wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein, isoform C (M9PG36)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
METLPCANQLQEHQQPQQQHVNLSIDPSLGENVVSIPKELILISLVSQEQSLYNPKHPHYRSTKIKDEKWLEIGSNVGWSDVQCKSKWKAMRDQYCRELKRAKACSKAVKWKYFKELDFLRPYALARKGRSGQTSNGAVGTVTPLSLPMTTSFSSNSSSQNLNLSGSIKIEDASASTLLDSCSFSSPSSTDKKPAATFLASHIGAVLQQQQQQQQHQQQMHSQPEANWNYLTDAGGGATPSIIVQCGTANTTTVVDTLYNEIVDCVNAANQSSSAATITSNVSTTSAAHNQSTNAEEEDDDPIHTFLNMESYFEKELITLIQQEDMIYNYGNENYRNAKLKMEVWEEIARKLKKSVKQCRLKWKALRDQYAREHKRLRTLMHIDATSRWKHYNSLSFLQKYIQQKTLESDSQLSMLLPKNDPVRELEDHMTQSHSPPTQQITLESSSSNSQLNLPTLPHLTGPHKAEQQQQQQQQEEQHQQQQQHQQQQQQQQASELCVATYDDMDIENYINGDVHHNDDDVEDDEDEEMETTTAAEQPPQQQDQHVMTYDHEDGPVYMAVPSVGSAMSKQEQLSDGATSLENQQLQSTAEFQKIEIQTPTTPRYQNAATTPSSTSTSRYHSAPITPSKPTHMEYPSSNGHNSGEDDEIGAFFKAVSMKIRNAQLEPVAFTELQIDILRVINEALRNH
Protein: Atypical chemokine receptor 2 (V9GYB7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Early endosome {ECO:0000256|ARBA:ARBA00004412}.
Interaction partners:
Sequence:
MAATASPQPLATEDADSENSSFYYYDYLDEVAFMLCRKDAVVSFGKVFLPVFYSLIFVLGLSGNLLLLMVLLRYVPRRRMVEIYLLNLAISNLLFLVTLPFWGISVAWHWVFGSFLCKMVSTLYTINFYSGIFFISCMSLDKYLEIVHAQPYHRLRTRAKSLLLATIVWAVSLAVSIPDMVFVQTHENPKGVWNCHADFGGHGTIWKLFLRFQQNLLGFLLPLLAMIFFYSRI
Protein: D-glyceraldehyde dehydrogenase (NADP(+)) (GADH) (Glyceraldehyde DH) (EC 1.2.1.89) (Q9HK01)
Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Function: NADP-dependent dehydrogenase of the nED (non-phosphorylated Entner-Doudoroff) pathway with highest activity towards glyceraldehydes (e.g. D,L-glyceraldehyde and D-glyceraldehyde), to a lesser extent towards D,L-glyceraldehyde-3-phosphate and glycolaldehyde, but no activity towards aliphatic or aromatic aldehydes.
