wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10) (Q14694)
Organism: Homo sapiens (Human)
Function: Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Deubiquitinates TBX21 leading to its stabilization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:37582970}. Nucleus {ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:24845384}. Early endosome {ECO:0000269|PubMed:19398555}. Note=Cytoplasmic in normal conditions (PubMed:20096447). After DNA damage, translocates to the nucleus following phosphorylation by ATM (PubMed:20096447). {ECO:0000269|PubMed:20096447}.
Interaction partners:
- Ras GTPase-activating protein-binding protein 1
- Ras GTPase-activating protein-binding protein 2
- Cystic fibrosis transmembrane conductance regulator
- Cellular tumor antigen p53
- SH3 domain-binding protein 5
- Caprin-1
- Ubiquitin carboxyl-terminal hydrolase 13
- Sorting nexin-3
- Polyubiquitin-C
- Polyadenylate-binding protein 1
Sequence:
MALHSPQYIFGDFSPDEFNQFFVTPRSSVELPPYSGTVLCGTQAVDKLPDGQEYQRIEFGVDEVIEPSDTLPRTPSYSISSTLNPQAPEFILGCTASKITPDGITKEASYGSIDCQYPGSALALDGSSNVEAEVLENDGVSGGLGQRERKKKKKRPPGYYSYLKDGGDDSISTEALVNGHANSAVPNSVSAEDAEFMGDMPPSVTPRTCNSPQNSTDSVSDIVPDSPFPGALGSDTRTAGQPEGGPGADFGQSCFPAEAGRDTLSRTAGAQPCVGTDTTENLGVANGQILESSGEGTATNGVELHTTESIDLDPTKPESASPPADGTGSASGTLPVSQPKSWASLFHDSKPSSSSPVAYVETKYSPPAISPLVSEKQVEVKEGLVPVSEDPVAIKIAELLENVTLIHKPVSLQPRGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPVPPKPRQALGDKIVRDIRPGAAFEPTYIYRLLTVNKSSLSEKGRQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEKLTISNGPKNHSVNEEEQEEQGEGSEDEWEQVGPRNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSSKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQGYTTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELLSPGVKNKNFKCHRTYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKPTAERTAYLLYYRRVDLL
Protein: Retinol-binding protein 1 (Cellular retinol-binding protein) (CRBP) (Cellular retinol-binding protein I) (CRBP-I) (mCRBPI) (Q00915)
Organism: Mus musculus (Mouse)
Function: Cytoplasmic retinol-binding protein. Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10487743}. Lipid droplet {ECO:0000269|PubMed:15632377}.
Interaction partners:
- Lecithin retinol acyltransferase
- Receptor for retinol uptake STRA6
- Retinol-binding protein 4
- Transthyretin
Sequence:
MPVDFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRAEGVICKQVFKKVH
Protein: Neuroendocrine protein 7B2 (Secretogranin V) (Secretogranin-5) (Secretory granule endocrine protein I) [Cleaved into: N-terminal peptide; C-terminal peptide] (P12961)
Organism: Mus musculus (Mouse)
Function: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01165}. Note=Neuroendocrine and endocrine secretory granules. {ECO:0000250|UniProtKB:P01165}.
