wanglab/gogpt-training-data huggingface dataset:
Protein: Fructose-bisphosphate aldolase A (EC 4.1.2.13) (Muscle-type aldolase) (P05065)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (By similarity). In addition, may also function as scaffolding protein (By similarity).
Subcellular location: Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+). {ECO:0000250|UniProtKB:P00883}.
Interaction partners:
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase, liver type
- Pyruvate kinase PKM
- ATP-dependent 6-phosphofructokinase, muscle type
- ATP-dependent 6-phosphofructokinase, platelet type
- Triosephosphate isomerase.
- Glyceraldehyde-3-phosphate dehydrogenase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
- Triosephosphate isomerase
Sequence:
MPHPYPALTPEQKKELADIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSSLAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYIKRALANSLACQGKYTPSGQSGAAASESLFISNHAY
Protein: Ion_trans_2 domain-containing protein (H9G2R3)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPYVPFLYIARTDSEAEGTVYKNSYASLMNELQPTTSFDDFKQSITQLTDIFRADPARMQYGEKKNIKHKLQQWFIENPSISARIRSCNVLIKLLTCILYCIRVVNDERSYPDDFPFSEEEAGKQDVTLYKYLLWVDFDFKIWFLQTMFACISMVYTILVFYLSYSGSVVRLLINIHFLLELITSFPFIISIFIPSLTYLYVPVFLNCWLAKGALQAMMNDLNRKSFISSSALFRQLLLLFSVLACLIFTGMCSIEHLQRARGKRIDLFTSFYFVMVTFSTVGYGDWYPDYWASQLCVVILICVALGLIPKQLDELGQTWSERQKSGTDFSSWNGVESHVVVTITTLEVEFIRDFLEEFYAHPENQRIQIVLLSPAELDNQTRMLLKIPLWNNRVHYVRGSSLRDEDLERANVATSKACFILSARHVNRKVATDEHTILRSWAIKDFAPNVKQYVQIFRAETKMHIEHAEVLICEDEFKYALLANNCICPGISTFITLLMHTSRGEEGQKSTEPWHKVYGFHSGNEMYQIKVQDSKFFCEYVGKSFSSTSFHAHKEYGIGLIAVSPDGDTSRMKLNPGSSHIIQPTDTVYYMGLTNEESLTDFRKGIRSQQKRANVASTIANIGTVAVDVPRSDKTELVGRKKKKRKEKAADEIHLIEVGEHVQSSRRPSIAMVTEGKIDSSSDSDQEEICDKCRGPCIQHKLQRTYPQVRTYIGTSNTVCHMMKERRSLCCLKLDEKCAHKSATSAHEYQWRNRPIILAADRTSSGMYNLVIPLRAYYRPVHDLHPIIILLELEEQDSLNDAFLDAISYFPDVYWMKGKVGNLDCLLRAGVSSAEHVVVVKETAVMAEEHTADCNTIITVQKIHRMFPRLRMITELTHATNMRFVQFNPHNAYSLAQSRFEKKERKRGSHMPFMFRLPFAQGGVFSANMLDRLLYQAIIKPFVVDLVRLLLGIDQHSDGGYLTSFVITSDDLWIRNYGRLYQKLCSSVADIPIGIFRTKKMDTKTVSLDLQEQCKDFENTEMGRNKDMYDHVKNRMRLLNIKDTHTLLEGSDEKSQISYVIINPAQDLELESGDIVYVIRSPIRKDATNARINPRRGLRRSKNVSETIDSTNQVPTIVIDENNL
Protein: Staphylococcal nuclease domain-containing protein 1 (100 kDa coactivator) (4SNc-Tudor domain protein) (p100 co-activator) (Q7ZT42)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12753931}.
Interaction partners:
- Metadherin a
- Metadherin b
- Tudor and KH domain-containing
- Protein argonaute-2
- Endoribonuclease Dicer
- Drosha ribonuclease III.
