wanglab/gogpt-training-data huggingface dataset:
Protein: Protein winged eye (Q3LHL9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions in the determination of disk-specific identity, downstream of Hox genes. Overexpression induces ectopic wings with antero-posterior and dorso-ventral axes in the eye field. Overexpression is sufficient for ectopic expression of vg in eye disks.
Subcellular location: Nucleus {ECO:0000269|PubMed:16247005}. Chromosome {ECO:0000269|PubMed:16247005}. Note=Chromatin-associated; colocalizes on polytene chromosomes with Psc.
Interaction partners:
Sequence:
MATFNPGASSSAADVLSATTATATFLVPTTAAVSHPGAHTAHLQLDQFGGFSAATATPLQHHHHQQTNSSYTFVQIKREPCQVSEISSNNCHQQQQQHHQHHQHQVQHQGLSSASMTASSKTMSSSTLTTLVKIEAPSPKVSELEKSTGNSVPIGIAVARKRPQEALVPAINTPATLPLQPPLNKDLNCFGIRVADLGATSCGNLYFTGNGDLMTTGTATAEELALSAAGVNRAPSTFWQYPNALPIESVISMSPATVGLQYSREASRGQVVLLPAGPTALDPFQQAAAAAAFVWPSAYIPQAPAPGGHSAAAAAAAASLQPTPNLSSLPNFIFPSMGGHQALSTTPSYASTLQLYLAAAATATGSSTMCQHSNQQTSTTTTNSTINLSLAAGSGVTQSGNAASSLSSSSSLSASSSRFLSLATGQTGIPSLLSLPPPTGLKEEYPMPLALPPLVPLEAARDKEQALNLMRLPTPPTSATMEPSSLGHATPHHLFQSGAMATPTPALLNLSMHGNGGELPAATPLPAVSDEAALNYKLHAPLTPQTPPRLADIPVSGSTQLLPQMQDVNIQTDTPVCSEDESFPGSAKPQDPAAEAFPPPTHVQPLELTKPSEASHTQPTECHTQTEPSDIPSASQEESAEQTPPEPIETMTQATQADQTSPEDLTGLELLSNISTNSKPLVRVKQEPVEHIEQPAPQPQPVNIMPSEPTLPMPPMLEMEPTSEREPLGGLKLLCALAEQRIQEEVVQGSSLFATPSSRTPTPTSLALGTTAATPPIFEAKSCYAFGQSQGSVFPSSTSSFQMPLSSPGFPSMQGIELPTTSAGIVAELTPVKRKKHKHSKSSGSDSRKSARCSKKSKKKRHHSSSRQQFSAPAEEDLDLQDDQLQSELRNALHAVDPSYAQRFGQEVFSIMDNSMRMRLAKITRQYRKKKRKLDEISKHKKKKKCSKQQLELQQQQASQQAVQPSSALQQPQMTLSSVLGTSSPLRDYKFPKFSSSNLQASSFLRFPDKTHSFPPPPSLQQSQPEPNPLPSSSSPSTSSFVRLEPSALDAAVAIAPTTSSTSTSGSPSTKQVASARKQRKMKASTVGAAGEQTAATEAKRRFSAIDRELQLTSEHLYRDETRVLTDMGGLFYAGVMKPLRPPDVYSITLDGERGNKSHVMSREDILKDTILEVAPKSVESVPVGTRLCAYWSQQYRCLYPGRAIDSEQVVDGTASSATNAATTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYPIAEYNDNPLYSVGKQKRSALRGGESGPGGVTQDHLTVPGCEDSHSHHSLGMSSDNTTSLAATMELFTQRSEKKRLKKSLKKMSKAQNGVSPATATNGGADAAALGDGVSAEDAARKHHKHKKRKKHKKHHRKNGSEEQEQQVVQQDYSAAGQEATEAPSTEMSSATSSRVKVEVKVKTEQLEMEEEESASNLMSEISDEAKGDDLVEHNNSKGSSKIAAFLPERQLWGWYGTAYRKAGVKGRARKQFYKTIKRGKETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKLKFPGALFESPHEDENDVQTISHRCEVLQFGSYFEKFGADSKQYQSIYDNNDTYYLAGHYNPRLQVLKLQDDIPTLEELQDTNTTTTTTETTTED
