wanglab/gogpt-training-data huggingface dataset:
Protein: Multidrug export protein AcrE (Acriflavine resistance protein E) (Protein EnvC) (P24180)
Organism: Escherichia coli (strain K12)
Function: Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:11274125}; Lipid-anchor {ECO:0000305|PubMed:11274125}.
Interaction partners:
- Multidrug export protein AcrF
- Multidrug efflux pump subunit AcrB
- Outer membrane protein TolC
- Probable aminoglycoside efflux pump
- Multidrug resistance protein MdtF
- Cation efflux system protein CusC
- Multidrug resistance protein MdtC
- Multidrug resistance protein MdtB
- Multidrug resistance outer membrane protein MdtP
- Macrolide export ATP-binding/permease protein MacB
Sequence:
MTKHARFFLLPSFILISAALIAGCNDKGEEKAHVGEPQVTVHIVKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLHKENATSNVELVMENGQTYPLKGTLQFSDVTVDESTGSITLRAVFPNPQHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGDATVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVSGLQKARPGEQVKATTDTPADTASK
Protein: Phosphorylase superfamily protein (Q94K59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- ATP-dependent protease La
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- At5g01015
- Fanconi anemia group E protein FANCE protein
- Fanconi anemia group F protein
- ARM repeat superfamily protein
- Small ribosomal subunit protein mL103
- RING-type E3 ubiquitin transferase
- Pentatricopeptide repeat-containing protein At2g18520
- Fanconi anemia group I-like protein
Sequence:
MDHTLSLLPFLFIIIISSFHVLPVSPTPSHKLKSATTIRKLNRGGPYIGLVTVIATEENAFLRSVDFRPDPTHPFLDLSGRRFRIGKIHGKKVVYVRCGRGMVNGAAATQQMIDVFNVKGIVHFGIAGNMNNSMSIGDVSIPKQITNAGLWDWLNPDKVKGVEDIAYLDVGNYNVPKGDGDNELGSIGYNYEQLYSVTGHINAPQNVFWINTTQEWLHLAADLEKMELSQCVNASLCLPKKPKLVVGLKAATAYIFVDNAAYRNFLYDTFGVSSSDMESSAVAMTCASNGYPIIVIRGLSDLAGEGGDNTVHKFGSLAATNTAKAVLEFIRKLPPY
Protein: Cell division protein FtsA (P0ABH0)
Organism: Escherichia coli (strain K12)
Function: Essential cell division protein that assists in the assembly of the Z ring. May serve as the principal membrane anchor for the Z ring. Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. Binds ATP.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:2203741}; Peripheral membrane protein {ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:2203741}; Cytoplasmic side {ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:2203741}. Note=Localizes to the Z ring in an FtsZ-dependent manner (PubMed:8917533, PubMed:8955398, PubMed:9495771). Targeted to the membrane through a conserved C-terminal amphipathic helix (PubMed:15752196). {ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:8917533, ECO:0000269|PubMed:8955398, ECO:0000269|PubMed:9495771}.
Interaction partners:
- Cell division protein FtsZ
- Peptidoglycan D,D-transpeptidase FtsI
- Cell division protein ZipA
- Cell division protein FtsN
- Cell division protein FtsQ
- Probable peptidoglycan glycosyltransferase FtsW
- Cell division protein FtsX
- DNA translocase FtsK
- Cell division protein FtsL
- Cell division ATP-binding protein FtsE
Sequence:
MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEKLRQQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLNGEAEVEKRVTASVGSWIKRLNSWLRKEF
Protein: Protein gurken (P42287)
Organism: Drosophila melanogaster (Fruit fly)
Function: Critical for defining the anterior-posterior and dorsal-ventral axes of the egg. May signal directly to dorsal follicle cells through the receptor torpedo (top). During oogenesis this signaling pathway instructs follicle cells to follow a dorsal pathway of development rather than the default ventral pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16396907}; Single-pass type I membrane protein {ECO:0000269|PubMed:16396907}. Note=Associates with the membranous cortex of yolk granules. Transiently inserted into the cell membrane, and then reinternalized during yolk uptake. cni is required for its transport to the oocyte cell membrane.
