wanglab/gogpt-training-data huggingface dataset:
Protein: Kremen protein 2 (Dickkopf receptor 2) (Kringle domain-containing transmembrane protein 2) (Kringle-containing protein marking the eye and the nose) (Q8K1S7)
Organism: Mus musculus (Mouse)
Function: Receptor for Dickkopf proteins. Cooperates with DKK1/2 to inhibit Wnt/beta-catenin signaling by promoting the endocytosis of Wnt receptors LRP5 and LRP6. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning and can also negatively regulate bone formation.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Dickkopf-related protein 1
- Fanconi anemia group M protein homolog
- Low-density lipoprotein receptor-related protein 6
- Low-density lipoprotein receptor-related protein 5
- Dickkopf-related protein 2
- Dickkopf-related protein 4
- Kremen protein 1
- Dickkopf-related protein 3
Sequence:
MGTPHLQGFLLLFPLLLRLHGASAGSLHSPGLSECFQVNGADYRGHQNYTGPRGAGRPCLFWDQTQQHSYSSASDPQGRWGLGAHNFCRNPDGDVQPWCYVAETEEGIYWRYCDIPTCHMPGYLGCFVDSGAPPALSGPSGTSTKLTVQVCLRFCRMKGYQLAGVEAGYACFCGSESDLARGRPAPATDCDQICFGHPGQLCGGDGRLGIYEVSVGSCQGNWSAPQGVIYSPDFPDEYGPDRNCSWVLGQLGAVLELTFRLFELADSRDRLELRDVSSGNLLRAFDGAHPPPPGPLRLRTAALLLTFRSDARGHAQGFALTYRGLQDTVEGRASPEDSTESLAGDPDGANASCSPKPGAAQASIGARVFSTVTAFSVLLLLLLSLLRLLRRRSCLLAPGKGSLAMGPSRGPGRSWAVWYRRPRGVALPCPPGDSQAEGPAAGYRPLSASSQSSLRSLVSAL
Protein: UL16-binding protein-like transcript 1 splicing variant (Q330P3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MELTASNKVLSCCLSLLCLLSVCLCPRIEEPLTLQAEVCGQYEVDKHFTGYAIVSLNGKNIFRVDTSTGNWTQLDHEFEKFIKMCKEDKVLAAFLKKTTEGDCRTWLDELMLHWKEHLEPAGSFSTLMIILCVIAIAFLGLIFGVSCKLRHLRTKKIGLQSSPPPFLDDSLTVPTSPQSSVCGTMIQCLCPRKLKSPVFMQIDLQSSAPPLLDDSLTVPETCSVKKEDEFPTASQNSVLLTSDDIDGIP
Protein: Carbohydrate-binding domain-containing protein Cthe_2159 (Polysaccharide lyase-like protein Cthe_2159) (PL-like protein Cthe_2159) (A3DHD2)
Organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
Function: Binds cellulosic and pectic substrates. Displays no enzyme activity (in vitro).
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305}.
Interaction partners:
- VTC domain-containing protein
- DUF4956 domain-containing protein
- DUF4956 domain-containing protein
- Ricin B lectin
Sequence:
MSIKKLILAASILTTLALTGCGGKGAVQPSGVSTGDVNAKIVFDNDKVNADNVDGLSVSEREVKITKPGMYTFSGTWNDGQILVDIGKEFEAVLVLDGVNITNTKSAPIYIKSAEKVKIELADGKDNVLTDAEFYEFEDPQDNKPNACIYSRDDITIKGNGNLTVNANFNNGIGTSNDLKITGGNITVKAFNNGLKGNDSVTISGGNIDITAEADGIKVENTEEPHKGYVNITGGTIKIRAKDDAIDSVRSVSINNADVKVSVGGKDVKCEGVLNIAEGCLGKLEE
Protein: Uncharacterized protein YKL018C-A (Q3E7A7)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MLGMIRWVVEGTLVAMLLSAIRRETGMIFFYNQYQLGGWIHRYLSWGEMCYTRTLKMVKRSKFFRKQLNEDGFGRINDSGPKRRGRDQSQYSSRFVELD
Protein: GDP-mannose 4,6 dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) (GMD) (O60547)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Interaction partners:
- GDP-L-fucose synthase
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
- Poly [ADP-ribose] polymerase tankyrase-1
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Forkhead box protein C1
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Poly [ADP-ribose] polymerase tankyrase-2
- Dolichol phosphate-mannose biosynthesis regulatory protein
- GDP-fucose transporter 1
- Dolichol-phosphate mannosyltransferase subunit 3
Sequence:
MAHAPARCPSARGSGDGEMGKPRNVALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTGRIEHLYKNPQAHIEGNMKLHYGDLTDSTCLVKIINEVKPTEIYNLGAQSHVKISFDLAEYTADVDGVGTLRLLDAVKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATGEVHSVREFVEKSFLHIGKTIVWEGKNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCTKAKQKLNWKPRVAFDELVREMVHADVELMRTNPNA
Protein: DNA-directed RNA polymerase 30 kDa polypeptide (EC 2.7.7.6) (P21603)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG134, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.