Interaction partners:
- Uncharacterized DapA-like lyase Ta1157
- Probable 2-keto-3-deoxy gluconate aldolase
- Glycerate kinase related protein
- Probable aldehyde ferredoxin oxidoreductase
- Tungsten-containing aldehyde ferredoxin oxidoreductase related protein
- Tungstealdehyde ferredoxaldehyde ferredoxin oxidoreductase related protein
Sequence:
MDTKLYIDGQWVNSSSGKTVDKYSPVTGQVIGRFEAATRDDVDRAIDAAEDAFWAWNDLGSVERSKIIYRAKELIEKNRAELENIIMEENGKPVKEAKEEVDGVIDQIQYYAEWARKLNGEVVEGTSSHRKIFQYKVPYGIVVALTPWNFPAGMVARKLAPALLTGNTVVLKPSSDTPGSAEWIVRKFVEAGVPKGVLNFITGRGSEIGDYIVEHKKVNLITMTGSTATGQRIMQKASANMAKLILELGGKAPFMVWKDADMDNALKTLLWAKYWNAGQSCIAAERLYVHEDIYDTFMSRFVELSRKLALGDPKNADMGPLINKGALQATSEIVEEAKESGAKILFGGSQPSLSGPYRNGYFFLPTIIGNADQKSKIFQEEIFAPVIGARKISSVEEMYDLANDSKYGLASYLFTKDPNIIFEASERIRFGELYVNMPGPEASQGYHTGFRMTGQAGEGSKYGISEYLKLKNIYVDYSGKPLHINTVRDDLFQ
Protein: Tubulin alpha chain (Q5VLK2)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Protein: Translationally-controlled tumor protein homolog (TCTP) (Q7ZYF2)
Organism: Xenopus laevis (African clawed frog)
Function: Involved in calcium binding and microtubule stabilization.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MIIYKDCITEDEMFSDIYKIIETPDGMCLEVEGKVIQREEGAIDDALIGGNASAEFQEDDVGGSSLTSGVDIVMNHKLQETGFTKDSYKNYIKDYVKQLKAHLEKTNPERVNTFMKGAQETVKKILGNFKNYQFYTGERMNPDGMVGLLDYREDGITPFMIFFKDGLIIEKC
Protein: DExD/H box helicase 60 (E9PZQ1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEKKYTGFLKIMSHLILETMSKADYSSLFNDFVESEFFLIDGDSLLITCACERSLKPGQSLHFFYLVERYLLDVISKGGQFAIVFFKDAEYAYFNVPELLTLRTALILHLQKNTTVEVWTKFSNCLSEEWNICLGQSCPYFLILADEGLNDLQTHLFNFVVIQAWAAKVNIVLFSGQTSDILRLYAYFMQSSHGMQMFFKENKRMIMIVYKSLIQQLEKYRDMALAHLFGDLKFNDMEEKVCETVSLLKQLWPEGSDIRCVFCVTSCSLFLEMYHCYLESREKGASEEMSKVKQKTDNCLTLKDMEDFCKLHCLSVALLLHVPLSQRARSRFITANWIQDLKTVLKMKKWCEYFILSNLDMFESWSLNLLHLSDLSDEPLLRNIAFYYENENKEGLDLNVGDAIMNEYVHLWDTVSKLVRKFDVGKPIPLRTTKVHFLEKTPSPIKESSQEMMPNLGFIPMSCNLVDEFTGDILKDLPFLMSDDPIVTSLVKHKEFDELVHWHSHRPLSDDYDRTKCIGDANRRDPNHLKRLQKYHSFQRFYGESLESVTSKTITTQGPKPKKDCIKSKSTKAHETKAEIIKRENKKRLIAEEEQKEEQKWNALSFSIEEEMRKNVDSGMKKLEEFLKSCKSRSVKAQVERVGLQACLKAWKEHCQAEGETTKDLSIAVNMMKRIHSLLDKHSELLQEADQKLIARCLKYLGFCELAVSLYPTQDASDGIKMKKKNKYSVGIGPARFQLQYMGHYLIREERKDPDPRVQDFIPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQVAATVEYRYAKNMPAGESLCGVFTRDYRHDALNCQVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIRCPFLALSATISNPQHLTEWLQSVKRYWKQVDSTMEERTVSKRTGTSRGSYYKDQAQARQSYKVRLVLYGERYNDLEKYLCSVRQGDVCFDHFHPCAALTIDHIEKYGFPSDLALSPRESIQLYDTMCQVWKSWPQAQSLCPENFTQFKNKIVIKKLDARKYEESLKEEFTNWVKNGNEEEARMVLKKLSPDYHEHSGRMLDFFPCLVEKLRKMEKLPALFFLFKLNIVEECAENAFEFLEKKQEEKRPPKADKEARTTANKLRKVKKSLEKQKTVDEKGQKSSRRLDESVMHETEHNYLLQTLEKNLEIPKDCTYANQKAIDDQLLQRVFHRVRFERKGETLKRLAERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVYLDALNYRQMSGRAGRRGQDLLGDVYFFDIPLPKIGKLIKSKVPELRGQFPLSISLILRLMLLASKADDLEDGKAKALSVLKHSLLSFKQPRAIDMLKLYFLYSLQFLVKEGHIDQEGNPTGFAGLVSHLHYHEPSNLVFVSFLVKGLFHKLCQPTREGPKRFSEDVMEKLVLVLANLFGRRYIPAKFYEVNSKFYQSKVFLDDLPEDFSHALLEYNTQVTEDFASFLLMVSRLADMKQEYQLSLSKIEFTGKECEDSPLVSHLMNCKEGRVAVSPFVCLSGNFDVDLLSPGVPNHVILHTLGINHTQAPVLWPYALDSQGRKIPLNAYALDFYKHGSLIGLVQDNRIHPGEAYSLLKDFNLIIKSISVSLRELCENEEDNVVLAFEQLSTSFQEKFELV
Protein: Cytochrome P450 monooxygenase ausI (EC 1.-.-.-) (Austinoid biosynthesis clusters protein I) (Q5AR27)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Cytochrome P450 monooxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- FAD-dependent monooxygenase ausM
- Austinoid biosynthesis clusters protein J
- Aldo-keto reductase ausK
Sequence:
MLQETISLTPLGQPLIAGFVVVSAVLYLLYNTQQWRPNNLPLLNDGGPFDFLQVTAVNRFRRDARRLIKSGFDSYKNVFAMRTDVGVELFASPEYADQFRNHPSLKVFPFTAKMHHGHLPGFELCRSQPVEDRILIESVRTQLAQSLGKLIQPLASDIGEAISDRWPSESGWQEIVLGSVVERTIAQGTSSVYCLDEAWPEFVVKMEMALGMASAALSAWPVMLRRIVAKFLPECLELYRIMKSGRELMSRDMRRRTALQASTGEEPLNFFEWFKEASHGEEYDELILNLRIAFASMHGLCDHLVKILLRLSEDPQLVSDLRKEVIQVYETHGWSKTALYHLKLMDSAFKEVQRVDPILFVGRVAVADVTLKDGLIIQKGQSIRISGHTMWDEDKYPDAAHFDPYRFYRLRQAPGQENTAQFTSPTSDHLGFGYGGRACPGRFFAAAVLKISLCHVLMKYDIKPANGETGQHVWEFAAAINANMTAKVLVRRRQPEIQI
Protein: Possible secreted protein (P95206)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Acyl-CoA dehydrogenase FadE7
- Possible conserved lipoprotein LpqK
Sequence:
MGVIARVVGVAACGLSLAVLAAAPTAGAEPTGALPPMTSSGSGPVIGDGDAALRQRISQQLFSFGDPTVQEVDGSDAAQFITAAAAVADRDVASVFLPLQRVLGCQQNTAGSGAGFGARAYRRTDGQWGGAMLVVAKSTVSDVDALKACVKSGWRKATAGTPTSMCNNGWTYPPFADTRRGEEGYFVLLAGTASDFCSAPNANYRTTASSWPG
Protein: DNA replication licensing factor MCM7 (EC 3.6.4.12) (A0A0S2Z4A5)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365012}.
