wanglab/gogpt-training-data huggingface dataset:
Protein: pH-response regulator protein palI/RIM9 (Q59WV0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- pH-response regulator protein palF/RIM8
- pH-response regulator protein palH/RIM21
- Calpain-like protease palB/RIM13
- pH-response regulator protein palA/RIM20
- Dfg16p
- pH-response transcription factor pacC/RIM101
- Srd1p
- Vacuolar-sorting protein SNF7
Sequence:
MFKAFIALLILLIVCWVIQLLPVIAVPFTTPDANIYLSYYNNYKFGVFGICNVERHICSKPSIGYPSTNSTFYAYDNDESFGTGGIVLPSDVRYTISKLLVVHVVAFCFSSLLLIVIFGLIIILFFKYIKTKKDLEGIQLNDSSHEITIHSDEEDNNNNNIDNTNHNNKRASVTINKTIFDLTPFLNLMLVFTFFSVLTTLLAFLADILLFTPNLSYLGWLQLIPIVSMALVTSMLCFIKRSISSRKFFESEYRYANDDMRIMRKTYVDEFWNDNASDDGFYVYTDGFYTRNGDNVQQPTSNTAGSLLSEHHDVSIVEPRTFLDTDDSRRGSSPHEFIELQNLRPV
Protein: Nucleus export protein brr6 (Q9UT30)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mRNA and protein export from nucleus.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Nuclear envelope protein ndc1
- Meiotically up-regulated gene 31 protein
- Nuclear membrane organization protein apq12
Sequence:
MEMYVEDVPMPDIGPDSVLNTPIRPKYEILKSKKKTQNENDPEPMDISMSPDEKNLKKSTVRRKLRKSKPNSSSNQVSSRTRALTKRSNSSNAIIKANNQDSVYVSDWTNVHRDIPIVVSGYLQLMFNACVASIFLYFLFKIVFGIQNDVRNRVEYHKILQEEQAADCQREYLSINCDSPGPAIFEVCQKLKQCKMESSNNVGSTKLAALVFAEIIDAFISHISYKTMVFSLILVFGSLLTSNYAFGLYRARHSQNIHDYAANAIPAMIPSSRFLPSNLSDISNRNLIEAASQEEEI
Protein: Mannose-6-phosphate isomerase 2 (EC 5.3.1.8) (Phosphohexomutase 2) (Phosphomannose isomerase 2) (PMI2) (Protein DARK INDUCIBLE 9) (Q9FZH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Interaction partners:
- Phosphomannomutase
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Hexokinase-2
- Hexokinase-3
- Probable hexokinase-like 2 protein
- Hexokinase-like 1 protein
- Hexokinase-4
- Hexokinase-1
- Probable fructokinase-5
Sequence:
MGADAIQTNGHDQAKLTGGEEIQRLRCFVKNYEWGKLGPESLVARLQEANTGQRVDSEIPYAEFWMGTHESGPSHVEFGSGHGVSDKCMVTLKSWVLDNPNLLGSKVVDKWGCDLPFLFKVLSVTKALSIQAHPNKALAEKLHREDPLLYRDNNHKPEIALAVTPFQALCGFVTLKELKEVITNVPEITELVGSKAADQIFNVHEHDEDERIKSVVRLIFTQLMSASNNETKQVVSRMKNRLLLETKHRELSEKEKLVLELEKQYTGDIGVISAFFFNYVKLNPGEALYLDANEPHAYISGDCVECMAASDNVVRAGLTPKHRDVQTLCSMLTYKLGYPEILKGFPLTPYVTRYLPPFDEFEVDHCDLPRGKSTVFPAVPGPSVYLVIEGKGQLRTGSSKVLVNRGDVLFVPADIEIHVTGESDVMKLYRAGVSSRFFQTL
