wanglab/gogpt-training-data huggingface dataset:
Protein: WD repeat domain 27 (H7C3H5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XEVEAALYYKDFQSLSILLAGSCALRNRTADQKVLCLLASLFGGKIAVLEINPAALVRAQQCPSMGQSLSVPASSCVLPTSPLYLGIAKEKSTKAASEQRRAARNVMKDQRLVFHSKVRSSGYASAPHVTMFSPKTNIKSEGKGSSRSRSSCAREAYPVECAVPTKPGPQVAAAPTCTRVCCIQYSGAPRPAGAG
Protein: Sphingosine-1-phosphate transporter SPNS2 (Protein spinster homolog 2) (Q8IVW8)
Organism: Homo sapiens (Human)
Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate (sphing-4-enine 1-phosphate, S1P) and sphinganine-1-phosphate in the lymph, thereby playing a role in lymphocyte trafficking. S1P is a bioactive signaling molecule that regulates many physiological processes important for the development and for the immune system. Regulates levels of S1P and the S1P gradient that exists between the high circulating concentrations of S1P and low tissue levels that control lymphocyte trafficking. Required for the egress of T-cells from lymph nodes during an immune response by mediating S1P secretion, which generates a gradient that enables activated T-cells to access lymph (By similarity). Also required for the egress of immature B-cells from the bone marrow (By similarity). In contrast, not involved in S1P release from red blood cells (By similarity). Involved in auditory function. S1P release in the inner ear is required for maintenance of the endocochlear potential in the cochlea (By similarity). In addition to export, also able to mediate S1P import (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:A2SWM2}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:A2SWM2}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sphingosine-1-phosphate transporter MFSD2B
- Sphingosine kinase 1
- Sphingosine 1-phosphate receptor 2
- Sphingosine kinase 2
Sequence:
MMCLECASAAAGGAEEEEADAERRRRRRGAQRGAGGSGCCGARGAGGAGVSAAGDEVQTLSGSVRRAPTGPPGTPGTPGCAATAKGPGAQQPKPASLGRGRGAAAAILSLGNVLNYLDRYTVAGVLLDIQQHFGVKDRGAGLLQSVFICSFMVAAPIFGYLGDRFNRKVILSCGIFFWSAVTFSSSFIPQQYFWLLVLSRGLVGIGEASYSTIAPTIIGDLFTKNTRTLMLSVFYFAIPLGSGLGYITGSSVKQAAGDWHWALRVSPVLGMITGTLILILVPATKRGHADQLGDQLKARTSWLRDMKALIRNRSYVFSSLATSAVSFATGALGMWIPLYLHRAQVVQKTAETCNSPPCGAKDSLIFGAITCFTGFLGVVTGAGATRWCRLKTQRADPLVCAVGMLGSAIFICLIFVAAKSSIVGAYICIFVGETLLFSNWAITADILMYVVIPTRRATAVALQSFTSHLLGDAGSPYLIGFISDLIRQSTKDSPLWEFLSLGYALMLCPFVVVLGGMFFLATALFFVSDRARAEQQVNQLAMPPASVKV
Protein: Neurogenic differentiation factor 2 (NeuroD2) (Class A basic helix-loop-helix protein 1) (bHLHa1) (NeuroD-related factor) (NDRF) (Q15784)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator implicated in neuronal determination. Mediates calcium-dependent transcription activation by binding to E box-containing promoter. Critical factor essential for the repression of the genetic program for neuronal differentiation; prevents the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Induces transcription of ZEB1, which in turn