wanglab/gogpt-training-data huggingface dataset:
Protein: C-type lectin domain family 10 member A (C-type lectin superfamily member 14) (DC-asialoglycoprotein receptor) (DC-ASGPR) (Macrophage galactose-type lectin) (MGL) (Macrophage lectin 2) (CD antigen CD301) (Q8IUN9)
Organism: Homo sapiens (Human)
Function: Probable role in regulating adaptive and innate immune responses. Binds in a calcium-dependent manner to terminal galactose and N-acetylgalactosamine units, linked to serine or threonine. These sugar moieties are known as Tn-Ag and are expressed in a variety of carcinoma cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16998493, ECO:0000269|PubMed:17616966, ECO:0000269|PubMed:17804752}; Single-pass type II membrane protein. Early endosome membrane {ECO:0000269|PubMed:17616966}; Single-pass type II membrane protein. Lysosome membrane {ECO:0000269|PubMed:17616966}; Single-pass type II membrane protein. Note=Recycles between the plasma membrane and the endolysosomal compartment. Upon antigen binding, internalizes via endocytosis and then dissociates from antigen at acidic pH characteristic of endolysosomal vesicles. {ECO:0000269|PubMed:17616966}.
Interaction partners:
- Integrin alpha-X
- T-cell surface glycoprotein CD1c
- Lethal
- Mucin-1
- High affinity immunoglobulin epsilon receptor subunit alpha
- Elongation factor 1-alpha 2
Sequence:
MTRTYENFQYLENKVKVQGFKNGPLPLQSLLQRLCSGPCHLLLSLGLGLLLLVIICVVGFQNSKFQRDLVTLRTDFSNFTSNTVAEIQALTSQGSSLEETIASLKAEVEGFKQERQAGVSELQEHTTQKAHLGHCPHCPSVCVPVHSEMLLRVQQLVQDLKKLTCQVATLNNNASTEGTCCPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQNFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGFQNWKPGQPDDWQGHGLGGGEDCAHFHPDGRWNDDVCQRPYHWVCEAGLGQTSQESH
Protein: Nitric oxide synthase 3 (EC 1.14.13.39) (Constitutive NOS) (cNOS) (EC-NOS) (NOS type III) (NOSIII) (Nitric oxide synthase, endothelial) (Endothelial NOS) (eNOS) (Q62600)
Organism: Rattus norvegicus (Rat)
Function: Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.
Subcellular location: Membrane, caveola {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle, which is favored by interaction with NOSIP and results in a reduced enzymatic activity. {ECO:0000250}.
Interaction partners:
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Calmodulin-1
- RAC-alpha serine/threonine-protein kinase
- Caveolin-1
- Arginase-2, mitochondrial
- Argininosuccinate lyase
- Argininosuccinate synthase
- Arginase-1
- Antizyme inhibitor 2
Sequence:
MGNLKSVGQEPGPPCGLGLGLGLGLCGKQGPASPAPEPSQAPVPPSPTRPAPDHSPPLTRPPDGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQSRPTQGPSPTEQLLGQARDFINQYYNSIKRSGSQAHEQRLQEVEAEVVATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRTAQEMFTYICNHIKYATNRGNLRSAITVFPQRYAGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPPELFTLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSSEIGMRDLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLYSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWKGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHEALVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSSPRPEQHKSYKIRFNSVSCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAARDIFSPKRSWKRQRYRLSTQAESLQLLPRLTHVHRRKMFQATILSVENLQSSKSTRATILVRLDTGSQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPPSTEPVAVEQLEKGSPGGPPPGWVRDPRLPPCTLRQALTYFLDITSPPSPRLLRLLSTLAEESSEQQELEALSQDPRRYEEWKWFRCPTLLEVLEQFPSVALPAPLILTQLPLLQPRYYSVSSAPSAHPGEIHLTVAVLAYRTQDGLGPLHYGVCSTWMSQLKAGDPVPCFIRGAPSFRLPPDPNLPCILVGPGTGIAPFRGFWQDRLHDIEIKGLQPAPMTLVFGCRCSQLDHLYRDEVLDAQQRGVFGQVLTAFSRDPGSPKTYVQDLLRTELAAEVHRVLCLEQGHMFVCGDVTMATSVLQTVQRILATEGSMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWSFDPPTQETPGS
