wanglab/gogpt-training-data huggingface dataset:
Protein: Cohesin subunit SA-3 (SCC3 homolog 3) (Stromal antigen 3) (Stromalin-3) (O70576)
Organism: Mus musculus (Mouse)
Function: Meiosis specific component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750, ECO:0000269|PubMed:22346761}. Chromosome {ECO:0000269|PubMed:22346761}. Chromosome, centromere {ECO:0000269|PubMed:22346761}. Note=Associates with chromatin. In prophase I stage of meiosis, it is found along the axial elements of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. It however remains chromatin associated at the centromeres up to metaphase I. During anaphase I, it probably dissociates from centromeres, allowing chromosomes segregation.
Interaction partners:
- Structural maintenance of chromosomes protein 1A
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1B
- Double-strand-break repair protein rad21-like protein 1
- Meiotic recombination protein REC8 homolog
- Double-strand-break repair protein rad21 homolog
- Synaptonemal complex central element protein 1
- Shugoshin 2A
- Synaptonemal complex protein 3
- Cohesin subunit SA-1
Sequence:
MPTLWSPSTQHHGSSSGSESSPLQKSVRRAQMALSPCSSSILPCDDRDSQGTAEWDSPSTNEDSDFEDSLRRNVKKRAAKQPPKAVPAAKHRKKQSRIVSSGNGKNESVPSTNYLFDAVKAARSCMQSLVDEWLDNYKQDENAGFLELINFFIRACGCKSTVTPEMFKTMSNSEIIQHLTEEFNEDSGDYPLTAPGPSWKKFQGSFCEFVKTLVYQCQYSLLYDGFPMDDLISLLIGLSDSQVRAFRHTSTLAAMKLMTSLVKVALQLSLHKDNNQRQYEAERNKGPEQRAPERLESLLEKRKEFQENQEDIEGMMNAIFRGVFVHRYRDILPEIRAICIEEIGYWMQSYSTSFLNDSYLKYIGWTLHDKHKEVRLKCVKALAGLYSNQELSLRMELFTNRFKDRMVSMVMDRECEVAVEAIRLLTLILKNMEGVLTSADCEKIYSIVYISNRAMASSAGEFVYWKIFHPECGAKAVSDRERRRSPQAQKTFIYLLLAFFMESEHHNHAAYLVDSLWDCAGSYLKDWESLTNLLLQKDQNLGDMQERMLIEILVSSARQAAEGHPPVGRITGKKSLTAKERKLQAYDKMKLAEHLIPLLPQLLAKFSADAENVAPLLQLLSYFDLSIYCTQRLEKHLELLLQQLQEVVVKHVEPEVLEAAAHALYLLCKPEFTFFSRVDFARSQLVDFLTDRFQQELDDLMQSSFLDEDEVYSLTATLKRLSAFYNAHDLTRWEISEPCSRLLRKAVDTGEVPHQVILPALTLVYFSILWTVTHISESTSHKQLMSLKKRMVAFCELCQSCLSDVDPEIQEQAFVLLSDLLLIFSPQMIVGGRDFLRPLVFFPEATLQSELASFLMDHVFLQPGELGNGQSQEDHVQIELLHQRRRLLAGFCKLLLYGVLELDAASDVFKHYNKFYEDYGDIIKETLTRARQIDRCQCSRILLLSLKQLYTELIQEQGPQGLTELPAFIEMRDLARRFALSFGPQQLHNRDLVVMLHKEGIKFSLSELPPAGSSHEPPNLAFLELLSEFSPRLFHQDKRLLLSYLEKCLQRVSKAPNHPWGPVTTYCHSLHPLEITAEASPRGPPHSKKRCVEGPCRPQEEESSSQEESLQLNSGPTTPTLTSTAVKRKQSLRTVGKKQKGRPGPGPGPGPELICSQQLLGTQRLKMSSAPCFQIRCDPSGSGLGKQLTRLSLMEEDEEEELRLLDEEWQRGDKMLHSPSSPSEHGLDLLDTTELNMEDF
Protein: Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC 3.1.3.27) (PTEN-like phosphatase) (PTEN-like protein) (Protein-tyrosine phosphatase mitochondrial 1-like protein) (EC 3.1.3.16, EC 3.1.3.48) (Q86BN8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Lipid phosphatase that may mediate dephosphorylation of mitochondrial proteins (By similarity). Protein phosphatase that may mediate dephosphorylation of mitochondrial proteins (By similarity). Does not dephosphorylate Akt.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P0C089}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C089}; Matrix side {ECO:0000250|UniProtKB:P0C089}.
