wanglab/gogpt-training-data huggingface dataset:
Protein: Calcineurin B-like protein 4 (Protein SALT OVERLY SENSITIVE 3) (O81223)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a calcium sensor involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Binding of a CBL protein to the regulatory NAF domain of a CIPK serine-threonine protein kinase lead to the activation of the kinase in a calcium-dependent manner. Operates in synergy with CIPK24/SOS2 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. Involved in salt stress responses by mediating calcium-dependent microfilament reorganization. The CBL4/CIPK6 complex mediates translocation of AKT2 from the endoplasmic reticulum to the plasma membrane. Both myristoylation and S-acylation are required for AKT2 activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19832944}; Lipid-anchor {ECO:0000269|PubMed:19832944}. Cytoplasm {ECO:0000269|PubMed:19832944}. Nucleus {ECO:0000269|PubMed:19832944}. Note=The cell membrane localization is S-acylation dependent.
Interaction partners:
- CBL-interacting serine/threonine-protein kinase 24
- CBL-interacting serine/threonine-protein kinase 6
- Sodium/hydrogen exchanger 7
- CBL-interacting serine/threonine-protein kinase 1
- Sodium/hydrogen exchanger 1
- Potassium channel AKT2/3
- Sodium transporter HKT1
- Potassium channel AKT1
- CBL-interacting serine/threonine-protein kinase 11
- CBL-interacting serine/threonine-protein kinase 14
Sequence:
MGCSVSKKKKKNAMRPPGYEDPELLASVTPFTVEEVEALYELFKKLSSSIIDDGLIHKEEFQLALFRNRNRRNLFADRIFDVFDVKRNGVIEFGEFVRSLGVFHPSAPVHEKVKFAFKLYDLRQTGFIEREELKEMVVALLHESELVLSEDMIEVMVDKAFVQADRKNDGKIDIDEWKDFVSLNPSLIKNMTLPYLKDINRTFPSFVSSCEEEEMELQNVSS
Protein: Pseudouridylate synthase RPUSD4, mitochondrial (RNA pseudouridylate synthase domain-containing protein 4) (Q38FJ3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GTP-binding protein, putative
- Uncharacterized protein
- Acyl carrier protein
- tRNA/rRNA methyltransferase SpoU type domain-containing protein
- Large ribosomal subunit protein bL21m
- EngB-type G domain-containing protein
- GTP-binding protein, putative
- Ribosomal protein L11, putative
- Large ribosomal subunit protein uL3m
- 50S ribosomal protein L17, putative
Sequence:
MLHAVRLLSCWRPAAIQHLPDVAPHAPVQEVEKSHARYRPLSLRARQTLSEKSDDLQYHVVTQEWFGERVDSFLTCHYPQWDYETIKRLVQQGHIYRYRKNGKKKFTRLTDRLEFDELLVVPTRAFWEKQLAPPSGVLEETDGPKFKLSATAREMAHNMVLFKNEHVIVINKPHGLPMMPTDDPQEMSIAAMLPAWKFTNVAKPVVCHNLDRETSGCVVLARTRNAHRMLGRMFVKRVVPNSVYWSFCVGKPTVNYGRVRMHFDITRGNKGDIIVARPSPTKTSKVAIAEFVVNASALEFGSFISFYPLTTRRHQERIMAAHALRCPVLGDAKYGGDAAFPSSLSLFWDPENKGLPLHLHHRKIQLPYKNTAGEFICVTAPLPTQMEKTFKKLGWPCEVDDPLIPG
Protein: DNA polymerase subunit gamma-1 (EC 2.7.7.7) (E5KNU5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|PIRNR:PIRNR000797}.