Interaction partners:
- Neuroendocrine convertase 2
- Secretogranin-1
- Secretogranin-3
- Secretogranin-2
- Rho GTPase-activating protein 11A
- ProSAAS
Sequence:
MASRLVSAMLSGLLFWLMFEWNPAFAYSPRTPDRVSETDIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPLGKTADDGCLENAPDTAEFSREFQLDQHLFDPEHDYPGLGKWNKKLLYEKMKGGQRRKRRSVNPYLQGKRLDNVVAKKSVPHFSEEEKEAE
Protein: Uncharacterized protein (Q8NLC5)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- Nitroreductase
- Permeases of the major facilitator superfamily
- Uncharacterized protein
- NYN domain-containing protein
Sequence:
MNRTLRTLGWLAAVIQEDPEPWFTTDPDTDYVPYVNSFSFESLSLVPDALMLLKRSLHLAMEQQDLPVKDLQEALRHVLVFKFHFREEWELELAWDSERTKSAVRIIESTKESLADQYRDYKYAFLPELIFQESRGIFDFELEGYTLKVGQSTLSIPWDMIANGYVPASLRNFGELMDRDTGDLDADPILRPRELKFEIHNCPDLNPWIMRETFDFMMEIATETGWFHALNPAYNSVYTYDLISRMPDFLVEGSFRPHSVKRSWEKIQKIAKAVESYASHDYCMSTLTHDYRAIELSLTPTKTEEPST
Protein: ALK tyrosine kinase receptor homolog scd-2 (EC 2.7.10.1) (Suppressor of constitutive dauer formation protein 2) (O76411)
Organism: Caenorhabditis elegans
Function: Probable tyrosine-protein kinase receptor which regulates the dauer/non-dauer developmental decision probably by controlling daf-3 transcriptional activity in parallel or together with the TGF-beta pathway. Regulates integration of conflicting sensory cues in AIA interneurons. May act as a receptor for hen-1. In AWA neurons, together with hen-1, plays a role in regulating olfactory adaptation by controlling the forgetting sensory responses to odorants such as diacetyl.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- HEN-1
- F-box/SPRY domain-containing protein 1
- Suppressor of Constitutive Dauer formation
- MAM domain-containing protein
- Mitogen-activated protein kinase sma-5
- Dwarfin sma.
- Heat shock protein 90
Sequence:
MRKRRLWWFVVLFRVTLVGAILPNETFDVRRYYADRFLIEDEENGSSRSYYISAESKAKAAEQFALLAPNCSLTSDIQENTCNETSSFCDHRVDSTYKTYHYEQEKCNCFIETCDEETNSTELMVLYPDCYCGKREKHCDLSKEKCHWTPDSDHDDLKFEVFESSNKVLFDYMLQAGSEKANLKMNKVSMVSKFFRQSGFNCSLRFMHHFTHQSSTSRLVVRSILQSGEKKNLYEHWLKPASVFWVPVQVAIGSYAEPFKISIDCETGFPPKKKKNKPFTCSIADIYFENCGEIRDPIEQCSRGDQFLCSISANTRCLQNAQCDSRIDCDDESDEMDCGNINGTMCDFNGQDYCNSWYQVTNVTDYHERLSEPTTVAPLNKLNEVPLHLFRLQSPSAKIKEAMRGSGNMLVFDHKPNPLTRRTSALVSPELPRTNPEAYDEKSPLFKSCKLRFYLCSRTYSKVWQISVISKGINPMESGRTIIYEAGYTLIPKENCTWERVFVNIPRQNAGFRIGIFVTNYFPGSEEYVAIDNLSFSPTCFERDINQSTWDIPDLFINTCGASGFEQPQNCDHNRELDGQTGHFLKEDGTQQWTVPVTGFYRMEICGAGGGSNSKASGDTGDCVTLQVHLIENLSLRMLIGQMGESPCFTEHDDELRPSSCSKISHNYVYDGKRGAAGGGATLLTVEKDLWNVVAGGGAGASWDGFDMEVGYGASAIHVKPDQRCNETCKAVSHTDFIVERRDNRCPGEKGESTVFGGFGGGGNSCGMLGGSGAGYQAGNPFGKSRARSGSSNVSIDFSKSPIYYQSERLDEGYIKIAFCRKRCEPPTVCRFRKDYFEEEYCGCPDGSNVTDTEEACAFPLVCPSSSTNQYRNFTYEPFCLCNNGKEIYDVYNDTCEEIQIWTLYNITFLIFAALTIIGALFVVYHYRNREKQMKQEILDLTQMKSPDYLYDDIYFGRTTRKAALDSLPSISRDSIERGRVLGRGNFGEVYYGEYSGVKLAVKMISRTFSASQASQSDFCNEALCMGTFVDENVVRLIGIDFEKVPYMIALEYMEGGDLLSFVKECRPNQVSLNPFQLAMSDLIKICCDVAAGCKCLETFGYVHRDIAARNILLTTRGPQRVAKIADFGMAKEITYGTEYYRINGRTMMPIKWTPPEAFIDGVFTTKSDIWSFGVLCWEVFSLGVVPYPNRRNEEVMLMLTEGARLEYPYGIPTRVYQLMRDCWKTAAADRPKFVDVVEIFQDIQDDPASVGMPFPIHPAVRATFAHSQSTPVSVETPMTAMTEISLNSTFTDASTVKVSAQQDMQDRIQLHELMLTREHPYTSELTSYVVNSIRKDLARVQYENGLTSVPQPEYLSPENNDESVQLIPQSNTVTDQTPPTSLIDLNRLGVQNTGPTLHRPDSLNFNDPYSSVPLLECQTR
Protein: Sporulation protein 24 (Q3E752)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for efficient sporulation.