Interaction partners:
- Epidermal growth factor receptor
- RNA-binding protein squid
- Protein rhomboid
- Maternal effect protein oskar
- Heterogeneous nuclear ribonucleoprotein 27C
- DNA-binding protein K10
- Homeotic protein bicoid
- FI20148p1
- Egalitarian, isoform B
- Protein bicaudal D
Sequence:
MMQIPFTRIFKVIFVLSTIVAVTDCCSSRILLLREHTLKIVQHQHSHMHEHAHELQQQIQETAVELLNRLELQRKQLEASAQEEADQLHPDTDPNPDSGGQLPNADDSIAADPEQDGIILGSSTDTWLASESSTPITDSETVTTPETVTHTGEPPPDPSSSSTPDSTTPSPNDKETEIQMLPCSEAYNTSFCLNGGHCFQHPMVNNTVFHSCLCVNDYDGERCAYKSWNGDYIYSPPTAQRKVRMAHIVFSFPVLLMLSSLYVLFAAVFMLRNVPDYRRKQQQLHLHKQRFFVRC
Protein: Ferredoxin (P50727)
Organism: Bacillus subtilis (strain 168)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. This ferredoxin may act as a phosphodonor to cytochrome P450 BioI.
Interaction partners:
- Ferredoxin--NADP reductase 2
- Intracellular iron chaperone frataxin
- Zinc-dependent sulfurtransferase SufU
- Na
- Ferredoxin--NADP reductase 1
- Na
Sequence:
MAKYTIVDKDTCIACGACGAAAPDIYDYDDEGIAFVTLDENKGVVEVPEVLEEDMIDAFEGCPTDSIKVADEPFEGDPLKFE
Protein: Protein lin-7 homolog B (Lin-7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2) (O88951)
Organism: Mus musculus (Mouse)
Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules. This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction {ECO:0000269|PubMed:15494546}. Postsynaptic density membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction, tight junction {ECO:0000269|PubMed:15494546}. Note=Mainly basolateral in renal epithelial cells.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Guanine nucleotide-binding protein G
- Rhotekin
- Liprin-alpha-2
- Amyloid-beta A4 precursor protein-binding family A member 1
Sequence:
MAALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRVLQSRFCSAIREVYEQLYDTLDITGSAEVRAHATAKATVAAFTASEGHAHPRVVELPKTDEGLGFNIMGGKEQNSPIYISRVIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVRYTPRVLEEMEARFEKMRSARRRQQHHSYTSLESRG
Protein: Fumarylacetoacetase-like C-terminal domain-containing protein (G8BL05)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- FAD-binding domain-containing protein
- 3-isopropylmalate dehydratase
- Cupin type-2 domain-containing protein
- Malate synthase
Sequence:
MTTAWKRLIRFVAHDDKIYRGEPLVSDAEYDVGKLALQGKTIKAKVIEGGNIFGDAVVTEKVLEVKKLLGPLTEEEVPIIKCVGLNYMKHIQEGGRTPPPYPSIFYKPRFAVADFGEPIPIPKIAQENQCDYEGELCVVIGKTGKDIKEEDALSYVAGYVSGNDVSARTWQRDPKHAGGVPQWCFSKSFDKYAPLGPQLVSSQVISDPATLHLTTRVNGEVRQDTDTDDLLFNVPKIIAFISQSTTLEQGTVIMTGTPSGVAMGMKVPKYLKNGDEVEVEITQIGTLSNKMDFV
Protein: Frizzled-7-A (Fz-7-A) (Xfz7-A) (Q9PUK8)
Organism: Xenopus laevis (African clawed frog)
Function: Receptor for Wnt proteins. Acts in both canonical and non-canonical Wnt pathways. Although different papers report differing Wnt preferences, wnt5a, wnt8b and wnt11 have been proposed as synergists. In the canonical Wnt pathway, acts via beta-catenin to promote the expression of the dorsal genes siamois, twin and nodal3 and to establish the dorsal axis of the embryo and induce dorsal mesoderm formation. In a non-canonical Wnt/planar cell polarity (PCP) pathway, acts with sdc4 and dvl2/dsh to regulate convergent extension cell movements during gastrulation. Triggers phosphorylation of dvl2/dsh and its translocation to the plasma membrane. In a third branch of Wnt signaling, acts in a non-canonical pathway via trimeric G proteins, and independently of dvl2/dsh, to recruit protein kinase C (PKC) to the membrane and thus activate PKC. PKC signaling controls cell sorting and tissue separation during gastrulation.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:O75084}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75084}. Note=Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in recycling endosomes in other conditions. {ECO:0000250|UniProtKB:O75084}.
