein
- Nuclear pore complex protein
- Protein transport protein SEC13
- Uncharacterized protein
- Nucleoporin
Sequence:
MPEYTNFESKFDDIDMLEIPEDDDGENSIDNSISSETEGISDSSDSSKSSYDQWSPVAIFKSDKEYIDLSDWLNTQKSLEFKFDVQKYRKGIEKSRPFDEKYILYVNNMFKIIQKLTEDDITRFDLEEDDSPIGLVMDSMGSKAKQVRKFKKIDEALREIIDYLQDLVNSIPKEEQESYDSQCLQHVLYILECFEANNFYFDIQQKPELIIKWVNTFDPKPDPELLNDVIVNTPQPYLHPRFWNTCISQLLTRGLFTQIHEVIEHSQYQELKEKCPELYAVIGDMDTLLSNYTSYSSKGQFTAWKLLACEFRDSLSSVRNESITETKHKLIIDQIYDLACIFTGLPKTISSYCDTWYEVYLALSLYQVRDSNEVYIDYFKTAVSEKPPSDIFDDENENLDGLTEACFLNILENNFLKVLETLHELDPPTTAYLAELMELRFLLRGYYFDVTVTSSASFEDLLNRRIVSEYFLTRHAYDCLNIHELVPVGIGLLLNNVVCTSNNAVSANRKVIATFLPNYICNTNDDLEWALTICANLNLVSTARQLYYQAGLKSLEEGYMYEALNNFVNCYDPTLLSGENHSEGMKKVHYIVWDLIFANCLVHNRPIKDELINNIVDKKVDLNFKIHPVIQQCLAPYAVLKEFYETLPQRDIKLSNKLSKLIHLLKFNYLPKKFVPLLLAQFIPFLSEPNTTFQLPDLVIIIELLDNYESDRNEKELKEGADLYLYSINNIESDADENDWRKLVGKDNLPKDIDSFTRLLRNLIAAKVGKVFI
Protein: BRISC complex subunit Abraxas 2 (Abraxas brother protein 1) (Protein FAM175B) (Q3TCJ1)
Organism: Mus musculus (Mouse)
Function: Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (By similarity). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins. Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination. Required for normal induction of p53/TP53 in response to DNA damage. Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q15018}. Nucleus {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15018}. Note=A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K-fibers. Co-localizes with NUMA1 at mitotic spindle poles. {ECO:0000250|UniProtKB:Q15018}.
Interaction partners:
- BRISC and BRCA1-A complex member 1
- Lys-63-specific deubiquitinase BRCC36
- BRISC and BRCA1-A complex member 2
- Serine hydroxymethyltransferase, mitochondrial
- Lys-63-specific deubiquitinase BRCC36-like
- Biorientation of chromosomes in cell division protein 1-like 1
Sequence:
MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSISDSQISNTEFLQVIEIHNHQPCSQLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNTQQQMSYREQVIHKQLTRILGVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLAIPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGTDFFDKDGVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAEVNKLRRQITQKKNEKEQERRLQQALLSRQMPSESLEPAFSPRMSYSGFSAEGRSTLAETEPSDPPPPYSDFHPNNQESTLSHSRMERSVFMPRPQAVGSSSYASTSGGLKFTGSGADLLPSQSAAGDSGEESDDSDYENLIDPAESPHSEYSHSKNSRPSTHPDEDPRNTQTSQI
Protein: SPI-2 type III secretion system translocon protein SseC (Type III secretion system apparatus protein) (A0A0H3NB70)
Organism: Salmonella typhimurium (strain SL1344)
Subcellular location: Host membrane {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004301}.
