wanglab/gogpt-training-data huggingface dataset:
Protein: Homeobox protein cut-like (A0A2R8Y852)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MAANVGSMFQYWKRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGSARRKGKDQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAGLSQDFFSSSLASPSLPLASTGKFALNSLLQRQLMQSFYSKAMQEAGSTSMIFSTGPYSTNSISSQSPLQQSPDVNGMAPSPSQSESAGSVSEGEEMDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEPFHKMKQFLSDEQNILALRSIQGRQRAEPAQPSSASGSGNSDDAIRSILQQARREMEAQQAALDPALKQAPLSQSDITILTPKLLSTSPMPTVSSYPPLAISLKKPSAAPEAGASALPNPPALKKEAQDAPGLDPQGAADCAQGVLRQVKNEVGRSGAWKDHWWSAVQPERRNAASSEEAKAEETGGGKEKGSGGSGGGSQPRAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASRSETPQNSPLPSSPIVPMSKPTKPSVPPLTPEQYEVYMYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREPFIRMQLWLNGELGQGVLPVQGQQQGPVLHSVTSLQDPLQQGCVSSESTPKTSASCSPAPESPMSSSESVKSLTELVQQPCPPIEASKDSKPPEPSDPPASDSQPTTPLPLSGHSALSIQELVAMSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREPFVRMQLWLNDPNNVEKLMDMKRMEKKAYMKRRHSSVSDSQPCEPPSVGTEYSQGASPQPQHQLKKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRELFIEEIQAGSQGQAGASDSPSARSGRAAPSSEGDSCDGVEATEGPGSADTEEPKSQGEAEREEVPRPAEQTEPPPSGTPGPDDARDDDHEGGPVEGPGPLPSPASATATAAPAAPEDAATSAAAAPGEGPAAPSSAPPPSNSSSSSAPRRPSSLQSLFGLPEAAGARDSRDNPLRKKKAANLNSIIHRLEKAASREEPIEWEF
Protein: Serine/threonine-protein kinase rio2 (EC 2.7.11.1) (Q9P7W5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the final endonucleolytic cleavage of 20S pre-rRNA at site D in the cytoplasm, converting it into the mature 18S rRNA. Involved in normal export of the pre-40S particles from the nucleus to the cytoplasm (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-rRNA-processing protein pno1
- 20S-pre-rRNA D-site endonuclease nob1
- Protein LTV1
- Ribosome biogenesis protein tsr1
- Uncharacterized protein C13G1.09
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS21
Sequence:
MVNLNIKAMRYLSAEDFRTLTAVEMGSRNHEVVPTNMINQIAKIRGGSCTKSLSVLFMHKLIAKVPHISYEGYRLTYAGYDYLALKALSKRASVYSVGNQIGVGKESDVYVVGDQKGKQYILKIHRLGRISFRSVKNNRDYLRNRKTGSWQYLSRLAATKEFAFMKILHEHGFPVPAPIDHSRHCIIMEMIDAFPLRAVTDIRDPPALYQTLMDIIVRFARNGLIHGDFNEFNIIVREDGTAVVIDFPQMVSTSHPDAQFYFDRDVQCIVQYFEKNYQYKGDVPNFEDISKMEKENNLDIMIEASGFNKKQSKELEKYRQEEEKRKENGDDLSDNYEEEEEEKE
Protein: TRP-like ion channel pkd2 (Polycystic kidney disease-related ion channel 2) (Q09917)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a key signaling component in the regulation of cell shape and cell wall synthesis through interaction with GTPase Rho1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15537393}; Multi-pass membrane protein {ECO:0000269|PubMed:15537393}. Golgi apparatus membrane {ECO:0000269|PubMed:15537393}; Multi-pass membrane protein {ECO:0000269|PubMed:15537393}.