represses neuronal differentiation by down-regulating REST expression. Plays a role in the establishment and maturation of thalamocortical connections; involved in the segregation of thalamic afferents into distinct barrel domains within layer VI of the somatosensory cortex. Involved in the development of the cerebellar and hippocampal granular neurons, neurons in the basolateral nucleus of amygdala and the hypothalamic-pituitary axis. Associates with chromatin to the DPYSL3 E box-containing promoter (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Complexin-2
- Cell division cycle protein 20 homolog
- G protein-activated inward rectifier potassium channel 1
- Anaphase-promoting complex subunit 1
- T-box brain protein 1
- Myelin transcription factor 1-like protein
- Achaete-scute homolog 1
Sequence:
MLTRLFSEPGLLSDVPKFASWGDGEDDEPRSDKGDAPPPPPPAPGPGAPGPARAAKPVPLRGEEGTEATLAEVKEEGELGGEEEEEEEEEEGLDEAEGERPKKRGPKKRKMTKARLERSKLRRQKANARERNRMHDLNAALDNLRKVVPCYSKTQKLSKIETLRLAKNYIWALSEILRSGKRPDLVSYVQTLCKGLSQPTTNLVAGCLQLNSRNFLTEQGADGAGRFHGSGGPFAMHPYPYPCSRLAGAQCQAAGGLGGGAAHALRTHGYCAAYETLYAAAGGGGASPDYNSSEYEGPLSPPLCLNGNFSLKQDSSPDHEKSYHYSMHYSALPGSRPTGHGLVFGSSAVRGGVHSENLLSYDMHLHHDRGPMYEELNAFFHN
Protein: Probable BOI-related E3 ubiquitin-protein ligase 2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRG2) (F4IDI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable E3 ubiquitin-protein ligase. Has no effect on the stability of the DELLA proteins.
Interaction partners:
- Monocopper oxidase-like protein SKS2
- Protein trichome birefringence-like 20
- Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 5
- F-box protein PP2-A14
- F-box/kelch-repeat protein At3g27150
- PsbP domain-containing protein 5, chloroplastic
- F-box/kelch-repeat protein At1g23390
Sequence:
MAVDAHHLFLSPPQLFSNRELTMNNNTMEPTSGGFCNNNQTGYGVVSPFSVPNHTSTTTTATPPLLHVYGGSDTIPTTAGYYADGATNLDCEFFPLPTRKRSRDSSRSNYHHLLLQNPRSSSCVNAATTTTTTTLFSFLGQDIDISSHMNQQQHEIDRFVSLHLYQMERVKYEIEEKRKRQARTIMEAIEQGLVKRLRVKEEERERIGKVNHALEERVKSLSIENQIWRDLAQTNEATANHLRTNLEHVLAQVKDVSRGAGLEKNMNEEDDAESCCGSSCGGGGEETVRRRVGLEREAQDKAERRRRRMCRNCGEEESCVLLLPCRHLCLCGVCGSSVHTCPICTSPKNASVHVNMSS
Protein: POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1) (P25425)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR.
Subcellular location: Nucleus.
Interaction partners:
- Host cell factor 1
- POU domain class 2-associating factor 1
- Breast cancer type 1 susceptibility protein homolog
- Transcription factor Sp1
- POU domain, class 2, transcription factor 2
Sequence:
MNNPSETNKSSMESEDASTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSSEESGDSQQSSQPSSQPPSVQSAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQPQPSITLTSQPTTPTRTIAAASVQTLPQSQSTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENLSSDSTASSPSALNSPGLGAEGLNRRRKKRTSIETNIRVALEKSFMENQKPTSEDITLIAEQLNMEKEVIRVWFCNRRQKEKRINPPSSGGTSSSPIKAIFPSPASLVATTPSLVTSSTATTLTVNPVLPLTSAAVTNLSLTDQDLRRGCSWEVLRSLPDRVTTTAGTTDSTSNNNTATVISTAPPASSAVTSPSLSPSPSASASTSEASSASETNTTQTTSTPLPSPLGASQVMVTTPGLQTAAAALQGAAQLPANASLAAMAAAAGLSPGLMAPSQFAAGGALLSLSPGTLGSALSPALMSNSTLATIQALASSGSLPITSLDATGNLVFANAGGAPNIVTAPLFLNPQNLSLLTSNPVSLVSAAAASTGNSAPTASLHASSTSTESIQSSLFTVASASGPASTTTAASKAQ