Subcellular location: Prospore membrane {ECO:0000269|PubMed:25127041}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Autophagy-related protein 41
- ERMES regulator 1
Sequence:
MVAFLELTSDVSQPFVIPSLSPVSQPSSRKNSDANVDDLNLAIANAALLDASASSRSHSRKNSLSLL
Protein: Estrogen receptor beta (Nuclear receptor subfamily 3 group A member 2) (G3V5S2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASSLSLSWRLFMLREASCHGVRQTPGGAHVSVSRSRSFEACQQPRE
Protein: Lysine histidine transporter-like 8 (Amino acid transporter-like protein 1) (Q9SX98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Amino acid transporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15308754}; Multi-pass membrane protein {ECO:0000269|PubMed:15308754}.
Interaction partners:
- Phosphatidylinositol 3-and 4-kinase family protein
- Ankyrin repeat family protein
- Putative cysteine-rich repeat secretory protein 24
- Nucleic acid-binding, OB-fold-like protein
- dCTP pyrophosphatase 1
- Probable xyloglucan glycosyltransferase 12
Sequence:
MDERPETELISIPATPRVSTPEILTPSGQRSPRPATKPSSATWTPTSFISPRFLSPIGTPMKRVLVNMKGYLEEVGHLTKLNPQDAWLPITESRNGNAHYAAFHNLNAGVGFQALVLPVAFAFLGWSWGILSLTIAYCWQLYTLWILVQLHEAVPGKRYNRYVELAQAAFGERLGVWLALFPTVYLSAGTATALILIGGETMKLFFQIVCGPLCTSNPLTTVEWYLVFTSLCIVLSQLPNLNSIAGLSLIGAVTAITYSTMVWVLSVSQPRPATISYEPLSMPSTSGSLFAVLNALGIIAFAFRGHNLVLEIQSTMPSTFKHPAHVPMWRGAKISYFLIALCIFPISIGGFWAYGNLMPSGGMLAALYAFHIHDIPRGLLATAFLLVVFSCLSSFQIYSMPAFDSFEAGYTSRTNKPCSIWVRSGFRVFFGFVSFFIGVALPFLSSLAGLLGGLTLPVTFAYPCFMWVLIKKPAKYSFNWYFHWGLGWLGVAFSLAFSIGGIWSMVTNGLKLKFFKPPN
Protein: F3H9.20 protein (Integral membrane family protein) (Q9FZ88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g22850/F29G20_19
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- RING-type E3 ubiquitin transferase
- Nuclear envelope-associated protein 2
- Phosphoglycolate phosphatase
- Calcineurin-like metallo-phosphoesterase superfamily protein
- E3 ubiquitin-protein ligase JMJ24
- Eukaryotic aspartyl protease family protein
- Eukaryotic LigT
- Uncharacterized protein
Sequence:
MASRLLSTTTLVTPPAYFNKSPAFLTARVGVRRGRANVKAVSNSSQGAVDGTVYKGVYGPWTIDQADVKEVILYRSGLVTAAASFVAASSAAFLPGDSWLSETIKQNHDLFYFVGASGLGLSLFLIHIYVTEIKRTLQALWALGFVGSFATYAALARPAGDNLVHYVVDHPSAVWFVGPLFASLTGLVFKEGLCYGKLEAGLLTFIIPSVLLGHLSGLMNDEVKLVLLGTWMALFLVFAGRKFTQPIKDDIGDKSVFTFMSLSDDEKKAIVEKLEQEKLG
Protein: DNA gyrase subunit B, mitochondrial (EC 5.6.2.2) (Q94BZ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15136745}.
