wanglab/gogpt-training-data huggingface dataset:
Protein: DnaJ homolog subfamily C member 5 (Ceroid-lipofuscinosis neuronal protein 4) (Cysteine string protein) (CSP) (Q9H3Z4)
Organism: Homo sapiens (Human)
Function: Acts as a general chaperone in regulated exocytosis (By similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By similarity). Involved in the calcium-mediated control of a late stage of exocytosis (By similarity). May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29455}. Membrane {ECO:0000250|UniProtKB:Q29455}; Lipid-anchor {ECO:0000250|UniProtKB:Q29455}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:Q29455}. Melanosome {ECO:0000269|PubMed:17081065}. Cell membrane {ECO:0000269|PubMed:21820099}. Note=The association with membranes is regulated by palmitoylation (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000250|UniProtKB:Q29455, ECO:0000269|PubMed:17081065}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Synaptotagmin-1
- Vesicle-associated membrane protein 2
- Ras-related protein Rab-3A
- Palmitoyl-protein thioesterase 1
- Battenin
- Vesicular inhibitory amino acid transporter
- Heat shock 70 kDa protein 4
- Synapsin-1
- Synaptophysin
Sequence:
MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVFCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN
Protein: Polybromo 1 (D3ZT52)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- AT-rich interactive domain-containing protein 2
- Bromodomain containing 7
- PHD finger protein 10
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- AT-rich interaction domain 1A
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1
- AT-rich interaction domain 1B
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1
Sequence:
MGSKRRRATSPSSSVSGDFDDGHHSVPTPGPSRKRRRLSSLPTVDPIAVCHELYNTIRDYKDEQGRLLCELFIRAPKRRNQPDYYEVVSQPIDLMKIQQKLKMEEYDDINLLTADFQLLFNNAKAYYKPDSPEYKAACKLWDLYLRTRNEFVQKGEADDEDDDEDGQDNQGTMADGSSPGYLKEILEQLLEAIVVATNPSGRLISELFQKLPSKVQYPDYYAIIKEPIDLKTIAQRIQNGSYKSIHAMAKDIDLLAKNAKTYNEPGSQVFKDANSIKKIFYMKKAEIEHHEMTKSSLRIRTATNLAAARLTGPSHNKSSLDEERNPTSKCYRNKRAVQGGRLSAITMALQYGSESEEDAALAAARYEEGESEAESITSFMDVSNPFHQLYDTVRSCRNNQGQLIAEPFFHLPSKKKYPDYYQQIKMPISLQQIRTKLKNQEYETLDHLECDLNLMFENAKRYNVPNSAIYKRVLKLQQVMQAKKKELARRDDIEDGDSMISSATSDTGSAKRKRNTHDSEMLGLRRLSSKKNIRKQRMKILFNVVLEAREPGSGRRLCDLFMVKPSKKDYPDYYKIILEPMDLKIIEHNIRNDKYAGEEGMMEDMKLMFRNARHYNEEGSQVYNDAHILEKLLKDKRKELGPLPDDDDMASPKLKLSRKSGVSPKKSKYMTPMQQKLNEVYEAVKNYTDKRGRRLSAIFLRLPSRSELPDYYLTIKKPMDMEKIRSHMMANKYQDIDSMVEDFVMMFNNACTYNEPESLIYKDALVLHKVLLETRRDLEGDEDSHVPNVTLLIQELIHNLFVSVMSHQDDEGRCYSDSLAEIPAVDPNFPSRPPLTFDIIRKNVESNRYRRLDLFQEHMFEVLERARRMNRTDSEIYEDAVELQQFFIRIRDELCKNGEILLSPALSYTTKHLHNDVEKEKKEKLPKEIEEDKLKREEEKREAEKSEDSSGTTGLSGLHRTYSQDCSFKNSMYHVGDYVYVEPAEANLQPHIVCIERLWEDSAGEKWLYGCWFYRPNETFHLATRKFLEKEVFKSDYYNKVPVSKILGKCVVMFVKEYFKLCPETFRDEDVFVCESRYSAKTKSFKKIKLWTMPISSVRFVPRDVPLPVVRVASVFANADKGDEEKSTDNSDDNRAEDSFNLEKEKEDVPVEMSNGEPGCHYFEQLRYNDMWLKVGDCVFIKSHGLVRPRVGRIEKVWVRDGAAYFYGPIFIHPEETEHEPTKMFYKKEVFLSNLEETCPMSCILGKCAVLSFKDFLSCRPTEIPENDILLCESRYNESDKQMKKFKGLKRFSLSAKVVDDEIYYFRKPIIPQKEPSPLLEKKIQLLEAKFAELEGGDDDTEEMGEEDSEVIEPPSLPQLQTPLANELDLMPYTPPQSTPKSAKGSAKKESSKRKINMSGYILFSSEMRAVIKAQHPDYSFGELSRLVGTEWRNLETAKKAEYEERAAKAAEQQERERAAQQQQPSASPRAGTPVGALMGVVPPPTPMGMLNQQLTPVAGVMNQGVTPMVGTPAPGGSPYGQQVGVLGPPGQQAPPPYPGPHPTGPPVIQQPTTPMFVAPPPKTQRLLHSEAYLKYIEGLSAESNSISKWDQTLAARRRDVHLSKEQESRLPSHWLKSKGAHTTMADALWRLRDLMLRDTLNIRQAYNLENV
Protein: ATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit) (F-ATPase epsilon subunit) (P0A6E6)
Organism: Escherichia coli (strain K12)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229}; Peripheral membrane protein {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229}.
Interaction partners:
- ATP synthase subunit beta
- ATP synthase subunit a
- ATP synthase subunit c
- ATP synthase subunit alpha
- ATP synthase subunit delta
- ATP synthase gamma chain
- ATP synthase subunit b
- NADH-quinone oxidoreductase subunit C/D
- Type 1 fimbrin D-mannose specific adhesin
- Uncharacterized fimbrial-like protein SfmH
Sequence:
MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGNVTVLADTAIRGQDLDEARAMEAKRKAEEHISSSHGDVDYAQASAELAKAIAQLRVIELTKKAM
Protein: Acetylxylan esterase (EC 3.1.1.72) (Acetyl-xylooligosaccharide esterase) (Q09LX1)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: Acetylxylan esterase involved in the degradation of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Cleaves acetyl side groups from the xylose backbone units of the hemicellulolytic polymer xylan and xylo-oligosaccharides. Hydrolyzes about 20%-30% of the available acetyl groups on fully acetylated birch wood xylan. Completely deacetylates xylobiose peracetate (fully acetylated), and is active on both the alpha- and beta-forms of the sugar. Also hydrolyzes fully acetylated methyl-beta-D-xylopyranoside and methyl-beta-D-glucopyranoside, and the synthetic substrates 2-naphthyl acetate, 4-nitrophenyl acetate, 4-methylumbelliferyl acetate, and phenyl acetate.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:21994937}.
Interaction partners:
Sequence:
MKIGSGEKLLFIGDSITDCGRARPEGEGSFGALGTGYVAYVVGLLQAVYPELGIRVVNKGISGNTVRDLKARWEEDVIAQKPDWVSIMIGINDVWRQYDLPFMKEKHVYLDEYEATLRSLVLETKPLVKGIILMTPFYIEGNEQDPMRRTMDQYGRVVKQIAEETNSLFVDTQAAFNEVLKTLYPAALAWDRVHPSVAGHMILARAFLREIGFEWVRSR
Protein: Ent-copalyl diphosphate synthase (Ent-CDP synthase) (EC 5.5.1.13) (Q5KSN5)
Organism: Streptomyces sp. (strain KO-3988)
Function: Involved in viguiepinol biosynthesis. Catalyzes the conversion of geranylgeranyl diphosphate (GGDP) into copalyl diphosphate (ent-CDP).
