wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-synuclein (P37377)
Organism: Rattus norvegicus (Rat)
Function: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (By similarity). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P37840}. Membrane {ECO:0000250|UniProtKB:P37840}. Nucleus {ECO:0000250|UniProtKB:P37840}. Synapse {ECO:0000250|UniProtKB:P37840}. Secreted {ECO:0000250|UniProtKB:P37840}. Cell projection, axon {ECO:0000250|UniProtKB:O55042}. Note=Membrane-bound in dopaminergic neurons (By similarity). Expressed and colocalized with SEPTIN4 in dopaminergic axon terminals, especially at the varicosities (By similarity). {ECO:0000250|UniProtKB:O55042, ECO:0000250|UniProtKB:P37840}.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Synphilin-1
- Tyrosine 3-monooxygenase
- Synaptic vesicular amine transporter
- Parkinson disease protein 7 homolog
- Heat shock 70 kDa protein 4
- Vesicle-associated membrane protein 2
- Amyloid-beta precursor protein
- RCG31562, isoform CRA_c.
- Microtubule-associated protein tau
Sequence:
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPSSEAYEMPSEEGYQDYEPEA
Protein: Autophagy-related protein 30 (C4R5T1)
Organism: Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Function: Acts as the peroxisome receptor for pexophagy. Required for both micropexophagy and macropexophagy, but not for the cytoplasm to vacuole transport (Cvt) or autophagy pathways. Required for functional micropexophagic apparatus (MIPA) and relocation of ATG11 to the peroxisome-sequestering arms of the vacuole.
Subcellular location: Vacuole lumen. Preautophagosomal structure. Peroxisome membrane; Peripheral membrane protein. Note=Surrounds the peroxisome cluster, but a small amount is also inside the vacuole in methanol-grown cells. Upon induction of micropexophagy, localizes inside the vacuolar lumen. Also localizes near peroxisomes during early stages of micropexophagy.
Interaction partners:
Sequence:
MFSRKQVQKRNNELSSLHCSNSSNSLNRIHKNEETAKGTVGVNARGNNRSDNVASPGQLRPRTSSILTDNSEWILFSPENAEGEYVITSSDGIRRTNSNHYYYNYNEDDILSSSRRSSEDVYDAEQEYTEQPVNNHVQVEDEEDDDSIINDLTHVVDDYDYEEEDDKQDLTTRIDNWRKKQVSELLNELNHDDDLDPVLNRDKIDLIQSWGIENEKLNTKPRAKKRQRKSKRASFYGQDLLSKYSMEDLKIIKQIVAQLRDDLDKVKHDKPSSPLPNYHNTLKQAPSSNSQNPSFISYYSNYLTKNNSQQTPNSQSTSGSLLNNPNLEKYLPLFLKNLLYEDSNGSHQHPETSEKEHFWDNDLKSVNSSILTLSSNSKLKQEIL
Protein: DH domain-containing protein (O02134)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKRTLPRFLSFRRSKRRLITSVSAPLIVMNYHDGHQYELDSKDVPSCSGESTPAGTLSPRRETREVTNAFDEMIATEISYVADLKDIIIHYLEPFEATENQNSLPDTLRGKPDCLFGNVRELYKFHHRTVLEDLVAARSTAEMCRVLMQHRNQIYVTYRTYCQIHGSNQKVRDSVKNHPFFKECQRNANHNMDMSSYLLKPIQRIMKYQLLLGNIMDDCPADVRDEVAMTRDSMVELLNQIDASMQQLHISGYNGDLKSLGLLRLQTECDVFTYNRKKKAKLSRAQKRFIFFFDGAVMFCKKRVSNPGTTLNSEPEYFEHKFCIPIISLGYDTSSRTGASRFEVWDDAKTDAYVIETIDQTARTKWIQRLGKSETAQDACLENRQRPKSWASTVSNESSCSSSTRESDSTDSTMDTNGNTQTTQVDVPYSPTLDSSIDLSMDTTTPLRTSEINNEVELVDSC