Protein: Oxidation resistance protein 1 (Q8IPN8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MHTAVFWRNGDILEGLRPGSPKPGHIERVGGSSQQQQAEEEANKSDDPVITQRFLKINVRHITDGQGVVGGVLLVTPNAVMFDPNVSDPLVIEHGPESYGVIAPMELVVNAAIFHDIAHMRVAGGAGQGLNSASGDAEKPEIYYPKPVLVEEDSKELPEQQSLLGEDGNKRLDAEIGSLEIADDQESLCSSTGRDGDAFPKAFDRERVEDSSMEAKDSAKTDALDDEDKKAGLGLSSTRSTLEERRKSLLDHHWAIPSKDRSSEDEGDNESNVTVDSGARVQDPHSANSSVSGVPLSQPPVAAAAAAAAVAPASAVVPLPPSGIDLEHLEQLSKQSCYDSGIDIREPVPNVQPIPKKTVYSDADIVLSSDWVPPKTIVPTHFSESPPRSTILGQSLDAGTGGAGGVRKKTSSVSFSVDDEAAQQAQAQSAALAVTDKQADKKNKMLKRLSYPLTWVEGLTGEGGAVPPGGVGSGSLNKSGDTDSAPNTGDSNQSVFSKVFSRRSSIGTFIRPHSSEGTSSSTKLKEAKQAPKLDYRSMVSMDDKPELFISVDKLIPRPARACLDPPLYLRLRMGKPIGKAIPLPTSVMSYGKNKLRAEYWFSVPKNRVDELYRFINTWVKHLYGELDEEQIKARGFELIQEDTEWTKSGTTKAGMGGGSQDGEEISDLTRESWEVLSMSTDEYRKTSLFATGSFDLDFPIPDLIGKTEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNPSFKVFHWTGENMYFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFVIKTLECWAFV
Protein: Microcephalin (A6MCV0)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MESVLKGICAFVEVWSSSRTENYSKAFEQQLLDMGAKVSKTFNKRVTHVVFKDGHSTTWRKAQDAGVKTVSVLWVEKCRETGVRVDESLFPAVYNNDGLPLKHKCMQPKDFVEKTPENDRKLQRRLDRMAKELAQQRIGINAETDIPVLLFEDDGSLVYSPVSKIRDQCSEMERRINEMKEKRENLSPTASQMFQASPRCSQGDCPLSTSLTNSEDAVLQGEKKKDCLNSSFDDFFGTVTSKRQKKEVENTCNTQTCTHVSMSASKNSLSCGCDQKSLTRKQASRRSIGDENHVSEYDGSCKVFKEQKNKRNGNVRKARRLQKPTRTLVMTSMSSEKQSMVIQVVNKLGDFLFSDDVCETTSHVVTGSPRRTLNVMLGIARGCWIVSYEWVLCSLEFGHWISEEPYELSSNFPAAPICRLQRHLSTGIYQLNLFSNQPVMFVSPTSQPPCKKLMELIELSGGKICKALRQAKICIGKYPGKKYQEIKCLSEKWILDSITQHTVCPMENYIFQL
Protein: Signal recognition particle 14 kDa protein (SRP14) (P16255)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.
Subcellular location: Cytoplasm.
Interaction partners:
- Signal recognition particle 9 kDa protein
- Signal recognition particle subunit SRP68
- Signal recognition particle 19 kDa protein
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP54
- Uncharacterized protein.
- Uncharacterized protein.
- Ribosomal protein L8.
- Ribosomal protein L24.
- Uncharacterized protein.