Protein: Pumilio homolog 1 (A0A0R4IWL6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
- Nanos homolog 1
- Clathrin interactor 1 isoform X1
- SH3 domain-containing 19
- Cytochrome c oxidase copper chaperone
- CCR4-NOT transcription complex subunit 7
Sequence:
MSVACVLKRKAVLWQDSFSPHLRLPPPDRPLPSMPVVLSAAGHTPQPGPSPQAPAPTQGAGRSQDDAMVDYFFQRQHGDQPGYNNCKHRWPTGDNIHADNQVRSMDELNHDFQALALEGRAMGEQLLTGKKFWETDDSGKDGPKGIFLDQWRDSAWGASDHSVSQPIMVQRRPGQGFHGVGEAGSVLSPRSESGGLGVSMVEYVLSSSPAEKMDSCLRKGAYGPRDSEADDPEKRVEQKPKTTFDPERKELKETEPDVLDNPNGLPNQNGLDVDVKDFSRTPGNCPPTGQEVELGGPEMVGGAGPKPAEEFSNVETQNVTLDPMESVSMETLQFEYPGGQLPLDSTAATVGLFDYNSPQQLFQRPNALAVQQLTAAQQQQYALAAAQQPHIGLAPAAFVPNPYIISAAPPGTDPYAAGLAAAATLGPAVMPPQYYGVTPWGVYPANLFQQQAATPSNSANQQSAAQNQQNQQQVMRAGGNQRPLTPSQGQQGQQTEQLVAAAAVNSALAFGQGLAAGVPGYPVLAPAAYYDQTGALVVNTGARGGPVRLMAPASVIISPSAAVAAAAASAGGANAGLGGGASGAFRALSSQQAPGQQGSGALGGSSFYGSGSPSSSSQSSSLFSQGSAQPGNTSLGFNANPTSSLGATLGAALGGFGTAVANSSSSGSRRDSLTGSSDLYKRTASSLTPIGHGAFYNGLSFSSSPGPVGMPLPNQGPSHSLTPPPSLSTHGSSSSLNLGGLTNGSGRFISAAPGAEAKYRSATTGSSLFSPSSQLFPSSRLRYGMSDVMPSGRSRLLEDFRNNRYPNLQLREIAGHVMEFSQDQHGSRFIQLKLERASPAERQLVFNEILQAAYQLMVDVFGNYVIQKFFEFGSLDQKLALAERIRGHVLSLALQMYGCRVIQKALEFIPSDQQVINEMVRELDGHVLKCVKDQNGNHVVQKCIECVQPHALQFIIDAFKGQVFALSTHPYGCRVIQRILEHCLPEQTLSILEEIHQHTEQLVQDQYGNYVIQHVLEHGRAEDKSKIVSEIRGNVLGLSQHKFASNVVEKCVTHSLRAERAMLIDEVCSMADGPHSALYTMMKDQYANYVVQKMIDVAEPTQRKIVMHKIRPHIATLRKYTYGKHILAKLEKYYMKNGVDLGPLCAPPNGIM
Protein: NAD(P) transhydrogenase, mitochondrial (EC 7.1.1.1) (Nicotinamide nucleotide transhydrogenase) (W5PFI3)
Organism: Ovis aries (Sheep)
Function: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity). May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NAD kinase
- Nicotinamide-nucleotide adenylyltransferase.
- NAD-dependent protein deacetylase
- Glutamine-dependent NAD
- protein acetyllysine N-acetyltransferase
- NAD-dependent protein deacetylase sirtuin-7
- NAD-dependent protein deacylase sirtuin-5
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
- Nudix hydrolase 12.
