wanglab/gogpt-training-data huggingface dataset:
Protein: 26S proteasome regulatory subunit RPN6 (Proteasome non-ATPase subunit 4) (Q12377)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.
Interaction partners:
- Proteasome subunit alpha type-2
- 26S proteasome regulatory subunit 8 homolog
- Proteasome subunit beta type-1
- Proteasome subunit beta type-2
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit RPN13
- Proteasome subunit beta type-5
- 26S proteasome regulatory subunit RPN7
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit RPN9
Sequence:
MSLPGSKLEEARRLVNEKQYNEAEQVYLSLLDKDSSQSSAAAGASVDDKRRNEQETSILELGQLYVTMGAKDKLREFIPHSTEYMMQFAKSKTVKVLKTLIEKFEQVPDSLDDQIFVCEKSIEFAKREKRVFLKHSLSIKLATLHYQKKQYKDSLALINDLLREFKKLDDKPSLVDVHLLESKVYHKLRNLAKSKASLTAARTAANSIYCPTQTVAELDLMSGILHCEDKDYKTAFSYFFESFESYHNLTTHNSYEKACQVLKYMLLSKIMLNLIDDVKNILNAKYTKETYQSRGIDAMKAVAEAYNNRSLLDFNTALKQYEKELMGDELTRSHFNALYDTLLESNLCKIIEPFECVEISHISKIIGLDTQQVEGKLSQMILDKIFYGVLDQGNGWLYVYETPNQDATYDSALELVGQLNKVVDQLFEKASVLY
Protein: Growth hormone (H6ULX1)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MAPGSWFSPLLIAVVTLGLPQEAAATFPAMPLSNLFANAVLRAQHLHLLAAETYKEFERTYIPEDQRYTNKNSQAAFCYSETIPAPTGKDDAQQKSDMEVVRFSLVFIQSWLTPVQYLSKVFTNKLVFGTSDRVFEKLKDLEEGIQALMRELEDRSPRGPQLLRPTYDKFDIHLRHGDALLNNYGLLSCFKKDLHKVETYLKVMKCRRFGESNCTI
Protein: DUF1279 domain-containing protein (Q57U97)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFVRLPTPGKTCVSRLLISRRFTSAKQHVTRRNISSHNGGATTGQKSVGGKNFAKRPEDIAPHSSKGSAAGPTMRRSRFYRIALDHGFGFAVYFYILGESMTLSVLYALHSNALGTGDTFAWMNAVGAERFVNLDRWAHAGPTVVGVTLSFRLLLNYLAANAIMYPMYGMQMRFCVATFGVLGKGFNPLRRLRALGRNVTSSGAKRTVPRAPSATAPKNKVNRLP
Protein: Sodium-coupled monocarboxylate transporter 1 (Apical iodide transporter) (Electrogenic sodium monocarboxylate cotransporter) (Sodium iodide-related cotransporter) (Solute carrier family 5 member 8) (Q8N695)
Organism: Homo sapiens (Human)
Function: Acts as an electrogenic sodium (Na(+)) and chloride (Cl-)-dependent sodium-coupled solute transporter, including transport of monocarboxylates (short-chain fatty acids including L-lactate, D-lactate, pyruvate, acetate, propionate, valerate and butyrate), lactate, mocarboxylate drugs (nicotinate, benzoate, salicylate and 5-aminosalicylate) and ketone bodies (beta-D-hydroxybutyrate, acetoacetate and alpha-ketoisocaproate), with a Na(+):substrate stoichiometry of between 4:1 and 2:1. Catalyzes passive carrier mediated diffusion of iodide. Mediates iodide transport from the thyrocyte into the colloid lumen through the apical membrane. May be responsible for the absorption of D-lactate and monocarboxylate drugs from the intestinal tract. Acts as a tumor suppressor, suppressing colony formation in colon cancer, prostate cancer and glioma cell lines. May play a critical role in the entry of L-lactate and ketone bodies into neurons by a process driven by an electrochemical Na(+) gradient and hence contribute to the maintenance of the energy status and function of neurons.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:12107270, ECO:0000269|PubMed:15001644, ECO:0000269|PubMed:17245649}; Multi-pass membrane protein {ECO:0000255}. Note=Expressed at the apical membrane of normal tall thyrocytes and of colonic epithelial cells. {ECO:0000269|PubMed:12107270, ECO:0000269|PubMed:15001644, ECO:0000269|PubMed:17245649}.