Interaction partners:
- Phosphatidate cytidylyltransferase, mitochondrial
- Probable cardiolipin synthase
- Tafazzin
Sequence:
MEMSAAMFARVSFYPTLLYNVLMEKASARNWYDRIDEHVILGALPFRSQANDLIEKENMKAVVSMNEDYELTAFSNNTEKWRKLGIEFLQLATTDIFESPNQEKLFRGVEFINKFLPLKQRIGGLSSSYQPENVGSVYVHCKAGRTRSATLVGCYLMMKNGWTPDQAVDHMRKCRPHILLHTKQWDALRLFYTNNVETKS
Protein: tRNA modification GTPase MnmE (EC 3.6.-.-) (P25522)
Organism: Escherichia coli (strain K12)
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00379, ECO:0000269|PubMed:10601028}. Note=Partially associated with the inner membrane.
Interaction partners:
- tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG
- tRNA-specific 2-thiouridylase MnmA
- Ribosomal RNA small subunit methyltransferase G
- Probable GTP-binding protein EngB
- tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC
- Membrane protein insertase YidC
- Ribonuclease P protein component
- Ribosomal large subunit pseudouridine synthase D synthase)
- Large ribosomal subunit protein bL34
- GTPase ObgE/CgtA
Sequence:
MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK
Protein: Superoxide dismutase [Mn] 3.3, mitochondrial (EC 1.15.1.1) (P41979)
Organism: Zea mays (Maize)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Superoxide dismutase 4A
- Large ribosomal subunit protein uL23m
- Ribosomal protein S5 family protein
- Ribosomal protein S24/S35 mitochondrial
- Large ribosomal subunit protein mL46
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Large ribosomal subunit protein bL27c
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS14c
- Large ribosomal subunit protein uL5c
Sequence:
MALRTLASKNALSFALGGAARPSAESARGVTTVALPDLSYDFGALEPVISGEIMRLHHQKNHATYVVNYNKALEQIDDVVVKGDDSAVVQLQGAIKFNGGGHVNHSIFWKNLKPISEGGGEPPHGKLGWAIDEDFGSFEALVKRMNAEGAALQGSGWVWLALDKEAKKVSVETTANQDPLVTKGASLVPLLGIDVWEHAYYLQYKNVRPDYLNNIWKVMNWKYAGEVYENVLA
Protein: Cilia- and flagella-associated protein 251 (WD repeat-containing protein 66) (Q8TBY9)
Organism: Homo sapiens (Human)
Function: Involved in spermatozoa motility. May also regulate cilium motility through its role in the assembly of the axonemal radial spokes (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8IRK7}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:30122540, ECO:0000269|PubMed:30122541}.