Subcellular location: Virion. Host cytoplasm. Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs are synthesized within minutes after virus entry into the cell and are extruded through pores in the core particle.
Interaction partners:
Sequence:
MENVYISSYSSNEQTSMAVTATDIRELLSQYVDDANLEDLIEWAMEKSSKYYIKNIGNTKSNIEETKFESKNNIGIEYSKDSRNKLSYRNKPSIATNLEYKTLCDMIKGTSGTEKEFLRYLLFGIKCIKKGVEYNIDKIKDVSYNDYFNVLDEKYNTPCPNCKSRNTTPMMIQTRAADEPPLVRHACRDCKQHFKPPKFRAFRNLNVTTQSIHENKEITEILPDNNPSPPESPEPASPIDDGLIRATFDRNDEPPEDDE
Protein: Doublecortin-like and CAM kinase-like protein (Q8MZC6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSEQSTSLGSRRVGPPLHKKALRVCFLRNGDRHFQGVNLVISRAHFKDFPALLQGVTESLKRHVVLRSAIAHFRRTDGSHLTSLSCFRETDIVICCCKNEEIICVKYSINKDFQRMVDSCKRWGQRHLDSGTLESMKSHDLPEAIQLYIETIEPVEHNTRTLIYRGQTRANRTKCTVKMVNKQTQSNDRGDTYMEAEVLRQLQSHPNIIELMYTVEDERYMYTVLEHLDCNMQKVIQKRGILSEADARSVMRCTVSALAHMHQLQVIHRDIKPENLLVCSSSGKWNFKMVKVANFDLATYYRGSKLYFRCGTPCYMAPEMIAKSGYDYQVDSWSLGVTLFYMLCGKMPFASACKNSKEIYAAIMSGGPTYPKDMESVMSPEATQLIDGLLVSDPSYRVPIAELDKFQFLAL
Protein: 26S proteasome regulatory subunit 7 (26S proteasome AAA-ATPase subunit RPT1) (Proteasome 26S subunit ATPase 2) (P35998)
Organism: Homo sapiens (Human)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC2 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22078707}. Note=Colocalizes with TRIM5 in cytoplasmic bodies. {ECO:0000269|PubMed:22078707}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 1
- Proteasome subunit beta type-2
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-3
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasome subunit beta type-1
Sequence:
MPDYLGADQRKTKEDEKDDKPIRALDEGDIALLKTYGQSTYSRQIKQVEDDIQQLLKKINELTGIKESDTGLAPPALWDLAADKQTLQSEQPLQVARCTKIINADSEDPKYIINVKQFAKFVVDLSDQVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTVTMMQVEEKPDVTYSDVGGCKEQIEKLREVVETPLLHPERFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKIEFSLPDLEGRTHIFKIHARSMSVERDIRFELLARLCPNSTGAEIRSVCTEAGMFAIRARRKIATEKDFLEAVNKVIKSYAKFSATPRYMTYN
Protein: Sex comb on midleg-like protein 1 (Q9UN30)
Organism: Homo sapiens (Human)
Function: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. May be involved in spermatogenesis during sexual maturation (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MMSNSSSEIDVIKTRIPTYDEDDNTILYAYETKPEFVNKEPNIVSDASCNTEEQLKTVDDVLIHCQVIYDALQNLDKKIDVIRRKVSKIQRFHARSLWTNHKRYGYKKHSYRLVKKLKLQKMKKNEVYETFSYPESYSPTLPVSRRENNSPSNLPRPSFCMEEYQRAELEEDPILSRTPSPVHPSDFSEHNCQPYYASDGATYGSSSGLCLGNPRADSIHNTYSTDHASAAPPSVTRSPVENDGYIEEGSITKHPSTWSVEAVVLFLKQTDPLALCPLVDLFRSHEIDGKALLLLTSDVLLKHLGVKLGTAVKLCYYIDRLKQGKCFEN
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (A0A1W2PS19)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}.