Interaction partners:
Sequence:
MSRLLWRKVAGATVGPGPVPAPGRWVSSSVPASDPSDGQRRRQQQQQQQQQQQQQPQQPQVLSSEGGQLRHNPLDIQMLSRGLHEQIFGQGGEMPGEAAVRRSVEHLQKHGLWGQPAVPLPDVELRLPPLYGDNLDQHFRLLAQKQSLPYLEAANLLLQAQLPPKPPAWAWAEGWTRYGPEGEAVPVAIPEERALVFDVEVCLAEGTCPTLAVAISPSAWYSWCSQRLVEERYSWTSQLSPADLIPLEVPTGASSPTQRDWQEQLVVGHNVSFDRAHIREQYLIQGSRMRFLDTMSMHMAISGLSSFQRSLWIAAKQGKHKVQPPTKQGQKSQRKARRGPAISSWDWLDISSVNSLAEVHRLYVGGPPLEKEPRELFVKGTMKDIRENFQDLMQYCAQDVWATHEVFQQQLPLFLERCPHPVTLAGMLEMGVSYLPVNQNWERYLAEAQGTYEELQREMKKSLMDLANDACQLLSGERYKEDPWLWDLEWDLQEFKQKKAKKVKKEPATASKLPIEGAGAPGDPMDQEDLGPCSEEEEFQQDVMARACLQKLKGTTELLPKRPQHLPGHPGWYRKLCPRLDDPAWTPGPSLLSLQMRVTPKLMALTWDGFPLHYSERHGWGYLVPGRRDNLAKLPTGTTLESAGVVCPYRAIESLYRKHCLEQGKQQLMPQEAGLAEEFLLTDNSAIWQTVEELDYLEVEAEAKMENLRAAVPGQPLALTARGGPKDTQPSYHHGNGPYNDVDIPGCWFFKLPHKDGNSCNVGSPFAKDFLPKMEDGTLQAGPGGASGPRALEINKMISFWRNAHKRISSQMVVWLPRSALPRAVIRHPDYDEEGLYGAILPQVVTAGTITRRAVEPTWLTASNARPDRVGSELKAMVQAPPGYTLVGADVDSQELWIAAVLGDAHFAGMHGCTAFGWMTLQGRKSRGTDLHSKTATTVGISREHAKIFNYGRIYGAGQPFAERLLMQFNHRLTQQEAAEKAQQMYAATKGLRWYRLSDEGEWLVRELNLPVDRTEGGWISLQDLRKVQRETARKSQWKKWEVVAERAWKGGTESEMFNKLESIATSDIPRTPVLGCCISRALEPSAVQEEFMTSRVNWVVQSSAVDYLHLMLVAMKWLFEEFAIDGRFCISIHDEVRYLVREEDRYRAALALQITNLLTRCMFAYKLGLNDLPQSVAFFSAVDIDRCLRKEVTMDCKTPSNPTGMERRYGIPQGEALDIYQIIELTKGSLEKRSQPGP
Protein: 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10) (Type I DHQase) (Type I dehydroquinase) (DHQ1) (Q186A6)
Organism: Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsilon-amino group of Lys-170 at the active site.
Interaction partners:
- Shikimate dehydrogenase
- Shikimate dehydrogenase
- 3-dehydroquinate synthase
- Shikimate kinase
- Transporter, Major Facilitator Superfamily
- Dihydroxy-acid dehydratase
Sequence:
MKRKVQVKNITIGEGRPKICVPIIGKNKKDIIKEAKELKDACLDIIEWRVDFFENVENIKEVKEVLYELRSYIHDIPLLFTFRSVVEGGEKLISRDYYTTLNKEISNTGLVDLIDVELFMGDEVIDEVVNFAHKKEVKVIISNHDFNKTPKKEEIVSRLCRMQELGADLPKIAVMPQNEKDVLVLLEATNEMFKIYADRPIITMSMSGMGVISRLCGEIFGSALTFGAAKSVSAPGQISFKELNSVLNLLHKSIN
Protein: Multidrug and toxin extrusion protein 2 (MATE-2) (mMATE-2) (H(+)/organic cation antiporter kidney-specific) (Solute carrier family 47 member 2) (Q3V050)
Organism: Mus musculus (Mouse)
Function: Multidrug efflux pump that functions as a H(+)/organic cation antiporter. May mediate testosterone efflux from the Leydig cells in the testes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17715386}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 22 member 2
- Solute carrier family 22 member 1
Sequence:
MEPAEDSLGATIQPPELVRVPRGRSLRILLGLRGALSPDVRREAAALVALAGPVFLAQLMIFLISIVSSIFCGHLGKVELDAVTLAVSVVNVTGISVGTGLASACDTLMSQSFGGKNLKRVGVILQRGILILLLCCFPCWAIFLNTERLLLLLRQDPDVARLAQVYVMICIPALPAAFLFQLQTRYLQSQGIIMPQVIVGIAANVVNVGMNAFLLYALDLGVVGSAWANTTSQFFLSALLFLYVWWKRIHIHTWGGWTRECFQEWSSYTRLAIPSMFMVCIEWWTFEIGTFLAGLVNVTELGAQAVIYELASVAYMVPFGFGVAASVRVGNALGAGNADQARCSCTTVLLCAGVCALLVGILLAALKDVVAYIFTNDKDIISLVSQVMPIFAPFHLFDALAGTCGGVLRGTGKQKIGAVLNTIGYYGFGFPIGVSLMFAAKLGIIGLWAGLIVCVSFQAFSYLIYILRTNWSRVAEQAQVRAGLKSTKELIPTPADLPILEREVMDGVILPDIIRPESQTGQLVVEENSQCAVPTVGEVLTGRQLVFYRGMALTVSVAVLIAGIVVRVFNDRG
Protein: RCC1 and BTB domain-containing protein 2 (Chromosome condensation 1-like) (Regulator of chromosome condensation and BTB domain-containing protein 2) (Q99LJ7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:22768142}. Note=Mainly found in the acrosomal cap region. {ECO:0000269|PubMed:22768142}.