Protein: Gamma-aminobutyric acid receptor subunit gamma-2 (GABA(A) receptor subunit gamma-2) (GABAAR subunit gamma-2) (P18508)
Organism: Rattus norvegicus (Rat)
Function: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel (By similarity). The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta2/gamma2 receptor, alpha2/beta2/gamma2 receptor and the alpha1/beta3/gamma2 receptor exhibit synaptogenic activity whereas the alpha2/beta3/gamma2 receptor shows very little or no synaptogenic activity (By similarity). Functions also as histamine receptor and mediates cellular responses to histamine (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:2561970, ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18507}. Cell membrane {ECO:0000269|PubMed:2561970, ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18507}. Cell projection, dendrite {ECO:0000250|UniProtKB:P22723}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25172774}. Note=The gamma-2 subunits are present in Golgi synapses and on the extrasynaptic membranes (when associated with alpha-1/6 and beta-2/3 subunits), and in some of the mossy fiber to granule cell synapses (when associated with alpha-6 and beta-2/3 subunits). Present in GABAergic and glutamatergic synapses on granule cells. {ECO:0000269|PubMed:9464994}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor subunit beta-3
- Gamma-aminobutyric acid receptor subunit beta-1
- Trafficking kinesin-binding protein 2
- Huntingtin-associated protein 1
- Inactive phospholipase C-like protein 1
- Vesicle-fusing ATPase
- Gamma-aminobutyric acid receptor-associated protein-like 1
Sequence:
MSSPNTWSTGSTVYSPVFSQKMTLWILLLLSLYPGFTSQKSDDDYEDYASNKTWVLTPKVPEGDVTVILNNLLEGYDNKLRPDIGVKPTLIHTDMYVNSIGPVNAINMEYTIDIFFAQTWYDRRLKFNSTIKVLRLNSNMVGKIWIPDTFFRNSKKADAHWITTPNRMLRIWNDGRVLYTLRLTIDAECQLQLHNFPMDEHSCPLEFSSYGYPREEIVYQWKRSSVEVGDTRSWRLYQFSFVGLRNTTEVVKTTSGDYVVMSVYFDLSRRMGYFTIQTYIPCTLIVVLSWVSFWINKDAVPARTSLGITTVLTMTTLSTIARKSLPKVSYVTAMDLFVSVCFIFVFSALVEYGTLHYFVSNRKPSKDKDKKKKNPAPTIDIRPRSATIQMNNATHLQERDEEYGYECLDGKDCASFFCCFEDCRTGAWRHGRIHIRIAKMDSYARIFFPTAFCLFNLVYWVSYLYL
Protein: NADPH-dependent diflavin oxidoreductase 1 (EC 1.18.1.-) (NADPH-dependent FMN and FAD-containing oxidoreductase) (Novel reductase 1) (Q9UHB4)
Organism: Homo sapiens (Human)
Function: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of CISD1 and activate this protein implicated in Fe/S cluster repair. In vitro can fully activate methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03178, ECO:0000269|PubMed:10625700, ECO:0000269|PubMed:12871939}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178, ECO:0000269|PubMed:12871939}.