Interaction partners:
Sequence:
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESMFTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSLCKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKPSHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYPLSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSLLLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLSTVLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTRQLLACTAWLFMYISASPNRLWMLSDPGLDLNLLHAIRAWYVKGTP
Protein: CAAX prenyl protease 2 (EC 3.4.26.1) (Prenyl protein-specific endoprotease 2) (PPSEP 2) (Ras and A-factor-converting enzyme) (RACE) (Q03530)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Proteolytically removes the C-terminal three residues of farnesylated proteins, including the a-factor mating pheromone and RAS.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9736709}; Multi-pass membrane protein {ECO:0000269|PubMed:9736709}.
Interaction partners:
- CAAX prenyl protease 1
- Protein-S-isoprenylcysteine O-methyltransferase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
- Putative protease AXL1
- A-factor-processing enzyme
- Conserved oligomeric Golgi complex subunit 6
- Alpha-factor-transporting ATPase
- Rho GDP-dissociation inhibitor
- Ras-like protein 2
Sequence:
MLQFSTFLVLLYISISYVLPLYATSQPEGSKRDNPRTIKSRMQKLTIMLISNLFLVPFLQSQLSSTTSHISFKDAFLGLGIIPGYYAALPNPWQFSQFVKDLTKCVAMLLTLYCGPVLDFVLYHLLNPKSSILEDFYHEFLNIWSFRNFIFAPITEEIFYTSMLLTTYLNLIPHSQLSYQQLFWQPSLFFGLAHAHHAYEQLQEGSMTTVSILLTTCFQILYTTLFGGLTKFVFVRTGGNLWCCIILHALCNIMGFPGPSRLNLHFTVVDKKAGRISKLVSIWNKCYFALLVLGLISLKDTLQTLVGTPGYRITL
Protein: N-terminal kinase-like protein (SCY1-like protein 1) (E9PPN3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAVFVDRAGEWKLGGLDYMYSAQGNGGGPPRKGIPELEQYDPPELADSSGRVVREKWSADMWRLGCLIWEVFNGPLPRAAALRNPGKIPKTLVPHYCELVGANPKVRPNPARFLQNCRAPGGFMSNRFVETNLFLEEIQIKEPAEKQKFFQELSKSLDAFPEDFCRHKVLPQLLTAFEFGNAGAVVLTPLFKVGKFLSAEEYQQKIIPVVVKMFSSTDRAMRIRLLQQMEQFIQYLDEPTVNTQIFPHVVHGFLDTNPAIREQTVKSMLLLAPKLNEANLNVELMKHFARLQAKDEQGPIRCNTTVCLGKIGSYLSASTRHRVLTSAFSRATRDPFAPSRVAGVLGFAATHNLYSMNDCAQKILPVLCGLTVDPEKSVRDQAFKAIRSFLSKLESVSEDPTQLEEVEKDVHAASSPGMGGAAASWAGWAVTGVSSLTSKLIRSHPTTAPTETNIPQRPTPEGVPAPAPTPVPATPTTSGHWETQEEDKDTAEDSSTADRWDDEDWGSLEQEAESVLAQQDDWSTGGQVSRASQVSNSDHKSSKSPESDWSSWEAEGSWEQGWQEPSSQEPPPDGTRLASEYNWGGPESSDKGDPFATLSARPSTQPRPDSWGEDNWEGLETDSRQVKAELARKKREERRREMEAKRAERKVAKGPMKLGARKLD
Protein: Cytochrome b5 heme-binding domain-containing protein (Q581R4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MDKAVGKLVKVGKVLAVAAAVSVISRAIIQRLYKLHKIHCHRGQGIRPVKPIVQRSFTADELQEYDGVRKSDVYVSVKGVVYEVAPQFYGPGQPYHIYAGREISRCLAKSDLTGDEINKDWRPGSTEEELQQLEGWVKKFESRYPVVGWFIWE
