wanglab/gogpt-training-data huggingface dataset:
Protein: Protein swallow (P40688)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has a role in localizing bicoid mRNA at the anterior margin of the oocyte during oogenesis, and a poorly characterized role in nuclear divisions in early embryogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:1806330, ECO:0000269|PubMed:7507030}. Note=Uniformly distributed in eggs, becomes localized to the nuclei during early mitotic divisions in early embryogenesis. Enters each nucleus at the beginning of mitosis, occupies a position complementary to that of condensed chromatin, and leaves each nucleus at the end of mitosis.
Interaction partners:
- Dynein light chain 1, cytoplasmic
- Dynein light chain 2, cytoplasmic
- Poly
- Maternal effect protein oskar
- Protein matrimony
- Cdc25-like protein phosphatase twine
- CG5272 protein
- Chorion peroxidase
- EG:8D8.1 protein
- pH-sensitive chloride channel 2
Sequence:
MSLQDESFPTDELFDQLNNLSSSGARNTWFAEHHKPAVFERDTAPFLEICYADPDFDADGDVANKSAKTCVSDPVGRDQEDEDDYDEDVDGDDHKLGCEKAPLGSGRSSKAVSYQDIHSAYTKRRFQHVTSKVGQYIAEIQAQDQKRRNVKFAGFQRVNSMPESLTPTLQQVYVHDGDFKVDKNCQTHSNSDSNYNSNSNNSSSSFDRLLAENESLQQKINSLRVEAKRLQGFNEYVQERLDRKTDDFVKMKCNFETLRTELSECQQKLRRQQDNSQHHFMYHIRSATSAKATQTDFLVDTIPASGNVLVTPHPLGDLTYNSSKGSIELALLSVAPSARVAQNPVQVQRAIHPQSLDFSSVSTEADGSGSGEHRVETSSRALVRRTPAPNNSETSQPSSNDSAIEVEAHEEERPSSRRQWEQQGELISPRQWGQHEGMYYFDKRNNRVIEVMGFNISQGRNQSHDTIHNQSINDSQTRLLVHSMSMSHLEAHDHFRSKRTTLGSRMLRFLGPCVRCRNGDPLNRSNVTYKDGLPAMPEEEFVDQRNQR
Protein: Protein SPIRAL1-like 2 (Q9LE54)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts redundantly with SPR1 in maintaining the cortical microtubules organization essential for anisotropic cell growth.
Interaction partners:
- ABC transporter A family member 5
- Tetratricopeptide repeat
- CRS1 / YhbY
- At1g11210)
- F28K20.8 protein
- Myb family transcription factor PHL12
- Root phototropism protein 2
- 23.6 kDa heat shock protein, mitochondrial
- Dehydration-responsive element-binding protein 1F
Sequence:
MGRGVSAGGGQSSLGYLFGSGEAPKLAAVNKTPAETESSAHAPPTQAAAANAVDSIKQVPAGLNSNSANNYMRAEGQNTGNFITDRPSTKVHSAPGGGSSLDYLFGGGSN
Protein: Zinc finger and BTB domain-containing protein 40 (Q9NUA8)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- WD repeat-containing protein WRAP73
- Multiple epidermal growth factor-like domains protein 6
Sequence:
MELPNYSRQLLQQLYTLCKEQQFCDCTISIGTIYFRAHKLVLAAASLLFKTLLDNTDTISIDASVVSPEEFALLLEMMYTGKLPVGKHNFSKIISLADSLQMFDVAVSCKNLLTSLVNCSVQGQVVRDVSAPSSETFRKEPEKPQVEILSSEGAGEPHSSPELAATPGGPVKAETEEAAHSVSQEMSVNSPTAQESQRNAETPAETPTTAEACSPSPAVQTFSEAKKTSTEPGCERKHYQLNFLLENEGVFSDALMVTQDVLKKLEMCSEIKGPQKEMIVKCFEGEGGHSAFQRILGKVREESLDVQTVVSLLRLYQYSNPAVKTALLDRKPEDVDTVQPKGSTEEGKTLSVLLLEHKEDLIQCVTQLRPIMESLETAKEEFLTGTEKRVILNCCEGRTPKETIENLLHRMTEEKTLTAEGLVKLLQAVKTTFPNLGLLLEKLQKSATLPSTTVQPSPDDYGTELLRRYHENLSEIFTDNQILLKMISHMTSLAPGEREVMEKLVKRDSGSGGFNSLISAVLEKQTLSATAIWQLLLVVQETKTCPLDLLMEEIRREPGADAFFRAVTTPEHATLETILRHNQLILEAIQQKIEYKLFTSEEEHLAETVKEILSIPSETASPEASLRAVLSRAMEKSVPAIEICHLLCSVHKSFPGLQPVMQELAYIGVLTKEDGEKETWKVSNKFHLEANNKEDEKAAKEDSQPGEQNDQGETGSLPGQQEKEASASPDPAKKSFICKACDKSFHFYCRLKVHMKRCRVAKSKQVQCKECSETKDSKKELDKHQLEAHGAGGEPDAPKKKKKRLPVTCDLCGREFAHASGMQYHKLTEHFDEKPFSCEECGAKFAANSTLKNHLRLHTGDRPFMCKHCLMTFTQASALAYHTKKKHSEGKMYACQYCDAVFAQSIELSRHVRTHTGDKPYVCRDCGKGFRQANGLSIHLHTFHNIEDPYDCKKCRMSFPTLQDHRKHIHEVHSKEYHPCPTCGKIFSAPSMLERHVVTHVGGKPFSCGICNKAYQQLSGLWYHNRTHHPDVFAAQNHRSSKFSSLQCSSCDKTFPNTIEHKKHIKAEHADMKFHECDQCKELFPTPALLQVHVKCQHSGSQPFRCLYCAATFRFPGALQHHVTTEHFKQSETTFPCELCGELFTSQAQLDSHLESEHPKVMSTETQAAASQMAQVIQTPEPVAPTEQVITLEETQLAGSQVFVTLPDSQASQASSELVAVTVEDLLDGTVTLICGEAK
Protein: Nucleobindin-1 (Bone 63 kDa calcium-binding protein) (CALNUC) (Q63083)
Organism: Rattus norvegicus (Rat)
Function: Major calcium-binding protein of the Golgi which may have a role in calcium homeostasis. Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates alpha subunits of guanine nucleotide-binding proteins (G proteins).
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:10639138, ECO:0000269|PubMed:9647645}; Peripheral membrane protein {ECO:0000269|PubMed:9647645}; Lumenal side {ECO:0000269|PubMed:9647645}. Cytoplasm {ECO:0000269|PubMed:10639138, ECO:0000269|PubMed:9647645}. Secreted {ECO:0000269|PubMed:7890746}. Note=A small fraction of the protein may be cytoplasmic. In bone at least part of it is found in the extracellular matrix and in the culture medium of calvaria explants. {ECO:0000269|PubMed:7890746, ECO:0000269|PubMed:9647645}.
Interaction partners:
- FAM20C
Sequence:
MPTSVPRGAPFLLLPPLLMLSAVLAVPVDRAAPHQEDNQATETPDTGLYYHRYLQEVINVLETDGHFREKLQAANAEDIKSGKLSQELDFVSHNVRTKLDELKRQEVSRLRMLLKAKMDAKQEPNLQVDHMNLLKQFEHLDPQNQHTFEARDLELLIQTATRDLAQYDAAHHEEFKRYEMLKEHERRRYLESLGEEQRKEAERKLQEQQRRHREHPKVNVPGSQAQLKEVWEELDGLDPNRFNPKTFFILHDINSDGVLDEQELEALFTKELEKVYDPKNEEDDMREMEEERLRMREHVMKNVDTNQDRLVTLEEFLASTQRKEFGETAEGWKTVEMYPAYTEEELKRFEEELAAREAELNARAQRLSQETEALGRSQDRLEAQKRELQQAVLQMEQRKQQQQEQSAPPSQPDGQLQFRADTGDAPVPAPAGDQKDVPASEKKVPEQPPVLPQLDSQHL
Protein: Venom prothrombin activator oscutarin-C catalytic subunit (vPA) (EC 3.4.21.6) (Factor VII activator) (Snake venom serine protease) (SVSP) (Venom coagulation factor Xa-like protease) [Cleaved into: Oscutarin-C catalytic subunit light chain; Oscutarin-C catalytic subunit heavy chain] (Q58L96)
Organism: Oxyuranus scutellatus (Coastal taipan)
Function: Snake prothrombin (F2) activator that attacks the hemostatic system of prey. This catalytic subunit is functionally similar to blood coagulation factor Xa. For prothrombin activation, it requires a non-catalytic subunit present in the venom, which is similar to coagulation factor Va, to be fully active. In contrast to the 8 other snake venoms tested, this protein is the only one to also activate factor VII (F7). However, in contrast to prothrombin activation, the factor Va-like subunit is not essential for this activation.
