wanglab/gogpt-training-data huggingface dataset:
Protein: PIN domain-like family protein (Q8L8C2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- KRR1 small subunit processome component
- Probable U3 small nucleolar RNA-associated protein 11
- F18K10.11 protein
- AT1G07840 protein
- U3 small nucleolar ribonucleoprotein protein IMP3
- WD repeat protein
- At5g11240
- Nucleolar-like protein
- At3g57000
- Protein NUCLEOLAR FACTOR 1
Sequence:
MRVKRQKKNRRTVRFFTVCYGFRQPYKVLCDGTFVHHLVTNEITPADTAVSELLGGPVKLFTTRCVIAELEKLGKDFAESLEAAQTLNTATCEHEEAKTADECLSEVIGVQNTEHFFLGTQDAEFRRKLQQESIVPLVFGLRNILLIDQPSDFQRQSAKDSENKRLTMTDTEKKLLVKRTAKIIASNRKEATIANEEWGMPRVVSTKNGLGVKDRPQFKRNRAKGPNPLSCMKKKKENPQSKSKADSNSNAQKEKKEGGSDTQKRSRKRSKKGKSGPERTE
Protein: Hgt8p (A0A1D8PG82)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Carbon catabolite-derepressing protein kinase
Sequence:
MSSTNSTENHAVEEKYEDPQQQQQQQQQQQQQQQQKDALAKKPMSAYIGISIMCVLIAFGGFVFGFDTGTISGFINMSDFLERFGGTRADGTLYFSNVRTGLLIGLFNVGCAIGALFLSKVGDMYGRRVGIMTAMIIYIVGIIVQIASQHAWYQVMIGRIITGLAVGTLSVLCPLFISEVSPKHLRGTLVCCFQLMITLGIFLGYCTTYGTKTYSDSRQWRIPLGLCFAWALCLLGGMVRMPESPRYLVGNDRIEDAKISLAKTNKVSPEDPALYRELQLIQAGVERERLAGSASWKSLITGKPRILERVFVGAMLQSLQQLTGDNYFFYYSTTIFKSVGLNDSFQTSIIIGVINFASTFVGIYAIEKLGRRHCLLIGSVAMSICFLIYSLIGTQHLYIDKPGGASRKPDGDAMIFITALYVFFFASTWAGGVYSIMSELYPLKVRSKAMGIASASNWLWGFLISFFTSFITDAIHFYYGFVFMGCLVFSIFFVYFMVYETKGLTLEEIDELYSTKVVPWKSAGWVPPSEEEMATSTGYAGDAKPTEEHV
Protein: GM06601p (Q95S77)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHLRNLFIGMFCLQRDFQQLLQCLENQISDVNKRKSAIQGLCHGEIPTSSKFPFKKEFRELENIDLPELREAIHDFQARLECMKSVNSEAISSYQGLQNEVKQLEEGIQESVNQAKSIESGMSNLYDKWEPKLNSLVETISTKFSEFMESIEYVGEVVLSKTDKVRT
Protein: DNA-directed RNA polymerase (EC 2.7.7.6) (Plastid-encoded RNA polymerase subunit alpha) (Q2LIP1)
Organism: Oryza punctata (Red rice)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
Sequence:
RVDSKRLYYGRFILSPLRKGQADTVGIALRRALLGETEGTCITHAKFGSVPHEYSTIAGIEESVQEILLNLKEIVLRSNLYGVRNASICVKGPRYITAQDIILPPSVEIVDTAQPIANLTEPEDFRIELRIKRDRGYHTEVRKNTQDGSYPIDAVSMPVRNVNYSIFSCGNGNAKYEILFLEIWTNGSLTPKEALYEASRNLIDLFLPFLHTEEEGTRFQENKNRFTSPLLSFQKRLTNLKKNKKRIPLNCIFIDQLELPSRTYNCLKRANIHTLLDLLSKTEEDLMRIDSFRMQDGKQIWDTLEKHLPMDLPKNKF