Protein: Target of rapamycin complex 2 subunit BIT61 (TORC2 subunit BIT61) (61 kDa binding partner of TOR2 protein) (P47041)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Target of rapamycin complex 2 subunit TSC11
- Target of rapamycin complex 2 subunit AVO2
- Target of rapamycin complex 2 subunit AVO1
- Target of rapamycin complex subunit LST8
- Serine/threonine-protein kinase TOR2
- Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
- Target of rapamycin complex 1 subunit TCO89
- Serine/threonine-protein kinase TOR1
- Probable target of rapamycin complex 2 subunit BIT2
- Target of rapamycin complex 1 subunit KOG1
Sequence:
MTAEDILLRERTSTTTQRPVNSEQYLNVQLATAPVKNFQTTSEISRQTLVDTSNDDVYSIKNLKGSRNPISPSVSNVGFQSIFHTVDHPRSKVSVASNHSLRSNDNASAATSKSGSSQIGESHSVDTVECSNNLSKKLSSDAISITQKSLHSTPSGRYMKGKASGFFNRRNRAHTTISSDPASFLTDSSTLHNSSHSFRNVIKNFFQNKSHRHIGQDAIEPAIPNSLSKFLHSSYGRHKSPSQFIHTNAGQLVDSGTSVYSLNVNPSGVNPNTIVEDPLSGTDPASPNPVSMLHDLLRNLPSLEANYKHFNSQELTTLTNNIWNIFCSNVAELFRTQRIWKLRAKIENFNEVLEFYCILKTDPRVTHSGMNRIISDLKEFLVSSLYNLENQIVFNYSNEDTINNALKRLGVIWRIFYQEVYYDLAAVLLPLDQSIREDGNSTVLKSGNESRTHINGNYSIGFLLLMCFRDSIVLPCYENFVNSNDGISKSFQLYIFNQEEESNVTETDKLTLLQCFGILSTIQSNDRNQRIIEELLAGIRMSI
Protein: At5g04440 (RAP release 2, galactose-binding-like domain protein, putative (DUF1997)) (Q500X2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Emb|CAB85507.1
- Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial
Sequence:
MALSSATLRLTSLSFSAKKTNRNPRNPALSFTITSSSSFDESPKPSSLATSSSTSPIRVSSSSTPKARFIARQKQSVSVRQLQRPLIEYMSLPASQYSVLDAERIERVDDNTFRCYVYTFKFFNFEVCPVLLVRVEEQPNGCCIKLLSCKLEGSPVVVAQNDKFDASMVNRVSCDSTQEGSSEQQITSDAVIEVNIEIPFAFRVFPVGAIEATGTQVLDQILKLMLPRFLSQLSKDYHAWASGDTSRQPLGTGEI
Protein: GH21964p (Kermit, isoform A) (Kermit, isoform B) (Kermit, isoform C) (Kermit, isoform D) (Kermit, isoform E) (LP09416p) (Q7JX82)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Myosin heavy chain 95F
- Unconventional myosin IC
- Receptor-type guanylate cyclase Gyc76C
Sequence:
MPLFTRKSPKQGPTSDGGSQFGSRSSMNSGSSQGSHISNNNNNSIPEKTKPPLVFHCQLAHGSPTGLIHDFSSVRELYQKIAECFDISEKDILFCTLNSHKVDMTRLLGGQIGLDDFIFAHRKGRPKEIEIVKSQDALGLTITDNGAGYAFIKRIKEDSIIDRIEHISVGDHIEKLNGQNMVGKRHYEVARMLKDIATGETFTLRLVEPVRSGFQGIGPRSQSRASGSAGGKNYGSGKETLRFKANGNAQIEPQFDEATVAGIEAINNLLESFMGINDTELASQIWDLGDQKSNSMDFAEAIDNSDLESFGFTDDFIIELWGAITDARRKSTTSPK
Protein: Probable MRF1 mitochondrial N(5)-glutamine methyltransferase mtq1 (EC 2.1.1.297) (O14028)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Methylates MRF1 on 'Gln-270' using S-adenosyl L-methionine as methyl donor.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P53944}.