- Piwi-like protein 1
- Transmembrane protein 208
Sequence:
MASAVPAQVQSSQASAPQLQRGIVKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGALARRAIQGQPDTKDTPDEPWAFQAREFMRKKVIGKEVCFTVENKTPQGREYGMVYLGKDTSGENIAESLVAEGLAMVRREGIRGNNPEQVRLCDLEDQAKSSKKGLWSEGGGSHTIRDLKYTIENPRNFVDSLHQKPVNAIIEHVRDGCMVRALLLPDYYLVTVMLSGIKSPTFKREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCPNQVILGTILHPNGNITELLLKEGFARCVDWSMAVYTQGAEKLRAAERSAKERKVRIWKDYVAPTANLDQKDRQFVAKVMQVVNADAIVVKLNSGEYKTIHLSSIRPPRLEGEEKNKDKDKRFRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRAATNAMEMGVPAFPERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGETQKAKQFFPFLQRAGRSEAVVEYVFSGSRLKLYMPKETCLITFLLAGIECPRGSRNMPGGMQVAEPYSEEAMLFTKELVLQREVEVEVESMDIAGNFIDWLHIDGVNLSVALVENALSKVHFTAERSSYYKTLVSAEESARQRKEKLWANYEEKPNEEVAQVTEAKERGRNTDPSTSLEITDGLHFYAQDVETGTKLENLMESMRGEIAAQPPVEGSFAPRRGEFCIAKFADGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPPAFSTRTLPPQATEYAFAYIQVPQDEDARADAVDSVVRDIHNTQCLLNVEYSGMVCPQVTLQFADTKEDVGLGLVKEGMVMVDIRKEKYLQKMVTEYLNAQESAKSARLNIWR
Protein: Interleukin-5 (IL-5) (B-cell growth factor II) (BCGF-II) (Cytotoxic T-lymphocyte inducer) (Eosinophil differentiation factor) (T-cell replacing factor) (TRF) (Q08125)
Organism: Rattus norvegicus (Rat)
Function: Homodimeric cytokine expressed predominantly by T-lymphocytes and NK cells that plays an important role in the survival, differentiation, and chemotaxis of eosinophils. Acts also on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation (By similarity). Mechanistically, exerts its biological effects through a receptor composed of IL5RA subunit and the cytokine receptor common subunit beta/CSF2RB. Binding to the receptor leads to activation of various kinases including LYN, SYK and JAK2 and thereby propagates signals through the RAS-MAPK and JAK-STAT5 pathways respectively (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Interleukin-5 receptor subunit alpha
- Interleukin-2
- Interleukin-3
- Interleukin-1 beta
- Interleukin-7
- Colony stimulating factor 2 receptor subunit beta
- Interleukin 9
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-10
- Interleukin-13
Sequence:
MRMLLCLNVLTLSCVWAIAMEIPMSTVVKETLIQLSTHRALLTSNETMRLPVPTHKNHQLCIGEIFQGLDILKNQTVRGGTVEILFQNLSLIKKYIDGQKEKCGEERRKTRHFLDYLQEFLGVMSTEWAMEV
Protein: Uncharacterized protein (Q389U4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cell division cycle protein 16, putative
- Cdc23 domain-containing protein
- Cyclosome subunit 1, putative
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 2
- Dynein heavy chain region D6 P-loop domain-containing protein
- Rev7, putative
- Anaphase-promoting complex subunit 10
- E2 ubiquitin-conjugating enzyme
- Uncharacterized protein
Sequence:
MTAQRDHRKSLVVQGLKEAIQESLASYIYPNAIFCAERLYSLEPTYESLHTLAHCYVTSGDAGTAYRLLQTHCPSLSPSNSVSSSNVSISGGPDATAKWNCQYLFGVTCAMSQRYAEGERVLDELDRHRTCSDVQYWLGVCRQRGRHGNGDDAFARSAILDPLNFVAYEEYLKITGTPKEEMCHMYSSAKAPTGAEETPRRPAPVGVTCSRSKTPSTSSKQSRRDFVRQYLSPFAAIAFMQRMYMCKDVQAALQQEGFPEQSTSWAVGALAMAYFHDGDVENAVKEFARLRQIAPWRLADPLLVHYSTALWQRKDTGALGSLSQTLINEMPVSPVTLCVAANAYSLLKESKEALCMLDRAVQLDSEFAYAHTLRGYELLHLDRKHDAYESFQNAVLIDSNHYNAYAGLGELYFRSENIPQAQYYFKQAIQINPLPSIMNRYAATYHRRDTSKENLSEALRIYDSAIKRHPTNLGARHQRAEVLIRLRRYPEAREALLEMTKACPDEAMLYVTLAKCVHFMGMPGKAVQYYHTAMDLDPRRAGFIKSCLQRISMEEPE
Protein: RE43665p (Q9W2P5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR006609}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm3
- U6 snRNA-associated Sm-like protein LSm1
- Probable small nuclear ribonucleoprotein Sm D2
- Protein associated with topo II related - 1, isoform A
- Probable small nuclear ribonucleoprotein G
Sequence:
MSRKEALSQFINQIHGRPVAVKLNNGVDYRGVLACLDGYMNICLEQTEEYVNGQLKNKYGDAFIRGNNVLYISTQKRRV
Protein: Scarecrow-like protein 6 (AtSCL6) (GRAS family protein 22) (AtGRAS-22) (SCL6-IV) (O81316)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in plant development.