Protein: Contactin associated protein-like 3 (E9PY62)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MARVNGAFLDALLLLLLLSVQTLPLVAAGDPHNCDAPLASSLPQLSFSSSSQLSSSHGPGFARLNRRDGAGGWTPLVSNKYQWLQIDLGERMEVTAVATQGGYGSSDWVTSYLLMFSDGGRNWKQYHQEESISGFPGNTNADSVVQYSLQPSFHTRFLRFLPLTWNPKGRIGMRIEVYGCSYKSEVVYFDGQSSLLYKFDNGAIRPVREVISLKFKAMQNSGIIFHGKGQHGTHIVLELNKGKLVVYLNSGDGNLPPVNSIMNFTLGSLLDDRHWHSVLIELHNMHMNFTLDKYMHHVHVNKETSYLDLNFEISFGEILMPGGRFLTFPHKNFHGCLENIYYNGVNIIKLAKKHESQILIKGNVSFTCPQPQTIPVTFLSSGSYLALPSSLREDKMSLAFQLRTWNKAGHVFFSQVGHGSGSLVLFLKNGKLILNLSEPGQPLQSITTGAVLNDGLWHSVSVSAKGSYLSLLVDGDTAQTLMSVEIHLGDTYYFGGCPNNSSSFGCEHSFGGFQGCLRLISVGDKVVDPIAVQQGVLGSFSDLQIDSCGIIDRCLPSYCEHGSRCTQSWDTFSCDCEGTGYTGTTCHSSIYEQSCEAHRHRGSPSGLYYIDVDGSGPLAPFLVYCNMTADTAWTVVQHGGPDVVTVRGGPEGHMHSATFSYAANAAQLHAVVNVAEHCEQQVDLQCRTSGPSDTGDGTSLSWWVGRSNETYTYWGGSLPNPQKCTCGFEGNCIDSQYHCNCDADRNEWTSDTIVLSHKEHLPVTEMVVTDTGRPYSEAAYTLGPLLCQGDKSFWNSASFNTEASYLHFPTFRGELTADVHFLFKTTISSGVFMENLGITDFIRIELRAPTEVTFSFDVGNGPCELTIQSPTPFNDNRWHHVRAERNVKGASLQVDQLPQKTQSTPADGHVRLQLNSQLFIGGTASRQKGFLGCIRSLQVNGMALDLEERAVMTPGVEPGCSGHCSSYGHLCRNGGMCQEKHRGIACDCAFSAYDGPLCSYEISAYFETGSSVTYNFQEYSTLSANTSYLASSLHGDVILSRETITLSFRTTQTPCLLLYVTSFYEEYLSIILANNGSLQVRYKLDRHRNADAFNFDLRNLADGHFHQLTINREEAVVSVEVNQSTKRQVILSSGTEFNAVKSLVLGKVLEPLDADPETQQAAAQGFTGCLSSVRFGLEVPLKAALNQNRARVTIQGSVAAAAHCAEGPGSAERKLSPGPSMDAGHSGSAEDRQPLPNTDRSDPGVIGGITAVVIFILLCVSAIAIRVHQQRRLHQKNESTVSKTEEC
Protein: RE29468p (Uncharacterized protein, isoform D) (Uncharacterized protein, isoform F) (Q8SWS2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MATTAAGIQQQQVIGLGAAYDRQQSTDSGWDNPFRPGGDLSREADEIVNMIRGGKPITPTEERTIGNGSAQHADDNCNGGTAIGESVIKSNLSQNLATAQNGTNSHASATADAGAGKAATATELSGGTGNNGVTSLGQVSKQVVPGPTSASHVVIDEKKNKKKGCCVLQ
Protein: AP-4 complex subunit epsilon (AP-4 adaptor complex subunit epsilon) (Adaptor-related protein complex 4 subunit epsilon) (Epsilon subunit of AP-4) (Epsilon-adaptin) (Q8L7A9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of novel type of clathrin- or non-clathrin-associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000250}. Membrane, coated pit {ECO:0000250}. Note=Associated with the trans-Golgi network. {ECO:0000250}.
