wanglab/gogpt-training-data huggingface dataset:
Protein: Pentatricopeptide repeat-containing protein At1g05670, mitochondrial (Q0WVK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- AT3g47961
- Dentin sialophosphoprotein-like protein
- Transmembrane protein
- Uncharacterized protein
- Benzoate--CoA ligase, peroxisomal
- Flavin-containing monooxygenase FMO GS-OX-like 6
- UDP-glycosyltransferase 74D1
- UDP-glycosyltransferase 74C1
Sequence:
MKKPFTGLLMKRGTLSSFRNFIQLFSLQSRGLSFSTLTDTRPFPDYSPKKASVRDTEFVHQITNVIKLRRAEPLRRSLKPYECKFKTDHLIWVLMKIKCDYRLVLDFFDWARSRRDSNLESLCIVIHLAVASKDLKVAQSLISSFWERPKLNVTDSFVQFFDLLVYTYKDWGSDPRVFDVFFQVLVDFGLLREARRVFEKMLNYGLVLSVDSCNVYLTRLSKDCYKTATAIIVFREFPEVGVCWNVASYNIVIHFVCQLGRIKEAHHLLLLMELKGYTPDVISYSTVVNGYCRFGELDKVWKLIEVMKRKGLKPNSYIYGSIIGLLCRICKLAEAEEAFSEMIRQGILPDTVVYTTLIDGFCKRGDIRAASKFFYEMHSRDITPDVLTYTAIISGFCQIGDMVEAGKLFHEMFCKGLEPDSVTFTELINGYCKAGHMKDAFRVHNHMIQAGCSPNVVTYTTLIDGLCKEGDLDSANELLHEMWKIGLQPNIFTYNSIVNGLCKSGNIEEAVKLVGEFEAAGLNADTVTYTTLMDAYCKSGEMDKAQEILKEMLGKGLQPTIVTFNVLMNGFCLHGMLEDGEKLLNWMLAKGIAPNATTFNSLVKQYCIRNNLKAATAIYKDMCSRGVGPDGKTYENLVKGHCKARNMKEAWFLFQEMKGKGFSVSVSTYSVLIKGFLKRKKFLEAREVFDQMRREGLAADKEIFDFFSDTKYKGKRPDTIVDPIDEIIENYLVDEQLRGAN
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (G8BFS5)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- Gluconokinase
- Transaldolase
- Ribulose-phosphate 3-epimerase
- 6-phosphogluconolactonase-like protein
- Transketolase
- Ribose-5-phosphate isomerase
- Glucosamine/galactosamine-6-phosphate isomerase domain-containing protein
- 2-deoxy-D-gluconate 3-dehydrogenase
- Xylulose kinase
Sequence:
MSSDSKAPAQPQGDLGLIGLAVMGQNLILNAADHGYTVVAYNRTVSKVDHFLENEAKGNKHIIGAHSIQELVDNLKRPRRIMLLVKAGPAVDAFIEQLLPYLDKGDIIIDGGNSHFPDSNRRFEELKQKGILFVGCGVSGGEEGARHGPSLMPGGNEEAWPHIKPIFQAIAAKSDGEPCCDWVGDAGAGHYVKMVHNGIEYGDMQLICEAYDVMKRVGKFEDKEIADVFAQWNNGVLDSYLIEITRDILKFNDPTDEKPVVEKILDTAGQKGTGKWTAINALDLGVPVTLIGEAVFARCLSALKNERVKASKILKGPEVGEKSPITDKKKFIDDLEQALYASKIISYAQGFMLMRQASVDYSWKLNYSVIALMWRGGCIIRSVFLKEITAAYRENPDLDNLLFHPFFLDAVTKAQSGWRSALGHAITQGIPTPAFSTALAFYDGLRSEQLPANLLQAQRDYFGAHTFQVQKGKGTSFVPEDKWVHVNWTGRGGDVSASNYDV
Protein: Hydroxymethylglutaryl-CoA synthase, cytoplasmic (HMG-CoA synthase) (EC 2.3.3.10) (3-hydroxy-3-methylglutaryl coenzyme A synthase) (P17425)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate, a precursor for cholesterol synthesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13704}.