Protein: Uncharacterized protein (Q57W01)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MASVGNCFRRFMSVITAVLLALSTTIYAVCLSVVVFREVKRDRFTVFHMLSVAFCSLSLFCYAALHCISLKQRYLLYIITFVLLITFGFLTHSTGLTLLVVLDCRDLGILNHSEFFDALNNPAELTSMLNESGTIDNETAVIGKSGRAVHSCSLHSMVVFAACVTALFQMLALFDVQKVLVEKTKKKMYNVDVCGVPCVK
Protein: Regulator of chromosome condensation domain-containing protein (Q54SA3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MDDEDYRNSKQIFYWGRGVNQGDKHIIEPIEVPELNKKNIVQLSCGSTHTLVLSDSGDLYSWGSSNSSGQLGHGDSKNQYGKPKNIKKFSLIKALSGDSVIQVSTGLDFTFVLTDQGSIYNWGSNIEGQLALGQPVNKNEKENNINNNTTNNNNSNSNKEGGGGGGGGVKGGKNILSPIPQPLDQFSSASSTSLLIDSLTSTYSTRSYITLSNEQQQQKIQQQQQKWINGRKSVNSSTITSSSPFSSVSNFIKEMVGSNNNNNNNENDENNNNNNNNNNNNNKRGATLGSLSSSTTTSNNSTPNTTANNSPNLLSSSSSSSSAATNNELKFKQTTPTKVLSFGGSNDNNFLGGVINNELQMMTDQMNSIKIIQISCGSNHILALSDQYHVYSWGSAEHGKLGHGEDYSFVSQNPRWINSPKKIKSLQEKGVTVISVSSGYSHCMALTLDSGILTWGKGSDGQLGTGFRHDIWSPFEIKRVIDKNEKIVQICCGYFNSFFITLEKRELYQFGWSIPLGKSDDILIPTKFIWLNPLKNKNNNNENEDKKDDDDDNDDEDENNDNSNRIKQISSGYSHTLILNENGECLSIGQGEFGQLGIPLDHSSIDKDSFVNYPTVIPALLPYFVESVQCGRWHSVAIVSNRNLRDHLTNSKKLKEKQKQKQQTNLEILEEFESNIEEIERMITDGIDGSKINKNNISSSLKRNSKSIINNSNSNNNNNNRGSLDVFDGLSVSFQSFIDFVNDKKNEEPSPDAIITTNDEFEKSFFLLQKDYISSKSNDLNCSLSSLEEGGGSGGGSGGGSRNEENDSHEGNNNNNGAGGGFETIKISKPFYRDLNDFLFKSKSTSQSLSTTTSLPSNNPILNQIELSSDGSEESTEELLIQVLLTKFLPDFDKMKTNKKEWRDLWRRGFPPTIRGIIWKRAIGNKLEINGTLYHGLLDQLSDLQDRYNRDLVLLGEGFEANLPPNLPKEYSTFIKTFNMIKVDLPRTFPQLRLFNPAGALHEQLRTTLLLFALYTPQIGYVQGMSYLAAVFCLFMDPFESFVYFTNLLNNHFFNSLFKMDIRGIVNHVKIFDLLFKNHVPKLYDKFQQLELSTEHFLLEWMMTLFTKQLPLNIVFRIWDSYFMEGEAFIYSTAIGILKLCRNFIIASNFEDSLAIIKSTPHNLKEEDLFDSISAVHIPKFIKKIILLINKDFI
Protein: CD180 antigen (Lymphocyte antigen 78) (Ly-78) (Radioprotective 105 kDa protein) (CD antigen CD180) (Q62192)
Organism: Mus musculus (Mouse)
Function: May cooperate with MD-1 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-kappa-B activation. Also involved in the life/death decision of B-cells.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Lymphocyte antigen 86
- Lymphocyte antigen 96
Sequence:
MAPDISCFFLVALFLASCRATTSSDQKCIEKEVNKTYNCENLGLNEIPGTLPNSTECLEFSFNVLPTIQNTTFSRLINLTFLDLTRCQIYWIHEDTFQSQHRLDTLVLTANPLIFMAETALSGPKALKHLFFIQTGISSIDFIPLHNQKTLESLYLGSNHISSIKLPKGFPTEKLKVLDFQNNAIHYLSKEDMSSLQQATNLSLNLNGNDIAGIELGAFDSAVFQSLNFGGTQNLLVIFKGLKNSTIQSLWLGTFEDMDDEDISPAVFEGLCEMSVESINLQKHYFFNISSNTFHCFSGLQELDLTATHLSELPSGLVGLSTLKKLVLSANKFENLCQISASNFPSLTHLSIKGNTKRLELGTGCLENLENLRELDLSHDDIETSDCCNLQLRNLSHLQSLNLSYNEPLSLKTEAFKECPQLELLDLAFTRLKVKDAQSPFQNLHLLKVLNLSHSLLDISSEQLFDGLPALQHLNLQGNHFPKGNIQKTNSLQTLGRLEILVLSFCDLSSIDQHAFTSLKMMNHVDLSHNRLTSSSIEALSHLKGIYLNLASNRISIILPSLLPILSQQRTINLRQNPLDCTCSNIYFLEWYKENMQKLEDTEDTLCENPPLLRGVRLSDVTLSCSMAAVGIFFLIVFLLVFAILLIFAVKYFLRWKYQHI