Interaction partners:
Sequence:
MNVTSFAALRAAAQDIVDEMIADPYGLTSPSVYETARMVVSAPWLEGHRQRVEFLLAQQHEDGTWGGPAAYGLLPTLSAVDALLSVAGTQDARRVAGAVESGLAALAGRFPRNVELPDTIAVELLVPWLIEQVDQRLSRMDDRGDLPGRLDLQADTGTLSGIRELLRQNTGIPEKTWHSLEALGAPAVRSGTVTPMGGAVGASPAATSAWLGDPPHTDAAKACLAYLHQTQARHGGPVSGITSISYFELAWVVTALSGSGLDVDIPAQVPDILRTALGANGLSAGPGLPADSDDTSAALHALDLLGKPESVDCLWEYDTGLYFTCFPKERTPSTSTNAHILVALADRRGQGDTRYDHAAERVGGWLVEQQQPDGRWMDKWHASPYYATACGAAAMARLDGPRTSAALDDAIRWVLDTQHADGSWGRWEGTGEETAYALQVLNHRAAPDRPALEAIRAGRAFLSGHVEDDRRNPPLWHDKDLYTPVRVIRAEILGTLAATQRLAEAEKEARA
Protein: Bucky ball (buc) (Prion-like protein Bucky ball) (H0WFA5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Prion-like protein required for the formation of Balbiani body (electron-dense aggregates in the oocyte) and germ plasm assembly, and for the establishment of oocyte polarity during early oogenesis. Mobility and aggregation properties are improved by tudor domain-containing protein tdrd6 through interaction with dimethylated arginines Tri-RG domains. Establishes oocyte polarity through interactions with RNA-binding proteins rbpms2 and dazl, initiating a positive feedback loop amplification mechanism in the Balbiani body. Interaction of BUC protein and mRNA with rbpms2 and dazl is required to mediate Balbiani body formation. Involved in recruitment of germ plasm to embryonic cleavage furrows and dorsoventral patterning through interaction with Kinesin-1/KIF5BA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19249209, ECO:0000269|PubMed:30086300}. Cleavage furrow {ECO:0000269|PubMed:26253407}. Note=Localizes to nuage (a peri-nuclear protein-RNA aggregate that associates closely with mitochondria), the Balbiani body during oogenesis, and in the germ plasm upon fertilization (PubMed:19249209, PubMed:30086300). Accumulates at embryonic cleavage furrows (PubMed:26253407). {ECO:0000269|PubMed:19249209, ECO:0000269|PubMed:26253407, ECO:0000269|PubMed:30086300}.
Interaction partners:
- Deleted in azoospermia-like
- Tudor domain-containing 6
- Microtubule actin crosslinking factor 1a.
- Nanos homolog 3
- Kinesin-like protein
- DAZ-associated protein 2.