Interaction partners:
- Uncharacterized membrane protein C1322.03
Sequence:
MRLWRSPLLLLVVVVELFSWADALTRFISADSLSTCMTDSQLSASKLYASYFPDNQSVAFDISIQSLVSTNVSIDVDISAYGIEIKKVIDPCDMEISGFCPMQTGNIALSGSHTLTGEALSILDSIPSIAYTVPDLDAVVTINIYESDTNTQLACVRTTVQNGRSVYHRAVYWVMCMVIGIPLLIFLLISPVLQTPALWEIVETMITLFQFAQIQALYSMMATSLPAIIYSWGRNFMWSMGIIRIGFMQDVFTWYVKSTGGTPSTLVDLGIHANVALAKRGIDLGSLAKRATTTVTTSTSDSITLRGIKRISYMMGIETTNFFATGFSFFIILLFFSLLVAMASRFIVEMVLLASRNQALKKQRIRLYWKSISKGFFYRVIFVGFTQMSVLSMWEIYTRDSSALAFLSMYVIVDMAVLLCYAFVRTIQIIRKTGPYSHPDVLYNLYSDTQHLMRWGFMYVQLDVRFFYFTFPLLLITLVRSMFIGFGQGSPKVQGCAMFGISVVVFALMVILRPYATKHMNTLHIGVALMNLISGSFILVMCQAFYVEELARQVIGIIFFALNAITMLLLILGIFIRTLIVLFRKSGHGTYYRILDDQSEKATSYNKSIKDMSSSDMAFSDPAYSGTTLRSSVDLNTPEYPFSNRNDSDSTFTNNKYVSPWDAIEEASYANLRGNTDVEQPFMESDYTRISENNNNAERRRKPLPNNAFR
Protein: S-(+)-linalool synthase, chloroplastic (EC 4.2.3.25) (Terpenoid synthase 14) (AtTPS14) (Q84UV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in monoterpene (C10) biosynthesis. The major product is (S)-linalool.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Tricyclene synthase, chloroplastic
- Beta-myrcene/
- Cytochrome P450 71B31
- 1,8-cineole synthase 1, chloroplastic
- Solanesyl diphosphate synthase 3, chloroplastic/mitochondrial)
- Cytochrome P450 76C3
- Probable alpha,alpha-trehalose-phosphate synthase 11
- Farnesyl pyrophosphate synthase 1, mitochondrial
- Farnesyl pyrophosphate synthase 2
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2
Sequence:
MALIATKISSRSCFVSAYPNNSPTFLISKFPNTVDSLSPANTAKRSILRNVHASVSNPSKQFHNKTSLEYLHELNIKKIKNILSANVDVPSENLEMIDVIQSLGIDLHFRQEIEQTLHMIYKEGLQFNGDLHEIALRFRLLRQEGHYVQEIIFKNILDKKGGFKDVVKNDVKGLTELFEASELRVEGEETLDGAREFTYSRLNELCSGRESHQKQEIMKSLAQPRHKTVRGLTSKRFTSMIKIAGQEDPEWLQSLLRVAEIDSIRLKSLTQGEMSQTFKWWTELGLEKDVEKARSQPLKWHTWSMKILQDPTLTEQRLDLTKPISLVYVIDDIFDVYGELEELTIFTRVVERWDHKGLKTLPKYMRVCFEALDMITTEISMKIYKSHGWNPTYALRQSWASLCKAFLVEAKWFNSGYLPTTEEYMKNGVVSSGVHLVMLHAYILLGEELTKEKVELIESNPGIVSSAATILRLWDDLGSAKDENQDGTDGSYVECYLNEYKGSTVDEARTHVAQKISRAWKRLNRECLNPCPFSRSFSKACLNIARTVPLMYSYDDDQRLPDEYLKSLM
Protein: Cryptochrome-1 (DmCRY1) (dcry) (Blue light photoreceptor) (O77059)
Organism: Drosophila melanogaster (Fruit fly)
Function: Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry. Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate. Required for both the naive and trained responses to magnetic field, consistent with the notion that cry is in the input pathway of magnetic sensing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Nucleus {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Note=Nuclear translocation initiates after the perception of a light signal. Accumulates in the perinuclear region about one hour before translocation into the nucleus. Translocation occurs through interaction with other Clock proteins such as tim and per. {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}.