Interaction partners:
- Anamorsin
- m7GpppX diphosphatase
- Cytochrome P450 4F8
- Cytochrome P450 3A4)
- Cytochrome P450 4X1
- Cytosolic Fe-S cluster assembly factor NUBP1
- Cytochrome P450 4F3
- Cytochrome P450 4F11
- Regulator of telomere elongation helicase 1
- Glutaredoxin-3
Sequence:
MPSPQLLVLFGSQTGTAQDVSERLGREARRRRLGCRVQALDSYPVVNLINEPLVIFVCATTGQGDPPDNMKNFWRFIFRKNLPSTALCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPVCLGDDQHELGPDAAVDPWLRDLWDRVLGLYPPPPGLTEIPPGVPLPSKFTLLFLQEAPSTGSEGQRVAHPGSQEPPSESKPFLAPMISNQRVTGPSHFQDVRLIEFDILGSGISFAAGDVVLIQPSNSAAHVQRFCQVLGLDPDQLFMLQPREPDVSSPTRLPQPCSMRHLVSHYLDIASVPRRSFFELLACLSLHELEREKLLEFSSAQGQEELFEYCNRPRRTILEVLCDFPHTAAAIPPDYLLDLIPVIRPRAFSIASSLLTHPSRLQILVAVVQFQTRLKEPRRGLCSSWLASLDPGQGPVRVPLWVRPGSLAFPETPDTPVIMVGPGTGVAPFRAAIQERVAQGQTGNFLFFGCRWRDQDFYWEAEWQELEKRDCLTLIPAFSREQEQKVYVQHRLRELGSLVWELLDRQGAYFYLAGNAKSMPADVSEALMSIFQEEGGLCSPDAAAYLARLQQTRRFQTETWA
Protein: Uncharacterized protein C9orf43 (Q8TAL5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLPDESQWDETTCGLAVCQHPQCWATIRRIERGHPRILGSSCKTPLDAEDKLPVLTVVDILDSGFAAHHLPECTFTKAHSLLSQSSKFYSKFHGRPPKGLPDKSLINCTNRLPKFPVLNLNETQLPCPEDVRNMVVLWIPEETEIHVSQHGKKKRKNSAVKSKSFLGLSGNQSAGTRVGTPGMIVPPPTPVQLSEQFSSDFLPLWAQSEALPQDLLKELLPGGKQTMLCPEMKIKLAMMKKNLPLEKNRPDSVISSKMFLSIHRLTLERPALRYPERLKKLHNLKTEGYRKQQQRQQQQQQQQKKVKTPIKKQEAKKKAKSDPGIQSTSHKHPVTTVHDRLYGYRTLPGQNSDMKQQQQMEKGTTSKQDSTERPKMNYYDHADFHHSVKSPELYETEPTNKDISAPVDAVPEAQAARQKKISFNFSEIMASTGWNSELKLLRILQDTDDEDEEDQSSGAE
Protein: Spore germination protein GerPC (A0A6L8PD99)
Organism: Bacillus anthracis
Interaction partners:
Sequence:
MNQDIYTYLHQLQQALQVQQATILNLEDQVRQLQEELNELKNRPSSSIGKVEYKFDQLKVENLNGTLNIGLNPFSTKEQQIEDFQVDTETLKVNPETDTNPDFYQGILQEMHRYLDEEAYNRILHFEKEERTPLDEMYRQMMVDDIKKQMEHRLPYYLSQAQSYEGTSTDPDYLRDIIIQAMKHDIDKAFLSFIQHIPGNFRKE
Protein: Dachshund variant 1 (Q24028)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDSVTSEQSENNNNKAGAINNNINSGIERAAGNMNTTAMLMHHQQQQQAAAAAAAAAAQQQQQQHNGRDGSNSSRGANEDRPNGRSSHTGRGSSCSPASSPSRHPSAVSPVSSLNHSMMQQMQQQQQQQQQQQQQQQHHQLSPPPHGMPSGNGLPTGLPPRMPHGLPPHSLGLLNSLQMMHHASPLELMAAAHHHVPPRSYNSPPPISTSDPSANECKLVEYRGQKVAAFIISNETMLCLPQAFELFLKHLVGGLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQPGVNRCKLLCCKDFDILYRDCTTARCLSIKPPESSRPGRPPKRGPVGLSLPPTHLSQHPQLKKHRLDNGDYAYENGHISDMKSPLLANGYNPPPINHMAFMQMNAHHPGAAALMSPGMPPHGLHARPESQMLKAAAQNAGMSAANMDALARSGIWENCRAAYEDIVKHLERLREERTDERQQAMGVGGAVVDRVGNVMVAEHKPRDLSSRNCSPTRQSPVLNLSKSGGNTDHGGSNCDAGSERSDCHSVAGSPARGGSRSLDEGSRSGVGGGVASHVGGGIIGVEDDEEEEENLSDENQSEVDERCLAKDDEDLSDTERDNLSTGSAAAAAAAAAAAAHQLHQHAASHHHQTVGLSHLGVVPPHQRGSPSSAEAAAAALQHQRALNYSQLAAAAAVANGAAVGGGAVANGPTGGGGALTPNEALLAANDAAALAGGLALGPLGIDAHAAVPASSTETLLRNIQSLLKVAADNARQQERQISYEKAELKMDVLREREVKDSLERQLVDERKLRVLYQKRFRRERKIRIRYQQQLGGGSGAVKGSPNANGSGGGGSGSACSESEACGGGGGDAKCNNNNNNNNNNNNSNSSSHGGDVETMKENDAGSEKSDKSLASNSSCDVTAGHSAGSVSGSISAGLNCPDSPTHFKREPSSDHEGSVERQPRSSAASLAAHDEDNIKRCGSRDRDERPPSGSAASVAAEGSLAAAAAAAAAAAAAAASNGKGPWSYPGIDLMATGAFWQNYSESLAQELEMERKSRAANAERDVKSPLSERPTAYYKNSVLFGSAN