Protein: Vesicular glutamate transporter 1 (VGluT1) (Brain-specific Na(+)-dependent inorganic phosphate cotransporter) (Solute carrier family 17 member 7) (Q3TXX4)
Organism: Mus musculus (Mouse)
Function: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter which transports preferentially L-glutamate but also phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, may function as a K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular glutamate uptake (By similarity). The vesicular K(+)/H(+) antiport activity is electroneutral (By similarity). At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic. Is necessary for synaptic signaling of visual-evoked responses from photoreceptors.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:16942593}. Cell membrane {ECO:0000305|PubMed:29642010}; Multi-pass membrane protein {ECO:0000305}. Synapse, synaptosome {ECO:0000269|PubMed:16595674}.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- Disks large homolog 4
- Vesicular acetylcholine transporter
- Synaptic vesicular amine transporter
- Synaptotagmin-1
- Vesicle-associated membrane protein 2
- Chromaffin granule amine transporter
- Vesicular glutamate transporter 2
- Glutamate decarboxylase 2
- Vesicular glutamate transporter 3
Sequence:
MEFRQEEFRKLAGRALGRLHRLLEKRQEGAETLELSADGRPVTTHTRDPPVVDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVSMVNNSTTHRGGHVVVQKAQFNWDPETVGLIHGSFFWGYIVTQIPGGFICQKFAANRVFGFAIVATSTLNMLIPSAARVHYGCVIFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTAFCGSYAGAVVAMPLAGVLVQYSGWSSVFYVYGSFGIFWYLFWLLVSYESPALHPSISEEERKYIEDAIGESAKLMNPVTKFNTPWRRFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFEISKVGLVSALPHLVMTIIVPIGGQIADFLRSRHIMSTTNVRKLMNCGGFGMEATLLLVVGYSHSKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPIIVGAMTKHKTREEWQYVFLIASLVHYGGVIFYGVFASGEKQPWAEPEEMSEEKCGFVGHDQLAGSDESEMEDEAEPPGAPPAPPPSYGATHSTVQPPRPPPPVRDY
Protein: Lactoperoxidase (LPO) (EC 1.11.1.7) (Lacrimal gland peroxidase) (Q8R481)
Organism: Mesocricetus auratus (Golden hamster)
Function: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:16469299}. Cytoplasm {ECO:0000250|UniProtKB:Q5SW46}. Note=Secreted by the lacrimal gland into tears. {ECO:0000269|PubMed:16469299}.