Subcellular location: Nucleus {ECO:0000269|PubMed:18500650}.
Interaction partners:
- Protein PAT1 homolog
- Scarecrow-like protein 9
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Holliday junction resolvase MOC1, chloroplastic
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
Sequence:
MPLPFEEFQGKGISCFSSFSSSFPQPPSSPLLSHRKARGGEEEEEEVPAAEPTSVLDSLISPTSSSTVSSSHGGNSAVGGGGDATTDEQCGAIGLGDWEEQVPHDHEQSILGLIMGDSTDPSLELNSILQTSPTFHDSDYSSPGFGVVDTGFGLDHHSVPPSHVSGLLINQSQTHYTQNPAAIFYGHHHHTPPPAKRLNPGPVGITEQLVKAAEVIESDTCLAQGILARLNQQLSSPVGKPLERAAFYFKEALNNLLHNVSQTLNPYSLIFKIAAYKSFSEISPVLQFANFTSNQALLESFHGFHRLHIIDFDIGYGGQWASLMQELVLRDNAAPLSLKITVFASPANHDQLELGFTQDNLKHFASEINISLDIQVLSLDLLGSISWPNSSEKEAVAVNISAASFSHLPLVLRFVKHLSPTIIVCSDRGCERTDLPFSQQLAHSLHSHTALFESLDAVNANLDAMQKIERFLIQPEIEKLVLDRSRPIERPMMTWQAMFLQMGFSPVTHSNFTESQAECLVQRTPVRGFHVEKKHNSLLLCWQRTELVGVSAWRCRSS
Protein: Sialidase-2 (EC 3.2.1.18) (Cytosolic sialidase) (Mouse skeletal muscle sialidase) (MSS) (Murine thymic sialidase) (MTS) (N-acetyl-alpha-neuraminidase 2) (Q9JMH3)
Organism: Mus musculus (Mouse)
Function: Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Recognizes sialyl linkage positions of the glycan moiety as well as the supramolecular organization of the sialoglycoconjugate (By similarity). Displays preference for alpha-(2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in both monomeric forms and micelles. Hydrolyzes exclusively monomeric GM1 ganglioside, but has no activity toward the miscellar form (By similarity). Has lower sialidase activity for glycoproteins such as fetuin and TF/transferrin that carry a mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages (By similarity). Cleaves milk oligosaccharide alpha-(2->3)-sialyllactose, but is inactive toward isomer alpha-(2->6)-sialyllactose isomer. Has no activity toward colominic acid, a homomer of alpha-(2->8)-linked Neu5Ac residues (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3R4}.
