wanglab/gogpt-training-data huggingface dataset:
Protein: Acidic endochitinase (EC 3.2.1.14) (P19172)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein functions as a defense against chitin containing fungal pathogens.
Subcellular location: Secreted, extracellular space. Note=Intercellular space of infected plants.
Interaction partners:
- Class V chitinase
- Basic endochitinase B
- Beta-hexosaminidase 2
- Glycosyl hydrolase family 18 protein
- Glycosyl hydrolase family 18 protein
- Cysteine/Histidine-rich C1 domain family protein
- Beta-hexosaminidase 1
- Beta-hexosaminidase 3
Sequence:
MTNMTLRKHVIYFLFFISCSLSKPSDASRGGIAIYWGQNGNEGNLSATCATGRYAYVNVAFLVKFGNGQTPELNLAGHCNPAANTCTHFGSQVKDCQSRGIKVMLSLGGGIGNYSIGSREDAKVIADYLWNNFLGGKSSSRPLGDAVLDGIDFNIELGSPQHWDDLARTLSKFSHRGRKIYLTGAPQCPFPDRLMGSALNTKRFDYVWIQFYNNPPCSYSSGNTQNLFDSWNKWTTSIAAQKFFLGLPAAPEAAGSGYIPPDVLTSQILPTLKKSRKYGGVMLWSKFWDDKNGYSSSILASV
Protein: Anthranilate phosphoribosyltransferase, hypothetical (Eurofung) (Q5B746)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- anthranilate synthase
- Multifunctional tryptophan biosynthesis protein
- Tryptophan synthase
- tryptophan synthase
- Alpha/beta hydrolase, putative
- aminodeoxychorismate synthase
- Histidine biosynthesis trifunctional protein
- Chorismate synthase
- Histidinol dehydrogenase
- 1-
Sequence:
MSASPRQKPESISISPLLKKLAYPASELAVEASEIASAFALIFEDRLSDIQTAALLTLLHSTQLDKDAEVIAKCSHRMREAARQTDKAALRQAIQSRGRKEGNYRGGLCDIVGTGGDSHSTFNISTTSSILASPLLMMAKHGNRAQTSFSGSADVLNAITPVPPKIGAVTAENLSQVYAASNYAFLFAPNFHYGMMYADNVRRNLGLRTIFNLMGPLANPVDWAIEARVVGVAYKALGPVFVEALRQNGVTKGLVICGEEDLDEISCAGKTNCWQLSEIPNPDYDLSKEDDEDEEYRTPPTIAKLDEFQLEPADFGLPSYPLTAVYGRKMPKDNAAKLMQILRNELPRDDPILSFVLMNVAALLVTSGICEADSSNMGPGDDGQVITERGPGGGRWKEGVRRARWAIESGSALKCFEEFIEVTNKL
Protein: Lethal(3)malignant brain tumor-like protein 3 (H-l(3)mbt-like protein 3) (L(3)mbt-like protein 3) (L3mbt-like 3) (MBT-1) (Q96JM7)
Organism: Homo sapiens (Human)
Function: Is a negative regulator of Notch target genes expression, required for RBPJ-mediated transcriptional repression. It recruits KDM1A to Notch-responsive elements and promotes KDM1A-mediated H3K4me demethylation. Involved in the regulation of ubiquitin-dependent degradation of a set of methylated non-histone proteins, including SOX2, DNMT1 and E2F1. It acts as an adapter recruiting the CRL4-DCAF5 E3 ubiquitin ligase complex to methylated target proteins. Required for normal maturation of myeloid progenitor cells (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:33980486}.