Interaction partners:
- Solute carrier family 22 member 12
- Pendrin
- Hydroxycarboxylic acid receptor 2
- CCAAT/enhancer-binding protein delta
- Solute carrier family 2, facilitated glucose transporter member 9
- Monocarboxylate transporter 1
- Solute carrier family 22 member 11
Sequence:
MDTPRGIGTFVVWDYVVFAGMLVISAAIGIYYAFAGGGQQTSKDFLMGGRRMTAVPVALSLTASFMSAVTVLGTPSEVYRFGAIFSIFAFTYFFVVVISAEVFLPVFYKLGITSTYEYLELRFNKCVRLCGTVLFIVQTILYTGIVIYAPALALNQVTGFDLWGAVVATGVVCTFYCTLGGLKAVIWTDVFQVGIMVAGFASVIIQAVVMQGGISTILNDAYDGGRLNFWNFNPNPLQRHTFWTIIIGGTFTWTSIYGVNQSQVQRYISCKSRFQAKLSLYINLVGLWAILTCSVFCGLALYSRYHDCDPWTAKKVSAPDQLMPYLVLDILQDYPGLPGLFVACAYSGTLSTVSSSINALAAVTVEDLIKPYFRSLSERSLSWISQGMSVVYGALCIGMAALASLMGALLQAALSVFGMVGGPLMGLFALGILVPFANSIGALVGLMAGFAISLWVGIGAQIYPPLPERTLPLHLDIQGCNSTYNETNLMTTTEMPFTTSVFQIYNVQRTPLMDNWYSLSYLYFSTVGTLVTLLVGILVSLSTGGRKQNLDPRYILTKEDFLSNFDIFKKKKHVLSYKSHPVEDGGTDNPAFNHIELNSDQSGKSNGTRL
Protein: Sensory transduction protein RegX3 (P9WGL9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Member of the two-component regulatory system SenX3/RegX3 involved in stress response. The system is involved in phosphate starvation response. Plays a role in modulating expression of aerobic response and in the regulation of response to hypoxia. Involved in virulence. Regulates dozens of genes, directly or indirectly. Is directly involved in the regulation of the expression of gltA, cydAB and ald. Binds to the upstream regions of the hypoxia-associated genes Rv3334, whiB7, Rv0195, Rv0196 and Rv1960c.
Interaction partners:
- Sensor-like histidine kinase SenX3
- histidine kinase
- Sensor histidine kinase component HK1
- Sensor histidine kinase TrcS
- Sensor-type histidine kinase PrrB
- Probable sensor histidine kinase TcrY
- Signal transduction histidine-protein kinase/phosphatase MprB
- Sensor histidine kinase MtrB
- Probable transcriptional regulatory protein NarL
Sequence:
MTSVLIVEDEESLADPLAFLLRKEGFEATVVTDGPAALAEFDRAGADIVLLDLMLPGMSGTDVCKQLRARSSVPVIMVTARDSEIDKVVGLELGADDYVTKPYSARELIARIRAVLRRGGDDDSEMSDGVLESGPVRMDVERHVVSVNGDTITLPLKEFDLLEYLMRNSGRVLTRGQLIDRVWGADYVGDTKTLDVHVKRLRSKIEADPANPVHLVTVRGLGYKLEG
Protein: NMDA receptor synaptonuclear signaling and neuronal migration factor (Juxtasynaptic attractor of caldendrin on dendritic boutons protein) (Jacob protein) (Nasal embryonic luteinizing hormone-releasing hormone factor) (Nasal embryonic LHRH factor) (Q9EPI6)
Organism: Rattus norvegicus (Rat)
Function: Couples NMDA-sensitive glutamate receptor signaling to the nucleus and triggers long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. Part of the cAMP response element-binding protein (CREB) shut-off signaling pathway. Stimulates outgrowth of olfactory axons and migration of gonadotropin-releasing hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH) neuronal cells.