Interaction partners:
- Cilia- and flagella-associated protein 91
- Cilia- and flagella-associated protein 43
- Cilia- and flagella-associated protein 61
- Cilia- and flagella-associated protein 69
Sequence:
MSDAAEAPREATGENGETEMKEEEEPNPNYKEVEDPQQESKDDTIAWRESQEEERKTGEEEGEEEGKEDKKIVMEETEEKAGEVQEKEASGIQEETTVEPQEVTASMIRLETQITDSQSITSGIFPKTQRGSKSKLSLQLEDAETDELLRDLSTQIEFLDLDQISPEEQQISSPERQPSGELEEKTDRMPQDELGQERRDLEPENREEGQERRVSDIQSKAGISRESLVSSTTEDILFQKDKSTPVYPLTMTWSFGWNSSLPVYYIREERQRVLLYVCAHTAIIYNVFRNNQYHLQGHANIISCLCVSEDRRWIATADKGPDCLVIIWDSFTGIPVHTIFDSCPEGNGIMAMAMTHDAKYLATISDAEVQKVCIWKWTLAVETPACTLELPTEYGVQNYVTFNPTNNKELVSNSKTRAIYYAWYEERDTLAHSAPLLTEKTFNKLVGKFSQSIFHLNLTQILSATMEGKLVVWDIHRPPSSASTFLGFPYIKPCKLVHLQKEGITVLTTIDSYIVTGDIKGNIKFYDHTLSIVNWYSHLKLGAIRTLSFSKTPATPPTEKSNYPPDCTLKGDLFVLRNFIIGTSDAAVYHLTTDGTKLEKLFVEPKDAICAISCHPYQPLIAIGSICGMIKVWNYENKQYLFSRVFEKGLGVQSLTYNPEGALLGAGFTEGTVYILDAMSLENESPEPFKYSRTSVTHISFSHDSQYMATADRSFTVAVYMLVVRNGQRVWEYLARLRSHRKSIRSLLFGVYLDSNEPRLLSLGTDRLLIEYDLLRSYKDHLEVLDIHHTDQGCYPTCMVWYPPLTRELFLLICNSGYKVKLFNATTKMCRKTLLGPAYGSPIEQTQVLPVRSMAELQKRYLVFINRDKVGLQILPVDGNPHKTSAIVCHPNGVAGMAVSYDGCYAFTAGGHDRSVVQWKITLSVLEAAVSLGGEDLTPFYGLLSGGREGKFYRELEDYFYYSQLRSQGIDTMETRKVSEHICLSELPFVMRAIGFYPSEEKIDDIFNEIKFGEYVDTGKLIDKINLPDFLKVYLNHKPPFGNTMSGIHKSFEVLGYTNSKGKKAIRREDFLRLLVTKGEHMTEEEMLDCFASLFGLNPEGWKSEPATCSVKGSEICLEEELPDEITAEIFATEILGLTISEDSGQDGQ
Protein: Soluble guanylate cyclase gcy-35 (EC 4.6.1.2) (O02298)
Organism: Caenorhabditis elegans
Function: Plays a central role in social feeding behavior and oxygen sensation by synthesizing 3',5'-cyclic guanosine monophosphate (cGMP) from GTP. Oxygen, which binds to its heme-binding sites, probably regulates social behavior by modulating its activity. cGMP is a common second messenger in sensory transduction and is implicated in oxygen sensation. Indeed, C.elegans exhibits a strong behavioral preference for 5-12% oxygen, avoiding higher and lower oxygen levels; a higher level of oxygen inducing a naturally polymorphic social feeding behavior. Involved in avoidance of hyperoxia and for oxygen-induced aggregation and bordering, probably by mediating oxygen-sensing in URX, AQR and PQR sensory neurons.
