wanglab/gogpt-training-data huggingface dataset:
Protein: AT14088p (Q8MR81)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSTNKLEKKDPRRHIPLQLNVFLRNDDDGEVREVTQNANTSSIGTIPSNGLVESDVTPIMTPTPKAGVYKPNVNVWRLSKEVTKPDRSFVVSAEEYPDLGQRPKRFKQRTPRVRNQDDGGTVSCLASRFSRVKDPPVLGNFLPDFMLPKSSNSNHQSVTTWLSSVRPSDSQKSLSDQARCSSSTNITLLSKDSVQPLTPKSSAQFSPGEKNIQQEQNTPAKSQQEETSPANSVEHQQKTPNSPKEQQKSSVGFTNMQQMASANSLQQQNSSASSLQQQNSSVHSLQKRKSWVNSSQQQRSSVNFIQKQRSWVNSSHHQKSSASSLQQKSSENSPSKFQQQQQKSPANNERSQNNQKSPGIQHSWKQQQQQKPKILQNCPKTSVQQQMNPVNHTQSQSERPTELIYLHSRSPAKRASVTNNSSAPIRIAPRQQTTQSSGPSVVHNEDEDVMPPTPNQSERRQRRFPRRNHNPRMVRSLQAVSREFTESLLEGSSGKTPEKEVVPYQQQEKPRQVKSSPEIHASSHMRKLAMGSVLNSNAKEFHPTGESHLTHKVSRLSQRRCRQRFTRSLHAKKNNPREQLPYPDSAPEPILEYTSEIDDQPCPPRQTVDTPIEAIVPPAMIEVSATGNLPPVFYFDQQSGIIWSNSSPQIPVEIQSNSVSQSVFRLASLPCTGVGTTNMDIFTSSPPPIQHMSSSRLPSSISGPTQLSHTLSSPPVENQHQQHLWESCIHQDEDLMYSRPLLDMDQEETQPEQQDQEWQWESEIEPPSFQSENQVVADAHGEENAYLAKDAGPPLERHMIFRAPSQHGQEYPKPDLNCVPSSIKKLHHLISSQYSDYSFVYALSAQISQDCVPMDCFVYLKMILLASIVSIESDEVRAPISLCIIATDSLMANRLLNKVGQLAPRFLGPHEYGLQPTFNALPTRFNWIVASPLLLAQQGVYYAGDWNRLSKDQGCQLEKCIENGAVPVPQLHIDQPLKAAVWTYWQPNNSTNQTLALAKLCPIFGLPIYMGAQASNSLWNSIIQKHNAEGQIVVNDGLSIPEDDMRMLIHLLHQRKTTLTDGAQHMLQKYYVISRKERPNVFSSKTYIVLKQLAECFAKLALRLEVLESDVCVAIFHCEHFVQGIFGAKENQAPPAVFNFNVISCIDPYMNKFTRWLLQYLNSYEDEELGMHADKRRRTDSWDMP
Protein: AT4g08810/T32A17_120 (Calcium binding protein involved in cryptochrome and phytochrome coaction) (Calcium ion binding protein) (Q9LE45)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKESDLTTEPIAQNLIKLISNVCFSVFVFTVLIFTVIAVTYQPPDPWLESAPALTKLLTETENATFKIDGSILKTGEDLASSPSSSPPSNSTEQVTEATIEKSEAKIGNMTVKNSIDCDEDLKIVNCSDPRVLVAVERFNLKVFKSIVFLEYETPVNGSKLDECDVSWRFRNKKEKSWRRYRDFRRFRFGFGENCTYKVFHTSGWHSGVNARRPRISRPSSSRGARGGDSEINDTIPTLGSQTSFRRGKYLYYSRGGDYCKGMNQYMWSFLCGLGEAMYLNRTFVMDLSLCLSSSYSSKGKDEEGKDFRYYFDFEHLKETASIVEEGEFLRDWKKWNRLHKRKVPVRKVKTHRVSPLQLSKDKSTIIWRQFDTPEPENYWYRVCEGQASKYVERPWHALWKSKRLMNIVSEISGKMDWDFDAVHVVRGEKAKNKKLWPHLDADTWPDAILTKLKGLVQVWRNLYVATNEPFYNYFDKLRSQYKVHLLDDYSYLWGNKSEWYNETSLLNNGKPVEFDGYMRVAVDTEVFYRGKTRVETFYNLTTDCKDGINTC
