wanglab/gogpt-training-data huggingface dataset:
Protein: Dopamine receptor 2 (Dopamine D2-like receptor dop-2) (E7EM37)
Organism: Caenorhabditis elegans
Function: G-protein coupled receptor which binds to the neurotransmitter dopamine with high affinity leading to the activation of an associated G-protein and downstream signaling pathways. Couples to G-proteins to inhibit adenylate cyclase (AC) activity and cAMP production. Inhibits synaptic vesicle fusion to negatively regulate the release of dopamine at dopaminergic neuron synapses. Antagonizes octopamine signaling in response to food by promoting the dopamine-mediated suppression of crh-1/CREB1 transcription factor activation in cholinergic SIA neurons. This is most likely in association with the G(o)-alpha G-protein subunit goa-1. In association with the G-alpha protein gpa-14, modulates two types of learning behavior: touch habituation and chemosensory associative conditioning. May act partly via tsp-17 to negatively regulate dopamine reuptake transporter dat-1 activity. Plays a role in behavioral plasticity and regulates the decision-making process when conflicting alternatives are present. Promotes male mating behavior by antagonizing acetylcholine signaling to control the protrusions of copulatory spicules from the tail of males during hermaphrodite vulval location. Modulates unc-7 activity at gap junctions to promote inhibitory neuronal signaling transduction between chemosensory and mechanosensory neurons, and thus ensures spicule insertion attempts are confined to the hermaphrodite vulva during copulation.
Subcellular location: Cell membrane {ECO:0000305|PubMed:12887685}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dopamine receptor 4
- Dopamine receptor 3
- Guanine nucleotide-binding protein alpha-14 subunit
- Aromatic-L-amino-acid decarboxylase
- Sodium-dependent dopamine transporter
Sequence:
MEAGETWNVSLEWPPPSLDLSTITQTPSTIVGSGIPLNYAGLSLIVIPLITLLGNLLVIISVLRYRALQSAINFLILGLAVADLLVAIIVMPYAVYVYVTNGDWYLGNLMCDIYMASDVCCSTASILLLAVISFDRYRAVSLPIQYSRQSQNVKRVWTLIAVIWLVSLTLASPMVFGVNVRPPDANPYECRFYNAEFSILSSMISFVIPCFLVLFVYIRIIIALKKREKAAKMRREKNTIAHGLTMRPDTGEEQVDEEAAGRIVAGPVVNVMMAALPSMTRRMRQFERHRRAIELAGDEEWEEDELDVMDECCGGDDAGDDDDDYHADNGQGVVEASAPRTTSMLRRIINAASVGTANSTAQSVASASGMPAFFAQNISTTSPSSSSCARTTTTTSAIPKASGDLPLPMLLNEREFGNSSTPRSSLESLSENVNVITNDFVSENCTTFSRRSSYADDSQPTSSQTSSGDGRSYSIKGQKRFRNLSRNYSTKHHRKVVKVNRGNSRNNSRTASITNQSDDALIPAIIRTISRKSPRLFRRDKTDIKKHSMILANPITEPPKEYRRVSMPIHPTNSQTETETISASRDIENLPTTTISRSTTANSAELLGSPDDFEKFPALITETVLEDVLAETREGCFMQPTVSFALTVREMEGNALNNLKGCSVESSRRVSQVDPPLAIQILTRPSLPHLDLQRMDSIGTTCSSKTRADSLRSVDSKGSKKSNRNGIAVKLVKRAIKHEHSLKRKVSKAQRKEKRATKTLGVVVGVFLVCWVPFFVINILNAVCILLNKDSCQVGYDLFFYCTWIGYMNSFMNPIIYTIFNTEFRRAFKSIIFGRNSTRHHFSNKQAHV
Protein: Peptidase S1 domain-containing protein (Q3V2G3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNALLILALVGAAVAFPVDDDDKIVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKTRIQVRLGEHNINVLEGNEQFVNAAKIIKHPNFNRKTLNNDIMLLKLSSPVTLNARVATVALPSSCAPAGTQCLISGWGNTLSFGVSETDLLQCLDAPLLPQADCEASYPGKITGNMVCAGFLEGGKDSCQGDSGGPVVCNRELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN
Protein: Charged multivesicular body protein 4b (Chromatin-modifying protein 4b) (CHMP4b) (SNF7 homolog associated with Alix 1) (SNF7-2) (hSnf7-2) (Vacuolar protein sorting-associated protein 32-2) (Vps32-2) (hVps32-2) (Q9H444)
Organism: Homo sapiens (Human)
Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15511219}. Late endosome membrane {ECO:0000269|PubMed:15511219, ECO:0000305|PubMed:12860994}; Peripheral membrane protein {ECO:0000305}. Midbody {ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:22422861}. Nucleus envelope {ECO:0000269|PubMed:26040712}. Note=Recruited to the nuclear envelope by CHMP7 during late anaphase (PubMed:26040712). Localizes transiently to the midbody arms immediately before abscission (PubMed:22422861). {ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:26040712}.