Interaction partners:
Sequence:
MNRIHSNSDSAAGVTALTHHHLSNVSCVSSGSLGKRQHRVNSTFGDGNAACLLSGKISLQEASNALKQLLDAVPGNHKRPSLPDFLQTNPAVLSMMMTSLILNVFGNNAQSLCQQLERATEVQNALRNKQVKEYQEQIQKAIEQEDKARKAGIFGAIFDWITGIFETVIGALKVVEGFLSGNPAEMASGVAYMAAGCAGMVKAGAETAMMCGADHDTCQAIIDVTSKIQFGCEAVALALDVFQIGRAFMATRGLSGAAAKVLDSGFGEEVVERMVGAGEAEIEELAEKFGEEVSESFSKQFEPLEREMAMANEMAEEAAEFSRNVENNMTRSAGKSFTKEGVKAMAKEAAKEALEKCVQEGGKFLLKKFRNKVLFNMFKKILYALLRDCSFKGLQAIRCATEGASQMNTGMVNTEKAKIEKKIEQLITQQRFLDFIMQQTENQKKIEQKRLEELYKGSGAALRDVLDTIDHYSSVQARIAGYRA
Protein: D-galactosamine-6-phosphate deaminase AgaS (GalN-6-P deaminase) (EC 3.5.99.-) (Glucosamine-6-phosphate deaminase) (GlcN-6-P deaminase) (EC 3.5.99.6) (A0KYQ7)
Organism: Shewanella sp. (strain ANA-3)
Function: Involved in the pathway of N-acetyl-D-galactosamine degradation. Catalyzes the conversion of D-galactosamine 6-phosphate (GalN-6-P) to D-tagatofuranose 6-phosphate (Tag-6-P). It can also catalyze the conversion of D-glucosamine 6-phosphate.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:22711537}.
Interaction partners:
- Tagatose-bisphosphate aldolase noncatalytic subunit
- N-acetylgalactosamine-6-phosphate deacetylase
- Transcriptional regulator, DeoR family
- Glycosyl hydrolase family 109 protein 2
- N-acetylgalactosamine kinase AgaK
- N-acetylgalactosamine-6-phosphate deacetylase
Sequence:
MLTSPLSPFEHEDSNLLLSAEQLTQYGAFWTAKEISQQPKMWRKVSEQHSDNRTIAAWLTPILAKPQLRIILTGAGTSAYIGDVLAAHIQQHLPLATQQVEAISTTDIVSHPELYLRGNIPTLLISYGRSGNSPESMAAVELAEQLVDDCYHLAITCNGQGKLANYCADKSHCYLYKLPDETHDVSFAMTSSFTCMYLATLLIFAPNSQALMQCIEMAEHILTERLADIRLQSEQPSKRVVFLGGGPLKAIAQEAALKYLELTAGQVVSAFESPLGFRHGPKSLVDSHTQVLVMMSSDPYTRQYDNDLIQELKRDNQALSVLTLSEELLTGSSGLNEVWLGLPFILWCQILAIYKAIQLKVSPDNPCPTGQVNRVVQGVNVYPFVK
Protein: Reversion-inducing cysteine-rich protein with Kazal motifs (mRECK) (Q9Z0J1)
Organism: Mus musculus (Mouse)
Function: Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation. Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7 (By similarity). ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex (By similarity). Also acts as a serine protease inhibitor: negatively regulates matrix metalloproteinase-9 (MMP9) by suppressing MMP9 secretion and by direct inhibition of its enzymatic activity. Also inhibits metalloproteinase activity of MMP2 and MMP14 (MT1-MMP).
Subcellular location: Cell membrane {ECO:0000269|PubMed:28803732}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O95980}.