Interaction partners:
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Acetyl-CoA acetyltransferase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Acetyl-CoA acetyltransferase, cytosolic
- 3-ketoacyl-CoA thiolase, mitochondrial
- Lanosterol 14-alpha demethylase
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Squalene monooxygenase
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- Squalene synthase
Sequence:
MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQARMGFCTDREDINSLCLTVVQKLMERNSLSYDCIGRLEVGTETIIDKSKSVKSNLMQLFEESGNTDIEGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAIYASGNARPTGGVGAVALLIGPNAPVIFDRGLRGTHMQHAYDFYKPDMLSEYPVVDGKLSIQCYLSALDRCYSVYRKKIRAQWQKEGKDKDFTLNDFGFMIFHSPYCKLVQKSLARMFLNDFLNDQNRDKNSIYSGLEAFGDVKLEDTYFDRDVEKAFMKASAELFNQKTKASLLVSNQNGNMYTSSVYGSLASVLAQYSPQQLAGKRIGVFSYGSGLAATLYSLKVTQDATPGSALDKITASLCDLKSRLDSRTCVAPDVFAENMKLREDTHHLANYIPQCSIDSLFEGTWYLVRVDEKHRRTYARRPSTNDHSLDEGVGLVHSNTATEHIPSPAKKVPRLPATSGEPESAVISNGEH
Protein: NKG2-D type II integral membrane protein (Killer cell lectin-like receptor subfamily K member 1) (NK cell receptor D) (NK lectin-like receptor) (NKLLR) (NKG2-D-activating NK receptor) (NKR-P2) (CD antigen CD314) (O70215)
Organism: Rattus norvegicus (Rat)
Function: Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Colocalized with HCST on the cell surface. {ECO:0000250}.
Interaction partners:
- Retinoic acid early-inducible protein 1-gamma-like
- Hematopoietic cell signal transducer
- MHC class I-like protein MILL2
- UL16-binding protein 1.
- TYRO protein tyrosine kinase-binding protein
- Retinoic acid early transcript 1L
- Retinoic acid early-inducible protein 1 domain-containing protein
- Natural cytotoxicity triggering receptor 1
- mRNA export factor
- Natural cytotoxicity triggering receptor 3
Sequence:
MSKCHNYDLKPAKWDTSQEHQKQRSALPTSRPGENGIIRRRSSIEELKISPLFVVRVLVAAMTIRFTVITLTWLAVFITLLCNKEVSVSSREGYCGPCPNDWICHRNNCYQFFNENKAWNQSQASCLSQNSSLLKIYSKEEQDFLKLVKSYHWMGLVQSPANGSWQWEDGSSLSPNELTLVKTPSGTCAVYGSSFKAYTEDCSNPNTYICMKRAV
Protein: Myeloperoxidase (A0A0G2K1A2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Cathepsin G
- Granzyme-like protein 2
- Proteinase 3
- Elastase, neutrophil expressed
- Membrane spanning 4-domains A3
- Bactericidal permeability-increasing protein
- Lactotransferrin
- Cathepsin S
- Matrix metalloproteinase-9
- Interleukin-6
Sequence:
MKLFLALAGLLAPLAMLQTSTGATPALPGEVANSVVLDCMEEAKRLVNKAYKERRESSIKQSLRSGSASPMELLSYFKQPVAGTRTAVRAADYLHVALDLLKRKLQPLWPRPFNVTDVLTPAQLNLLSVSSGCAYQDVGVTCPPQDKYRTITGHCNNRRSPTLGASNRAFVRWLPAEYEDGISLPFGWTPKVNRSGFKVPLARQVSNAIVRFPNDQLTKDQERALMFMQWGQFLDHDITLTPEPATRFSFLTGLNCETSCLQQQPCFPLKIPPNDPRIKNQKDCIPFFRSCPACTGSNITIRNQINALTSFVDASGVYGSEDPLARRLRNLTNQLGLLAVNTRFQDNGRALLPFDSLHDDPCLLTNRSARIPCFLAGDMRSSEMPELTSMHTLFVREHNRLATELKRLNPRWNGEKLYQEARKIVGAMVQIITYRDYLPLVLGPAAMKKYLPQYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNQYRSTGPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPSTVGELGTVLKNLELARKLMAQYGTPNNIDIWMGGVSEPLEPNGRVGQLLACLIGTQFRKLRDGDRFWWENPGVFSKQQRQALATISLPRIICDNTGITTVSKNNIFMSNSHPRDFVSCNTLPKLNLASWKET
Protein: PAK4-inhibitor INKA1 (Induced in neural crest by AP2-alpha protein homolog) (Inca) (Inka-box actin regulator 1) (Q96EL1)
Organism: Homo sapiens (Human)
Function: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:26607847}. Cytoplasm {ECO:0000269|PubMed:26607847}. Note=Mainly nuclear (PubMed:26607847). Relocalizes to the cytoplasm following interaction with PAK4 (PubMed:26607847). {ECO:0000269|PubMed:26607847}.