Protein: Probable serine/threonine-protein kinase IKS1 (EC 2.7.11.1) (IRA1 kinase suppressor 1) (P47042)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Probable serine/threonine-protein kinase KKQ8
Sequence:
MSLVPYEEGSLILDDPNSKSVVVVNPTSGTLSFFQQDNSNNDSELNEDQTASLSALDFPSGIHQYKSPIASYVCPQCGTEINPDIINRRQLHRRASAGVESESSRLSIPENTVPLGFEFANSSFSRRYFQSLERNHRHYALQNDSNNKQGQFSKNKYFIPDDLFIPGYFRKFFKILSLLGNGARGSVYKVVHTIGNTELGVFALKKIPIGNDMEWFNKCIREVKALSSLTHKSANLITYNHVWLEMDSSVGFVRSIDGSQSDSQEEVPCIFILQQYCSGGNLEDCILRKVFNRFSDTESPEERKKKFRTRKKNHGKSGEVGLSTEQLVSIIRDIARGLHELHSIGLIHRDLKPSNCLLLTPFKSDNENDNVYDREHNSDEFFPSIVIGDLGESQLEGESRLGTGCTGTLEFTAPDLIIQGRPVSSSTLPSRSSHTYNEYTFASDMYSLGMICYFIVFGELPFEPQLDIVDLKVRIKNFRFDTEGMIEKHQAMKLKPIDRRIFHLMDALLQPNNDARPTAKTVEETLDEMLINSKPGKKFWKENVDSTLNFSTISEVNENTNSFTDDYIDGDNVTLSLPAPEENLSTVSTQNLQKYSALNRTIQVCYKLVSMILTIIIFKCTKTGSWLSYMSLILLGMVFKSPADERGKHARALVLLAFIAACKKYIY
Protein: Outer membrane exporter of proteases (E0SC31)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004442}.
Interaction partners:
- Membrane fusion protein
- Alkaline protease secretion ATP-binding protein aprD
- serralysin
- serralysin
- serralysin
- Alkaline proteinase inhibitor
- serralysin
- Pyoverdine export ATP-binding/permease protein PvdT
Sequence:
MRRKAVLLTVVLSLSCGSAQAMGLLDAWELALRNDAQLRAAGFERDAGQEEVAIGRAGLLPSLQYTYGANYSHSKVTQRDRTLNNTTKRDYDNYVSTLTLRQPLLDYAAWARYQQGVTRKLMADQRFRDRSQDLMVRLYQSWSEALLAQEKLMLLDAQRRAYQEQLALNRRLLAAGEGTQTDLRETEARYTVTEAQRIEQEDTLDAAMTDLENMMGSPLQIQDLSPLALDTLPDNVTENRSLSQWRELTVRHNAKLAVQRENVDYSRYEIERNRAGHLPTLDLVASTRNSLSESEYNYNQKYDTQTVGLQVRVPLYSGGAVSASMRQAAAEYQQSQAELDNQTRQTFAELRRQFNLCANGAAKIRAWQMSVAAAEEAIRATRQSVAGGERINLDVLMAEQEWYNARRELTEVKYRWLQAWLNLRYTAGTLNEQDMMQLAAWFQSAPVINKTGINKTGINAATGNKTN
Protein: LD38671p (Q960R8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MYHPMGTIHDGWGNYSVSVKCSWLIDARHPHWNRRHNTNPSRTANIRIHLREFATECGWDHLYIYDGDSVDSPLLAVFSGLMYRGNFSIRRVPQVIATSGTALVHFFSDDAYNMSGFNLTYKMNSCPSDSDEVECSGHGKCRDGDCICDPMYRGEACNIAACPNNCFESKNQGHCRLDQERCSCYEGFAGDDCSQISAHGAWSTVHPKHSPAPAGSASHGATIWRDTLHIVGGESYGRGKLMSTYDFNGNVWETVHPEDGSEVPDKRYGASTVMYGDKIFMYGGVVKGHGISNELWAFDVSARTWANISVRADPSCNATGGTTAMCGPLHVVGHTATLVPGYGDKNNYQYMVVIFGHSPNYGYLNTVQEFNFASREWRIVPTTGYVVKGGYGHSAAYDFLTEKVYVYGGIVSESESSQVLSSRLYAYEPATRVWSLLSAAPSARLLHTANFVNQGLMMVFGGNTHNDTSQSYGAKCYSQDLLVYDVYCDSWHYHPMPGHLQADLARFGHSSVVFEESLYIYGGFNGQLLNDMLRYQPGYCSYYTKQEKCTAARPGVKCIWDVQKMRCIAITQVQRSAIYGREQYDYVACPSKSRLTLTSELLHDVHRCQELASCQSCVSTAFGCTYCGNGVCSKERCRETTSMASVFFESSTQMAVSTASPPLNAKHLDSCPISEEYLVSSVCDQLHNCRACSANLACRWDSEHNRCKSYTSYGGLALNRTQDEVACSPSCASLTNCQNCTEDECIWCQNEQRCVDRNAYTASFPYGQCREWTTFTAKCRSAPIQSTALAVGSTTALSSAQCGYYNSCQMCLDDPACGWCDNGSNTGLGRCVVGGALAPYDDTECALKHWFFTSCPRCNCNGHSYCNDQQHCEQPCNNLTTGAHCEKCRTGYWGNPINGGKCQRCDCNGQGVYCHPDTGKCFCTTKGIVGDHCEKCDSQNHYHGDPLKGSCYYELTIDYQFTFNLSKKEDRHFTQINFRNSPGKPEIDADFTITCSVPAKMDISVKRAGSPDMLILVGVNCSTFRHRFPKTDYQFGHSPDDNSSLTTFYVFVHDFQPPIWIQIAFSQYPKLNLQQFFITFSSCFLLLLLMAAVLWKIKQKYDMFRRRQRLFVEMEQMASRPFSQVLVDIENRESIDLSLTLEGIGHLSKKRKKECPSPIALEPCSGNRAAVLSLLVRLPTGGLSQAPSGQSAGLAVASALVTLGNPRRPSIDQHPKEPKSKRKQSQHPDSCT
Protein: Protein NETWORKED 1A (Q9LUI2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant-specific actin binding protein. Associates with F-actin at the plasma membrane and plasmodesmata. May be part of a membrane-cytoskeletal adapter complex.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22840520}. Cell membrane {ECO:0000269|PubMed:22840520}. Cell junction, plasmodesma {ECO:0000269|PubMed:22840520}. Note=Localizes to the cell cortex and shows polar enrichment at the apical and basal cell boundaries. {ECO:0000269|PubMed:22840520}.
Interaction partners:
- Vesicle-associated protein 1-1
- Large ribosomal subunit protein uL18c
- COP1-interactive protein 1
Sequence:
MATVLHSESRRLYSWWWDSHIPKNSKWIQQNLSDMDSKVKAMIKLIEEDADSFARRAEMYYKKRPELMKLVEEFYRAYRALAERYDHATVELCHAHKTMAEAFPNQVPFDMIEDSASSSCSEPRTPEKMPPGIQPFYDSDSATSKRGLSQLTEYLGNSETEVESLKRTLVELGAEKEALNLQYQLSLNKFSRLEKDLEVAQKDVSGLDERASKAEIETKILAEALAKLEAERDAALLRYNESMQKITELEESFSHAQEDVKGLTNRATKAETEVENLKQAHSRLHSEKEAGLAEYNRCLEMISNLEKKVRDAEENAQNFSNQSAKAEDEIKALRHELVKVNEVKDGLRLRYQQCLETISKLEREVSHAQDNAKRLSSEVLAGAAKLKTVEDQCTLLESSNETLKLEADGLTHKLAAKDQEIFQKQNELEKFQSLIEDEHSRYLEIEVSLKTLQSLYSQSQEEQKVITSELQSRIGMLRDLETRNLKLEGDISSVKEENQNLSELNDSSMIFLETQKCEISSLKEIKEKLEEEVARHINQSSAFQEEIRRLKDEIDSLNKRYQAIMEQVNLAGLDPKSLACSVRKLQDENSKLTELCNHQSDDKDALTEKLRELDNILRKNVCLEKLLLESNTKLDGSREKTKDLQERCESLRGEKYEFIAERANLLSQLQIMTENMQKLLEKNSLLETSLSGANIELQCVKEKSKCFEEFFQLLKNDKAELIKERESLISQLNAVKEKLGVLEKKFTELEGKYADLQREKQFKNLQVEELRVSLATEKQERASYERSTDTRLADLQNNVSFLREECRSRKKEFEEELDRAVNAQVEIFILQKFIEDLEQKNFSLLIECQKYAEASSFSEKLIAELESENLEQQMEAEFLVHEIDNFRGAICQVFKALQVEADCKTADQKIAKERIPVSRVLGEINELKCSLSSAEYETQRLVIENSVLLSLLGQFQSDGMKLESEKRDVEKDLETIVHHYGMLKKDRLELLEMNRQLKSELIDREQRELELKAELQTEHLKFENLHESYMALHQDYSDALGKNKSLHLKFSELKGEICILEEENGAILEEAIALNNVSVVYQSLGSEKAEQAEAFAKNLNSLQNINSGLKQKVETLEEILKGKEVDSQELNSKLEKLQESLEEANELNDLLEHQILVKEETLRQKAIELLEAEEMLKATHNANAELCEAVEELRKDCKESRKLKGNLEKRNSELCDLAGRQDEEIKILSNLKENLESEVKLLHKEIQEHRVREEFLSSELQEKSNEFGLWDAEATSFYFDLQISAVREVLLENKVQELTGVCENLKDEAVTKTTEINQIKETVGFLEFEVSELKTQLSAYDPVVASLAEDVRSLEQNALSLMKLPVPAGRRREGVQNDEHQEAAVSQEPVGHCSTNLDNGIVLLQDMKTRIKTIKQAVAEEKKRRGKLRRRSSSHRSKDRKLFEEIELEDQFSGEIRQPRSPAMTESKNGSLMKDIPLDQVADTTSYGRSRRTSRGSSDQMLELWEEAAEPESSIKFLINNKNSKKPLIPRLHRRSRNPSVESQSEKMVGVVDKLELSRSTEDNAKILERLLSDSRRLASLRISLRDLKSKLEINEKPGKFTNPDFARVRKQMKEMEEAIFQLANTNEILSNEIEETGDVRDIYRKVVMEKSRIGSEKIEQMQQEMQNIERTVLKLEEGATKSKGRRKFSESRTVILLRDIIHKGGKRTARKKKNRFCGCMRSSGNEE
Protein: UPF0183 family protein (Q55AH8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MFLKLELVPGKSLGDFILGMSISEALNIVKHNNVQINTVQIIFNDNDPLSLDIVIKLVDDGVLLRFEPKSQRLKVIEIFDVKKLSLSYRGSIFNQEDHTATFVDIYSKFGPSYPGDFNLEKSIYHLHYPGLSFSFRIPTAFKSLYQSSTELPVELPDGSTPLVEKIFVYSGLQMKTPLPVIPIHNEEILVCPNEGVYFSKRNCILTFNSTTQDVLSELGPPSKIYHKEEDNMKIHTNVEGSVAQDYFYNYFHFGIDILFDIKKNTIKKFILHTNFPTHYEFNLYTKCSFKIISDLQTPNSSSIIFNTIKRHLSGKPINNLTITQSNISQKKELNSILPSDAKNNNNNNNNNNNNNNNNNNNNNYNEFHLETDINYVHPDQKWEEVQKIFGKCGKPVVNNRGSISNPFGSTYFYGYSGIIFEIMKNNYIASVCLFNDIESNNNNFNNNNNFNNNNNNNNNNNNNNNNNNNNNNNNNNNNIFNNNNFNNNNNYNNNMADISNNLNNMNMNYQPQIKGNQKQ
Protein: Ornithine decarboxylase 1B, chloroplastic (Nt-ODC) (EC 4.1.1.17) (P93351)
Organism: Nicotiana tabacum (Common tobacco)
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine (By similarity). Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- arginase
- Putrescine N-methyltransferase 1
- Putrescine N-methyltransferase 2.
- Putrescine N-methyltransferase 4.