Protein: Signal transducer CD24 (Small cell lung carcinoma cluster 4 antigen) (CD antigen CD24) (P25063)
Organism: Homo sapiens (Human)
Function: May have a pivotal role in cell differentiation of different cell types. Signaling could be triggered by the binding of a lectin-like ligand to the CD24 carbohydrates, and transduced by the release of second messengers derived from the GPI-anchor. Modulates B-cell activation responses. Promotes AG-dependent proliferation of B-cells, and prevents their terminal differentiation into antibody-forming cells. In association with SIGLEC10 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90. Plays a role in the control of autoimmunity (By similarity).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Sialic acid-binding Ig-like lectin 10
- P-selectin
- High mobility group protein B1
- Neural cell adhesion molecule L1
- Epithelial cell adhesion molecule
- E-selectin
- CD44 antigen
- Prominin-1
- Tyrosine-protein phosphatase non-receptor type substrate 1
- Platelet endothelial cell adhesion molecule
Sequence:
MGRAMVARLGLGLLLLALLLPTQIYSSETTTGTSSNSSQSTSNSGLAPNPTNATTKAAGGALQSTASLFVVSLSLLHLYS
Protein: Arginine N-succinyltransferase subunit beta (EC 2.3.1.109) (AOST) (AST) (ARUAII) (P80358)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- N-succinylarginine dihydrolase
- N-succinylglutamate 5-semialdehyde dehydrogenase
- Arginine N-succinyltransferase subunit alpha
- Succinylglutamate desuccinylase
- Succinylornithine transaminase/acetylornithine aminotransferase
- Lysine decarboxylase LdcA
- Biosynthetic arginine decarboxylase
- Arginine--pyruvate transaminase AruH
- Arginine/ornithine transport ATP-binding protein AotP
- HTH-type transcriptional regulator ArgR
Sequence:
MIVRPVTSADLPALIELARSTGTGLTTLPANEQRLQHRVSWAEKAFRGEAERGDADYLFVLEDDAGKVVGISAIAGAVGLREPWYNYRVGLTVSASQELNIHREIPTLFLANDLTGNSELCSLFLHADHRSGLNGKLLSRARFLFIAEFRHLFGDKLIAEMRGMSDEEGRSPFWESLGRHFFKMEFSQADYLTGVGNKAFIAELMPKFPLYTCFLSEEARGVIGRVHPNTEPALAMLKAEGFSYQGYVDIFDAGPAIEAETDKIRAIAESQNLVLAVGTPGDDAEPYLIHNRKREDCRITAAPARAAAGTLVVDPLTAKRLRLSAGASVRAVPLSAQKRG
Protein: Ubiquitin-ribosomal protein eL40 fusion protein (CEP52) [Cleaved into: Ubiquitin; Large ribosomal subunit protein eL40 (60S ribosomal protein L40)] (P18101)
Organism: Drosophila melanogaster (Fruit fly)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40]: Cytoplasm {ECO:0000250}.