Interaction partners:
- Protein timeless
- Protein cycle
- Jetlag, isoform A
- Period circadian protein
- Circadian locomoter output cycles protein kaput
- Timeout
- GH23983p
- Discs overgrown protein kinase
- Crystallin, isoform A
- Protein kinase shaggy
Sequence:
MATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQMFLHTVQIIGLPPRPTADARLEDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKVEQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWREYFYTMSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHGLQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQEQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLADVVV
Protein: Acyl-coenzyme A oxidase (Q9VIX4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- Probable enoyl-CoA hydratase, mitochondrial
- Sterol carrier protein 2
- acetyl-CoA C-acyltransferase
- Peroxisomal multifunctional enzyme type 2
- Trifunctional enzyme subunit alpha, mitochondrial
- Acetyl-CoA acetyltransferase 2
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acetyl-coenzyme A synthetase
- HL08109p)
- Acetyl-CoA acetyltransferase 1, isoform A)
Sequence:
MGSEDTSFIPDLPSGGPLAVYRKRANFDWKRLRLIFEKEQGLRIKYKVWRRLENDPLFAHPSRTLPMDEQKRLCAMQVNRMKHLDLVPKEIESLSFSAKTKYLMYINEALACYSPSLSVKIALGVGLFNNAIRAMGTEKHQKYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDPTTQEFVINTPDFEAAKCWVGNLGKTATVAMTFANLYTADGQNHGLHGFLIPIRDPKTLLSYPGVLVGDIGEKCGLNGIDNGFVVFTNYRIPRDNLLNRTSDVTPEGVYESVFTEPGKVLGAALESFSAGRIGIMQESANTLCSAAVIAVRYSAVRKQFGPERHGEEMAILEYQLHQYRIFPYLAAACVQKIATEELTSTYMEIIARSQADSNGFDVLTQNAAEIHALISSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQASNWLLRQWSAKELETPIGSVKFLERRSELLALNYASLAQKTPIASWQFSLRCYEWLLCHLMAKTTAHIEGQLAAGSSKFEARNNSQVAGARELSLAYAEYYALTRYVDHVSTLTVEAPYASVLRLLFDVYAMWLLEKHMTTFYVGGFAAGRDFSAAVRQLLLDSCLKLKDVAVSVADAISPPDFALNSVIARADGLLYENLQNEFMTNEGAFQRPSWWRDVIIPQAQSKL
Protein: 5'-3' exonuclease PLD4 (EC 3.1.16.1) ((S,S)-bis(monoacylglycero)phosphate synthase PLD4) (EC 3.1.4.-) (Phospholipase D family member 4) (Phospholipase D4) (Q8BG07)
Organism: Mus musculus (Mouse)
Function: 5'->3' DNA exonuclease which digests single-stranded DNA (ssDNA). Regulates inflammatory cytokine responses via the degradation of nucleic acids, by reducing the concentration of ssDNA able to stimulate TLR9, a nucleotide-sensing receptor. Involved in phagocytosis of activated microglia.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21085684}; Single-pass type II membrane protein {ECO:0000305|PubMed:21085684}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21085684}; Single-pass type II membrane protein {ECO:0000305|PubMed:21085684}. Nucleus {ECO:0000269|PubMed:22102906}. Early endosome {ECO:0000305|PubMed:22102906}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:22102906}. Lysosome {ECO:0000250|UniProtKB:Q8IV08}. Note=Activation of microglia induces translocation of PLD4 from the nucleus to the phagosomes. {ECO:0000269|PubMed:22102906}.
