wanglab/gogpt-training-data huggingface dataset:
Protein: Sodium- and chloride-dependent GABA transporter 1 (GAT-1) (Solute carrier family 6 member 1) (P23978)
Organism: Rattus norvegicus (Rat)
Function: Mediates transport of gamma-aminobutyric acid (GABA) together with sodium and chloride and is responsible for the reuptake of GABA from the synapse. The translocation of GABA, however, may also occur in the reverse direction leading to the release of GABA. The direction and magnitude of GABA transport is a consequence of the prevailing thermodynamic conditions, determined by membrane potential and the intracellular and extracellular concentrations of Na(+), Cl(-) and GABA. Also mediates sodium- and chloride-dependent transport of hypotaurine (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15234345}; Multi-pass membrane protein {ECO:0000255}. Presynapse {ECO:0000250|UniProtKB:P31648}. Note=Localized at the presynaptic terminals of interneurons. {ECO:0000250|UniProtKB:P31648}.
Interaction partners:
- Cytosolic arginine sensor for mTORC1 subunit 2
- Glutamate decarboxylase 1
- Glutamate decarboxylase 2
- Vesicular inhibitory amino acid transporter
- Parvalbumin alpha
- Syntaxin-1A
- Gamma-aminobutyric acid receptor subunit delta
- Excitatory amino acid transporter 2
- Gamma-aminobutyric acid receptor subunit gamma-2
- Excitatory amino acid transporter 1
Sequence:
MATDNSKVADGQISTEVSEAPVASDKPKTLVVKVQKKAGDLPDRDTWKGRFDFLMSCVGYAIGLGNVWRFPYLCGKNGGGAFLIPYFLTLIFAGVPLFLLECSLGQYTSIGGLGVWKLAPMFKGVGLAAAVLSFWLNIYYIVIISWAIYYLYNSFTTTLPWKQCDNPWNTDRCFSNYSLVNTTNMTSAVVEFWERNMHQMTDGLDKPGQIRWPLAITLAIAWVLVYFCIWKGVGWTGKVVYFSATYPYIMLIILFFRGVTLPGAKEGILFYITPNFRKLSDSEVWLDAATQIFFSYGLGLGSLIALGSYNSFHNNVYRDSIIVCCINSCTSMFAGFVIFSIVGFMAHVTKRSIADVAASGPGLAFLAYPEAVTQLPISPLWAILFFSMLLMLGIDSQFCTVEGFITALVDEYPRLLRNRRELFIAAVCIVSYLIGLSNITQGGIYVFKLFDYYSASGMSLLFLVFFECVSISWFYGVNRFYDNIQEMVGSRPCIWWKLCWSFFTPIIVAGVFLFSAVQMTPLTMGSYVFPKWGQGVGWLMALSSMVLIPGYMAYMFLTLKGSLKQRLQVMIQPSEDIVRPENGPEQPQAGSSASKEAYI
Protein: Nanchung, isoform B (M9PI57)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Transient receptor potential cation channel trpm
- MIP30126p
- SD02261p
- Ankyrin 2, isoform U
- Ankyrin, isoform B
- Transient-receptor-potential-like protein
- Calmodulin
- Calcium-binding protein E63-1
- GEO12020p1
- MIP05401p
Sequence:
MGNTESNVTSGVKKQAGVSTQALYKFVNLKGGGLLVDMMKRACQTKQFAEIDHAIKTKVEPFLYNKGAGRYFPISKLVLLRNRDRPRTRQLPEIRALENPDDDFNIHDYCPEVSEAEYISNPTAYRFVCWDLNMRGAVGETILHLCLLNASSLHADLAKRLLKFYPKLILDIYMSDEYYGESVLHIAIVNEDPAMVKYLLDANADVQERCCGAFMSAEDTKFSRTDSPDHEYVALCPMTNYDGYVYWGEYPLSFAACLSQEECFRLVLARGADPDFQDTNGNTVLHMLVIYEKIEMFDVGYEVGTNIHIKNIQNLTPLTLAAKLGRVEMFFHVMSIEREIYWQLGSITCAAYPLLMIDTINEETGNINKDSVLNFVVFGDKLEHLELLDGVVIDLLKTKWDTFCKSRFYKQFYMFALYFLISLFSFILRPGPDAKDEDEDGANSTTAKSDLYRQNGSDSYHLHSKRATMTTEYKTFWLNFTEYYDPSEVEVLPAWWESYAQCPLMNLESDLAKLRIMAELLNFVGAILYLLVALREARFLGLKMFIENLMTAPSRVMFLFSCALMMTIPWLRVSCLTEIDDHVTVVIMLTTAPYFLFFCRGFKTVGPFVVMIYRMVMGDLLRFVSIYLVFVMGFSQAFYIIFLTFDNPSSPEDQDAESNPMPSPMESIVAMFLMSLTNFGDYYGAMVSTQHEYEAKILFFLFMVIVSVLLVNMLIAMMGNTYQKIAEIRNEWQRQWARIVLVVERSVPPAERLKNFMQYSQSMSDGRRALVLRLNMTEEEKEEMKEVQEMKRIHQRFAKKRQMEREARALRRQQEYEKFFGTAPKSECSDNNNF