Interaction partners:
- Adhesion G protein-coupled receptor A2
- Catenin beta-1
- Programmed cell death protein 4
- Matrix metalloproteinase-14
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 3
- Protein Wnt-3a
- Low-density lipoprotein receptor-related protein 6
- Glycogen synthase kinase-3 beta
- Segment polarity protein dishevelled homolog DVL-1
Sequence:
MASVRASPRSALLLLLAAAGVAEVTGGLAPGSAGAVCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWSCMNSSLPGVFKKSDGWVGLGCCELAIGLECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREFCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRICEYNPVEVSMLTCLADVREPCQLGCTNLTYCTNFNNRPTELFRSCTAQSDQGAMSDMKLWEKGSIKMPFISIPVLDIKTCQPEMWKAVACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEEHTAESICEFLSPADDLESCIPLDTYLRPSALGNIIEEVTHPCNPNPCPANELCEVNRKGCPSADPCLPYSCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFTIDCNVCSCFAGNLVCSTRLCLSEHSSDDDRRTFTGLPCNCADQFVPVCAQNGRTYPSACIARCVGLQDHQFEFGPCISKNPCNPNLCPKSQRCVPKPQVCLTTFDKFGCSQYECVPRQLTCDQARDPVCDTDHMEHSNLCTLYQRGKSLSYRGPCQPFCRAKEPVCGHNGETYSSVCAAYSDRVAVDYYGPCQAVGVLSEYSAVAECAAVKCPSLSAIGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTSKKPITVVEILQKVRMHVSVPQCDVFGYLSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSLPSSAVVGRPLFHSLLLLLSLGLTVHLLWTRP
Protein: Transposon Ty2-GR2 Gag-Pol polyprotein (TY2A-TY2B) (Transposon Ty2 TYA-TYB polyprotein) [Cleaved into: Capsid protein (CA); Ty2 protease (PR) (EC 3.4.23.-); Integrase (IN); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)] (P0CX64)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty2 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLHQNPHSLHGSAYASVTSKEVPSNQDPLAVSASNLPEFDRDSTKVNSQQETTPGTSAVPENHHHVSPQPASVPPPQNGQYQQHGMMTPNKAMASNWAHYQQPSMMTCSHYQTSPAYYQPDPHYPLPQYIPPLSTSSPDPIDSQNQHSEVPQAETKVRNNVLPPHTLTSEENFSTWVKFYIRFLKNSNLGDIIPNDQGEIKSQMTYEEHAYIYNTFQAFAPFHLLPTWVKQILEINYADILTVLCKSVSKMQTNNQELKDWIALANLEYDGSTSADTFEITVSTIIQRLKENNINVSDRLACQLILKGLSGDFKYLRNQYRTKTNMKLSQLFAEIQLIYDENKIMNLNKPSQYKQHSEYKNVSRTSPNTTNTKVTTRNYHRTNSSKPRAAKAHNIATSSKFSRVNNDHINESTVSSQYLSDDNELSLGQQQKESKPTHTIDSNDELPDHLLIDSGASQTLVRSAHYLHHATPNSEINIVDAQKQDIPINAIGNLHFNFQNGTKTSIKALHTPNIAYDLLSLSELANQNITACFTRNTLERSDGTVLAPIVKHGDFYWLSKKYLIPSHISKLTINNVNKSKSVNKYPYPLIHRMLGHANFRSIQKSLKKNAVTYLKESDIEWSNASTYQCPDCLIGKSTKHRHVKGSRLKYQESYEPFQYLHTDIFGPVHHLPKSAPSYFISFTDEKTRFQWVYPLHDRREESILNVFTSILAFIKNQFNARVLVIQMDRGSEYTNKTLHKFFTNRGITACYTTTADSRAHGVAERLNRTLLNDCRTLLHCSGLPNHLWFSAVEFSTIIRNSLVSPKNDKSARQHAGLAGLDITTILPFGQPVIVNNHNPDSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQDKQSKLDQFNYDTLTFDDDLNRLTAHNQSFIEQNETEQSYDQNTESDHDYQSEIEINSDPLVNDFSSQSINPLQLDKEPVQKVRAPKEVDADISEYNILPSTIRSRTPHIINKESTEMGGTVESDTTSPRHSSTFTARNQNRPGSTNEMIDLTSQDRVNYGLENIKTTRLGGTEEPYIQRNSDTNIKYRTTNSTPSIDDRSSNSESTTPIISIETKAVCDNTPSIDTDPPEYRSSDHATPNIMPDKSSKNVTADSILDDLPLPDLTHKSPTDTSDVSKDIPHIHSRQTNSSLGGMDDSNVLTTTKSKKRSLEDNETEIEVSRDTWNNKNMRSLEPPRSKKRINLIAAIKGVKSIKPVRTTLRYDEAITYNKDNKEKDRYVEAYHKEISQLLKMNTWDTNKYYDRNDIDPKKVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSDMQSNTVHHYALMTSLSIALDNDYYITQLDISSAYLYADIKEELYIRPPPHLGLNDKLLRLRKSLYGLKQSGANWYETIKSYLINCCDMQEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRSKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGHYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Sporulation-specific protein 13 (C6Y4C9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in sporulation. Plays a significant role in modification of the spindle pole body prior to spore formation and is required for initiating forespore membrane formation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:18367542}.
