wanglab/gogpt-training-data huggingface dataset:
Protein: Aminopeptidase (EC 3.4.11.-) (B0BCZ3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MNFAEREGSKRYCIQTKHVAILCAVVVGVGLIVGLAVGLTRSCDSSGDGGPGTAPAPSHLPSSTASPSGPPAQDQDICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINLSAPTRYLWLHLRETRITRLPELKRPSGDQVQVRRCFEYKKQEYVVVEAEEELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGQVKSIVATDHEPTDARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTTFEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANITKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFLGVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFDGISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEEASRLPVKEVMDTWTRQMGYPVLNVNGVKNITQKRFLLDPRANPSQPPSDLGYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSSNPSGNAFLKINPDHIGFYRVNYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVTLNLTKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREWFFNLLESG
Protein: Ribosomal protein uL30-like (60S ribosomal protein L7-like 1) (Large ribosomal subunit protein uL30-like 1) (Q6DKI1)
Organism: Homo sapiens (Human)
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein eL14
Sequence:
MISSCTTRKMAEQEQRKIPLVPENLLKKRKAYQALKATQAKQALLAKKEQKKGKGLRFKRLESFLHDSWRQKRDKVRLRRLEVKPHALELPDKHSLAFVVRIERIDGVSLLVQRTIARLRLKKIFSGVFVKVTPQNLKMLRIVEPYVTWGFPNLKSVRELILKRGQAKVKNKTIPLTDNTVIEEHLGKFGVICLEDLIHEIAFPGKHFQEISWFLCPFHLSVARHATKNRVGFLKEMGTPGYRGERINQLIRQLN
Protein: START domain-containing protein 10 (StARD10) (Antigen NY-CO-28) (PCTP-like protein) (PCTP-L) (Serologically defined colon cancer antigen 28) (StAR-related lipid transfer protein 10) (Q9Y365)
Organism: Homo sapiens (Human)
Function: May play metabolic roles in sperm maturation or fertilization (By similarity). Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:17561512}. Membrane {ECO:0000269|PubMed:17561512}. Note=In testis was predominantly detected at the flagella of elongated spermatids, with a strong signal also found at the tail of epididymal sperm (By similarity). Mainly cytosolic. {ECO:0000250}.
Interaction partners:
- Lysophosphatidylcholine acyltransferase 1
Sequence:
MEKLAASTEPQGPRPVLGRESVQVPDDQDFRSFRSECEAEVGWNLTYSRAGVSVWVQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACLKYPEWKQKHLPHFKPWLHPEQSPLPSLALSELSVQHADSLENIDESAVAESREERMGGAGGEGSDDDTSLT
Protein: Keratin-associated protein 6-3 (Q3LI67)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 6-1
- Keratin-associated protein 22-1
- Keratin-associated protein 6-2
- Keratin-associated protein 20-1
- Keratin-associated protein 26-1
- Keratin-associated protein 20-2
- Keratin-associated protein 24-1
- Keratin-associated protein 15-1
- Small cysteine and glycine repeat-containing protein 1
- Keratin-associated protein 8-1
Sequence:
MTSTTNTMCGSYYRNYNGGHGYGCCGYGGLGCGYGGCGYGCCGYGGLGFGYGGLDCGYGGLGCGYGSFCGCGYRGLDCGYGCGYGYVSHSFCGCGYRCGSGYGSSFGYYY
Protein: Epithelial V-like antigen 1 (Myelin protein zero-like 2) (Q8JG36)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRRMWIYLSSALCALVFTGVYQVEGMEVFTSSELEAVNGTEIRLKCTFKSNRPLSEERTSVSWSFMPLGKTKEEPFFHYQGHAYLPPGGLFKDHVVWSGDVMKGDGSITLQDVQFSFNGTYSCQVLNPPDIQGFAGEIKLRVVQKVSFSEIGILAIAVGGSIGVILLILIIYIVVRVFRRREEDMTIETEDHRSKDQVL
Protein: Nucleus-vacuole junction protein 2 (O94464)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, induces contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Single-pass type II membrane protein {ECO:0000305}. Note=Enriched at the nucleus-vacuole junction (By similarity). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (By similarity). {ECO:0000250|UniProtKB:Q06833}.