Interaction partners:
Sequence:
MEEEVPGFYGESGKSVQATLSSLKMLDVGKWPIFSLCSEEELQLIRQACVFGSAGNEVLYTTVNDEIFVLGTNCSGCLGVGDIQSTIEPRRLDSLTGKKIASLSYGSGPHIVLATTDGEVFTWGHNAYSQLGNGTTNHGLVPCHISTNLSNKQVIEVACGSYHSLVLTSDGEVFAWGYNNSGQVGSGSTANQPIPRRVTGCLQNKVVMNIACGQMCSMAVVDTGEVYVWGYNGNGQLGLGSSGNQPTPCRVAALQGIRVQRVACGYAHTLVLTDEGQIYAWGANSYGQLGTGNKSNQSYPTPVVVEKDRIIEIAACHSAHTSAAKTQGGHVYMWGQCRGQSVILPHHTHFCCTDDVFACFATPAVTWRLLSVEPDDHLTVAESLKREFDNPDTADLKFLVDGKYIYAHKVLLKIRCEHFRSSLEDSEDDIVEMSEFSYPVFRAFLEYLYTDNISLSPEEAVGLLDLATFYSETRLKKLCQQTIKQGICEENAIALLSAAVKYDAQDLEEFCFRFCINHLTVVTQTSGFAEMDHDLLKNFISKASRVGAFKN
Protein: Acyl-homoserine-lactone synthase (EC 2.3.1.184) (Autoinducer synthesis protein LasI) (P33883)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for the synthesis of PAI consisting of 3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide also known as N-(3-oxododecanoyl)homoserine lactone, an autoinducer molecule which binds to LasR and thus acts in elastase biosynthesis regulation.
Interaction partners:
- Transcriptional activator protein LasR
- HTH-type quorum-sensing regulator RhlR
- Quorum-sensing control repressor
- Regulatory protein RsaL
- Acyl-homoserine-lactone synthase
- Multiple virulence factor regulator MvfR
- S-adenosylmethionine synthase
- Elastase
- Amidohydrolase-related domain-containing protein
- S-adenosylmethionine decarboxylase proenzyme
Sequence:
MIVQIGRREEFDKKLLGEMHKLRAQVFKERKGWDVSVIDEMEIDGYDALSPYYMLIQEDTPEAQVFGCWRILDTTGPYMLKNTFPELLHGKEAPCSPHIWELSRFAINSGQKGSLGFSDCTLEAMRALARYSLQNDIQTLVTVTTVGVEKMMIRAGLDVSRFGPHLKIGIERAVALRIELNAKTQIALYGGVLVEQRLAVS
Protein: Desmoglein-3 (130 kDa pemphigus vulgaris antigen homolog) (O35902)
Organism: Mus musculus (Mouse)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9701552}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, desmosome {ECO:0000269|PubMed:9166409}. Cytoplasm {ECO:0000250|UniProtKB:P32926}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q7YRU7}. Cell junction {ECO:0000269|PubMed:18343367}.
