wanglab/gogpt-training-data huggingface dataset:
Protein: aspartate transaminase (EC 2.6.1.1) (Q7YWB4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSIYADVPKGPAIEVFALTQAFKDDSNPNKVNLSVGAYRTDAGVPWVLPVVRKTEISIASDEQVNHEYLPVTGLETFTNAATELVLGADSPAIKENRAFGVQTISGTGALRVAADFLHTQLNRNVVYYSNPTWENHHKIFCDAGFTTVKSYRYWDQNKRELDFKNMLADLNDAPPGAVIILHACAHNPTGIDPTQEQWTELADLMEKKKLFPLFDSAYQGFASGDPDRDAWAARYFVQRGFELFICQSFAKNFGLYCERTGNLTVVQKNGATKAAVHSQLTLLIRGQYSNPPAYGARIVSKVLNTPELRKEWMASIQAMSSRIREMRTALRDKLVALGTPGTWDHIVNQIGMFSYTGLNESHVRVLIDQYHIYLLKTGRISMSGLNKGNVEYVAKAIHAAVTGSGESASCPCENKL
Protein: cDNA, FLJ94397, highly similar to Homo sapiens uroplakin 1B (UPK1B), mRNA (B2R9H7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAKDNSTVRCFQGLLIFGNVIIGCCGIALTAECIFFVSDQHSLYPLLEATDNDDIYGAAWIGIFVGICLFCLSVLGIVGIMKSSRKILLAYFILMFIVYAFEVASCITAATQRDFFTPNLFLKQMLERYQNNSPPNNDDQWKNNGVTKTWDRLMLQDNCCGVNGPSDWQKYTSAFRTENNDADYPWPRQCCVMNNLKEPLNLEACKLGVPGFYHNQGCYELVSGPMNRHAWGVAWFGFAILCWTFWVLLGTMFYWSRIEY
Protein: Germin-like protein subfamily 2 member 4 (Q9M263)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250}.
Interaction partners:
- Chitinase-like protein 2
- Coatomer subunit epsilon-2
- SKU5 similar 3
Sequence:
MDSRCFGFFFTLLSLNVIVLAYDPDTLQDLCVADRTSGIKVNGFTCKPESNITASDFFFAGIGKPAVVNNTVGSAVTGANVEKIAGLNTLGVSLARIDYAPGGLNPPHTHPRATEVIFVLEGELDVGFITTANKLFAKTVKKGEVFVFPRGLIHYQKNNDKAKPASVISAFNSQLPGTQSIAATLFTATPAIPDHVLTTTFQIGTKEIEKIKSKFAPKKV
Protein: Mulatexin (MLX56) (Latex protein) (A7XQ02)
Organism: Morus alba (White mulberry)
Function: Chitin-binding protein which slows larval growth when consumed by the lepidopteran species S.ricini and M.brassica, but not when consumed by the mulberry specialist B.mori. Lacks chitinase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:19476960}.
Interaction partners:
Sequence:
MKFRTLLIIFSLVFLLEIVSASEPQCGRDAGGALCHGNLCCSHWGFCGTTAIYCDVDQGCQSQCWSSPPPPSPPPPPPSPPPPSPPPPSPPPPSPPPPSPPPPSPPPPSPPPPSPPPPGGPERPDHRCGRALGNPPCNPGRCCSIHNWCGSTAAYCRGSSCQYQCWNSLLSALISNGNNAISKIISKSVFDEMFKHMKDCPSKGFYSYDAFIIATTSFPHFGTTGDITTRKRELAAFFAQTSLATTGQRFDSQDLYVWGYCHINETTNGNDNDYCTSAHWPCPSGKKYNSRGAVQLTHNYNYGLAGEALGLDLINNPDLVATDPVISFKTAIWFWMAQHDNKLSCHDILINANSGYVIGNIIKNSGYQNGLITNTISTMRGIGYYKRYCDMLGVSYGDNLDSWYDQTHFSEVARM
Protein: histidine kinase (EC 2.7.13.3) (A0A0F6B632)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
Sequence:
MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSSEYGMNLQNRESIGQLISVLHRRHSDIVRAISVYDDHNRLFVTSNFHLDPSQMQLPAGAPFPRRLSVDRHGDIMILRTPIISESYSPDESAIADAKNTKNMLGYVALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTELNPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRNTLDEVVTLLAHSSHDKGLELTLNIKNDVPDNVIGDPLRLQQVITNLVGNAIKFTESGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNVIIDGPSTACLAGKRLAYVEPNATAAQCTLDLLSDTPVEVVYSPTFSALPLAHYDIMILSVPVTFREPLTMQHERLAKAASMTDFLLLALPCHAQINAEKLKQGGAAACLLKPLTSTRLLPALTEYCQLNHHPEPLLMDTSKITMTVMAVDDNPANLKLIGALLEDKVQHVELCDSGHQAVDRAKQMQFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLSAGMNDYLAKPIEEEKLHNLLLRYKPGANVAARLMAPEPAEFIFNPNATLDWQLALRQAAGKPDLARDMLQMLIDFLPEVRNKIEEQLVGENPNGLVDLVHKLHGSCGYSGVPRMKNLCQLIEQQLRSGVHEEELEPEFLELLDEMDNVAREAKKILG
Protein: CASP8 and FADD-like apoptosis regulator (C0H5Y5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- FAS-associated death domain protein
- Caspase-8
- Tumor necrosis factor receptor superfamily member 6
- Receptor-interacting serine/threonine-protein kinase 1
- E3 ubiquitin-protein ligase
- Ubiquitin-like-conjugating enzyme ATG3
- Caspase-3
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- TNF receptor superfamily member 10b
- TNF receptor-associated factor
Sequence:
MALSTVSAEVIHQVEESLDEDEKEMMLFLCRDVTENLAPPNVRDLLDCLSERGQLSFAALAELLYRVRRFDLLKRILKTDKAAVEDHLCRSPHLVSDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQKYTQSSQEARSNMNALQASLPKLSIKEHLYNSRLQNGRSKEPRFVEHHGIQRKPVKTSIQESGIFLPPHIHEESYRMQSKPLGICLIIDCIGNDTEYLRETFTSLGYRVQPFLFPSSHEITQIVRRFSNMTQHQDYDSFVCVLVSRGGSQSMMGVDQVYSGFSLENVKDMFKGDMCPSLRGKPKLFFIQNYEALEDNSLEVDGPAIKNVNSRHLHPRHCTTHPDADIFWSLCTADVSRLEQPSSSLSVYLQKLSQLLEQGRKRSLVDLHVELMDKVYAWNSNVPSKEKYYLSLQHTLRKKLILSHT
Protein: Maltooligosaccharide ABC transporter solute-binding lipoprotein (Maltodextrin-binding protein) (Solute-binding protein MalX) (P59213)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Part of an ABC transporter complex involved in the uptake of maltodextrins. Binds glycogen-derived linear maltooligosaccharides increasing in size from maltotriose to maltooctaose with the highest affinity for maltotriose. Has a very weak affinity for maltose. Has also a very low affinity for maltotetraitol, indicating that the binding is selective for maltooligosaccharides with an intact reducing end.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MSSKFMKSAAVLGTATLASLLLVACGSKTADKPADSGSSEVKELTVYVDEGYKSYIEEVAKAYEKEAGVKVTLKTGDALGGLDKLSLDNQSGNVPDVMMAPYDRVGSLGSDGQLSEVKLSDGAKTDDTTKSLVTAANGKVYGAPAVIESLVMYYNKDLVKDAPKTFADLENLAKDSKYAFAGEDGKTTAFLADWTNFYYTYGLLAGNGAYVFGQNGKDAKDIGLANDGSIVGINYAKSWYEKWPKGMQDTEGAGNLIQTQFQEGKTAAIIDGPWKAQAFKDAKVNYGVATIPTLPNGKEYAAFGGGKAWVIPQAVKNLEASQKFVDFLVATEQQKVLYDKTNEIPANTEARSYAEGKNDELTTAVIKQFKNTQPLPNISQMSAVWDPAKNMLFDAVSGQKDAKTAANDAVTLIKETIKQKFGE