Subcellular location: Cytoplasm {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:29879119}. Note=Enriched localization at the URX dendrite ending. {ECO:0000269|PubMed:29879119}.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Bis
- Neuropeptide receptor npr-1
- Cyclic nucleotide-gated channel
- Globin domain-containing protein
- Cyclic nucleotide-binding domain-containing protein
- Phosphodiesterase delta-like protein
- GTP cyclohydrolase 1
- Probable 3',5'-cyclic phosphodiesterase pde-2
- Probable 3',5'-cyclic phosphodiesterase pde-5
Sequence:
MFGWIHESFRQLVTRKYGKDIWEKIVHMSKFELGTESEIAHYYNDDETLRLVNSMANVIGIPIEEIWEAYGGFLIQFTMETGWDELLRAMAPDLEGFLDSLDSLHYFIDHVVYKTKLRGPSFRCDVQADGTLLLHYYSKRSGLYPIVKGVVREVARRIYDTEVVMKVQERKQEHLDAFVTEHVVFVITQIENANSTQPKSISSKADSQIDLSTGIYEISSSDFSLAFPYHICFDPDLFVEHFGNFIKKTFPNAMRQETRVTDLLELVHPEVPFSYESIKYYKNSLFVFRLKGLGDIVHNANDEAKTVLLKGSMVFIDEGKYILYMCSVNVTTVRELIERNLHLSDMQRHDGTRDVIMLNQSRMSQVELNRTLEETTKKLKKMAQELEIEKQKTDELLCELMPASVADSLRSGKAMDAKEFADCTLLFTDIVTFTNICAMCTPYDVVTLLNDLYLRFDRLVGLHDAYKVETIGDAYMIVGGVPERCENHAERVLNISIGMLMESKLVLSPITHKPIKIRLGVHCGPVVAGVVGIKMPRYCLFGDTVNVANKMESNGIQCKIHVSETGKLNGLKANPSYVFIDRGNTEIRGKGMMYTYFLERNDRKSVWELCSRPRSGEQTIDGYMELHDQSIYQEEGGQQENLTVENGNSAQNNHNNNNNTHHSGRKLMNGSSVDPGSHHIRSPTCTIS
Protein: MAM domain-containing glycosylphosphatidylinositol anchor protein 2 (MAM domain-containing protein 1) (Q7Z553)
Organism: Homo sapiens (Human)
Function: May be involved in cell-cell interactions.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Neuroligin-2
- Neuroligin-1
Sequence:
MDLLYGLVWLLTVLLEGISGQGVYAPPTVRIVHSGLACNIEEERYSERVYTIREGETLELTCLVTGHPRPQIRWTKTAGSASDRFQDSSVFNETLRITNIQRHQGGRYYCKAENGLGSPAIKSIRVDVYYLDDPVVTVHQSIGEAKEQFYYERTVFLRCVANSNPPVRYSWRRGQEVLLQGSDKGVEIYEPFFTQGETKILKLKNLRPQDYANYSCIASVRNVCNIPDKMVSFRLSNKTASPSIKLLVDDPIVVNPGEAITLVCVTTGGEPAPSLTWVRSFGTLPEKTVLNGGTLTIPAITSDDAGTYSCIANNNVGNPAKKSTNIIVRALKKGRFWITPDPYHKDDNIQIGREVKISCQVEAVPSEELTFSWFKNGRPLRSSERMVITQTDPDVSPGTTNLDIIDLKFTDFGTYTCVASLKGGGISDISIDVNISSSTVPPNLTVPQEKSPLVTREGDTIELQCQVTGKPKPIILWSRADKEVAMPDGSMQMESYDGTLRIVNVSREMSGMYRCQTSQYNGFNVKPREALVQLIVQYPPAVEPAFLEIRQGQDRSVTMSCRVLRAYPIRVLTYEWRLGNKLLRTGQFDSQEYTEYAVKSLSNENYGVYNCSIINEAGAGRCSFLVTGKAYAPEFYYDTYNPVWQNRHRVYSYSLQWTQMNPDAVDRIVAYRLGIRQAGQQRWWEQEIKINGNIQKGELITYNLTELIKPEAYEVRLTPLTKFGEGDSTIRVIKYSAPVNPHLREFHCGFEDGNICLFTQDDTDNFDWTKQSTATRNTKYTPNTGPNADRSGSKEGFYMYIETSRPRLEGEKARLLSPVFSIAPKNPYGPTNTAYCFSFFYHMYGQHIGVLNVYLRLKGQTTIENPLWSSSGNKGQRWNEAHVNIYPITSFQLIFEGIRGPGIEGDIAIDDVSIAEGECAKQDLATKNSVDGAVGILVHIWLFPIIVLISILSPRR
Protein: Transcription termination factor 2, mitochondrial (Mitochondrial transcription termination factor 2) (mTERF2) (mTERF domain-containing protein 3, mitochondrial) (Q8BKY8)
Organism: Mus musculus (Mouse)
Function: Binds mitochondrial DNA and plays a role in the regulation of transcription of mitochondrial mRNA and rRNA species.