Interaction partners:
- Beta-adaptin-like protein C
- AP-1 complex subunit mu-2
- Beta-adaptin-like protein A
- Beta-adaptin-like protein B
- AP-4 complex subunit mu
- Clathrin heavy chain 2
- AP-4 complex subunit sigma
- AP-2 complex subunit mu
- AP3-complex subunit beta-A
- Clathrin heavy chain 1
Sequence:
MEQLKTIGRELAMGSQGGFGQSKEFLDLVKSIGEARSKAEEDRIVLSEVDILKRRLLEPDIPKRKMKEYIIRLVYIEMLGHDASFGYIYAVKMTHDDNLLLKRTGYLAVTLFLNEDHDLIILIVNTIQKDLRSDNYLVVCAALNAICRLINEETIPAVLPQVVELLNHQKEAVRKKAIMALHRFHRKSPSSVSHLVSNFRKRLCDNDPGVMGATLCPLFDLISEDVNSYKDLVSSFVSILKQVTERRLPKSYDYHQMPAPFIQIKLLKIMALLGSGDKNASDIMSMVLGDLFRKCDSSTNIGNAILYECIRCISCILPNPKLLEAAADAISKFLKSDSHNLKYMGIDGLGRLIKISPDIAEQHQLAVIDCLEDPDDTLKRKTFELLYKMTKSSNVEVIVDRMIDYMISINDNHYKTEIASRCVELAEQFAPSNQWFIQIMNKVFEHAGDLVNIKVAHNLMRLIAEGFGEDDDDADSKLRLSAVESYLQLISEPKLPSLFLQVISWVLGEYGTADGKYSASYISGKLCDVADAYSSDETVKGYAVSALMKIYAFEIASGRKVDVLPECQSLIEELLASHSTDLQQRAYELQALLALDARAVETILPLDASCEDIEVDKDLSFLNGYIQQAIESGAQPYISERERSGMFETTDYHPQDHHEVPTHALRFEAYELPKPSVPPQASNELVPVPEPSYYSESHQPISTSLVSERESSEIKLRLDGVKQKWGRPSYQSTTAASSTTPQAANGISTHSDAGVGSSSSKPRSSYEPKKPEIDPEKQRLAASLFGGSSSRTDKRSSSGGHKPAKGTANKTATVPKENQTPVQPPPDLLDFGEPTATTATAMDPFKELEGLMDSSSQDGGSSDVMGLYSDAAPVTTTTSVDSLLSELSDSSKGNSRTYQPQTSKGPNTKEALEKDALVRQMGVNPTSQNPTLFKDLLG
Protein: Peroxiredoxin TSA2 (Prx) (EC 1.11.1.24) (Cytoplasmic thiol peroxidase 2) (cTPx 2) (Thiol-specific antioxidant protein 2) (Thioredoxin peroxidase type Ib) (TPx type Ib) (Thioredoxin-dependent peroxiredoxin TSA2) (Q04120)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Can act alternatively as peroxidase and molecular chaperone. Oxidative stress and heat shock exposure cause a reversible shift of the protein structure from low MW species to high MW complexes, triggering a peroxidase-to-chaperone functional switch. The chaperone function of the protein enhances resistance to heat shock.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10681558}.
Interaction partners:
- Sulfiredoxin
- Peroxiredoxin TSA1
- Thioredoxin-2
- Peroxiredoxin AHP1
- Catalase T
- Peroxiredoxin DOT5
- Glutathione peroxidase-like peroxiredoxin 1
- Thioredoxin reductase 1
- Glutathione peroxidase-like peroxiredoxin HYR1
- Superoxide dismutase, mitochondrial
Sequence:
MVAEVQKQAPPFKKTAVVDGIFEEISLEKYKGKYVVLAFVPLAFSFVCPTEIVAFSDAAKKFEDQGAQVLFASTDSEYSLLAWTNLPRKDGGLGPVKVPLLADKNHSLSRDYGVLIEKEGIALRGLFIIDPKGIIRHITINDLSVGRNVNEALRLVEGFQWTDKNGTVLPCNWTPGAATIKPDVKDSKEYFKNANN
Protein: Beta-1,4-galactosyltransferase 2 (Beta-1,4-GalTase 2) (Beta4Gal-T2) (b4Gal-T2) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2) (O60909)
Organism: Homo sapiens (Human)
Function: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Trans cisternae of Golgi stack.