Interaction partners:
- Serine/threonine-protein kinase PAK 4
- Serine/threonine-protein kinase PAK 5
Sequence:
MDMHSARLDSFLSQLRWELLCGRDTGSPSMPGPLQPTSQTGPDVQPSHQLRASGALEEDSVCCVEEEEEEEEEAVVTEDRDAALGGPREHALDWDSGFSEVSGSTWREEELPVSQRPAPSAQPLRRQCLSVSGLPMPSRAPVASVPPVHHPRPKSTPDACLEHWQGLEAEDWTAALLNRGRSRQPLVLGDNCFADLVHNWMELPETGSEGGDGGGHRARARPPQFLLGLSEQLRRRLARARRTAMAGKRLSCPPRPEPELPADVSRFAALMSCRSRQPIICNDVSYL
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FKK2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAGTNQVGDTNSSTLNSSNDISDKMSLNNVDVRDPSPNDSEECKKASAEHEELEEDEDVGVDPKTLDWDGPGDLDNPHNWPSWKKWYATMVAAFLCLAVTMNSSLYVSGVPELVAKYHVNQTLALAGLTFYLLGLANVIGAPLSEVFGRKPIYLFSLPISMLFTMGVGLSGGHMRTILPLRFFAGFFASPCLSVGSGTILDVFDVDEVSVAMTFFSLAPFLGPVISPIIAGFAVEERSWRYTQWIQLWASGLILPLIAIMPETHKGLILRKRAQKRNIKLKAFTNAEKKEFLKLTFTITIMRPIKMLMVEPIVLVFSIYVAFIFAVLFAFFEAYPVIYRGVYHMKLGVSGLPFIGIGLGLWMGAFTYILIDRKFLFPKAPKGTPPIENPTSLRTTPFRGHRDPETGQLKPIHPEKFLLACKIGSVALPIALFWQAWTSRPDVHWMAPIAAGVPFGFGLILIFFSVLMYFSTCYPPLVVASTLAANNLLRYITSSVFPLFTIQMYTNMKIKWASTLFALICVVMIPIPWIFERWGPKLRDISQFGYSAMAREQAEKIKAEHPDEEIEDNDDHDLDLTRITTLRTIETAYSHQNSNTLEHTISNTSGNHNVRKVATNNLSQTASHQKPTDEMYNMADSGSAFDESSENSSRMV
Protein: MHC class I like protein GS8 (Q0WXI7)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
TAVSRPGLGEPRFIIVGYVDDTQFVRFDSDAENPRMEPRAPWMEQEGPEYWERNTQVSKENEQSFRVSLGTALSYYNQSKGGSHTLQWLVGCDLGPDGSLLRGYEQSAYDGRDYLALNEDLITWTAADLAALKTRSKLEQAGLAEKRRAYLEVDCLTWLRRYLELGKETLL
Protein: Nuclear factor 1 (B1AKN5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MYSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKEEERAVKDELLSEKPEVKQKWASRLLAKLRKDIRPEYREDFVLTVTGKKPPCCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKSPQCSNPGLCVQPHHIGVSVKELDLYLAYFVHAAGHLGFQDSFVTSGVFSVTELVRVSQTPIAAGTGPNFSLSDLESSSYYSMSPGAMRRSLPSTSSTSSTKRLKSVEDEMDSPGEEPFYTGQGRSPGSGSQSSGWHEVEPGMPSPTTLKKSEKSGFSSPSPSQTSSLGTAFTQHHRPVITGPRASPHATPSTLHFPTSPIIQQPGPYFSHPAIRYHPQETLKEFVQLVCPDAGQQAGQVGFLNPNGSSQGKVHNPFLPTPMLPPPPPPPMARPVPLPVPDTKPPTTSTEGGAASPTSPTYSTPSTSPANRFVSVGPRDPSFVNIPQQTQSWYLG
Protein: Succinate-semialdehyde dehydrogenase (EC 1.2.1.24) (Q9VBP6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU365091}.