- spermidine synthase
- Ornithine aminotransferase
- spermidine synthase
- spermidine synthase
- Ornithine aminotransferase
- N-carbamoylputrescine amidase
Sequence:
MAGQTIIVSGLNPAAILQSTIGGGASPTAAAAAENGTRKVIPLSRDALQDFMLSIITQKLQDEKQPFYVLDLGEVVSLMDQWKSALPNIRPFYAVKCNPEPSFLSILSAMGSNFDCASRAEIEYVLSLGISPDRIVFANPCKPESDIIFAAKVGVNLTTYDSEDEVYKIRKHHPKSELLLRIKPMLDGNARCPMGPKYGALPEEVDPLLRAAQAARLTVSGVSFHIGSGDADSNAYLGAIAAAKEVFETAAKLGMSKMTVLDVGGGFTSGHQFTTAAVAVKSALKQHFDDEPELTIIAEPGRFFAETAFTLATTIIGKRVRGELREYWINDGLYGSMNCVLYDHATVNATPLAVLSNRSNVTCGGSKTFPTTVFGPTCDALDTVLRDYQLPELQVNDWLVFPNMGAYTKAAGSNFNGFNTSAIVTHLAYSYPS
Protein: Flavohemoprotein (FHP) (Flavohemoglobin) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (EC 1.14.12.17) (P39662)
Organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha)
Function: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MLTQKTKDIVKATAPVLAEHGYDIIKCFYQRMFEAHPELKNVFNMAHQEQGQQQQALARAVYAYAENIEDPNSLMAVLKNIANKHASLGVKPEQYPIVGEHLLAAIKEVLGNAATDDIISAWAQAYGNLADVLMGMESELYERSAEQPGGWKGWRTFVIREKRPESDVITSFILEPADGGPVVNFEPGQYTSVAIDVPALGLQQIRQYSLSDMPNGRSYRISVKREGGGPQPPGYVSNLLHDHVNVGDQVKLAAPYGSFHIDVDAKTPIVLISGGVGLTPMVSMLKVALQAPPRQVVFVHGARNSAVHAMRDRLREAAKTYENLDLFVFYDQPLPEDVQGRDYDYPGLVDVKQIEKSILLPDADYYICGPIPFMRMQHDALKNLGIHEARIHYEVFGPDLFAE
Protein: Dorsal-related immunity factor Dif (P98149)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mediates an immune response in larvae. DIF binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of the immunity gene CECA1. Involved in the melanization immune response to bacterial challenge, possibly by acting in a Toll signaling pathway that down-regulates Spn27A in response to infection. Part of a signaling pathway involving NF-kappa-B (rel) and Toll-related receptors, that functions in the apoptosis of unfit cells during cell competition. May be part of a NF-kappa-B and Tollo signaling cascade that regulates development of the peripheral nervous system.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:8242747}. Nucleus {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:8242747}. Note=Accumulates in the nucleus upon bacterial infection or injury. {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:8242747}.
Interaction partners:
- NF-kappa-B inhibitor cactus
- Cecropin-A1
- Nuclear factor NF-kappa-B p110 subunit
- Defensin
- Cecropin-C
- Embryonic polarity protein dorsal
- Cecropin-B
- Bomanin Short 1
- Drosomycin
- LD20892p
Sequence:
MFEEAFGDIQEIINASMELNGGATGGGSVAGAVGGGGAAHHILSQSTSLPVMPSHIPLHLQNQNMNQNLPEPSARSGPHLRIVEEPTSNIIRFRYKCEGRTAGSIPGMNSSSETGKTFPTIEVCNYDGPVIIVVSCVTSDEPFRQHPHWLVSKEEADACKSGIYQKKLPPEERRLVLQKVGIQCAKKLEMRDSLVERERRNIDPFNAKFDHKDQIDKINRYELRLCYQAFITVGNSKVPLDPIVSSPIYGKSSELTITRLCSCAATANGGDEIIMLCEKIAKDDIEVRFYETDKDGRETWFANAEFQPTDVFKQMAIAFKTPRYRNTEITQSVNVELKLVRPSDGATSAPLPFEYYPNPELLTKHNRRVAQKTVESLKRSLMSTNLHPSKQVKTSSQYTIFSKPQIATTTPQTQVSPGMPLMFPGGSPNFVQDIKMENGFMDVDSQSSQCPSVERNFASPRSNCSTVDSIPPMQMGQNQTHLYLPDATNFTFNGNFASPSSNCSTVDSIPPFQIGQRNNHMYLPENSNFPVNGCSPTHFSGGSMTPINNNNNVLINNNNNDFLSQKMSAISIPPQGNFGIKQVYQQTQQFLPQLQPESIPYLAQSHPEQSQYQQQQQPQEQQPPADEPTQSFSDLISSSIGMAPIDTSELIQDIEAELNSLGIQPFK
Protein: Ly6/PLAUR domain-containing protein 6 (Q8BPP5)
Organism: Mus musculus (Mouse)