Sequence:
MVLLESEQFLTELTRLFQKCRLSGSVFITLKKYDGRTKPIPRKGSVEGFEPSDNKCLLRATDGKKKISTVVSSKEVNKFQMAYSNLLRANMDGLKKRDKKSKSKKSKPAQ
Protein: POU class 2 homeobox 2 (U3KQN1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
VGILSGLHLTFWGPGPCLSPPQIKAEDPSGDSAPAAPLPPQPAQPHLPQAQLMLTGSQLAGLTALMPAQQQLLLQQAQAQLLAAAVQQSSAAAAANAAAAAAAASASSSTSSSSSSSASSSTSQPPASSGGGDLPPPQPASQPPGTPQLTLSQPIQLTAQDIQQLLQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQAVTRPTLPDPHLSHPQPPKCLEPPSHPEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLL
Protein: Granulysin (NK2C) (Q24JZ1)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MTSWAVLLITSVLLVAPGLAFSGLTPESHDQATAHLCDGDELCQGLALEDPQGDLLLQGEELSLRCGSCRRIIQHLMDKLGDQPDENTVIEEASKVCSKMRLLKGLCKSIMKKFLRTIAEDIVAGKTSQVICVDIKMCKSKPVGFI
Protein: Cytochrome P450, family 724, subfamily A, polypeptide 1 (F4K6S3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MFILQNEGKLFTSDYPKAMHDILGKYSLLLATGEIHRKLKNVIISFINLTKSKPDFLHCAENLSISILKSWKNCREVEFHKEVKIFTLSVMVNQLLSIKPEDPARLYVLQDFLSYMKGFISLPIPLPGTGYTNAIKARKRLSARVMGMIKEREREEEDMNNAIREEDFLDSIISNEDLNYEEKVSIVLDILLGGFETSATTLSLVVYFLAKSPNLLHKLKEEHAAIRAKKGDGELLNWEDYQKMEFTQCVISEALRCEYVIPKGWKVFPIFTAVHLDPSLHENPFEFNPMRWTDKAKMNKKTTAFGGGVRVCPGGELGKLQIAFFLHHLVLSYRWKIKSDEMPIAHPYVEFKRGMLLEIEPTKFLED
Protein: Maintenance of mitochondrial morphology protein 1 (Mitochondrial outer membrane protein MMM1) (Yeast mitochondrial escape protein 6) (P41800)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:11266455, ECO:0000269|PubMed:12972421, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:14981098, ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:19556461, ECO:0000269|PubMed:22250200, ECO:0000269|PubMed:8089172}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:11266455, ECO:0000269|PubMed:12972421, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:14981098, ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:19556461, ECO:0000269|PubMed:8089172}. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03103}.
Interaction partners:
- Mitochondrial distribution and morphology protein 34
- Mitochondrial distribution and morphology protein 10
- Mitochondrial distribution and morphology protein 12
- Mitochondrial Rho GTPase 1
- Mitochondrial import receptor subunit TOM7
- Sorting assembly machinery 37 kDa subunit
- Dynamin-related protein DNM1
- Mitochondrial import receptor subunit TOM40
- Mitochondrial import receptor subunit TOM70
- Sorting assembly machinery 35 kDa subunit
Sequence:
MTDSENESTETDSLMTFDDYISKELPEHLQRLIMENLKGSTTNDLKQTSNNSEFNVSKNGSFKGLDDAIQALQMQSVLHPSSLGSLATSSKFSGWSFAQGFFVGQLSIVLLFIFFLKFFIFSDEPSKSKNPKPAASRHRSKFKEYPFISREFLTSLVRKGAKQHYELNEEAENEHLQELALILEKTYYNVDVHPAESLDWFNVLVAQIIQQFRSEAWHRDNILHSLNDFIGRKSPDLPEYLDTIKITELDTGDDFPIFSNCRIQYSPNSGNKKLEAKIDIDLNDHLTLGVETKLLLNYPKPGIAALPINLVVSIVRFQACLTVSLTNAEEFASTSNGSSSENGMEGNSGYFLMFSFSPEYRMEFEIKSLIGSRSKLENIPKIGSVIEYQIKKWFVERCVEPRFQFVRLPSMWPRSKNTREEKPTEL
Protein: Protein unc-13 homolog D (Munc13-4) (Q9R189)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Late endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Lysosome {ECO:0000250}. Note=Colocalizes with cytotoxic granules at the plasma membrane. Localizes to endosomal exocytic vesicles. {ECO:0000250}.