Protein: DRBM domain-containing protein (Q57WD9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRCTMTFSTLVRRRAFLPLITPHNICSWAFVGNRSYALLRTLSPHTCPAAVSCSTRSPSIRRSHLPLVTAPMTDCLLHGRRQLFTAGETVEEVGTDNGGCGLPEAEALLRERFGPQAKLVLRRCQRRHSRNSTKAAPHGEEEEEVVEDDEPVGGGASFDSEEQSKQEQQLCGVTEYRASATCRLLGFPLELAVASGGEAKEVLHAVLNDALESDVVFIHPQQRASASSHGCRGTGRNRGYQKRGSYRKGKEEPTLSPRQLELKAIIDELRELCVHFSRVLKFSIKSPRNSSGKQGQESEQGADLRWRCRAYERDEWGMTPSLSFSAEARGQSANDSLVRCLAMLRDRYRAELESPSVQLESVREVEVLVRPWEKIVESHCFEECTEGSLEKEKGDSQRHDQETPSPSSPSPVTCHGEGAEPTEPIPVEEQYRVLRAATFTAAVTVEDARGNISVHQVKRQATPLVAYQNASLQALRAELTFSPDANIATQLLPSSPLLVRMRWQFDAMVQHLSREYGKKTEDIALVRVEGDGAGDDKERDISTAPKDGDGDQGVPHGKHRYFFTASFTSDGCVVWQQSGPGRYRLEFDCYVQALTYLLDQYPEVGRVYFDPRGGGVFFPTTQLLSLAVQKHDNYNVATNHRGKWNAYALLGTLTSQLIGSFYQTTYHTDRATGEATAVLTVDDGLRSNQLLIERRARKRGEAWRNACLDALRENFPNQYRDALLLHPDIDLSGDTMARGSKFRALPREKRVEHMGNIFSLVSAFAEEDLGWHNLRVRLRNASGDLGLPQWVAEMEAQVEGEEQRRVVAVSPPYPQVKHARRVLVYSLAKRYFPKELEAYAKLNRGDAVNPDQDAQNVYNSVFRVGSESFVHQVMLLLEEQAPSMAPFTWSLEQQESDGAEEEAGNDGSVEYLLRPFRARFRAAVCGQKGDLLVSERIGEEGESAACVLCSALRAATNRLAGDKGEQLWTEYECHAPPPITNSRELSLYMFNTFFGVSTGTATAIEDDGASPSTVEQQVVDIDARELGGYWFVTLSFSRAGGLAVARAVATSKREGVRDVLLLACRQSFPRALTYLSAHSKEIHSFAEEILTAPVVEVLPAAVLRDLQRQLERAESAGPPRPYTLLRRCVTREFRNERWLRVEQQPSNGGGFQCRIYLQRHRRETRKGEVQLVGFGAALTRAQALHIASLRALENLFEQDLADAIARSPTYTDLPPLE
Protein: A disintegrin-like and metallopeptidase (Reprolysin type) with thrombospondin type 1 motif, 14 (B2RXR8)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MAWLRALLHCLLPWYCALCAAAGSQTPDLRLSGKLHDYVVTVPCSTDFQGRFLSHVVSAPAAPSPRSHLRVARSPLSLERETPRPGGPRQHFLYFNVTVFGKLLHLRLQPNRRLVAPGAPVEWQEDFRELFRQPLQQDCVYTGGVTGMPGAAVAISNCDGLAGLIRTDNSDYFIEPLERGQQEKEAGGRTHVVYRREAVQREWKEPHGDLHNEAFGLGDLPNVLDLVGDRLGDAERKRRHAKPGSYSIEVLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMVGYRQSLSLIERGNPARSLEQVCRWAHSQQRQDPSHTEHHDHVIFLTRQNFGPSGYAPVTGMCHPLRSCALNHEDGFSSAFVVAHETGHVLGMEHDGQGNGCDDETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSYDCLLDDPFERTWPQPPELPGIDYSMDEQCRFDFGTGYHTCLAFRTFEPCKQLWCSHPDNPYFCKTKKGPPLDGTECAPGKWCFKGHCIWKSPEQTYGQDGGWSSWTNFGSCSRSCGGGVRSRSRSCDNPPPAYGGRPCSGSMFEYQICNSEDCPGPYEDFRAQQCAKRNSYYTHQDAKHSWLPYEPDSDAQKCELICQSADTGDVVFMNQVVHDGTRCSYRDPYSVCARGECVPFGCDKEVGSMKTDDKCGVCGGDNSHCRTVKGTLGKGSKQAAALKQVQIPAGARHIQIELLEKAPHRIAVKNQVTGSFIFNPKGKEASSRTFTALGLEWEHEAEDTKDSLRTNGPLPEAIAILVLPPAEGKPRGSLAYKYVIHEDLLPLIGSNNVLLEETDTYEWALKSWSPCSKACGGGIQFTKYGCRRRRDHHMVHRHLCDHKKRPKPIRRRCNQHSCPQPTWVTEEWGACSRSCGKLGLQTRGVQCLLPLSNGTHKAMPAKACLGNRPEAKKPCLRVPCPAQWRTGAWSQCSATCGEGIQQRQVVCRNTSSALGPCEGVKPDMVQICSLPACGGDLQNSTVKVEVQDPVTKTGYREPQSRPLTPEDRISTMEPCVRDRSVFCRMEVLDRYCTIPGYHRLCCESCIKKTSGPNASLASPPTFSTPGSLLPAPKATLEDVKSTRGPTSLEDHRQSQPTQLPDVADRISPVTQYPVTPQMLSPKAFPGNSPATPRRPPQDWTQTAMPTSEGQGQSREEPGHGGTSLPATSPVT