Interaction partners:
Sequence:
MSSTVSLLFCCLFLQLCPSAQQYHGEKGISVPDHGFCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLEQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDNSPSGPTARPSPYLPDSITFQPHPHRDFTCPRQLKVPPYLAYRFLGEKDCGAPCEPGKANGLMYFKEEEVRFARLWVGIWAILCCISTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAYTAGFLLEERAVCVERFSEDSYRTVAQGTKKEGCTILFMILYFFGMASSIWWVILSLTWFLSAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDVLSGVCYVGINSVDSLRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVMYTVPATIVLACYFYEQAFRDTWEKTWLVQTCKGYAVPCPNYNFAPMSPDFTVFMIKYLMTMIVGITSSFWIWSGKTLQSWRRFYHRLSNGSKGETAV
Protein: Aldo-keto reductase family 1 member B10 (A0A8I6ADG6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MATFVELSTKAKMPIVGLGTWKSTPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDDPSLLQDPKIKEIAAKHKKTTAQDALELLSFQVFDFQLSDQEMATILSFNRNWRACLLPETVNMEEFPYDAEY
Protein: Mitochondrial RNA binding complex 1 subunit (Q57ZF2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYHRGYGGHYRGGRGGGRGHSHWHNNAPMERGGHMPSNNEGAAISSGSTGFSPLMDFFHSVEGRNYGELRSLTNETYQISENVRCTFLSIQSDPFAPGSQVRLVCPCTFSLEKVLQTTDLAAANPCRRVAAEDFILRSFHAGYRNGIPRRTSGAVQVLRPSQHVLERSTVGLVKAHQQKSGMQAEIEIFARVKLPGHGRRIDGHGAIDIFYNELVPLLEQCVVGLNEEDLHQHVICVHDQEVLRSNLLGAGYVAFVANGAILPRDAGNSDKPLRDNAVPFQSPKSLECSFTLPHSGKTITGMGLPPGLTLIAGGGFHGKSTLLRALEVGIYNHVPDDGRTYVVVDPTAVKIRAEDRRSVHGVDISPFINNLPFGKTTNFFVTADASGSTSQAANIMEALELGSQLLLLDEDTCATNLMYRDALMQMLVPRAQEPITPFVERVADLSQNHGVSSIMVIGGSGQYFPQARVVLVMNAYQISDCTKEAKEIASNSSLPALNPPGDTASVFIPDVNRCFDPDGSFTTVRRRRGREGTKVSGIGTESIRFSEETIDLSMVEQIVEEGQVNAIAQCLALLYDGEPRIVPEMTTKGGALTQLPSPGGVCEIQRGKFNSNFSSMIAGCCSHQHDKRLELRTPSCYLPRGFTSATRHIEIGAALNRLRTLRTVTAKR
Protein: Kelch-like protein 6 (Q6V595)
Organism: Mus musculus (Mouse)
Function: Involved in B-lymphocyte antigen receptor signaling and germinal center formation.
Interaction partners:
Sequence:
MAGQRGACTMSDVVERSLEGPLALTTDKSSQKRGDLVEILTGEKVKFDDTRLSLILQNGLETLREENALTDVILCVDVQEFSCHRVVLAAASNYFRAMFCNDLKEKYEKRIIIKGVDAETMHTLLVYTYTSKALITKQNVQRVLEAANLFQFLQLVDACASFLTEALNPENCIGILRLADTHSLDSLKMQVQSYIIQNFVQILNSEEFLELPVDTLYHILRSDDLCVTEEAQVFETVMSWVRHKQSERLCLLPCVLENVRLPLLDPWYFVEMVEADPLIRQCPEVFPLLQEARMYHLSGNEIISERTKPRMHEFQSEVFMIIGGCTKDERFVAEVTCLDPLRRSRLEVAKLPLTEHELESENKKWVEFACVTLKNEVYISGGKETQHDVWKYNSSINKWIQIEYLNIGRWRHKMVVLGGKVYVLGGFDGLQRINNVETYDPFHNCWSEAAPLHVHVSSFAATSHKKKLYVIGGGPNGKLATDKTQCYDPSTNKWVLKSAMPVEAKCINAVSFQDHIYVVGGAMRALYAYSPLEDSWCLVTQLSHERASCGIAPCNNKLYITGGRDEKNEVIATVLCWDPEAQKLTEECVLPRGVSHHGSVTIRKSYTHIRRVVPGAVSV
Protein: MFS-type transporter SLC18B1 (Solute carrier family 18 member B1) (Vesicular polyamine transporter) (VPAT) (D4A9K4)
Organism: Rattus norvegicus (Rat)
Function: Proton-coupled polyamine antiporter involved in the translocation of polyamines from cytosol into secretory vesicles prior to their release via exocytosis. Uses the electrochemical proton gradient generated by a V-type proton-pumping ATPase to couple the efflux of protons with the uptake of a polyamine molecule (By similarity). Facilitates vesicular storage of spermine and spermidine in astrocytes with an impact on glutamatergic neuronal transmission and memory formation (By similarity). Upon antigen stimulation, regulates polyamine accumulation and release in mast cell secretory granules, which in turn potentiates mast cell degranulation and histamine secretion (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:25355561}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:25355561}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with VAMP3 and VAMP8 in mast cell secretory granules, which are distinct from histamine- and serotonin-containing granules (By similarity). Partly colocalizes with SYP in synaptic vesicles in hippocampal neurons. Localizes in VAMP2-containing secretory vesicles in astrocytes (PubMed:25355561). {ECO:0000250|UniProtKB:D3Z5L6, ECO:0000269|PubMed:25355561}.