Interaction partners:
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
- Alpha-
- Beta-galactoside alpha-2,6-sialyltransferase 2
- Beta-galactoside alpha-2,6-sialyltransferase 1
- Beta-1,3-galactosyltransferase 1
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4
- Beta-1,3-galactosyltransferase 5
- Type 2 lactosamine alpha-2,3-sialyltransferase
Sequence:
MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASSSSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLERVQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYVINQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIAMDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPDIRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITVDIGRPPSWPPRG
Protein: Ninjurin-B (dNINJ-B) (Q9VVT9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Homophilic transmembrane adhesion molecule that mediates cell adhesion (By similarity). Able to mediate plasma membrane rupture (cytolysis), leading to release intracellular molecules that propagate the inflammatory response.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDSGEVKISLEDSPSSGESFASTTSGPCCGSGRDLDIQVHESHIKDDQFPSRATSELQESKKSNKKCSSDLSTENSYAANKNVAEGLMDIALLSANANQLRFLITYNDKASTYIYSMIMVILSLVLQLLVGIMLIFKRRLKRFRNRSYERTNDLLVMGVFMITVINILLAAFTTTDGGGSH
Protein: Neurexin 1, isoform G (A0A0B4KH61)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKAPHSATYQDNYADAAMTARTRPSMDMDQQRNRNQAELRLLPAQRTSTSAFESPDLRFNKARRRRRSEQVPPVVVEYRRSYRVLIVSALLVSLAASFVTLSAGFQLDGSQNSFYTFRKWYTGLNGTLELEFKTEQPNGLVLYTDDGGTYDFFELKLVEGALRLRYNLGGGAQIITVGRELHDGHWHKVQVLRNDEQTSLIVDGVSQQRSTKGKEFQFGKFASNSDVYVGGMPNWYSSKLALLALPSVIFEPRFRGAIRNLVYADQPGGSTRRQEIKQQRDIKCGDVPCDHGELPARERPLRGVRGGNTTDACERNDPCQHGGICISTDSGPICECRNLEYDGQYCEKEKAPSEATFRGTQFLSYDLGQTGAEPIVSAQDAISFYFRTRQPNGLLFYTGHGTDYLNLALRDGGVSLTMGLANGKQEMHIKPSKVRFDDHQWHKVTVHRRIQEISSITSFCRLVTVVDDVYTDHSHIAGKFTMLSSSRVYVGGAVNPRALLGARVHTNFVGCLRKVEFSADTLNLNLIDLAKSGSKLIQVAGNLEYQCPSGDPQDPVTFTTRESHLVLPPWETGKQSSISFKFRTKEPNGIIVLATGSKQPRAKNPVLIAIELLNGHIYIHLDLGSGASKVRASRRRVDDGDWHDLILRRNGRDAKVSVDGVWNDFRTPGDGTILELDGHMYLGGVGPAYNSVSWPAAIWTATLRQGFVGCLRDLVLSGKAIDIAAFARVQDSASVKPSCHVQANVCNGNPCLNGGTCLEGWNRPICDCSATLYGGPTCGRELATLAFNGSQHMTIWLGNGQGTKTQTEELVIRFKTSRPAGLLLLTSAESNSPDRLEIALVAGRVRASVRLSDREKNLLAGQSVLNDNNWHTIRFSRRASNLRLQVDGAPPVRGMLSETILGRHSTMEIRSVHLGGLFHAEEEIQMTSTMPNFVGQMQGLVFNGQRYLDIVKSLGPELSALPSATFKLTARFVNSPAGQPYHAATFRSKHSYVGLAMLKAYNSISIDFRFKTVEPNGLLVFNGGRRNDFVAVELVNGHIHYTFDLGDGPVTMRDKSRIHMNDNRWHQVSIRRPGPKTHTLTVDDSFEIISLTGNNMHLELAGILYIGGVFKDMYSKLPASISSRSGFEGCLASLDLGDASPSLTSDAVVPSSLVVSGCEGPTKCSQNACANRGNCVQQWNAYACECDMTSYTGPTCYDESIAYEFGNNKGMVQYTFPENAQADTEEDNIALGFITTRPDAVLLRVESATTQDYMELEIVEGNIFMVYNIGSVDLPLGEIGTKVNDNAYHVVRFQRKGGNATLQLDDYNVQALTPQSHHSTVFNTMSNVQVGGKFSRNGRNRIERPFAGVIAGLSVNKLRILDLAVERDPHITIRGDVQLVTGVLDRNDLQRMQQTPASGYPGALDDLIFSGAGSGCRGDDEDECTPPFESGSGDDLITPVYVPPTKQTTTSQQGNSLSTGGSSSGGVITNGTERACDDEDCVHGSGDYGETTEQFTSTSTARGSECEIAFIFLTVIAPWILCKFP