Protein: Copper resistance P-type ATPase (Eurofung) (Q5B756)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU362081}.
Interaction partners:
- Superoxide dismutase 1 copper chaperone
- Iron/copper transporter Atx1, putative
- RNA polymerase I-specific transcription initiation factor RRN6-like protein
Sequence:
MAVSNTLAARGGALSPSQTTSQMATTTVSVEGMTCGACTSAVEGAFNGVEGAGEVSVSLMMSRAVIHHDPTLLPPGKVAEIIEDCGFDATVISTDSSSIPSRSASDHGASEANVVTTTLAVAGMTCGACTSAVESGLAENPGVRSVNVSLLSERAVIEHDLSTVSAEQLAEIVEDRGFGARVLETSTSRAGPRGSESTDPSSQSMTTTVAIEGMTCGACTSSVQAAFDGVEGVIQFNISLLAERAIITHNPQILPSRKIVEIIEDAGFDAKVVSEVQALGQKGGPTQVTLDVHGLRDANSAAALEDSLMQKPGIISASVTLATSRLVVSYDTSMVGIRTIVAVIEAAGCNALLADSDDKNTQLESLAKTKEVLEWRRAFLFSLSFAIPVFLINMILPMYLPTLDFGGIRIIPGLYLGDSVCLLLTIPVQFGIGKRFYITSYKSLRHRAPTMDVLVMLGTSAAFFYSVFTMIVAIVIDPHQRPNTVFDTSTMLITFITLGRWLENRAKGQTSAALSRLMSLAPSMTTIYDDPIAAEKMVEEWDKVDGQEQKTATNEMSTVSQKIIPTELIEVGDIVVLHPGDKVPADGVVIRGETYVDESMITGEALPIHKAKGSLVIAGTVNGTSAVDIKVIRTGKDTQLSKIVKLVQDAQTSRASIQRMADIVAGYFVPSIISLGLVTFFGWMFVSHLLPHPPKIFVTKEGGGKVMVCLKLCISVIVFACPCALGLSTPTAVMVGTGVGATQGILVKGGAVLEAATKITHVVYDKTGTLTTGQMSVTEARIEPHWSSSDWRRRLWWLIVGLAEMNSEHPIGKAIHLAAKSESGNSGEGGLPGSLGDFEARIGKGIAALVEPASGVERVRYRVLIGNAAFLQSHSVAVPESAETTPDASGYKNSRVGITQIHVAIDGHFAGTIALQDTVKVTAVAAVAALHRMGISTSLITGDSRAAAISIASAVGIAPEAVHASVSPSDKQSIIASLQETGDRVAMVGDGINDSPALATASVGIALASGTDVAMEAADIVLMRPDDLLSVPASLALSRSVFNRIKLNLVWACGYNIIGLPFAMGLFLPFGGFMLPPMAAGAAMALSSVSVVVSSLLLKFWRRPSWMDAELLEKEVGIASDGNSRKNWLGATLFTSPNKTRRAAQWAQGIGARVWSVFTGRPSQSASIEPSYVPLQTVEPAV
Protein: Pyruvate carboxylase (EC 6.4.1.1) (Q5B4R8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- 2-methylcitrate synthase, mitochondrial
- Citrate synthase, mitochondrial
- Biotin apo-protein ligase, putative
- Malate dehydrogenase
- Phosphoenolpyruvate carboxykinase
- L-lactate dehydrogenase
- ATP citrate synthase
- Malic enzyme
- Malic enzyme
- ATP citrate synthase
Sequence:
MASIVPHNQPEEAVDETEFVDDHHHAHHRDSVHHRLRANSAIMQFQKILVANRGEIPIRIFRTAHELSLQTVAIFSHEDRLSMHRQKADEAYMIGKRGQYTPVGAYLAIDEIVKIALEHGVHLIHPGYGFLSENAEFARKVEQSGMVFVGPTPETIEGLGDKVSARRLAIKANVPVVPGTEGPVERFEEVKAFTDTYGFPIIIKAAFGGGGRGMRVVRNQADLRDSFERATSEARSAFGNGTVFVERFLDKPKHIEVQLLGDNHGNVVHLFERDCSVQRRHQKVVEIAPAKDLPQNVRDSILADAVKLAKSVNYRNAGTAEFLVDQQNRYYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGATLEQLGLTQDRISTRGFAIQCRITTEDPAKGFSPDTGKIEVYRSAGGNGVRLDGGNGFAGAIITPHYDSMLVKCTCRGSTYEIARRKVVRALVEFRIRGVKTNIPFLTSLLSHPTFIDGNCWTTFIDDTPELFALVGSQNRAQKLLAYLGDVAVNGSSIKGQIGEPKLKGDIIKPTLHDAAGKPIDVSSPCTKGWKQILDQEGPEAWAKAVRANKGCLIMDTTWRDAHQSLLATRVRTIDLLNIAHETSHALSNAYSLECWGGATFDVAMRFLYEDPWDRLRKLRKAVPNIPFQMLLRGANGVAYSSLPDNAIYHFCKQAKRCGVDIFRVFDALNDIDQLEVGIKAVHAAGGVVEATVCYSGDMLNPSKKYNLEYYLKLVDKIVALKPHVLGIKDMAGVLKPQAARLLIGSIRERYPDLPIHVHTHDSAGTGVASMIACAQAGADAVDAATDSLSGMTSQPSIGAILASLEGTEQDPGLDSAQVRALDSYWAQLRLLYSPFEAGLTGPDPEVYEHEIPGGQLTNLIFQASQLGLGQQWAETKKAYEVANDLLGDIVKVTPTSKVVGDLAQFIVSNKLTPEDVINRAGELDFPGSVLEFLEGLMGQPYGGFPEPLRSKALRDRRKLDKRPGLFLEPLDLAKIKNDLREKYGSATEYDVASYAMYPKVFEDYKKFVQKYGDLSVLPTRFFLAKPEIGEEFHVELEKGKVLILKLLAIGPLSDQTGQREVFYEVNGEVRQVSVDDKKASVENIARPKADVTDSSQVGAPMSGVVVEIRVHEGSEVKKGDPIAVLSAMKMEMVISAPHSGKVSGLLVKEGDSVDGQDLICKIAKA
Protein: Chaperonin Hsp60, mitochondrial, putative (Q381T1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 10 kDa heat shock protein, putative
- Chaperonin HSP60, mitochondrial
- Heat shock 70 kDa protein, putative
- Heat shock 70 kDa protein, mitochondrial, putative
- GrpE protein homolog
- Uncharacterized protein
- CCT-theta
Sequence:
MLRRSFACCMQYGSTPKDIRYGIEARKLLLLGVENLVKAVGVTLGPKGRNVVLEMPYASPKITKDGVTVAKHIEFENSFENLGANLVRQVAGLTNDTAGDGTTTATILSGAIFREGFRSVSTGTNPMDLKRGIDLACREVLASLAEQAKPVTSKSEVTQIAMISANMDVEIGALIGDAMQQVGKDGVITTQEGRSLNTELELVEGMSFERGFTSPYFVTNTKSQKCELENALVFVANRKLSSVAHILPALNHAIQKKRPLLVISEDLEGEAMHTFLYNKIQGRITGCSVKAPGFGDMRINQLQDIAVFTGAQMISEDLGLSLDQSDFSERLLGSCKKATISRDECILMEGGGSAIAVEERVQMIRDMIAAEDHEYNRERLVERLAKLSGGVAVIKVGGASEVEISEKKDRIVDALNATRAAVAEGILAGGGTALLVASVRLDSVAKDRSLPPDIRTGVNIVKRAVRLPCRYIASNAGVEGSVVASKIMRRNDPTFGYNAQTGEYVNMFNEGIIDPMKVVKSAVVNACSVAGMMITTEAAVVEKDVLAKESRIEDRGLEDKEKREGLNTMRKRVNESQAPLPALAPPMKFQMKGI
Protein: Cadherin-6 (Kidney cadherin) (K-cadherin) (P97326)
Organism: Mus musculus (Mouse)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Catenin alpha-1
- Cadherin-2
- Cadherin-3
- Catenin beta-1
- Cadherin-20
- Cadherin-4
- Cadherin-7
- Cadherin-10
- Cadherin-11
Sequence:
MRTYRYFLLLFWVGQPYPTFSNPLSKRTSGFPAKRKALELSANSRNELSRSKRSWMWNQFFLLEEYTGSDYQYVGKLHSDQDRGDGSLKYILSGDGAGDLFIINENTGDIQATKRLDREEKPVYILRAQAVNRRTGRPVEPESEFIIKIHDINDNEPIFTKDVYTATVPEMADVGTFVVQVTATDADDPTYGNSAKVVYSILQGQPYFSVESETGIIKTALLNMDRENREQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRFPQSTYQFKTPESSPPGTPIGRIKASDADVGENAEIEYSITDGEGHEMFDVITDQETQEGIITVKKLLDFEKKKVYTLKVEASNPHVEPRFLYLGPFKDSATVRIVVDDVDEPPVFSKLAYILQIREDARINTTIGSVAAQDPDAARNPVKYSVDRHTDMDRIFNIDSGNGSIFTSKLLDRETLLWHNITVIATEINNPKQSSRVPLYIKVLDVNDNAPEFAEFYETFVCEKAKADQLIQTLRAVDKDDPYSGHQFSFSLAPEAASSSNFTIQDNKDNTAGILTRKNGYNRHEMSTYLLPVVISDNDYPVQSSTGTVTVRVCACDHHGNMQSCHAEALIHPTGLSTGALVAILLCIVILLVTVVLFAALRRQRKKEPLIISKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPEAMEDSKSRRDIVPEALFLPRRTPTARDNTDVRDFINQRLKENDTDPTAPPYDSLATYAYEGTGSVADSLSSLESVTTDGDQDYDYLSDWGPRFKKLADMYGGMDSDKDS