Interaction partners:
- Syntaxin-11
- Ras-related protein Rab-27A
- Syntaxin-binding protein 2
- Ras-related protein Rab-27B
Sequence:
MATHLSHPQRRPPLLRQAVKIRRRRVRDLQDPPPQATPEVQVQSHHFSPEERDLLYEEALYTVLHRLGQPEPNHVKEASELLCYLQEAFQVQPEEHQQMLQRVRELEKPIFCLKATVKQAKGILGKDVSGFSDPYCLLGIEQKVGVPEGSPVSRRRQKAVVRHTIPEEETHRTQVKTQTLNPVWDETFILEFEDITNASFHLDMWDLDTVESVRHKLGELTDLHGLRRIFKEARKDKGQDDFLGNVMLRLQDLRCREDQWFPLEPCTETYPDRGQCHLQFQFIHKRRATVASRSQPSYTVHFHLLQQLVSHEVTQHQAGGTSWGRIAESQAVTILFLHATQKDLSDFHQSMAQWLAYSRLYQSLEFPSSCLLHPITSIEYQWIQGRLKAEQREELATSFTSLLAYGLSLIRKFRSVFPLSVSDSPSRLQSLLRVLVQMCKMKAFGELCPDSAPLPQLVSEALRMGTVEWFHLMQQHHQPMVQGILEAGKALLSLVQDVMGDLYQCRRTWNKIFHNVLKIDLFTMAFLELQWLVAKRVQDHTAAVGDLVSPDVGESLFQLYVSLREFCQLGPSDSHEVLALDGFHRWFQSAIPSWLQRTYSVALERVQRAVQMDSLVPLGELTKHSTSAVDLSTCFAQISHTARQLDWPDPEEAFMITVKFVEDTCRLALVYCSLIKARARELSAVQKDQSQAADMLCVVVNNVERLRLIIDKLPTQLAWEALEQRVGAVLEQGQLQNTLHTQLQGALAGLGHEIRTGVRTLAEQLEVGIATHIQKLIDAKGSILPEDAILPLMKFLEVKLCYMNTNLVQENFSSLLTLLWTHTLTVLVEAAASHRNSSLASSRLKVALQNLEICFHAEGCGLPPEALHTDTFLALQSDLELQAASSRELIQKYFRSRIQQQAETTSERLGAVTVKASYRASEQKLHVELLSASSLLPLDSNGSSDPFVQLTLEPRHEFPELAPRETQKHKKELHPLFDETFEFLVPAEPCQKDGACLLLTVLDHDRLGADDLEGEAFLPLCRVPGLTGCVEPGEAPQMRLPLTYPAPNGDPILRLLESRKGDREAQAFVKLRRQRAKQASQHAPATEP
Protein: Lipid transferase CIDEA (Cell death activator CIDE-A) (Cell death-inducing DFFA-like effector A) (O60543)
Organism: Homo sapiens (Human)
Function: Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter (By similarity). Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:18509062}. Nucleus {ECO:0000250|UniProtKB:O70302}. Note=Enriched at lipid droplet contact sites. {ECO:0000269|PubMed:18509062}.
Interaction partners:
- Perilipin-1
- Lipid transferase CIDEC
- Mitochondrial brown fat uncoupling protein 1
- Histone-lysine N-methyltransferase PRDM16
- DNA fragmentation factor subunit beta
- Hormone-sensitive lipase
- Very long chain fatty acid elongase 3
- Peroxisome proliferator-activated receptor gamma
- Cytochrome c oxidase subunit 7A1, mitochondrial
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
Sequence:
MEAARDYAGALIRPLTFMGSQTKRVLFTPLMHPARPFRVSNHDRSSRRGVMASSLQELISKTLDALVIATGLVTLVLEEDGTVVDTEEFFQTLGDNTHFMILEKGQKWMPGSQHVPTCSPPKRSGIARVTFDLYRLNPKDFIGCLNVKATMYEMYSVSYDIRCTGLKGLLRSLLRFLSYSAQVTGQFLIYLGTYMLRVLDDKEERPSLRSQAKGRFTCG
Protein: Kinesin, putative (Q388Z4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Kinesin-like protein, putative
