wanglab/gogpt-training-data huggingface dataset:
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 (Complex I-B18) (CI-B18) (NADH-ubiquinone oxidoreductase B18 subunit) (Q9CR61)
Organism: Mus musculus (Mouse)
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 inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}. Mitochondrion intermembrane space {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH-ubiquinone oxidoreductase chain 5
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
Sequence:
MGAHLTRRYLWDASVEPDPEKIPSFPPDLGFPERKERVMVATQQEMMDAQLTLQQRDYCAHYLIRLLKCKRDSFPNFLACKHEQHDWDYCEHLDYVKRMKEFERERRLLQRKKRRALKEARVAQGQGEGEVGPEVAL
Protein: Protein 4.1 (Band 4.1) (Erythrocyte membrane protein band 4.1) (A0A2R8Y7Y3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEIADE
Protein: Large ribosomal subunit protein uL22m (54S ribosomal protein L22, mitochondrial) (P53881)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL32m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS15m
Sequence:
MNFHTARISQVGVISRALLSSVSRRWIHVTPISLNNSGGSLFGSITENKPKEGKNRGDEDAGSFSNRLAIASDSSGEAPEVNRDSITIENDKLLQQHIISLQQPEQLASQSLLSPLKREIYEANCKINGGFYKKDTIVKLPNSSERYKLKLTKREIEVLEPSVYAQSYRIKSSMKKATLLLRLLGGLDVMKAISQCHFSNKKIAREVAELLQKGVKDGQKLGLKPEDLYISQIWTGSDGFWRKRVEFKARTRIGIISHPYIHVRCILRTKSVTKRRLAYEAHLKEQKRAPWVQLGDKPIRGVTGGVYKW
Protein: Nosiheptide precursor [Cleaved into: Nosiheptide (NOS) (Antibiotic 9671-RP) (Multhiomycin)] (C6FX52)
Organism: Streptomyces actuosus
Function: Inhibits bacterial protein biosynthesis by binding to ribosomes. Specifically, binds to the complex of 23S rRNA and ribosomal protein L11 (RPLK) in the 50S ribosomal subunit. While allowing a weak binding of elongation factor G (EF-G) to the ribosome and subsequent GTP-hydrolysis, probably impairs conformational changes in both the ribosome and EF-G which are necessary for translocation. In vitro, inhibits Gram-positive bacteria S.aureus strain 209P (MIC=0.0009 ug/ml), S.aureus strain 133 (MIC=0.0019 ug/ml), S.aureus strain B3 (MIC=0.003 ug/ml), S.aureus strain Hb (MIC=0.003 ug/ml), M.citreus strain ATCC 8411 (MIC=0.0038 ug/ml), M.lysodeikticus strain ATCC 4698 (MIC=0.003 ug/ml), S.lutea strain ATCC 9341 (MIC=0.0011 ug/ml), S.faecalis strain ATCC 9790 (MIC=0.0007 ug/ml), S.viridans (MIC=0.0065 ug/ml), S.pyogenes hemolyticus strain Dig7 (MIC=0.00028 ug/ml), D.pneumoniae strain Til (MIC=0.00015 ug/ml), N.catrrhalis (MIC=0.0017 ug/ml), L.casei strain ATCC 6633 (MIC=0.003 ug/ml), B.cereus strain ATCC 6630 (MIC=0.0071 ug/ml) and various isolates of L.monocytogenes. In vitro, inhibits Gram-negative bacterium P.multocida strain A125 (MIC=0.0024 ug/ml) but not M.smegmatis strain ATCC 6630, S.typhimurium, A.aerogenes strain ATCC 8308, P.vulgaris, K.pneumoniae strain ATCC 10031, S.marcescens strain A476, P.aeruginosa strain Bass or B.bronchiseptica strain CN387. Does not inhibit Gram-negative bacterium E.coli strain ATCC 9637 but does inhibit purified ribosomes from E.coli. In vivo, has no systemic effect in mice infected with staphylococci or streptococci when applied orally or subcutaneously. Has a local effect in mice infected subcutaneously or intraperitoneally with staphylococci when applied immediately afterwards. Is not toxic to mice.