Interaction partners:
- Sterile alpha motif domain-containing protein 1
- DDB1- and CUL4-associated factor 5
- Recombining binding protein suppressor of hairless
- Bcl-2-associated transcription factor 1
Sequence:
MTESASSTSGQEFDVFSVMDWKDGVGTLPGSDLKFRVNEFGALEVITDENEMENVKKATATTTWMVPTAQEAPTSPPSSRPVFPPAYWTSPPGCPTVFSEKTGMPFRLKDPVKVEGLQFCENCCQYGNVDECLSGGNYCSQNCARHIKDKDQKEERDVEEDNEEEDPKCSRKKKPKLSLKADTKEDGEERDDEMENKQDVRILRGSQRARRKRRGDSAVLKQGLPPKGKKAWCWASYLEEEKAVAVPAKLFKEHQSFPYNKNGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKEEEFNWQTYLKTCKAQAAPKSLFENQNITVIPSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNVKHFSWDKYLEETNSLPAPARAFKVKPPHGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPPLSPLELMEASEHGGCSTPGCKGIGHFKRARHLGPHSAANCPYSEINLNKDRIFPDRLSGEMPPASPSFPRNKRTDANESSSSPEIRDQHADDVKEDFEERTESEMRTSHEARGAREEPTVQQAQRRSAVFLSFKSPIPCLPLRWEQQSKLLPTVAGIPASKVSKWSTDEVSEFIQSLPGCEEHGKVFKDEQIDGEAFLLMTQTDIVKIMSIKLGPALKIFNSILMFKAAEKNSHNEL
Protein: Methyl-accepting chemotaxis protein IV (MCP-IV) (Dipeptide chemoreceptor protein) (P07018)
Organism: Escherichia coli (strain K12)
Function: Mediates taxis toward dipeptides via an interaction with the periplasmic dipeptide-binding protein.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:22380631}; Multi-pass membrane protein {ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell poles.
Interaction partners:
- Protein-glutamate methylesterase/protein-glutamine glutaminase
- Chemotaxis protein methyltransferase
- Chemotaxis protein CheA
- Chemotaxis protein CheW
- Chemotaxis protein CheY
- Methyl-accepting chemotaxis protein II
- Motility protein B
- Protein phosphatase CheZ
- Motility protein A
- Flagellar secretion chaperone FliS
Sequence:
MFNRIRISTTLFLILILCGILQIGSNGMSFWAFRDDLQRLNQVEQSNQQRAALAQTRAVMLQASTALNKAGTLTALSYPADDIKTLMTTARASLTQSTTLFKSFMAMTAGNEHVRGLQKETEKSFARWHNDLEHQATWLESNQLSDFLTAPVQGSQNAFDVNFEAWQLEINHVLEAASAQSQRNYQISALVFISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMIDIVSSVTRVNDIMGEIASASEEQQRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEEHEVARHESVQLQIAPVVS
Protein: Ribosomal oxygenase 2 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA) (EC 1.14.11.79) (Histone lysine demethylase MINA) (MYC-induced nuclear antigen) (Q8CFC1)
Organism: Rattus norvegicus (Rat)
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39' (By similarity). May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8IUF8}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8IUF8}.
Interaction partners:
- Large ribosomal subunit protein uL2
Sequence:
MPKKVKPTGDENEEESVPCKQVKEELPNTLSVLNFDSPSSFFESLISPIKVETFFKEFWEQKPLLIQRDDPSLAAYYQSLFSLSDLRSLCSQGLYYGRDVNVCRCIGGKKKVLNKDGKAQFLQLRKDFDQKRATIQFHQPQRFKDELWRIQEKLECYFGSLVGSNVYMTPAGSQGLPPHYDDVEVFILQLEGRKRWRLYSPTVPLAREYSVEPEDRIGTPTHDFLLKPGDLLYFPRGTIHQAETPSGLAHSIHLTISTYQNNSWGDYLLDSISGLVFDIAKEDVALRTGMPRRMLMNVETPADVTRKLSGFLRTLADQLEGRKELLSSDMKKDFVMHRLPPFCVGNGTESMNPGGKLPRLNSIVRLQFKDHIVLTVGPDQNQSDEAQQKVVYIYHSLKNERQTHMMGKEVETEIYGLRFPLSYVDALKQIWCGSPVRVKDLKLGTDEEKENLAVSLWTECLVHVL
Protein: Ubiquitin carboxyl-terminal hydrolase 16 (EC 3.4.19.12) (Deubiquitinating enzyme 16) (AtUBP16) (Ubiquitin thioesterase 16) (Ubiquitin-specific-processing protease 16) (Q9SB51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Involved in salt tolerance by modulating sodium transport activity and repressing cell death at least partially through modulating SHM1 stability and activity. Involved in cadmium tolerance by interacting with HIPP27 and probably modulating its stability.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Serine hydroxymethyltransferase 1, mitochondrial
- Heavy metal-associated isoprenylated plant protein 27
Sequence:
MLLVLDLGISSLVLVVSLVLPLIGLFVRHKWRVAAQRREEIRRLLIHASEEAARAELEASVEFSSVAVSNVFHCPVCYCLATTRCSRCKAVRYCSGKCQIIHWRQGHKDECHPASIVYDSEDESDSDLRLGEENGQNTPEETLLVGPEPVTIPIGESLLSNRARSPEDGNGDIADNKDDLIDKEEAVSVAETSGSSFSGFSSSPRNDSGDEISRCESFSSSESERSESLLDAHVSVEPEDTCFSTIEDAPSKLLSPKFVHLVESVDNLANLPKLSVHKPEDDAGQNQSQSRSLHSLVTDRHPVSADPSLKSSDFWGTALGSAERVSDSCVKSKSGRPGNSSLHFSFGSGSSRDTSAAKVSEQRSSILKEAPRGTGYISDGVNLRERNAKRFDEAEIALPISSSTDALSPLDSSNLSHVTLPKSKSASSENGSMLAPLKVGEVQLLASKASNTKKCADLMKHSPLGAKSVRVLDHQKQNGAVVQHINSLHGRSGLKASVLKVVDQWTRPKSENEMAGRHGHKGLFPYEVFAKLYTYKIEFQPCGLINVGNSCFANVVFQCLMFTPPLTTYFLQQFHSRACTKKEQCFTCGFEKLVVKAKEEKSPLSPNGLLSQLQNIGIFLGNGKEEDAHEFLRFVVDTMQSVCIKASEYDMTKSSKLEDTTLIGLTFGGYLRSKIKCMKCQVKSELREKMMDLTVEIDGDISTLDDALRRFTRTEILDGENKYRCGSCKSYERAKKKLKITEPPNVLTIALKRFQAGKFGKLNKLIRFPETLDLAPYVSGGSEKSHDYKLYGVIVHLDVMNAAFSGHYVCYIRNQNKWYKADDSTVVTSDVERILTKGAYMLFYARCTPTPPRLAVCTKTEASNKKSRVPLPKANEKSTISRSVSTSSPELSSNTPGGGRSGNIQSFYSSFQRLQKILEEDSASDSSSLFDSNSDECSCSTDSTSMDDFADFIFGDHQGRAHGQSETPSPTSSSSSSSPPFTRRSPLSRSSPETYGTSRHQLPLGGER
Protein: Cell shape-determining protein Mbl (Actin-like Mbl protein) (Rod shape-determining protein Mbl) (P39751)
Organism: Bacillus subtilis (strain 168)
Function: Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and Mbl localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on Mbl polymerization. Organizes peptidoglycan synthesis in the lateral cell wall. Also required for proper chromosome segregation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17064365, ECO:0000305|PubMed:11290328}. Note=Membrane-associated (PubMed:17064365). Localizes in the form of helical filaments that run the length of the cell (PubMed:11290328). Colocalizes with MreB, MreBH and MreC (PubMed:16950129, PubMed:17064365). {ECO:0000269|PubMed:11290328, ECO:0000269|PubMed:16950129, ECO:0000269|PubMed:17064365}.