Interaction partners:
- Arylsulfatase A
- Galactocerebrosidase
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Galactosylceramide sulfotransferase
- Alpha-galactosidase A
Sequence:
MATCPVLQKETLFRTGVHAYRIPALLYLKKQKTLLAFAEKRASKTDEHAELIVLRRGSYNEATNRVKWQPEEVVTQAQLEGHRSMNPCPLYDKQTKTLFLFFIAVPGRVSEHHQLHTKVNVTRLCCVSSTDHGRTWSPIQDLTETTIGSTHQEWATFAVGPGHCLQLRNPAGSLLVPAYAYRKLHPAQKPTPFAFCFISLDHGHTWKLGNFVAENSLECQVAEVGTGAQRMVYLNARSFLGARVQAQSPNDGLDFQDNRVVSKLVEPPHGCHGSVVAFHNPISKPHALDTWLLYTHPTDSRNRTNLGVYLNQMPLDPTAWSEPTLLAMGICAYSDLQNMGQGPDGSPQFGCLYESGNYEEIIFLIFTLKQAFPTVFDAQ
Protein: ABC-type antigen peptide transporter (EC 7.4.2.14) (E7ENX8)
Organism: Homo sapiens (Human)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004530}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004352}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004352}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Antigen peptide transporter 1
- ABC-type oligopeptide transporter ABCB9
Sequence:
MRLPDLRPWTSLLLVDAALLWLLQGPLGTLLPQGLPGLWLEGTLRLGGLWGLLKLRGLLGFVGTLLLPLCLATPLTVSLRALVAGASRAPPARVASAPWSWLLVGYGAAGLSWSLWAVLSPPGAQEKEQDQVNNKVLMWRLLKLSRPDLPLLVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDRQPNLPSPGTLAPTTLQGVVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQANGFWVGPLGGGSASESDPTGFLHDSRHRLSSDVGMFVALTKLGQPDAEQWNSRLDLLERSRQAVDGVCRHNYRLGAPFTVGRKVQPEVTVYPERTPLLHQHNLLHCSVTGFYPGDIKIKWFLNGQEERAGVMSTGPIRNGDWTFQTVVMLEMTPELGHVYTCLVDHSSLLSPVSVEWRAQSEYSWRKMLSGIAAFLLGL
Protein: Protein phosphatase EYA3 (EC 3.1.3.48) (Eyes absent homolog 3) (P97480)
Organism: Mus musculus (Mouse)
Function: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1 (By similarity). Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. The phosphatase activity has been shown in vitro. Coactivates SIX1. Seems to coactivate SIX2, SIX4 and SIX5. The repression of precursor cell proliferation in myoblasts by SIX1 is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex and seems to be dependent on EYA3 phosphatase activity. May be involved in development of the eye. May play a role in mediating the induction and differentiation of cranial placodes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10490620}. Nucleus {ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:14628052}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q99504}.
Interaction partners:
- Homeobox protein SIX1
- Mediator of DNA damage checkpoint protein 1
- Homeobox protein SIX5
- Dachshund homolog 1
Sequence:
MQEPREQTLSQVNNPDASDEKPETSSLASNLSMSEEIMTCTDYIPRSSNDYTSQMYSAKPYAHILSVPVSETTYPGQTQYQTLQQSQPYAVYPQATQTYGLPPFASSTNASLIPTSSAIANIPAAAVASISNQDYPTYTILGQNQYQACYPSSSFGVTGQTNSDAETTTLAATTYQTEKPSAMVPAPATQRLPSDSSASPPLSQTTPNKDADDQARKNMTVKNRGKRKADASSSQDSELERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLSNYSFSTDGFSGSGGSGSHGSSVGVQGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLGTALKSLLLIQSRKNCANVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDEEIAAKQHNMPFWRITNHGDLVSLHQALELDFL
Protein: Auxin efflux carrier component 6 (AtPIN6) (Q9SQH6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the intracellular auxin-transport pathway. Regulates auxin transport and auxin homeostasis. Directly involved in the regulation of nectar production. Involved in unfolded protein response (UPR) activation. Involved in the control of vein patterning. Redundantly with PIN8, inhibits the vein-formation-promoting functions of PIN5. PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19506555, ECO:0000269|PubMed:23437008}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Auxin transporter-like protein 2