Protein: C-1-tetrahydrofolate synthase, cytoplasmic (EC 1.5.1.5) (EC 3.5.4.9) (EC 6.3.4.3) (V9GZ78)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAPEKDVDGLTSINAGKLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKPGKWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSALERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLVPSVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLPKAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAFDAVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
Protein: Lysosome-associated membrane glycoprotein 5 (Brain and dendritic cell-associated LAMP) (Brain-associated LAMP-like protein) (BAD-LAMP) (Lysosome-associated membrane protein 5) (LAMP-5) (Q9UJQ1)
Organism: Homo sapiens (Human)
Function: Plays a role in short-term synaptic plasticity in a subset of GABAergic neurons in the brain.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21642595}; Single-pass type I membrane protein {ECO:0000269|PubMed:21642595}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q9D387}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:21642595}; Single-pass type I membrane protein {ECO:0000269|PubMed:21642595}. Endosome membrane {ECO:0000269|PubMed:21642595}; Single-pass type I membrane protein {ECO:0000269|PubMed:21642595}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9D387}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9D387}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:Q9D387}; Single-pass type I membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q9D387}; Single-pass type I membrane protein {ECO:0000305}. Recycling endosome {ECO:0000250|UniProtKB:Q9D387}. Note=Recycles from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane (By similarity). Colocalizes with UNC93B1 in large endosomal intracellular vesicles (PubMed:21642595). Accumulates in the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) before its disappearance upon activation by CpG dinucleotides (PubMed:21642595). Associates with cortical membranes (PubMed:21642595). Localizes mostly in cytoplasmic vesicles of neuronal cell body (By similarity). Localizes to synaptic vesicles in a subset of GABAergic neurons (By similarity). {ECO:0000250|UniProtKB:Q9D387, ECO:0000269|PubMed:21642595}.