Interaction partners:
- Cell shape-determining protein MreC
- Rod shape-determining protein MreD
- Peptidoglycan glycosyltransferase RodA
- Penicillin-binding protein H
- Uncharacterized membrane protein YmfM
- Cell division protein FtsZ
- Probable peptidoglycan endopeptidase LytE
- Penicillin-binding protein 2A
- Peptidoglycan DL-endopeptidase CwlO
- Cell division protein FtsA
Sequence:
MFARDIGIDLGTANVLIHVKGKGIVLNEPSVVALDKNSGKVLAVGEEARRMVGRTPGNIVAIRPLKDGVIADFEVTEAMLKHFINKLNVKGLFSKPRMLICCPTNITSVEQKAIKEAAEKSGGKHVYLEEEPKVAAIGAGMEIFQPSGNMVVDIGGGTTDIAVISMGDIVTSSSIKMAGDKFDMEILNYIKREYKLLIGERTAEDIKIKVATVFPDARHEEISIRGRDMVSGLPRTITVNSKEVEEALRESVAVIVQAAKQVLERTPPELSADIIDRGVIITGGGALLNGLDQLLAEELKVPVLVAENPMDCVAIGTGVMLDNMDKLPKRKLS
Protein: C2 calcium-dependent domain-containing protein 4B (Nuclear-localized factor 2) (Protein FAM148B) (A6NLJ0)
Organism: Homo sapiens (Human)
Function: May be involved in inflammatory process. May regulate cell architecture and adhesion.
Subcellular location: Nucleus {ECO:0000269|PubMed:15527968}.
Interaction partners:
- Rho-related GTP-binding protein Rho6
Sequence:
MRLLEKLCSSAAGSSAPKPAFAKVLTPNRIPEFCIPPRLPAPCTLESPIRAAAVPRRCAAESDLWPRAADEDAGRTDWDPRSQAALSLPHLPRVRTTYGFCALLESPHTRRKESLLLGGPPAPRPRAHSCGGGGGPDAPLGTLCGPRGPGPATPAAPGGPRLPQDALAAGPRRCRLLRVPDGLLSRALRAGRSRRLARVRSVSSGNEDEERRAGSESPARAPSSSPLSSRAPLPERLEAKGTVALGRAGDALRLAAEYCPGTRRLRLRLLRAESLFGGAPGPRAVRCRLSLVLRPPGTARWQCSAVVGRSRKASFDQDFCFDGLSEDEVRRLAVRVKARDEGRGRDRGRLLGQGELSLGALLLL
Protein: Opacity protein opA59 (Q04883)
Organism: Neisseria gonorrhoeae
Function: Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
Subcellular location: Cell outer membrane.
Interaction partners:
Sequence:
AGEDHGRGPYVQADLAYAYEHITHDYPEPTGTKKDKISTVSDYFRNIRTHSIHPRVSVGYDFGGWRIAADYARYRKWNNNKYSVNIKELLRNDNANSGGSHLNIKTRKTEHRENGTFHAASSLGLSAVYDFDTGSRFKPYIGMRVAYGHVRHQVRSVQQETIAVTTYPQNAASSVTTNAPIRKLPHHESRSISSLGFGAVAGVGIDITPNLTLDAGYRYHNWGRLENTRFKTHEASLGVRYRF
Protein: CUB and LDLa domain, isoform B (Q9VSI3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLAEALGYGYLLAYVICLLCWPGEAYPASSSYRDLDICNHWDGRRHFLELGSPAGEVHARNVTTTAYRSSPLVFKNDAVAGDVWYQCSLELVTCAECVIRVAFTYANFSKSCGNTGGKSSMCPCEHIQFSEPPYDSTISGQEFCGDGKVFRSKTRTLQLKFFYRASNAHVFSLQYFSERNVRIVSGSPKQSIVGNGSTKSQPQVISTPYFPMAYPRDYGIEHILTCEADNCQVRLDFTDFQLGLTSTLEIFDSNGQMLDSYTGEHFRPPITVSSGKSLLLQFRGNSATGVGFRAEVSFVSSKQLKDERLVPYTDCGGMVTGPGGAITMMNMIENATDVRLFDCIWIIKPGNNYMMMKTHISLRVDDFYGMAARSELTIRQGTTSDAVEIENVMWPNNGLSKESHVAPILNGYYIRLRGVFGMSSKLAIVYSVFNYLNCYIGSEFLCGNNHCISIRLHCDGFDHCGDGSDEPDSCEEDWAHLHHDRRWYSHKPNYYFPKIDQYPDLKTATGIFIISTLGIFGVLSGWMVILYRMGVRARHQRELQSHLQTISELLDRQDEDRTPDEPPSYEAPPDYEEVIKVGMQQELREPRRQRRARRAPPRDRSCSRAASNCTVQSVLPLHRSCTLERDQEQPSTSAAAMTHAVAATDTTEDAEHVQTMAQRMLLATAICESHLQALQARLSRQQRSQGSGSNPWGFQRARHRYPLGVNYPQQVGQPQRPAARQMSAPREATHLAFHSL
Protein: Congested-like trachea protein (Q9VQG4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Putative mitochondrial carrier of unknown solute specificity. Required for gas-filling of the tracheal system at hatching time of the embryo and for normal epithelial morphogenesis of the wings.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Carnitine palmitoyltransferase 2