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:19366608}.
Interaction partners:
Sequence:
MPWRLPTGHQLCRLCLLRKPRPALKIKPSSACVTYGTDSQSDKENKRTVEKLSACSVDIRKIRRLKGWVLLEEETYVEEIANILKELGANKTVIASILERCPEAIICSPAAVNTKRKLWQMVCKNEAELVQLIEQFPESFFTVKNQENQKLNVQFFQELGLRNVVISRFLTTASSIFHNPVENNKQMIGVLQESYLNLGGSEANAKVWLLKLLSQNPFIVLHSPRAVGETLKCLQGQGFTDSEVLQLLSKLKGFLFQLQPGSIQNSISFTKTTFECTDYDLRQLVVKCPALLCYPASVLEERIQALLKEGISIAQIRESPMVLELTPQIIQYRIRKLNSLGYGIKDGHLASLNGTKKEFEANFSKMQAKQGRPLFNPVASLKVEE
Protein: Signal transducing adaptor molecule (A0A0G2JTT5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Early endosome membrane {ECO:0000256|ARBA:ARBA00004469}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004469}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004469}.
Interaction partners:
Sequence:
MFILPFELNTAEDWGLILDICDKVGQSRTGPKDCLRSIMRRVNHKDPHVAMQALTLLGACVSNCGKIFHLEVCSRDFASEVSNVLNKGHPKVCEKLKALMVEWTDEFKNDPQLSLISAMIKNLKEQGVTFPAIGSQAAEQAKASPALVAKDPGTVATKKEEEDLAKAIELSLKEQRQQAAPLSTLYPSTSSLLTNHQHEGRKVRAVYDFEAAEDNELTFKAGEVITVLDDSDPNWWKGETHQGMGLFPSNFVTADLTAEPEMIKTEKKTVQFSDDVQIETIEPEPEPEPAFIDEDKMDQLLQMLQSTDPSDNQPDLPELLHLEAMCHQMGPLIDEKLEDIDRKHSELSELNVKVMEALSLYTKLMNEDPVYSVYAKSQSQQYYVQASGVSAPQVYPGPAQSGAYLVAGNAQMTHLQSYSLPPEQLASISQGAVPPSATPALPNQQAQASYPNAMVSSVQGNSYPSQASIYSPAAAAAAVAVTAVPVPADVTIYQNPGPNMSQVPNYTLTSSTLPHTGGSQQPPQPQQAYSQKALL
Protein: 5-hydroxytryptamine receptor 3A (5-HT3-A) (5-HT3A) (5-hydroxytryptamine receptor 3) (5-HT-3) (5-HT3R) (Serotonin receptor 3A) (Serotonin-gated ion channel receptor) (P35563)
Organism: Rattus norvegicus (Rat)
Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses in neurons. It is a cation-specific, but otherwise relatively nonselective, ion channel.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P46098}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23979}. Cell membrane {ECO:0000250|UniProtKB:P46098}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23979}.