Sequence:
MANLLKTVVTGCSCPFLSNLGSCKVLPGKKNFLRAFHTHRILWCKAPVKPGIPYKQLTVGVPKEIFQNEKRVALSPAGVQALVKQGFNVVVESGAGEASKFSDDHYRAAGAQIQGAKEVLASDLVVKVRAPMLNPTLGIHEADLLKTSGTLISFIYPAQNPDLLNKLSKRNTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFTGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEFIEAEMKLFAQQCKEVDILISTALIPGKKAPILFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYVHKGITHIGYTDLPSRMATQASTLYSNNITKLLKAISPDKDNFYFEVKDDFDFGTMGHVIRGTVVMKDGQVIFPAPTPKNIPQGAPVKQKTVAELEAEKAATITPFRKTMTSASVYTAGLTGILGLGIAAPNLAFSQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAISGLTAVGGLVLMGGHLYPSTTSQGLAALATFISSVNIAGGFLVTQRMLDMFKRPTDPPEYNYLYLLPAGTFVGGYLASLYSGYNIEQIMYLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLAATLGGLKPCPELLAQMSGAMALGGTIGLTIAKRIQISDLPQLVAAFHSLVGLAAVLTCIAEYIIEYPHFATDAAANLTKIVAYLGTYIGGVTFSGSLVAYGKLQGILKSAPLLLPGRHLLNAGLLAASVGGIIPFMMDPSFTTGITCLGSVSALSAVMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGGKPMEISGTHTEINLDNAIDMIREANSIIITPGYGLCAAKAQYPIADLVKMLSEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQEDPNSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDALQAKVRESYQK
Protein: Interferon gamma (IFN-gamma) (Immune interferon) (P01579)
Organism: Homo sapiens (Human)
Function: Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation. Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription. Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits. In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading. Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference. Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL. Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Interferon gamma receptor 1
- Interferon gamma receptor 2
- Tyrosine-protein kinase JAK2
- Interleukin-1 beta
- Interleukin-10
- Tyrosine-protein kinase JAK1
- T-cell surface glycoprotein CD4
- Tumor necrosis factor
- T-cell surface glycoprotein CD8 alpha chain
- Interleukin-2
Sequence:
MKYTSYILAFQLCIVLGSLGCYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ
Protein: Probable lysophospholipase 2 (EC 3.1.1.5) (Phospholipase B) (Q9UTH5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the release of fatty acids from lysophospholipids.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase gde1
- Lysophospholipid acyltransferase
- Triacylglycerol lipase ptl3
Sequence:
MYFQSFYFLALLLATAVYGQVASPELHSLSRRNWKKPPPFPSTNASYAPVIRSCDSSEIMVNSLPRGELPDLENDFIEKRLSNANEALTTFLQSKNTTADLDLSSIVGDNGPRLGIAVSGGGWRSMLFGGGALAALDSRSNETTLGGLLQSAHYITGADGGSWLLSSLAVNEFRTIQNISKSIWYTRLGIFFIEETHFGDLKNYYTNVVDEVNQKAAAGFNVSLTDYWGRAIARHFVGQLRGGPNLTYSSVQNASWFQTAEYPYPLIVTQGLTGGLPDGSNGTATNSSIYEISPYYLTSFDNNVRSYTPTQYLGTNYSNGTAVDGKCVTQFDNVGFLVGTSSTRYNEALIDVSLRQSRMSRRLGFTLRHMRINGSSVSFYPNPYTDATDIAGNATAVSEDIVDTPYLDLFDGGYDGQNIPIWPLLQPERKLDVVFAFDSSGDTSNFWPNGSSLVATYERVTQRASDAVYDVEDFVHVPTPETFVNLGLNANPTFFGCDGRNTTRGDVPVDHNTPPLVVYMPNTPWTMKSNLVDHRYRIANSEIQALIQNGFVATTQDNSTDFASCLACAVVQRSLERRNQSTSAACQQCFSQYCWNGTVDNTPVDDDSKNPTYNPAVKTSSASGVHANILLSFFVLLATLLVTA
Protein: Myc-associated zinc finger protein (MAZI) (Pur-1) (Purine-binding transcription factor) (P56671)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator (By similarity). Acts as a transcriptional activator that binds to purine-rich GAGA sites found in the promoter of many genes including insulin I and II and islet amyloid polypeptide.
Subcellular location: Nucleus {ECO:0000269|PubMed:26089202}.
Interaction partners:
Sequence:
MFPVFPCTLLAPPFPVLGLDSRGVGGLMNSFPPPQGHAQNPLQVGAELQSRFFASQGCAQSPFQAAPAPPPTPQAPAAEPLQVDLLPVLAAAQESAAAAAAAAAAAAAVVTAPPAPAAASTVDTAALKQPPAPPPPPPAVSAPAAEAAPPAAAATIAAAAATAVVAPTSTVAVAPVASVLEKKTKSKGPYICALCAKEFKNGYNLRRHEAIHTGAKAGRVPSGAMKMPTMVPLSLLSVPQLSGASGGGGEAGAGGGTTAVAAGGVVTTTASGKRIRKNHACEMCGKAFRDVYHLNRHKLSHSDEKPYQCPVCQQRFKRKDRMSYHVRSHDGAVHKPYNCSHCGKSFSRPDHLNSHVRQVHSTERPFKCEKCEAAFATKDRLRAHTVRHEEKVPCHVCGKMLSSAYISDHMKVHSQGPHHVCELCNKGTGEVCPMAAAAAAAAAAAAAVVAAPPTAVGSLSGAEGVPVSSQPLPSQPW
Protein: Sigma non-opioid intracellular receptor 1 (Sigma 1-type opioid receptor) (Sigma1-receptor) (Sigma1R) (Q7ZWG9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May function in lipid transport from the endoplasmic reticulum and be involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. May regulate calcium efflux at the endoplasmic reticulum (By similarity).