Interaction partners:
- Putative peptide chain release factor 1, mitochondrial
- eRF1 methyltransferase catalytic subunit mtq2
- Protein arginine N-methyltransferase 2
- Alpha N-terminal protein methyltransferase 1
- Multifunctional methyltransferase subunit trm112
- tRNA wybutosine-synthesizing protein 2
- Protein-lysine N-methyltransferase efm4
- Protein arginine N-methyltransferase 1
Sequence:
MRLPRITKFALYRENPCLLPLYHATRDPSLAKREWTWICKELKLLYPEISKHGLRKKIVNACQLRARNYPLQYILKSQPFGNIKIDCQQGVLIPRWETEEWVERVVDKLNRLERLKPLKILDLCTGSGCISSFVLANLRVPHTIEAVDVSKKALKLAVKNCDRAIAHGTVGKINFHQIDVLNEHERVESLLQTSHVLLCNPPYISDDDFAAQTDISVRKYEPKLALLAKNGGNEFYYKFSQYIKRMLQRNAKDFVPLSLIVFEIGSTHQAKIVKSLFDDTNWQANIEQDGAHQDRVVIITRKDRRLIDI
Protein: P-type Cu(+) transporter (EC 7.2.2.8) (E7ET55)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}. Membrane {ECO:0000256|RuleBase:RU362081}.
Interaction partners:
Sequence:
MPEQERQITAREGASRKILSKLSLPTRAWEPAMKKSFAFDNVGYEGGLDGLGPSSQVATSTVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFEASIAEGKAASWPSRSLPAQEAVVKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAAIKSKVAPLSLGPIDIERLQSTNPKRPLSSANQNFNNSETLGHQGSHVVTLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEALPPGNFKVSLPDGAEGSGTDHRSSSSHSPGSPPRNQVQGTCSTTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSESCSTNPLGNHSAGNSMVQTTDGTPTSVQEVAPHTGRLPANHAPDILAKSPQSTRAVAPQKCFLQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVMEDYAGSDGNIELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIELLGGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLVILVVAVAEKAERSPVTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFIDFGVVQRYFPNPNKHISQTEVIIRFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATLPLRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLGYCTDFQAVPGCGIGCKVSNVEGILAHSERPLSAPASHLNEAGSLPAEKDAVPQTFSVLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIGIVLQPWMGSAAMAASSVSVVLSSLQLKCYKKPDLERYEAQAHGHMKPLTASQVSVHIGMDDRWRDSPRATPWDQVSYVSQVSLSSLTSDKPSRHSAAADDDGDKWSLLLNGRDEEQYI
Protein: Protein PARTING DANCERS homolog (OsPTD) (EC 3.1.-.-) (Protein PARTING DANCERS homolog 1) (OsPTD1) (Q6L5B5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Essential for normal crossover (CO) formation during meiosis. Essential component for the formation of class I meiotic COs. Interacts with SHOC1, another meiotic component, to regulate CO formation, possibly by stabilizing the recombination intermediates during meiosis. PTD and SHOC1 may form transient heterotrimeric or heterotetrametric complexes with HEI10 and/or ZIP4 to promote class I COs formation. Does not seem to be involved in early meiotic recombination steps involving double-strand break (DSB) formation, processing, and single-strand invasion. Does not seem to be involved in homologous pairing or synaptonemal complex (SC) assembly.
Subcellular location: Chromosome {ECO:0000269|PubMed:31266799}. Nucleus {ECO:0000269|PubMed:30589140, ECO:0000269|PubMed:31266799}. Cytoplasm {ECO:0000269|PubMed:30589140}. Cell membrane {ECO:0000269|PubMed:30589140}. Note=Predominantly localized in the nucleus (PubMed:30589140). Localized in punctuate foci onto meiocyte chromosomes from leptotene to early pachytene with a maximal number of foci at zygotene (PubMed:31266799). {ECO:0000269|PubMed:30589140, ECO:0000269|PubMed:31266799}.