Interaction partners:
Sequence:
MDAAHLSDLDIDALEISEFLDESRLEDSEVVAKVMSASCTTCECCCSCSS
Protein: Sorting nexin-12 (Q9USN1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Meiotically up-regulated gene 122 protein
- PXA domain protein 1
- PX domain-containing protein C1450.12
- tRNA
- Uncharacterized protein C663.15c
Sequence:
MYQQHIFYFITGGIFILWILAHSFFVKIIYLWASGCLLWYCLETRTFENKNNLGTSEPFLVNPAIFQKRARQLALSKLLLRQPLYPGIPEISEEIESIISHFMQKYIKVWSYQIIPEPTISNSIESHLRKCLMVLLSRVDEIDLADVLVKTVLPLITKHLRLFVEAEQLVVGNKAVSFTDHSELSREVAAKYDHGRLHEAVLLSGNPMVAQKRYLRNWTTQVLSIILPNYYETSPLVLSLVTEVIINTTLLPLVSYISDPDFFNYLIIQASGSIIQRRRKIRRLKRAIRKQSNHFQVGARRLRLKDSQHSFEQYIHEIKKISNISDARRLRSELMVQRRQLEQTEAFDFEFKQYRERLQIAIITAEKRISLLSGTPFQHKEAVLFEQVQSLLQILSDSAAVSCFLEFMERKNRSRYLHFWLVVEGLKESQDDPLNAHMIAPFSDIVSDHTDFTAIVKSYFESVDNPLDIPKPLTNTINKFVNQSKDNLNPDLWVEARNAMLMAQEHVFDIMQNSDYSEFVNSEIYYRFLAQDVVSDHKSTNSSATFSRLEELGENIPAISKQPSYLSISSSSKSINSSPSPSIQLSVSSSISRDKNLSPLDLELDDPTYSDEEEVLFAPPGDLQLSESIDELNNNIEELKAQLNAINTLIKKAELVADQKQLKSLTKNHQEIEKAIHRKERQRDQYMSQEEDSKLFNRSRVSIDSFKISKEENTPDFAVYTIRIERLENGHVRSGWMVARRYREFAELHKQLKQTYPGVRSLKFPQKSIITSLNKNVLEYRRGALEEYLQSLFRMPEVCDSKMLRMFLSQQNITAPQMFNPKEVGKKWKQLLEVLGFEVNNSFNASNVNTNSSFSGPISEFLVELFSPNDDAKQQWLPKKTYISILEQLFGGALEKRIRLQLFQLFTPEKIYRKLREFRRGLEGKSNHDHSKDRRHSRARKPAYADRNQLKAEAGILLASMFPGYTPDIAVKRIFRILQNQSLNAHVIYTLLDEILLALKKHARSTNKAT
Protein: Histone H3 methyltransferase DOT1 variant a (Q6XZL7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
GASAHGAGGAGAGSRSLAVAPTGFYAGSVAISGALASSPAPLASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHQLTASPRLSVTTQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSPLNLNSMVSNINQPLEITAISSPESSLKSSPTPYQDHDQPPVLRKERPLGLTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLVGRKSAPSSEPINSSKWKSTFSPISDLGLAKAVDSPLQAGSALSHSPLFSFRPSLEEPAAEAKLPTHPRKSFAGSLGAAEGPSPGTNPPNGLAFSGGLAADLGLHSFNDGASLSHKGPDVTGLSASLSFPSQRGKDSTTEANPFLSRRQPEGLGGLKGEGNANKESGESLPLCGPSDKASLPHGSRASKGRDRELDFKGGHNLFISAAAVPPGGLLGGPGLVTVASSAGSATPTAQAPRPFLSTFAPGPQFTLGPMSLQANLGSVAGSSVLQSLFSTVPAAAGLVHVSSTATRLTNSHTMGSFSSGVAGGTVGGN