Interaction partners:
Sequence:
MALKDYALEKEKVKKFLQEFYQDDELGKKQFKYGNQLVRLAHREQVALYVDLDDVAEDDPELVDSICENARRYAKLFADAVQELLPQYKEREVVNKDVLDVYIEHRLMMEQRSRDPGMVRSPQNQYPAELMRRFELYFQGPSSNKPRVIREVRADSVGKLVTVRGIVTRVSEVKPKMVVATYTCDQCGAETYQPIQSPTFMPLIMCPSQECQTNRSGGRLYLQTRGSRFIKFQEMKMQEHSDQVPVGNIPRSITVLVEGENTRIAQPGDHVSVTGIFLPILRTGFRQVVQGLLSETYLEAHRIVKMNKSEDDESGAGELTREELRQIAEEDFYEKLAASIAPEIYGHEDVKKALLLLLVGGVDQSPRGMKIRGNINICLMGDPGVAKSQLLSYIDRLAPRSQYTTGRGSSGVGLTAAVLRDSVSGELTLEGGALVLADQGVCCIDEFDKMAEADRTAIHEVMEQQTISIAKAGILTTLNARCSILAAANPAYGRYNPRRSLEQNIQLPAALLSRFDLLWLIQDRPDRDNDLRLAQHITYVHQHSRQPPSQFEPLDMKLMRRYIAMCREKQPMVPESLADYITAAYVEMRREAWASKDATYTSARTLLAILRLSTALARLRMVDVVEKEDVNEAIRLMEMSKDSLLGDKGQTARTQRPADVIFATVRELVSGGRSVRFSEAEQRCVSRGFTPAQFQAALDEYEELNVWQVNASRTRITFV
Protein: Lysyl endopeptidase (EC 3.4.21.50) (Protease IV) (PvdS-regulated endoprotease) (Q9HWK6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Lysine-specific endoprotease. Involved in corneal virulence.
Subcellular location: Secreted {ECO:0000269|PubMed:12419815}. Note=Experiments performed in E.coli.
Interaction partners:
- Elastase
- Serralysin
- Aminopeptidase
- Exotoxin A
- Sigma factor PvdS
- FpvR
- Chitin-binding protein CbpD
- Protease LasA
- Ferripyoverdine receptor
- Immunomodulating metalloprotease
Sequence:
MHKRTYLNACLVLALAAGASQALAAPGASEMAGDVAVLQASPASTGHARFANPNAAISAAGIHFAAPPARRVARAAPLAPKPGTPLQVGVGLKTATPEIDLTTLEWIDTPDGRHTARFPISAAGAASLRAAIRLETHSGSLPDDVLLHFAGAGKEIFEASGKDLSVNRPYWSPVIEGDTLTVELVLPANLQPGDLRLSVPQVSYFADSLYKAGYRDGFGASGSCEVDAVCATQSGTRAYDNATAAVAKMVFTSSADGGSYICTGTLLNNGNSPKRQLFWSAAHCIEDQATAATLQTIWFYNTTQCYGDASTINQSVTVLTGGANILHRDAKRDTLLLELKRTPPAGVFYQGWSATPIANGSLGHDIHHPRGDAKKYSQGNVSAVGVTYDGHTALTRVDWPSAVVEGGSSGSGLLTVAGDGSYQLRGGLYGGPSYCGAPTSQRNDYFSDFSGVYSQISRYFAP
Protein: Cytoplasmic FMR1-interacting protein 1 (Specifically Rac1-associated protein 1) (Sra-1) (p140sra-1) (Q7L576)
Organism: Homo sapiens (Human)
Function: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). May act as an invasion suppressor in cancers.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7TMB8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q7TMB8}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q7TMB8}. Note=Highly expressed in the perinuclear region (By similarity). Enriched in synaptosomes (By similarity). Also enriched in membrane ruffles and at the tips of lamellipodia (By similarity). {ECO:0000250|UniProtKB:Q7TMB8}.