Interaction partners:
- Seipin homolog
- Protein bem46
- Putative cell signaling protein
Sequence:
MFFAFLITYLLGGVTFLPFILFIYLLTRPTHKSEELRIIEPNNDCLTKLDKDIRIQGWIRVTTKFLQGKSGSVKVQEIPQDQLPKSSSDNAVTDRKTISPSGINNQYVIRNPKDVYYATVQAGKLHLFDPVKTSELLHVINLHEYLVVFYPGTVTENELFSNRNAIFLKYPAVSHKKESSTKSLLNKDLYVYGRTPSNKEDWNYALLSYSKISPAIKPLEAPIDFDYASVHHNLTALSSPDTDWLNAFIGRIFLGIHKTEGFKSLVVEKLTKKLSRIKTPGIMTDVKVIDVDVGEAIPTVNGLKFESLSNGGELIVSADIWYEGDCSFKAETTANIKFGSHFPSKTVPLALVIRLTHVSGKVRLLIKPPPSNRVWYAFYEKPRLHLIVEPMVARKQLTNNYLINFITQKLVELVHETIVMPNMNDLAFFIDNEAPIKGGLWDIELFRAPTIQKPAEKDAKAERKKSGLSSSTSEESLNRHISKRSSNSNDTAPSSHIIADKNLEPTSNIQLKKNPDGNLVETSELSDSDENSVLSNKSSTLSKKVVENTSPLKYTHSASKSFIGEVQDSLQALKTKAHKPRSIGGDSSQTTLSETTKKYGSVAKKSFFQGVSDAKSFVKKIKSTYIDDSSSNSPSDIESNYSADDNEISKSKAQNAIDFNVTNTHSPSRSISSEKSYKAAERGQQDKHNDVLVDLNPNVEAEKSNPHSNSQKTSKNDMSRNQRNKYAKEIMTGQPTLHPQGQLPIQNVEQRATHKPLPRPPVQVETREPVRPVPPIPKL
Protein: Nostrin (A8WFV6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKDPLSSCTYNLLYQELKRISKNGEFFCKELLAVFQQRSELEINYSKGLQKIAGKLLKVSKEMSDNSTYHAWSFISDEMFASADAHRILGNALNQDVIQEIRQILDEHGKRKRPLDNAVEKSGKLVLTNWSEQIKLKKKLIGLTREHEALFSFVEKNKQICTEKEKQKMFNRLSKSAELQVRVDEEYFNTNMEGHHIRLKLENTVKTCYQIVQELEKQRIETLANTLNKYSLFMTVYSQTVIHSHKQIDQAVRRVDVEKDIQSLVEDVATTADENKAEFLMADYFEEEGKTMMGKDRRKDAIRTKLQRLEDWITKSKTDREGLEKMVKVYTEQPNFSNQKNLEETEQLLEEAILKLDLLEATHCKLTHSLAEIEGKPKSRHRFSDSITKWKEKDCEHSVVQLSRPVRIKKTPFRSRQSMRATVSNETSPSPEGTGENPLNEATNSDGQKNGPVNGSVSEYEDDKGAELCCIGRCKALYSFASEREDELNINEGDVLEIFEKDDTGWWFGELNGQRGLFPSTYVEELPVFTAMKSSDA
Protein: Lysophospholipase L2 (EC 3.1.1.5) (Lecithinase B) (P07000)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Peripheral membrane protein.