Interaction partners:
- Phospholipase D2
- Phospholipase D1
- 5'-3' exonuclease PLD3
- Lysophospholipid acyltransferase 5
- Phosphatidylethanolamine N-methyltransferase
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Phospholipase A and acyltransferase 3
- Phosphatidylcholine-sterol acyltransferase
- Plasmanylethanolamine desaturase 1
- Phosphatidylserine synthase 2
Sequence:
MDKKKEHPEMRIPLQTAVEVSDWPCSTSHDPHSGLGMVLGMLAVLGLSSVTLILFLWQGATSFTSHRMFPEEVPSWSWETLKGDAEQQNNSCQLILVESIPEDLPFAAGSPTAQPLAQAWLQLLDTARESVHIASYYWSLTGLDIGVNDSSSRQGEALLQKFQQLLLRNISVVVATHSPTLAKTSTDLQVLAAHGAQIRQVPMKQLTGGVLHSKFWVVDGRHIYVGSANMDWRSLTQVKELGAIIYNCSNLAQDLEKTFQTYWVLGTPQAVLPKTWPRNFSSHINRFHPLRGPFDGVPTTAYFSASPPSLCPHGRTRDLDAVLGVMEGARQFIYVSVMEYFPTTRFTHHARYWPVLDNALRAAALNKGVHVRLLVSCWFNTDPTMFAYLRSLQAFSNPSAGISVDVKVFIVPVGNHSNIPFSRVNHSKFMVTDKTAYVGTSNWSEDYFSHTAGVGLIVSQKTPRAQPGATTVQEQLRQLFERDWSSHYAMDLDRQVPSQDCVW
Protein: DNA replication terminus site-binding protein (Ter-binding protein) (P16525)
Organism: Escherichia coli (strain K12)
Function: Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.
Subcellular location: Cytoplasm.
Interaction partners:
- Replicative DNA helicase DnaB
- Chromosomal replication initiator protein DnaA
- ATP-dependent DNA helicase RecG
- Ribonuclease HI
- Replicative helicase loader DnaC
- Protein RecA
Sequence:
MARYDLVDRLNTTFRQMEQELAIFAAHLEQHKLLVARVFSLPEVKKEDEHNPLNRIEVKQHLGNDAQSLALRHFRHLFIQQQSENRSSKAAVRLPGVLCYQVDNLSQAALVSHIQHINKLKTTFEHIVTVESELPTAARFEWVHRHLPGLITLNAYRTLTVLHDPATLRFGWANKHIIKNLHRDEVLAQLEKSLKSPRSVAPWTREEWQRKLEREYQDIAALPQNAKLKIKRPVKVQPIARVWYKGDQKQVQHACPTPLIALINRDNGAGVPDVGELLNYDADNVQHRYKPQAQPLRLIIPRLHLYVAD
Protein: Adhesion G-protein coupled receptor G1 (G-protein coupled receptor 56) (Protein TM7XN1) [Cleaved into: ADGRG1 N-terminal fragment (ADGRG1 NT) (GPR56 N-terminal fragment) (GPR56 NT) (GPR56(N)) (GPR56 extracellular subunit) (GPR56 subunit alpha); ADGRG1 C-terminal fragment (ADGRG1 CT) (GPR56 C-terminal fragment) (GPR56 CT) (GPR56(C)) (GPR56 seven-transmembrane subunit) (GPR56 7TM) (GPR56 subunit beta)] (Q9Y653)
Organism: Homo sapiens (Human)
Function: Receptor involved in cell adhesion and probably in cell-cell interactions. Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells. Receptor for collagen III/COL3A1 in the developing brain and involved in regulation of cortical development, specifically in maintenance of the pial basement membrane integrity and in cortical lamination (By similarity). Binding to the COL3A1 ligand inhibits neuronal migration and activates the RhoA pathway by coupling to GNA13 and possibly GNA12. Plays a role in the maintenance