Function: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain. Inhibits nicotine-induced Ca(2+) influx through nAChRs (By similarity). In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner (By similarity). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q86Y78}. Cytoplasm {ECO:0000250|UniProtKB:Q86Y78}. Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Synapse, synaptosome {ECO:0000250|UniProtKB:D3ZTT2}. Membrane raft {ECO:0000250|UniProtKB:Q66IA6}. Cell projection, dendrite {ECO:0000250|UniProtKB:D3ZTT2}. Perikaryon {ECO:0000250|UniProtKB:D3ZTT2}. Note=Colocalizes with alpha-3:beta-4- and alpha-7- nicotinic acetylcholine receptors (nAChRs) in the primary cortex and hippocampus. {ECO:0000250|UniProtKB:D3ZTT2}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 6
- Ly-6/neurotoxin-like protein 1
- Lymphocyte antigen 6H
- Secreted Ly-6/uPAR-related protein 1
- Frizzled-8
Sequence:
MEPSPALAWLLLLSLVADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRDTRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGYKICTSCCEGNICNLPLPRNETDATFATTSPINQTNGHPHCVSVIVSCLWVWLGLTL
Protein: Coiled-coil domain-containing protein 80 (E7FD69)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Non-histone chromosomal protein HMG-like
- Sema domain, transmembrane domain
- Neurite extension and migration factor b.
- FAU ubiquitin-like and ribosomal protein S30 fusion a ubiquitously expressed
- FAU ubiquitin-like and ribosomal protein S30 fusion b
Sequence:
MKNLQVQFFLMTLTWIQASDLDYPKTDRGNAQLQPNTFVNKYTKDVQTNRRLSGLSTSGNTHILRKPQNDQENSRPPARRVLKGQRPALFRKPSVNDSIPAQETSLGAASSINILAGFAGKNRVLIISAPNESDGYYRLMMNLLKPDVYCEMADRHMQQIIMFHEKGKMGGKVRRVSNQGSLVEEPLDPALVPRLMGFLKLEDGKFGMVLLRKTLQIEERYPYPVQLEAIYETIDQTPMRRLEKARHKGFVQKCKTAGIEGQVVQSAGSNTVGLQPQVNTAVHTRRQRVRPVPQPTQMTQAQISSALTTTKTTTTLKTTTTKPPTTTTQPATTITITTTTAPTTTILPSTTTTVTTVVPTTMEQTHPDTTRTTTPNEKTQNSHPVTSNLRKQPQEKYLVPTQKMPIAVLPTHRSAQKPKNKLPAVKHGWREKLSQHTRERDALRPTAEKPETELMTSPKGRAKPDSADRGKKTDRPEKPLKKIPAGKKDPKVTKETNISIQNKNTAQKPNAFEEGAVVDQTTNPKKSLETFLSYFQRRRRLIVITAPDEQNHMYSEQRDEYLEQVCDMALRKISIISIFGPLTNSTMKIEHYQTEQDKPLRGLPDSDLINQDLITAFRKQFGMIDNDFNMVLTDFDMKVKQRYEVPIVMKAMFDYIDTLSTRIKEIEQQRKLGAMCKKEDKSRSLEDFLSRFRWRRRLFIISTPSDEEWAYQQQLYAINSQACNLGLRHMSLLKLLGKTLDDMSGVLELYPINGSSSVDREALSASLVQDIRNYFQISLEYFSMLLVGKDGNVKSWYPSPMWSMSIIYELVDSMQLRRQEMAIQQSLGMRCPDHDYTHHDGYHEAYHQGYAY
Protein: Intracellular hyaluronan-binding protein 4 (IHABP-4) (IHABP4) (Hyaluronan-binding protein 4) (Ki-1/57 intracellular antigen) (Q5JVS0)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that plays a role in the regulation of transcription, pre-mRNA splicing and mRNA translation. Negatively regulates DNA-binding activity of the transcription factor MEF2C in myocardial cells in response to mechanical stress (By similarity). Plays a role in pre-mRNA splicing regulation. Binds (via C-terminus) to poly(U) RNA. Involved in mRNA translation regulation, probably at the initiation step. Seems to play a role in PML-nuclear bodies formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055, ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:9523163}. Cytoplasm {ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055, ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:9523163}. Cytoplasm, Stress granule {ECO:0000269|PubMed:21771594}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A1L1K8}. Nucleus, nuclear body {ECO:0000269|PubMed:19523114}. Nucleus, nucleolus {ECO:0000269|PubMed:19523114}. Nucleus speckle {ECO:0000269|PubMed:19523114}. Nucleus, Cajal body {ECO:0000269|PubMed:19523114}. Nucleus, gem {ECO:0000269|PubMed:19523114}. Note=Transported into the nuclear compartment in activated leukocytes (PubMed:9523163). Inhibition of methylation alters its distribution between the nuclear and cytoplasmic compartments (PubMed:16879614, PubMed:19523114). Methylation