Interaction partners:
Sequence:
MDTAGPPAPAGTEGDGPGGSTGETSRRLSKEQIFVLVSAASMNLGCMMTYSILGPFFPKEAEKKGASNTTIGMIFGCYALFELLASLVFGKYLVHIGAKFMFIAGMFVSGGVTILFGVLDQLPEGPIFIAMCFLVRIVDAIGFGAAITASSSILAKAFPNNVATVMGSLEVFSGLGLVAGPPLGGLLYQSFGYEVPFIFLGCIVLLMIPLNLCILPSYESDAGKQSFWKLVTLPKIGLIAFVIISLSSCFGFLDPTLSLFVMKKFSLSTGYVGLVFLGLSLSYAISSPLFGLLSDKMPNLRKWFLVFGNLITAGCYMLLGPIPLLHIKSQLWLLVLVLVINGVSAGMSIIPTFPEMLSCAYANGFEDGISTLGLVSGLFGAMWSVGAFMGPILGGFLCEKIGFEWAAAIQGLWTLLSGVAMALFYLWEDSTMRRSKAQNILGTEEEQAALLPNDT
Protein: Beta-mannosidase (EC 3.2.1.25) (Lysosomal beta A mannosidase) (Mannanase) (Mannase) (O00462)
Organism: Homo sapiens (Human)
Function: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides.
Subcellular location: Lysosome {ECO:0000305}.
Interaction partners:
- Lysosomal alpha-mannosidase
- N-sulphoglucosamine sulphohydrolase
- Alpha-mannosidase 2C1
- Fatty acid-binding protein, intestinal
- Alpha-galactosidase A
Sequence:
MRLHLLLLLALCGAGTTAAELSYSLRGNWSICNGNGSLELPGAVPGCVHSALFQQGLIQDSYYRFNDLNYRWVSLDNWTYSKEFKIPFEISKWQKVNLILEGVDTVSKILFNEVTIGETDNMFNRYSFDITNVVRDVNSIELRFQSAVLYAAQQSKAHTRYQVPPDCPPLVQKGECHVNFVRKEQCSFSWDWGPSFPTQGIWKDVRIEAYNICHLNYFTFSPIYDKSAQEWNLEIESTFDVVSSKPVGGQVIVAIPKLQTQQTYSIELQPGKRIVELFVNISKNITVETWWPHGHGNQTGYNMTVLFELDGGLNIEKSAKVYFRTVELIEEPIKGSPGLSFYFKINGFPIFLKGSNWIPADSFQDRVTSELLRLLLQSVVDANMNTLRVWGGGIYEQDEFYELCDELGIMVWQDFMFACALYPTDQGFLDSVTAEVAYQIKRLKSHPSIIIWSGNNENEEALMMNWYHISFTDRPIYIKDYVTLYVKNIRELVLAGDKSRPFITSSPTNGAETVAEAWVSQNPNSNYFGDVHFYDYISDCWNWKVFPKARFASEYGYQSWPSFSTLEKVSSTEDWSFNSKFSLHRQHHEGGNKQMLYQAGLHFKLPQSTDPLRTFKDTIYLTQVMQAQCVKTETEFYRRSRSEIVDQQGHTMGALYWQLNDIWQAPSWASLEYGGKWKMLHYFAQNFFAPLLPVGFENENTFYIYGVSDLHSDYSMTLSVRVHTWSSLEPVCSRVTERFVMKGGEAVCLYEEPVSELLRRCGNCTRESCVVSFYLSADHELLSPTNYHFLSSPKEAVGLCKAQITAIISQQGDIFVFDLETSAVAPFVWLDVGSIPGRFSDNGFLMTEKTRTILFYPWEPTSKNELEQSFHVTSLTDIY
Protein: 26S proteasome regulatory subunit 6B homolog (Tat-binding protein homolog 2) (P34123)
Organism: Dictyostelium discoideum (Social amoeba)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 6A homolog