- Peroxisomal multifunctional enzyme type 2
- Choline/carnitine acyltransferase domain-containing protein
- Electron transfer flavoprotein subunit beta
- Electron transfer flavoprotein-ubiquinone oxidoreductase
- Carnitine O-Acetyl-Transferase, isoform A
- Choline/carnitine acyltransferase domain-containing protein
- Choline O-acetyltransferase
Sequence:
MTTTENVSTERKANPVKSFLTGGFGGICNVLSGHPLDTIKVRLQTMPRPAPGEQPLYRGTFDCAAKTIKNEGVRGLYKGMSAPLTGVAPIFAMCFAGYALGKRLQQRGEDAKLTYPQIFVAGSFSGLFSTLIMAPGERIKVLLQTQQGQGGERKYNGMIDCAGKLYKEGGLRSVFKGSCATMLRDLPANGLYFLVYEALQDVAKSKSETGQISTASTIFAGGVAGMAYWILGMPADVLKSRLQSAPEGTYKHGIRSVFKDLIVKDGPLALYRGVTPIMLRAFPANAACFFGIELANKFFNIVAPNF
Protein: Calsenilin isoform 4 (P0C092)
Organism: Mus musculus (Mouse)
Function: Unknown for isoform 4. Csen is involved in calcium-dependent transcriptional repression, regulation of potassium channels, and perhaps in processing of PSEN2 and apoptosis.
Interaction partners:
Sequence:
MRQLPAGPSSLACSGCKAGRLVTVPFSSRDAEDQGSREGIGWQPPGRSWAHTTEQEGKHQVAKATVHPPGPDALLLNQVDPVQCCPTRL
Protein: Microtubule-associated protein (A0A0B4KHQ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU000686}.
Interaction partners:
Sequence:
MADVLEKSSLLDAVPPLGDPHPPLPHQQLQQEAAAAAAANAAPPAPPQQQQPPPHQLQQQQPQQQQLQQKPANARANQDQKEGDNDSGVDESTQEKDRNGPNSPSSPVKTPTSTSSKPDKSGTSRPPSATPSNKSAPKSRSASKNRLLLKTPEPEPVKKVPMNKVQVGHAPSPNLKAVRSKIGSLDNATYKPGGGHVKIESKKIDIKAAPRIEAKNDKYMPKGGEKKIVTTKLQWNAKSKIGSLENAAHKPGGGDKKIETLKMDFKDKAKPKVGSTANVKHQPGGGDIKIQTQKLEIKAQSKVGSLDNVKHKPGGGEKKIFDDKDYLKNVEHSVALTTPPTQEYIYNFY
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial (Complex I-42kD) (CI-42kD) (NADH-ubiquinone oxidoreductase 42 kDa subunit) (O95299)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:12611891}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 2, mitochondrial
Sequence:
MALRLLKLAATSASARVVAAGAQRVRGIHSSVQCKLRYGMWHFLLGDKASKRLTERSRVITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRIQKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLKFDKGPWLKQDNRTLYHLRLLVQDKFEVLNYTSIPIFLPEVTIGAHQTDRVLHQFRELPGRKYSPGYNTEVGDKWIWLK
Protein: pH-response regulator protein palA/RIM20 (Regulator of IME2 protein 20) (Q12033)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the proteolytic cleavage of the transcriptional repressor RIM101 in response to alkaline ambient pH, which is necessary for sporulation and invasive growth. May act as a scaffold protein that recruits the calpain-like protease RIM13 via SNF7 to its substrate RIM101.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Vacuolar-sorting protein SNF7
- pH-response transcription factor pacC/RIM101
- Calpain-like protease 1
- pH-response regulator protein palH/RIM21
- pH-response regulator protein palF/RIM8
- pH-response regulator protein palI/RIM9
- Vacuolar protein-sorting-associated protein 25