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
Interaction partners:
- Phosphoethanolamine methyltransferase.
- Lanosterol 14-alpha demethylase
- Ergosterol biosynthesis 28 homolog
- Squalene epoxidase b.
- Squalene epoxidase a.
- Sterol-C5-desaturase
- 7-dehydrocholesterol reductase
- Transmembrane 7 superfamily member 2.
- Lamin B receptor.
- VAMP-associated protein B and C
Sequence:
MSLIRTILKLVVVVGFLSLTVQFIRHWMANKQYVFTKEEVAKLAKQYAGQDHEQAFSKVVVELRRRYPGHILPDEDLQWVFVNAGGWMGSMCLLHASLTEYVLLFGTAVDTGGHSGRYWAEISDTIISGTFRQWKEGTTKSETYYPGDTIVHSAGEATSVQWSSGTWMVEYGRGFIPSTLGFALADTMFSTQDFLTLFYTARVYVKGMILEASTFLTESGVL
Protein: Coiled-coil domain-containing protein 78 (D3Z5T1)
Organism: Mus musculus (Mouse)
Function: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}. Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in reticular pattern within the sarcoplasm (By similarity). {ECO:0000250}.
Interaction partners:
- Basal body-orientation factor 1
Sequence:
MDQRPELLSSMEYVASPDPKPGVPLRVAENVAPGAEDWLPSASGHLAWATSLETEHQTHLELSEEQRLQISKELVDLQIATHHLREQHEAEVFELRREILRLESRVLELELHGNGACQGHKVQPMANLGQHQVPPLEPPGGQQKLQEELKWLLEHHRARQQALETQVGVLSQQLQGAREEARTTGQQLASQAMVLASCKGQLRQAEAENTQLQLQLKKMNEEYAVRLQHYARETVENASSTNQAALQAFLESTLQDIRAAHRTREQQLAQAARTYRKRLADLNQRQELLLTTCRATFATAINLEPLPMHWATELSHPRENEYGRHRTLLLYPEKGSGETSKENKSQPLALDTASWAQIQQRLQDFSQDTQAELERERAQLMVRATMAEQQLSELQEYVDQHLGRYKQEILKLRKLVNIGDPQGVEAVSSPGSGGARL
Protein: Cytochrome b-c1 complex subunit 8-2, mitochondrial (Complex III subunit 8-2) (Complex III subunit VIII) (Ubiquinol-cytochrome c oxidoreductase subunit 8-2) (Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C) (Q9FLB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08525}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08525}.
Interaction partners:
- Cytochrome b-c1 complex subunit 7-1, mitochondrial
- Cytochrome c1 2, heme protein, mitochondrial
- Probable mitochondrial-processing peptidase subunit beta, mitochondrial
- Uncharacterized protein At2g27730
- Cytochrome b-c1 complex subunit 7-2, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-2, mitochondrial
- Cytochrome c1 1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
- Probable mitochondrial-processing peptidase subunit alpha-2, chloroplastic/mitochondrial
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
Sequence:
MGKQPVKLKAVVYALSPFQQKIMTGLWKDLPEKIHHKVSENWISTILLVAPVVGTYSYAQYFKEQEKLEHRF
Protein: ATP-sensitive inward rectifier potassium channel 11 (IKATP) (Inward rectifier K(+) channel Kir6.2) (Potassium channel, inwardly rectifying subfamily J member 11) (Q14654)
Organism: Homo sapiens (Human)
Function: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium (By similarity). Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- ATP-binding cassette sub-family C member 8
- ATP-binding cassette sub-family C member 9
- ATP-sensitive inward rectifier potassium channel 8
- Diablo IAP-binding mitochondrial protein
- Gamma-aminobutyric acid type B receptor subunit 1
- Gamma-aminobutyric acid type B receptor subunit 2
- Hexokinase-4
- E3 ubiquitin-protein ligase XIAP
- Insulin
- Threonylcarbamoyladenosine tRNA methylthiotransferase
Sequence:
MLSRKGIIPEEYVLTRLAEDPAKPRYRARQRRARFVSKKGNCNVAHKNIREQGRFLQDVFTTLVDLKWPHTLLIFTMSFLCSWLLFAMAWWLIAFAHGDLAPSEGTAEPCVTSIHSFSSAFLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAETLIFSKHAVIALRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPMENGVGGNSIFLVAPLIIYHVIDANSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQARTSYLADEILWGQRFVPIVAEEDGRYSVDYSKFGNTVKVPTPLCTARQLDEDHSLLEALTLASARGPLRKRSVPMAKAKPKFSISPDSLS
Protein: Ureide permease 1 (AtUPS1) (Q9ZPR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proton-coupled transporter that transports a wide spectrum of oxo derivatives of heterocyclic nitrogen compounds, including allantoin, uric acid and xanthine, but not adenine. Mediates high affinity transport of uracil and 5-fluorouracil (a toxic uracil analog). Mediates transport of free pyrimidines and may function during early seedling development in salvage pathways, by the utilization of pyrimidines from seed storage tissue.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dihydropyrimidine dehydrogenase
- Allantoate deiminase
- Allantoinase
- Uracil phosphoribosyltransferase, chloroplastic
- AT4g32140/F10N7_50
- Ureidoglycolate hydrolase
- Equilibrative nucleotide transporter 1
Sequence:
MYMIESKGGAIACMLLALLFLGTWPAIMTLTERRGRLPQHTYLDYTLTNLLAAVIIALTLGEIGPSRPNFFTQLSQDNWQSVMFAMAGGIVLSLGNLATQYAWAYVGLSVTEVITASITVVIGTTLNYFLDDRINRAEVLFPGVACFLIAVCFGSAVHKSNAADNKTKLQNFKSLETTSSFEMETISASNGLTKGKAKEGTAAFLIELEKQRAIKVFGKSTIIGLVITFFAGICFSLFSPAFNLATNDQWHTLKHGVPKLNVYTAFFYFSISAFVVALILNIRFLYWPILGLPRSSFKAYLNDWNGRGWSFLAGFLCGFGNGLQFMGGQAAGYAAADAVQALPLVSTFWGILLFGEYRRSSRKTYTLLISMLLMFIVAVAVLMASSGHRK
Protein: Protein RUFY3 (Rap2-interacting protein x) (RIPx) (Single axon-regulated protein 1) (Singar1) (Q9D394)
Organism: Mus musculus (Mouse)
Function: Plays a role in the generation of neuronal polarity formation and axon growth. Implicated in the formation of a single axon by developing neurons. May inhibit the formation of additional axons by inhibition of PI3K in minor neuronal processes (By similarity). Plays a role in the formation of F-actin-enriched protrusive structures at the cell periphery (By similarity). Plays a role in cytoskeletal organization by regulating the subcellular localization of FSCN1 and DBN1 at axonal growth cones. Promotes gastric cancer cell migration and invasion in a PAK1-dependent manner (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7L099}. Endomembrane system {ECO:0000250|UniProtKB:Q7L099}. Cell projection, invadopodium {ECO:0000250|UniProtKB:Q7L099}. Cell projection, growth cone {ECO:0000269|PubMed:24720729}. Perikaryon {ECO:0000269|PubMed:24720729}. Cell projection {ECO:0000269|PubMed:24720729}. Cell projection, filopodium {ECO:0000269|PubMed:24720729}. Cell projection, lamellipodium {ECO:0000269|PubMed:24720729}. Lysosome {ECO:0000250|UniProtKB:Q7L099}. Note=Colocalizes with PAK1, F-actin, myosins and integrins in invadopodia at the cell periphery (By similarity). Colocalizes with Ras-related Rab-5 proteins in cytoplasmic vesicles (By similarity). Accumulates in axon growth cones in a F-actin-dependent manner (PubMed:24720729). Colocalizes with FSCN1 and F-actin at filipodia and lamellipodia of axonal growth cones (PubMed:24720729). Colocalizes with DBN1 and F-actin at transitional domain of the axonal growth cone (PubMed:24720729). Recruitment to endolysosomes partially depends upon the presence of ARL8 (By similarity). {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q7L099, ECO:0000269|PubMed:24720729}.