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 8
- Probable 26S proteasome non-ATPase regulatory subunit 8
Sequence:
MEELGLATAKVTVTKEASHHREADLYQKMKSLESKLDFFNIQEEYIKYEYKNLKRELLHAQEEVKRIRSVPLLIGQLLEMVDSNTGIVQSTSGSTLCVRILSTIDRELLKPSASVALQRHSNALVDTLPPESDSSIHLLGADEKPSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEKGYKASIKKNTHEFNFYN
Protein: Uncharacterized protein C5H10.05c (Q09677)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MKILLINGAQEFAHSQGKFNKTLHNVAKDTLIQLGHTVQETVVDEGYDENTEVEKILWANVIIYQWPGWWMGTPWKLKRYMDEVFTAGYGQLYANDGRSSKNPTQNYGKGGLLHEHRYMISCTWNAPAAAFEEVGNFFDGRGVDGTLLTFHKANQFLGMKPLPTFMVNDVIKNPKVDIAVCAYKDHLNDVFGSANA
Protein: UNC93B1 (A0A0A8LEX5)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MMAEADTEENVYREAVAESPVAPPNGDINIDDLLPDGPQGNIQGQMEEFLGPQPEYDEEEEEKKYYRRKKLGVVKNVLGASVGGMIIYSVYMGLLQMQLILHYDETYREVKYGNLGLEDIDKKMLMGINVTPIIALLYTPILIRFLGTKWMMFLASGIYALFVSTNYWERYYTLVPSAVAIGAAIVPLWASLGNYITRMAQQYYEYVNYKDDHVQEQKKLPKGACHRYVIVFQSVFFVIFHLSLVFAEFPQRIFLHQYLSDYNHTLYNVKHCGAEGSGMIEGFNRTVLKHLPRSLALIQVESVLMGAAFLSMIIFLAVCGAAYRPTEEIDLRSIGWGNIFQLPFKHLRDYRLRLLIPFFIYSGLDTLFSVTGLTLSYGVCTVGLEWLYLLVMVYGLSCSLFSCLSLSLLRLPRYVSLLGGAVIHGPLLVFLLFWSPAPRSPDQLPYLLVVIALWGMGSALNKTGLSILLGMLYEDKERLDFVYTIYHWWQAIAIFIVYLWTGLVMRAKLSILLVILLLACFCYWTMERRLSKNMHFRLPRIPRPKHKVKGYRYLEEENSDESNSEESDEDEDEEQQEEVIREDFGGDAGSQGSDSTRERRGGARGRRRRRDDDYEQAVEREEREKEG
Protein: Ornithine transcarbamylase, mitochondrial (OTCase) (EC 2.1.3.3) (Ornithine carbamoyltransferase, mitochondrial) (Q9YHY9)
Organism: Gallus gallus (Chicken)
Function: Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion (Probable).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P00480}.
Interaction partners:
- Argininosuccinate synthase
- Uncharacterized protein.
- Arginase
- 1,4-alpha-glucan branching enzyme 1.
- Ornithine aminotransferase
- M20_dimer domain-containing protein.
- Agmatinase, mitochondrial
- Phosphoglucomutase 5.