- Nanos homolog 1
- Dead end protein 1
- Meiosis expressed gene 1 protein homolog
- RNA binding protein
Sequence:
MEGINNNSQPMGVGQPHHPVNHTRPFFYVQPPSQPYFMYQWPMNPYGHYGFPGPALHFGRPYMAPYQFMQYPGYVIPHAPMQPIDYRRINPHYPSVASYDLRVRHHFQNAGMHRETACSEVQTDPSDSVNKLIDKIESLKACELGSDKGPNNVVSSTPDVVQGEKLTRLNEDSNLEVATKECKEDPVTRPTTYSDSAYDAESSQGRLDECVFSDVLPLDSSSVHEEEEEEEKDVNEEDEPQTVADEICSQNEMSASTTSNVFCSGVQSIADPTECHDLEKLGDEQKQDIPSADAAAVIEPLISLSEDFDLPYQILRLPCNKTTTGLSLEREIDPLVYFDSPSTLLPPQNYLSSIGSAYSYSYYPQVTQERQSVLSPSIDELSSRDEMFSTDVEDLEVVPGHVYVGGGRLAEASDMPVRSRKELPSVDKTCSVCQKTCACCGSTLQDEVGMCKMAEHSHPERDEMSDQDCDYDLEAEVRSNCESPRVSKRKCCSRHALPSCGHHCAKHRHRKLLCEGQESCDLREQARVHPKGECCEEYGALAKADKRIQKGALCRPCIEQQWREGVVSDQENWASCGAKPRSWRQVTGPQDQGRTPLRRSTCKSIHQQRPRSEYNDYDETEFTYCQRGRGSMKKRGSRY
Protein: Transketolase (TK) (EC 2.2.1.1) (P50137)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Interaction partners:
- Transaldolase
- Glucose-6-phosphate isomerase
- ribulose-phosphate 3-epimerase
- Ribose-5-phosphate isomerase
- Fructose-1,6-bisphosphatase isozyme 2
- Fructose-1,6-bisphosphatase 1
- Ribokinase
- Fructose-bisphosphate aldolase A
- Ribose-phosphate pyrophosphokinase 1
- ATP-dependent 6-phosphofructokinase, muscle type
Sequence:
MEGYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDVYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQIIQEIYSQVQSKKKILATPPQEDAPSVDIANIRMPTPPNYKVGDKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYSNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATKGRILTVEDHYYEGGIGEAVSAVVVGEPGVTVTRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVKGLVTKG
Protein: Nitrilase and fragile histidine triad fusion protein NitFhit [Includes: Bis(5'-adenosyl)-triphosphatase (EC 3.6.1.29) (AP3A hydrolase) (AP3Aase) (Diadenosine 5',5'''-P1,P3-triphosphate hydrolase) (Dinucleosidetriphosphatase); Nitrilase homolog (EC 3.5.-.-)] (O76463)
Organism: Caenorhabditis elegans
Function: Cleaves A-5'-PPP-5'A to yield AMP and ADP.
Interaction partners:
- PABS domain-containing protein
- GrpE protein homolog
- Acyl-CoA dehydrogenase family member 11
- Adenylosuccinate lyase