Protein: Proteasome inhibitor PI31 subunit (Q5QPM9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGLEVLFASAAPAITCRQDALVCFLHWEVVTHGYFGLGVGDQPGPNDKKSELLPAGWNNNKDLYVLRYEYKDGSRKLLVKAITVESSMILNVLEYGSQQVADLTLNLDDYIDAEHLGDFHRTYKNSEELRSRIVSGIITPIHEQWEKANVSSPHREFPPATAREVDPLRIPPHHPHTSRQPP
Protein: Heat shock protein 101 (Q8IIJ8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Exported protein 2
- Translocon component PTEX150
- Thioredoxin 2
- Endoplasmic reticulum chaperone GRP170
- Endoplasmic reticulum chaperone BIP
- Heat shock 70 kDa protein
- Heat shock protein 70
- Translocon component PTEX88
- Heptatricopeptide repeat-containing protein
- ATP-dependent Clp protease proteolytic subunit
Sequence:
MTRRYLKYYIFVTLLFFVQVINNVLCAPDNKQEQGKYLNRTINILNAGKNIAKSYGHNKLKPIHILSALAKSDYGSTLFKENNVNAANLKEYIDIALEQTRAGAPLDNKSKIVNSAEVKETLALAEAAANKYKSPKVDVEHLLSGLSNDELVNEIFNEVYLTDEAIKAILKRKFEKTKKDKDGKTGTLYIEQFGSNMNEKVRNGKLQGIYGRDEEIRAIIESLLRYNKNSPVLVGNPGTGKTTIVEGLVYRIEKGDVPKELQGYTVISLNFRKFTSGTSYRGEFETRMKNIIKELKNKKNKIILFVDEIHLLLGAGKAEGGTDAANLLKPVLSKGEIKLIGATTIAEYRKFIESCSAFERRFEKILVEPPSVDMTVKILRSLKSKYENFYGINITDKALVAAAKISDRFIKDRYLPDKAIDLLNKACSFLQVQLSGKPRIIDVTERDIERLSYEISTLEKDVDKVSKKKYNKLIKEFEEKKEQLKKYYEEYVITGERLKRKKEIEKKLNDLKELTQNYVYSNKEPPIELQNSLKEAQQKYLELYKETVAYVEAKTHNAMNVDAVYQEHVSYIYLRDSGMPLGSLSFESSKGALKLYNSLSKSIIGNEDIIKSLSDAVVKAATGMKDPEKPIGTFLFLGPTGVGKTELAKTLAIELFNSKDNLIRVNMSEFTEAHSVSKITGSPPGYVGFSDSGQLTEAVREKPHSVVLFDELEKAHADVFKVLLQILGDGYINDNHRRNIDFSNTIIIMTSNLGAELFKKKLFFDADNSGTPEYKRVMEDVRLSLIKKCKKVFKPEFVNRIDKIGVFEPLNKKNLHKIVALRFKKLEKRLEEKNIQVSVSEKAIDYIIDQSYDPELGARPTLIFIESVIMTKFAIMYLKKELVDDMDVFVDYNSKAKNLVINLSKT
Protein: Uncharacterized protein (Q386L5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSALPDASVSDVSPQFGWYQPRYLERREPPMSTFPSLSKVVVSTTLDGKISDEEAVKRRVALGFAWERVRPIEEVWNGPPMSDKVPPAKDYERLLLGGSGEESEMKAL
Protein: Late cornified envelope protein 1D (Late envelope protein 4) (Q5T752)
Organism: Homo sapiens (Human)
Function: Precursors of the cornified envelope of the stratum corneum.