- Phosphoglucomutase-1
- Nitric oxide synthase
Sequence:
MLFNLKNLYRITKLTQNSKHLPRHFCRGPPNQMNVCLKGRDLLTLQNYTADELKYLLWVASDLKQRIKDKGEYLPLMQGKSLAMIFEKRSTRTRLSAETGFALLGGHSSFLTKQDIHLGTNESLTDTARVLSSMTNAILARVYKHNDLDLMTKEATIPVINGLSDLYHPLQILADYLTLQEHYGGLNGLTIAWIGDGNNVLHSIMTSAAKLGMHLRIATPKGFEPDLRITKVTEQYSKEYGTRLLLTTDPLEAANGANVLVTDTWISMGQEEEKRRRLKAFQGYQITMQTVQSAASNWTFLHCLPRKPEEVDDEVFYSPRSLVFQEAENRKWTIMAVMVSLLTDYSPQLQMPTF
Protein: Submandibular gland protein C (Q6JHY3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKLILLYLAVVLCTVCKATSVRGRAGLGTYSRFGLGVLLSGKKTLSAKNSGGNKDDSVSAGGKENSNDALRLGLDGAASVNTNLDASATHRVGGSGSSTTPQKDERSPFDLIKAILRLQGATSGSSKLSVHSTNDPSAEPGDDPTAQGPQATASSTPKQNVDTNLSSAGSATSNDGAPTPREQSSADSLLEESQNLGNESPTEASGSADKPTAHSGKENSNDALRLGLDGAASVNTNLDASATHRVGRSGSSTTPQKDERSPFDLIKAILRLQGSGKGGSSAETGSSRGRGRGSGATSGSSKLSVHSTNDPSAEPGDDPTAQGPQATASSTPKQNVDTNLSSAGSATSNDGASPAREQSSADPLMEESQNLGNESPTETSGSEDSSNEENLKKVLKAFADRIPQSSTGSSDSADRPNAYSGNSFSGELERIFDSNPTKASGTGKENSNDALRLGLDGAASVNTNLDASATHHVGRSGSSTTPQKDERSLFDLIKAILRLQGSGKGGSSAETGSSRGRGRGSGNGLMLQDQPAPASGRNDKTVDTSGLSTESAISNEENLSGSGDSNKVSGPSSSAVVSTDSGDDGNLEDKQVPRFNGDERDGENNSDFFGAGSLDTGNTSDSGSHNLSSGSGSSVRSNVSIGAGPSDQNESADLGGSGRVTCAGKTVSGASSVA
Protein: Protein kinase C-like 1 (EC 2.7.11.13) (P36582)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the control of the cell shape. Target of the inhibitor staurosporine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GTP-binding protein rho1
- GTP-binding protein rho5
- MAP kinase kinase kinase mkh1
- Serine/threonine-protein kinase ksg1
- GTP-binding protein rho2
- Protein kinase C-like 2
- Rho1 guanine nucleotide exchange factor 1
- Rho1 guanine nucleotide exchange factor 3
- Rho1 guanine nucleotide exchange factor 2
- Rho-type GTPase-activating protein 1
Sequence:
MVQLDDALQDAYKKVEREESLILGAKAMVASTKNPEVKRRLESNIAVSENNIKYLRERIDALKVESGSERESQSDKDSSKKYSDSAKSTNSDDHLLSYNRSAFDLFNSEKPLSPEKISTMLQHLQMRLSIEQQCVSGIEKIMSLYSKEQKDKTDVIIKLKEGKQKVNLLKRSLKRYNELHIPFDISTPSSEEKQQASGLNFRGLAKPISGTLKVTIHSLRNIEHTSFLQTHSFTMPSYAVLYVDDAQVAKSRISQTDTWDETFIFDVHRAKEFQIIIYEKKKDFDIPIALILIPTTIIAEELRRKRNIQEMSETSWKPSIAESASRSDEKGSKSDPINAPNSSSSISTNSPLAPTAYYKLLSKSWLSLEPVGQICISLSFSKRTTKRQFPETGLGRQGAIRQKKEDVVASQVGHQFVQRQFYQIMRCAVCAELFSYSPGLQCENCSFVCHKKCVTKVLASCIAQSNSEKSDFGGLRYRIPHRFEPFNSLGAQWCAHCGFFLPLRRKDCFKCVECGITCHGQCAHLIPDYCGMSNDLKHQLLTELEVSKRPKKPELPNQENKTTNEKVYRKPLSSQNTFDTLPTISQGLLAATQPVTSVLNTSPLPKTPEKDRSLNVTPSSSTPTPASVLAPPSSASLSSSKDANRSVPESPRREKKNRVTLDDFTFLAVLGKGNFGKVMLAEYKVNKKFYAIKVLKKEAILKNEELESLKTEKHVFEVANKEKHPFLLNLFASFQTSTRVYFVMEYILGGDLMVHIQRQQFSVKRARFYGAEVCLALKYFHENGIAYRDLKLDNILLCPDGHIRIADYGLCKENMLLGNTTSTFCGTPEFMAPEILLEQQYSKDVDWWAFGVLMYQMLLGQSPFKGEDEEEIFDAILSDEPLFPINMPADAVSLLRGLLTRDPNQRLGSGPKDANEVMAHPFFASIVWDDLYNKLYEPSYKPLINDPRDLNNFDEEFTSACPTLTPVNTVLTRQQQECFRGFSSFATE
Protein: RNA-binding protein 28 (RNA-binding motif protein 28) (Q9NW13)
Organism: Homo sapiens (Human)
Function: Nucleolar component of the spliceosomal ribonucleoprotein complexes.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:17081119, ECO:0000269|Ref.7}.