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- NAD-capped RNA hydrolase ndx-9
- JmjC domain-containing protein
- Alanine--glyoxylate aminotransferase
- Trifunctional purine biosynthetic protein adenosine-3
- 5-oxoprolinase
Sequence:
MLSTVFRRTMATGRHFIAVCQMTSDNDLEKNFQAAKNMIERAGEKKCEMVFLPECFDFIGLNKNEQIDLAMATDCEYMEKYRELARKHNIWLSLGGLHHKDPSDAAHPWNTHLIIDSDGVTRAEYNKLHLFDLEIPGKVRLMESEFSKAGTEMIPPVDTPIGRLGLSICYDVRFPELSLWNRKRGAQLLSFPSAFTLNTGLAHWETLLRARAIENQCYVVAAAQTGAHNPKRQSYGHSMVVDPWGAVVAQCSERVDMCFAEIDLSYVDTLREMQPVFSHRRSDLYTLHINEKSSETGGLKFARFNIPADHIFYSTPHSFVFVNLKPVTDGHVLVSPKRVVPRLTDLTDAETADLFIVAKKVQAMLEKHHNVTSTTICVQDGKDAGQTVPHVHIHILPRRAGDFGDNEIYQKLASHDKEPERKPRSNEQMAEEAVVYRNLM
Protein: Uncharacterized protein (Q57Z39)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L10, putative
- Histone-binding protein RBBP4-like N-terminal domain-containing protein
- U3 small nucleolar RNA-associated protein 13 C-terminal domain-containing protein
- Nucleotide exchange factor Fes1 domain-containing protein
- NLE domain-containing protein
Sequence:
MTFLPVFFSILFLLATKKENCLFWGEKLSLQQLKMQRPLTAGNLPEQTMRDGIVDPEMAQDAFIDLDDPNNEIVDEDNMAEIEEDDDNVAYNVPAHGSRKRMAETDLNNGEEDNYDDDGVGNGAGTDGEEDDADVEDLNEVPDCEPERDDALCFFTARDASPVHAVAVHPADSGLFVAGGQSDEVYVLKLDEESRSVHNLAVLREAHADTISILAFSPDGTTLASGGLDGVVAIWCTVTWKLRHALRDLSGELLTLLWHPSGLVLVAGADDGQAAMWNVSKGTLAMYFAGHGGGITCTAWTPCRKRLVAGASDGAVVVFAPRTGQQEFHIAKGLSADRASVTTLCCLGDSSGEAPLGDYDDRCVVGCADGTLHVISLNSGRVVTSLPEVHTQAIESLHVNVGSRGSHTTPPQLLLSASCDCRVAVWSAADLKLRTVFQVGESVIPAAWASGYFVVAGCSDGEIKVWDGRSQQQEPLVRLMGHRRMVLSFAIVESSGVVASTSDDGTVRFFKLSL
Protein: Nucleobindin-2 (DNA-binding protein NEFA) (Prepronesfatin) [Cleaved into: Nesfatin-1] (P81117)
Organism: Mus musculus (Mouse)
Function: Calcium-binding protein which may have a role in calcium homeostasis. Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein (G-protein) alpha subunit GNAI3 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10915798}. Perikaryon {ECO:0000269|PubMed:10915798}. Endoplasmic reticulum {ECO:0000269|PubMed:10915798}. Golgi apparatus {ECO:0000250}. Nucleus envelope {ECO:0000269|PubMed:10915798}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000269|PubMed:10915798}. Note=In dendrites and perikarya of brain neurons. Abundant in the ER cisternae and nuclear envelope, but not detected in Golgi, mitochondria or nucleoplasm in neurons. In cell culture, cytoplasmic and secreted.; SUBCELLULAR LOCATION: [Nesfatin-1]: Secreted {ECO:0000250}.
Interaction partners:
- Appetite-regulating hormone
Sequence:
MRWRIIQVQYCFLLVPCMLTALEAVPIDVDKTKVHNTEPVENARIEPPDTGLYYDEYLKQVIEVLETDPHFREKLQKADIEEIRSGRLSQELDLVSHKVRTRLDELKRQEVGRLRMLIKAKLDALQDTGMNHHLLLKQFEHLNHQNPNTFESRDLDMLIKAATADLEQYDRTRHEEFKKYEMMKEHERREYLKTLSEEKRKEEESKFEEMKRKHEDHPKVNHPGSKDQLKEVWEETDGLDPNDFDPKTFFKLHDVNNDGFLDEQELEALFTRELEKVYNPQNAEDDMIEMEEERLRMREHVMSEIDNNKDRLVTLEEFLRATEKKEFLEPDSWETLDQQQLFTEDELKEYESIIAIQENELKKRAEELQKQKEDLQRQHDHLEAQKQEYHQAVQHLEQKKLQQGIAPSGPAGELKFEPHT
Protein: DEAD-box ATP-dependent RNA helicase 36 (EC 3.6.4.13) (Q9SA27)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Nucleolar protein
- Protein NUCLEOLAR FACTOR 1
- At3g56510 family protein)
- rRNA biogenesis protein RRP5
- F18K10.11 protein
- Protein THALLO
- Something about silencing protein
- ATP-dependent RNA helicase DEAH13
- At3g57000
- KRR1 small subunit processome component
Sequence:
MEEPTPEEEGGITIMSKSRKNPKTVVNIQSQKLDSDQNTPQFEKFTNPNPSSDTTSATNFEGLGLAEWAVETCKELGMRKPTPVQTHCVPKILAGRDVLGLAQTGSGKTAAFALPILHRLAEDPYGVFALVVTPTRELAFQLAEQFKALGSCLNLRCSVIVGGMDMLTQTMSLVSRPHIVITTPGRIKVLLENNPDVPPVFSRTKFLVLDEADRVLDVGFQDELRTIFQCLPKSRQTLLFSATMTSNLQALLEHSSNKAYFYEAYEGLKTVDTLTQQFIFEDKDAKELYLVHILSQMEDKGIRSAMIFVSTCRTCQRLSLMLDELEVENIAMHSLNSQSMRLSALSKFKSGKVPILLATDVASRGLDIPTVDLVINYDIPRDPRDYVHRVGRTARAGRGGLAVSIITETDVKLIHKIEEEVGKKMEPYNKKVITDSLEVTKVSKAKRVAMMKMLDNGFEDKVKDRRKLKRKTLADKGLLKKRGKRQKSTEN
Protein: Glyoxalase 3 (EC 4.2.1.130) (Glutathione-independent glyoxalase) (Q5AF03)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. Selective for MG, does not use glyoxal as substrate. Plays a role in detoxifying endogenously produced MG, particularly when glycerol is the principal carbon source. Important for viability in stationary phase (By similarity).