Protein: 17.6 kDa class II heat shock protein (At4g14830) (O23338)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Calcium-dependent protein kinase 10
- Calcium-dependent protein kinase 11
- Peroxidase
- Calcium-dependent protein kinase 4
- E3 UFM1-protein ligase 1 homolog
- Calcium-dependent protein kinase 13
- Remorin 4.1
Sequence:
MKIHPLPRNENNNNLIHHARDPTREPGKKLRRLPHIFSRVLELPLKSDADVAVEESHDCFRFVAETDGGGGGGVRAYMVEIHPGVTKILVRTNGSSSLGLSLDELELDVWRFRLPESTRPELVTVDCDGDGELIVTVPKIEDNGRDLIVLVQ
Protein: RNA polymerase II elongation factor ELL3 (Q9HB65)
Organism: Homo sapiens (Human)
Function: Enhancer-binding elongation factor that specifically binds enhancers in embryonic stem cells (ES cells), marks them, and is required for their future activation during stem cell specification. Does not only bind to enhancer regions of active genes, but also marks the enhancers that are in a poised or inactive state in ES cells and is required for establishing proper RNA polymerase II occupancy at developmentally regulated genes in a cohesin-dependent manner. Probably required for priming developmentally regulated genes for later recruitment of the super elongation complex (SEC), for transcriptional activation during differentiation. Required for recruitment of P-TEFb within SEC during differentiation. Probably preloaded on germ cell chromatin, suggesting that it may prime gene activation by marking enhancers as early as in the germ cells. Promoting epithelial-mesenchymal transition (EMT) (By similarity). Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III.
Subcellular location: Nucleus {ECO:0000269|PubMed:10882741}.
Interaction partners:
- AF4/FMR2 family member 4
- AF4/FMR2 family member 1
- Protein ENL
- Protein AF-9
- Cyclin-T1
- RNA polymerase II elongation factor ELL
- ELL-associated factor 1
- Cyclin-T2
- ELL-associated factor 2
- Little elongation complex subunit 1
Sequence:
MEELQEPLRGQLRLCFTQAARTSLLLLRLNDAALRALQECQRQQVRPVIAFQGHRGYLRLPGPGWSCLFSFIVSQCCQEGAGGSLDLVCQRFLRSGPNSLHCLGSLRERLIIWAAMDSIPAPSSVQGHNLTEDARHPESWQNTGGYSEGDAVSQPQMALEEVSVSDPLASNQGQSLPGSSREHMAQWEVRSQTHVPNREPVQALPSSASRKRLDKKRSVPVATVELEEKRFRTLPLVPSPLQGLTNQDLQEGEDWEQEDEDMDPRLEHSSSVQEDSESPSPEDIPDYLLQYRAIHSAEQQHAYEQDFETDYAEYRILHARVGTASQRFIELGAEIKRVRRGTPEYKVLEDKIIQEYKKFRKQYPSYREEKRRCEYLHQKLSHIKGLILEFEEKNRGS
Protein: Signal recognition particle 54 kDa protein (EC 3.6.5.-) (G3V4F7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364034}. Nucleus speckle {ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum {ECO:0000256|RuleBase:RU364034}.
Interaction partners:
Sequence:
MASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFKNENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNEALIEKLKHGQFTLRDMYEQFQNIMKMGPFSQILGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDSTDGAKVFSKQPGRIQRVARGSGVSTRDVQELLTQYTKFAQMVKKMGGIKGLFKGGDMSKNVSQSQMAKLNQQMAKMMDPRVLHHMGGMAGLQSMMRQFQQGAAGNMKGMMGFNNM
Protein: Ribonuclease-like 3 (RNase ZF-3) (RNase-like 3) (ZF-RNase-3) (EC 3.1.27.-) (Dr-RNase 1) [Cleaved into: N-terminal peptide; LF-ZF3] (A5HAK0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Ribonuclease. Angiogenic. Plays a role in host defense. Exhibits strong antibacterial activity against Gram-negative bacteria but mild antibacterial activity against Gram-positive bacteria. The RNase activity is not required for the bactericidal activity.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P34096}.
Interaction partners:
- Ribonuclease T2,-like
- Ladderlectin
- Si:dkey-241l7.5
- Odorant receptor, family D, subfamily 107, member 1.