Protein: 26S proteasome non-ATPase regulatory subunit 2 (Q9GZH5)
Organism: Caenorhabditis elegans
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 14
- Probable 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 3
- Probable 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 7
- 26S protease regulatory subunit 6A
Sequence:
MVATTQQTPKEADKKKADDKKVPEKAEPKKEEMSEEDQKLEEDLNLLVQRLSEPDTTLYKPSLETMRTLIRASTTSMTSVPKPLKFMRPHYNKMKEIFTSIVAPDVKKLCADIISVLAMTSDERTDTINYRILGSHEPIGDWGHEYVRHLAMEMSEEWKKEGTSDARKAELLKLTQDIVSHHMKHNAEVEACDLLIEIERIDLLISYVQEVDHQRVCLYLLSCAPLTPDPDNIILIRTALQLYLKFNRYLEAVRCAIMVNDIPQVHQIFAKASDPLLRKQMAILLGRHQIFLDYEGSADSDALAELNSNAHLYEYFHSLARELDIMEPKTPEGIYKSHLEHSRPFGNSAQPDSTRMNLAAALVNGFVNCGFGVDKMMAETEEASRWFYKNKEYGMLTAAASQGLIWRWDIDTGLAQCDRFLYINDDYIKAGTLLAIGIISSGIQDACDPASALLLDHVQSDRSIMRVGSILGLGLAYANSKRETVTKNEERGVIFELKKVLSDQKPSAIPEVKGLAGLSLGLILVGTADAEAAMEMLQALMDKSETELTDPNMRFLALGIALIFLQTQDKSDVFVESLRSLPDPFGAMVSTLVEVCAYAGTGNVLKIQKLLHLCSEHYETPAAEKKTAASRGPRGPAPAAATPARPAAQPGNVNVAGTPAPTGTPAVAPAAPRRDLPGAASAATPGAPETAAADATPAPPAKPDLSSQQAVAVLGIGLIAMGDDIGSQMALRMFGHLIRYGEPVIRRAVPLALSLLSVSNPQLNILETLSKFSHDSDADTAHNAIFAMGLVGAGTNNARLVAMLRNLASYHYKDQVSLMLVRIAQGLTHLGKGTMTLNPWHSDRQLLSPSALASLLSICFSFLDANNTILNNRQHYLLYTLVLAMQPRMLTTLVEDEMKPGSLKQLNVSVRVGQAVDVVAQAGKPKTITGFQTHTTPVLLAHGERAELANDEYLSVTPHLEGLVILKKNPDYQPVVVSTKK
Protein: Interleukin-5 receptor subunit alpha (IL-5 receptor subunit alpha) (IL-5R subunit alpha) (IL-5R-alpha) (IL-5RA) (CD antigen CD125) (P21183)
Organism: Mus musculus (Mouse)
Function: Cell surface receptor that plays an important role in the survival, differentiation, and chemotaxis of eosinophils. Acts by forming an heterodimeric receptor with CSF2RB subunit and subsequently binding to interleukin-5. In unstimulated conditions, interacts constitutively with JAK2. Heterodimeric receptor activation leads to JAK2 stimulation and subsequent activation of the JAK-STAT pathway.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-5
- Cytokine receptor common subunit beta
- Interleukin-3
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-3 receptor class 2 subunit beta
- Interleukin-4
- Tyrosine-protein kinase JAK2
- Interleukin-13
- Thymic stromal lymphopoietin
- Interleukin-2 receptor subunit beta
Sequence:
MVPVLLILVGALATLQADLLNHKKFLLLPPVNFTIKATGLAQVLLHWDPNPDQEQRHVDLEYHVKINAPQEDEYDTRKTESKCVTPLHEGFAASVRTILKSSHTTLASSWVSAELKAPPGSPGTSVTNLTCTTHTVVSSHTHLRPYQVSLRCTWLVGKDAPEDTQYFLYYRFGVLTEKCQEYSRDALNRNTACWFPRTFINSKGFEQLAVHINGSSKRAAIKPFDQLFSPLAIDQVNPPRNVTVEIESNSLYIQWEKPLSAFPDHCFNYELKIYNTKNGHIQKEKLIANKFISKIDDVSTYSIQVRAAVSSPCRMPGRWGEWSQPIYVGKERKSLVEWHLIVLPTAACFVLLIFSLICRVCHLWTRLFPPVPAPKSNIKDLPVVTEYEKPSNETKIEVVHCVEEVGFEVMGNSTF
Protein: Triacylglyceride transporter Rv1410c (MFS-type drug efflux transporter P55) (P9WJY3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: In association with lipoprotein LprG probably transports triacylglycerides (TAG) across the inner cell membrane into the periplasm; TAG probably regulates lipid metabolism and growth regulation. Confers resistance to ethidium bromide, possibly acting as an efflux pump, requires LprG lipoprotein for normal function. With LprG maintains cell wall permeability. Probably required with LprG for normal surface localization of LAM. Overexpression of LprG and Rv1410c leads to increased levels of TAG in the culture medium.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:26751071}; Multi-pass membrane protein {ECO:0000250|UniProtKB:K5B8L6}.
Interaction partners:
- Lipoarabinomannan carrier protein LprG
- Riboflavin synthase
Sequence:
MRAGRRVAISAGSLAVLLGALDTYVVVTIMRDIMNSVGIPINQLHRITWIVTMYLLGYIAAMPLLGRASDRFGRKLMLQVSLAGFIIGSVVTALAGHFGDFHMLIAGRTIQGVASGALLPITLALGADLWSQRNRAGVLGGIGAAQELGSVLGPLYGIFIVWLLHDWRDVFWINVPLTAIAMVMIHFSLPSHDRSTEPERVDLVGGLLLALALGLAVIGLYNPNPDGKHVLPDYGAPLLVGALVAAVAFFGWERFARTRLIDPAGVHFRPFLSALGASVAAGAALMVTLVDVELFGQGVLQMDQAQAAGMLLWFLIALPIGAVTGGWIATRAGDRAVAFAGLLIAAYGYWLISHWPVDLLADRHNILGLFTVPAMHTDLVVAGLGLGLVIGPLSSATLRVVPSAQHGIASAAVVVARMTGMLIGVAALSAWGLYRFNQILAGLSAAIPPNASLLERAAAIGARYQQAFALMYGEIFTITAIVCVFGAVLGLLISGRKEHADEPEVQEQPTLAPQVEPL
Protein: Popeye domain-containing protein 1 (Popeye protein 1) (Blood vessel epicardial substance) (BVES) (hBVES) (Q5PQZ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Involved in skeletal muscle and heart development as well as in the maintenance of heart function. May play a role in vamp3-mediated vesicular transport and recycling of receptor molecules. Involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells. May induce primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. May be involved in epithelial movement during corneal sheet formation and regeneration. May play a role in the regulation of cell shape and movement by modulating the Rho-GTPase activity. May also be involved in striated muscle regeneration and in the regulation of cell spreading (By similarity).