Interaction partners:
- Lactoylglutathione lyase
- hydroxyacylglutathione hydrolase
- Tropomyosin
- Nuclear control of ATPase protein 2
- Gre2p
- Methylglyoxal reductase
- Putative NADPH-dependent methylglyoxal reductase GRP2
- D-2-hydroxyglutarate dehydrogenase, mitochondrial
- D-lactate dehydrogenase
- NAD-dependent epimerase/dehydratase domain-containing protein
Sequence:
MVKVLLALTSYNETFYSDGKKTGVFVVEALHPFEVFRKKGYEIQLASETGTFGWDDHSVVPDFLNGEDKEIFDNVNSEFNVALKNLKKASDLDPNDYDIFFGSAGHGTLFDYPNAKDLQKIATTVYDKGGVVSAVCHGPAIFENLNDPKTGEPLIKGKKITGFTDIGEDILGVTDIMKKGNLLTIKQVAEKEGATYIEPEGPWDNFTVTDGRIVTGVNPQSAVKTAEDVIAAFECN
Protein: Leucine--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) (Protein EMBRYO DEFECTIVE 2369) (Q9XEA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16251277}. Mitochondrion {ECO:0000250|UniProtKB:Q8RXK8}.
Interaction partners:
- Lysine--tRNA ligase, chloroplastic/mitochondrial
- Arginine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, chloroplastic/mitochondrial
- Lysine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, chloroplastic/mitochondrial
- Methionine-tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, chloroplastic/mitochondrial
- Glutamate--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MSSHHQILQIRSDPFVLSHCCRHTRLTSSLTLQSPLKQPFSCLPFRWRRSYRGGVRSSTTETHGSKKEALVSETATTSIELKRVYPFHEIEPKWQRYWEDNRIFRTPDDVDTSKPKFYVLDMFPYPSGAGLHVGHPLGYTATDILARLRRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKTTTLKNIDRFRLQLKSLGFSYDWDRELSTTEPDYYKWTQWIFLQLYKKGLAYQAEVPVNWCPALGTVLANEEVVDGVSERGGHPVIRKPMRQWMLKITAYADRLLEDLDELEWPESIKEMQRNWIGRSEGAELNFSILDGEGRETDKEITVYTTRPDTLFGATYMVVAPEHQLLSYFVTAEQKQQVEEYKDFASRKSDLERTELQKDKTGVFTGCYAKNPANGDAIPIWVADYVLASYGTGAIMAVPAHDTRDNEFALKYNIPIKWVVRNEANSSDDAKQVYPGLGIIENSSTLETGLDINQLSSKEAALKVIEWAERTGNGKKKVNYKLRDWLFARQRYWGEPIPILILDESGETIAISESELPLTLPELNDFTPTGTGEPPLSKAVSWVNTVDPSTGKPAKRETSTMPQWAGSCWYYLRFMDPKNPEALVDKEKEKYWSPVDVYVGGAEHAVLHLLYSRFWHKVLYDIGVVSTKEPFKCVINQGIILGEVQYTAWKDQEGNYVSADTEERLNEHQQVTIPEEKVIKSGDHFVLKEDPSIRLIPRVYKMSKSRGNVVNPDDVVLEYGADSLRLYEMFMGPFRDSKTWNTSGIEGVHRFLARTWRLVIGLPQSDGSFKDGTLVTDDEPTLEQLRTLHKCIAKVTEEIESTRFNTGISGMMEFVNAAYKWNNQPRGIIEPFVLLLSPYAPHMAEELWSRLGHPNSLAYESFPKANPDYLKNTTIVLPVQINGKTRGTIEVEEGCSEDDAFVLASQDDKLRKYLDGQSIKKRIYVPGKILNVILDRTNVKVTTK
Protein: Rifin (Q8I1V4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYFKILLLFAHPLNILLLSSSHVHNKKNPYIITSHTPSQESLKTCRSLCECDLYTSIYDNDPEMQKVIQEFDNRTSQRFEEYDRRMVKNRQKCKERCDKEIEQIILKDKIEKELTEKLGALQTEIQSDAVPTCTCQKSVADKVEKTCLKCGSVLGGGIAPGWGLVSGIGYSTWTHYVATTVAKAATDAGIKEATEALGRIYTLNEVTVINWTSKITATNYYKPMELVEIVNGVNNMCGETGVAGNTSFCLAAESIKPSDVFTRIISRQAQEAATYAASKAKDVTTAEFANSASSTATLTNTIIASVVAILVIVLVMIIIYLILRYRRKTKMKKKLQYIKLLNE
Protein: BRCT domain-containing protein (Q38E24)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPVTKPREMKTSAARRVIDPIDSTVATSGWTCTNCSVEVPKEEAFCKICSFARPMDRHGVPQIFTDLTITFNGIIPRSVKHQSHSVEWRMAERHGATCMVELDFGRVNVLVYRPGYERSEKVRKCVEAGRGVFVVPITWMLDCLLQSRQIHPSLFHLAAIPLVPQPTVKGMDLPHHHHPYYVMNVKEYTLAAAGRAVADGAIAAREVVTSPENMKLPPTFQIPELRYTNIDIYEAVCSAAGEGRLVEKEDEHSDDVREGRNRATDIEVFKGDQRNNRVNNALFSGIKFLLTPVLESNPLVVKALVACGGRVIISSHGKLGELLRNSTTHVLYDHSEKKCPILIEAAHVKKTVPGLILVQSNWAEDCMIFKELIPPYGPYAPSAKLMETLEKKYKKRAAA
Protein: Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5) (Q8AWE7)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000256|HAMAP-Rule:MF_03205}.