of hematopoietic stem cells and/or leukemia stem cells in bone marrow niche (By similarity). Plays a critical role in cancer progression by inhibiting VEGFA production threreby inhibiting angiogenesis through a signaling pathway mediated by PRKCA. Plays an essential role in testis development (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21349848, ECO:0000269|PubMed:24949629}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [ADGRG1 N-terminal fragment]: Secreted {ECO:0000269|PubMed:21349848}.; SUBCELLULAR LOCATION: [ADGRG1 C-terminal fragment]: Membrane raft {ECO:0000269|PubMed:24949629}. Note=Interaction with its ligand COL3A1 leads to the release of ADGRG1 NT from the membrane and triggers the association of ADGRG1 CT with lipid rafts. {ECO:0000269|PubMed:24949629}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Protein-glutamine gamma-glutamyltransferase 2
- Guanine nucleotide-binding protein G
- CD9 antigen
- Collagen alpha-1
Sequence:
MTPQSLLQTTLFLLSLLFLVQGAHGRGHREDFRFCSQRNQTHRSSLHYKPTPDLRISIENSEEALTVHAPFPAAHPASRSFPDPRGLYHFCLYWNRHAGRLHLLYGKRDFLLSDKASSLLCFQHQEESLAQGPPLLATSVTSWWSPQNISLPSAASFTFSFHSPPHTAAHNASVDMCELKRDLQLLSQFLKHPQKASRRPSAAPASQQLQSLESKLTSVRFMGDMVSFEEDRINATVWKLQPTAGLQDLHIHSRQEEEQSEIMEYSVLLPRTLFQRTKGRSGEAEKRLLLVDFSSQALFQDKNSSQVLGEKVLGIVVQNTKVANLTEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGCETVRRETQTSCFCNHLTYFAVLMVSSVEVDAVHKHYLSLLSYVGCVVSALACLVTIAAYLCSRVPLPCRRKPRDYTIKVHMNLLLAVFLLDTSFLLSEPVALTGSEAGCRASAIFLHFSLLTCLSWMGLEGYNLYRLVVEVFGTYVPGYLLKLSAMGWGFPIFLVTLVALVDVDNYGPIILAVHRTPEGVIYPSMCWIRDSLVSYITNLGLFSLVFLFNMAMLATMVVQILRLRPHTQKWSHVLTLLGLSLVLGLPWALIFFSFASGTFQLVVLYLFSIITSFQGFLIFIWYWSMRLQARGGPSPLKSNSDSARLPISSGSTSSSRI
Protein: WW domain binding protein 2 (K7EMC9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALNKNHSEGGGVIVNNTESILMSYDHVELTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLSKGKDAMQSFMMPFYLMKDCEIKQPVFGANYIKGTVKAEAGGGWEGSASYKLTFTAGGAIEFGQRMLQVASQASRGEVPSGAYGYSYMPSGAYVYPPPVANGMYPCPPGYPYPPPPPGPPMMDGAMGYVQPPPPPYPGPMEPPVSGPDVPSTPAAEAKAAEAAASAYYNPGNPHNVYMPTSQPPPPPYYPPEDKKTQ
Protein: t-SNARE coiled-coil homology domain-containing protein (Q5B4W4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Vesicle transport v-SNARE protein vti1
- Vesicular-fusion protein sec17
- Synaptobrevin homolog YKT6
- Vacuolar sorting protein
- Golgi SNAP receptor complex member 1
- Synaptobrevin homologue SNC1/2
- Protein transport protein SEC9
- SNARE complex subunit
- Vacuolar assembly protein, putative
- Vesicular-fusion protein SEC18
Sequence:
MSFNHLSSLESQPTTYRRSDDPQYHDDPEFQRLTESLSNQLFTLTSNITRLSDQIALLGTKRDTERVRERVHNLLEQTRTGFRDVGEGIKKVQNWEDVNPSQKWTQQKLSTEFKATLEEFQTIQRRALEKQRASAVAARTAVEEAGHSTEDDAQQQQQQQLLEVEQPRLANQDEVDFQEALIIEREAEIRNIEQSVGELNELFRDVAHIVHEQGEQLDTISGNVENVHANTQGANVELRSASRYQKNARTKACCLLIILAVILAIIILAAVLG
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (Q95V83)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MNWAIYLLLALISLGRATPVPNRQYSCMSYQEDDNSFHDDDGDQDSSGELQEQQVESTPIPSEPHRRTCPDGYTFCFTIWNQTANGARVVKQGCWKDNTDRTSICSQSECTSSAPTSKTSSLYYCCCSGGVCNAQYSVVEPAPLELGSNEGRTSITNRATEKQHQSFLASTMLGLAGGLTALTIGIFLAVQYCRTAKEKPEPEESPLAPSGPGYSSNLRNVDNMNLIGMLGSGKYGTVMKGLLHDQEVAVKIYPEEHHQYYVNERNIYALPLMECPALLSYFGYDERCTMDGRMEYQLVLSLAPLGCLQDWLIANTLTFSECCGMLRSITRGISHLHTELRLGDQHKPCVAHRDINTRNVLVQADLSCCIADFGFALKVFGSKYEYKGEVAMAETKSINEVGTLRYMAPELLEGAVNLRDCETSLKQMDVYALGLVLWEVATRCSDFYAPGQATPPYKAPYEQEVGSHPSFDQMQALVVRHKARPLFPTGWGGGAAAKVVRDTCEDCWDHDADARLTSLCAEERMQEMSTLRPRAQAQPSSPLLNTNNLVASPTAEQGINIIATTTTAAAVHHQMSSDTTGLIQPPPNQQIPLAALEREKNHLSYPQQQLQPYQGRNPCQERNLAPLTMRTPPVLVERSKKHSFQTQPQENSLSCLEHDVSVEELIASHQHQQQKNTIVSTGGNGNSCLGQGFPKQQNTDQKLRGWHGVRALIHKKLFRKEHAEELCRQLQLGEEKSNLVTALRRPNNLDLSPRLDKPPPDQLRSAEQRMGTPAHIVPRSLSSSLIKHINGTTNNNSIQSHGSELQTLTRPASKRRPGHLRTNSLMATTGQGPPTEQQMRRQHSLEVFREVFSGRGSSERLRDPSERVKTPGDVPPSVRKARASKTLSLYDDRMMDSSLLNIL
Protein: Non-muscle caldesmon (CDM) (L-caldesmon) (Q62736)
Organism: Rattus norvegicus (Rat)
Function: Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P13505}. Cytoplasm, myofibril {ECO:0000250|UniProtKB:P13505}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:P13505}. Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle). {ECO:0000250|UniProtKB:P13505}.
Interaction partners:
- Leiomodin-1
- Calmodulin-1
- Actin, aortic smooth muscle
- Myosin regulatory light polypeptide 9
- Myosin regulatory light chain 12B
- Calmodulin-like protein 3
- Calmodulin-like protein 4
Sequence:
MLSRSGSQGRRCLATLSQIAYQRNDDDEEEAARERRRRARQERLRQKQEEESLGQVTDQVEAHVQNSAPDEESKPATANAQVEGDEEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSVPSRRMQNNSAENETAEGEEKGESRSGRYEMEETEVVITSYQKNSYQDAEDKKKEEKEEEEEEEKLKGGNLGENQIKDEKIKKDKEPKEEVKNFLDRKKGFTEVKAQNGEFMTHKLKQTENAFSPSRSGGRASGDKEAEGAPQVEAGKRLEELRRRRGETESEEFEKLKQKQQEAALELEELKKKREERRKVLEEEEQRRKQEEADRKAREEEEKRRLKEEIERRRAEAAEKRQKMPEDGLSEDKKPFKCFTPKGSSLKIEERAEFLNKSVQKSGVKSTHQAAVVSKIDSRLEQYTNAIEGTKASKPMKPAASDLPVPAEGVRNIKSMWEKGSVFSSPSASGTPNKETAGLKVGVSSRINEWLTKSPDGNKSPAPKPSDLRPGDVSGKRNLWEKQSVDKVTSPTKV
Protein: Hexosyltransferase (EC 2.4.1.-) (Q80VD4)
Organism: Mus musculus (Mouse)
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004447, ECO:0000256|RuleBase:RU364016}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004447, ECO:0000256|RuleBase:RU364016}.