Interaction partners:
- (S)-3-amino-2-methylpropionate transaminase (GABA aminotransferase) (Gamma-amino-N-butyrate transaminase) (L-AIBAT)
- Probable citrate synthase, mitochondrial
- Citrate synthase
- Isocitrate dehydrogenase
- Pyruvate carboxylase
- Malate dehydrogenase, mitochondrial
- ATP-citrate synthase
- 2-oxoglutarate dehydrogenase, mitochondrial
- Malate dehydrogenase
- Malate dehydrogenase
Sequence:
MWRQLSGVARTGSSLSLCRMRGFSALVQDKALVDGAWVDSSNAKATFEVRNPANGAVIGKVPNMTVADAQKAIDAAKQAYESKEWRSLTAKDRSNLLKKWHKLIEQHSQEIAEIMTAESGKPINESKGEVAYGNAFVEWFAEEARRIYGEIVPSASPNREIIVMKQPIGVAALITPWNFPMAMITRKAGAALAAGCTVVVKPSEDTPLTALAVAKLAVDAGIPKGVINVVTTNKAAPIGDLFCKSPDVRGISFTGSTEVGKLLFRNSADGIKRICLELGGNAPFIVFDSADIEKAVDGAMASKFRNCGQTCVSANRFFVQDSVYDKFVGQLKKRVEALKIGDGQGCDVQIGPLINEMQFNKVSGFVEDARSKKANIILGGQPLPDKGSLFYAPTIVTDVPPSAQLYSEEVFGPVVSIIRFRDEEEAVKKANDTRRGLAGYFYSENLQQVFRVAKRLEVGMVGVNEGIISAAEAPFGGVKESGVGREGSKHGIDDYVDIKYICMGNLKYD
Protein: Photoreceptor dehydrogenase, isoform D (EC 1.1.1.-, EC 1.1.1.105) (B7Z061)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFRGKNAVVTGGAGGIGLQVSKQLLAAGAAVAIIDLQDNLEEFVKLRAAHPTQSVMIIKMDVANKKGVEATYEEIAKTFGNIDIVVNVAGIFNDKDVQRTLLVNLGGIINSTLSALPYMGKDNGGKGGIVVNMSSVVGLDPMFIIPVYGATKAGIINFTRCLANEKYYQRSGIKFVTVCPGATMTDMFTNFTEKIIFPETSDETYRILDRLNKQSAADVSRCILNVLEKDKNGAVYVIEGKRVYPLEIKPQWTGKEQAL
Protein: DNA-directed RNA polymerase III subunit RPC7-like (RNA polymerase III subunit C7-like) (DNA-directed RNA polymerase III subunit G-like) (Q8R0C0)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BT43}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC8
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerases I and III subunit RPAC2
Sequence:
MASRGGGRGRGRGQLTFNMEAVGIGKGDALPPPTLQPSPLFPPLEFHPVPLPAGEEGEYVLALKQELRGAMRQLPYFIRPAVPKRDVERYSDKYQMSGPIDNAIDWNPDWRRLPSELKIRVRKVQKERTTIILPKRPPKSTDDKEETIQKLETLEKKEEEVTSEEDEEKEEEEEKEEGEEEEYDEEEHEEETDYIMSYFDNGEDFGGDSDDNMDEAIY
Protein: PAPS synthetase, isoform D (EC 2.7.1.25, EC 2.7.7.4) (Q8IQV1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FAD synthase
- FAD synthase
- Sulfite oxidase, mitochondrial
- 3'
- Putative inositol monophosphatase 3
- Elongation factor 1-alpha 1
- Elongation factor 1-alpha 2
- Cystathionine beta-synthase
- Eukaryotic translation release factor 3, isoform A
- Protein HBS1
Sequence:
MFTRCANSLGLYHNNINNNNSACCAASPKRSCLPSVEKPEDACLQVATNVTEQKHHVTRETRGKNLGLCRGFRGCTVWLTGLSGAGKTSIAFELEAYLVSRGIPAYGLDGDNIRTGLNKNLGFTPADREENIRRVGEVAKLFADSGVVAICSFVSPFADDREMARKIHKDAGLKFYEIFVDTPLDVCETRDVKGLYKKAREGVIKGFTGITQEYERPQMPELVVNTHGYTVRESTQKLVTLLEQEGIIPRSLRDVDLLPELYPSESIATEALRHEAESLQAIEISTVELQWVQVLAEGWAYPLRGFMREDEYLQTLHFNTLQSGMDGSYRENHSVPIVLSATQADKDRLDGCSSLTLKYQGKAVAILRRPEFYFQRKEERLARQFGTSNPNHPYSKQVYESGDYLVGGDLAVIERIRWEDGLDQYRLTPNELRRRFKELNADAIFAFQLRNPIHNGHALLMQDTRRQLLERGFKQPVLLLHPLGGWTKDDDVPLDVRMKQHQAVLDAGVLRREDTVLAIFPSPMMYAGPTEVQWHAKARMNAGANFYIVGRDPAGMPHPAKETYPDGNLYDATHGARVLKMAQGLDSMEILPFRVAAYDKSASRMAFFEPKRKDEFEFISGTKMRTLAKTGASPPDGFMEPEAWRILATYYQNLPQS
Protein: Antifungal protein Lap (C0HM10)
Organism: Lyophyllum shimeji (Hon-shimeji) (Tricholoma shimeji)
Function: Displays antifungal activity against M.arachidicola and P.piricola, but not against R.solani, C.gossypii and C.comatus. Inhibits mycelial growth in P.piricola with an IC(50) of 70 nM. Displays very low cell-free translation inhibitory activity in a rabbit reticulocyte lysate system (IC(50)=70 uM) but is able to inhibit HIV-1 reverse transcriptase activity (IC(50)=5.2 nM).
Interaction partners:
Sequence:
AGTEIVTCYNAGTKVPRGPSAXGGAIDFFN
Protein: Chromatin assembly factor 1 subunit B, putative (Q38AQ8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Proliferating cell nuclear antigen
- Uncharacterized protein
- Anti-silencing protein ASF 1 like protein, putative
- Uncharacterized protein
- Chromatin assembly factor 1 subunit A dimerization domain-containing protein
- Histone H3 variant
- Histone H3, putative
- Histone-binding protein RBBP4-like N-terminal domain-containing protein
- Guanine nucleotide-binding beta subunit-like protein
- Uncharacterized protein
Sequence:
MATSIQQNPLRVRTLEVLWHWREIDDEALQFGLQGGSIEGIVSIDYNRVEDRIVTSGGDRYIRLWNLNIAAIDRWLKNSESGMEDCVQFICGGVTPWMPLTARWAPNGRLIASGHCDGKICLWWKESSRDGEPEQWKDYRHLSGHVIDVHDVCFSPDSRYLLSAGGDGTVVLHDLEGSTMPVVQLQEAHSKFCRGVAWDPWMHYVASCGSGPALYIMQGPKHGAKRASLVSQRKAQGDFIGESCSASYRRLAWSPDGAILAVPYGKVSQHKHSRSACSGGGSEDATAGAAAGEDRWKNSMVHCVYMYIRNAPDKVAARLTVRGDAEVRGVQWAPCFLEPIDEITCNEEQNDTTAAEVSNQARKSGPTAEEKGSWGPADYRMALAVWTADAVMVYTTDSEVRHSDFTDLHMRSIYDVAWSPDASYLLTAGLDGYITVISTGGSLGVAHRLPLFSKKPTTRRLCTVLQNVKTESETLGPGRGATKTTNAATKKEPVGGEEAENASSNTVVHAPVKKKKKLEPQAQEMYPAKEEPDTAVSLGELSKLMDNLND
Protein: Polypeptide N-acetylgalactosaminyltransferase 4 (pp-GaNTase 4) (EC 2.4.1.41) (Protein-UDP acetylgalactosaminyltransferase 4) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) (Q8I136)
Organism: Caenorhabditis elegans
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
- GLY-16
- LYSozyme
- LYSozyme
Sequence:
MLPRMLKMKTVGTVLAVIWLFGLAFIYVQSTSSSLRPPGRHPPPLPQLDPLIPQNPPQNDEIRPKKSAPPIPTINLAEDTTIHERTEKDVTWKTFDVEKFLNKGKWHQGEDKYKANSFNQEASDALNPTRKIPDSREPQCRDVDYSKVGMQPTTVIITYHNEARSSLLRTVFSVFNQSPEELLLEIVLVDDNSQDVEIGKELAQIQRITVLRNNQREGLIRSRVKGAQVARAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFMNEQLRKERHAHPTAPIRSPTMAGGLFAISKEWFNELGTYDLDMEVWGGENLEMSFRVWQCGGSLEIMPCSRVGHVFRKKHPYTFPGGSGNVFQKNTRRAAEVWMDEYKAIYLKNVPSARFVNFGDITDRLAIRDRLQCKSFKWYLENVYPQLEIPRKTPGKSFQMKIGNLCLDSMARKESEAPGLFGCHGTGGNQEWVFDQLTKTFKNAISQLCLDFSSNTENKTVTMVKCENLRPDTMVVEKNGWLTQGGKCLTVNQGSGGDWLIYGAHCELNNGAQRWIFEKLDTYE
Protein: Sec24d protein (Q80V21)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
Sequence:
MVVTDVGEVFVPLLDGFLVNYEESQSVIHNLLDQIPEMFADSNENETVFAPVIQAGMEALKAAECPGKLFIFHSSLPTAEAPGKLKNRDDKKLVNTDKEKILFQPQTAVYESLAKDCVANSCSVTLFLFPSQFVDVASLGLVPLLTGGTLYKYNVFQIHSDSQRFLTDLRNDIEKKIGFDAIMRVRTSTGFRATDFFGGIFMNNTTDVEMAAIDCDKAVTVEFKHDDKLSEDVGALIQCAVLYTTISGQRRLRIHNLALNCSTQLADLYKSCETDALINFFAKSAFKAVLNQPLKAIREILVNQTAHMLACYRKHCASPSAASQLILPDSMKVLPVYMNSLLKNCVLLSRSEISPDERAYQRQLVMTMGVADSQLFFYPLLLPIHTLDVKSAALPPAVRCSESRLSEEGIFLLANGLNMFLWFGVGSPPELIQGIFNVPSFAHINTDMTSLPEVGSPHSQQLRMIMNNIQQKKPYSMKLIVVKQREQREMAFRQFLVEDKGLYGGSSYVDFLCCVHKEICQLLN
Protein: Nitrate reductase molybdenum cofactor assembly chaperone NarJ (Redox enzyme maturation protein NarJ) (P0AF26)
Organism: Escherichia coli (strain K12)
Function: Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with the NarI subunit on the membrane.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9305880}.
Interaction partners:
- Respiratory nitrate reductase 1 alpha chain
- Respiratory nitrate reductase 1 gamma chain
- Respiratory nitrate reductase 1 beta chain
- Nitrate/nitrite antiporter NarK
- Respiratory nitrate reductase 2 alpha chain
- Respiratory nitrate reductase 2 beta chain
- Respiratory nitrate reductase 2 gamma chain
- Probable nitrate reductase molybdenum cofactor assembly chaperone NarW
- Nitrate/nitrite transporter NarU
- Nitrite reductase small subunit
Sequence:
MIELVIVSRLLEYPDAALWQHQQEMFEAIAASKNLPKEDAHALGIFLRDLTTMDPLDAQAQYSELFDRGRATSLLLFEHVHGESRDRGQAMVDLLAQYEQHGLQLNSRELPDHLPLYLEYLAQLPQSEAVEGLKDIAPILALLSARLQQRESRYAVLFDLLLKLANTAIDSDKVAEKIADEARDDTPQALDAVWEEEQVKFFADKGCGDSAITAHQRRFAGAVAPQYLNITTGGQH
Protein: Nucleolar protein 12 (25 kDa nucleolar protein) (Q5D1Z3)
Organism: Rattus norvegicus (Rat)
Function: May bind to 28S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UGY1}. Nucleus {ECO:0000250|UniProtKB:Q9UGY1}. Cytoplasm {ECO:0000250|UniProtKB:Q9UGY1}.