Interaction partners:
- Plakophilin-3
- Plakophilin-1
- Desmoplakin
- Junction plakoglobin
- Plakophilin-2
- Desmocollin-1
- Desmocollin-3
- Desmocollin-2
- Envoplakin
- Caspase-3
Sequence:
MTCLFPRALGSLALLMVVLLVQGELHVKPGGQHREDGTALQLAKRRYKREWVKFAKPCREREDNSRRNPIAKITSDFQKNQKITYRISGVGIDQPPFGIFVVDPNNGDINITAIVDREETPSFLITCRALNALGQDVERPLILTVKILDVNDNPPIFSQTIFKGEIEENSASNSLVMILNATDADEPNHMNSKIAFKIVSQEPAGMSMFLISRNTGEVRTLTSSLDREQISSYHLVVSGADNDGTGLSTQCECSIKIKDVNDNFPVLRESQYSARIEENTLNAELLRFQVTDWDEEYTDNWLAVYFFTSGNEGNWFEIETDPRTNEGILKVVKALDYEQVQSMQFSIAVRNKAEFHQSVISQYRVQSTPVTIQVIDVREGISFRPPSKTFTVQRGVSTNKLVGYILGTYQATDEDTGKAASSVRYVLGRNDGGLLVIDSKTAQIKFVKNIDRDSTFIVNKTISAEVLAIDENTGKTSTGTIYVEVPSFNENCPSVVLEKKDICTSSPSVTLSVRTLDRGKYTGPYTVSLEEQPLKLPVMWTITTLNATSALLQAQQQVSPGVYNVPVIVKDNQDGLCDTPESLTLTVCQCDDRSMCRAPIPSREPNTYGESSWRLGPAAIGLILLGLLMLLLAPLLLLTCDCGSGPIGGAATGGFIPVPDGSEGTIHQWGIEGAQPEDKEITNICVPPVTTNGADFMESSEVCTNTYAGGTMVEGASGMEMITKLGGATGATAALGPCSLGYSGTMRTRHSTGGTLKDYAAPVNMTFLGSYFSQKSLAYAEEEDEREVNDCLLIYDDEGEDAAPHSPTLSSCSIFGDDLDDNFLDSLGPKFKKLAEICLGIDDEAKQAKPGPKDSGSGADTCARSMEVPQSGSNRYQTLPGSLEVTQTGSKICHTLSGNQETSVMSTSGSVHPAVAIPDPLQLGNYLLTETYSTSGSFAQPTTVTFDPHVTQNVTVTERVICPLPSASSSIVAPTELRGSYNMLYTKETCSHL
Protein: APOBEC3A (Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A) (A0A0K0MJ49)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEASPASGPRHLMDPHIFTSNFNNGIGRHKTYLCYEVERLDNGTSVKMDQHRGFLHNQAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFKHCWDTFVDHQGCPFQPWDGLDEHSQALSGRLRAILQNQGN
Protein: ZNF85 protein (Zinc finger protein 85) (Q49A12)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLSAQPSSSFYKPVSEVMCSHFAQDLWPEQNIKDSFQKVTLKRYGKCRHENLPLRKGCESMDECKMHKGGCNGLNQCLTATQSKIFQCDKYVKVAHKFSNSNRHEIRHTKKKPFKCTKCGKSFGMISCLTEHSRIHTRVNFYKCEECGKAFNWSSTLTKHKRIHTGEKPYKCEECGKAFNQSSNLIKHKKIHTGEKPYKCEECGKTFNRFSTLTTHKIIHTGEKPYKCKECGKAFNRSSTLTTHRKIHTGEKPYKCEECGKAFKQSSNLTTHKIIHTGEKPYKCKKCGKAFNQSAHLTTHEVIHTGEKPYKCEKCGKAFNHFSHLTTHKIIHTGEKPYKCKECGKAFKHSSTLTKHKIIHTGEKPYKCKECEKAFNQSSKLTEHKKIHTGEKPYECEKCGKAFNQSSNLTRHKKSHTEEKPYKCEECGKGFKWPSTLTIHKIIHTGEKPYKCEECGKAFNQSSKLTKHKKIHTGEKPYTCEECGKAFNQSSNLTKHKRIHTGEKPYKCEECDKAFKWSSVLTKHKIIHTGEKLQI
Protein: Glyoxylate reductase 1 (EC 1.1.1.26) (EC 1.1.1.79) (EC 1.1.1.81) (P53839)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Glyoxylate reductase that reversibly reduces glyoxylate to glycolate, or alternatively hydroxypyruvate to D-glycerate, using either NADPH or NADH as a cosubstrate. Does not act as a hydroxyisocaproate dehydrogenase even though it also has minor activity on alpha-ketoisocaproate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. Mitochondrion {ECO:0000269|PubMed:14576278}.