Interaction partners:
- Elongation of very long chain fatty acids protein 2
- Elongation of very long chain fatty acids protein 5
- 3-ketoacyl-CoA reductase
- Very-long-chain 3-oxoacyl-CoA reductase-like isoform X1
- Estradiol 17-beta-dehydrogenase 12-B
- hydroxymethylglutaryl-CoA lyase
- Delta-6 fatty acyl desaturase
Sequence:
METFNYKLNMYIDSWMGPRDERVQGWLLLDNYPPTFALTVMYLLIVWLGPKYMRHRQPVSCRGLLLVYNLGLTILSFYMFYEMVSAVWHGDYNFYCQDTHSAGETDTKIINVLWWYYFSKLIEFMDTFFFILRKNNHQITFLHIYHHASMLNIWWFVMNWVPCGHSYFGASLNSFIHVLMYSYYGLSAVPALRPYLWWKKYITQGQLIQFFLTMSQTICAVIWPCGFPRGWLYFQIFYVVTLIALFSNFYIQTYKKHLVSQKKECHQNGSVASLNGHVNGVTPTETITHRKVRGD
Protein: Dishevelled, dsh homolog 2 (Drosophila) (Segment polarity protein dishevelled homolog DVL-2) (Q803Q5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAETKIIYHIDEEETPYLVKIPIAAEKITLLDFKQVLNKPNYKFFFKSMDQDFGVVKEEISDDSAKLPCFNGRVVSWLVSSDTPAAEPVAPPVEVPSQPSPPPPPLPPPPAERMAGIGDSRPPSFHPNTTGSLESLDDQTETESVVSFRRERPRPRESLEQHGPRMNGQSHLDRHLAGYESATTVMSSELDTTSFCDSDDDDTMSRFSSSTEQSTASRLLKRHRRRRKQRPRLERASSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDINFENMSNDDAVRVLREIVHKPGPITLTVAKCWDPSPQGYFTLPRNEPIRPIDPAAWVNHSVALTGAFPSYPSSTITSSSSVTETERFDEFNLSLRSDMASVAKAMASPESGLEVRDRMWLKITIPNAFLGSDVVEWLYHHIDGFQDRREARKYACNLLKAGFIRHTVNKITFSEQCYYIFGDFSNCENYMANLSLNDNDGSSGASDQDTLAPLPLPGATPWPLLHSFTYQYPHPYSTQPPPYHELSNYSYGPGSAGSQHSEGSHSSGSTRSDGEKRRGPKSVSESTVGGSVRDDKSPGGGGADSRSGSGSESDYSVRSTLRRDHGSATPSEHSRSSQRSHHRVPPPHLAPYPPGIPIPYNPMMVMMVPQHPHLALGAPHPQTPTLPPHPGLPPTGIPGGPPGAPPTRDLGSVPPELTASRQSFHLAMGNPSEFFVDVM
Protein: Calmodulin-like protein 3 (CaM-like protein) (CLP) (Calmodulin-related protein NB-1) (P27482)
Organism: Homo sapiens (Human)
Function: May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Nitric oxide synthase 3
- Ryanodine receptor 2
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Ryanodine receptor 1
- Nitric oxide synthase 1
- Calcium/calmodulin-dependent protein kinase kinase 2
- Calcium/calmodulin-dependent protein kinase type IV
- GTPase KRas
- Myosin light chain kinase, smooth muscle
Sequence:
MADQLTEEQVTEFKEAFSLFDKDGDGCITTRELGTVMRSLGQNPTEAELRDMMSEIDRDGNGTVDFPEFLGMMARKMKDTDNEEEIREAFRVFDKDGNGFVSAAELRHVMTRLGEKLSDEEVDEMIRAADTDGDGQVNYEEFVRVLVSK
Protein: Nociceptin receptor (Kappa-type 3 opioid receptor) (Orphanin FQ receptor) (Q7T3Q4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}.
Interaction partners:
- Prepronociceptin a.
- Proenkephalin a
- Pro-opiomelanocortin protein
- Proenkephalin b.
- Prodynorphin.
Sequence:
MEFPNDSIGFTDPRHFHLYNESLFQNNFSTFNESDSFFPKGFKITIAVVYMIVCVVGLVGNCLVMYVIIRYTKMKTATNIYIFNLALADALVLATLPFQGTDVFLGFWPFGNALCKVVVSIDYYNMFTSVFTLTVMSMDRYVAVCHPVKALDMRTPHKAKVVNICVWVLASAIGVPAMVLGDVEQDNGESIECILVLPDPRSYWDPVFGTCVFLLSFLIPVAIISVCYSLMVKRLRSVRILSGSKEKDRNLRRITRMVLVVVAAFVVCWTPIQIMALAQSLGFNLASVQTVVFMHFCIALGYVNSSLNPVLYAFLDENFKRCFREFCHPSRFGIDAQQSGRMRHITREVAFNCKTTDGNSNPA