Sequence:
MGIHQCTAVVLLLLCASLSTYGQPAEIRRRYEHFLTQHVYGGITEQTCDRVMRQRRITRFPTGNDCKEVNTFIQANGNHVRTVCTGGGTRQTDNRDLYMSNNQFTVITCTLRSGERHPNCRYRGKESSRKIVVACEGEWPTHYEKGVIV
Protein: Hepatic triacylglycerol lipase (EC 3.1.1.3) (EC 3.1.1.32) (EC 3.1.1.5) (Lipase member C) (Lysophospholipase) (Phospholipase A1) (Q7T359)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKTLIKIVLCFLMISQLTDGATFQGNRADTEPEARMKMRYEPKSVFRVYTDGEYTEDTCALELFQPHTLDACGFNSSLPLAIIIHGWSVDGMMEKWISRLASALKSSEGNINVLIADWLTLAHQHYPIAAQNTRIVGQDIAHLLSWLEDFKQFPLGKVHLIGYSLGAHISGFAGSNLAMSGRTLGRITGLDPAGPMFEGMSHTDRLSPEDAKFVDAIHTFTLQRMGLSVGIKQPVAHFDFYPNGGSFQPGCQLHMQNIYAHLAQHGIMGFEQTVKCAHERAVHLFIDSLLNKDKQIMAYKCSDNTAFDKGNCLDCRKNRCNTLGYDIKKVRTGKSKRLFLKTRSHMPYKLFHYQFRIQFINQIDKIDPTLTVSLSGTLGESENLPITLVEEISGNKTFTFLITLDTDIGDLMIMRFTWEGNPVWANMWNTVKTIIPWGKKSKGPQLTFGKITVKSGESQRKTTFCPQTDEGMSIEMLQEKVFVRCEKQKPGGIKHTHLRHFHIQSDLSFWMGDS
Protein: Cyclic nucleotide-gated ion channel subunit B, isoform A (GH25102p) (Q9W2D5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Cyclic nucleotide-gated cation channel subunit A
- Uncharacterized protein, isoform E
- Cyclic nucleotide-gated ion channel-like, isoform E
- Dystrobrevin, isoform F
Sequence:
MTSMARFRKVNRQSEKLEPEASASLLKSSPNILENFAYDEFQPIQTNHPLLKRMATTPVAQSGSQSSSSSTSSTRKAEPKFCDTLERHAFMRNVINQQPESTRRYSTPGEKEAQVRRSLEEITKDLKEIEQFVSATEELMQREKEQEQMMYSNKENKCPSPVKRVTYKINAYKAPPRRHRPGSPRFYHSRLYFRNGKIGCVDSTEHQNNVGATHALVKHILHHEKPLVSPDSVRRVLEQDSFEMVPLPGAVPEIVPDPIAIQRAEELAAATGQVVLPKEEEEEEKSSPLHQVESQPDVDEDEQDVQICYNESPELQNEDRNERTQRTPSINESEIVAVDEPDTEMNSDVDHRKPSSAGSLDSQGQQFLRDQVRHLVRRFTARANKVKSRIELPPTPSSSSTVSSPSPPPTKSLHPSPQHKVRLVPAGQSPHRGRLFEADTPRSNVWLCSSLCGANNDERTLDPQGKIYISWLCVVSLSFLYNAWVIPLRASFPFQTKENTNIWLACDFCADIIYLLDVVFFKHRVMYLFEGFWVKNKNLTRKNYMRKLQFKLDLLALLPLELLYFKLGTQAVWLRFPRFFKIQSFWEVFRLLDRVISSPHFVRVAKTLTYMLYMIHITAALYYAYSDYQGLGQNRWVFSGKGHPYVRCFAFATKTATSIGKNPKPERQGEYVFMTVAWLMGVFVFALLIGQIRDIISTATRNKHEYRQLEDETLEYMRRLNLSQEVQSRVKMWFQFTWEQQRTLDESNILDALPINLKTDIAISVHIQTLSKVQLFADCEEALLRDLVLKLRAVTFLPGDFVCRKGEVGREMYIVKLGQVQVMGGPSSDVVLATLTEGSVFGEISLLGINGADRRTADVRSKGYSNLFVLSKSDLNEVIAYYPTAQAILKKRARQLMRKNAAREREEERERARSALQADVVIGNPKTPETAPKLLQTVIQALPFESPAVVLITRGSKRMRRKRQSVQMETIVEPKMEVTGAAETQDQKGLKTGRCSPDLLSSIQQELKSKHKFINLTDSEKALISQSANNSLEDMKVVDL
Protein: AT-hook motif nuclear-localized protein 20 (Q8GWQ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Negatively regulates plant innate immunity (PTI) to pathogens through the down-regulation of the PAMP-triggered NHO1 and FRK1 expression.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8VYJ2}.