Interaction partners:
Sequence:
MSALTPPTDMPTPTTDKITQAAMETIYLCKFRVSMDGEWLCLRELDDISLTPDPEPTHEDPNYLMANERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFCMKGEDLDSQVGVIDFSMYLKDGNSSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKLIPKHH
Protein: Neuropeptide-like protein 31 [Cleaved into: QWGYGGY-amide; GYGGYGGY-amide; GYGGY-amide; GMYGGY-amide; PYGGYGW-amide] (O44662)
Organism: Caenorhabditis elegans
Function: Antimicrobial peptides that have antifungal activity against D.coniospora. Has weak antibacterial activity against Gram-positive bacteria M.luteus and Gram-negative E.coli.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Neuropeptide-Like Protein
- CaeNaCin
- CaeNaCin
- Neuropeptide-like protein 33
- CaeNaCin
- CaeNaCin
- CaeNaCin
Sequence:
MISTSSILVLVVLLACFMAANAQWGYGGYGRGYGGYGGYGRGYGGYGGYGRGYGGYGRGMYGGYGRPYGGYGWGK
Protein: Pyrokinin 2 receptor 1 (Q9VFW5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Protein hugin
Sequence:
MLQGVAITIANDSNDDGINQSFMAHVSPSPNQSPSIGVGIGIASSTMANPSESPEMLLLKNDKFLTHVAHLLNITTENLSNLLGSTNGTNASTMAADSPVDESLTLRTALTVCYALIFVAGVLGNLITCIVISRNNFMHTATNFYLFNLAVSDLILLVSGIPQELYNLWYPDMYPFTDAMCIMGSVLSEMAANATVLTITAFTVERYIAICHPFRQHTMSKLSRAIKFIFAIWLAAFLLALPQAMQFSVVYQNEGYSCTMENDFYAHVFAVSGFIFFGGPMTAICVLYVLIGVKLKRSRLLQSLPRRTFDANRGLNAQGRVIRMLVAVAVAFFLCWAPFHAQRLMAVYGLNLINIGISRDAFNDYFRILDYTSGVLYFLSTCINPLLYNIMSHKFREAFKITLTRQFGLARNHHHQQSQHHQHNYSALLRQNGSMRLQPASCSVNNNALEPYGSYRVVQFRCRDANHQLSLQDSIRTTTTTTTINSNSMAAGNGVGGGAGGGGGGRRLRKQELYGPGPGTAVPHRMLQAQVSQLSSLGDANSLLEAEVVDRHYASGRAKRALLATKSGALLVTPPQSGDPSEVSQPATRLKLTRVISRRDEVANTSTPPFCGSHSLPDPETCQSASVAGRSSRKFPWRKRRQKTEDPSSEGLTYGSPKSQ
Protein: Actin-like protein ARP6 (Q12509)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Vacuolar protein sorting-associated protein 72
- Helicase SWR1
- RuvB-like protein 2
- Vacuolar protein sorting-associated protein 71
- RuvB-like protein 1
- SWR1-complex protein 5
- Protein AF-9 homolog
- SWR1-complex protein 4
- SWR1-complex protein 3
- SWR1-complex protein 7
Sequence:
METPPIVIDNGSYEIKFGPSTNKKPFRALNALAKDKFGTSYLSNHIKNIKDISSITFRRPHELGQLTLWELESCIWDYCLFNPSEFDGFDLKEGKGHHLVASESCMTLPELSKHADQVIFEEYEFDSLFKSPVAVFVPFTKSYKGEMRTISGKDEDIDIVRGNSDSTNSTSSESKNAQDSGSDYHDFQLVIDSGFNCTWIIPVLKGIPYYKAVKKLDIGGRFLTGLLKETLSFRHYNMMDETILVNNIKEQCLFVSPVSYFDSFKTKDKHALEYVLPDFQTSFLGYVRNPRKENVPLPEDAQIITLTDELFTIPETFFHPEISQITKPGIVEAILESLSMLPEIVRPLMVGNIVCTGGNFNLPNFAQRLAAELQRQLPTDWTCHVSVPEGDCALFGWEVMSQFAKTDSYRKARVTREEYYEHGPDWCTKHRFGYQNWI