- Uncharacterized protein YGR122W
- Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease
- Vacuolar protein-sorting-associated protein 36
Sequence:
MSELLAIPLKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKFPNNQIEFTWFQTLSQKSRGTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDHQKNLETIPVVDDATLNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAINDAQRGKLIRSDWINHLKAKKAYFSAVTYYRIALSFNEKKQFGNVVKALQMGLQFINESTLSSQAKFKTVVESSLKEAQRDNEFIYLQEVPSELPSIKPALMVKPSSSATLLPSIKKDETLFKDLIPIEVMEYCTAYNERQDEYVEQRVTNPLASLNKLLKESLTTFQIPQGLTKVSEAELSHYQASLNNLLINNKNVQVQLDNIEQILNEEAFTDNQLRLKHGTLNWTLPESSTTNTAYYEKLKKLRGYLDEGSAIDKQTNELFQSIDKNLIGSEIRLPESNDPLTNKIKMIIQERNDYIDRTRRKSSEYRILPKIITSYKKNGTVDFEPIFIGHLKYFDEDLRYVNSTKEENIKLIEEVNLSKKNNPGRSGIEPKKMVRIDPRELYIEDLRYSFKLLDEVKENLSAGTAFYENLITSTSNLYNEVQEYDTARRAEKARLDKSLTFEDQ
Protein: NTF2-related export protein (Q9VRD6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU369002}. Nucleus {ECO:0000256|RuleBase:RU369002}.
Interaction partners:
- NTF2-related export protein
- Nuclear pore glycoprotein p62
- Ran GTPase-activating protein
- GTP-binding nuclear protein Ran
- Nuclear RNA export factor 1
- Probable nucleoporin Nup54
- GTP-binding nuclear protein Ran-like
- Protein Rae1
- Nuclear pore complex protein Nup153
- NTF2-related export protein
Sequence:
MSLNPQYEDIGKGFVQQYYAIFDDPANRANVVNFYSATDSFMTFEGHQIQGAPKILEKVQSLSFQKITRVITTVDSQPTFDGGVLINVLGRLQCDDDPPHAFSQVFFLKANAGTFFVAHDIFRLNIHNSA
Protein: D-aminoacyl-tRNA deacylase 2 (EC 3.1.1.96) (Animalia-specific tRNA deacylase) (ATD) (D-tyrosyl-tRNA deacylase 2) (L-alanyl-tRNA deacylase) (Q8BHA3)
Organism: Mus musculus (Mouse)
Function: Deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr). By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS. Can deacylate L-Ala due to a relaxed specificity for substrate chirality caused by the trans conformation of the Gly-Pro motif in the active site. Also hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo EEF1A1/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- D-aminoacyl-tRNA deacylase 1
- Tyrosine--tRNA ligase, cytoplasmic
- RNA-binding protein 42
Sequence:
MADGGRVAQARALLQQCLHARLQVRPADGDAAAQWVEIRRGLVIYVCFFKGADTDLLPKMVNTLLNVKLSETETGKHVSILDLPGDVLIIPQATLGGRVKGRSMQYHSNSGKEEGSELYSQFVSLCEKAVANNTKSVEAGVAVAHGTYGNRQVLKLDTNGPYTHLIEF
Protein: Kinesin-like protein unc-104 (Uncoordinated protein 104) (P23678)
Organism: Caenorhabditis elegans
Function: Motor protein involved in microtubule-associated anterograde transport. Regulates the transport of synaptic vesicle precursors in the axon of DA motor neurons. Regulates the polarized sorting of axonal proteins. Essential for the transport of synaptic components during the synaptic remodeling of the DD motor neuron, probably downstream of cdk-5 and/or pct-1/cyy-1 complex. Required for the anterograde transport of neuropeptide-containing dense core vesicles along axons. Involved in necrotic cell death.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:22101643}.