Interaction partners:
- Late cornified envelope protein 1E
- Late cornified envelope protein 1A
- Late cornified envelope protein 1F
- Late cornified envelope protein 2D
- Late cornified envelope protein 1B
- Late cornified envelope protein 1C
- Late cornified envelope protein 2C
- Late cornified envelope protein 2B
- Late cornified envelope protein 6A
- Late cornified envelope protein 2A
Sequence:
MSCQQSQQQCQPPPKCTPKCTPKCPAPKCPPKCPPVSSCCSVSSGGCCGSSSGGGCGSNSGGCCSSGGGGCCLSHHRRHRSHRRRPQSSDCCSQPSGGSSCCGGGSSQHSGGCC
Protein: Protein MRG3-like (P36066)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- PUP1 protein homolog
- Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR1
- Uncharacterized mitochondrial outer membrane protein YPR098C
Sequence:
MWKYLHRSVKNEGTVERLTNLNLFTNHRFKFYSTLKEQSFWRIPFKRRSKLQKWVLSTGIVSFIAFNIWWVYWPHHTFPKPVAKILRKGLHSEIKKEGANYQKSLEYYLEALEECKAENVDLLSDEYTGIEIKIGEMYEKLHMYNDATALYGDMLKKFYNELSKTTDKSTKRKFFLLKRDLQILVRFNEINKDSETNATLLIMHLLLAQREFLENSPEFKNVLSKSELLNNQQLDWKNFKGLPFIGKSKPDYQMHLNSKRKQELKIKEPESEQCVFMKELLTARDLYTRYCLNRSNLSGALNSKITTLEWMLLADSPLDDILLAQAELGSIFYLNSEKFEGSLYAIDNEPYKKSEPLELIRSRLQENQNSCLQYSADCYKSIISFANENQYPKVAMESEMDQRILKALSLAHYGIGVINLHKGRLRASKKELKKAIRISEMIRFNELIEEAQRELKKVDGTPI
Protein: Glycerol-3-phosphate dehydrogenase 1-like protein (EC 1.1.1.8) (Q3ULJ0)
Organism: Mus musculus (Mouse)
Function: Plays a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3-phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- Glycerol-3-phosphate acyltransferase 3
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase 4
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
- Glycerol-3-phosphate dehydrogenase [NAD
- Triokinase/FMN cyclase)
- Lysocardiolipin acyltransferase 1
- Membrane-bound glycerophospholipid O-acyltransferase 1
Sequence:
MAAAPLKVCIVGSGNWGSAVAKIIGSNVKTLQKFSSTVKMWVFEETVNGRKLTDIINNDHENVKYLPGHKLPENVVAVPNLSEAVQDADLLVFVIPHQFIHKICDEITGRVPEKALGITLIKGIDEGPDGLKLISDIIREKMGIDISVLMGANIASEVAAEKFCETTIGSKVMQNGLLFKELLQTPNFRITVVDDADTVELCGALKNIVAVGAGFCDGLRCGDNTKAAVIRLGLMEMIAFAKIFCKGQVSTATFLESCGVADLITTCYGGRNRRVAEAFARTGKTIEELEKELLNGQKLQGPQTSAEVYRILRQKGLLDKFPLFTAVYQICYEGRPVTQMLSCLQSHPEHI
Protein: LicD/FKTN/FKRP nucleotidyltransferase domain-containing protein (Q5AHE5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MFIIRRSRGILLLVSIVVFNLIVLSLFQFTPIDNYVIGNKYIDNIKQLLINYQPDSPSSLFSSWSLSNDAGFALSMNHDKEIAFHNQVASAADNHESTNELYNQLDSTTIKASQFNVIDIPNDIPLAYQPFDPRFTLGLILNYINEQENKDLELPSFHWSDFVDMSPLEDQFFHDENDIENYQKKKLNCKDFDATKKNPRINQKNMLFPTKEYCIDDDEIDNILNDQEQLSSYDSYVVEQLKKIKQQNSPMSLGFHIFEFPGRNAKKYRPILGKAYVYEFMKNPSTLTMLLPTTNQEQQGFQMMYQMPVNQQNRNKISNSNQIFKSGVTIDLKQELNKLITSNKPQKLTSLTYEKHLSHDMFVDNSPAIIMSIQQQLQTQPLNQTDTNYLNSLKFSLLYENPGKYFHEANILTREANFALGGHYDWRFMNGIINNTPQLSVSINQLIKSWFRLTNQFGLNTWIAHGSLLSWYWNGLQFPWDSDIDVQMPISDLHKLSRYLNQSVIVDFGHDINNIRLGRYFLDCSSLISQRVRGNGNNNIDARFIDMDTGLYIDITGLALSNTMAPARYNHLLHSSPNNGELARENSRDATISELARNEFLQVYNCRNNHFSRLEELSPIRLSLVEGEFGYIPNEFESILKIEYNEKSINNKDYNGFVFLPKLRIWVKKKPIVNFVAAKEEKEQQQKPNQSSKKTADVITIDLTDEEYSQYLLENQSELISYLITSNVTLFHQDELVHYFNGRSAKSLFFTDEESQQVQEESQSQLILKKGLIQDLSQDLFKFNSFQSNYNYADKLNKIKLLLGEKQQQQNNDDSNSKNSSGDNDDPLNRNEIVNEIN
Protein: 2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic (EC 2.5.1.130) (1,4-dihydroxy-2-naphthoate phytyltransferase) (1,4-dihydroxy-2-naphthoate polyprenyltransferase) (Protein ABERRANT CHLOROPLAST DEVELOPMENT 4) (menA-like protein) (AtMENA) (Q0WUA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of phylloquinone (vitamin K1). Catalyzes the transfer of a prenyl chain to 2-carboxy-1,4-naphthoquinone.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:15686525}; Multi-pass membrane protein {ECO:0000269|PubMed:15686525}.