Interaction partners:
- DNA gyrase subunit A, chloroplastic/mitochondrial
- DExH-box ATP-dependent RNA helicase DExH6
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- F3F19.21 protein family protein)
- ATP-dependent DNA helicase Q-like SIM
- Mannosylglycoprotein endo-beta-mannosidase
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH2
- U-box domain-containing protein 7
- SUMO-conjugating enzyme SCE1
- DNA repair protein RadA-like protein
Sequence:
MALLQRASYLRLYYLRLMGSRPRLFSSSLSPALHRHSSTLSSPPFSSPSPSFRLKFQLTSVLSQRLIQRNAISSRFLSTEASQETTTSKGYSSEQIQVLEGLDPVRKRPGMYIGSTGSRGLHHLVYEILDNAIDEAQAGYASKVDVVLHADGSVSVVDNGRGIPTDLHPATKKSSLETVLTVLHAGGKFGGTSSGYSVSGGLHGVGLSVVNALSEALEVSVWRDGMEHKQNYSRGKPITTLTCRVLPLESKGTKGTSIRFWPDKEVFTTAIEFDHNTIAGRIRELAFLNPKVTISLKKEDDDPEKTQYSEYSFAGGLTEYVSWLNTDKNPIHDVLGFRREINGATVDVALQWCSDAYSDTMLGYANSIRTIDGGTHIEGVKASLTRTLNTLAKKSKTVKEKDISLSGEHVREGLTCIVSVKVPNPEFEGQTKTRLGNPEVRKIVDQSVQEYLTEFLELHPDILESIISKSLNAYKAALAAKRARELVRSKSVLKSSSLPGKLADCSSTDPEVSEIFIVEGDSAGGSAKQGRDRRFQAILPLRGKILNIERKDEAAMYKNEEIQNLILGLGLGVKGEDFKKENLRYHKIIILTDADVDGAHIRTLLLTFFFRYQRALFDAGCIYVGVPPLFKVERGKNAQYCYDDADLKKITSNFPANASYNIQRFKGLGEMMPEQLWETTMNPETRILKQLVVDDIAEANMTFSSLMGARVDVRKELIKNAATRINLQRLDI
Protein: Calcium uniporter protein, mitochondrial (CeMCU) (W2SDE2)
Organism: Cyphellophora europaea (strain CBS 101466) (Phialophora europaea)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:29995857}; Multi-pass membrane protein {ECO:0000269|PubMed:29995857}.
Interaction partners:
- FYVE-type domain-containing protein
- Prohibitin
Sequence:
MTKGKLLTTPSRLLKLVLPLSTVDHNTDRKDVAPLALLVHPQQPLSYLERLIQAELPPPDPQDSKSTTRSVTFRAMEAKDDEIKPRKKADTEGGGGSDGSVQSYSGAGREGEGKDEGEFVRWSPSTEIGDFIRDAARAKEFEVEIEGSPGVIKVAVPSFNDRTYYLRQRLRRTSRKISKLAAIKEECDKAAHRGAQRIALAGCGGLIGYWYIVYRLTFETDLGWDVMEPVTYLVGLSTLIGGYMWFLWHNREVSYRSALNITVSARQNKLYQAKGFSLQDWEGYLEEANAMRREIKAVASEYDVDWNETQDEGGDEKVTKALRDERKNNNGTKNKSKEGEEDDEDD
Protein: Alpha-longipinene synthase (EC 4.2.3.80) (Terpene synthase TPS-Lonp) (PsTPS-Lonp) (C0PPM5)
Organism: Picea sitchensis (Sitka spruce) (Pinus sitchensis)
Function: Terpene synthase (TPS) involved in the biosynthesis of sesquiterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to alpha-longipinene.