Interaction partners:
- Liprin-alpha
- Ras-related protein Rab-3
- ADP-ribosylation factor-like protein 8B
- Kinesin light chain
- Synaptobrevin-1
- Rab-3-interacting molecule unc-10
- Kinesin light chain
- JNK-interacting protein
- ELKS/RAB6-interacting/CAST family member 2
- C2 domain-containing protein
Sequence:
MSSVKVAVRVRPFNQREISNTSKCVLQVNGNTTTINGHSINKENFSFNFDHSYWSFARNDPHFITQKQVYEELGVEMLEHAFEGYNVCIFAYGQTGSGKSYTMMGKANDPDEMGIIPRLCNDLFARIDNNNDKDVQYSVEVSYMEIYCERVKDLLNPNSGGNLRVREHPLLGPYVDDLTKMAVCSYHDICNLMDEGNKARTVAATNMNSTSSRSHAVFTIVLTQKRHCADSNLDTEKHSKISLVDLAGSERANSTGAEGQRLKEGANINKSLTTLGLVISKLAEESTKKKKSNKGVIPYRDSVLTWLLRENLGGNSKTAMLAALSPADINFDETLSTLRYADRAKQIVCQAVVNEDPNAKLIRELNEEVIKLRHILKDKGIDVTDVQETPGKHKKGPKLPAHVHEQLEKLQESEKLMAEIGKTWEQKLIHTEEIRKQREEELRDMGLACAEDGTTLGVFSPKKLPHLVNLNEDPLMSECLIYYLKEGVTSVGRPEAEHRPDILLSGEAILELHCEFINEDGNVTLTMKPNASCYINGKQVTTPTVLHTGSRVILGEHHVFRYNDPQEARQSRHNLAAIAEQPIDWKYAQQELLDKQGIDLKADMEKKMLEMESQYRREKVELEQKMYHQTREYESMIENLQKQVDLAQSYISGGGSIWEGERMLTSSLLEFPEELKWTSDQKRVVLKAAIKWRYHQFTSVRDDLWGNAIFVKEANAISVELKKKVQFQFALLTDTMYSPLPPDLLPPGEDLTLRPYPKTVVAIQVQDLKNGATHYWSIEKLKQRLEAMRDMYETDAEMSPADGDPMMDALMGTDPFYDRFPWFRMVGRAFVYLNNLLHNVPLIHKVAVVNEKGEVKGYLKVAIEPVQKDEVINQKKGVRQTAKLHFRKEDFLKSHKNGETSDSDALAFPEHMQEEVEFCFRVVVLQAIDVADTYSDVFCQFNFLHRHDEAFSTEPMKNSKSPLTFEHTQNLHIKMSKTFLHYLHHFPIIFEVFGHFQPKSEQFNFERQNSALGRRLSTKLTFQQPSLVISTPVKSKKANAPIQNNNASVKSKHDLLVWFEICELANNGEYVPTIVDHAQGLPTHGIFLLHQGIQRRIKITICHEKGELKWKDCQELVVGRIRAGPEWAGGDDVDVLSLGLFPGTFMEFSMDDRTFFQFEAAWDSSLHNSPLLNRVSNYGDQIYMTLSAYMELDGCAQPAVVTKDLCLLIYARDSKISAASRFCRSLVGGISKSPEMNRVPGVYQLCLKDGSDSGSPGAIRRQRRVLDTSSAYVRGEENLGQWRPRGDSLIFEHQWELEKLTRLQQVERVRLFLRLRDRLKGKKNKGEARTPVSPCDPVCAIPESIKLDEKDKGIVGKVLGLIRRKIPMNKDPPTGNKAQELSDESGSNSITSPVSDKSLIKSSRSSDLLCRQKSKSDQNLASNDDIVDNLGGMKRSLSGSRILQLNILVPEVLEERVGVVVSKKGYMNFLEEKTQGWTRRWVIVRRPYILLFRDDRDLVIRGIINLANARIEHSEDQQAMVKVPNTFSVCTNQRGFLMQMMPGDEMYDWLYAINPLMAGQMKLHGNQNGTTLKSPTSSSSIAAS