Subcellular location: Nucleus. Nucleus envelope. Nucleus membrane. Nucleus matrix. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell projection, dendrite. Synapse. Synapse, synaptosome. Postsynaptic density. Membrane. Note=Found on the outside of the luteinizing-hormone-releasing hormone (LHRH) cell membrane and axons projecting from the olfactory pit and epithelium (By similarity). Associates with transcriptionally active chromatin regions. Detected at the nuclear membranes of CA1 neurons. Cortical cytoskeleton. Localized in proximal apical dendrites. Colocalizes with CABP1 in dendrites and dendritic spines. Myristoylation is a prerequisite for extranuclear localization. Translocates from dendrites to the nucleus during NMDA receptor-dependent long-term potentiation (LTP) induction of synaptic transmission at Schaffer collateral/CA1 synapses of hippocampal primary neurons and in an importin-dependent manner. {ECO:0000250}.
Interaction partners:
- Calcium-binding protein 1
- Heparan-sulfate 6-O-sulfotransferase
- Prokineticin receptor 2
- Prokineticin-2
- Neuromedin-K receptor
Sequence:
MGAAASRRRALRSEAMSSVAAKVRAARAFGEYLSQSHPENRNGADHLLADAYSGHEGSPEMQPAPHNKRRLSLVSNGRYEGSISDEAVSGKTATEGPQPRVYTISREPALLPGSEAEAIELAVVKGRRQRERHPHHHSQPLRASPGSSREDISRPCQSWAGSRQGSKECPGCAKLVPGPSPRAFGLEQPPLPEASGRHKKLERMYSVDGVSDDVPIRTWFPKENPFSFQTATTTMQAISVFRGYAERKRRKRENDSASVIQRNFRKHLRMVGSRRVKAQTFAERRERSFSRSWSDPTPMKADTSHDSRDSSDLQSSHCTLDEACEDLDWDTEKGLEATACDTEGFLPPKVMLISSKVPKAEYIPTIIRRDDPSIIPILYDHEHATFEDILEEIEKKLNIYHKGAKIWKMLIFCQGGPGHLYLLKNKVATFAKVEKEEDMIHFWKRLSRLMSKVNPEPNVIHIMGCYILGNPNGEKLFQNLRTLMTPYKVTFESPLELSAQGKQMIETYFDFRLYRLWKSRQHSKLLDFDDVL
Protein: H1.12 linker histone, cluster member (HIST1H1E protein) (A5PK20)
Organism: Bos taurus (Bovine)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU003894}.
Interaction partners:
Sequence:
MSETVPAAPPAPSPAEKTPVKKKARKSTSAPKRKASGPSVSDLITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAATGEAKPKAKKAGAAKPKKAAGAAKKPKKSTGAATPKKTAKTTLKKVKPATGAKKVAKSPKKVKTAKPKAAKSPVKAKVNKPKVAKPKAVQPKKATPKK
Protein: DNA-directed RNA polymerase II subunit RPB4 (RNA polymerase II subunit B4) (DNA-directed RNA polymerase II subunit D) (Q9D7M8)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB4 is part of a subcomplex with RPB7 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O15514}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB2
Sequence:
MAAGGSDPRAGDVEEDASQLIFPKEFETAETLLNSEVHMLLEHRKQQNESAEDEQELSEVFMKTLNYTARFSRFKNRETIASVRSLLLQKKLHKFELACLANLCPETAEESKALIPSLEGRFEDEELQQILDDIQTKRSFQY
Protein: Trafficking kinesin-binding protein 1 (106 kDa O-GlcNAc transferase-interacting protein) (Protein Milton) (Q9UPV9)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of endosome-to-lysosome trafficking, including endocytic trafficking of EGF-EGFR complexes and GABA-A receptors. Involved in mitochondrial motility. When O-glycosylated, abolishes mitochondrial motility. Crucial for recruiting OGT to the mitochondrial surface of neuronal processes. TRAK1 and RHOT form an essential protein complex that links KIF5 to mitochondria for light chain-independent, anterograde transport of mitochondria (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18986759}. Nucleus {ECO:0000269|PubMed:12435728}. Mitochondrion {ECO:0000269|PubMed:15644324, ECO:0000269|PubMed:16630562, ECO:0000269|PubMed:18675823, ECO:0000269|PubMed:19528298}. Early endosome {ECO:0000269|PubMed:18675823}. Endosome {ECO:0000269|PubMed:18675823}. Mitochondrion membrane {ECO:0000269|PubMed:24995978}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q6PD31}. Note=Predominantly associated with early endosome. The localization to early endosomes depends on its interaction with HGS/HRS (PubMed:18675823). Colocalizes with MGARP at the mitochondria (PubMed:19528298). {ECO:0000269|PubMed:18675823, ECO:0000269|PubMed:19528298}.