Interaction partners:
Sequence:
MERSTHSTGWTCLPPPPPEPAAPGRGVCAMSTSWRDKQQPSLINFIAAFLAANSYRLNFLSISPDFIFNNGELSVAFIFETNWDCQNEGAVFSRVNMLKRQLKHLYVVVAVPTKEQNESFNRSYHKYGMKLGFPTFVPVTDPEMGFEKIVKIAHALGVCKQQDIISRLKNEREQAVQCTDSFLRVLTSIPGIDNHDANALAQAIGSIEAIAKASKKFILENTDLSTDKAETIVRFFRDPQYYLSPKIN
Protein: Protein NrdI (Q8ZDC6)
Organism: Yersinia pestis
Function: Probably involved in ribonucleotide reductase function.
Interaction partners:
- Ribonucleoside-diphosphate reductase 2 beta chain
- Ribonucleoside-diphosphate reductase
- Putative glutaredoxin
- Similar to Escherichia coli ribonucleoside-diphosphate reductase 1 beta chain NrdB or FtsB SW:RIR2_ECOLI
- Ribonucleoside-diphosphate reductase 1 alpha chain
- Glutaredoxin
- Similar to Vibrio cholerae peroxiredoxin family protein/glutaredoxin VC2637 TR:Q9KNU3
- Glutaredoxin 1
- Similar to Escherichia coli anaerobic ribonucleoside-triphosphate reductase NrdD SW:NRDD_ECOLI
Sequence:
MNPLVYFSSSSENSHRFVEKLQLPAIRIPIAGAREKLRVEQPYILLVPSYGGGSPVGAVPIQVIRFLNDVHNRSLIRGVIAAGNTNFGDAYCLAGDIISHKCQVPYLYRFELLGTAEDVANVRKGVTEFWQRQN
Protein: Arachidonate 5-lipoxygenase-activating protein (F1QKS8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}.
Interaction partners:
- Leukotriene C4 synthase
- Si:dkey-17e16.9.
Sequence:
MYASVMDNIFLLVLVTLLSVVQNVFFALKVEKECTGHQSKRSAAFERLSCAKRNCMDTYPTFLAVLWCAGICLSQAPAAFAGILYLVVRQKYFVGYLGETCQSTPGFLFGKRILFFLSLMCVVGIINHLMLTYGGSDYKEYIQTITKAASTLLLLP
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (Q386Y6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367045}.
Interaction partners:
- Sec1 family transport protein, putative
- Paraflagellar rod component
- Soluble N-ethylmaleimide sensitive factor
- Soluble N-ethylmaleimide sensitive factor
- Gamma-soluble NSF attachment protein
- t-SNARE coiled-coil homology domain-containing protein
- Target SNARE, putative
- Vesicle transport v-SNARE N-terminal domain-containing protein
- Vesicle-associated membrane protein, putative
- Syntaxin 5
Sequence:
MIVKTTVSKRQAFRTLNPLSSLFLLCACVACLYSVNLGAASYHPGGPAKYSNYQRLEILWITGCTRPVLTERGRQTISCFSDLNSYHPVQLTVRGRGFPQLGNLSIVLEEHTPIPHHGGEEDLDLISMPCLHVRPSSLFPRQILSCTLLNPMDSLRHKPLWLERLTTRSTWMNLKLLQTVTSDNSNKTTIVTLASVPRAVELDLTPYGNGSHSGGEEDEEEDAEDPLEYMFRRVRHSAMNDEWVSLGIGGLSEQLHELFRRVFLSRTRQLRGVVESLNIPPVRGVLLHGPPGTGKTLIARMIAKLEGKGTRVTIVNAADIISKYVGDSEKNLRRLFDANNMWGDDDDEDEHGGTRHASGADEETANSKSLHIVIMDELDALFKRRADLGEESSTKAVYDGLTNQFLTIMDGVNKARNILIIGLTNRLHAIDRALLRPGRFEVVIEVPLPDVKGRREMFFIHTRELRDKDFLAEDVSLDILAERTGGFSGADVAGTVRAAVSHALLRFRDSSLNTSIPTGDIGIEDELSGAATEHFKVTNSDFQLALRDVWDSKAQVNGGQDLAGDGKGLDNAVDKLVDFDGTISRGMGVVRRLMRSIQHSQITNAAVVVIHGSSGSGKTVFARNVVSSIRFSVTKFLTGRELSGRAARDIQEVIDALRDAGAFKGDYCLVVDNVERYVRSGDSGAADALRSAINEFKSVSSSGLFPHSEWDVSQPRRKRLLIITTAEEEVLQGALGSVEYDVRLNLQPIRREGVLKLLHHYGILPQTAKLPNEVVRAYPTSLTYRQFLRITDLALWRAHEEHHRTAETTSTGEAESLETSLYSSLNELFTKGGPQRSGGDHHSPPVLTESQQAELAAAIRDVASEMGISDAFDGVLNADGSIHGEEMY