Interaction partners:
Sequence:
MAQISKCSSLSTELNESSIISHHHGNLWDDDFIQSLKSSNGAPQYHERAEKLVEEIKNLVVSEMKDCNDDLIRHLQMVDIFECLGIDRHFQNEIQVALDYVYRYWNELEGIGIGSRDSLIKDFNATALGFRALRLHRYNVSSDVLENFKNENGQFFCSSTVEEKEVRCMLTLFRASEISFPGEKVMDEAKAFTTEYLTKVLTGVDVTDVDQSLLREVKYALEFPWHCSLPRWEARNFIEICGQNDSWLKSIMNKRVLELAKLDFNILQCAHHRELQLLSRCWWSQSDIAQQNFYRKRHVEFYFWVVIGTFEPEFSTCRITFAKIATLMTILDDLYDTHGTLEQLKIFTEGVKRWDLSLVDSLPDYIKITFEFFLNTSNELIAEVAKTQERDMSAYIRKTWERYLEAYMQEAEWITAGHVPTFDEYMKNGISSSGMCILNLYSLLLMGQLLPDDVLEQIHSPSKIHELVELTARLVDDSKDFETNKVGGELASGIECYVKDNPECTLEDASNHLNGLLDLTVKELNWEFVRHDSVALCFKKFAFNVARGLRLIYKYRDGFDVSNQEMKTHIFKILIDPLT
Protein: Transcriptional regulator (A0A1D8PCC3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
- Histone deacetylase
- Chromatin modification-related protein EAF3
- Transcriptional regulatory protein SDS3
- histone deacetylase
- PHD-type domain-containing protein
- Zinc finger PHD-type domain-containing protein
- Serine/threonine-protein kinase TOR
- DNA-binding transcriptional regulator
- Transcriptional regulatory protein UME6
- Transcriptional regulatory protein RXT2 N-terminal domain-containing protein
Sequence:
MSNHQEPWNNQQRPLGQPFNRQHPPVLPPPATLEQGGQAFYPLPSLPSLGNGSGHHPHGFNIPSINPASDQIQMGQSPSDQSRQTAELRRPSNVALNPPQTTNSTHLPPPSSLGHVGNEQGAYPPTISQPAPQASPVIGGVPNRSTTTNVYRPLNVKDALSYLDQVKVQFSNQAEVYNNFLDIMKDFKSQSIDTPGVIDRVSTLFRGHPNLIQGFNTFLPPGYKIECSLDPSDPNPIRVTTPTGTTTRPNLSSATYNQRWGGEESSTINQQEQSSPQSQSAQQAQQFADQASMEAQNGASGQVGFNHAISYVNKIKTRFASQPDIYKQFLEILQTYQREQKQIAEVYEQVTVLFANSPDLLDDFKQFLPDTSNLNYQQTPAQDGYYVNNGTQLPPVGNFQPAGQATNQQYAQLQQTAAQQQNNFQGAASPESVYGAPSNEQVVGKKKSVSEPYQDNYNQESQYSNMRTGAVPQRGQKVSNKAQVPVPVTTNPTLVPGVPEPVPPSGTVKSTSFSEEIGFFDKVKKAIGNKQTYGDFLKLLNLFTQDIIDKDTLVERVQGFIGDTNVELFNWFKMFVGYEDKPQNIENITFKKHHLELSLCKAYGPSYRQLPKAETYMPCSGRDEMCWEVLNDEWVGHPTWASEDSGFIAHRKNQYEEILFKIEEERLEFDYYMESNLRTIQILETIANRIANMTPEQKATFKLPPGLGHNSSTIYKKIIRKIYDKDRGFEVIDALHENPSIAVPIVLKRLKQKDEEWKRAQREWNKVWREMEQKVFYKSLDHVGLTFKQADKKLLTVKQLVSEISTVKVEQQNKRLHPLTPKPQEQLNYDFKDNEVLFDILKLAEVFINKSSTYSVHDREKLLQFLQFFMSLFFSIPTETIETALVARGRIEKSSEEENEKGDVEMSENGSDSSKKRSRDTDLLKDVLKKQSKSKKDDRSGSPGLQSAELAIQEANEELEKSSELWITTANTKFSLNDENIQTRRDKYNLFCNTTIYVFFRHLQTLYTRLAEIKSMNEKVGKEIRNRKFPKFAKDLNLLSHQLEDMGVEIVGTKDCYKQVLELSEKLIEGEIEHQWFEESLRQGYRNRAYKIYTIDKVVQAMIKHMHSMITDAKTSEIMVLFENDRLKPVSSAKEQILYRISVRSFMSPEENMFKISFKESDSSVNIQFISLDDLTINDHENVEEKYNYYVTSYVMSHPTEGVPASKLNMPFARSFIESVDEESVEGRTGSGLKVSVSENSYSLFFESGSHDEFVSKAVYKKQDSNSKREDKLAHLKDLIDGENGWKSSLPEDQNLEVTEQKVAILFDKGGVEFKKFEEVLNSSDKSKESEANEPTKGATENVEVIENNNDNNTEPDAKSATTENKQEDTIVEETNDSTIQHDVDDTTADETNNTEVLGENDKAQSETKSS
Protein: Eukaryotic translation initiation factor 4E nuclear import factor 1 (B1AKL4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDRRSMGETESGDAFLDLKKPPASKCPHRYTKEELLDIKELPHSKQRPSCLSEKYDSDGVWDPEKWHASLYPASGRSSPVESLKKELDTDRPSLVRRIVDPRERVKEDDLDVVLSPQRRSFGGGCHVTAAVSSRRSGSPLEKDSDGLRLLGGRRIGSGRIISARTFEKDHRLSDKDLRDLRDRDRERDFKDKRFRREFGDSKRVFGERRRNDSYTEEEPEWFSAGPTSQSETIELTGFDDKILEEDHKGRKRTRRRTASVKEGIVECNGGVAEEDEVEVILAQEPAADQEVPRDAVLPEQSPGDFDFNEFFNLDKVPCLASMIEDVLGEGSVSASRFSRWFSNPSRSGSRSSSLGSTPHEELERLAGLEQAILSPGQNSGNYFAPIPLEDHAENKVDILEMLQKAKVDLKPLLSSLSANKEKLKESSHSGVVLSVEEVEAGLKGLKVDQQVKNSTPFMAEHLEETLSAVTNNRQLKKDGDMTAFNKLVSTMKASGTLPSQPKVSELLGQPVQRPASSNLLSGLMGSLEPTTSLLGQRAPSPPLSQVFQTRAASADYLRPRIPSPIGFTPGPQQLLGDPFQGMRKPMSPITAQMSQLELQQAALEGLALPHDLAVQAANFYQPGFGKPQVDRTRDGFRNRQQRVTKSPAPVHRGNSSSPAPAASITSMLSPSFTPTSVIRKMYESKEKSKEEPASGKAALGDSKEDTQKASEENLLSSSSVPSADRDSSPTTNSKLSALQRSSCSTPLSQANRYTKEQDYRPKATGRKTPTLASPVPTTPFLRPVHQVPLVPHVPMVRPAHQLHPGLVQRMLAQGVHPQHLPSLLQTGVLPPGMDLSHLQGISGPILGQPFYPLPAASHPLLNPRPGTPLHLAMVQQQLQRSVLHPPGSGSHAAAVSVQTTPQNVPSRSGLPHMHSQLEHRPSQRSSSPVGLAKWFGSDVLQQPLPSMPAKVISVDELEYRQ
Protein: Cytosine deaminase (CD) (CDA) (CDase) (EC 3.5.4.1) (Cytosine aminohydrolase) (Isoguanine deaminase) (EC 3.5.4.-) (P25524)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolytic deamination of cytosine to uracil. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis. Is also able to catalyze deamination of isoguanine, a mutagenic oxidation product of adenine in DNA, and of isocytosine. To a lesser extent, also catalyzes the conversion of 5-fluorocytosine (5FC) to 5-fluorouracil (5FU); this activity allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor.