- FG-GAP repeat protein, putative
- PTHB1 N-terminal domain-containing protein
- Bardet-Biedl syndrome 8 protein
- FG-GAP repeat protein, putative
- Kinesin, putative
- Kinesin-like protein
- Kinesin, putative
Sequence:
MMSSSSSAQVLAGIPQIGATTPVTTQSTVKREGSTPVRCRGKVERTPRGSQSSQDAVRVAVRVKPSSDNSNLLRYVIETGTLATTPRTGCRRESARLGSANQCAKSAEEAANIGGGGQGDERGSLSNMSLSSSSNINGGPVVTGRGATRPVPCFAPIAGTEEGNMLTVITPTADGAKEVQRTYEFGRVFGPSVSDSEICESIVPGIVEQLRAGFNACVLCYGQTGSGKTHTINVLAPAFINALFDNLDAENDIIELWYIQIYTNNAYNLLGRGKSEHGMLLQKPLGTAVPEPRYLVQNATLAIARIAEAQRKRFVSHHALNARSSRSHVLLSLHVTKCVGGIPVFTSRLTLGDLAGSERVKRTGVVGDELGEAIAINKSLSVLHSVIRATAEEADVLPVRESMLTLYLASTLADCYLLLIATVSLDKRSAAETKSSLDFATTAKRCVLTKTKERVRDLLMRNGCSFEEAYGNLTREIETLRHRVATLQEEVNIEKQLSSLTRREKHAPNSNDGMDHEGKEPEQPQKVNGDAATNTENSLANASGANSAEDPVIRDHVVALERQCAIFQSVLRERERDLCSLESRGDVAEELRQELEQRVRQCDEAQQTLEEAVLEVGTSELLHKVTDTFRWMQEQFDSMSEQKQVMAKTVEAMRSEQKRTMAELLEARKHIVQTEKSCEELRQRLERVTNENTGLTDQLEELNLKLLHEYTERVIREETVAWFKASGERAEECERLTTAFEDQRNLCDVLQSRLTSTEEELERGNKEHCALLQEMQKKDEAFRSIWILLTPQQKARFMSVGYGGDVVENSGSASLHQGHENVQLRSQVRTLKKQLEDEILCSRERDYRIEDLECENRLLQERLLHRENEYKSLVALDQDYMDEREQMEGQIAHLYTYIEEHNMKQRTSERQLREVQIEWEKLNEEYCNSQREVAELTAKLNKAKEEIRIQEANKHVLKNRHQHESRERDMKLAVLQHQLAVKQRTTDEVSRRLGLAERRRQHVTATVTAHKHHSDLVRRKAMKRNPELLRCQVGQPITTSQLIRATSLQTSLKRGHSQRPQRDAPKGLLRSRSSVSVDAAAGMRWDSRSSSNNQNGYVRRRTFSLNKQRDAPARSKFARTNSTLVERPALFF
Protein: 5'-nucleotidase, cytosolic II,-like 1 (Zgc:92102) (Q66I11)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Deoxycytidylate deaminase
- Adenosine deaminase
- Nudix-type motif 12.
- 5'-nucleotidase, ecto
- Cytosolic 5'-nucleotidase 3
- 5'-nucleotidase, cytosolic IAa
- 5'-nucleotidase, cytosolic IB b
- 5'-nucleotidase, cytosolic IAb
- 5'-nucleotidase, cytosolic IB a.
- Hypoxanthine phosphoribosyltransferase
Sequence:
MEPRINKKELQHRVFVNRSLTLENIKCYGFDMDYTLAVYKSPEYESLGFELLRDRLVSIGYPHELLGYTYDSTFPTRGLVYDTTYGNLLKIDSNGNILVCTHGFEYLRGEQVDEYYPNKFIQRDDTDRFYVLNTLFNLSETYLYACLVDFYTKSTRYKNWPKGFKHGDLFMSHRSMFQDVRDAMDHLHDTGTLKERTLKNLDKYVIKDPRIPVLLSRIKEVAKVFLATNSDFNYTEAIMKYLLDAATSSKGMKKSWRSYFDLVVVDTRKPLFFAGGTVLRQVDTDTGKLRIGTYTGDLQHGTVYSGGSSDLVCDLLDVKGKDILYVGDHIFGDILKSKKRQGWKTFLVVPELVKELHVWADKSSMFEELKHLDIFLAELYQHLDSGSQECPDISAIQTRIKMVTYGMDLCYGKMGSLLRCGSTKTLFASQLLRYADIYSTTCLNLLNYPFSFLFRAPLVLLPHEAAVETQNKEQMAELSEHMRRTSLKQRQCECEDGDCGQDDNCAARNSASTSTSDK