Protein: Malate synthase (EC 2.3.3.9) (Q5APD2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- Isocitrate lyase
- Citrate synthase
- Acetyl-coenzyme A synthetase
- Phosphoenolpyruvate carboxykinase
- Acetyl-coenzyme A synthetase 2
- Malate dehydrogenase, cytoplasmic
- Acetyl-CoA hydrolase
- malate dehydrogenase
- Pyruvate carboxylase
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MSSPFPKTADKIKGVQILGPVPESAKHIFNQETLAFVATLHRGFEARRQELLNNRKEQQKLRDQGFLPDFLPETEYIRNDATWTGPPLAPGLVDRRCEITGPTDRKMVINALNSNVATYMADFEDSLTPAWKNLVEGQVNLYDGVRRNLTANINGKNYALNLDKGRHIPTLIVRPRGWHLDEKHVLVDGKPVSGGIFDFAVYFFNNAQETLARGFGPYFYLPKMEHHLEAKLWNDIFNYAQDYIGLRRGTIRASVLIETIPAVFQMDEIIYQLREHSAGLNCGRWDYIFSYIKCLRNHPDFILPDRSQVTMAAPFMSSYVKLLVHTTHKRKVHALGGMAAQIPIKDDEERNRAALANVTKDKLREVTLGCDSCWVAHPALVPVVLKVFNENMKGPNQISLPPKEPFKPITQRDLLSPFVPNAKITEQGIRANIIIGISYIEAWLRNVGCVPINYLMEDAATAEVSRTQIWQWVTHGAKTDTGKVIDKQYVKQLLDEEYAKLVKSAKPGNKFKRAFEYFAPEALGEKYSDFVTTLIYDDITTIGRSLPGERL
Protein: DNA topoisomerase 1 (EC 5.6.2.1) (DNA topoisomerase I) (P11387)
Organism: Homo sapiens (Human)
Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the BMAL1 promoter.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12149243}. Nucleus, nucleoplasm {ECO:0000269|PubMed:12149243}. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli.
Interaction partners:
- DNA topoisomerase 2-alpha
- Tyrosyl-DNA phosphodiesterase 1
- DNA topoisomerase 2-beta
- Cellular tumor antigen p53
- E3 ubiquitin-protein ligase Topors
- Poly [ADP-ribose] polymerase 1
- THO complex subunit 4
- Serine/arginine-rich splicing factor 1
- BTB/POZ domain-containing protein 1
- RNA-binding motif protein, X chromosome
Sequence:
MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF
Protein: 60S ribosomal protein L21 (Q8ILK3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 40S ribosomal protein S11, putative
- 40S ribosomal protein S28e, putative
- 60S ribosomal protein L29
- Small ribosomal subunit protein eS12
- 40S ribosomal protein S15
- 60S ribosomal protein L3
- 60S ribosomal protein L27
- Small ribosomal subunit protein eS30
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S5, putative
Sequence:
MGGKSRGKRSGTRYKFSKKFRKHGECTANKYLEKLNYGDYVDIVCDSTQQKGMPFNYYHGKTGKIFHITKRGVGVLVNKRVKHRIEQKKVCVRIEHVRKSRCNEDFLLRKIKNAELIKEAKLKNEHINIKRKTEGPKPAAMIKVPPSKIITIEPLPFYEEY
Protein: Nuclear factor Y, subunit B1 (F4ITZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MADTPSSPAGDGGESGGSVREQDRYLPIANISRIMKKALPPNGKIGKDAKDTVQECVSEFISFITSEASDKCQKEKRKTVNGDDLLWAMATLGFEDYLEPLKIYLARYREVFETNSVLFIPWDWLLTHHLLMQLEGDNKGSGKSGDGSNRDAGGGVSGEEMPSW
Protein: Stress-activated protein kinase alpha (SAPK-alpha) (EC 2.7.11.1) (Q86AT8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May be involved in cortical F-actin organization and resistance to osmotic stress. Activated upon cell detachment, in vitro.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14593072}. Note=Associated with the cytoskeletal cortex in response to chemoattractant stimulation. Colocalizes with F-actin in F-actin-enriched structures, including membrane ruffles and pseudopodia during chemotaxis.