Subcellular location: Secreted {ECO:0000269|PubMed:1604437, ECO:0000269|PubMed:3531198, ECO:0000269|PubMed:6986908}.
Interaction partners:
Sequence:
MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRANSLYEEFRSGNIERECIEERCSKEEAREVFEDDEKTETFWNVYVDGDQCSSNPCHYRGTCKDGIGSYTCTCLSGYEGKNCERVLYKSCRVDNGNCWHFCKPVQNDIQCSCAEGYLLGEDGHSCVAGGNFSCGRNIKTRNKREASLPDFVQSQNAILLKKSDNPSPDIRIVNGMDCKLGECPWQAVLVDEKEDAFCGGTILSPIYVLTAAHCINQTKMISVVVGEINISRKNPGRLLSVDKIYVHQKFVPPKKGYEFYEKFDLVSYDYDIAILQMKTPIQFSENVVPACLPTADFANQVLMKQDFGIVSGFGRIFEKGPQSKTLKVLKVPYVDRHTCMLSSESPITPTMFCAGYDTLPRDACQGDSGGPHITAYRDTHFITGIVSWGEGCAQTGKYGVYTKVSKFILWIKRIMRQKLPSTESSTGRL
Protein: Connector of kinase to AP-1, isoform E (MIP15828p) (D3DML3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- AT25231p
- FGFR1 oncogene partner 2 homolog
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- MOB kinase activator-like 4
- CTTNBP2 N-terminal-like protein
- Serine/threonine-protein phosphatase PP2A
- Sarcolemmal membrane-associated protein
- Cerebral cavernous malformation 3
- non-specific serine/threonine protein kinase
- Stress-activated protein kinase JNK
Sequence:
MGTNSGATAGINNKPVGGATGAGVLVGGGVGGANSSIGGVLSNSLGGGGSGGLSISGLNAGGQNANVGGMGNVGGDDGGNGMVGGGVNNQQATTPQYTIPGILHFIQHEWSRFELERSQWDVDRAELQARIAMLLGERKCLESLKSDLTRRIKMLEYALRQERAKFYRLKYGTDPPQLNEFKPSNEDAGLAGEVATDSEVPYSSVSNTTWRQGRQMLRQYLAEIGYTDNIIDVRSNRVRSILGLNNNAEHDGSGGGLGGGLGGGTGGENLSPNINGNESNKRASETEGRHTPAKKVQQSIDEIIVDTEAAVMANFEFLGATEMSDDDEISDDLEMVATDNDDTDVKLAKRAKSGKDMLTEDLEADVGEQLLNDMNLMTEEVDGSLGLGELAQLTVNNESDGAYDANSKDGTGGSAGGAGYRKTWNAKYTLRSHFDGVRSLIFHPEEPVLITASEDHTLKLWNLQKTVQAKKSASLDVEPLYTFRAHTGPVLCLGMSSSGETCYSGGLDGNIECWQLPSPNIDPYDCYDPNVHSGTLEGHTDAVWGLTTMQSNIVSCSADGTVKLWSPYNKEPLLRTYTASEAEGVPSSVDFVRNEVDHIVVAYNSAHCIVYDTETGKQVVRLEAAQEMSGNTGKFINKVVSHPTLPITITAHEDRHIRFWDNTSGTLVHSMVAHLEPVTSLAVDAHGLYLLSGSHDCSIRLWNLDNKTCVQEITAHRKKFDESIFDVAFHATKPYIASAGADGLAKVFV
Protein: Inactive cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMP-NeuAc hydroxylase-like protein) (Cytidine monophosphate-N-acetylneuraminic acid hydroxylase pseudogene) (Q9Y471)
Organism: Homo sapiens (Human)
Function: Sialic acids are components of carbohydrate chains of glycoconjugates and are involved in cell-cell recognition and cell-pathogen interactions. That protein has no CMP-N-acetylneuraminate monooxygenase activity and is not able to convert CMP-N-acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly expressed at the surface of many cells in vertebrates. However, it may play a role in Wnt signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19890979}. Note=May localize to membranes, nucleus and cytoskeleton. {ECO:0000269|PubMed:19890979}.