Interaction partners:
- Programmed cell death 6-interacting protein
- Charged multivesicular body protein 3
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 6
- Charged multivesicular body protein 1b
- Tyrosine-protein phosphatase non-receptor type 23
- Charged multivesicular body protein 2b
- BRO1 domain-containing protein BROX
- Vacuolar protein-sorting-associated protein 25
- Charged multivesicular body protein 4c
Sequence:
MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSIALPSKPAKKKEEEDDDMKELENWAGSM
Protein: Claudin-1 (Senescence-associated epithelial membrane protein) (O95832)
Organism: Homo sapiens (Human)
Function: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:23407391}. Cell membrane {ECO:0000269|PubMed:23704991}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:20375010}. Note=Associates with CD81 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:0000269|PubMed:20375010}.
Interaction partners:
- Tight junction protein 1
- Occludin
- Tight junction protein 2
- CD81 antigen
- Tight junction protein ZO-3
- Junctional adhesion molecule A
- InaD-like protein
- Claudin-12
- Claudin-4
- Scavenger receptor class B member 1
Sequence:
MANAGLQLLGFILAFLGWIGAIVSTALPQWRIYSYAGDNIVTAQAMYEGLWMSCVSQSTGQIQCKVFDSLLNLSSTLQATRALMVVGILLGVIAIFVATVGMKCMKCLEDDEVQKMRMAVIGGAIFLLAGLAILVATAWYGNRIVQEFYDPMTPVNARYEFGQALFTGWAAASLCLLGGALLCCSCPRKTTSYPTPRPYPKPAPSSGKDYV
Protein: EP2K protein (Q8SQD1)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRQRLLPFFTSLLLVALLFPGLSQARHVNHSATEALRELREGATGQGTNRSQLLRHPVKRAPIIRRIPYYPEVESDLRIVDCKRSEGFCQEYCNYLETQCTSLTRRLEDPDLRAAWAF
Protein: TBRG1 protein (Q05BL0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKKLPKKSQNEKYRLKYLRLRKAAKATVFENAAICDEIARLEEKFLKAKEERRYLLKKLLQLQALTEGEVQAAAPSHSSSLPLTYGVASSVGTIQGAGPISGPSTGAEEPFGKKTKKEKKEKGKENNKLEDHHRPTWLS
Protein: Alanine aminotransferase, mitochondrial (EC 2.6.1.2) (Glutamate pyruvate transaminase) (GPT) (Glutamic--alanine transaminase) (Glutamic--pyruvic transaminase) (P52893)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11502169}.