Interaction partners:
- RNA-binding protein FXR1
- Nck-associated protein 1-like
- Abl interactor 1
- Fragile X messenger ribonucleoprotein 1
- Protein BRICK1
- Nck-associated protein 1
- Actin-binding protein WASF2
- Actin-binding protein WASF1
- RNA-binding protein FXR2
- Abl interactor 2
Sequence:
MAAQVTLEDALSNVDLLEELPLPDQQPCIEPPPSSLLYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGQEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMNFMYFQRNAIERFCGEVRRLCHAERRKDFVSEAYLITLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNKITQSLQQQLEVISGYEELLADIVNLCVDYYENRMYLTPSEKHMLLKVMGFGLYLMDGSVSNIYKLDAKKRINLSKIDKYFKQLQVVPLFGDMQIELARYIKTSAHYEENKSRWTCTSSGSSPQYNICEQMIQIREDHMRFISELARYSNSEVVTGSGRQEAQKTDAEYRKLFDLALQGLQLLSQWSAHVMEVYSWKLVHPTDKYSNKDCPDSAEEYERATRYNYTSEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTVYAALQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFSETLQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTRFNKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVMAGSLLLDKRLRSECKNQGATIHLPPSNRYETLLKQRHVQLLGRSIDLNRLITQRVSAAMYKSLELAIGRFESEDLTSIVELDGLLEINRMTHKLLSRYLTLDGFDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTVLPFSQEFQRDKQPNAQPQYLHGSKALNLAYSSIYGSYRNFVGPPHFQVICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKICRLPRHEYGSPGILEFFHHQLKDIVEYAELKTVCFQNLREVGNAILFCLLIEQSLSLEEVCDLLHAAPFQNILPRVHVKEGERLDAKMKRLESKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSFLDDPIWRGPLPSNGVMHVDECVEFHRLWSAMQFVYCIPVGTHEFTVEQCFGDGLHWAGCMIIVLLGQQRRFAVLDFCYHLLKVQKHDGKDEIIKNVPLKKMVERIRKFQILNDEIITILDKYLKSGDGEGTPVEHVRCFQPPIHQSLASS
Protein: Synaptonemal complex central element protein 1 (Cancer/testis antigen 76) (CT76) (Q8N0S2)
Organism: Homo sapiens (Human)
Function: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Requires SYCP1 in order to be incorporated into the central element. May have a role in the synaptonemal complex assembly, stabilization and recombination.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9D495}. Chromosome {ECO:0000250|UniProtKB:Q9D495}. Note=Associates with chromatin. In prophase I stage of meiosis, localizes in the transverse central elements of the central region between lateral elements of the synaptonemal complexes. Found only where the chromosome cores are synapsed. Colocalizes with SYCE2 in the central elements. {ECO:0000250|UniProtKB:Q9D495}.
Interaction partners:
- Synaptonemal complex central element protein 2
- Synaptonemal complex protein 1
- Testis-expressed protein 12
- Synaptonemal complex central element protein 3
- Synaptonemal complex protein 3
- Cohesin subunit SA-3
- Synaptonemal complex protein 2
- Deleted in azoospermia-like
- Protein SIX6OS1
- Meiotic recombination protein REC8 homolog
Sequence:
MAGRSLTSKAEPTAGAVDRAEKAGGQDTSSQKIEDLMEMVQKLQKVGSLEPRVEVLINRINEVQQAKKKANKDLGEARTICEALQKELDSLHGEKVHLKEILSKKQETLRILRLHCQEKESEAHRKHTMLQECKERISALNLQIEEEKNKQRQLRLAFEEQLEDLMGQHKDLWDFHMPERLAKEICALDSSKEQLLKEEKLVKATLEDVKHQLCSLCGAEGPSTLDEGLFLRSQEAAATVQLFQEEHRKAEELLAAAAQRHQQLQQKCQQQQQKRQRLKEELEKHGMQVPAQAQSTQEEEAGPGDVASPKPLKGERPGAAHQAGPDVLIGQEDTLHPDLSPRGFQEIKELF
Protein: Synaptonemal complex protein 3 (SCP-3) (Q63520)
Organism: Rattus norvegicus (Rat)
Function: Component of the synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for centromere pairing during meiosis in male germ cells. Required for normal meiosis during spermatogenesis and male fertility. Plays a lesser role in female fertility. Required for efficient phosphorylation of HORMAD1 and HORMAD2.
Subcellular location: Nucleus {ECO:0000269|PubMed:18391527, ECO:0000269|PubMed:9679134}. Chromosome {ECO:0000269|PubMed:8289794, ECO:0000269|PubMed:9933407}. Chromosome, centromere {ECO:0000250|UniProtKB:Q60547}. Note=It is present in early unpaired cores, in the lateral domains of the synaptonemal complex and in the chromosome cores when they separate at diplotene. It is found axial to the metaphase I chromosomes and in association with pairs of sister centromeres. The centromere-associated protein becomes dissociated from the centromeres at anaphase II and is not found in mitotic metaphase centromeres. {ECO:0000250|UniProtKB:Q60547}.