Interaction partners:
- Mitochondrial Rho GTPase 2
- Mitochondrial Rho GTPase 1
- Trafficking kinesin-binding protein 2
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Mitofusin-2
- Nuclear distribution protein nudE homolog 1
- Kinesin-1 heavy chain
- Kinesin heavy chain isoform 5A
- Disrupted in schizophrenia 1 protein
- Kinesin heavy chain isoform 5C
Sequence:
MALVFQFGQPVRAQPLPGLCHGKLIRTNACDVCNSTDLPEVEIISLLEEQLPHYKLRADTIYGYDHDDWLHTPLISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEASQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKACAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPNTTSRRYHSLGLFPMDSLAAEIEGTMRKELQLEEAESPDITHQKRVFETVRNINQVVKQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDIGNVVLDNKTNSIILETEAADLGNDERSKKPGTPGTPGSHDLETALRRLSLRRENYLSERRFFEEEQERKLQELAEKGELRSGSLTPTESIMSLGTHSRFSEFTGFSGMSFSSRSYLPEKLQIVKPLEGSATLHHWQQLAQPHLGGILDPRPGVVTKGFRTLDVDLDEVYCLNDFEEDDTGDHISLPRLATSTPVQHPETSAHHPGKCMSQTNSTFTFTTCRILHPSDELTRVTPSLNSAPTPACGSTSHLKSTPVATPCTPRRLSLAESFTNTRESTTTMSTSLGLVWLLKERGISAAVYDPQSWDRAGRGSLLHSYTPKMAVIPSTPPNSPMQTPTSSPPSFEFKCTSPPYDNFLASKPASSILREVREKNVRSSESQTDVSVSNLNLVDKVRRFGVAKVVNSGRAHVPTLTEEQGPLLCGPPGPAPALVPRGLVPEGLPLRCPTVTSAIGGLQLNSGIRRNRSFPTMVGSSMQMKAPVTLTSGILMGAKLSKQTSLR
Protein: Diacylglycerol kinase gamma (DAG kinase gamma) (EC 2.7.1.107) (Diglyceride kinase gamma) (DGK-gamma) (P49619)
Organism: Homo sapiens (Human)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (By similarity). Has no apparent specificity with regard to the acyl compositions of diacylglycerol. Specifically expressed in the cerebellum where it controls the level of diacylglycerol which in turn regulates the activity of protein kinase C gamma. Through protein kinase C gamma, indirectly regulates the dendritic development of Purkinje cells, cerebellar long term depression and ultimately cerebellar motor coordination (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:8034597}. Cytoplasm, cytosol {ECO:0000269|PubMed:8034597}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P49620}.
Interaction partners:
- Lipoprotein lipase
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
- Phospholipase D2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
Sequence:
MGEERWVSLTPEEFDQLQKYSEYSSKKIKDALTEFNEGGSLKQYDPHEPISYDVFKLFMRAYLEVDLPQPLSTHLFLAFSQKPRHETSDHPTEGASNSEANSADTNIQNADNATKADEACAPDTESNMAEKQAPAEDQVAATPLEPPVPRSSSSESPVVYLKDVVCYLSLLETGRPQDKLEFMFRLYDSDENGLLDQAEMDCIVNQMLHIAQYLEWDPTELRPILKEMLQGMDYDRDGFVSLQEWVHGGMTTIPLLVLLGMDDSGSKGDGRHAWTMKHFKKPTYCNFCHIMLMGVRKQGLCCTYCKYTVHERCVSRNIPGCVKTYSKAKRSGEVMQHAWVEGNSSVKCDRCHKSIKCYQSVTARHCVWCRMTFHRKCELSTLCDGGELRDHILLPTSICPITRDRPGEKSDGCVSAKGELVMQYKIIPTPGTHPLLVLVNPKSGGRQGERILRKFHYLLNPKQVFNLDNGGPTPGLNFFRDTPDFRVLACGGDGTVGWILDCIDKANFAKHPPVAVLPLGTGNDLARCLRWGGGYEGGSLTKILKDIEQSPLVMLDRWHLEVIPREEVENGDQVPYSIMNNYFSIGVDASIAHRFHVMREKHPEKFNSRMKNKLWYFEFGTSETFAATCKKLHDHIELECDGVGVDLSNIFLEGIAILNIPSMYGGTNLWGENKKNRAVIRESRKGVTDPKELKFCVQDLSDQLLEVVGLEGAMEMGQIYTGLKSAGRRLAQCASVTIRTNKLLPMQVDGEPWMQPCCTIKITHKNQAPMMMGPPQKSSFFSLRRKSRSKD