Interaction partners:
- GEO07453p1
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS7A
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS10
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLRILAQKYNCDKMICRKCYARLHPRATNCRKKKCGHTNNLRPKKKLK
Protein: MAGE family member A10 (C9J9A2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPRAPKRQRCMPEEDLQSQSETQGLEGAQAPLAVEEDASSSTSTSSSFPSSFPSSSSSSSSSCYPLIPSTPEEVSADDETPNPPQSAQIACSSPSVVASLPLDQSDEGSSSQKEESPSTLQVLPDSESLPRSEIDEKVTDLVQFLLFKYQMKEPITKAEIL
Protein: Elongation factor Tu GTP binding domain containing 2 (A0A8I6GKG9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLDGLRKVNKSYPSLTTKVEESGEHVILGTGELYLDCVMHDLRKMYSEIDIKVADPVVTFCETVVETSSLKCFAETPNKKNKITMIAEPLEKGLAEDIENEVVQITWNRLEQGPHYGFLAWSPDTIPPSLLSRLWCG
Protein: C21orf58 protein (Q0VAL7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARSRLPATSLRKPWKLDRQKLPSPDSGHSLLCGWSPGGKARPAGNTGAWAPAEQFFPASNRTREGGGLWPPLPLQSSPAAPTMLDSSAAEQVTRLTLKLLGQKLEQERQNVEGGPEGLHLEPGNEDRPDDALQTALKRRRDLLQRLRVGPAPSERTWLSSL
Protein: Heat shock protein Hsp (Heat-stress-induced ribosome-binding protein A) (O53673)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Chaperone protein ClpB
- Chaperone protein DnaK
- ATP-dependent Clp protease ATP-binding subunit ClpC1
- Uncharacterized protein Rv2667
- Protein GrpE
Sequence:
MNNLALWSRPVWDVEPWDRWLRDFFGPAATTDWYRPVAGDFTPAAEIVKDGDDAVVRLELPGIDVDKDVNVELDPGQPVSRLVIRGEHRDEHTQDAGDKDGRTLREIRYGSFRRSFRLPAHVTSEAIAASYDAGVLTVRVAGAYKAPAETQAQRIAITK
Protein: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase TPTE2 (EC 3.1.3.67) (Lipid phosphatase TPIP) (TPTE and PTEN homologous inositol lipid phosphatase) (Q6XPS3)
Organism: Homo sapiens (Human)
Function: Acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate.
Subcellular location: [Isoform 3]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11716755}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14659893}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:14659893}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:11716755}.
Interaction partners:
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2
- DNA-dependent metalloprotease SPRTN
Sequence:
MNESPQTNEFKGTTEEAPAKESPHTSEFKGAALVSPISKSMLERLSKFEVEDAENVASYDSKIKKIVHSIVSSFAFGIFGVFLVLLDVTLLLADLIFTDSKLYIPLEYRSISLAIGLFFLMDVLLRVFVEGRQQYFSDLFNILDTAIIVIPLLVDVIYIFFDIKLLRNIPRWTHLVRLLRLIILIRIFHLLHQKRQLEKLMRRLVSENKRRYTRDGFDLDLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLCSERAYDPKHFHNRVSRIMIDDHNVPTLHEMVVFTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTNKTHSNKFQGVETPSQNRYVGYFAQVKHLYNWNLPPRRILFIKRFIIYSIRGDVCDLKVQVVMEKKVVFSSTSLGNCSILHDIETDKILINVYDGPPLYDDVKVQFFSSNLPKYYDNCPFFFWFNTSFIQNNRLCLPRNELDNPHKQKAWKIYPPEFAVEILFGEK