Interaction partners:
- Synaptonemal complex protein 1
- HORMA domain containing 2
- Breast cancer type 2 susceptibility protein homolog
- SPO11, initiator of meiotic double stranded breaks.
- Phenylalanyl-tRNA synthetase subunit alpha
- Synaptonemal complex central element protein 1
- Meiotic recombination protein REC8 homolog
- Probable E3 SUMO-protein ligase RNF212
- Stimulated by retinoic acid 8
- Deleted in azoospermia-like.
Sequence:
MLRGCGEVGAVDCSPEQLNKHLKMVPGGRKHSGKSGKPPLIDQPKKAFDFEKEDKDLSGSEEDAVDEKTQVFDKHGKKRSAGIIEDVGGEVQNMLEKFGADINKALLAKKKRIEMYTKASFKASNQKIEQIWKTQQEEIQKLNNEYSQQFLSVLQQWELDMQKFEEQGEKLTNLFRQQQKIFQQTRIVQSQRMKAIKQLHEQFIKSLEDVEKNNDNLFTGTQSELKKEMAMLQKKVMMETQQQEMANVRKSLQSMLF
Protein: HLA class I histocompatibility antigen, alpha chain E (MHC class I antigen E) [Cleaved into: Soluble HLA class I histocompatibility antigen, alpha chain E (sHLA-E)] (P13747)
Organism: Homo sapiens (Human)
Function: Non-classical major histocompatibility class Ib molecule involved in immune self-nonself discrimination. In complex with B2M/beta-2-microglobulin binds nonamer self-peptides derived from the signal sequence of classical MHC class Ia molecules (VL9 peptides). Peptide-bound HLA-E-B2M heterotrimeric complex primarily functions as a ligand for natural killer (NK) cell inhibitory receptor KLRD1-KLRC1, enabling NK cells to monitor the expression of other MHC class I molecules in healthy cells and to tolerate self. Upon cellular stress, preferentially binds signal sequence-derived peptides from stress-induced chaperones and is no longer recognized by NK cell inhibitory receptor KLRD1-KLRC1, resulting in impaired protection from NK cells. Binds signal sequence-derived peptides from non-classical MHC class Ib HLA-G molecules and acts as a ligand for NK cell activating receptor KLRD1-KLRC2, likely playing a role in the generation and effector functions of adaptive NK cells and in maternal-fetal tolerance during pregnancy. Besides self-peptides, can also bind and present pathogen-derived peptides conformationally similar to VL9 peptides to alpha-beta T cell receptor (TCR) on unconventional CD8+ cytotoxic T cells, ultimately triggering antimicrobial immune response.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17179229, ECO:0000269|PubMed:37264229, ECO:0000269|PubMed:9427624}; Single-pass type I membrane protein. Golgi apparatus membrane {ECO:0000269|PubMed:17179229}.; SUBCELLULAR LOCATION: [Soluble HLA class I histocompatibility antigen, alpha chain E]: Secreted {ECO:0000269|PubMed:17179229}.