- Protein PIN-LIKES 2
- Auxin transporter protein 1
- ABC transporter B family member 19
- ABC transporter B family member 1
- Auxin transporter-like protein 3
- ABC transporter B family member 4
- Protein PIN-LIKES 5
- Peptidyl-prolyl cis-trans isomerase Pin1
- Protein PIN-LIKES 4
Sequence:
MITGNEFYTVMCAMAPLYFAMFVAYGSVKWCKIFTPAQCSGINRFVSVFAVPVLSFHFISQNNPYKMDTMFILADTLSKIFVFVLLSLWAVFFKAGGLDWLITLFSIATLPNTLVMGIPLLQAMYGDYTQTLMVQLVVLQCIIWYTLLLFLFELRAARLLIRAEFPGQAAGSIAKIQVDDDVISLDGMDPLRTETETDVNGRIRLRIRRSVSSVPDSVMSSSLCLTPRASNLSNAEIFSVNTPNNRFFHGGGGSGTLQFYNGSNEIMFCNGDLGGFGFTRPGLGASPRRLSGYASSDAYSLQPTPRASNFNELDVNGNGTPVWMKSPAAGRIYRQSSPKMMWESGQRHAAKDINGSVPEKEISFRDALKAAPQATAAGGGASMEEGAAGKDTTPVAAIGKQEMPSAIVMMRLILTVVGRKLSRNPNTYSSLLGLVWSLISFKWNIPMPNIVDFSIKIISDAGLGMAMFSLGLFMALQPKMIPCGAKKATMGMLIRFISGPLFMAGASLLVGLRGSRLHAAIVQAALPQGIVPFVFAREYNLHPDLLSTLVIFGMIVSLPVTILYYVLLGL
Protein: Uncharacterized protein (Q38BM4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cell division control protein, putative
- MI domain-containing protein
- Splicing factor YJU2
Sequence:
MSSTGKFVDANHASMRIDRECLHDATFNESAEEQLEKLTPGGFLHYDYRTPMAKEKRLPDQFHVVQWNIERGIQWDRVKDTFRALKADILILQELDINCRRSGYRNVAKELAKALEMEVYFLCEFEELDSTLRSPKNAVGPLSQPTLHLDSRSGNSGAGGISGQRRGQRHFHGNAILSSVATLSNVTAIPHYVGLDWEKHGVKLREPRCGFRYFMRCCIKSCERENVSMPDLYLYSCHFEIFCGVLGRARQLVDVLRDANALLKESEGMDQQPAFVLGGDLNTVVYGVVRLSKTVANDRMRFLSIGEKESCWLQRKILSRGMQWVDSAEPASQLSNIVSTLRRLYNRVINSDTMYRLLYGFSPEELEAMDNKSLCFYDPSDKVRSVTLDNPDFYGFVKGKLDWTLLSNVRVLPPELPEDIVHRLQESGSITSSSAESLRSGQPVPDGYVLFNEDFSASDHKGLLIHLMQNPGKSTETYPGDTTFRITPVSNVMFLSFLWITLWLVVAVFARSIINRNL
Protein: Non-structural maintenance of chromosomes element 4 homolog A (NS4EA) (Non-SMC element 4 homolog A) (Q9NXX6)
Organism: Homo sapiens (Human)
Function: Component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Is involved in positive regulation of response to DNA damage stimulus.
Subcellular location: Nucleus {ECO:0000269|PubMed:18086888}. Chromosome, telomere {ECO:0000305|PubMed:18086888}.
Interaction partners:
- Non-structural maintenance of chromosomes element 1 homolog
- Structural maintenance of chromosomes protein 6
- Structural maintenance of chromosomes protein 5
- Non-structural maintenance of chromosomes element 3 homolog
- E3 SUMO-protein ligase NSE2
- Small ubiquitin-related modifier 4
- EP300-interacting inhibitor of differentiation 3
- SMC5-SMC6 complex localization factor protein 2
- SMC5-SMC6 complex localization factor protein 1
- Zinc finger protein 597
Sequence:
MSGDSSGRGPEGRGRGRDPHRDRTRSRSRSRSPLSPRSRRGSARERREAPERPSLEDTEPSDSGDEMMDPASLEAEADQGLCRQIRHQYRALINSVQQNREDILNAGDKLTEVLEEANTLFNEVSRAREAVLDAHFLVLASDLGKEKAKQLRSDLSSFDMLRYVETLLTHMGVNPLEAEELIRDEDSPDFEFIVYDSWKITGRTAENTFNKTHTFHFLLGSIYGECPVPKPRVDRPRKVPVIQEERAMPAQLRRMEESHQEATEKEVERILGLLQTYFREDPDTPMSFFDFVVDPHSFPRTVENIFHVSFIIRDGFARIRLDQDRLPVIEPVSINEENEGFEHNTQVRNQGIIALSYRDWEEIVKTFEISEPVITPSQRQQKPSA
Protein: Cytochrome b6-f complex subunit 8 (Cytochrome b6-f complex subunit PetN) (Cytochrome b6-f complex subunit VIII) (P61042)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MDIVSLAWAALMVVFTFSLSLVVWGRSGL
Protein: L-Ala-D/L-Glu epimerase (AE epimerase) (AEE) (EC 5.1.1.20) (P51981)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has a role in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Arg, L-Ala-L-Lys and L-Ala-L-Pro. Is also active with L-Gly-L-Glu, L-Phe-L-Glu, and L-Ser-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala.