Protein: Lantibiotic lichenicidin VK21 A2 (LchA2) (P86476)
Organism: Bacillus licheniformis
Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually, LchA2 exhibits activity towards B.subtilis L1 (IC(50)=30 uM), Rhodococcus sp. SS2 (IC(50)=16.6 uM), M.luteus B1314 (IC(50)=2.6 uM), B.megaterium VKM41 (IC(50)=2 uM), S.aureus 209p (IC(50)=20 uM), B.pumilus 2001, B.globigii I, B.amyloliquefaciens I, M.smegmatis 1171 and M.phlei 1291. However, when combined with LchA1, it displays much stronger activity against B.subtilis L1 (IC(50)=0.64 uM), Rhodococcus sp. SS2 (IC(50)=0.64 uM), M.luteus B1314 (IC(50)=0.09 uM), B.megaterium VKM41 (IC(50)=0.12 uM) and S.aureus 209p (IC(50)=0.64 uM). The activity of the combined LchA1 and LchA2 peptides is strongest at a molar ratio of 1. Even when applied at 17-fold concentration of the highest IC(50) values for Gram-positive bacteria, neither the individual nor the combined peptides display activity against Gram-negative bacteria P.aeruginosa PAO1, P.putida I-97 or E.coli C600.
Subcellular location: Secreted {ECO:0000269|PubMed:20578714, ECO:0000305}.
Interaction partners:
Sequence:
MKTMKNSAAREAFKGANHPAGMVSEEELKALVGGNDVNPETTPATTSSWTCITAGVTVSASLCPTTKCTSRC
Protein: Alpha-mannosidase (EC 3.2.1.-) (O97043)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFKLFRRGSARCIGLLSAFVTILLCLYYISIGQPNPTPISETGAPSAALRGSPLSGLTGFSVDGGSSSIIHQQKQQLVIASNQKKSSETKSAQTSVSPEEQSEEQYTNSNWGDKCYELIQSNTNITASEEHSKFDFQPEWMRSKEYWDRGFEERFDAQKKDKQRPPLKIIVVPHSHNDPGWLKTSTNYFQSDSRQILNLLVTKMQEYTDMTFIWSEISFLQLWWDQAHPTKQRALKRLIDAGRIEITTGGWVMTDEANVHIYPMLDQLIEGHQWLKNNLNVTPKVGWSIDPFGHGSTVPYLLSGANFEGTIIQRIHYAWKQWFARQQSGDFIWKPYWRSRKDKDSEAGSLLTHNMPFDIYSIKGSCGPHPFICLNFDFRKIPGEYTEYSVKAQFITDDNLESKAQLLLEQYARTASLFPHNVALIPVGDDFRYNKDREVDQQYQNYKKLIDHIMANRRLYNADIRFGTPSDYFEAIKERMKDHTPGFPTFKGDFFVYSDIFSEGRPAYWSGYFTTRPFYKLLSSELEHQLRSAEIVFTLAYNTARQAKRENAIKIYEKNYELIINARRNLGLFQHHDAITGTSKAAVMRDYAMRLFESTQNMVKMQESCLELLLQKGQPRHHGFLLSEFERDNFNKLPRKMPIQMANGDESTPTVPAGEGGAGGSSSSGSVGSFVLYNSLAQKRLEVVTLRVQHPNVKIVNDKGVELNHIQINPVWNITDTYEQGLGTSVSGTVGRIRTSTRQFEVMFVAELEPLSLSTYRVQVDEVNFKRNIATIYCDDCTESQPASVSPPEEIESSPTSVFEARGKPAGDIQLENPHMRLLFDEKSGFLKTITRKNQKKELLKPLQCNIKFAAYRSAQFHSGAYLFKTDPEQSEAEKEVLEGYTDMRIIITSGPIASDVTVIYGPFLAHTVRIFNTRTHLDAAIYVENDIDFEPPPKNRETELFMRFVTNIDNIAQAPMQRDPLKEPVDAATMPELPVFYSDQNGFQYHERIKVPAIGIEGNYFPITSGAFIQDSRLRLTLLTTHAQGAASYEPGQLEVMLDRRTLYDDYRGMGEGVVDSRLTRHKFWLLVEDLPGGQHVTQPPSYKVLSQQAQQLANALRYPPNLYFVSNLEQPELAAALLPLVRLLPKGPLPCDVHLTTLRTLSDPELQLFPSASALLVLHRQGFDCSVSAGRELSMEAICPLSSKGLGNVQLGRLSLHTIEATSLTGTEQKSSRESYHIRSLAEISLEPMELRTFNLTFRSEV