Protein: Nickel/cobalt efflux system (O05804)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362101}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362101}. Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MASSQLDRQRSRSAKMNRALTAAEWWRLGLMFAVIVALHLVGWLTVTLLVEPARLSLGGKAFGIGVGLTAYTLGLRHAFDADHIAAIDNTTRKLMSDGHRPLAVGFFFSLGHSTVVFGLAVMLVTGLKAIVGPVENDSSTLHHYTGLIGTSISGAFLYLIGILNVIVLVGIVRVFAHLRRGDYDEAELEQQLDNRGLLIRFLGRFTKSLTKSWHMYPVGFLFGLGFDTATEIALLVLAGTSAAAGLPWYAILCLPVLFAAGMCLLDTIDGSFMNFAYGWAFSSPVRKIYYNITVTGLSVAVALLIGSVELLGLIANQLGWQGPFWDWLGGLDLNTVGFVVVAMFALTWAIALLVWHYGRVEERWTPAPDRTT
Protein: GH01161p (TNF-receptor-associated factor 6) (Q9W3I9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Serine/threonine-protein kinase pelle
- LD20892p
- RE66324p
- LD40663p
- ubiquitinyl hydrolase 1
- Mitogen-activated protein kinase kinase kinase 7
- FI05319p
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Tumor necrosis factor receptor superfamily member wgn
- FI16976p1
Sequence:
MQRVQADQKPARMHQHAHTHSHAHSLQHAEEKEHNSNEMTTNLSSTGRIAASSSATPSAAAGGGASGAPTPPKSLALNQNHHYAPGSDTSGEQEEELLDSRYECAICIDWLNEPVLTSCGHRFCRSCLTAWMQKNNQCCPMDNKRLSAEHDIFPDNYTRREIEQLKRDCPNSSLGCSVVASPIELHRHLPSCPYRRQQEPQEEKCPFAKIKCDFVGRPETNQLEEHLKADMPHHMQLMLQAFQQTAIATWQPHKPSTSGAAVENGHGQQQLPPPPQYANGVDEQIVQTMYQRIVVLEQRTREQETRLENMQKQLRLARQQAPVDPRYSNGTIVWRIEQLGALVARLRANANNQVYSHECYTSPHGYKFCARLNIQPRKPHVLSLHVHLMQSENDYHLDWPFKGRIKLCMVHPADATLSQHDTIMTKPEILAFHKPREAISTRGFGFLEYANISNIIQLGFCADDRLLIKIEINIV
Protein: Amine oxidase [copper-containing] alpha 3, peroxisomal (AtCuAO2) (AtCuAOalpha3) (Copper amine oxidase 2) (EC 1.4.3.21) (F4IAX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Copper amine oxidase that can use putrescine and spermidine as substrates. Involved in putrescine catabolism in peroxisomes.
Subcellular location: Peroxisome {ECO:0000269|PubMed:23915037}.
Interaction partners:
- Polyamine oxidase 1
- Probable polyamine oxidase 5
- Tyrosine decarboxylase 2
- Probable polyamine oxidase 4
- Phenylacetaldehyde synthase
- Polyamine oxidase 3
- Polyamine oxidase 2
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Precursor of CEP12
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
Sequence:
MAPLHFTILILFSFVIVVSSSSFTPPRHPFDPLTETELKLVRTIINKSYPVGPNHKFTFQYVGLNEPNKSLVLSWYSSPNHTIKPPPRQAFVIARDNGKTREIVLDFSSRAIVSDKIHVGNGYPMLSNDEQEASTELVVKFKPFIDSVAKRGLNVSEIVFTTSTIGWYGETKAEAERVIRLMPFYLDGTVNMYLRPIEGMTIIVNLDEMKVSEFKDRSVVTMPIANGTEYRISKLNPPFGPTLHNAVLLQPDGPGFKVDGHIVRWANWEFHISFDVRAGIVISLASLFDTDVNKYRQVLYKGHLSEMFIPYMDPSDDWYFITYLDCGDFGCGQCAVSLQPYTDCPAGAVFMDGIFAGQDGTPAKIPKVMCIFEKYAGDIMWRHTEAEIPNLEITEVRPDVSLVARIVTTVGNYDYIVDYEFKPSGSIKMGVGLTGVLEVKPVEYIHTSEIKLGEDIHGTIVADNTVGVNHDHFVTFRLHLDIDGTENSFVRNELVTTRSPKSVNTPRKTYWTTKPKTAKTEAEARVKLGLKAEELVVVNPNRKTKHGNEVGYRLLHGSAAGPLLAQDDFPQIRAAFTNYNVWITPYNRSEVWAGGLYADRSQGDDTLAVWSQRNRKIEKEDIVMWYTVGFHHVPSQEDYPTMPTLSGGFELRPTNFFERNPVLKTKPVKVTTARKCTPKND