Protein: Nuclear pore complex interacting protein family member B2 (A0A5F9ZI19)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKVTTKINHHDKINGKRKTAKKQKLSVKECEHAEKERQVSEAEENGKLDMKEIHTYMKMFQRAQELRRRAEDYHKCKIPPSARKALCNWVRMAAAEHRHSSGLPYWPYLTAETLKNRMGHQPPPPTQQHSITDNSLSLKTPPECLLTPLPPSADDNLKTPPECLLTPLPPSAPPSADDNLKTPPLATQEAEAEKPPKPKRWRAAEMESPPEPKRRRAAEVESPPEPKRRRAAEVEPSSPEPKRRRLSKLRTGHCTQA
Protein: FAD-linked oxidoreductase easE (EC 1.-.-.-) (Ergot alkaloid synthesis protein E) (Q4WZ61)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: FAD binding oxidoreductase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Interaction partners:
- Festuclavine dehydrogenase easG
- Chanoclavine-I dehydrogenase easD
- Tryptophan dimethylallyltransferase
- Catalase easC
- 4-dimethylallyltryptophan N-methyltransferase easF
- Chanoclavine-I aldehyde reductase easA
Sequence:
MSHRILCVAFCVCSLVAVSSIYSPPFNHPIVYSNNAICFQLSTWRIPQLYLAVLIRRFDLSLSTRGVMLAVTVGVGSSQHHSQRSGLSLTFAMTPSMITLLVKTCVISQRTAVGEPHRPGWVWEVGRTEDETCHAHSPRGAPCHQGRIPLYSAAVESVDQIQVAVRFAQRHRLRLVVRNTGHDTAGRSSGSDSFQIHCHRMKQIEYHDNFRALGSDIDRGPAVSVGAGVTLGEMYARGARDGWVVVGGECPTVGAAGGFLQGGGVSSFHSFIDGLAVDNVLEFEVVTAKGDVVVANDHQNPDIFWALRGGGGGTFGIVTRATMRVHLNSPVCVSEVAVSGLRNNSLLWTKGITGLFSILRSFNQQGIPGQFILRPLSKDQVNASLTLYSLNTDDTRRSAENMLSIRNILESTTLPFTLASRCLPKISDALRKGPDMLPVNYGIITGSVLVSEDLFNSEEGPLHLAKQLEHFPMGPMDLLFTSNLGGNVSANTGKKHRDTSMHPGWRQAAHLINFVRSVSTPTAHEKARSLEELHSVQMRQLYDIEPDFRVSYRNLGDPLESDAAQVYWGPNYKRLLEIKRKWDPEDLFFSQLGVGSEGWTEDQMCKRQQRLQQMLQYLMSSIAQRVYR
Protein: Fc receptor-like A (Fc receptor homolog expressed in B-cells) (Fc receptor-like and mucin-like protein 1) (Fc receptor-like protein) (Fc receptor-related protein X) (FcRX) (Q7L513)
Organism: Homo sapiens (Human)
Function: May be implicated in B-cell differentiation and lymphomagenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11754007, ECO:0000269|PubMed:11891275, ECO:0000269|PubMed:15551350}. Note=Seems not to be secreted. {ECO:0000269|PubMed:11891275}.
Interaction partners:
- B-lymphocyte antigen CD19
- Pre-B lymphocyte protein 3
- Tyrosine-protein kinase Blk
- B-cell antigen receptor complex-associated protein alpha chain
- B-lymphocyte antigen CD20
- Protein Niban 3
- Homeobox protein Meis1
- B-cell antigen receptor complex-associated protein beta chain
- Homeobox protein Hox-A9
- Nuclear pore complex protein Nup98-Nup96
Sequence:
MKLGCVLMAWALYLSLGVLWVAQMLLAASFETLQCEGPVCTEESSCHTEDDLTDAREAGFQVKAYTFSEPFHLIVSYDWLILQGPAKPVFEGDLLVLRCQAWQDWPLTQVTFYRDGSALGPPGPNREFSITVVQKADSGHYHCSGIFQSPGPGIPETASVVAITVQELFPAPILRAVPSAEPQAGSPMTLSCQTKLPLQRSAARLLFSFYKDGRIVQSRGLSSEFQIPTASEDHSGSYWCEAATEDNQVWKQSPQLEIRVQGASSSAAPPTLNPAPQKSAAPGTAPEEAPGPLPPPPTPSSEDPGFSSPLGMPDPHLYHQMGLLLKHMQDVRVLLGHLLMELRELSGHRKPGTTKATAE
Protein: Chaperonin 60 subunit beta 2, chloroplastic (CPN-60 beta 2) (Q9LJE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in protein assisted folding.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19344532}.