Interaction partners:
Sequence:
MDENNGLLLLELNPPNPWDLQPRSPEELAFGEVQITYLTHACMDLKLGDKRMVFDPWLIGPAFARGWWLLHEPPSDWLERLCQADLIYISHLHSDHLSYPTLKKLAGRRPDIPIYVGNTERPVFWNLNQSGVQLTNINVVPFGIWQQVDKNLRFMILMDGVHPEMDTCIIVEYKGHKILNIVDCTRPNGGRLPMKVALMMSDFAGGASGFPMTFSGGKFTEEWKAQFIKTERKKLLNYKARLVKNLQPRIYCPFAGYFVESHPSDKYIKETNTKNDPNELNNLIKKNSDVITWTPRPGATLDLGRMLKDRTDSKGIIEPPEGTKIYKDSWDFEPYLEILNAALGDEIFLHSSWIKEYFTWAGFKDYNLVVRMIETDEDFNPFPGGYDYLVDFLDLSFPKERPQREHPYEEIHSRVDVIRHVVKNGLLWDELYIGFQTRLQRDPDIYHHLFWNHFQIKLPLTPPNWKSFLMCCEQNGPVILQFSTERTNEPNRNKFSVENKA
Protein: T7-like mitochondrial DNA helicase (Q54J94)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MISQCRNLNKTIQRLSLPSNIFRLQYFSTTTSSTIPKVTNKKLKVTIKNKDKLDIPLNNFVNNKDNNNGPSLKINYVGGELENNPTTSSSSPVQTSSKSSPQSTTTFKNNNINNNNNNNNNNNNNNNNNNNNNNNYNNNSNENNSSTFVSSHYKVNEESMLSYLDRKKLVYKIIGKQIIVKECPLCHDTKGKFDNFWKLYISRETAAFFCHRCGCKGSWIDLKVNLGDLSLDHSNHKPIIKSPTTTSTNKTSNNETEESTISIADLKKMLNYSNELNNHQDVIKKLTGKEKGERGLSKEVLEFYKVGVTSQQFFFNDEWQEHKCITFPWTTLDKKGNIQVHRCKLRSTKEKSLQRIEPKGGKWGFFGWHTIPSDAKEIILTEGEYDAMAVYQETGIPTISLPNGANSLPIALLPLLERFEKIYLWMDDDVPGMEGAAKFSEKLGIQRTFIVSTKQNDPNGPKDANDALLAGKDLKAILSTAANIPHDQICDFSDVRSIIHNELKDPLSVIGKQSKWFPSFNKVLKGHRKGELTIFSGPTGIGKTSVLSQLSLDFCSQGTRTLWGSFELKVPRLARKMLSQFSNCNLDKHVENYQEIADNFSNMPMYFLRFFGSTQVDKVIDAMEYAVYVQDVEHIVLDNLQFMLGSQAKGIERFEIMDDSIEKLRKFASQKNVHITLVIHPRKQDIDQVLNINDIFGTAKATQEADNVIILQNSKNNQRYLDIKKNRFSGDLGIIPLSFEKETNRFSESNEFDNNNLNNNNNNNNNNNNINL
Protein: RNA helicase (EC 3.6.4.13) (O05855)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Polyribonucleotide nucleotidyltransferase
- Large ribosomal subunit protein uL4
- Bifunctional NAD
- Large ribosomal subunit protein uL13
- Ribonuclease PH
- Ribonuclease E
- Elongation factor G
- Large ribosomal subunit protein uL3
- Probable helicase HelZ
- Peptidyl-prolyl cis-trans isomerase A
Sequence:
MTAVKHTTESTFAKLGVRDEIVRALGEEGIKRPFAIQELTLPLALDGEDVIGQARTGMGKTFAFGVPLLQRITSGDGTRPLTGAPRALVVVPTRELCLQVTDDLATAGKYLTAGPDTDDAAAVRRRLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLCQQGHLQLGGLSVLVLDEADEMLDLGFLPDIERILRQIPADRQSMLFSATMPDPIITLARTFMVRPTHIRAEAPHSSAVHDATEQFVYRAHALDKVELVSRVLQARDRGATMIFTRTKRTAQKVADELTERGFAVGAVHGDLGQLAREKALKAFRTGGIDVLVATDVAARGIDIDDVTHVINYQCPEDEKMYVHRIGRTGRAGRTGVAVTLVDWDELPRWSMIDQALGLGSPDPAETYSNSPHLYAELAIPATAGGTVGPARKSQGRRRDTDCDGQKTAQHARNTPRRRRTRGGKPVTGHPGTNPISSPIVGGDATSEPGSGTASDSGSDVVSGSRSGNGEAARRRRRRRRRPTHAQDGFAARAN