Interaction partners:
- Cytosine permease
- Uracil phosphoribosyltransferase
- Uridine phosphorylase
- Thymidine phosphorylase
- Purine nucleoside phosphorylase DeoD-type
- Carbamoyl phosphate synthase large chain
- Pyrimidine-specific ribonucleoside hydrolase RihB
- Pyrimidine/purine nucleoside phosphorylase
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreA
- Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase
Sequence:
MSNNALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITENSLDAEQGLVIPPFVEPHIHLDTTQTAGQPNWNQSGTLFEGIERWAERKALLTHDDVKQRAWQTLKWQIANGIQHVRTHVDVSDATLTALKAMLEVKQEVAPWIDLQIVAFPQEGILSYPNGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFALAQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVTASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQGRFDTYPKRRGITRVKEMLESGINVCFGHDDVFDPWYPLGTANMLQVLHMGLHVCQLMGYGQINDGLNLITHHSARTLNLQDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKVIASTQPAQTTVYLEQPEAIDYKR
Protein: D-xylose reductase [NAD(P)H] (EC 1.1.1.307) (G5EB57)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MSSGKTFKLSNGVTIPAVGFGTFASEGASGETYRAVKKALEVGYRHLDCAWFYQNEDEVGDAVRDFLKENPSVKREDIFICTKVWNHLHRPEDVRWSIEDSLKKLKTDYVDLFLIHWPIAAEKESQDKPKIGPDGKYVILKDLTEDPKPTWQAMEKLYEDKLARSIGVSNWTIEGLEKLLKYAKVKPHVNQIEIHPFLPNEELIQYCWKNDILPEAYSPLGSQNQVPTTGERVSENKTLNEIAQKGGNTLAQVLIAWGLRRGYVVLPKSSNPARIESNFKTIELSDEDYEAVNAVAKGRHFRFVNMKDTFGYDVWPEETAKNISA
Protein: Oxalyl-CoA decarboxylase (EC 4.1.1.8) (P0AFI0)
Organism: Escherichia coli (strain K12)
Function: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA.
Interaction partners:
- Formyl-CoA:oxalate CoA-transferase
- Uncharacterized transporter YfdV
- Acetyl-CoA:oxalate CoA-transferase
- Protein YfdX
- Protein YdeP
- HTH-type transcriptional regulator YdeO
- Acetolactate synthase isozyme 3 small subunit
- Probable multidrug resistance protein EmrK
- Probable multidrug resistance protein EmrY
- Uncharacterized MFS-type transporter YhjX
Sequence:
MSDQLQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALANATVNGFPMIMISGSSDRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSMAKGILEDTHPLSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPIAVPVVGDIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQNAQKMHEKLSTDTQPLNYFNALSAVRDVLRENQDIYLVNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTSGSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNGGIYRGDGVDLSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPAAGTESGHITKLNPKQVAGN
Protein: Melanopsin (Opsin-4) (Q9UHM6)
Organism: Homo sapiens (Human)
Function: Photoreceptor that binds cis-retinaldehydes. Contributes to pupillar reflex, photoentrainment and other non-image forming responses to light (By similarity). May be involved in the optokinetic visual tracking response (By similarity). May be involved in the regulation of retinal hyaloid vessel growth and regression (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9QXZ9}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:Q9QXZ9}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9QXZ9}. Perikaryon {ECO:0000250|UniProtKB:Q9QXZ9}.