Interaction partners:
- Inactive alanine aminotransferase
- NAD-specific glutamate dehydrogenase
- Alanine--glyoxylate aminotransferase 1
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- NADP-specific glutamate dehydrogenase 2
- Arginine biosynthesis bifunctional protein ArgJ, mitochondrial
- NADP-specific glutamate dehydrogenase 1
- Glutathione hydrolase proenzyme
- Amino-acid acetyltransferase, mitochondrial
Sequence:
MLSLSAKNHFTVSNSITHVIKSYHIRTLTSSAEKMPHITTPFSTSASSTKLKAFRKVRPVLQRHSSSWIVAQNHRRSLSGQSSLNDLRHLNRFPHHTLKTSNNEFYPAEQLTLEDVNENVLKAKYAVRGAIPMRAEELKAQLEKDPQSLPFDRIINANIGNPQQLQQKPLTYYRQVLSLLQYPELLNQNEQQLVDSKLFKLDAIKRAKSLMEDIGGSVGAYSSSQGVEGIRKSVAEFITKRDEGEISYPEDIFLTAGASAAVNYLLSIFCRGPETGVLIPIPQYPLYTATLALNNSQALPYYLDENSGWSTNPEEIETVVKEAIQNEIKPTVLVVINPGNPTGAVLSPESIAQIFEVAAKYGTVVIADEVYQENIFPGTKFHSMKKILRHLQREHPGKFDNVQLASLHSTSKGVSGECGQRGGYMELTGFSHEMRQVILKLASISLCPVVTGQALVDLMVRPPVEGEESFESDQAERNSIHEKLITRAMTLYETFNSLEGIECQKPQGAMYLFPKIDLPFKAVQEARHLELTPDEFYCKKLLESTGICTVPGSGFGQEPGTYHLRTTFLAPGLEWIKKWESFHKEFFDQYRD
Protein: Keratin-associated protein 22-1 (Q3MIV0)
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 20-1
- Keratin-associated protein 6-3
- Keratin-associated protein 6-1
- Keratin-associated protein 20-2
- Keratin-associated protein 15-1
- Keratin-associated protein 24-1
- Keratin-associated protein 26-1
- Keratin-associated protein 13-3
- Keratin-associated protein 6-2
- Small cysteine and glycine repeat-containing protein 1
Sequence:
MSFDNNYHGGQGYAKGGLGCSYGCGLSGYGYACYCPWCYERSWFSGCF
Protein: Putative fucose kinase (EC 2.7.1.52) (Q4QEX2)
Organism: Leishmania major
Interaction partners:
- Putative fucose kinase
- Phosphotransferase
- Phosphotransferase
Sequence:
MNVSFLFSLPCNLAEFKGAAKLLADAAALPLRECGAKGGVAVPGLFCGCDPEGRPLGSGGGTVHLLHACYVDEQRHAPASAKRSFLSWLRLADNDGRVIVHAGGLSRRLPAYAAMGKALLPLPPRRWHRGSQLSRTLLSTQVPMYREIVAMAPARLRTLIACGDVCVDARGALPSLAHFADSDVLCFGINADASLFQNHGVLFTARERPLDLDYMLQKPSLDEVRRRVAEGRHSVLLDVGMWMLSDRAVEVLTRKCLGGALDAEDATDGGYDGHRCTAVRTAYDLYSEFASALGNNAPIADPEIAGLKASVVELRDAEFLHYGTNRQLISAVATLQGRESPTPPWSWGTPLDGVLAPERGGGGEELDFAAGDAMPLLATPSSVIVQNSVVLAPLDGSAAAAAADAPAGAPLSPVRHLWVESSWVGARWALRDQHILTGVPRNDWALALPPGACVSVVPVLPAALGGCGDGAVPHAARPYHMDDAFCGDVRSGSTMYMGVRLHDWLSSRGFSVAELYPAARAADGGAAQPLDMYEAALFPVCATEQQLGDFLYVATLPLEAATGGCAGVDAARLAAGQAVWRTQPRVSAMDLLRLTDVPAMLRNSEYYERRMLTLMLALVAGDPAAPRARSPVLPGPMVALLQQQFFLLDLNRVAQRVVELGVPLPRHSGPTEWWGGVDAAGNAVALSRQVAPAAPFAKGAAASAGSWAQVFSDEGSPSGGGRGAPLCTAPGRIVAAHYHAFASRLMELALEAMDAAEPPVSAAEKARRLALLRASSAEEARSLVALHDAAALAELRAAIMDSFPDERHDPEMSVHLDQIIWGRCPIRIDVAGAWTDTPPYAILSGGSVINVAVELNGQPPVQVYVRVREDPIIMMHSIDSGEQLSVSSFDEIRTYATMQNPFSIPKAALALCGFLPEFCATEYATLREQLAARFGGHGLEISLFVAIPTGSGLGTSSIVAGTVLRSLAEFCKLPWDNHDVCRRVLLIEQMLTAGGGWQDQYGGLFEGLKLVQCVPGLPCLPTVRWMPDSVYTDPRFAACHLLYYTGITRMAKGILGEIVRDVLLNNGATLQLLREMGGPTTAAMYDAITTGNYKGYARLVHRTWEQKKRLDDGVCNPTVQSIVDIVEPYVWGLTLPGAGGGGYMYMCAKDEACARRIRELLTANPPNGNARFVEMSVSASGLQISRS
Protein: AP2-associated protein kinase 1 (EC 2.7.11.1) (Adaptor-associated kinase 1) (F1SPM8)
Organism: Sus scrofa (Pig)
Function: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Preferentially, may phosphorylate substrates on threonine residues (By similarity). Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes (By similarity). Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes (By similarity). Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:F1MH24}; Peripheral membrane protein {ECO:0000250|UniProtKB:F1MH24}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P0C1X8}. Presynapse {ECO:0000250|UniProtKB:P0C1X8}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells. {ECO:0000250|UniProtKB:P0C1X8}.