Interaction partners:
- Pyridoxal phosphate phosphatase YigL
- Phospholipase A1
- Bifunctional protein Aas--phospholipid O-acyltransferase); Acyl-[acyl-carrier-protein] synthetase
- Glycerophosphodiester phosphodiesterase, periplasmic
- Glycerophosphodiester phosphodiesterase, cytoplasmic
- Biotin transporter
- NADH-quinone oxidoreductase subunit C/D
- Thioesterase 1/protease 1/lysophospholipase L1
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit G
Sequence:
MFQQQKDWETRENAFAAFTMGPLTDFWRQRDEAEFTGVDDIPVRFVRFRAQHHDRVVVICPGRIESYVKYAELAYDLFHLGFDVLIIDHRGQGRSGRLLADPHLGHVNRFNDYVDDLAAFWQQEVQPGPWRKRYILAHSMGGAISTLFLQRHPGVCDAIALTAPMFGIVIRMPSFMARQILNWAEAHPRFRDGYAIGTGRWRALPFAINVLTHSRQRYRRNLRFYADDPTIRVGGPTYHWVRESILAGEQVLAGAGDDATPTLLLQAEEERVVDNRMHDRFCELRTAAGHPVEGGRPLVIKGAYHEILFEKDAMRSVALHAIVDFFNRHNSPSGNRSTEV
Protein: CD160 antigen (Natural killer cell receptor BY55) (CD antigen CD160) [Cleaved into: CD160 antigen, soluble form] (O95971)
Organism: Homo sapiens (Human)
Function: Receptor on immune cells capable to deliver stimulatory or inhibitory signals that regulate cell activation and differentiation. Exists as a GPI-anchored and as a transmembrane form, each likely initiating distinct signaling pathways via phosphoinositol 3-kinase in activated NK cells and via LCK and CD247/CD3 zeta chain in activated T cells. Receptor for both classical and non-classical MHC class I molecules. In the context of acute viral infection, recognizes HLA-C and triggers NK cell cytotoxic activity, likely playing a role in anti-viral innate immune response. On CD8+ T cells, binds HLA-A2-B2M in complex with a viral peptide and provides a costimulatory signal to activated/memory T cells. Upon persistent antigen stimulation, such as occurs during chronic viral infection, may progressively inhibit TCR signaling in memory CD8+ T cells, contributing to T cell exhaustion. On endothelial cells, recognizes HLA-G and controls angiogenesis in immune privileged sites. Receptor or ligand for TNF superfamily member TNFRSF14, participating in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. Upon ligation of TNFRSF14, provides stimulatory signal to NK cells enhancing IFNG production and anti-tumor immune response (By similarity). On activated CD4+ T cells, interacts with TNFRSF14 and down-regulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response. In the context of bacterial infection, acts as a ligand for TNFRSF14 on epithelial cells, triggering the production of antimicrobial proteins and pro-inflammatory cytokines (By similarity).
Subcellular location: [CD160 antigen]: Cell membrane {ECO:0000269|PubMed:12486241, ECO:0000269|PubMed:18193050, ECO:0000269|PubMed:9973372}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23761635, ECO:0000269|PubMed:9743336}.; SUBCELLULAR LOCATION: [CD160 antigen, soluble form]: Secreted. Note=Released from the cell membrane by GPI cleavage. {ECO:0000269|PubMed:17237375, ECO:0000269|PubMed:23761635, ECO:0000269|PubMed:9743336}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 14
- HLA class I histocompatibility antigen, alpha chain G
- Tumor necrosis factor ligand superfamily member 14
- B- and T-lymphocyte attenuator
- HLA class I histocompatibility antigen, C alpha chain
- T-cell surface glycoprotein CD8 alpha chain
- Killer cell lectin-like receptor subfamily F member 1
- Killer cell lectin-like receptor subfamily G member 1
- Natural killer cells antigen CD94
- Lymphocyte activation gene 3 protein
Sequence:
MLLEPGRGCCALAILLAIVDIQSGGCINITSSASQEGTRLNLICTVWHKKEEAEGFVVFLCKDRSGDCSPETSLKQLRLKRDPGIDGVGEISSQLMFTISQVTPLHSGTYQCCARSQKSGIRLQGHFFSILFTETGNYTVTGLKQRQHLEFSHNEGTLSSGFLQEKVWVMLVTSLVALQAL
Protein: Serine/threonine-protein kinase D6PK (EC 2.7.11.1) (D6 protein kinase) (Serine/threonine-protein kinase 64) (AtPK64) (Serine/threonine-protein kinase AGC1-1) (Q9FG74)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein kinase that regulates the auxin transport activity of PIN auxin efflux facilitators by direct phosphorylation. D6PK-mediated PIN phosphorylation promotes auxin transport in the hypocotyl and this is a prerequisite for PHOT1-dependent hypocotyl bending. Phosphorylates PIN1, PIN2, PIN3, PIN4 and PIN7 in vitro and PIN1 in vivo. Acts as a lipid domain-dependent mediator of root epidermal planar polarity via the binding to phosphatidylinositol phosphates (e.g. PtdIns(3)P, PtdIns(4)P, PtdIns(5)P, PtdIns(3,5)P(2), PtdIns(4,5)P(2), PtdIns(3,4,5)P(3) and phosphatidic acid).