Protein: Meiosis-specific protein PAIR2 (OsASY1) (Protein HOMOLOGOUS PAIRING ABERRATION IN RICE MEIOSIS 2) (Q76CY8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Essential factor for meiotic homologous chromosome pairing (synapsis). Plays an essential role in promoting homologous chromosome synapsis. Does not seem to play a role in chromosomal axial element formation, sister chromatid cohesion at centromeres or kinetochore assembly in meiosis I.
Subcellular location: Chromosome {ECO:0000269|PubMed:16410547, ECO:0000269|PubMed:21119003, ECO:0000269|PubMed:27436711}. Chromosome, centromere {ECO:0000269|PubMed:16410547}. Nucleus {ECO:0000269|PubMed:21119003}. Note=During interphase-early leptotene, distributed as numerous punctuate foci throughout the chromatin. Associates with chromosomal axes at leptotene and zygotene (PubMed:16410547, PubMed:21119003). Associates with chromosomal axes at zygotene (PubMed:27436711). Removed from the axes of arm regions when homologous chromosomes have been synapsed (PubMed:16410547, PubMed:21119003). Localizes to centromeres until diakinesis (PubMed:16410547). {ECO:0000269|PubMed:16410547, ECO:0000269|PubMed:21119003, ECO:0000269|PubMed:27436711}.
Interaction partners:
- Pachytene checkpoint protein 2 homolog
- Meiotic recombination protein DMC1 homolog A
- Synaptonemal complex protein ZEP1
- Meiotic recombination protein DMC1 homolog B
Sequence:
MVMAQKTKEAEITEQDSLLLTRNLLRIAIYNISYIRGLFPEKYFNDKSVPALEMKIKKLMPMDTESRRLIDWMEKGVYDALQKKYLKTLLFCICEKEEGPMIEEYAFSFSYPNTSGDEVAMNLSRTGSKKNSATFKSNAAEVTPDQMRSSACKMIRTLVSLMRTLDQMPEERTILMKLLYYDDVTPEDYEPPFFKCCADNEAINIWNKNPLKMEVGNVNSKHLVLALKVKSVLDPCDDNNVNSEDDNMSLDNESDQDNDFSDTEVRPSEAERYIVAPNDGTCKGQNGTISEDDTQDPVHEEELTAQVREWICSRDTESLEVSDVLVNFPDISMEMVEDIMERLLKDGLLSRAKKDSYSVNKIADPTTPHIKKEVIMQNVSPTEGTKNSNGDLMYMKALYHALPMDYVSVGKLHGKLDGEASQNMVRKLIEKMVQDGYVKNSANRRLGKAVIHSEVTNRKLLEIKKILEVDIAEQMAIDTNAEPGEPERKDHLSGHEMRDGSTMGCLQSVGSDLTRTRELPEPQQNVSMQSGQEASTVDKDPSRTPTSVREQASVCSLESGVLGQKVRKSLAGAGGTQCSQDKRFRKASTVKEPILQYVKRQKSQVQVQVQ
Protein: Transcriptional enhancer factor TEF-4 (ETEF-1) (Embryonic TEA domain-containing factor) (ETF) (TEA domain family member 2) (TEAD-2) (P48301)
Organism: Mus musculus (Mouse)
Function: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction (By similarity). Binds to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3'). May be involved in the gene regulation of neural development. Binds to the M-CAT motif.