Interaction partners:
- 5-hydroxytryptamine receptor 3B
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor 1
- 5-hydroxytryptamine receptor 2A
- Glutamate receptor ionotropic, NMDA 1
- 5-hydroxytryptamine receptor 2C
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor ionotropic, NMDA 3A
- Glutamate receptor ionotropic, kainate 4
Sequence:
MPLCIPQVLLALFLSVLIAQGEGSRRRATQAHSTTQPALLRLSDHLLANYKKGVRPVRDWRKPTLVSIDVIMYAILNVDEKNQVLTTYIWYRQFWTDEFLQWTPEDFDNVTKLSIPTDSIWVPDILINEFVDVGKSPSIPYVYVHHQGEVQNYKPLQLVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRTPEEVRSDKSIFINQGEWELLGVFTKFQEFSIETSNSYAEMKFYVVIRRRPLFYAVSLLLPSIFLMVVDIVGFCLPPDSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVQLVHKQDLQRPVPDWLRHLVLDRIAWLLCLGEQPMAHRPPATFQANKTDDCSAMGNHCSHVGSPQDLEKTSRSRDSPLPPPREASLAVRGLLQELSSIRHSLEKRDEMREVARDWLRVGYVLDRLLFRIYLLAVLAYSITLVTLWSIWHYS
Protein: C2H2-type zinc finger family protein (F18K10.4 protein) (Q7G8T1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- HAT family dimerization domain-containing protein
- Ac-like transposase
Sequence:
MEAAAEAVSAAREQSLILKGKRTKRQRPQSPIPFSIIPPMSSHEPDAEEESTSLVSKEKSLNDEINNNNIKNNNNTLINGVTSSSSASSSSNNNATLKATADEEDQDMANCLILLAQGHSLPHLQPQPHPQQQTRQLMMSYQDSGNNNNNAYRSSSRRFLETSSSNGTTTNGGGGRAGYYVYQCKTCDRTFPSFQALGGHRASHKKPKAAMGLHSNHDHKKSNYDDAVSLHLNNVLTTTPNNNSNHRSLVVYGKGSNNKVHECGICGAEFTSGQALGGHMRRHRGAVVAAAAASTATVSVAAIPATANTALSLSPMSFDQMSEGPIQAPVKRARSAVVSLDLDLNLPAPEDENRVNGLSFASKQEHEQEHEQTQQKKQREEQKSLVLSSAPTLVDCHY
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (Q9U010)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
Sequence:
MGGGSGACPPAHMYGAVAPQDIIVRDMVQMPPPPSNAPTSADACLSIVHSLMCHRQGGESEGFAKRAIESLVKKLKEKRDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARIWRWPDLHKNELKHVKYCAFAFDLKCDSVCVNPYHYERVVSPGIDLSGLSLQSGPSRLVKDEYSAGPLVGSMDIDGNDIGTIQHHPTQMVGPGGYGYPQGPSEYVGDANPMSAMFPTGRTIPKIEPQDGVAGSRGSWMVPPPPRLGQPPQQQQQQPQQQTPQPTQQQQAQSQASAHSLPVPHGMPGMPGPMNPGPVMAPPPPPQQAQNPQGNGVHHTQANSPTDPASALAMQQQQQQQQQQQQQQQQQQQQSGGVPNGSVNAGGGAAAGGQYYGQPPPVSQMQGAGGGGTSVAPSVHAQQNGYVSQPGSAGSAPVGGGGVFGTAQPTPQQPQQPPTGVQANTGSAGAQAGAGGGAAGTWTGPNTLTYTQSMQPPDPRSLPGGFWNSSLSGDLGSPQQTPPQQQQQQQQPRLLSRQPPPEYWCSIAYFELDTQVGETFKVPSAKPNVIIDGYVDPSGGNRFCLGALSNVHRTEQSERARLHIGKGVQLDLRGEGDVWLRCLSDNSVFVQSYYLDREAGRTPGDAVHKIYPAACIKVFDLRQCHQQMHSLATNAQAAAA
Protein: Solute carrier family 22 member 17 (24p3 receptor) (24p3R) (Brain-type organic cation transporter) (Lipocalin-2 receptor) (Neutrophil gelatinase-associated lipocalin receptor) (NgalR) (Q8WUG5)
Organism: Homo sapiens (Human)
Function: Cell surface receptor for LCN2 (24p3) that plays a key role in iron homeostasis and transport. Able to bind iron-bound LCN2 (holo-24p3), followed by internalization of holo-24p3 and release of iron, thereby increasing intracellular iron concentration and leading to inhibition of apoptosis. Also binds iron-free LCN2 (apo-24p3), followed by internalization of apo-24p3 and its association with an intracellular siderophore, leading to iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration and resulting in apoptosis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17253959}; Multi-pass membrane protein {ECO:0000269|PubMed:17253959}. Vacuole membrane {ECO:0000269|PubMed:17253959}; Multi-pass membrane protein {ECO:0000269|PubMed:17253959}. Note=Upon LCN2-binding, it is internalized.