Interaction partners:
Sequence:
MSSTQQQQHQLFSAVEQNDVTKVKKLSSKKKISKSNLTSFDQYGQSALTIALKNNNEEMVELLLSLCVTLKADINTFDKNGFSALHQAVSSDDRILMRVLQYENINVDVQNDDLNTPIHYFCQKFRSPNCQEPFQLFIQKGVNVNAQNKNGETPLHKAIFNNSVRLMMVGLLLKNGANVNLATQFQESPLHYAVRLGREDLVSVLLKAGADVDCVGTKERKTPYQLAVEEGNKDMTARIKKYKDLFDWLQKHGFEQYKDAFLKEEMFLDELGEMSEDILNKMGITSTGTRLRILKETSNLANEQTKKPKTPELIIEEDPTPPDTPDISGLRHSLHTLRHVGEVNIINDNELEYTEKLGAGSSGKVYKGLYRGKEVAIKVLKSMTESKEIEEFKKEFQIMSAIRSKHVVHFYGAVLEPKLCMVMENCSRGSLYHVMDNNSLDIGWERTFRFAIETVRGIECLHKWDPPIVHRDLKSLNLLVNDKWEIKVCDFGLSRFNTGSNLETLVKMRGTFAYCAPEVYYGEQFSGKSDVYSIAVILWELVTRCINGRYERPFSEYKNLQHDFQIIIQTAKKNLRPTIPNACPESLVSLIQDCWDPNLENRPTCTDILSRLVTIENEYRSNIQTWNNLIVPLPKNQE
Protein: Putative esterase C31F10.02 (EC 3.1.2.-) (P87304)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
Sequence:
MAINSSGTKVLSFVRSVWQDFVNTNGFDAHVVSDIQIISAVPGFVECSLKLQKHHLNRMGNLHGGCIAALTDLGGSLALASRGLFISGVSIDMNQTFLQSGGTLGSSILLHAKCDRLGSNIAFTSVDFLTSSNEVFAKGRHTKFVRNALGDPRNCLDLAED
Protein: Bystin (Protein bys) (P51406)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q13895}.
Interaction partners:
- Pre-rRNA-processing protein TSR1 homolog
- Protein LTV1 homolog
- KRR1 small subunit processome component homolog
- Nucleolar protein 14 homolog
- RNA-binding protein NOB1
- LD10780p
- RRP12-like protein
- LD38375p
- RNA cytidine acetyltransferase
- U3 small nucleolar RNA-associated protein 18 homolog
Sequence:
MGKPKKANVATIKNVNLEKQITEGRVAKNKNKDKVKLRAEESANIDARSSQKILAAAKLQQLELDEENFPSLVTVKKVNFSLNDGHVKEDEEVNETDLMADLDMDEDDVAAFERFQQPAQEGKRTLHLSKMIMQKIQEKEADIHTKISDEGSLKIEEIDPKVKEMYEGVRDVLKRYRSGKIPKAFKIIPKLRNWEQILFITEPHNWSAAAMFQGTRIFCSVLSQAMAQRFYNLVLLPRVRDDLCEYKKLNMHLYNALKRALFKPAAFMKGIILPLLEGGDCTLREAIIFGSVVARSSIPVLHSSACLLKICEMAYSGANSIFIRYFLDKRYALPYRVVDAAVFHFLRFENDKRELPVLWHQSLLTFAQRYKNDISSEQRDALLQLLKKKSHFKITPDVRRELQAASCRDVEMMETDNGLAGQPAKMYTDADVEYEG
Protein: Glc operon transcriptional activator (Glc regulatory protein) (HTH-type transcriptional regulator GlcC) (P0ACL5)
Organism: Escherichia coli (strain K12)
Function: Transcriptional activator of the glcDEFGB operon which is associated with glycolate utilization, and encodes malate synthase G and the genes needed for glycolate oxidase activity. Also negatively regulates the transcription of its own gene. Glycolate acts as an effector, but GlcC can also use acetate as an alternative effector.