Interaction partners:
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Chorismate synthase
- MLP-like protein 31
- Jacalin-related lectin 44
- Protein REVEILLE 1
Sequence:
MANPWWTNQSGLAGMVDHSVSSGHHQNHHHQSLLTKGDLGIAMNQSQDNDQDEEDDPREGAVEVVNRRPRGRPPGSKNKPKAPIFVTRDSPNALRSHVLEISDGSDVADTIAHFSRRRQRGVCVLSGTGSVANVTLRQAAAPGGVVSLQGRFEILSLTGAFLPGPSPPGSTGLTVYLAGVQGQVVGGSVVGPLLAIGSVMVIAATFSNATYERLPMEEEEDGGGSRQIHGGGDSPPRIGSNLPDLSGMAGPGYNMPPHLIPNGAGQLGHEPYTWVHARPPY
Protein: Clathrin light chain A (Lca) (P04973)
Organism: Bos taurus (Bovine)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (By similarity).
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P09496}. Note=Cytoplasmic face of coated pits and vesicles. In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250|UniProtKB:P09496}.
Interaction partners:
- Clathrin heavy chain 1
- AP-2 complex subunit alpha
- AP-2 complex subunit mu
- Cyclin-G-associated kinase
- AP-2 complex subunit sigma
- AP-2 complex subunit alpha-2
- EH-domain containing 2
- AP-1 complex subunit beta-1
- Huntingtin-interacting protein 1
- Unconventional myosin-VI
Sequence:
MAELDPFGVPAGGPALGNGVAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAPGSQPHGEPPGIPDAVDGVTNGDYYQESNGPTDSYAAISQVDRLQSEPESIRKWREEQTERLEALDANSRKQEAEWKEKAIKELDEWYARQDEQLQKTKANNRVADEAFYKQPFADVIGYVTNINHPCYSLEQAAEEAFVNDIEESSPGTEWERVARLCDFNPKSSKQAKDVSRMRSVLISLKQAPLVH
Protein: Activator of basal transcription 1 (Q9W393)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- rRNA biogenesis protein RRP36
- KRR1 small subunit processome component homolog
- ATP-dependent RNA helicase
- Probable ATP-dependent RNA helicase Dbp45A
- Bystin
- Uncharacterized protein, isoform A
- Nucleolar protein 14 homolog
- EG:8D8.4 protein
- U3 small nucleolar RNA-associated protein 18 homolog
- RE67794p
Sequence:
MKVEETKLDEARWGKPQTKEGESANGIANPSNDDKKELANFKATFNSWAPEKKREKMHKVGVILISNIPKDMDGDCLKEIMNLHSVVGRVYVQPETLSSFKTKKNMRKGWVEFISKSGAKKIALELNNKPITDGKSSRFRGLLWKMKFLPRFKWYYLTDRMDYELAVCKVRVWSQARKRATFWYDPDQMEYFKKQVKKMKKMKKVKEAEMATRNAEMAAKKAEMAAKKLKKSA
Protein: Kinesin-like protein (G5EGL7)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MASRKKHSEPTSNLRVAVRIRPMNGTERSEKCTNVVKVDKGKQAIELKGKSFGPFFRTYDPDTTQEEIYSDLVSSQIKKVIAGFNCTVFAYGQTGTGKTFTMEGGRTDAKSSTDDPTTGIIPRAVEDIFEQLERCGCEEYSLRVSYIELYNEELFDLLASTDNEDRERLRIFDDPNKKGVIVSGVEEVPVRNRSDVFKLLQLGAEKRRTAATLMNMHSSRSHSLFMVNVVIRENTTTGEELVKQGKLNLVDLAGSENIGRSGAQGNRAKEAGSINQSLLTLGRVIRLLTTNGQHIPYRESKLTRLLQDSLGGSTITSLIATLSPSSSNFEESQSTLEYAMRAANIKNKPVCNTKLSKKTILKEYSDEIEKLRRDLRAAREKNGVIISQESHDEFQKNSEKVQELEQHLDNAVDRLRIFTEDQMHMDEQYRQLYERKGELEDRLRDRIREMAVKEKELADTNDVLNKHIEVIGLMHTSALKAFDQLTTSQGAADEMQTDLRAFWRKVDEMERADDRNKIVIDHFSKKMSDFIDTTSKLTNSLKADGDLLSKKLSENICPHVKSMESAHRDIESTAMDMETHAICIMKKSSEAEKKVIDNMTAISMENRIRLETVMKTCDDFYKSYSAKSQEFTQMVVDKLDEVKKQVSDFTEDMKPLVSTLHQTTCDSYEARTNESKKNVEHVRAACSSMADSMKALMLQVEQLSTKVAENHEKQVIADQNNQETILDTLNTAETVVQSLEDNIVETCDVKQEMDDTKKTLKQTDAKQENHIQVEKERAEEKENEVKVALKSFSDEAEATRGEAREFSNTLKSRFSATSEKCKVTGELVSDCTKKATDELSSLLDEFTKSTIVVTKESAAVVNSVVLVHVDPSVNVPQRILPSFPLVSELNQPVEPEVLLGFGEGNDDFDTDELATKKRRVTSFVRRDSLLETTNNFLSPSSIIKRREQAIEEEEDFEN
Protein: Antirestriction protein ArdA (Q47730)
Organism: Enterococcus faecalis (Streptococcus faecalis)
Interaction partners:
Sequence:
MDDMQVYIANLGKYNEGELVGAWFTFPIDFEEVKEKIGLNDEYEEYAIHDYELPFTVDEYTSIGELNRLWEMVSELPEELQSELSALLTHFSSIEELSEHQEDIIIHSDCDDMYDVARYYIEETGALGEVPASLQNYIDYQAYGRDLDLSGTFISTNHGIFEIVY
Protein: Heme exporter protein D (Cytochrome c-type biogenesis protein CcmD) (P0ABM5)
Organism: Escherichia coli (strain K12)
Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome c-type biogenesis protein CcmE
- Heme exporter protein B
- Cytochrome c biogenesis ATP-binding export protein CcmA
- Heme exporter protein C
- Cytochrome c-type biogenesis protein CcmF
- Thiol:disulfide interchange protein DsbE
- Cytochrome c-type biogenesis protein CcmH
- Periplasmic nitrate reductase, electron transfer subunit
- UPF0352 protein YejL
- Negative modulator of initiation of replication
Sequence:
MTPAFASWNEFFAMGGYAFFVWLAVVMTVIPLVVLVVHSVMQHRAILRGVAQQRAREARLRAAQQQEAA
Protein: Anoctamin-10 (Transmembrane protein 16K) (Q8BH79)
Organism: Mus musculus (Mouse)
Function: Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1 (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane. {ECO:0000250}.
Interaction partners:
Sequence:
MRVTLSTLDTCESSFTPLVVIELAQDVKDETKEWLKNRIIAKKKDGGAQLLFRPLLNKYEKETLENQNLYLVGASNVRLLLGAEAVGLVKECTDAAMRAFTYGTRHNFKGFHDNNNDFLTMAECQFIIKHELENLRARDEKMIPGYPQAKLYPGKSLMRRLLTSGIVTQVFPLHDTEALKKLEDTWYTRFALKYQPIDSIRSYFGETIALYFGFLEYFTFALIPMAIIGLPYYLFVWEDYDKYVIFASFNLIWSTVILEVWKRGCANMTYRWGTLVMKRQFEEPRPGFHGVLGINSVTGREEPLYSSYKRQLRIYLVSLPFVCLCLYFSLYVMMIYFDMEDWALSLHEDSGSEWTSLLLYVPSIVYAVVIEIMNRLYRYAAEFLTSWENHRLESAYQNHLVLKVLVFNFLNCFASLFYIAFVLKDMKLLRQSLATLLITSQILNQVVESLLPYWLQRKYCARVKRKVQALKSEVDTTLYEQVLLEKEMGTYLGTFDDYLELFLQFGYVSLFSCVYPLAAAFAVLNNFTEVNSDALKMCRVFKRPFAEPSASIGVWQLAFETMSVISVVTNCALIGMSPQVNAVFPESKTDLVLIVVAVEHALLALKFILAFAIPDKPRHIQQKLARLEFESLEALKQQQMKLVAENLKEEYQEDGKEAT
Protein: Mitogen-activated protein kinase 1 (EC 2.7.11.24) (MAP kinase Mkp1) (O94737)
Organism: Pneumocystis carinii
Function: Serine-threonine protein kinase which may be involved in maintenance of cell integrity. Functionally complements SLT2 null mutant in S.cerevisiae.