may be required for its localization in subnuclear structures, such as nucleoli, nuclear speckles, Cajal bodies and Gemini of coiled bodies (gems) (PubMed:19523114). Colocalizes with FMR1, FXR1 and FXR2 in cytoplasmic stress granules (PubMed:21771594). In myocardial cells, localization at the sarcoplasm is reduced in response to mechanical stress (By similarity). {ECO:0000250|UniProtKB:A1L1K8, ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:21771594, ECO:0000269|PubMed:9523163}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL15
Sequence:
MKGALGSPVAAAGAAMQESFGCVVANRFHQLLDDESDPFDILREAERRRQQQLQRKRRDEAAAAAGAGPRGGRSPAGASGHRAGAGGRRESQKERKSLPAPVAQRPDSPGGGLQAPGQKRTPRRGEQQGWNDSRGPEGMLERAERRSYREYRPYETERQADFTAEKFPDEKPGDRFDRDRPLRGRGGPRGGMRGRGRGGPGNRVFDAFDQRGKREFERYGGNDKIAVRTEDNMGGCGVRTWGSGKDTSDVEPTAPMEEPTVVEESQGTPEEESPAKVPELEVEEETQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKAVVIHKSKYRDDMVKDDYEDDSHVFRKPANDITSQLEINFGNLPRPGRGARGGTRGGRGRIRRAENYGPRAEVVMQDVAPNPDDPEDFPALS
Protein: Immunoglobulin superfamily member 5 (IgSF5) (Junctional adhesion molecule 4) (JAM-4) (Q7TSN7)
Organism: Mus musculus (Mouse)
Function: Provides, together with MAGI1, an adhesion machinery at tight junctions, which may regulate the permeability of kidney glomerulus and small intestinal epithelial cells. Mediates calcium-independent homophilic cell adhesion. In testis, it may function as a cell adhesion molecule rather than a tight-junction protein. It may participate in the adhesion between spermatogonia-spermatogonia, spermatogonia-Sertoli cells, and Sertoli cells-Sertoli cells.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q5VJ70}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q5VJ70}.
Interaction partners:
- Junctional adhesion molecule A
- Occludin
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Junctional adhesion molecule B
- Junctional adhesion molecule C
- Junctional adhesion molecule-like
- E3 ubiquitin-protein ligase LNX
- MARVEL domain-containing protein 2
Sequence:
MEGSWRDVLAVLVILAQLTASGSSYQIIEGPQNVTVLKDSEAHFNCTVTHGWKLLMWTLNQMVVLSLTTQGPIITNNRFTYASYNSTDSFISELIIHDVQPSDSGSVQCSLQNSHGFGSAFLSVQVMGTLNIPSNNLIVTEGEPCNVTCYAVGWTSLPDISWELEVPVSHSSYNSFLESGNFMRVLSVLDLTPLGNGTLTCVAELKDLQASKSLTVNLTVVQPPPDSIGEEGPALPTWAIILLAVAFSLLLILIIVLIIIFCCCCASRREKEESTYQNEIRKSANMRTNKADPETKLKGGKENYGYSSDEAKAAQTASLPPKSAEVSLPEKRSSSLPYQELNKHQPGPATHPRVSFDIASPQKVRNVTLV
Protein: Frizzled-9 (Fz-9) (mFz3) (mFz9) (CD antigen CD349) (Q9R216)
Organism: Mus musculus (Mouse)
Function: Receptor for WNT2 that is coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). Plays a role in neuromuscular junction (NMJ) assembly by negatively regulating the clustering of acetylcholine receptors (AChR) through the beta-catenin canonical signaling pathway. May play a role in neural progenitor cells (NPCs) viability through the beta-catenin canonical signaling pathway by negatively regulating cell cycle arrest leading to inhibition of neuron apoptotic process (By similarity). During hippocampal development, regulates neuroblast proliferation and apoptotic cell death. Controls bone formation through non canonical Wnt signaling mediated via ISG15. Positively regulates bone regeneration through non canonical Wnt signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24860427}; Multi-pass membrane protein {ECO:0000255}. Note=Relocalizes DVL1 to the cell membrane leading to phosphorylation of DVL1 and AXIN1 relocalization to the cell membrane. {ECO:0000250|UniProtKB:Q8K4C8}.