Subcellular location: Cell membrane {ECO:0000269|PubMed:19168677, ECO:0000269|PubMed:27251533, ECO:0000269|PubMed:33705718}; Peripheral membrane protein {ECO:0000269|PubMed:19168677}. Note=Colocalizes with PIN1 to the basal (lower) membrane of root stele, cortex, epidermis and lateral root cap cells (PubMed:19168677). Undergoes a phosphatidylinositol-4,5-bisphosphate- and sterol-dependent basal-to-planar polarity switching into the polar, lipid-enriched domain of root hair-forming cells just before hair formation; this process is mediated by DRP1A and PIP5K3 (PubMed:27251533). {ECO:0000269|PubMed:19168677, ECO:0000269|PubMed:27251533}.
Interaction partners:
- Auxin efflux carrier component 3
- Auxin efflux carrier component 4
- Auxin efflux carrier component 2
- Auxin efflux carrier component 7
- Protein BREVIS RADIX
- Peptidyl-prolyl cis-trans isomerase Pin1
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Peptidyl-prolyl cis-trans isomerase FKBP42
- ABC transporter B family member 1
- Phototropic-responsive NPH3 family protein NPY1
Sequence:
MMASKTPEGSLTNSSQSMSINTLADQVSSSLSFADPSSDGKTGNSKINEQGESGKSSTCRPSTSSDISDESTCSSFSSSINKPHKANDVRWEAIQAVRTKHGGLGLNHFRLLKRLGCGDIGTVHLAELNGTRCYFAMKVMDKTALASRKKLLRAQTEREILQCLDHPFLPTLYSHFETEKFSCLVMEFCPGGDLHTLRQRQPGKRFTEQAAKFYVAEVLLAMEYLHMLGIIYRDLKPENVLVRDDGHVMLSDFDLSLRCTVSLSIVRSANVGSEGLSKNSVSCSQQPACIQQPSCISMAPTSCFGPRFFSSKSKKDKKPKTENGNHQVTPLPELVAEPTGARSMSFVGTHEYLAPEIIKGEGHGSAVDWWTFGIFLYELLFGKTPFKGSGNRATLFNVVGQPLRFPESPVVSFAARDLIRSLLVKEPQHRLAYKRGATEIKQHPFFEGVNWALVRCASPPEIPKPVDLEALNPTPTVPAAASSSVRSDQSNYLEFDFF
Protein: E3 ubiquitin-protein ligase SIAH1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1) (Seven in absentia homolog 1) (Siah-1) (Siah-1a) (Q8IUQ4)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2 through proteasomal degradation. It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling. Has some overlapping function with SIAH2. Induces apoptosis in cooperation with PEG3 (By similarity). Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus (By similarity). GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins (By similarity). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1.
Subcellular location: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic. Partially nuclear.