Interaction partners:
Sequence:
MDSKHSVFNVMGQEFVLQKGYEVIKGLGKGSYGVVCSAKNIEVEDNNKVAIKKITNIFSKKMLAKRALREIMLLQHFRNHKNITTLYDMDIVDPSKFNELYLYEELMQANLNSIIRSDQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPSNLLINADCKLKICDFGLSRGISVNQGQGTEYMTEYVTTRWYRAPEVMLSFQSYSKAIDLWSVGCILAELLGRKPFFKGSNYVDQLNQIFCILGTPNENIISKIKSASAQSYIRSLPTLPKMPYSKIFPYANPDALDLLNCLLTFDPYDRISCEEALEHPYLIIWHDPNKEPVCSEQFDFGFEAIDSIEEIRQMIINEVSRFKGLTGNQKLYHSISNT
Protein: APETALA2-like protein 4 (Protein GLOSSY 15) (OsGL15) (A0A0N7KMH0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription factor (By similarity). Involved in spikelet transition (Probable). Prevents lemma and palea elongation as well as grain growth.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366}.
Interaction partners:
Sequence:
MAATFYGVGSIALAMHEDDEEEGSGRVFGFAAGDLVRPAVVTQQLFPMTAAAAAVVPESTEQRHVAAAAEQWARPPSRKTRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAQAAARAYDQAAIKFRGVEADINFTLDDYKEDIKKMNNFSKEEFVQVLRRQGAGFVRGSSRFRGVTLHKCGKWEARIGQLMGKKYVYLGLYDTEMEAAKAYDKAAIKCCGKEAVTNFDTQAYEDELNLQSWDSELDLELSLGCSGGERAAGEVLHSAPSNQRTSLTFMLPEEEEMTACHRQRSIWARPSLAPAMPDGGAVIRPDQHQHHPSSRNMLLMSQVISSSGGGGGSGRQGAAELHMRPRHGWSSGGNNWAPPYAARPRLPGAEDDEDDDSAAAASSGFPMGQVATASSPSRPSSSSCSSRRSSTAAATATTGR
Protein: Erythrocyte membrane protein band 4.1 like 2 (E9PK52)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTEVGSVSEVKKDSSQLGTDATKEKPKEVAENQQNQSSDPEEEKGSQPPPAAESQSSLRRQKREKETSESRGISRFIPPWLKKQKSYTLVVAKDGGDKKEPTQAVVEEQVLDKEEPLPEEQRQAKGDAEEMAQKKQEIKVEVKEEKPSVSKEEKPSVSKVEMQPTELVSKEREEKVKETQEDKLEGGAAKRETKEVQTNELKAEKASQKVTKKTKTVQCKVTLLDGTEYSCDLEKHAKGQVLFDKVCEHLNLLEKDYFGLLFQESPEQKNWLDPAKEIKRQLRNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLPCSFVTHALLGSYTLQAELGDYDPEEHGSIDLSEFQFAPTQTKELEEKVAELHKTHRGLSPAQADSQFLENAKRLSMYGVDLHHAKDSEGVDIKLGVCANGLLIYKDRLRINRFAWPKILKISYKRSNFYIKVRPAELEQFESTIGFKLPNHRAAKRLWKVCVEHHTFYRLVSPEQPPKAKFLTLGSKFRYSGRTQAQTRQASTLIDRPAPHFERTSSKRVSRSLDGAPIGVMDQSLMKDFPGAAGEISAYGPGLVSIAVVQDGDGRREVRSPTKAPHLQLIEGKSSHETLNIVEEKKRAEVGKDERVITEEMNGKEISPGSGPGEIRKVEPVTQKDSTSLSSESSSSSSESEEEDVGEYRPHHRVTEGTIREEQEYEEEVEEEPRPAAKIDGGAGGDSGTLLTAQTITSESVSTTTTTHITKTVKGGISETRIEKRIVITGDGDIDHDQALAQAIREAREQHPDMSVTRVVVHKETELAEEGED
Protein: Astacin-like metalloendopeptidase (EC 3.4.-.-) (Oocyte astacin) (Ovastacin) (ZP2-proteinase) (Q6HA08)
Organism: Homo sapiens (Human)
Function: Oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization. Plays a role in the polyspermy inhibition. Probably acts as a protease for the post-fertilization cleavage of ZP2. Cleaves the sperm-binding ZP2 at the surface of the zona pellucida after fertilization and cortical granule exocytosis, rendering the zona pellucida unable to support further sperm binding.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6HA09}. Cell membrane {ECO:0000250|UniProtKB:Q6HA09}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:Q6HA09}. Note=Probably exocytosed from cortical granules during post-fertilization. Detected throughout the ooplasm of germinal vesicle stage oocytes in early bilaminar secondary follicles at postnatal (PN) day 3. Detected in the microvillar domain of the oolemma in arrested ovulated secondary oocytes and in the first polar body prior to fertilization. Upon fertilization, detected in the perivitelline space (PVS) and occasionally on the oolemma in 2-cell through morulae stages. Colocalizes with SPACA3 at the microvillar domain of the oolemma and in the perivitelline space (PVS). {ECO:0000250|UniProtKB:Q6HA09}.