Interaction partners:
- 20 kDa chaperonin, chloroplastic
- 10 kDa chaperonin 1
- 10 kDa chaperonin 2, chloroplastic
- Heat shock 70 kDa protein 10, mitochondrial
- Heat shock 70 kDa protein 7, chloroplastic
- Heat shock 70 kDa protein 6, chloroplastic
- Heat shock 70 kDa protein 9, mitochondrial
- Heat shock 70 kDa protein 4
- Protein groES
- T-complex protein 1 subunit theta
Sequence:
MASTFTATSSLGSLLAPNAIKLSSATSISSSSFGRRHNVCVRRSRPAIVCAAKELHFNKDGTTIRKLQTGVNKLADLVGVTLGPKGRNVVLESKYGSPRIVNDGVTVAREVELEDPVENIGAKLVRQAAAKTNDLAGDGTTTSVVLAQGFIAEGVKVVAAGANPVLITRGIEKTAKALVNELKLMSKEVEDSELADVAAVSAGNNHEVGSMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKVTNARDLVGVLEDAIRGGYPILIIAEDIEQEALATLVVNKLRGTLKIAALKAPGFGERKSQYLDDIAILTGATVIREEVGLSLDKAGKEVLGNASKVVLTKEMTTIVGDGTTQEAVNKRVVQIRNLIEQAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDALNATKAAVEEGIVVGGGCTLLRLASKVDAIKDTLENDEEKVGAEIVKRALSYPLKLIAKNAGVNGSVVSEKVLANDNVKFGYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLMSDCVVVEIPEPEPVPAGNPMDNSGYGY
Protein: ATP-dependent RNA helicase DBP3 (EC 3.6.4.13) (DEAD box protein 3) (Helicase CA3) (P20447)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent RNA helicase required for 60S ribosomal subunit synthesis. Involved in efficient pre-rRNA processing, predominantly at site A3, which is necessary for the normal formation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9032262}.
Interaction partners:
- Pescadillo homolog
- Ribosome biogenesis protein RLP7
- Ribosome biogenesis protein SSF1
- Nucleolar GTP-binding protein 2
- Ribosome biogenesis protein ERB1
- ATP-dependent RNA helicase DRS1
- 27S pre-rRNA
- Ribosome biogenesis protein YTM1
- Ribosome biogenesis protein MAK21
- Probable metalloprotease ARX1
Sequence:
MTKEEIADKKRKVVDEEVIEKKKSKKHKKDKKDKKEKKDKKHKKHKKEKKGEKEVEVPEKESEKKPEPTSAVASEFYVQSEALTSLPQSDIDEYFKENEIAVEDSLDLALRPLLSFDYLSLDSSIQAEISKFPKPTPIQAVAWPYLLSGKDVVGVAETGSGKTFAFGVPAISHLMNDQKKRGIQVLVISPTRELASQIYDNLIVLTDKVGMQCCCVYGGVPKDEQRIQLKKSQVVVATPGRLLDLLQEGSVDLSQVNYLVLDEADRMLEKGFEEDIKNIIRETDASKRQTLMFTATWPKEVRELASTFMNNPIKVSIGNTDQLTANKRITQIVEVVDPRGKERKLLELLKKYHSGPKKNEKVLIFALYKKEAARVERNLKYNGYNVAAIHGDLSQQQRTQALNEFKSGKSNLLLATDVAARGLDIPNVKTVINLTFPLTVEDYVHRIGRTGRAGQTGTAHTLFTEQEKHLAGGLVNVLNGANQPVPEDLIKFGTHTKKKEHSAYGSFFKDVDLTKKPKKITFD