Interaction partners:
- Calcyclin-binding protein
- Glyceraldehyde-3-phosphate dehydrogenase
- Axin-1
- Catenin beta-1
- Synphilin-1
- Ubiquitin carboxyl-terminal hydrolase 19
- Alpha-synuclein
- Ubiquitin/ISG15-conjugating enzyme E2 L6
- Adenomatous polyposis coli protein
- S-phase kinase-associated protein 1
Sequence:
MSRQTATALPTGTSKCPPSQRVPALTGTTASNNDLASLFECPVCFDYVLPPILQCQSGHLVCSNCRPKLTCCPTCRGPLGSIRNLAMEKVANSVLFPCKYASSGCEITLPHTEKADHEELCEFRPYSCPCPGASCKWQGSLDAVMPHLMHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFFAIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQLFAENGNLGINVTISMC
Protein: Chaperone DnaJ-domain superfamily protein (Q8RWZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Actin-related protein 4
- Armadillo repeat-containing protein LFR
- At3g01890
- SWI/SNF complex component SNF12 homolog
- Histone H4
- SWI/SNF complex subunit SWI3D
- SWI/SNF complex subunit SWI3B
- SWI/SNF complex subunit SWI3C
- SWI/SNF complex subunit SWI3A
- Putative high mobility group B protein 11
Sequence:
MRSIYVHRKEVMGENRQIRSRSWNRMPTKRCSANGIMEEFILVDDDDVIILDFPESSKRKAPGTSRTRKESIMPRVISIDDDDDETENVQKAGSSSSGNLQTSAEVDNDDCQFIQEKCATFRFSKCKQTFSTMPSHGIRFGLGSDTYSDFSESDCSDCEILEGSHRDVREQWEQAALLRKMKKAGKAGLSEEAGPSNLHCDTNFEPGFERRTEQHDQTSFFFAARNPDGGKAGLTEEAGPSNLHCDNNFRPGFESRTEQHDQTSFFFTASNPDGEKETSSTFFGADGRIPDMTTYFGSVMEEDNQAKHTANSTFSSKEDFRGPSPLSPGIRVEHERFDTPPTHFTSPKEPIHQTSFKKVVEQPNKVQVQCETSLSPEENQNKNVAYQSYTKEVEEEEDASKLSPPQTSNGYGDTTHVFGTQSNGARCEHGISLDESREPIIDPIPSTSGQVQGTNGTAPAIDVMLNREILKETDEYKRAQEEEWESRQRQLQIQADEAQKQRKRRKLENMRKLEMERRQKERVEEVRETQKKDEENMNMKEKVRAEITKSLKLLELKSFNMAALLRGLGIQVGGGISPLPNEVHAAYKRAVLKFHPDRASRGGDIKQQVEAEEKFKLIARMKDKFKLIAP
Protein: Small GTP-binding protein Rab18 (D6XLL1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Rab GDP dissociation inhibitor
- Rab3 GTPase-activating protein catalytic subunit
- Geranylgeranyl transferase type-2 subunit alpha
- Geranylgeranyl transferase type-2 subunit beta
- Small GTP-binding protein RAB6, putative
Sequence:
MAQGDNSPVKIVLLGESGVGKSSLLLSFSLGTFDGDVRSTIGIDFRTKDVSVVDSMGRQKKLKLHLWDTAGQERFRTLTSSYYRGAHAVVLVYDVNEPQTFHALRKWIDEADAFCRLDGVEEAVVYLLVGNKIDKCEVGGGATGMAVPKEDAQQLARDRHMLLAFTSAKTRVGVEQAFDEVARSAYEKMMSKSESRYSGVNLSKTSDPTSGAVCC
Protein: Nitrogen regulatory protein P-II 1 (P0A9Z1)
Organism: Escherichia coli (strain K12)
Function: P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme.
Interaction partners:
- Sensory histidine kinase/phosphatase NtrB)
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- Ammonium transporter AmtB
- Glutamine synthetase
- Nitrogen regulatory protein GlnK
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- DNA-binding transcriptional regulator NtrC)
- Aspartate ammonia-lyase
- Glucosamine-6-phosphate deaminase
- Uncharacterized protein YfhG
Sequence:
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI
Protein: Homeobox protein BarH-like 1 (BarH-class homeodomain transcription factor 4) (Q503F2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor, is involved in craniofacial development, and in stomach organogenesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Paired box protein Pax-9
- LIM homeobox 6
- LIM homeobox 8a.