Protein: RE28166p (Q7YU37)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSISMSMDETICAYFVNNLKPGDGGVQEADTLQQFEAARELLGQQLAETQIRQIKPSEGYPLIAAGNLTKKDVFVLTQFEGEFFEQLQQTRALILGPPCLITCLRRNEPIPEGSSAIYSTAMRDLQVSATGITPQKKEELSRLINWMGGIYFQSFGHRTTHLISNTIKSSKYEQATLNGVPVMHVDWVQYVWDQSRRSQREGIMATDPDFDKYRLPIFFGANITCSGLDVARKDQVMRLVNDNGGIYHRAFRSQVVDIVITEQTKTDTEKYKAAIRYKKDVLLPEWIFDSCNRGYALPTKDYEVRPGKTSSTPTKTTRPGAAPGADQTHLSDLSRISFVSGSRRMCSDLSTVNESVSSVGSSSPAKQLLKQATSSGRNYQQVLAEIEPRQAKKAGAFLDGCCVYLSGFRSEEREKLNRVLNTGGATRYDEANEGISHIIVGQLDDAEYRQWQRDGLMGSVHVVRLDWLLESIRAGRVVSELVHRVSMPQNREPDVASPASKRTLRSMNHSFKQPTLPIKKKLFDQEPDPVQEQEHEEPDHTLLDQYSQDQGAVAQLPPADVSLLQPAASSTQMDIRQRVSVANPKPPAEGLQLPDLSASTLSIDFDKLDYFAGVSVYVHRECFNEEFFNQMLTECEAAQGLLVPSSFSDEVDFAIVSFEVAFDVKQLPVKARHVVTELFLESCMKKNQLLPIEYYHKHVPATALRQPLKGMTIVVSIYAGLERDFINATAELLGASVNKTFIKKEKPLLVCPSAEGSKYEGAIKWNYPVVTSDWLVQCARTGQKLPFVGYLVGKSPEDFPISPRLRDSNSRTARRPNESTLVAQPDVTMEEAENQPAGSVTPVTAGSPGAPELTPLRNKRVSELAGIPGGSALHRGSNSTSSPDSPCTPLSQVGAQQYNLDFLEQFVQRLDTEEGKDCVREIIREMRENQTPELERIRRQAYTPVSRKHQRPAPGIPDFCLTPEFQQRMADDFERRWRLPTMKIKPDTPLAVIRQRVMRITCETLGIEYEESNAKTPTLSESPSTVKKKPPTRTTQATKLNFDRSPKTPKLSLGKKTPLRVSMGSPRSGTQSPFVPNTQSPIEAAPPRRSDGPTLSEEGQSTINFDKISFEESAVPVLAPDVPTVAPDVKQITDYLKNCESRGNSLKRSHDNDMDCGESEVQYVQPFESEGFALGTEDMVDWRDPAEFNAAKRRSSGGSPKMQYAGIPCFSISCGDDDEKRAELIARITQLGGKVCENLVNYDDSCTHLLCERPNRGEKMLACIAAGKWILNIQYIEQSHARGDFLDETLYEWGNPKAINLPTLAPEEEPIAAAVHRWRTELSACGGGAFSDHRVILSMNERSGAPIRNVLRAGGACILEPTTPFSKDPVAKSASHCFVDVKKAPLSTQDMEYLHKCGVQVLSQIAINAYLMNGRDADLGKYQLL
Protein: Histone deacetylase 6 (A0A1L5YJQ7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTSTGQDSSTRQRKSRHNPQSPLQDSSATLKRGGKKGAVPHSSPNLAEVKKKGKMKKLSQPAEEDLIVGLQRLDLNSETRVPVGTGLVFDEQLNDFHCLWDDSFPENPERLHAIKEQLILEGLLGRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLAGTYDSVYLHPNSYSCACLATGSVLRLVDAVMGAEIRNGMAVIRPPGHHAQRSLMDGYCMFNHLAVAARYAQKKHRIQRILIVDWDVHHGQGTQFIFDQDPSVLYFSIHRYEHGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHILLPVAFEFQPQLVLVAAGFDALHGDPKGEMSATPAGFAHLTHFLMGLAGGKLILSLEGGYNLHALAKGVSGSLHTLLGDPCPMLESPVAPCASAQTSISCTLEALEPFWEVLERSVEPQDEDEVEGDMLEDEEEEGHWEATALPMDTWPLLQNRTGLVYDERMMSHCNLWDNHHPETPQRILRIMCHLEEVGLAARCLILPARPALDSELLTCHSAEYVERLRATEKMKTRDLHREGANFESIYICPSTFACAQLATGAACRLVEAVLSGEVLNGIAIVRPPGHHAEPDAACGFCFFNSVAVAARHAQVIAGRALRILIVDWDVHHGNGTQHIFEEDPSVLYVSLHRYDRGTFFPMGDEGASSQVGRAAGTGFTVNVPWNGPRMGDADYLATWHRLVLPIAYEFNPELVLISAGFDAAQGDPLGGCQVTPEGYAHLTHLLMGLAGGRIILILEGGYNLTSISESMAACTHSLLGDPPPQLTSLRPPQSGALASISEVIQVHRKYWRSLRLMKMEDKEERSSSRLVIKKLPQSASPVSAKGMTTPKGKVLEAGMRKPTAALPTKESTLGQAKAKTAKALLAQGQSSEQAAKGTTLDLATSKDTVGGATTDQCASVAATENSANQTTSGEEASGETESFGTSPSSNASKQTTGASPLHGAAAQQSPELGLSSTLELSSEAQEVQESEEGLLGEAAGGQDMNSLMLTQGFGDFNTQDVFYAVTPLSWCPHLMAVCPIPAAGLDVSQPCKTCGSFQENWVCLTCYQVYCSRYVNAHMVCHHEASEHPLVLSCVDLSTWCYLCQAYVHHEDLQDVKNAAHQNKFGEGMPHLQ
Protein: CSC1-like protein 2 (Transmembrane protein 63B) (Q3TWI9)
Organism: Mus musculus (Mouse)
Function: Acts as an osmosensitive calcium-permeable cation channel. Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion.
Subcellular location: Early endosome membrane {ECO:0000250|UniProtKB:Q5T3F8}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:27045885, ECO:0000269|PubMed:31243992, ECO:0000269|PubMed:32375046, ECO:0000269|PubMed:37543036}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with cortical F-actin (PubMed:31243992). Localizes at lamellar body membrane in alveolar type 2 cells (Probable). {ECO:0000269|PubMed:31243992, ECO:0000305|PubMed:38127458}.
Interaction partners:
Sequence:
MLPFLLATLGTAALNSSNPKDYCYSARIRSTVLQGLPFGGVPTVLALDFMCFLALLFLFSILRKVAWDYGRLALVTDADRLRRQERERVEQEYVASAMHGDSHDRYERLTSVSSSVDFDQRDNGFCSWLTAIFRIKDDEIRDKCGGDAVHYLSFQRHIIGLLVVVGVLSVGIVLPVNFSGDLLENNAYSFGRTTIANLKSGNNLLWLHTSFAFLYLLLTVYSMRRHTSKMRYKEDDLVKRTLFINGISKYAESEKIKKHFEEAYPNCTVLEARPCYNVARLMFLDAERKKAERGKLYFTNLQSKENVPAMINPKPCGHLCCCVVRGCEQVEAIEYYTKLEQRLKEDYRREKEKVNEKPLGMAFVTFHNETITAIILKDFNVCKCQGCTCRGEPRASSCSEALHISNWTVTYAPDPQNIYWEHLSIRGFIWWLRCLVINVVLFILLFFLTTPAIIITTMDKFNVTKPVEYLNNPIITQFFPTLLLWCFSALLPTIVYYSAFFEAHWTRSGENRTTMHKCYTFLIFMVLLLPSLGLSSLDLFFRWLFDKKFLAEAAIRFECVFLPDNGAFFVNYVIASAFIGNAMDLLRIPGLLMYMIRLCLARSAAERRNVKRHQAYEFQFGAAYAWMMCVFTVVMTYSITCPIIVPFGLMYMLLKHLVDRYNLYYAYLPAKLDKKIHSGAVNQVVAAPILCLFWLLFFSTMRTGFLAPTSMFTFVVLVITIVICLCHVCFGHFKYLSAHNYKIEHTETDAVSSRSNGRPPTAGAVPKSAKYIAQVLQDSEGDGDGDGAPGSSGDEPPSSSSQDEELLMPPDGLTDTDFQSCEDSLIENEIHQ
Protein: Interferon type B (IFN-beta) (Q90873)
Organism: Gallus gallus (Chicken)
Function: Has antiviral activities.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Interferon regulatory factor 3
- Uncharacterized protein.
- Uncharacterized protein.