Interaction partners:
- Protein GlcG
- Glycolate oxidase subunit GlcD
- Malate synthase G
- DNA-binding transcriptional activator MhpR
- Hca operon transcriptional activator HcaR
- Glycolate oxidase iron-sulfur subunit
- Glycolate permease GlcA
- Glycolate oxidase subunit GlcE
Sequence:
MKDERRPICEVVAESIERLIIDGVLKVGQPLPSERRLCEKLGFSRSALREGLTVLRGRGIIETAQGRDSRVARLNRVQDTSPLIHLFSTQPRTLYDLLDVRALLEGESARLAATLGTQADFVVITRCYEKMLAASENNKEISLIEHAQLDHAFHLAICQASHNQVLVFTLQSLTDLMFNSVFASVNNLYHRPQQKKQIDRQHARIYNAVLQRLPHVAQRAARDHVRTVKKNLHDIELEGHHLIRSAVPLEMNLS
Protein: Collagen, type I, alpha 1b precursor (Collagen, type I, alpha 3) (Q6PEI9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MFSFVDIRLGLLLAAVVLAVRGQGEDDISFGSCTLEGQNYNDKDVWKPEPCQICVCDSGTVMCDEVICEDTSDCANPEIPDGECCPICPDEEVTAAPEPPYVDTVGPAGPRGDPGPVGPPGRDGTPGENGLPGPPGPPGTSGLGGGSFLSQMAYGSEKSSGPPQPGPPGPMGPRGLPGPAGSPGPQGFTGPPGEPGEPGAPGPMGSRGPPGPPGKNGEDGEAGKAGRPGERGAAGPQGARGFPGTPGLPGIKGHRGFPGLDGAKGDAGIAGPKGEAGSPGEAGTPGAMGARGLPGERGRPGPPGPSGARGNDGNTGAAGPPGPTGPAGPPGFPGGAGAKGETGAAGGRGSEGPQGPRGEPGNPGPAGAAGPAGGPGSDGTPGGKGSPGAAGIAGAPGFPGARGPPGPAGPNGAPGPKGNNGDPGLQGPKGDAGPKGEPGPVGPQGLAGNAGEEGKRGARGEPGAAGPVGPPGARGAPGNRGLPGSDGAPGPLGAPGERGANGPMGAQGASGESGRPGEPGLPGSKGMTGAPGSPGPDGKAGPSGAPGQDGRPGPPGPAGSRGAPGVMGFPGPKGTDGESGKPGERGLAGPTGPLGAPGKDGDIGSPGAPGPAGPAGEKGEQGSAGPSGFQGLPGAQGATGETGKPGEQGLPGEAGPSGPSGPRGDRGFPGERGAPGPGGPTGPRGAPGSPGNDGAKGEPGAAGANGGVGPAGMQGMPGERGAGGMPGARGDRGDGGPKGPDGAPGKDGVRGMTGPIGPPGPSGAPGDKGEPGAVGPPGLTGPRGGPGERGEVGAPGPAGFAGPPGGNGQPGAKGETGDSGPKGDAGAPGPAGPVGASGPQGPAGATGPKGARGGAGPPGATGFPGAAGRVGPPGPSGASGPPGPTGPAGKEGQRGARGEKGPAGRPGEAGAAGPPGPSGERGSPGPDGPLGLAGAPGPPGVIGSRGIVGLPGQRGERGFGGLAGPSGEPGKQGPSGPVGERGPPGPMGPPGLSGAPGEAGREGNPGHDGVSGRDGPPGPKGDRGESGNSGPPGAPGAPGAPGPIGPSGKTGDRGEAGPAGPAGPSGPAGARGALGPAGPRGDRGEAGEAGERGMKGHRGLSGMPGVPGPPGTSGEQGPAGATGPAGPRGPAGSNGSPGKDGMNGVPGPVGPPGPRGRSGEMGPAGAPGLPGPPGPPGSAGPGEPFLPMPQQEKGPDPLRGGYRADDASVRDRDSEVDTSLKSLSQKIENIRSPEGTQANPARMCRDLRMCHPEWKSGSYWVDPNQGSPLDAIKVFCNMETGETCVSPYHSDIPRKNWYTSKNIREKKHVWFGESMPNGFQFQYGSDGSDPEDVNIQLTFMRLMSNQGSQNITYHCKNSIAYMDETSGNLKKALLLQGSNDIEIRAEGNSRFTYRVSEDGCTSHTGTWGKTVIDYKTTKTSRLPIIDIAPMDIGAPDQEFGVEVGPVCFL