Interaction partners:
- AP-2 complex subunit mu
- AP complex subunit beta.
Sequence:
MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTESEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSFFSFKLLKKECPVPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRAMVQPPPQVAGSSNQPGLLASVPQPKTQAPPSQPLPQSQAKQPQAPPAPQQPPSAPAQGLPAQAQATPQHQQQLFLKQQPQPPQPQPQAQAPPVKSLKFYPFYPMCKGRQTVSSQFQAVHPAAQQPAIAQFPAVSQGSSQQQLIQNFYQQQQQQQQQQQLATTLHQQQLLTQQAALQQKTTVAAIQPPQAQPATASQPPPAQEPAQIQAPVRQQPKVQTTPPPAIQGQKLGSLTPPSSPKAQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRASQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQPTQGDAFAASSFAAGTAEKRKGGQAVDSSLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVASNRTDSLTGEDALIDCSLLSNPTTDLLEEFAPIAISAPAHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL
Protein: Lamina-associated polypeptide 2, isoforms alpha/zeta (Thymopoietin isoforms alpha/zeta) (TP alpha/zeta) (Q61033)
Organism: Mus musculus (Mouse)
Function: May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Expressed diffusely throughout the nucleus. {ECO:0000250}.
Interaction partners:
- Prelamin-A/C
- Barrier-to-autointegration factor
- Barrier-to-autointegration factor-like protein
- Lamin-B1
- Emerin
- Lamin-B2
- Delta
Sequence:
MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLAAGANSKGPPDFSSDEEREPTPVLGSGASVGRGRGAVGRKATKKTDKPRLEDKDDLDVTELSNEELLDQLVRYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTVSSSAENTRQNGSNDSDRYSDNDEGKKKEHKKVKSARDCVPFSELASTPSGAFFQGISFPEISTRPPLGRTELQAAKKVQTTKRDPPRETCTDTALPGKGQTHKLAPGRSLFIPSESSYDRCVEKSSSPSSQREFAARLVSAAASPSLIRETTTTYSKDIVENICRGGKSRAQPLRAEEPGVSDQSVFSSEREVLQESERSQVISPPLAQAIRDYVNSLLVQGGVGSLPGTSDSVPTLDVENICKRLSQSSYQDSESLSPPRKVPRLSEKPARGGDSGSCVAFQNTPGSEHRSSFAKSVVSHSLTTLGVEVSKPPPQHDKIEASEPSFPLHESILKVVEEEWQQIDRQLPSVACRYPVSSIEAARILSVPKVDDEILGFISEATPRAATQASSTESCDKHLDLALCRSYEAAASALQIAAHTAFVAKSLQADISQAAQIINSDPSDAQQALRILNRTYDAASYLCDAAFDEVRMSACAMGSSTMGRRYLWLKDCKISPASKNKLTVAPFKGGTLFGGEVHKVIKKRGNKQ
Protein: Cellulose synthase (EC 2.4.1.12) (Q1EG93)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361116}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361116}.