Subcellular location: Lateral cell membrane {ECO:0000250|UniProtKB:Q8NE79}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8NE79}. Membrane {ECO:0000269|PubMed:26642364}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000269|PubMed:26642364}. Membrane, caveola {ECO:0000250|UniProtKB:Q9ES83}. Note=Detected at points of cell-cell contact in confluent epithelial sheets. Colocalizes with components of the adherens and tight junctions (By similarity). {ECO:0000250|UniProtKB:Q9ES83}.
Interaction partners:
- Tight junction protein 1a
- Potassium channel subfamily K member 2 isoform X1
- Potassium channel subfamily K member 2b
- Vesicle-associated membrane protein 3
- Caveolin
- NDRG family member 4
Sequence:
MSNTTSALPSSVPAVSLDPNATLCQDWEQSHHLLFHLANLSLGLGFLIPTTLALHMIFLRLLLMTGCSLFIAWATLYRCTLDVMVWNVVFLLVNFMHFFFLLYKRRPIKIDRELKSVYKRMFEPLHVREALFQRLTGQFCTIQTLKKGQVYAAEDKTSVDERLSILLKGKMKVSYRGHFLHNIYTNAFIDSPEFRSTQMNRGERFQVTIAAEENCKLLCWSRERLTYFLESESFLNEVFRYLIGKDITNKLYSLNDPTLSDKAVKKMDRQPSLCSQLSMMQMRNSMASTSDTDDVLNQILRGGSTGSSLQKNPLTKTSTTMKPIEEGLEDDVFESESPTTSQNVSKTTKKDI
Protein: Big defensin (AiBD) (Q0H293)
Organism: Argopecten irradians (Bay scallop) (Aequipecten irradians)
Function: Significantly inhibits the growth of Gram-negative and Gram-positive bacteria and fungi in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:16597463}.
Interaction partners:
Sequence:
MTRPSLVRCYSLFFTALIVMAIICPAWSEEIPKSRKKRAIPIAYVGMAVAPQVFRWLVRAYGAAAVTAAGVTLRRVINRSRSNDNHSCYGNRGWCRSSCRSYEREYRGGNLGVCGSYKCCVT
Protein: Large ribosomal subunit protein bL28m (39S ribosomal protein L28, mitochondrial) (L28mt) (MRP-L28) (Melanoma antigen p15) (Melanoma-associated antigen recognized by T-lymphocytes) (Q13084)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein mL64
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL37
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL38
- Large ribosomal subunit protein mL66
- Large ribosomal subunit protein uL3m
Sequence:
MPLHKYPVWLWKRLQLREGICSRLPGHYLRSLEEERTPTPVHYRPHGAKFKINPKNGQRERVEDVPIPIYFPPESQRGLWGGEGWILGQIYANNDKLSKRLKKVWKPQLFEREFYSEILDKKFTVTVTMRTLDLIDEAYGLDFYILKTPKEDLCSKFGMDLKRGMLLRLARQDPQLHPEDPERRAAIYDKYKEFAIPEEEAEWVGLTLEEAIEKQRLLEEKDPVPLFKIYVAELIQQLQQQALSEPAVVQKRASGQ