Interaction partners:
- Murein peptide amidase A
- Cytosol non-specific dipeptidase
- o-succinylbenzoate synthase
Sequence:
MRTVKVFEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMAQIMSVVPQLEKGLTREELQKILPAGAARNALDCALWDLAARRQQQSLADLIGITLPETVITAQTVVIGTPDQMANSASTLWQAGAKLLKVKLDNHLISERMVAIRTAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSNLKALKGRYEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAALPLVPQVSFADLDGPTWLAVDVEPALQFTTGELHL
Protein: Adenine nucleotide transporter BT1, chloroplastic/mitochondrial (Protein BRITTLE 1 homolog) (AtBT1) (Protein EMBRYO DEFECTIVE 104) (Protein EMBRYO DEFECTIVE 42) (Protein SODIUM HYPERSENSITIVE 1) (Q9SUV1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable mitochondrial adenylate carrier that catalyzes the transport of ATP, ADP and AMP, but not ADP-glucose. Recombinant BT1 shows a unidirectional mode of transport in intact E.coli cells. May function as a plastidial nucleotide uniport carrier required to export newly synthesized adenylates into the cytosol. May be involved in abiotic stress response.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Dually targeted to mitochondria and plastids. The N-terminal extension acts as a plastidic transit peptide. Dual localization of BT1 does not seem to be due to alternative transcription start sites, translation initiation sites or alternative exon splicing (PubMed:21330298). {ECO:0000269|PubMed:21330298}.
Interaction partners:
- BTB/POZ and TAZ domain-containing protein 5
- BTB/POZ and TAZ domain-containing protein 3
- BTB/POZ and TAZ domain-containing protein 4
- Small ribosomal subunit protein eS28z/eS28y
- Xylulose 5-phosphate/phosphate translocator, chloroplastic
Sequence:
MGKTGIQLFDDSRNGFFSVSDLGFDSSLNSSNYHPIGGLFASVNQTNPFASLSSSDLSNRGNNSFSTQLNDLYTKYMPGKEEEEEVVNGEKRKRKKKGGLTLKIKIANPSLRRLLSGAVAGAVSRTVVAPLETIRTHLMVGSGGNSSTEVFSDIMKHEGWTGLFRGNLVNVIRVAPARAVELFVFETVNKKLSPPHGQESKIPIPASLLAGACAGVSQTLLTYPLELVKTRLTIQRGVYKGIFDAFLKIIREEGPTELYRGLAPSLIGVVPYAATNYFAYDSLRKAYRSFSKQEKIGNIETLLIGSLAGALSSTATFPLEVARKHMQVGAVSGRVVYKNMLHALVTILEHEGILGWYKGLGPSCLKLVPAAGISFMCYEACKKILIENNQEA