Interaction partners:
- Neutrophil gelatinase-associated lipocalin
- Syntaxin-binding protein 6
- Cochlin
- Low-density lipoprotein receptor-related protein 2
Sequence:
MAPRVATGTPEPNGGGGGKIDNTVEITPTSNGQVGTLGDAVPTEQLQGEREREREGEGDAGGDGLGSSLSLAVPPGPLSFEALLAQVGALGGGQQLQLGLCCLPVLFVALGMASDPIFTLAPPLHCHYGAFPPNASGWEQPPNASGVSVASAALAASAASRVATSTDPSCSGFAPPDFNHCLKDWDYNGLPVLTTNAIGQWDLVCDLGWQVILEQILFILGFASGYLFLGYPADRFGRRGIVLLTLGLVGPCGVGGAAAGSSTGVMALRFLLGFLLAGVDLGVYLMRLELCDPTQRLRVALAGELVGVGGHFLFLGLALVSKDWRFLQRMITAPCILFLFYGWPGLFLESARWLIVKRQIEEAQSVLRILAERNRPHGQMLGEEAQEALQDLENTCPLPATSSFSFASLLNYRNIWKNLLILGFTNFIAHAIRHCYQPVGGGGSPSDFYLCSLLASGTAALACVFLGVTVDRFGRRGILLLSMTLTGIASLVLLGLWDCEHPIFPTVWAQQGNPNRDLNEAAITTFSVLGLFSSQAAAILSTLLAAEVIPTTVRGRGLGLIMALGALGGLSGPAQRLHMGHGAFLQHVVLAACALLCILSIMLLPETKRKLLPEVLRDGELCRRPSLLRQPPPTRCDHVPLLATPNPAL
Protein: BTB/POZ domain and ankyrin repeat-containing protein NH5.1 (Q2RAQ5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in defense response against pathogens.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:S4VGD0}. Cytoplasm {ECO:0000250|UniProtKB:S4VGD0}.
Interaction partners:
- Os01g0314700 protein
- Transcription factor TGAL10
- Kinesin-like protein KIN-14I
- Transcription factor TGA2.3
- Transcription factor TGA2.1
- Transcription factor TGAL1
- BTB/POZ domain and ankyrin repeat-containing protein NPR1
- Transcription factor TGA2.2
- Transcription factor TGAL6
Sequence:
MSSEDSLKSLSLDYLSLLINGQAFSDVAFSVEGRLVHAHRCVLAARSLFFRKLFCGLDPNHQPPPPPPPLNWPMAGGGGGGSGGGGRGGAGGGGGAPATPELVIPVSSIRYEVLVLVLQFLYSGQASVAAPKSGPLPGCGARGCWHTRCGAAVDLALDTLAAARSFGVEQLALLVQKQLESMVKEASVDDVMKVLMASRKFEMQELWATCSHLVARSGLSADLLAKHLPIDVVAKIEEIRAKSPLAAVAAPRSPFLTHHYLPMNPASSAADRDNKIRRMRRALDAADIELVKLMVMGEGLDLDDALAVHYAVQHCNRDVVKALLELGAADVNSRAGPTGKTALHLAAEMVSPDMVSVLLDHHADPNSRTLDGVTPLDVLRSLTSEFLFKGAVPGLTHIEPNKLRLCLELVQSAVMVTTRDDGAPVTGGAEAGGSDGGNFPRSDADDSLVSLTMNSTLMYQGQEMAAAVAAGEGRKSNNGRGSPPPAMYFPNGFA
Protein: Vacuolar-processing enzyme beta-isozyme 1 (Beta-VPE 1) (OsVPE1) (EC 3.4.22.34) (Asparaginyl endopeptidase VPE1) (Q84LM2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Asparagine-specific endopeptidase that may be involved in processing of proteins targeted to vacuoles. Cysteine protease required for post-translational proteolysis of seed storage proteins in the protein storage vacuole (PSV) of developing seeds, by processing of proglutelin precursor to mature glutelin subunits, thus contributing to the formation of protein crystalline structures in PSV.