Interaction partners:
Sequence:
MMESGVPVCHTCGEHVGLNVNGEPFVACHECNFPICKSCFEYDLKEGRKACLRCGSPYDENLLDDVEKATGDQSTMAAHLSKSQDVGIHARHISSVSTLDSEMTEDNGNPIWKNRVESWKEKKNKKKKPATTKVEREAEIPPEQQMEDKPAPDASQPLSTIIPIPKSRLAPYRTVIIMRLIILGLFFHYRVTNPVDSAFGLWLTSVICEIWFAFSWVLDQFPKWYPVNRETYIDRLSARYEREGEPNELAAVDFFVSTVDPLKEPPLITANTVLSILALDYPVDKVSCYISDDGAAMLTFESLVETADFARKWVPFCKKFSIEPRAPEFYFSQKIDYLKDKVQPSFVKERRAMKRDYEEYKIRINALVAKAQKTPEEGWTMQDGTPWPGNNPRDHPGMIQVFLGYSGAHDIEGNELPRLVYVSREKRPGYQHHKKAGAENALVRVSAVLTNAPFILNLDCDHYVNNSKAVREAMCFLMDPQVGRDVCYVQFPQRFDGIDRSDRYANRNTVFFDVNMKGLDGIQGPVYVGTGCVFNRQALYGYGPPSMPSFPKSSSSSCSCCCPGKKEPKDPSELYRDAKREELDAAIFNLREIDNYDEYERSMLISQTSFEKTFGLSSVFIESTLMENGGVAESANPSTLIKEAIHVIGCGYEEKTAWGKEYPFTSLPLIAYCSLPAICLLTGKFIIPTLSNLASVLFLGLFLSIIVTAVLELRWSGVSIEDLWRNEQFWVIGGVSAHLFAVFQGFLKMLAGIDTNFTVTAKAADDADFGELYIVKWTTLLIPPTTLLIVNMVGVVAGFSDALNKGYEAWGPLFGKVFFSFWVILHLYPFLKGLMGRQNRTPTIVVLWSVLLASVFSLVWVRINPFVSTADSTTVSQSCISIDC
Protein: Submandibular gland protein C (A0A8I6AAS6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKLILLYLAVVLCTVCKGDSNKVSGPSSSAVVSTDSGDDGNLEDKQVPRFNGDERDGENNSDFFGAGSLDTGNTSDSGSHNLSSGSGSSVRSNVSIGAGPSDQNESADLGGSGRVTCAGKTVSGASSVA
Protein: GDP-mannose transporter GONST1 (Protein GOLGI NUCLEOTIDE SUGAR TRANSPORTER 1) (Q941R4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen. Required for the luminal synthesis of a variety of plant cell surface components. Is required for the correct mannosylation of the glycosylinositol phosphoceramides (GIPC). Can indifferently transport GDP-mannose, GDP-Glucose, GDP-Fucose or GDP-Galactose in vitro.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11595802, ECO:0000269|PubMed:27381418}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- F3F20.10 protein
- Glucosamine inositolphosphorylceramide transferase 1
- 3-dehydrosphinganine reductase TSC10B
- Inositol phosphorylceramide glucuronosyltransferase 1
- UDP-xylose transporter 3
- UDP-galactose/UDP-glucose transporter 2
- 3-dehydrosphinganine reductase TSC10A
- Sugar transport protein 2
- Phosphatidylinositol:ceramide inositolphosphotransferase 2
- UDP-galactose/UDP-glucose transporter 1
Sequence:
MKLYEHDGVDLEDGKTVKSGGDKPIPRKIHNRALLSGLAYCISSCSMILVNKFVLSSYNFNAGIFLMLYQNFVSVIIVVGLSLMGLITTEPLTLRLMKVWFPVNVIFVGMLITSMFSLKYINVAMVTVLKNVTNVITAVGEMYLFNKQHDNRVWAALFLMIISAVSGGITDLSFNAVGYAWQIANCFLTASYSLTLRKTMDTAKQVTQSGNLNEFSMVLLNNTLSLPLGLLLSYFFNEMDYLYQTPLLRLPSFWMVMTLSGLLGLAISFTSMWFLHQTGATTYSLVGSLNKIPLSIAGIVLFNVPTSLQNSASILFGLVAGVVFARAKMREKS
Protein: Gamma-hemolysin component A (H-gamma-2) (H-gamma-II) (P0A071)
Organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)
Function: Toxin that seems to act by forming pores in the membrane of the cell. Has a hemolytic and a leucotoxic activity (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MIKNKILTATLAVGLIAPLANPFIEISKAENKIEDIGQGAEIIKRTQDITSKRLAITQNIQFDFVKDKKYNKDALVVKMQGFISSRTTYSDLKKYPYIKRMIWPFQYNISLKTKDSNVDLINYLPKNKIDSADVSQKLGYNIGGNFQSAPSIGGSGSFNYSKTISYNQKNYVTEVESQNSKGVKWGVKANSFVTPNGQVSAYDQYLFAQDPTGPAARDYFVPDNQLPPLIQSGFNPSFITTLSHERGKGDKSEFEITYGRNMDATYAYVTRHRLAVDRKHDAFKNRNVTVKYEVNWKTHEVKIKSITPK
Protein: N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) (Peptidoglycan recognition protein 2) (Peptidoglycan recognition protein long) (PGRP-L) (TagL) (Q8VCS0)
Organism: Mus musculus (Mouse)
Function: May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity.