Interaction partners:
- Beta-2-microglobulin
- NKG2-A/NKG2-B type II integral membrane protein
- T-cell surface glycoprotein CD8 alpha chain
- NKG2-C type II integral membrane protein
- Natural killer cells antigen CD94
- NKG2-E type II integral membrane protein
- NKG2-D type II integral membrane protein
- Leukocyte immunoglobulin-like receptor subfamily B member 1
- HLA class I histocompatibility antigen, alpha chain F
- HLA class I histocompatibility antigen, B alpha chain
Sequence:
MVDGTLLLLLSEALALTQTWAGSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPIVGIIAGLVLLGSVVSGAVVAAVIWRKKSSGGKGGSYSKAEWSDSAQGSESHSL
Protein: Late cornified envelope-like proline-rich protein 1 (Novel small proline-rich protein) (Q5T871)
Organism: Homo sapiens (Human)
Interaction partners:
- Small proline-rich protein 2A
- Small proline-rich protein 3
Sequence:
MSSDDKSKSNDPKTEPKNCDPKCEQKCESKCQPSCLKKLLQRCFEKCPWEKCPAPPKCLPCPSQSPSSCPPQPCTKPCPPKCPSSCPHACPPPCPPPE
Protein: Fe(2+) transport protein 3, chloroplastic (Fe(II) transport protein 3) (Iron-regulated transporter 3) (Q8LE59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in the transport of iron in the plastids.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- TPR repeat-containing protein ZIP4
- Metal transporter Nramp3
- Putative cadmium/zinc-transporting ATPase HMA4
- Nicotianamine synthase 2
- Cadmium/zinc-transporting ATPase HMA2
- Metal tolerance protein 1
- Basic leucine zipper 19
- Nicotianamine synthase 3
- Putative inactive cadmium/zinc-transporting ATPase HMA3
- Nicotianamine synthase 1
Sequence:
MFFVDVLWKLVPLYLFGSETKSLSATESILQIVPEAMAATSSNVLCNASESDLCRDDSAAFLLKFVAIASILLAGAAGVTIPLIGRNRRFLQTDGNLFVTAKAFAAGVILATGFVHMLAGGTEALKNPCLPDFPWSKFPFPGFFAMIAALITLFVDFMGTQYYERKQEREASESVEPFGREQSPGIVVPMIGEGTNDGKVFGEEDSGGIHIVGIHAHAAHHRHSHPPGHDSCEGHSKIDIGHAHAHGHGHGHGHGHVHGGLDAVNGARHIVVSQVLELGIVSHSIIIGLSLGVSQSPCTIRPLIAALSFHQFFEGFALGGCISQAQFRNKSATIMACFFALTTPIGIGIGTAVASSFNSHSVGALVTEGILDSLSAGILVYMALVDLIAADFLSTKMRCNFRLQIVSYVMLFLGAGLMSSLAIWA
Protein: Glycogen synthase kinase-3 beta (EC 2.7.11.26) (Q6FI27)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST
Protein: Urease accessory protein UreD (Q09063)
Organism: Klebsiella aerogenes (Enterobacter aerogenes)
Function: Necessary for the functional incorporation of the urease nickel metallocenter.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01384}.
Interaction partners:
Sequence:
MLPPLKKGWQATLDLRFHQAGGKTVLASAQHVGPLTVQRPFYPEEETCHLYLLHPPGGIVGGDELTISAHLAPGCHTLITMPGASKFYRSSGAQALVRQQLTLAPQATLEWLPQDAIFFPGANARLFTTFHLCASSRLLAWDLLCLGRPVIGETFSHGTLSNRLEVWVDNEPLLVERLHLQEGELSSIAERPWVGTLLCYPATDALLDGVRDALAPLGLYAGASLTDRLLTVRFLSDDNLICQRVMRDVWQFLRPHLTGKSPVLPRIWLT
Protein: NADH-dependent flavin reductase (EC 1.5.1.36) (4-nitrophenol 2-monooxygenase, flavin reductase component) (4-nitrophenol hydroxylase, flavin reductase component) (4-NP hydroxylase, flavin reductase component) (Two-component 4-nitrophenol hydroxylase) (Q8RQP9)
Organism: Rhodococcus sp
Function: Catalyzes the reduction of FAD with the concomitant oxidation of NADH. NAD is the physiological electron donor. Subsequently, the reduced flavins diffuse to the oxygenase component NphA2.
Interaction partners:
Sequence:
MTETAGELDPEVTPLHLRKALGRFASGVTIVTTAECEDEDSVHGMTANAFTSVSLDPPLVLVSISTRAKMDTKIRETGTYGISILAGDQEPVSLHFAGAAHEPDRVRFVWRRGVPLLEGALVHLACTVVASHPAGDHTLHVGRVEQLWYDDGHPLVFYTGSFRSLELLGRDEPWGF