Interaction partners:
Sequence:
MDLQGRGVPSIDRLRVLLMLFHTMAQIMAEQEVENLSGLSTNPEKDIFVVRENGTTCLMAEFAAKFIVPYDVWASNYVDLITEQADIALTRGAEVKGRCGHSQSELQVFWVDRAYALKMLFVKESHNMSKGPEATWRLSKVQFVYDSSEKTHFKDAVSAGKHTANSHHLSALVTPAGKSYECQAQQTISLASSDPQKTVTMILSAVHIQPFDIISDFVFSEEHKCPVDEREQLEETLPLILGLILGLVIMVTLAIYHVHHKMTANQVQIPRDRSQYKHMG
Protein: Ras-like GTP-binding protein RhoL (Q24192)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for the maturation of hemocytes.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase kinase kinase
- Rho guanine nucleotide exchange factor 3, isoform L
- non-specific serine/threonine protein kinase
- Rho GDP-dissociation inhibitor 3
- Serine/threonine-protein kinase PAK mbt
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Rho guanine nucleotide exchange factor at 64C, isoform A
- Cdc42 homolog
Sequence:
MTANITKSPRPLKITIVGDGMVGKTCMLITYTRNEFPEEYIPTVFDNHACNIAVDDRDYNLTLWDTAGQEDYERLRPLSYPSTNCFLLCYSISSRTSFENVKSKWWPEIRHFSAHVPVVLVGTKLDLRIPNSEKFVTTQEGKKMRKEIHAFNLVECSAKKKQNLQQVFEEAVRAVERKPKTTSKQSCKIL
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (B5DFD6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Angiopoietin-1
- Angiopoietin-2
- Nitric oxide synthase 3
- Angiopoietin 4
- Cadherin-5
Sequence:
MVWWGSPFLLPILFLASHVGASVDLTLLANLRITEPQRFFLTCVSGEAGAGRSSDVWGPPLLLEKDDRIVRTFPPGQPLHLTRNGSHQVTLRGFSKPSDLVGVFSCVGGAGTRRTRVLYVHNSPGAHLFPDKVTHTVNKGDTAVLSARVHKEKQTDVIWKNNGSYFHTLDWHEAHDGRFQLQLQNVQPPSSGIYSATYLEASPLGSAFFRLIVRGCEAGRWGPGCVKDCPGCLHGGVCHDHDGECVCPPGFTGTRCEQACREGRFGQSCQEQCPGTAGCRGLTFCLPDPYGCSCGSGWRGSQCQEACAPGHFGADCRLQCQCQNGGTCDRFSGCVCPSGWHGVHCEKSDRIPQILNVATELEFNLGTMPRINCAAAGNPFPVRGSMELRKPDGTMLLSTKAIVEPDRTTAEFEVPRLTLGDSGFWECRVSTSGGQDSRRFKVNVKVPPVPLTAPRLLAKQSRQLVVSPLVSFGGDGPISSVRLHYRPQDSMITWSAIVVDPSENVTLMNLKPRTGYNVRVQLSRPGEGGEGAWGPSTLMTTDCPEPLLQPWVESWNVEGPDRLRVSWSLPSVPLSGDGFLLRLWDGARGQERRENISSPQARTALLTGLTPGTHYQLDVRLYHCTLLGPASPSAHVHLPLSGPPAPRHLRAQALSDSEIRLMWQHPEAPPGPISKYIVEIQVAGGSGDPQWMDVDKPEETSTTVRGLNASTRYLFRVRASVQGLGDWSNTVEETTLGNGLQSASPVQESRVAEDGLDQQLVLAVVGSVSATCLTILAALLALVCIRRSCLHRRHTFTYQSGSGEETILQFSSGTLTLTRRPKPQPEPLSYPVLEWEDITFEDLIGEGNFGQVIRAMIKKDGLKMNAAIKMLKEYASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYIAIEYAPYGNLLDFLRKSRVLETDPAFAREHGTASTLSSRQLLRFASDAANGMQYLSEKQFIHRDLAARNVLVGENLASKIADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEQPRNCDDEVYELMRQCWRDRPYERPPFAQIALQLGRMLEARKAYVNMSLFENFTYAGIDATAEEA
Protein: Protein FAM81A (Q8TBF8)
Organism: Homo sapiens (Human)
Subcellular location: Postsynaptic density {ECO:0000250|UniProtKB:Q3UXZ6}. Cytoplasm {ECO:0000269|PubMed:31429579}.