Subcellular location: Secreted. Membrane.
Interaction partners:
Sequence:
MKAWGALWIVLGLLLWPEPGAASSLPLLMDSIIQALAELEQKVPVTEASITASAWILSAKNSSTHNSLHQRLLLKAPSHNTTEPDPHSLSPELQALISEVAQHDVQNGREYGVVLAPDGSTVAVKPLLFGLEAGLQAHSVANLPSDCLAIPCDTGDTLANIRATWPGLMDAFPNASSPDVGATLPNDKAKTPTTVDRLLAITLAGDLGLTFLHRSQTWSPPGLGTEGCWDQLTAPRVFTLLDPQASRLTMAFLNGALDGALLGNHLSQIPRPHPPLSHLLREYYGAGVNGDPVFRSNFRRQNGAALTSAPTLAQQVWEALVLLQKLEPEHLQLQNISQEQLAQVATLATKEFTEAFLGCPAIHPRCRWGAAPYRGHPTPLRLPLGFLYVHHTYVPAPPCTTFQSCAADMRSMQRFHQDVRKWDDIGYSFVVGSDGYLYQGRGWHWVGAHTRGYNSRGFGVAFVGNYTGSLPNEAALNTVRDALPSCAIRAGLLRPDYKLLGHRQLVLTHCPGNALFNLLRTWPHFTEVEN
Protein: G protein-activated inward rectifier potassium channel 4 (GIRK-4) (Cardiac inward rectifier) (CIR) (Heart KATP channel) (Inward rectifier K(+) channel Kir3.4) (IRK-4) (KATP-1) (Potassium channel, inwardly rectifying subfamily J member 5) (P48544)
Organism: Homo sapiens (Human)
Function: This potassium channel 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 external barium.
Subcellular location: Membrane {ECO:0000269|PubMed:22315453, ECO:0000269|PubMed:24037882}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- G protein-activated inward rectifier potassium channel 1
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- G protein-activated inward rectifier potassium channel 2
- G protein-activated inward rectifier potassium channel 3
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid type B receptor subunit 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MAGDSRNAMNQDMEIGVTPWDPKKIPKQARDYVPIATDRTRLLAEGKKPRQRYMEKSGKCNVHHGNVQETYRYLSDLFTTLVDLKWRFNLLVFTMVYTVTWLFFGFIWWLIAYIRGDLDHVGDQEWIPCVENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIILLLVQAILGSIVNAFMVGCMFVKISQPKKRAETLMFSNNAVISMRDEKLCLMFRVGDLRNSHIVEASIRAKLIKSRQTKEGEFIPLNQTDINVGFDTGDDRLFLVSPLIISHEINQKSPFWEMSQAQLHQEEFEVVVILEGMVEATGMTCQARSSYMDTEVLWGHRFTPVLTLEKGFYEVDYNTFHDTYETNTPSCCAKELAEMKREGRLLQYLPSPPLLGGCAEAGLDAEAEQNEEDEPKGLGGSREARGSV
Protein: Large ribosomal subunit protein bL32m (54S ribosomal protein L32, mitochondrial) (YmL32) (P25348)
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.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16239145}. 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:16239145, ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein uL3m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL27m
Sequence:
MNSLIFGKQLAFHKIVPTTAIGWLVPLGNPSLQIPGQKQLGSIHRWLREKLQQDHKDTEDKDFFSNNGILLAVPKKKVSHQKKRQKLYGPGKKQLKMIHHLNKCPSCGHYKRANTLCMYCVGQISHIWKTHTAKEEIKPRQEEELSELDQRVLYPGRRDTKYTKDLKDKDNYLERRVRTLKKD