Subcellular location: Protein storage vacuole {ECO:0000269|PubMed:19154227}.
Interaction partners:
- Os02g0219400 protein
Sequence:
MAARCWVWGFVVALLAVAAAADGEEEEGKWEPLIRMPTEEGDDAEAAAPAPAPAAADYGGTRWAVLVAGSSGYGNYRHQADVCHAYQILQKGGVKEENIVVFMYDDIAHNILNPRPGTIINHPKGGDVYAGVPKDYTGHQVTTENFFAVLLGNKTAVTGGSGKVIDSKPEDHIFIYYSDHGGPGVLGMPNLPYLYAGDFIKVLQKKHASNSYSKMVIYVEACESGSIFEGLMPENLNIYVTTASNAVENSWGTYCPGEEPSPPPEYITCLGDMYSVAWMEDSETHNLKKETIEDQYELVKKRTSNANKLNEGSHVMEYGDKTFKDEKLFLYQGFNPANGNITNELIWPVPKATVNQRDADLLFMWKRYEQLNGVSEDKLRALREIEDTIAHRKHLDSSIDFIGKLVFGFENGPLALEAARSSGQPLVDNWDCLKKMVRIFESQCGSLTQYGMKYMRAFANICNNGVSEAKMMEASINACGRYNSARWSPMTEGGHSA
Protein: Pancreatic lipase-related protein 2 (PL-RP2) (Cytotoxic T lymphocyte lipase) (Galactolipase) (EC 3.1.1.26) (Triacylglycerol lipase) (EC 3.1.1.3) (P17892)
Organism: Mus musculus (Mouse)
Function: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides. In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides. Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity. Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (By similarity). Hydrolyzes medium- and long-chain fatty acyls in galactolipids (By similarity). May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency (By similarity). In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity. Also has low phospholipase activity (By similarity). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P54317}. Zymogen granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000250|UniProtKB:P54318}.
Interaction partners:
- Bile salt-activated lipase
- Inactive pancreatic lipase-related protein 1
- Colipase
- Gastric triacylglycerol lipase
- Pancreatic triacylglycerol lipase
- Diacylglycerol O-acyltransferase 1
- 1-acylglycerol-3-phosphate O-acyltransferase Pnpla3
- Patatin-like phospholipase domain-containing protein 2
- Monoglyceride lipase
- Hepatic triacylglycerol lipase
Sequence:
MPMDVRGCLFPSVQMLLCWLVSLLLATVGGKEVCYGHLGCFSNDKPWAGMIQRPSKIFPWSPEDIDTRFLLYTNENPNNYQIISATDPATINASNFQLDRKTRFIIHGFIDKGEEGWLLDMCKKMFQVEKVNCICVDWKRGSRTEYTQASYNTRVVGAEIAFLVQVLSTEMGYSPENVHLIGHSLGSHVAGEAGRRLEGHVGRITGLDPAEPCFQGLPEEVRLDPSDAMFVDVIHTDSAPIIPYLGFGMSQKVGHLDFFPNGGKEMPGCQKNILSTIVDINGIWEGTRNFAACNHLRSYKYYASSILNPDGFLGYPCSSYEKFQHNDCFPCPEQGCPKMGHYADQFEGKTATVEQTFFLNTGDSGNFTRWRYKVSVTLSGAKKLSGYILVALYGCNGNSKQYEVFKGSLQPEARYIRDIDVDVNVGEIQKVKFLWNNKVINLFRPTMGASQITVQRGKDGKEFNFCSSNTVHEDVLQSLYPC