Interaction partners:
Sequence:
MENMHLRRVRTMPRHSQSLTMAPYSSVSLVEQLEDRILCHEKTTAALVEHAFRIKDDIVNSLQKMQNKGGGDRLARLFLEEHIRNITAIVKQLNRDIEVLQEQIRARDNISYGTNSALKTLEMRQLSGLGDLRGRVARCDASIARLSAEHKTTYEGLQHLNKEQQAAKLILETKIKDAEGQISQLLNRVDLSISEQSTKLKMSHRDSNHQLQLLDTKFKGTVEELSNQILSARSWLQQEQERIEKELLQKIDQLSLIVKENSGASERDMEKKLSQMSARLDKIEEGQKKTFDGQRTRQEEEKMHGRITKLELQMNQNIKEMKAEVNAGFTAVYESIGSLRQVLEAKMKLDRDQLQKQIQLMQKPETPM
Protein: Beta-site APP-cleaving enzyme, isoform A (Beta-site APP-cleaving enzyme, isoform B (EC 3.4.23.-)) (GH11417p) (Q9VLK3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cathepsin B, isoform A)
- cathepsin L
- Cathepsin L1
- FI04419p
- Cathepsin F
- Amyloid-beta-like protein
- Trypsin alpha
- RH58587p
- Presenilin homolog
- Vacuolar protein sorting-associated protein 35
Sequence:
MFKTIAVVVLLAALASAELHRVPILKEQNFVKTRQNVLAEKSYLRTKYQLPSLRSVDEEQLSNSMNMAYYGAISIGTPAQSFKVLFDSGSSNLWVPSNTCKSDACLTHNQYDSSASSTYVANGESFSIQYGTGSLTGYLSTDTVDVNGLSIQSQTFAESTNEPGTNFNDANFDGILGMAYESLAVDGVAPPFYNMVSQGLVDNSVFSFYLARDGTSTMGGELIFGGSDASLYSGALTYVPISEQGYWQFTMAGSSIDGYSLCDDCQAIADTGTSLIVAPYNAYITLSEILNVGEDGYLDCSSVSSLPDVTFNIGGTNFVLKPSAYIIQSDGNCMSAFEYMGTDFWILGDVFIGQYYTEFDLGNNRIGFAPVA
Protein: Programmed cell death protein 2 (Zinc finger protein Rp-8) (P47816)
Organism: Rattus norvegicus (Rat)
Function: May be a DNA-binding protein with a regulatory function. May play an important role in cell death and/or in regulation of cell proliferation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein LTV1 homolog
- Constitutive coactivator of peroxisome proliferator-activated receptor gamma
Sequence:
MAAVVPVTVELGFVEEAPAWRLRSEQFPSKVGGRPAWLALAELPGPGALACARCGRPLAFLLQVYAPLPGRDEAFHRSLFLFCCREPLCCAGLRVFRNQLPRKNAFYSYEPPSETGASDTECVCLQLKSGAHLCRVCGCLAPMTCSRCKQAHYCSKEHQTLDWQLGHKQACTQSDHLDHMVPDHNFLFPEFEIVTETEDEIGPEVVEMEDYSEVIGSMEGVPEEELDSMAKHESKEDHIFQKFKSKIALEPEQILRYGRGIKPIWISGENIPQEKDIPDCSCGAKRIFEFQVMPQLLNHLKADRLGTSVDWGILAVFTCAESCSLGIGYTEEFVWKQDVTETP