Interaction partners:
- Ribosome biogenesis protein BRX1 homolog
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- ATP-dependent RNA helicase
- Ribosome assembly factor mrt4
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- Probable ribosome biogenesis protein RLP24
- Ribosome biogenesis protein BOP1
- GTP-binding protein 4
- Ribosome biogenesis protein WDR12
- EBNA1 binding protein 2
Sequence:
MGRNKKKKRDGDDRRPRLILNFDEEKRREYLTGFHKRKVERKKAAIEEIKQRLKQEQKKLREERHQEYLKMLAEREEALEEADELERLVTAKTESVQYDHPNHTVTVTTVSDLDLSGARLLGLPLPEQGDQDGSQEEEVSSMEKPTKALPKKSKDPLLSQRISSLTATLHAHSRKKVKRKHPRRAQDSTKKPPSATRTSKTQRRRRMTGKARHNGE
Protein: DnaJ homolog subfamily C member 9 (HDJC9) (DnaJ protein SB73) (Q8WXX5)
Organism: Homo sapiens (Human)
Function: Acts as a dual histone chaperone and heat shock co-chaperone. As a histone chaperone, forms a co-chaperone complex with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2 in histone H3-H4 heterodimer recognition and facilitate the assembly of histones into nucleosomes. May also act as a histone co-chaperone together with TONSL. May recruit histone chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers. Also plays a role as co-chaperone of the HSP70 family of molecular chaperone proteins, such as HSPA1A, HSPA1B and HSPA8. As a co-chaperone, may play a role in the recruitment of HSP70-type molecular chaperone machinery to histone H3-H4 substrates, thereby maintaining the histone structural integrity. Exhibits activity to assemble histones onto DNA in vitro.
Subcellular location: Nucleus {ECO:0000269|PubMed:17182002}. Cytoplasm {ECO:0000269|PubMed:17182002}. Cell membrane {ECO:0000269|PubMed:17182002}. Note=Predominantly nuclear. Translocates to the cytoplasm and membrane after heat shock. {ECO:0000269|PubMed:17182002}.
Interaction partners:
- Histone H4
- Primary cilium assembly protein FAM149B1
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit eta
- DNA replication licensing factor MCM2
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
Sequence:
MGLLDLCEEVFGTADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTVDEDSPVLTQDRDWEAYWRLLFKKISLEDIQAFEKTYKGSEEELADIKQAYLDFKGDMDQIMESVLCVQYTEEPRIRNIIQQAIDAGEVPSYNAFVKESKQKMNARKRRAQEEAKEAEMSRKELGLDEGVDSLKAAIQSRQKDRQKEMDNFLAQMEAKYCKSSKGGGKKSALKKEKK
Protein: Neuronal acetylcholine receptor subunit beta-4 (Q8R493)
Organism: Mus musculus (Mouse)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:P04757}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P04757}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-3
- Tyrosine-protein kinase JAK2
- Neuronal acetylcholine receptor subunit alpha-5
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit alpha-6
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit alpha-2
- Neuronal acetylcholine receptor subunit alpha-9
- Neuronal acetylcholine receptor subunit beta-2
- Acetylcholine receptor subunit alpha
Sequence:
MRGTPLLLVSLFALLQPGDCRLANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIRLELSLSQLISVNEREQIMTTSIWLKQEWTDYRLAWNSSCYEGVNILRIPAKRVWLPDIVLYNNADGTYEVSVYTNVIVRSNGSIQWLPPAIYKSACKIEVKHFPFDQQNCTLKFRSWTYDHTEIDMVLKSPTAIMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDIPLIGKYLLFTMVLVTFSIVTTVCVLNVHHRSPSTHTMASWVKECFLHKLPTFLFMKRPGLEVSPARVPHSSQLHLTTAEATSTSALGPSSPSNLYGNSMYFVNPVPATPKSAVSSHTAGLPRDARLRSSGRFRQDLQEALEGVSFIAQHLESDDRDQSVIEDWKFVAMVVDRLFLWVFVIVCILGTMGLFLPPLFQIHAPSKGL