Protein: Spectrin beta chain, non-erythrocytic 2 (Beta SpIII sigma 1) (Beta-III spectrin) (Glutamate transporter EAAT4-associated protein 41) (SPNB-3) (Spectrin-like protein GTRAP41) (Q9QWN8)
Organism: Rattus norvegicus (Rat)
Function: Probably plays an important role in neuronal membrane skeleton.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Interaction partners:
- Metabotropic glutamate receptor 1
- Spectrin alpha chain, non-erythrocytic 1
- Spectrin alpha chain, erythrocytic 1
- Protein kinase C beta type
- Ankyrin 1
- Spectrin beta chain
Sequence:
MSSTLSPTDFDSLEIQGQYSDINNRWDLPDSDWDNDSSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRVGDLYSDLRDGRNLLRLLEVLSGETLPKPTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLVWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLLDFESLKKCNAHYNLQNAFNLAEKELGLTKLLDPEDVNVDQPDEKSIITYVATYYHYFSKMKALAVEGKRIGKVLDHAMEAEHLVEKYESLASELLQWIEQTIVTLNDRQLANSLSGVQNQLQSFNSYRTVEKPPKFTEKGNLEVLLFTIQSKLRANNQKVYTPREGRLISDINKAWERLEKAEHERELALRTELIRQEKLEQLAARFDRKAAMRETWLSENQRLVSQDNFGLELAAVEAAVRKHEAIETDIVAYSGRVQAVDAVAAELAAEHYHDIKRIAARQNNVARLWDFLREMVAARRERLLLNLELQKVFQDLLYLMDWMAEMKGRLQSQDLGKHLAGVEDLLQLHELVEADIAVQAERVRAVSASALRFCDPGKEYRPCDPQLVSERVATLEQSYEALCELAATRRARLEESRRLWRFLWEVGEAEAWVREQQHLLASAETGRDLTGVLRLLNKHTALRGEMSGRLGPLKLTLEQGQQLVAEGHPGANQASTRAAELQAQWERLEALAEERAQRLAQAASLYQFQADANDMEAWLVDALRLVSSPEVGHDEFSTQALARQHRALEEEIRAHRPTLDALREQAAALPPALSHTPEVQGRVPTLEQHYEELQARAGERARALEAALAFYTMLSEAGACGLWVEEKEQWLNGLALPERLEDLEVVQQRFETLEPEMNALAARVTAVSDIAEQLLKASPPGKDRIIGTQEQLNQRWQQFRSLADGKKAALTSALSIQNYHLECTETQAWMREKTKVIESTQDLGNDLAGVLALQRKLAGTERDLEAISARVGELTQEANALAAGHPAQAPAINTRLGEVQTGWEDLRATMRRREESLGEARRLQDFLRSLDDFQAWLGRTQTAVASEEGPATLPEAEALLAQHAALRGEVERAQSEYSRLRTLGEEVTRDQADPQCLFLRQRLEALGTGWEELGRMWESRQGRLAQAHGFQGFLRDARQAEGVLSSQEYFLSHTEMPGTLQAADAAIKKLEDFMSTMDANGERIRGLLEAGRQLVSKGNIHAEKIQEKADSIEKRHRKNQEAVQQLLGRLRDNREQQHFLQDCQELKLWIDEKMLTAQDVSYDEARNLHTKWQKHQAFMAELAANKDWLDKVDKEGRELTLEKPELKVLVSEKLEDLHRRWDELETTTQAKARSLFDANRAELFAQSCSALESWLESLQAQLHSDDYGKDLTSVNILLKKQQMLEREMAVREKEVEAIQAQAKALAQEDQSAGEVERTSRAVEEKFRALCQPMKDRCRRLQASREQHQFHRDVEDEILWVTERLPMASSLEHGKDLPSVQLLMKKNQTLQKEIQGHEPRIADLKERQRTLGTAAAGPELAELQEMWKRLSHELELRGKRLEEALRAQQFYRDAAEAEAWMGEQELHMMGQEKAKDELSAQAEVKKHQVLEQALADYAQTIKQLAASSQDMIDHEHPESTRLTIRQAQVDKLYAGLKELAGERRERLQEHLRLCQLRRELDDLEQWIQEREVVAASHELGQDYEHVTMLRDKFREFSRDTSTIGQERVDSANALANGLIAGGHAARATVAEWKDSLNEAWADLLELLDTRGQVLAAAYELQRFLHGARQALARVQHKQQQLPDGTGRDLNAAEALQRRHCAYEHDIQALSTQVQQVQDDGLRLQKAYAGDKAEEIGRHMQAVAEAWAQLQGSSAARRQLLLDTTDKFRFFKAVRELMLWMDGINLQMDAQERPRDVSSADLVIKNQQGIKAEIEARADRFSACIDMGQELLARNHYAAEEISEKLSQLQSRRQETAEKWQEKMDWLQLVLEVLVFGRDAGMAEAWLCSQEPLVRSAELGCTVDEVESLIKRHEAFQKSAVAWEERFSALEKLTALEERENEQKRKREEEERRKQPPTSEPMASQPEGSLVDGQRVLDTAWDGTQSKLPPSTQAPSINGVCTDTESSQPLLEQQRLEQSNVPEGPGSGTGDESSGPRGERQTLPRGPAPSPMPQSRSSESAHVATLPARGAELSAQEQMEGTLCRKQEMEAFNKKAANRSWQNVYCVLRRGSLGFYKDARAASAGVPYHGEVPVSLARAQGSVAFDYRKRKHVFKLGLQDGKEYLFQAKDEAEMSSWLRVVNAAIATASSASGEPEEPVVPSASRGLTRAMTMPPVSQPEGSIVLRSKDGREREREKRFSFFKKNK
Protein: GH18520p (Q961L2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSYITTNIGRISRALFSIVLRQNNAVLSGNMLQLCKMFERRQWDFDCHLKQFPTINAETIDKLERRGLSVYRLRDMEHRELKEWLRSNTYADLVIRSAHELPLLEVEASLQPITRTVLRIKVDIWPSFTWNDRVHGKTCQSFWLWIEDPESNYIYHSELFQVTRKLVMSGQSQQLVMTIPLKEPLPPQYYIRVSSDNWLGSTTCIPLSFQHLVLPEHHPPLTELLPLRPLPVSCLKNVVYESLYKFTHFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVKERIADWEQRFQRSSLGLKVVELTGDVTPDIQAIRESQLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIHLLGEDRGPVIEVIVSRTNFISSHTGRAIRIVGLSTALANAQDLANWLGINKMGLYNFKPSVRPVPLQVHINGFPGKHYCPRMATMNRPTFQAIRTYSPCEPTIVFVSSRRQTRLTALDLITFVAGESNPKQFLHIPEDEIELILQNIREQNLKFCLAFGIGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLPAHLVVIKGTEYFDGKVKKYVDMPITDVLQMMGRAGRPQFDNEGVAVVLVHDEKKNFYKKFLYDPFPVESSLLGVLPEHINAEIVAGTVQSKQAALDYLTWTYFFRRLLRNPSYYQLQDIEPENVNNFMSNLVERVVYELSAAACLVERDGCLIPTFLGRISSYYYLSYRTMKHFLEDLQPWHEHQESSPRHSRFL
Protein: GTPase activating protein BUD2 (Bud site selection protein 2) (Q5A506)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: GTPase activating protein (GAP) for RSR1 which is involved in the polarization of yeast and hyphal cells. Directs the site of new daughter cell growth in yeast and hyphal cells. Important for hyphae to maintain linear growth and necessary for hyphal responses to directional cues in the environment (tropisms). Required for correct localization of the septin rings and stabilization of the polarisome at hyphal tips. Involved in cell adhesion.
Subcellular location: Cytoplasm, cell cortex. Cell tip. Cell septum. Note=Enriched just behind the apices of hyphal tips, appearing as a faint ring at the membrane with a relatively reduced intensity at the extreme tip. Also enriched in the concave angle of some curved hyphae and shows discrete localization to septa.