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- Signal transducer and activator of transcription
- Toll-like receptor 3
- Interleukin-6
- Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog
- Interleukin-1
Sequence:
MTANHQSPGMHSILLLLLLPALTTTFSCNHLRHQDANFSWKSLQLLQNTAPPPPQPCPQQDVTFPFPETLLKSKDKKQAAITTLRILQHLFNMLSSPHTPKHWIDRTRHSLLNQIQHYIHHLEQCFVNQGTRSQRRGPRNAHLSINKYFRSIHNFLQHNNYSACTWDHVRLQARDCFRHVDTLIQWMKSRAPLTASSKRLNTQ
Protein: Thrombospondin type-1 domain-containing protein 1 (Transmembrane molecule with thrombospondin module) (Q9NS62)
Organism: Homo sapiens (Human)
Function: Is a positive regulator of nascent focal adhesion assembly, involved in the modulation of endothelial cell attachment to the extracellular matrix.
Subcellular location: [Isoform 1]: Endosome membrane {ECO:0000269|PubMed:29069646}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, focal adhesion {ECO:0000269|PubMed:29069646}. Note=Localizes to nascent focal adhesions. {ECO:0000269|PubMed:29069646}.; SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
Interaction partners:
Sequence:
MKPMLKDFSNLLLVVLCDYVLGEAEYLLLREPGHVALSNDTVYVDFQYFDGANGTLRNVSVLLLEANTNQTVTTKYLLTNQSQGTLKFECFYFKEAGDYWFTMTPEATDNSTPFPWWEKSAFLKVEWPVFHVDLNRSAKAAEGTFQVGLFTSQPLCPFPVDKPNIVVDVIFTNSLPEARRNSRQPLEIRTSKRTELAQGQWVEFGCAPLGPEAYVTVVLKLLGRDSVITSTGPIDLAQKFGYKLVMVPELTCESGVEVTVLPPPCTFVQGVVTVFKEAPRYPGKRTIHLAENSLPLGERRTIFNCTLFDMGKNKYCFDFGISSRSHFSAKEECMLIQRNTETWGLWQPWSQCSATCGDGVRERRRVCLTSFPSSPVCPGMSLEASLCSLEECAAFQPSSPSPLQPQGPVKSNNIVTVTGISLCLFIIIATVLITLWRRFGRPAKCSTPARHNSIHSPSFRKNSDEENICELSEQRGSFSDGGDGPTGSPGDTGIPLTYRRSGPVPPEDDASGSESFQSNAQKIIPPLFSYRLAQQQLKEMKKKGLTETTKVYHVSQSPLTDTAIDAAPSAPLDLESPEEAAANKFRIKSPFPEQPAVSAGERPPSRLDLNVTQASCAISPSQTLIRKSQARHVGSRGGPSERSHARNAHFRRTASFHEARQARPFRERSMSTLTPRQAPAYSSRTRTCEQAEDRFRPQSRGAHLFPEKLEHFQEASGTRGPLNPLPKSYTLGQPLRKPDLGDHQAGLVAGIERTEPHRARRGPSPSHKSVSRKQSSPISPKDNYQRVSSLSPSQCRKDKCQSFPTHPEFAFYDNTSFGLTEAEQRMLDLPGYFGSNEEDETTSTLSVEKLVI
Protein: MICOS complex subunit MIC12 (Altered inheritance of mitochondria protein 5, mitochondrial) (Found in mitochondrial proteome protein 51) (Mitochondrial contact site complex 12 kDa subunit) (P38341)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Enriched at crista junctions. {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21944719, ECO:0000269|PubMed:21987634, ECO:0000269|PubMed:22009199}.