Protein: Rap guanine nucleotide exchange factor 2 (G5ECB8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSVDSIAMPPPPVPPRPLRLPQTAAKGPAPLPPRGLPRTYPLDFPVDIPTTSSSSSNTSYNDQHRSQVYLNGLSADEDTLVRVKHRREKSNSVGGQAQNGISTARRLRGRSTASSTTTEGETASNEGADSDEDEGSMPSQESSSGGFMDLRDSVRECLEKEPSERNSEDLAVLLDFMQHMSAFAALPMSIKRQLCLKMVFAVVNDAGTVVLAHNEKLDSWSVIVNGCVEVVKPSGERVEYKLGDSFGAEPTPATQIHIGEMRTMVDDCEFVLVEHRDFCSIMSTIGDHIEKDRDGLTGEVVSEVERRTVGTHCGQVLIKGKPDKLIHHLVDERDHNVDPHYVDDFLLTYRVFIRDPTTIFEKLMLWFADSIYRDKVARLVLLWVNNHFNDFETNDEMWNLLERFEGALERDGMHSQLSLLNIACSVKAKPRQVILTRRKDDKMMMRLVGGQESGNSVYVAEVFPDTSAAREGVKRADEMLEVNQQSAKYLSAKKAEDLLTGSLSLTLMLKNNVLGYKETIGKIEHNKPKNGTSRSGAGIPMVIPVHKTSITGKKSSTTSSKSGMMEKLMTILKSSKEDSMDFTDEAKISSADLRPSRSNPDITSISQYYGPVRSECPEHVLKIYRNDQTFKYLPVYKETSAQNVVQLALQEFNMTAEGSPEWSLCECTVTIDGVIKQRRLPPQMENLAERIALNSRYYLKNNSRSEPLVPDELAPELLKEAQTQLLSLNAQVVAAQLTLQDFSVFSAIEPTEFLDNLFKLDSKYGSPKLEEFEQLFNREMWWVATEICTERHVQKRAKLIKKFIKVARYCRDLRNFNSMFAIMSGLDKPAVRRLHSSWERVSSKYIRMLDEIHQLVDPSRNMSKYRQHLAEVAQEPPVVPIYPVIKKDLTFAHDGNATYSEKLINFEKLRLIAKSIRGVMKLSSAPYEIASMAERSGGVVMDALLHMNSFENSNVATMRKGMSGKQNQPRKKVYEQALMVRKVKSYLEGLHVVDNEMELDSMSYDIEPQVQTAHRGANSSSTANIRRVPSPTPSSLSSQSAGSADQSSRHRLLFNGTGSISSAGGGSKFGVESPQAVQKMLSLVQNSKVKGAPPQITSPSTSARSSLQRNMPRVTGRQATSSAQGPVQLNEETSTVTTYYQSDVLI
Protein: Pho100p (Q59WE5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- IMP-specific 5'-nucleotidase 1
- Adenylate kinase
- Purine nucleoside phosphorylase
- Guanylate kinase
- Uridine kinase
- Trifunctional uridine nucleosidase/nicotinamide riboside hydrolase/nicotinic acid riboside hydrolase
- Adenosine kinase
- Apyrase
- uracil phosphoribosyltransferase
- Uridine kinase
Sequence:
MQFLTSALVLLLSVGALAKNILLTNDDGWQATNIRATYYKLKEAGHNVFLVAPVSQRSGFSGKFDIPTSPTLQTNGEFNYPPAGAPSWGHEVDDNHIWYFNGTPASSAVFGINYVIPKYGDNVTIDLVVSGPNEGTNMSPGLFTISGTVGATYTSIYRGIPGVAFSGSNSNNSFFKDSLDLKDNKEPSTIYANKVVEFVNQIFKAQGNNPRALGLGVGLNVNFPKVGYENETCTNPKWVFTRLTGQYAAGANLVYNETSNSFTWGQKSWDGLTVCNNGDCSLPSENFIVEHTNCQSSVSVFSVDYDANLGLTSQVKQILNPLF