Interaction partners:
- Alternative NAD
- Geranylgeranyl diphosphate reductase, chloroplastic
- 2-phytyl-1,4-beta-naphthoquinone methyltransferase, chloroplastic
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2
- Solanesyl diphosphate synthase 2, chloroplastic
- Solanesyl diphosphate synthase 1, chloroplastic
- 1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1
- 2-succinylbenzoate--CoA ligase, chloroplastic/peroxisomal
- Protein PHYLLO
Sequence:
MVNFVSLCDIKYGFVPKNSTDLFVKRKIHKLPSRGDVITRLPVFGSNARENLNAKPRRNLRVRPIFCKSYGDAAKVYQEEEIPRAKLIWRAIKLPMYSVALVPLTVGASAAYLETGLFLARRYVTLLLSSILIITWLNLSNDVYDFDTGADKNKMESVVNLVGSRTGTLAAAITSLALGVSGLVWTSLNASNIRAILLLASAILCGYVYQCPPFRLSYQGLGEPLCFAAFGPFATTAFYLLLGSSSEMRHLPLSGRVLSSSVLVGFTTSLILFCSHFHQVDGDLAVGKYSPLVRLGTEKGAFVVRWTIRLLYSMLLVLGLTRILPLPCTLMCFLTLPVGNLVSSYVEKHHKDNGKIFMAKYYCVRLHALLGAALSLGLVIAR
Protein: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (AtGFAT) (AtGFAT1) (Glutamine:fructose-6-phosphate amidotransferase 1) (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase GFAT1) (Hexosephosphate aminotransferase GFAT1) (Q9LIP9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Controls the flux of glucose into the hexosamine biosynthetic pathway (HBP) leading to glucosamine (GlcN) content homeostasis. Involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Required during pollen maturation and pollen tube formation by triggering polar deposition of pectin and callose in the pollen cell wall. Promotes tolerance to tunicamycin (Tm), an inhibitor of proteins N-glycosylation in endoplasmic reticulum (ER).
Interaction partners:
- Glucosamine 6-phosphate N-acetyltransferase
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Phosphoacetylglucosamine mutase
- Glutamine synthetase, chloroplastic/mitochondrial
- Glutamine synthetase cytosolic isozyme 1-3
- Glutamine synthetase cytosolic isozyme 1-2
- Glutamine synthetase cytosolic isozyme 1-1
- Glutamine synthetase cytosolic isozyme 1-4
- Glutamine synthetase cytosolic isozyme 1-5
Sequence:
MCGIFAYLNFHANKERRYILDVLFNGLRRLEYRGYDSAGIAIDNSSPSSSPLVFRQAGNIESLVNSVNEEITNTDLNLDEVFYFHAGIAHTRWATHGEPAPRNSHPQSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFDKANEEGGQTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKELDQGESNSHVFQDAHFLSKNDHPKEFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERGRCNGLSRPASVERALSVLEMEVEQISKGKYDHYMQKEIHEQPESLTTTMRGRLIRGGSRKTKTVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVMVMLALAIGSDTISSQKRREAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSSSGSCRAIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ
Protein: Rifin (Q8IC49)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKFHYFNILLLNIPLNILIFSSHVNDQKNAYNSSIHHAPKTKTTKIPNIRLLCECELYAAPNYDNSEMKVVMQNFDRQTEQRFNEYEERMLKNRKKCKEQCDKDIQKIILKDKIEKELEEKLAALETNINTNDIPTCICKKSVADKVEKTCLKCGGILGTTVPQLGILGGISTHMLTTAATSAAIDAGMKAVVDKLKDFVIGFRGNTVDLTPIVNPSSYNCGNLLLENAKNLTKTTCMPNSAGKVSTLCAQIQNSGSISTFNGFAEAGTDAYNTTWATKTAEINSFNIAMMASIIAIVVIVLVMVIVYLILRYRRKEIIKKKLQYIKLLNQ
Protein: Vomeronasal 2, receptor 83 (A0A3B2WD89)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLFSCLFFTWLLQMPTLIWTFATSSCLSESEYLLHHDGTVVIGAFFPILKSLPVSETIDWKTLSFDIDNVLEMNVHNYQLVLTMLFAINEINLNSHILPNTSLGLEIYNVPYLQRNALRNVFYWLTGLSTFIPNYSCRKNSKSAATLTGILWKTSENIGTVLDLYKFPQITFGPFDHDQIDRKQFPSLYQVAPKDTSLLSGIASLMLHFNWTWVGLLSTDDHRGAQFLSDLRKVLENNTVCIAFMETVSLWGESLNSLQTHYQMHILESSANVIVIYGSIAFILTVIKNRHSKYITKKVWVMNSKWVGQKFEQYTMLELSHGALSFSHHHGEIFGFTNFVHEATPFKYPEDIFLHVLWNKYFNCSLLQSDCKIIEKCLPNSSLELLPGNIFEMIMTEESYNVYNAVYAVAHSLHEMTLSQMQVQPQAYKDRTMLFPWQVFHY
Protein: Glutamate receptor-interacting protein 1 (GRIP-1) (Q9Y3R0)
Organism: Homo sapiens (Human)
Function: May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons. Through complex formation with NSG1, GRIA2 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity).
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:10197531}. Perikaryon {ECO:0000250|UniProtKB:P97879}. Cell projection, dendrite {ECO:0000250|UniProtKB:P97879}. Cytoplasm {ECO:0000250|UniProtKB:P97879}. Endomembrane system {ECO:0000250|UniProtKB:P97879}; Peripheral membrane protein {ECO:0000250|UniProtKB:P97879}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P97879}. Postsynaptic density {ECO:0000250|UniProtKB:P97879}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10197531}; Peripheral membrane protein {ECO:0000250|UniProtKB:P97879}. Note=Membrane-associated with vesicles, peri-Golgi complexes and endoplasmic reticulum. Enriched in postsynaptic plasma membrane and postsynaptic densities. {ECO:0000250|UniProtKB:P97879}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 3
- GRIP1-associated protein 1
- PRKCA-binding protein
- Glutamate receptor 1
- GRIP and coiled-coil domain-containing protein 2
- GRIP and coiled-coil domain-containing protein 1
- Liprin-alpha-1
- Glutamate receptor 4
- FRAS1-related extracellular matrix protein 2
Sequence:
MIAVSFKCRCQILRRLTKDESPYTKSASQTKPPDGALAVRRQSIPEEFKGSTVVELMKKEGTTLGLTVSGGIDKDGKPRVSNLRQGGIAARSDQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEVEYELPPVSVQGSSVIFRTVEVTLHKEGNTFGFVIRGGAHDDRNKSRPVVITCVRPGGPADREGTIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQEAALLIEYDVSVMDSVATASGPLLVEVAKTPGASLGVALTTSMCCNKQVIVIDKIKSASIADRCGALHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVKLEILPHHQTRLALKGPDHVKIQRSDRQLTWDSWASNHSSLHTNHHYNTYHPDHCRVPALTFPKAPPPNSPPALVSSSFSPTSMSAYSLSSLNMGTLPRSLYSTSPRGTMMRRRLKKKDFKSSLSLASSTVGLAGQVVHTETTEVVLTADPVTGFGIQLQGSVFATETLSSPPLISYIEADSPAERCGVLQIGDRVMAINGIPTEDSTFEEASQLLRDSSITSKVTLEIEFDVAESVIPSSGTFHVKLPKKHNVELGITISSPSSRKPGDPLVISDIKKGSVAHRTGTLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLVKLKIRKDEDNSDEQESSGAIIYTVELKRYGGPLGITISGTEEPFDPIIISSLTKGGLAERTGAIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTLKIKKQTDAQSASSPKKFPISSHLSDLGDVEEDSSPAQKPGKLSDMYPSTVPSVDSAVDSWDGSAIDTSYGTQGTSFQASGYNFNTYDWRSPKQRGSLSPVTKPRSQTYPDVGLSYEDWDRSTASGFAGAADSAETEQEENFWSQALEDLETCGQSGILRELEEKADRRVSLRNMTLLATIMSGSTMSLNHEAPTPRSQLGRQASFQERSSSRPHYSQTTRSNTLPSDVGRKSVTLRKMKQEIKEIMSPTPVELHKVTLYKDSDMEDFGFSVADGLLEKGVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLDLVISRNPLASQKSIDQQSLPGDWSEQNSAFFQQPSHGGNLETREPTNTL
Protein: SET domain-containing protein 4 (EC 2.1.1.-) (EC 2.1.1.364) (Q9NVD3)
Organism: Homo sapiens (Human)
Function: Histone-lysine N-methyltransferase that acts as a regulator of cell proliferation, cell differentiation and inflammatory response. Regulates the inflammatory response by mediating mono- and dimethylation of 'Lys-4' of histone H3 (H3K4me1 and H3K4me2, respectively), leading to activate the transcription of pro-inflammatory cytokines IL6 and TNF-alpha (By similarity). Also involved in the regulation of stem cell quiescence by catalyzing the trimethylation of 'Lys-20' of histone H4 (H4K20me3), thereby promoting heterochromatin formation. Involved in proliferation, migration, paracrine and myogenic differentiation of bone marrow mesenchymal stem cells (BMSCs) (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24738023, ECO:0000269|PubMed:37926288}. Nucleus {ECO:0000269|PubMed:24738023}.
Interaction partners:
- N-lysine methyltransferase SETD6
Sequence:
MQKGKGRTSRIRRRKLCGSSESRGVNESHKSEFIELRKWLKARKFQDSNLAPACFPGTGRGLMSQTSLQEGQMIISLPESCLLTTDTVIRSYLGAYITKWKPPPSPLLALCTFLVSEKHAGHRSLWKPYLEILPKAYTCPVCLEPEVVNLLPKSLKAKAEEQRAHVQEFFASSRDFFSSLQPLFAEAVDSIFSYSALLWAWCTVNTRAVYLRPRQRECLSAEPDTCALAPYLDLLNHSPHVQVKAAFNEETHSYEIRTTSRWRKHEEVFICYGPHDNQRLFLEYGFVSVHNPHACVYVSREILVKYLPSTDKQMDKKISILKDHGYIENLTFGWDGPSWRLLTALKLLCLEAEKFTCWKKVLLGEVISDTNEKTSLDIAQKICYYFIEETNAVLQKVSHMKDEKEALINQLTLVESLWTEELKILRASAETLHSLQTAFT
Protein: Peroxidase 64 (Atperox P64) (EC 1.11.1.7) (ATP17a) (PRXR4) (Q43872)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- Casparian strip membrane protein 1
- Dirigent protein 10
- Transcription factor MYB36
- LRR receptor-like serine/threonine-protein kinase GSO1
- Cinnamyl alcohol dehydrogenase 4
- Probable cinnamyl alcohol dehydrogenase 6
- UDP-glycosyltransferase 72E2
- UDP-glycosyltransferase 72E3
- Cinnamyl alcohol dehydrogenase 5
- UDP-glycosyltransferase 72E1
Sequence:
MNAHMLNLLVIVIFVVSFDVQALSPHYYDHTCPQADHIVTNAVKKAMSNDQTVPAALLRMHFHDCFVRGCDGSVLLDSKGKNKAEKDGPPNISLHAFYVIDNAKKALEEQCPGIVSCADILSLAARDAVALSGGPTWAVPKGRKDGRISKAIETRQLPAPTFNISQLRQNFGQRGLSMHDLVALSGGHTLGFAHCSSFQNRLHKFNTQKEVDPTLNPSFAARLEGVCPAHNTVKNAGSNMDGTVTSFDNIYYKMLIQGKSLFSSDESLLAVPSTKKLVAKYANSNEEFERAFVKSMIKMSSISGNGNEVRLNCRRVR