Interaction partners:
- MICOS complex subunit MIC10
- MICOS complex subunit MIC19
- MICOS complex subunit MIC60
- MICOS complex subunit MIC27
- MICOS subunit MIC26
- Sorting assembly machinery 50 kDa subunit
- Mitochondrial import receptor subunit TOM40
- Altered inheritance of mitochondria protein 24, mitochondrial
- Mitochondrial import receptor subunit TOM22
- mRNA-binding protein PUF3
Sequence:
MSKLGPLARSVKWTLSVGVIGSVFYLYRYSNNGYFYDHDATWLKQDHQVQDLVDRKEVVPGETRNRKLVVTDDGTAWSRTMGESIKDIWNEQIRNSVDWIYSWGKN
Protein: Serine/threonine-protein kinase rio1 (EC 2.7.11.1) (EC 3.6.3.-) (O42650)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the final endonucleolytic cleavage at site D converting 20S pre-rRNA into the mature 18S rRNA. Required for the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 20S-pre-rRNA D-site endonuclease nob1
- Protein LTV1
- Ribosome biogenesis protein tsr1
- Pre-rRNA-processing protein pno1
- Serine/threonine-protein kinase rio2
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Uncharacterized protein C13G1.09
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS7
Sequence:
MVEELKNDAQTNEEESEYSDFSDGSDNDYFREDDIDWNQASSNYSARQENFGNNSSKINSVNDHVSTLSRYVNNIKLNDRFEAEDKSSIKDKSDRATSEQVLDPRTRMILLKLINNGTISEINGCISTGKEANVYHATNEDGKHFAIKIYKTSILVFKDRDRYVSGEFRFRHGYNKRNPRKMVRLWAEKEIRNLKRVAAAGIPCPEPILLKQHVLLMSFLGDKKGWAYPKLKDIDMTPGEATKLYQLVARNMRILFHVCHLVHADLSEYNLLYHKGKVYFIDVSQSVEHDHPQSIDFLRMDILNISTFFRRLNAGCLSLPQLFKFITEEGSCEKEAMKTRLNAIYEEEPTTEEYEEEFLKTYVPRTLDEVYDIDRDTEIVNAGGVNSLVYKHLLNTDFQKLDLNDTTKNQNDQILPNETSESDDDANSISSMENEEERTSDSKSSAKQGKGNGRAKETPEEKRARKKKTKEDKAEKRKSKIPKYEKKRKLKQSGRKK
Protein: YEATS domain-containing protein (Q389H2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
Interaction partners:
- RuvB-like helicase
- RuvB-like helicase
- Transmembrane protein, conserved
- SNF2 DNA repair protein, putative
Sequence:
MQATSKSTGSSVSITGEHEYVVYTGATLIPFCVGSVALPLTLCRASSSAVAASSQAHALSSASRGNAKQKRSGKGSGQQETSRDEDTGDNVHDYCAGISRCTHVRYIYFRDGSVASQDLSYRHQLFMKADGVKRSEMLDGKESNQVYSASPLYALVDRVVFTLPNGFPERRREVTHPPFFIVDDTWAEHLVEVEVHFHPWLGIAPFTASHMVLLNQRVDVTPQLLSSTQGQCKPPSTVILSPDEEERLAGVGSSSLIGTKRSRVPECGVVLPEETSAVRMDLSNSVYSPDMVILGEPGFRERLVDLVGAPVVAERRDAMRIFHPTLDVVRYLAAVRAMPQPELMAPPRICLLPWYQQSVQPLATQHTEKKCEKSERCDRHGTRSRSVMNDDNICDDSDHEIDVGSLPPWCFPFEVIIHACESRRQSGAVDAMRAVLAELKKEQLELRESIEQNIAAATANAEELRDVIKHMSQRCAALQTSWKR
Protein: B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (mCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (mCIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10) (Q9Z0H7)
Organism: Mus musculus (Mouse)
Function: Plays a key role in both adaptive and innate immune signaling by bridging CARD domain-containing proteins to immune activation. Acts by channeling adaptive and innate immune signaling downstream of CARD domain-containing proteins CARD9, CARD11 and CARD14 to activate NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines. Recruited by activated CARD domain-containing proteins: homooligomerized CARD domain-containing proteins form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10, subsequent recruitment of MALT1 and formation of a CBM complex (By similarity). This leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (By similarity). Activated by CARD9 downstream of C-type lectin receptors; CARD9-mediated signals are essential for antifungal immunity. Activated by CARD11 downstream of T-cell receptor (TCR) and B-cell receptor (BCR) (By similarity). Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95999}. Membrane raft {ECO:0000250|UniProtKB:O95999}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:O95999}.
Interaction partners:
- Caspase recruitment domain-containing protein 11
- Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog
- Caspase recruitment domain-containing protein 9
- Caspase-8
- NF-kappa-B essential modulator
- TNF receptor-associated factor 6
- Caspase recruitment domain-containing protein 10
- Protein kinase C theta type
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MEAPAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPRGLDTLVESIRREKTQSFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFAAGATNNLSRCNSDESNLSEKQRASTVMYHPEGESSTAPFFSMASSLNLPVLEVGRTENSSFSSATLPRPGDPGAPPLPPDLRLEEGGSCGNSSEMFLPLRSRALSRQ