Interaction partners:
- Alanine--glyoxylate aminotransferase 1
- Malate synthase 1
- Isocitrate lyase
- Malate synthase 2
- Probable ATP-dependent kinase TDA10
- Mitochondrial 2-methylisocitrate lyase ICL2
- Probable oxidoreductase AIM17
- Large ribosomal subunit protein uL22A
- Large ribosomal subunit protein uL22B
- Ureidoglycolate lyase
Sequence:
MSKKPIVLKLGKDAFGDQAWGELEKIADVITIPESTTREQFLREVKDPQNKLSQVQVITRTARSVKNTGRFDEELALALPSSVVAVCHTGAGYDQIDVEPFKKRHIQVANVPDLVSNATADTHVFLLLGALRNFGIGNRRLIEGNWPEAGPACGSPFGYDPEGKTVGILGLGRIGRCILERLKPFGFENFIYHNRHQLPSEEEHGCEYVGFEEFLKRSDIVSVNVPLNHNTHHLINAETIEKMKDGVVIVNTARGAVIDEQAMTDALRSGKIRSAGLDVFEYEPKISKELLSMSQVLGLPHMGTHSVETRKKMEELVVENAKNVILTGKVLTIVPELQNEDWPNESKPLV
Protein: Interleukin enhancer-binding factor 2 (K7GS49)
Organism: Sus scrofa (Pig)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPAEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEETPQGEEEESMETQE
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (Q9XZ54)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
RTCLHFTSAVCSRVFCCSPAASAPAPSPESSDIRLWKTKAMSKSILVISCLLLVAISNSLVRAEDLKVEVISTPEVCEQKSKNGDSLTMHYTGTLQADGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQGAGNVIPPKATLLFDVELINIGNAPPTTNVFKEIDDNADKQLSREEVSEYLKKQMTAVEGQDSEELKNMLAENDKLVEEIFQHEDKDKNGFISHDEFSGPKHDEL
Protein: Protein PLASTID TRANSCRIPTIONALLY ACTIVE 16, chloroplastic (pTAC16) (Q9STF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in the regulation of plastid gene expression.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:16326926, ECO:0000269|PubMed:22616989}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:21877139, ECO:0000269|PubMed:22616989}; Peripheral membrane protein {ECO:0000269|PubMed:22616989}; Stromal side {ECO:0000269|PubMed:22616989}.
Interaction partners:
- Photosystem I reaction center subunit IV A, chloroplastic
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 7
Sequence:
MASSSTSFPLTTAPPQGVRFNRRKPRLTVWAKQTAFQLGKTKGDDDSEGKQKGKNPFQFDFGKLPDMKSLIPVVTNPSTGLVFGNNRKKDPGTIFVAGATGQAGIRIAQTLLQRGFSVRAGVPDLGAAQDLARVAATYKILSNDEVKRLNAVQSPFQDAESIAKAIGNATKVVVTVGATENGPDAQVSTSDALLVVQAAELAGVSHVAIVYDGTISGSTYNVLDGITSFFGNLFAKSQPLTISDLIEKVAQTDVAYTLIKTSLTEDFSPEKAYNVVVSAEGSNSGSGSSSSEAYKVPKLKIASLVADIFANTAVAENKVVEVSTDPSAPSRPVDELFSVIPEDGRRKVYADAIARERAEEEAKVAADKAREAAEAAKEFEKQMQKLSEKEAEAASLAEDAQQKADAVGVTVDGLFNKAKDISSGLSWNKLGSQFATAIQNASETPKVQVATVRGQAKARNLPPKKAVVKQRPSSPFASKPKEERPKKPEKEVRKVFGGLFKQETIYIDDD
Protein: Acyl-coenzyme A oxidase acox-1.4 (EC 1.3.3.-) (O62139)
Organism: Caenorhabditis elegans
Function: Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior. Specifically, shortens ascarosides with a 9-carbon side chain (asc-C9) and, in association with acox-1.1, may contribute to the shortening of ascarosides with a 11-carbon side chain (asc-C11). May contribute to the production of indol-3-carbonyl(IC)-ascarosides in association with acox-1.1 and acox-3.
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:O62140}.