Interaction partners:
- Zona pellucida sperm-binding protein 2
- Metalloproteinase inhibitor 1
- Fetuin-B
Sequence:
MEGVGGLWPWVLGLLSLPGVILGAPLASSCAGACGTSFPDGLTPEGTQASGDKDIPAINQGLILEETPESSFLIEGDIIRPSPFRLLSATSNKWPMGGSGVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKGRGIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYGRLAFSRRGLPTITPLWAPSVHIGQRWNLSASDITRVLKLYGCSPSGPRPRGRGSHAHSTGRSPAPASLSLQRLLEALSAESRSPDPSGSSAGGQPVPAGPGESPHGWESPALKKLSAEASARQPQTLASSPRSRPGAGAPGVAQEQSWLAGVSTKPTVPSSEAGIQPVPVQGSPALPGGCVPRNHFKGMSED
Protein: Stress-activated protein kinase JNK (EC 2.7.11.24) (A0A0R4IB91)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368052}.
Interaction partners:
Sequence:
MVFMNRRFLYNCSAPVLDVKIAFCQGFGKQVDVSYIAQHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAGYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPSPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDCLFPADSEHNKLKASQARDLLSKMLIIDPAKRISVDEALQHPYINVWYDPAEVEAARNQQISMPPPQIYDKQLDEREHSIDEWKELIYKEVMNFEERTKNGVVKGQPSPSAQVQP
Protein: LD21715p (Omega, isoform F (EC 3.4.14.1, EC 3.4.14.2, EC 3.4.14.4, EC 3.4.14.5)) (Q9VUH1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGNDVSVTETAQSDQNLMHTKEKKRRVRIILTVVTTVIAVALLATALVFILRTDEKDADDSDSNSNNAIDLEDVLSGQLYAKRFNGSWSNGNSLIYKENTSIMEFDAKTGERSILLEDAQHYVLYEKSADGEFLLLAKNYKKNFRYSFLAEYDLYNLNTKEFIQLTIQNEQHYLSMVQWSPVGNALVINYDRNLYYKESALAQEIALTSDEQAGILNGIPDWVYEEEVFSSNVATWFNPSGTQLAFIKFDDSSTHLINFPYYGDAGDLRYQYPLHQVIAYPKAGSSNPRVELVMVDLKRAVAGGDFVTVMPVPSALNTETDYIVTVVSWVDDDNVLSIWMNRIQNAAYVVTFDGLNRKVIYSAESKTGWVDLYTAPFRNRNGSRLAFVLPHNNYKHVQLLSSTVASSEPQALEPLTEGKYVVDSILHWDGKNDIIFYTANTEDHPEQLHLYAIRALAKQSPKCLTCNLIKSGDVQQTYFSATFNDNNHIVITSLGPGIPTTHIYEWKYENSQVVISKVLDWETNESLRAKLKGVALPSHKILTVDIDGGFQAKVLLQLPPNLDTSGATKYPMLVDVYGGPDSYSVTNKWMVDWGTYLSSNQSVIYAKIDGRGSGLRGESLLHAIYLKLGTVEISDQINVTQKLSTLFNYIDPDHVGIWGWSYGGYAAAMALANDEAKVFKCAASIAPVTDWAYYDSIYTERYMGLPNTNELGYANSRLSTMAVKLRGKKYLLVHGTLDDNVHYQQAMILAKNLERQDILFKQISYADEDHGLSNVRPHLYHSLDRFFGECFASSRLMKSAK