Interaction partners:
- Sporulation-specific protein 2
- Sporulation-specific protein 15
- GTP-binding protein ypt2
- Syntaxin-like protein psy1
- Sporulation-specific protein 3
- Rab guanine nucleotide exchange factor sec2
- Sec14 cytosolic factor
- Serine/threonine-protein kinase ppk35
- Membrane glycoprotein spo14
- Monopolar attachment protein 1
Sequence:
MMSNSQISKLFSSISNKENSNENALKESTNKQLNNANTLAITHLKEQLSREVQRREELEGLLEQSQKEMEDLSVSLFTEANEMVAKARQDTEVLKRELDYLRAKEKGRIGKLRSIQTAVRTSIEARKLLSYSNESNYH
Protein: Receptor activity-modifying protein 2 (Calcitonin-receptor-like receptor activity-modifying protein 2) (CRLR activity-modifying protein 2) (O60895)
Organism: Homo sapiens (Human)
Function: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL.
Subcellular location: Cell membrane {ECO:0000269|PubMed:32296767}; Single-pass type I membrane protein {ECO:0000269|PubMed:32296767}.
Interaction partners:
- Calcitonin gene-related peptide type 1 receptor
- Calcitonin receptor
- Pro-adrenomedullin
- Calcitonin
- Islet amyloid polypeptide
- Receptor activity-modifying protein 3
- Calcitonin gene-related peptide 2
- Guanine nucleotide-binding protein G
- Receptor activity-modifying protein 1
- Vasoactive intestinal polypeptide receptor 1
Sequence:
MASLRVERAGGPRLPRTRVGRPAALRLLLLLGAVLNPHEALAQPLPTTGTPGSEGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAELFDLGFPNPLAERIIFETHQIHFANCSLVQPTFSDPPEDVLLAMIIAPICLIPFLITLVVWRSKDSEAQA
Protein: DNA polymerase II small subunit (Pol II) (EC 2.7.7.7) (DP1) (Exodeoxyribonuclease small subunit) (EC 3.1.11.1) (P81412)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase.
Interaction partners:
- DNA polymerase sliding clamp
- DNA polymerase
- DNA polymerase II large subunit
- DNA primase large subunit PriL
- DNA primase small subunit PriS
- Flap endonuclease 1
- ORC1-type DNA replication protein
- DNA ligase
- Replication factor C small subunit
- Single-stranded-DNA-specific exonuclease RecJ
Sequence:
MDEFVKSLLKANYLITPSAYYLLREYYEKGEFSIVELVKFARSRESYIITDALATEFLKVKGLEPILPVETKGGFVSTGESQKEQSYEESFGTKEEISQEIKEGESFISTGSEPLEEELNSIGIEEIGANEELVSNGNDNGGEAIVFDKYGYPMVYAPEEIEVEEKEYSKYEDLTIPMNPDFNYVEIKEDYDVVFDVRNVKLKPPKVKNGNGKEGEIIVEAYASLFRSRLKKLRKILRENPELDNVVDIGKLKYVKEDETVTIIGLVNSKREVNKGLIFEIEDLTGKVKVFLPKDSEDYREAFKVLPDAVVAFKGVYSKRGILYANKFYLPDVPLYRRQKPPLEEKVYAILISDIHVGSKEFCENAFIKFLEWLNGNVETKEEEEIVSRVKYLIIAGDVVDGVGVYPGQYADLTIPDIFDQYEALANLLSHVPKHITMFIAPGNHDAARQAIPQPEFYKEYAKPIYKLKNAVIISNPAVIRLHGRDFLIAHGRGIEDVVGSVPGLTHHKPGLPMVELLKMRHVAPMFGGKVPIAPDPEDLLVIEEVPDVVHMGHVHVYDAVVYRGVQLVNSATWQAQTEFQKMVNIVPTPAKVPVVDIDTAKVVKVLDFSGWC