Interaction partners:
Sequence:
MRLSSLLALLRPVLPLILGLSLGCSLSLLRVSWIQGEGEDPCVEAVGKPGGPQNPDSKNGLDQGDEDFRPRIVPYYRDPNKPYKKVLRTRYIQTELGSRERLLVAVLTSRATLSTLAVAVNRTVAHHFPRLLYFTEQLNRRYQPRLRFRKQRLLNGYRRFDPARGMEYTLDLLLEAVTQRGHRRSLARRVSLLRPLSRVEILPMPYVTEATRVQLVLPLLVAEAPAALAFLEAFAASVLEPREHALLTLLLVYGPREGRGGPDPFLGVKAAAAELERRYPGARLAWLAVRAEAPSQVRLMDVISKKHPVDTLFFLTTVWTRPGSEVLNRCRMNAISGWQAFFPVHFQEFNPALSPQRSPPGVPGADPPSPGVDPSRGAPVGGRFDRQASAEGCFYNADYLAARARLAGELAGQEEEEALEGLEVMDVFLRFSGLHLFRAVEPGLVQKFSLRDCSPRLSEELYHRCRLSNLEGLGARTQLAMALFEQEQANST
Protein: Melanoma antigen family A, 2B (Q96E03)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQQTASSSSTLVEVTLGEVPAADSPSPPHSPQGASSFSTTINYTLWRQSDEGSSNQEEEGPRMFPDLESEFQAAISRKMVELVHFLLLKYRAREPVTKAEMLESVLRNCQDFFPVIFSKASEYLQLVFGIEVVEVVPISHLYILVTCLGLSYDGLLGDNQVMPKTGLLIIVLAIIAIEGDCAPEEKIWEELSMLEVFEGREDSVFAHPRKLLTQDLVQENYLEYRQVPGSDPACYEFLWGPRALIETSYVKVLHHTLKIGGEPHISYPPLHERALREGEE
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q5M7Y2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- GTPase NRas
- HRas proto-oncogene, GTPase a.
- Mitogen-activated protein kinase kinase 1
- Dual specificity mitogen-activated protein kinase kinase 2
- Mitogen-activated protein kinase kinase 2b
- small monomeric GTPase
- small monomeric GTPase
- RAS-related 2
- Muscle RAS oncogene homolog
- Ras-related protein M-Ras
Sequence:
MSNTSSCSSSGETSPDDTPRGGGTIRVYLPNKQRTVVNVRPGQTVYDSLDKALKVRGLSQDCCAVFRLLEGRKRLTEWDTDITPLVGEELLVEVLDDVPLTMHNFVRKTFFKLAYCDFCHKFLFNGFRCQTCGYKFHQHCSSKVPTVCVDMDTMTKRCVNNTEDCPAILIYPATNSISQSDLPLTSDSPGGELPSSPSNFCLFIRGEDGQSLQRHRSTSTPNVHMVSTLEPGAAGLLEEPFKISTVGYESSPKPSTSPPHLGSPGRKPPKSPSEPKERKQSSSDDKKKVHRGGYRDSSYYWEVHPREVSMLKRIGAGSFGTVFKGKWHGDVAIKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAIITQWCEGSSLYRHLHVTETKFDTMRRIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGWTVKIGDFGLATVKSRWSGSQQVEQPSGSILWMAPEVIRMQDTNPYTFQSDVYGYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSPDLSKLYSNCPKSMKRLIIDCLKFKRDERPLFPQILVSIEQVQELLPKIERSASEPSLHRAVHAEDLNPLLLHTTRFL