Interaction partners:
- Ras-related protein RSR1
- Ras family guanine nucleotide exchange factor
- Ras-like protein 1
- Cell division control protein 42 homolog
Sequence:
MPPAYQSAFHKIISRDKGVFEGHNFLVSVDTINWIHVNTLTITEQGQLFSSDSKDNHYLLLQSLQSCFIQIYPDSNISGSGKSSISQPPPTTSTRRNLLRKSSNLNSSDQSHSKSSEDNEHQPPAILIKTFDNDKLYIRIPSKANFGNLLSCLMVWQNLKPQGLAKKWYCENKVIEGFNPNAPIYELLVCRFKIYGPLPNKYKNLNIVPGPKAPVYQQKMDDFKANFDNSYIITPQISSDNHNSINEGWFYAMGALNSHGILNFISELDGTLLYSIDIKQILSSEIREMHNSIFNSSNILFIGQLKELRYNNVIRTLSTLTPDQLLTPFLTRDGKIIPNNQRILIEFPLHIDLEDWFVGLNYFAKREYIGSFDNESKLIHNVEHPQLYDFSKANFRVSKKMSIDIIEAKFENTETNKSGKIYAEVRMWGFPWSRTAIVNHTNNPFWKEEFSTDLPISTQMVHILIKKCSFNDSSYSTGDKLIGTVYVTPDILTKQIKTTSTIMTSSESSQAIQMNTVPLSSMASNSNAGLDIVRLTINDPNNIPIGKLLLEVHLQEYHILSPSVFKPLEKMLVNAPMKDLIKFCNENVPSSDFERVSLVLLDIFQSLEVEDDWFKSLMEVELVNVDIMTRKNYHQRNSQDQAVSNSKTQQQSSHNNVFNTLFRGSSIFSKSLEKYNLRIGQEYLEKVFGDFFAKISNEKKNCEVDPRYVRIQERALRKGKSIHEATGLENGQNEDVSDDDDDDDDNSSDDDADYNAEKERERNERIKQMVEENFQNLYGYVEEIWYKIYITSNDLPDQIKLQLKNFRTKVELVCDPEDKVTSLNCLSAFIFLRFFCPAILNPKLFYLAKNHQTGSTQRTLTLIAKILLNFANRQEFSPHKEPHLVRMNVFLRKHTPEIYDYFDKLTGRKNDFNEKILDLSHEVKRFDLGLDKTSNELPTTPYLIDKYLRLTEIVHLLDYSKYVKNIGNNNNGSMSNLGTPVNSPSRDMEREQDRSRSRSQSGTPDLDPILNLSDLKLNYENKYQIGSLEFEKSEFLELTGDNETEGFIKSLCKGNEEIFSFINSNITLKDIQKQSTKIMNKIQELEIYLENYEFPNNYKDQIIWDSFTDDIMNKCWLDTSRNCLIYSDHVPSSNNQYKKLVDHAFSGLKLKFNDHQKLNGNSTMNSLINNGGMGNRNGHDVNGHNNNNNNNNNNTGDGYNETDRNQRLSSTFSTISIGSAIKPNTSKNPFKKWLRKN
Protein: Myeloid differentiation primary response protein MyD88 (P22366)
Organism: Mus musculus (Mouse)
Function: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Increases IL-8 transcription. Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. Upon TLR8 activation by GU-rich single-stranded RNA (GU-rich RNA) derived from viruses, induces IL1B release through NLRP3 inflammasome activation (By similarity). MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine. Mediates leukocyte recruitment at the inflammatory site.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17018642}. Nucleus {ECO:0000250|UniProtKB:Q99836}.
Interaction partners:
- Toll-like receptor 2
- Toll/interleukin-1 receptor domain-containing adapter protein
- Interleukin-1 receptor-associated kinase 4
- Interleukin-1 receptor-associated kinase-like 2
- Toll-like receptor 9
- Interferon regulatory factor 7
- Toll-like receptor 8
- Interleukin-1 receptor-associated kinase 1
- Toll-like receptor 4
- Interleukin-1 receptor type 1
Sequence:
MSAGDPRVGSGSLDSFMFSIPLVALNVGVRRRLSLFLNPRTPVAADWTLLAEEMGFEYLEIRELETRPDPTRSLLDAWQGRSGASVGRLLELLALLDREDILKELKSRIEEDCQKYLGKQQNQESEKPLQVARVESSVPQTKELGGITTLDDPLGQTPELFDAFICYCPNDIEFVQEMIRQLEQTDYRLKLCVSDRDVLPGTCVWSIASELIEKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGVQQKRLIPIKYKAMKKDFPSILRFITICDYTNPCTKSWFWTRLAKALSLP