Interaction partners:
- Protein Wnt-5a
- Protein Wnt-11
- Protein Wnt-7a
- Proto-oncogene Wnt-1
- Protein Wnt-4
- Tyrosine-protein kinase RYK
- Protein Wnt-2
- Protein Wnt-6
- Protein Wnt-2b
- Protein Wnt-3a
Sequence:
MAVPPLLRGALLLWQLLATGGAALEIGRFDPERGRGPAPCQAMEIPMCRGIGYNLTRMPNLLGHTSQGEAAAQLAEFSPLVQYGCHSHLRFFLCSLYAPMCTDQVSTPIPACRPMCEQARLRCAPIMEQFNFGWPDSLDCARLPTRNDPHALCMEAPENATAGPTEPHKGLGMLPVAPRPARPPGDSAPGPGSGGTCDNPEKFQYVEKSRSCAPRCGPGVEVFWSRRDKDFALVWMAVWSALCFFSTAFTVFTFLLEPHRFQYPERPIIFLSMCYNVYSLAFLIRAVAGAQSVACDQEAGALYVIQEGLENTGCTLVFLLLYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEAHGSYFHMAAWGLPALKTIVVLTLRKVAGDELTGLCYVASMDPAALTGFVLVPLSCYLVLGTSFLLTGFVALFHIRKIMKTGGTNTEKLEKLMVKIGVFSILYTVPATCVIVCYVYERLNMDFWRLRATEQPCTAATVPGGRRDCSLPGGSVPTVAVFMLKIFMSLVVGITSGVWVWSSKTFQTWQSLCYRKMAAGRARAKACRTPGGYGRGTHCHYKAPTVVLHMTKTDPSLENPTHL
Protein: Apolipoprotein A-II (Apo-AII) (ApoA-II) (Apolipoprotein A2) [Cleaved into: Proapolipoprotein A-II (ProapoA-II)] (P09813)
Organism: Mus musculus (Mouse)
Function: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P02652}.
Interaction partners:
- Apolipoprotein A-I
- Apolipoprotein C-III
- Apolipoprotein E
- Apolipoprotein A-IV
- Apolipoprotein B-100
- Beta-2-glycoprotein 1
- Apolipoprotein C-I
- Apolipoprotein C-II
- Apolipoprotein D
- Serum paraoxonase/arylesterase 1
Sequence:
MKLLAMVALLVTICSLEGALVKRQADGPDMQSLFTQYFQSMTDYGKDLMEKAKTSEIQSQAKAYFEKTHEQLTPLVRSAGTSLVNFFSSLMNLEEKPAPAAK
Protein: RNA-binding protein 47 (RNA-binding motif protein 47) (B7ZLP7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTAEDSTAAMSSDSAAGSSAKVPEGVAGAPNEAALLALMERTGYSMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVDNCRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKPMDKEQYSRYQKAARGGGAAEAAQQPSYVYSCDPYTLAYYGYPYNALIGPNRDYFVKAGSIRGRGRGAAGNRAPGPRGSYLGGYSAGRGIYSRYHEGKGKQQEKGYELVPNLEIPTVNPVAIKPGTVAIPAIGAQYSMFPAAPAPKMIEDGKIHTVEHMISPIAVQPDPASAAAAAAAAAAAAAAVIPTVSTPPPFQGRPITPVYTVAPNVQRIPTAGIYGASYVPFAAPATATIATLQKNAAAAAAVYGGYAGYIPQAFPAAAIQVPIPDVYQTY