Interaction partners:
- MaoC-like domain-containing protein
- SCP2 domain-containing protein
- Non-specific lipid-transfer protein-like 2
- Acetyl-coenzyme A synthetase
- Acetyl-CoA C-acetyltransferase
- Probable 3-ketoacyl-CoA thiolase
- 3-ketoacyl-CoA thiolase
- Acetyl-CoA acetyltransferase homolog, mitochondrial
- Ethylmalonyl-CoA decarboxylase
- Enoyl-CoA Hydratase
Sequence:
MHLNTSICEVDNPDLTEEREKGTFDTDKMAAVIYGSEKLARRRREISEAVSKIPELADTQPFPFMDRLEKITEGSRKLEVLNNNIRDIIDYDDNGERLHIYQEVTGMEGHPLALHEVMFIPALVSQASKEQQEKWLGRARRREIIGCYAQTEMGHGTNLRKLETTATYFPDTQEFVLNTPTTTALKWWPGALGKSSNYAVVVVDMIIKGKSYGPHPFMVQLRDEKTHIPLKGIVVGDIGPKMSFNGGDNGFLGFDKFRVPRTNLLMRHVRVEADGTYVKPPHAKVNHSAMVHVRSHMATGQGALLAQALIIAVRYSAVRRQGFLENKTQEVKVLDYQTQQHRLFPSLARAYAFIFTGFETIHLYSQLLKDVDMGNTSGMADLHALTSGLKSVVTHQTGEGIEQARMACGGHGYSMASYISEIYGIAIGGCTYEGENMVMLLQLARYLVKSVELIKSGEAKKLGPMVSYLAAKGGHPDLSSLNGYVTAFEHMARRQAWKATEKFLKLMESGESREIAWNKSTVELTRASRLHTRLFIIEAFMRRVSRIEDIPVKEVLTDLLHLHVNYELLDVATYALEFMSSTQLDYIRDQLYLYLEKIRPSAVSLVDSFQISDMQLRSVLGRRDGNVYENLFKWAKSSPLNKSDVLPSVDKYLMPMMEKAKL
Protein: GTPase NRas (EC 3.6.5.2) (Transforming protein N-Ras) (P08556)
Organism: Mus musculus (Mouse)
Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P01111}; Lipid-anchor {ECO:0000250|UniProtKB:P01111}; Cytoplasmic side {ECO:0000250|UniProtKB:P01111}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P01111}; Lipid-anchor {ECO:0000250|UniProtKB:P01111}. Note=Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250|UniProtKB:P01111}.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Serine/threonine-protein kinase B-raf
- RAF proto-oncogene serine/threonine-protein kinase
- Neurofibromin
- Serine/threonine-protein kinase A-Raf
- Epidermal growth factor receptor
- Ral guanine nucleotide dissociation stimulator
- Dual specificity mitogen-activated protein kinase kinase 1
Sequence:
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRLKKLNSSDDGTQGCMGSPCVLM
Protein: Collagen type XI alpha 2 chain (A0A8I6A1U6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MERCSRCHRLLLLLPLVLGLSAAPGWAGAPSVDVLRALRFPSLPDGVRKSKGVCPADVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRSGLQAPLLTLYSAQGVQQLGLELGRPVRFLYEDQRGRPQASAQPIFRGLSLADGKWHHVAVAVKGQSVTLIVDCKKRVTRPLPRSVHPVLDTHGVVIFGAHVLDDEVFEGDVQELLIVPGVQAAYQSCGQKDLECEREQRDGPQTQKPHRAQRSPKKEPARLHKPQNQEPQQQPTESLYYDYEPPYYDVMTTETSPDYQVAHGPRGLKGEKGEPAVLEPGMFVEGPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPGTSLMLPFRFGSSGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGEPGVKGDRGFDGLPGLPGEKGQRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPHGPKGSLGPQGEPGPPGQQGTPGTQGLPGPQGAIGPHGEKGPRGKPGLPGMPGSDGLPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPTGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPPGPAGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGESGPMGERGHPGPPGPPGEQGLPGTAGKDGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPAGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPFGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPPGGVGNLGPPGEKGEPGESGSPGVQGEPGVKGPRGERGEKGESGQAGEAGPPGPKGPTGDDGPKGNPGPVGFPGDPGPPGEAGPRGQDGAKGSQGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGTPGPEGRQGEKGAKGDPGAVGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPTGEQGEKGDRGLPGPQGSPGQKGETGIPGASGPIGPGGPPGLPGPSGPKGAKGATGPAGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSKLMQDEEATPTGGAPGSPAGLEEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPTRRGGVLLGPVCFMG
Protein: RE09158p (Q86P15)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTSLVYTVFHLASLQCSVRPEISPCTCETGKAWNHVELSCEKLESFNAVVDSLANKLNADTNIDLKITHSQLDDLEMRSFTDMNFNLYKLRMQWNSLKSLPEVPFRGLSNVTYLSIGDNDLDEIPKHALSHMPSLLTLDIGRCKIRAVQQEDFRGIQRVTNLILVSNIITRLDRGSFPKSLLILHLGRNQLESLNGSLHDLHNLESLFINANNITSLDDELPDGGQLRLLMAHNNRLERLPANMAGMHSLETVHIHCNQLRSFDRVLRNAVNLSEVMADNNELEYLAQDEFASCSKVETLQMGCNHIKSLNYSLLPILKLKNANFSFNDIEEFSMAELHGLRSLKTLQLSSNRIQRLLPDPRGVQELMLVNLDLDNNRIDSLNGALAGLGNLRILNLAGNRLEHLQVGDFDGMIRLDILDLTGNQLAELKPLEMTLLPSLKILKVAYNNITKLEQDFKGLPVLCQANLTNNQISTISSELVTNTRCKNHNVPGKLEIHLDDNPIMCDVGLNELCRLMAVQEARIRGRSQCFENDQEVCTVLPMLYNVNLPIMVTNLKLTGREVPKPMVRVIVPSLIKANNELLPPLIATLGNPVLISTDLVNPVISPLPPPLLLATTTPPPPLPLPVESEVEKNESTTANPVPTNYTQETTTTTSTTTTTTTTETSSQVAPIEIITTTAPTTTTTSTTTPKPNETLPVIVELQDPNPPDTTVNQTALVPPVVLDPLQQDLERERERERERELERDLDHEAVAKTEYETVEYIPNLVQPPVGSDALTPPPSKANALEEDSESVHSNSVHAEYPHAAQSLQIPEEPPEE
Protein: Probable xyloglucan endotransglucosylase/hydrolase protein 17 (At-XTH17) (XTH-17) (EC 2.4.1.207) (O80803)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues.
Subcellular location: Secreted, cell wall {ECO:0000305}. Secreted, extracellular space, apoplast {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:24948835}.
Interaction partners:
- Protein DETOXIFICATION 13
- At1g12090/T28K15.14
Sequence:
MKLSCGTSFAFLLLFLLAAQSVHVYAGSFHKDVQIHWGDGRGKIHDRDGKLLSLSLDKSSGSGFQSNQEFLYGKAEVQMKLVPGNSAGTVTTFYLKSPGTTWDEIDFEFLGNISGHPYTLHTNVYTKGTGDKEQQFHLWFDPTVNFHTYCITWNPQRIIFTVDGIPIREFKNPEAIGVPFPTRQPMRLYASLWEAEHWATRGGLEKTDWSKAPFTAFYRNYNVDGCVWANGKSSCSANSPWFTQKLDSNGQTRMKGVQSKYMIYNYCTDKRRFPRGVPAECT
Protein: Glutamate receptor 3 (GluR-3) (AMPA-selective glutamate receptor 3) (GluR-C) (GluR-K3) (Glutamate receptor ionotropic, AMPA 3) (P19492)
Organism: Rattus norvegicus (Rat)
Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane {ECO:0000269|PubMed:25524891}; Multi-pass membrane protein. Postsynaptic density membrane {ECO:0000269|PubMed:25524891, ECO:0000305|PubMed:10027300}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 1
- Glutamate receptor 4
- Voltage-dependent calcium channel gamma-2 subunit
- PRKCA-binding protein
- Glutamate receptor-interacting protein 1
- Voltage-dependent calcium channel gamma-8 subunit
- Protein cornichon homolog 2
- Voltage-dependent calcium channel gamma-4 subunit
- Glutamate receptor ionotropic, NMDA 1
Sequence:
MGQSVLRAVFFLVLGLLGHSHGGFPNTISIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLSYYKWEKFVYLYDTERGFSVLQAIMEAAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFSDQQISNDSSSSENRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHLEDNNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMMVALIEFCYKSRAESKRMKLTKNTQNFKPAPATNTQNYATYREGYNVYGTESVKI