Protein: Proto-oncogene c-Rel (Q04864)
Organism: Homo sapiens (Human)
Function: Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- NF-kappa-B inhibitor alpha
- NF-kappa-B inhibitor epsilon
- NF-kappa-B inhibitor beta
- Nuclear factor NF-kappa-B p100 subunit
- Transcription factor p65
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor RelB
- Tumor necrosis factor receptor superfamily member 5
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Serine/threonine-protein kinase TBK1
Sequence:
MASGAYNPYIEIIEQPRQRGMRFRYKCEGRSAGSIPGEHSTDNNRTYPSIQIMNYYGKGKVRITLVTKNDPYKPHPHDLVGKDCRDGYYEAEFGQERRPLFFQNLGIRCVKKKEVKEAIITRIKAGINPFNVPEKQLNDIEDCDLNVVRLCFQVFLPDEHGNLTTALPPVVSNPIYDNRAPNTAELRICRVNKNCGSVRGGDEIFLLCDKVQKDDIEVRFVLNDWEAKGIFSQADVHRQVAIVFKTPPYCKAITEPVTVKMQLRRPSDQEVSESMDFRYLPDEKDTYGNKAKKQKTTLLFQKLCQDHVETGFRHVDQDGLELLTSGDPPTLASQSAGITVNFPERPRPGLLGSIGEGRYFKKEPNLFSHDAVVREMPTGVSSQAESYYPSPGPISSGLSHHASMAPLPSSSWSSVAHPTPRSGNTNPLSSFSTRTLPSNSQGIPPFLRIPVGNDLNASNACIYNNADDIVGMEASSMPSADLYGISDPNMLSNCSVNMMTTSSDSMGETDNPRLLSMNLENPSCNSVLDPRDLRQLHQMSSSSMSAGANSNTTVFVSQSDAFEGSDFSCADNSMINESGPSNSTNPNSHGFVQDSQYSGIGSMQNEQLSDSFPYEFFQV
Protein: Anoctamin (A0A8I6ASC3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU280814}.
Interaction partners:
Sequence:
MVLENFDQTIVCSTFGSLESQEDFRTPEFEEFNGKPDSLFFTDGQRRIDFVLVYEDESKKENNKKGTNEKQKRKRQAYESNLISHGLQLEATRSVSDDKLVFVKVHAPWEVLCTYAEIMHIKLPLKPNDLKTRSTFDTFNWFTKVLRVNESVIKPEQEFFTAPFEKSRMNDFYILDRDSFFNPATRSRIVYFILSRVKYQVMNNVNKFGINRLVSSGIYKAAFPLHDCKFNYKSEDPNCPSERYLLYREWAHPRSIYKKQPLDLIRKYYGEKIGIYFAWLGYYTQMLLLAAVVGVACFLYGYLNQDNCTWSKEVCDPDIGGQILMCPQCDRLCPFWRLNITCESSKKLCIFDSFGTLIFAVFMGVWVTLFLEFWKRRQAELEYEWDTVELQQEEQPRPEYEAQCNHVVINEITQEEERIPFTTCGKCIRITLCASAVFFWILLIIASVIGIIVYRLSVFIVFSTTLPKNPNGTDPIQKYLTPQMATSITASIISFIIIMILNTIYEKVAIMITNFELPRTQTDYENSLTMKMFLFQFVNYYSSCFYIAFFKGKFVGYPGDPVYWLGKYRNEECDPGGCLLELTTQLTIIMGGKAIWNNIQEVLLPWVMNLIGRYKRVSGSEKITPRWEQDYHLQPMGRLGLFYEYLEMIIQFGFVTLFVASFPLAPLLALVNNILEIRVDAWKLTTQFRRMVPEKAQDIGAWQPIMQGIAILAVVTNAMIIAFTSDMIPRLVYYWSFSIPPYGDHTYYTMDGYINNTLSVFNITDFKNTDKENPYIGLGNYTLCRYRDFRNPPGHPQEYKHNIYYWHVIAAKLAFIIVMEHVIYSVKFFISYAIPDVSKITKSKIKREKYLTQKLLHESHLKDLTKNMGLIAERIGGVADSSVRPKLE