Subcellular location: Nucleus.
Interaction partners:
- Transcriptional coactivator YAP1
- WW domain-containing transcription regulator protein 1
- Transcription factor 7-like 2
- Transcription cofactor vestigial-like protein 4
- Lymphoid enhancer-binding factor 1
- Transcription factor 7-like 1
- Transcription factor 7
- Transcriptional enhancer factor TEF-3
- Transcriptional enhancer factor TEF-1
- Homeobox protein notochord
Sequence:
MGDPRTGAPLDDGGGWTGSEEGSEEGTGGSEGVGGDGSPDAEGVWSPDIEQSFQEALAIYPPCGRRKIILSDEGKMYGRNELIARYIKLRTGKTRTRKQVSSHIQVLARRKSREIQSKLKDQVSKDKAFQTMATMSSAQLISAPSLQAKLGPSGPQATELFQFWSGSSGPPWNVPDVKPFSQAPFSVSLTPPASDLPGYEPPPALSPLPPPAPSPPAWQARALGTARLQLIEFSAFVEPPDAVDSFQRHLFVHISQQCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPHAFFLVKFWADLNWGPSAEEAGSSGGGGGFYGVSSQYESRELMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLLRSPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQYHIYRLVRD
Protein: Uncharacterized protein (Q584I7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTKRHSGRGVETSPDLAFIKRGHLNMLIHTKDGERRLVPVDSLAFIDDPQLVRGRTMDRVNFNNECVFKVTLEFTEPIPCMEEIAVREMTDWVLCSCKGNYSFYSPVEKLLVLQNCMVCVQSNVLPLVDPFILVLFYDEGSWVVERVLK
Protein: Granzyme B (EC 3.4.21.79) (C11) (CTLA-1) (Cathepsin G-like 1) (CTSGL1) (Cytotoxic T-lymphocyte proteinase 2) (Lymphocyte protease) (Fragmentin-2) (Granzyme-2) (Human lymphocyte protein) (HLP) (SECT) (T-cell serine protease 1-3E) (P10144)
Organism: Homo sapiens (Human)
Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse. It cleaves after Asp. Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -9 and -10 (CASP3, CASP9 and CASP10, respectively) to give rise to active enzymes mediating apoptosis. Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:8258716}. Cytolytic granule {ECO:0000269|PubMed:1985927, ECO:0000269|PubMed:24088571, ECO:0000269|PubMed:8258716}. Note=Delivered into the target cell by perforin (PubMed:20038786). {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:8258716}.
Interaction partners:
- Perforin-1
- Granulysin
- Caspase-3
- DNA fragmentation factor subunit alpha
- BH3-interacting domain death agonist
- Serglycin
- SHC-transforming protein 1
- T-cell surface glycoprotein CD8 alpha chain
- Caspase-8
- Serpin B9
Sequence:
MQPILLLLAFLLLPRADAGEIIGGHEAKPHSRPYMAYLMIWDQKSLKRCGGFLIRDDFVLTAAHCWGSSINVTLGAHNIKEQEPTQQFIPVKRPIPHPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGKHSHTLQEVKMTVQEDRKCESDLRHYYDSTIELCVGDPEIKKTSFKGDSGGPLVCNKVAQGIVSYGRNNGMPPRACTKVSSFVHWIKKTMKRY