Sequence:
MQHPLEIGAHYYPPDAHLDQRSHRYRSFMIEEILTDHPDQKISSPTGDLLKFGVHALLSARPYHNHLVLKADQTGILKFPVSPLSCSLGAPLSSALLSGAAGLQVGSSSHHLPLDLHLRGKLDPGADAVSKTKKGRRSRTVFTELQLMGLEKRFEKQKYLSTPDRIDLAESLGLSQLQVKTWYQNRRMKWKKIVLQGGGLESPTKPKGRPKKNSIPTSEQLSEQERTREADRLSDGGASSLSDANQEE
Protein: Large ribosomal subunit protein bL31m (54S ribosomal protein L36, mitochondrial) (YmL36) (P36531)
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. Overexpression of bL31m suppresses mutations in the COX2 leader peptide-encoding and initiation codon regions.
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 uL23m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein mL38
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL5m
Sequence:
MLKSIFAKRFASTGSYPGSTRITLPRRPAKKIQLGKSRPAIYHQFNVKMELSDGSVVIRRSQYPKGEIRLIQDQRNNPLWNPSRDDLVVVDANSGGSLDRFNKRYSSLFSVDSTTPNSSSETVELSEENKKKTQIKKEEKEDVSEKAFGMDDYLSLLDDSEQQIKSGKLASKKRDKK
Protein: Fumarate hydratase 1, mitochondrial (AtFUM1) (Fumarase 1) (EC 4.2.1.2) (P93033)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:20202172, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Malate dehydrogenase 2, cytoplasmic
- Malate dehydrogenase 1, cytoplasmic
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Malate dehydrogenase 1, peroxisomal
- Malate dehydrogenase 1, mitochondrial
- NAD-dependent malic enzyme 2, mitochondrial
Sequence:
MSIYVASRRLSGGTTVTALRYATSLRSYSTSFREERDTFGPIQVPSDKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGVLKKCAAKVNMEYGLDPTIGKAIMQAAQEVAEGKLNDHFPLVVWQTGSGTQSNMNANEVIANRAAEILGRKRGEKCVHPNDHVNRSQSSNDTFPTVMHIAAATEINSRLIPSLKTLHSTLESKSFEFKDIVKIGRTHTQDATPLTLGQEFGGYATQVKYGLNRVTCTLPRLYQLAQGGTAVGTGLNTKKGFDVKIAAAVAEETNLPFVTAENKFEALAAHDACVETSGSLNTIATSLMKIANDIRFLGSGPRCGLGELVLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAVTVGGSNGHFELNVFKPVIASALLHSVRLIADASASFEKNCVRGIEANRERISKLLHESLMLVTSLNPKIGYDNAAAVAKKAHKEGCTLKEAALNLGVLTAEEFDTLVVPEKMIGPSD
Protein: Transcription elongation factor SPT4 (J3QSB9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR025023}.
Interaction partners:
Sequence:
MLISPFPLFFFHSQTIDQFEYDGCDNCDAYLQMKGNREMVYDCTSSSFDGIIAMMSPEDSWVSKWQRVSNFKPGVYAVSVTGRLPQGIVRELKSRGVAYKSRDTAIKT
Protein: Sarcoglycan, alpha (A0A8I5Y0I5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004513}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004513}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MVAAATWIPLLAGLLAGLRDSKAQQTTLHPLVGRVFVHPLEHATFLRLPEHIAVPPTVRLTYHAHLQGHPDLPRWLHYTQRSPYNPGFLYGTPTPEDRGHQVIEVTAYNRDSFDTTRQRLLLLIGDPEGPRLPYQAEFLVRSHDVEEVLPSTPANRFLTALGGLWEPGELQLLNITSALDRGGRVPLPIEGRKEGVYIKVGSATPFSTCLKMVASPDSYARCAQGQPPLLSCYDTLAPHFRVDWCNVSLVDKSVPEPLDEVPTPGDGILEHDPFFCPPTEATGRDFLTDALVTLLVPVLVALLLTLLLVYIMCCRREGRIQMFHHCSIHGNTEELRQMAASREVPRPLSTLPMFNVRTGERLPPRVDSAQMPLILDQH