Protein: Synaptopodin 2-like protein (Q8BWB1)
Organism: Mus musculus (Mouse)
Function: Actin-associated protein that may play a role in modulating actin-based shape.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Myozenin-1
Sequence:
MGAEEEVQVTLAGGAPWGFRLQGGTEQRKPLQIRRRSQAGRAGLRERDQLLAINGVSCTNFSHASAMTLIDASGRQLVLTVRRVTDEGSVRSPSPGELQVLSPLSPLSPEPPGAPVSQALQPTSLRSPPDSEAYYGETDSDVDGPATQEKPRRTRRRGPARPSLPGAPPDEVYLSDSPAEPAPVKTGSPSQGDSRVSSPSWEEGAALQPPPAEALLLPHGPLRPGPHLIPMVGPVPHPVAEDLTTTYTQKAKQAKLQRAESLQEKSVKEARTKCRTIASLLTAAPNPHSKGVLMFKKRRQRAKKYTLVSFGAAAGTGTEEEDGIPPTSESELDEETFSDARSLTNQSDWDSPYLDMELARAGLGTAESQNSGLGGQLSEVSGRGVQLFEQQRQRVASSSQELAQVGPAAMLNGQSLQSPPRAQSAPPEAAVLPLSPLSVPAVSPTPFFPDGGAPIPAPSIFNRSARPFTPGLQGQRSGTTSVIFRPLAPKKVNEGLGSTSPAPSPFAAPPQGPTPLPSFTTVVPSHTPVSGASSSTQRSSGPVTATSSLYIPAPSRPVTPGGAPEPPTPPSAAAMTSTASIFLSTPLRNSARPEAPGPAVPEPASVREQRISVPAARTGILQEARRRGTRKQMFRPGKEETKNSPNPELLSLVQNLDEKPRAGGAESGPEEDALSLGAEACNFMQPLGGRSYKTLPQVSPKTPPPMAPKTPPPTTPKTPPPVAPKPGSRGLLDGLVNGSTPMVGIPEPPRLQGRGGELFAKRQSRADRYVVEATSGSSLNPGLRPRSPSPTPSLPPSWKYSPNIRAPPPIAYNPLLSPFFPQAARTLPNKAQSQGPRVTPKQGIKALDFMRHQPYQLKTAMFCFDEGSSTPGPTSGPPKTARVQEIRRFSTPAPQPTAEPLAPTVLVPRAATTLDEPIWRAELASTPVPNPDHQESLRSFAAAPSSCGFQVARPRFSATRTGLQAHVWRPGAGHQ
Protein: Rhamnogalacturonase A (RGase A) (RHG A) (EC 3.2.1.171) (Q5ARE6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins. Active against linseed rhamnogalacturonan.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Pectin lyase B
- Pectin lyase A
- Probable pectin lyase F
Sequence:
MYVSRLLLFLAPLLVKGQLSGSVGPLTSVSSKSQTKTCNVLDYGAVADKSTDIGPALSSAWDECADGGVVYIPPGDYAIETWVKLSGGKACAIQLDGIIYRTGTDGGNMIMIEHTSDFEFFSSTSKGAFQGYGYEFHAKGSSDGPRILRLYDVSDFSVHDVALVDSPLFHFSMDTCSNGEVYNMAIRGGNMGGLDGIDVWSTNVWIHDVEVTNKDECVTVKSPSKNILVENIYCNWSGGCAMGSLGTDTDISDIVYRNVYTWKSNQMYMVKSNGGSGTVSNLVLENFIGHGNAYSLDIDSAWSSMSTIEGDGVELKNVTIRNWKGTEADGSQRGPIKVKCASGAPCTDVTVEDFAMWTESGDEQTYVCENAFGDGFCLADGDGTSTFTTTLTASAAPSGYSAPSMDADLETAFGTDSEIPIPTIPTSFYPGATPYSALAGASVSSSQVPAASSSAEAKFVASPATSSPTATSTAISSVDPVSAATTTATSHGHGKSHHKHQCRAHRH