Protein: Lysophospholipase NTE1 (EC 3.1.1.5) (Intracellular phospholipase B) (Neuropathy target esterase homolog) (Q04958)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium. NTE1 activity impacts the repressing transcriptional activity of OPI1, the main regulator of phospholipid synthesis gene transcription.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15044461}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15044461}. Lipid droplet {ECO:0000269|PubMed:24868093}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase GDE1
- Lysophospholipase 3
- Lysophospholipase 2
- Lysophospholipid acyltransferase
- Triacylglycerol lipase 5
- Triacylglycerol lipase 4
- Lysophospholipase 1
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Importin subunit beta-3
- cAMP-dependent protein kinase type 2
Sequence:
MRSMNCTTNNTNNTGQNTKNSLGSSFNSSNYTSYRFQTCLTDQIISEAQTWSLSSLFNFSWVVSYFVMGASRMIFRYGWYLATLSLLRIPKWIFFKLHHVQFTLSFWLILFALAVIVFVTYTIMKERILSQYKRLTPEFLPLENTGKSGSSANINAASTQSANAPPAIGSSTTGASSIIDSKKHSLKDGNENETFLSSYLDQFLSAIKIFGYLEKPVFHDLTKNMKTQKMDEGEILLLDSTIGFAIVVEGTLQLYHEVDHSDKDHGDETDHSDTDGLDDQDRDEEDEEEDDDIDNYDTKSCSSNLIDEEDESVGYIHLKNGLGNFQLLNTVKPGNPLTSLVSILNLFTHSMSSYGNSNFPSELSSPIDTTVSVNNMFCSSEQNFSNTDSMTNSTNSFPTFPSSMPKLVARAATDCTIGIIPPQSFAKLTAKYPRSASHIIQMVLTKLYHVTFQTAHDYLGLTKEIMDIEVLLNKSIVYELPYYLKEAVIRKFKTVDKSSGSADLEPKPKNSNASSKLKKPPKAKPSDGIIQSLKIANANANTSSNSLSLKPEFTHHPSSRHVVLGSRDQFNPGDLLSNVPLSRTMDILSPNPIHNNNRNKSNGINTSTSNQHKRSSRSSSNNASVHSKKFSSLSPELRNAQLSTSPLSLDNTSVHDHIHPSPVHLKGRVSPRPNLLPTTSFSAAQEETEDSALRMALVEAMLTYLGVNKSNMSVSSSSIANMSSLNSPQLNEMYSRRPSNASFLMSPHCTPSDISVASSFASPQTQPTMLRILPKEYTISNKRHNKSKSQDKKKPRAYKEELTPNLDFEDVKKDFAQGIQLKFFKKGTTIVEQNARGKGLFYIISGKVNVTTNSSSSVVSSMSKPEQVSAQSSHKGENPHHTQHLLYSVGSGGIVGYLSSLIGYKSFVNIVAKSDVYVGFLSSATLERLFDKYFLIYLRISDSLTKLLSSRLLKLDHALEWVHLRASETLFSQGDSANGIYVVLNGRLRQLQQQSLSNSNTSSEEVETQNIILGELAQGESFGEVEVLTAMNRYSTIVAVRDSELARIPRTLFELLALEHPSIMIRVSRLVAKKIVGDRTVPALTGDPLSIKENDFTSLIPPTKASYSSSLSHKPQNITSGTITFRTITILPITSGLPVEAFAMKLVQAFKQVGRTTIGLNQRTTLTHLGRHAFDRLSKLKQSGYFAELEEMYQTVVYISDTPVKSNWTRTCIAQGDCILLLADARSPSAEIGEYEKLLLNSKTTARTELILLHPERYVEPGLTHKWLRYRPWVHSHHHIQFSLTGTTLMNEGKMHVLNNGALALMDKLIQTEFSRKTQQNISKLLPDSIKNTVENFSSRFMKSKRQYYTPVHRHKNDFLRLARILSGQAIGLVLGGGGARGISHLGVIQAIEEQGIPVDVIGGTSIGSFVGGLYAKDYDLVPIYGRVKKFAGRISSIWRMLTDLTWPVTSYTTGHEFNRGIWKTFGDTRIEDFWIQYYCNSTNITDSVQEIHSFGYAWRYIRASMSLAGLLPPLEENGSMLLDGGYVDNLPVTEMRARGCQTIFAVDVGSADDRTPMEYGDSLNGFWIIFNRWNPFSSHPNIPNMAEIQVRLGYVASVNALEKAKNTPGVVYVRPPIEEYATLDFSKFEEIYHVGVDYGRIFLQGLIDDDKMPYIPGSQETTLNSQVPEFLLHRRNSI