Interaction partners:
- Phospholipase A2
- Alpha-lactalbumin
- Tyrosinase
Sequence:
MKVLLRLPALLASLTLLQMAASTRNATRTATIRETVDEVKVQVNKAFLDSRDRLKTDMSNLAPTVRHLSGYLKQAKGRTRTAIRVGQVWEQSLKRLRRMVPLTNVTGQGLDLTSLSWEVGCGHPAPTVTCNISNPYRTITGDCNNRKNPELGSANRALARWLPAEYEDGLSLPFGWTPGKTRNGFPLPQPRDVSNQVLDYLNEEEILDQNRSLLFMQWGQIVDHDLDFAPETEMGSDNYSKAQCDELCIQGDNCFPIMFPKGDPKLKTQGKCLPFFRAGFVCPTSPYQSLAREQINALTSFMDASMVYGSEPSLANRLRNLSSPLGLMAVNEEVSDHGRPLLPFVNVKPSPCEVINRTAGVPCFLAGDSRASEQILLATSHTLFLREHNRLARELSRLNPQWDGEKLYQEARRIMGALIQIITFRDYLPILLGDELQKWIPPYQGYKETVDPRISNVFTFAFRFGHLEVPSTVSRLDENYQPWGSEPELPLHKLFFNTWRVVKDGGIDPLVRGLLAKKAKLAHQDKMMTGELRNMLFQPNHTVHGFDLAAINIQRCRDHGQPGYNSWRAFCGLSQPKTLEELSAVLRNEVLAKKLMDLYGTPDNIDIWLGAIAEPLVRRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGVFTEKQRDSLQKMSFSRLVCDNTGINKVPLNPFQPNSYPHSFVDCSAIEKLDLTPWASVKK
Protein: Transmembrane protein, putative (DUF1191) (Q5S4T6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNSKSLTCCVVFLLHTSLFSSTLQSSLIHLNSTTSILNVTLPHSLSQSLENFALKTLTTQHHTGALYRAILPENLSGIEVSVVRLTGKSLWNSGAKFSNVLIPERSVSVPPARRVVIVYQNLGNWSNHWYTVPGYRLITSVLGFKVLDVSDQDNVKEIILKMKNPVEVSFRDLPKERDEEMLSRVRCVSFKAQTKDEEATHISRMVIPGVCYGSSHGDYSVIEPLENDKKNVESWSTWWWLWIVGFVLGFGLLGFLCTMGIRVSRAKKIQVMMERDANDGEVFESRWFGGSKMPSAAVTRTLPELESGFERVS
Protein: Kl-2 protein (Q281W6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SELCVIRQTNTEHWYGYEYTGNSGRLVITPLTDRCYITLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIWVIVTNCSEGLDYKSIGKNFSGLAQSGCWGCFDEFNRINIEVLSVVAQQIMSIMAALSTKA
Protein: Regucalcin, isoform D (EC 3.1.1.17) (Q76NR6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
Sequence:
MMLLIPVIAVCLFGLTMSYKVEPLPDSYAGLGEGPHWDVARQSLYYVDLEAGSLLRYDYAQNKVYKTKIEGETLAGFVLPVEGRPQEFAVGCGRRVVIVNWDGVSPSAKVVRTLFEVQPLMEKNRLNDAKVDPRGRFFGGTMRYIGDEFEFRHGELYRWEAGGQVSVIKGDVGISNGLAWDEKAKKFYYIDTTDYEVKSYDYDFETGVASNPKVIFNLRKNSPKDHLLPDGLTIDTEGNLYVATFNGATIYKVNPNTGKILLEIKFPTKQITSAAFGGPNLDILYVTTAAKFDQPAPAGTTYKVTGLNATGYPGVNLKV
Protein: Chloroplast N receptor-interacting protein 1 (B2C7Y6)
Organism: Nicotiana benthamiana
Interaction partners:
Sequence:
MRILSLPSTSFSLVDCHIPKNLTYGNVSSVTLTPMARSQFQPQKRRNFGNSNRTPGFSWMATVGEKVQVSTVPTSVPVRVALELLQAGHRYLDVRTAEEFSDGHAPGAINIPYMFRIGSGMIKNPNFAEQVLEHFGKDDEIIVGCQLGKRSFMAATDLLAAGFSGVTDIAGGYAAWTENGLPTDS
Protein: FG-GAP repeat protein, putative intergrin alpha chain protein, putative (Q4GZ85)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MACSTKRDASDIRDGRTERRLPAIPLDAWAFRRMAPQGSITPSGLITADVDGDGVEEVIIGTTEGQLLLLKMGYRTPVYSRTIPATISVVLYSAKTLRLLLVTLEGQCEVIEGFITGSKTIACSSRGGSTTSSRKRDEDATAGVMGSEMCSGGSHSGVYSECLDKEYQPCGASYIFSIPPNCICGDIGVDEKSGEGNIVFLGSYDGHVYVYSVSPLGERLGLLFLHSHVSSIKSFIVPANGTALPPSRDDHLTCAESSSTTTASFTMETWRRCSLLLVCCSQRIVLLGASREEIMHWQGHHQPRTVSMVGYVCEGCAATSACMRPTDAVGSLTIGMETPLSDSSTSLNKTAPLEPKWQFPLYHLSKSNVHLPTEEGGRQVAPQEESTAELHAPWLLPWKYSQHQGSSNATVTTLEIQQCRHSYQRQHDSVASTSTTHDHGESSPKVNDADVIIRSPAAVDVATAPHAAQFAVATEDGRWFIFEMLLAGSSIGTASPGRIGDGPVEGSTSSFRGTVVCLMSGCVQDAGFVERVRVVNVGNDGFQAIFLSMDGTCYALDAHKNTVVTSRVKAGALSFTVMGCASENGEAGSPAGNTAAAAMRQNEALSSLAPCGFSLVSVAVDEVVVLSIGGESHEWTPPTGADGLVRDRGSSALQTRISTNEGGRGIHEGSEQSNRKLLDQTENDAPDEDAVMLKLGALLLKGSHNPGDVERFSEEYRRFVARKFCAFGLTQKEWRMLQQLGE
Protein: Meiotic fizzy-related protein 2 (Meiotically up-regulated gene 55 protein) (O94411)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mitotic spindle checkpoint component mad2
- Anaphase-promoting complex subunit 4
- Meiotically up-regulated gene 112 protein
- Meiotically up-regulated gene 133 protein
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit cut9
- G2/mitotic-specific cyclin cdc13
- Anaphase-promoting complex subunit 8
- Serine/threonine-protein kinase plo1
- Anaphase-promoting complex subunit 1
Sequence:
MIIKKKESFKSPGRLWRVTKIRKLTAAKKNELQNRKCNQASNEEKKILYKSNFLDRFIPSKANSDAFRIMENAFTEKLNTQESLLPDILNLNVKGVLHYKDNKKQKTTRLIESTNYQRQTIHGASSSLVIEVEENGHLSNMQGSLYETPLRILDAPGLLDDFYISPLAWSTNGELAVALAQNVYLWSEISGPSIMELSPTTYEVSSLAYSSDGGFLAIARVNGFVEIWNRKTKNNRCDYKFHHDGDISCMAWSPINWTLLVGGSTGNIYVYRRTKSMMRRVHTIKKVHQEQVCGLEWNYDGTQFASGGNDNLVCIFDIDSLENKKFYWIHLAAVKALAFCPWQKSLLAVGTGSNDQQIYFYDTFRGHRIHSLFCGAQVTSVIWSRRYKEFCYSLGYSPEGTNSSLIVYRWPQLTKVFDIPSAAIDGWGQDLRTIMAIHTHRKYSNNTWEEGEYVVVANSDETVKFYKIWGNEMQEIHNDRVLYREGIFGSHILEMLENIPEQVLTNGVR