Interaction partners:
- 28S rRNA
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- Ribosome biogenesis protein BMS1 homolog
- Probable ATP-dependent RNA helicase DDX27
- CCAAT/enhancer-binding protein zeta
- RRP12-like protein
- Protein RRP5 homolog
- GTP-binding protein 4
- RNA-binding protein 34
- Nucleolar complex protein 2 homolog
Sequence:
MAGLTLFVGRLPPSARSEQLEELFSQVGPVKQCFVVTEKGSKACRGFGYVTFSMLEDVQRALKEITTFEGCKINVTVAKKKLRNKTKEKGKNENSECPKKEPKAKKAKVADKKARLIIRNLSFKCSEDDLKTVFAQFGAVLEVNIPRKPDGKMRGFGFVQFKNLLEAGKALKGMNMKEIKGRTVAVDWAVAKDKYKDTQSVSAIGEEKSHESKHQESVKKKGREEEDMEEEENDDDDDDDDEEDGVFDDEDEEEENIESKVTKPVQIQKRAVKRPAPAKSSDHSEEDSDLEESDSIDDGEELAQSDTSTEEQEDKAVQVSNKKKRKLPSDVNEGKTVFIRNLSFDSEEEELGELLQQFGELKYVRIVLHPDTEHSKGCAFAQFMTQEAAQKCLLAASPENEAGGLKLDGRQLKVDLAVTRDEAAKLQTTKVKKPTGTRNLYLAREGLIRAGTKAAEGVSAADMAKRERFELLKHQKLKDQNIFVSRTRLCLHNLPKAVDDKQLRKLLLSATSGEKGVRIKECRVMRDLKGVHGNMKGQSLGYAFAEFQEHEHALKALRLINNNPEIFGPLKRPIVEFSLEDRRKLKMKELRIQRSLQKMRSKPATGEPQKGQPEPAKDQQQKAAQHHTEEQSKVPPEQKRKAGSTSWTGFQTKAEVEQVELPDGKKRRKVLALPSHRGPKIRLRDKGKVKPVHPKKPKPQINQWKQEKQQLSSEQVSRKKAKGNKTETRFNQLVEQYKQKLLGPSKGAPLAKRSKWFDS
Protein: Ammonium transporter 2 (Q9US00)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transporter for ammonium to use as a nitrogen source.
Subcellular location: Membrane {ECO:0000269|PubMed:10759889}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Ribosomal protein arginine N-methyltransferase rmt3
- tRNA
Sequence:
MSSVNSIPTATSTVYISVLPATATPSGGSGGNVLHEDLNKFYDYGNTSWILACTPLCLIMVPGVAFFYSGLARRKNTLALIMLSMLGLCVSFFQWYFWGYSLAFSQTGTSGYIGNLRHFAFIRTLADYSPGSNNIPELVFANFQGMFAAITVALFTGAAAERGRIGPMLIITFVWLTVVYCPIACWIWNPNGWAFKFGVYDFAGGGPVEVGSGFAALAYTVCLGRRSKFVEEQFRPHSVLNVVLGTSLLWFGWLGFNGGSAYGSNLRAAMAITNTNLAGAVAGLVWVIYDYIFRTRKWSTIGFCSGVVAGLVAATPCAGFVSPHASLAIGAITGLCCNWAIKLKSHMRIDDAMDIFAIHGVAGFVGTFLNGLFAVDYIAAMDGIYVGENKIRGGWFDHHWRQLGLQMAYICAVGAYDFVVTFIILFITDKIPYLQLRVSPDAEEIGVDADQIGEYAFDYIEERREYKHWKISPAGVPEEIIISNGVAQPTGNVAAPGKILESTNPLELGLTI