Interaction partners:
- Cyclic nucleotide-gated channel alpha-3
- Guanine nucleotide-binding protein G
- Serotonin N-acetyltransferase
- Retinoid isomerohydrolase
- Glycine N-acyltransferase-like protein 1
- Guanine nucleotide-binding protein G
- Lecithin retinol acyltransferase
- Beta-adrenergic receptor kinase 1
- Cyclic nucleotide-gated channel beta-3
- Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
Sequence:
MNPPSGPRVPPSPTQEPSCMATPAPPSWWDSSQSSISSLGRLPSISPTAPGTWAAAWVPLPTVDVPDHAHYTLGTVILLVGLTGMLGNLTVIYTFCRSRSLRTPANMFIINLAVSDFLMSFTQAPVFFTSSLYKQWLFGETGCEFYAFCGALFGISSMITLTAIALDRYLVITRPLATFGVASKRRAAFVLLGVWLYALAWSLPPFFGWSAYVPEGLLTSCSWDYMSFTPAVRAYTMLLCCFVFFLPLLIIIYCYIFIFRAIRETGRALQTFGACKGNGESLWQRQRLQSECKMAKIMLLVILLFVLSWAPYSAVALVAFAGYAHVLTPYMSSVPAVIAKASAIHNPIIYAITHPKYRVAIAQHLPCLGVLLGVSRRHSRPYPSYRSTHRSTLTSHTSNLSWISIRRRQESLGSESEVGWTHMEAAAVWGAAQQANGRSLYGQGLEDLEAKAPPRPQGHEAETPGKTKGLIPSQDPRM
Protein: Protein espinas (A0A0K3AQM0)
Organism: Caenorhabditis elegans
Interaction partners:
- CTD small phosphatase-like protein 1
- CRE-UNC-96 protein
- Muscle M-line assembly protein unc-89
- PDZ domain-containing protein
- Copine family protein 1
- Zinc finger protein unc-98
- Paralyzed arrest at two-fold protein 6
- Protein vav
- LIM domain-containing protein unc-95
- Alpha-actinin, sarcomeric
Sequence:
MSDNVGPRELSNAFKYLLAYQLDSIAQDGVMPSAHGALHKLLCSCYSKNTEVVDIYDMPENNNAQEKEDHYTKRAIDIGETKKRLELLPPPPTSSSPRPTSSNSIIQKSDGKRKDQKNEKQASPIIVEVYDDTPQSKMMLSTMNNPYRGGGNNNSNNNNSNHGMVIEDVTDDPEYSSYGNENEKPENEEEGAFVEYEKLDKTEDPAAFKVCQATTAVNRTYNNIRPSYRMPIGGGSGSSSGSISREIRIESMNLTDVEDGARCRDKECHLGWKQHPWRKVCVHCKSDRSDHELPPNQALNVYNRLGIQPPAGMPQSGVAEPEVPGSVGHGYAWVPPGLSRKKVEEYMSQLPNNVVPRTNSNGEKLREKQLLLQLPRQDLSVAYCRHLTSQTERKVYEEFVNARNEIALDIGYVSSNINKAMECHKCSGILETNEMAVIAPKLGDSTGWHPACFTCQACEQLLVDLTYCVKDNQIYCERHYAELHKPRCSACDELIFAGEYTKAMNKDWHSDHFCCWQCDQTLTGQRYIMRDEQPYCIKCYEDVFANQCDECAKPIGIDSKDLSYKDKHWHEHCFLCSMCKISLVDMPFGSKNDRIFCSNCYDQAFATRCDGCNEIFRAGMKKMEYKGKQWHDKCFCCAHCKLAIGTKSFIPKNDDVFCGPCYEEKFATRCSKCKKVITAGGVTYKNEPWHRECFCCTNCNSSLAGQRFTSKDEKPYCANCYGDLFAKRCNACTKPITGIGGAKFISFEDRHWHNDCFICAQCTTSLVGKGFITDGHEILCPECAKARLMAANS