Protein: Glycosylphosphatidylinositol anchor attachment 1 (A0A8I6GMH5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGLLSDPVRRRALARIVLRLNTPLCVLSYVAGIAWFLALAFPPLTQRTYMSENAMGSTMVEEQFVGGDRARNFARDFAAHRKKPGALPVAWLERAMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRAASTESLVLTVPCGPDTTNSQALGLWSGRNMIFWCSLLAPTGIQSSPLQGRAGAIQAAVALELSSDVVTSLDVTVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPQDWTSLEGPLQGLQTLLLMVLRQASGRPHGPHGLFLRYGVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFFYLLPALSRFVSIGLYMPATGFLLLVLGLKISSTLLWMQLHEAGVNPEEAGKAPGPGSPPLATQSVSLASLMAPLLISQAMGLALYFLPVLGQHVAAQHFPVAEAEAVVLTLLAIYVAGLALPHNTHRVVSSQVPDRGWMALKLVALIYLALQLGCIALLNFSLGFLLAATMVPAAALTKPHGPRTLYAALLVVTSPAVTLFGSLFLWRELQEVPLSLAEGWQLFLTALAQGVLEHYTYGALLFPILALGLYPCWLLFWNVLFWK
Protein: inositol-polyphosphate 5-phosphatase (EC 3.1.3.56) (Q8T8Q6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MESAQEDASSTDVFLVTANVGSLFEDPERLLQLWLSEFLAKIAVAQPRFLALHLQEVGGKTYEKSMEYVQEFIRCLCDAPEMGDFTCVHIFMDEDFKSAEHFTALGSLYFVHKDVASLKIWNFLTHSWEESLQDVKDKHIYSGNIETIATKEKSKFPQHFFPECKWSRKGFMRTRWEINGTVIDLVNIHLFHDASNLAACENFPSVYCKTRRRALVHTIERFHLDEQNGTVPFFLFGDFNFRCDTEGVVKELTENLTPHRVQNVKNENDKIHYRNSTGNNVLTVGKKEFSHADHQLKFKEDWLKKFDRELEPLKDVLVEYPIKFVPSYPFEEDPEMPTDYMSTRCPAWCDRILMSPQVNEIIQSDDWTYGMIGEAVCMGDHKALRIPQLYRSYRRAWRTW
Protein: AP-1-like transcription factor YAP7 (Q08182)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable transcription activator linked to cell cycle that induces transcription activation of genes in the environmental stress response and metabolism control pathways, like the closely related YAP5.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- AP-1-like transcription factor YAP1
- AP-1-like transcription factor YAP2
- AP-1-like transcription factor YAP4
- AP-1-like transcription factor YAP6
Sequence:
MRQRRSVVAVSVKPKGFKLGHKQGSMSTTSPPPSSPDGNVSTSGPSAIKLSKNWELPQRLKPGRKPKSKRGDASANNDGSSKIKKVQTSNQKDQMTTKDHENEGAKGHEGKSDDEGNGSGDENGVDSVEKRRRQNRDAQRAYRERRTTRIQVLEEKVEMLHNLVDDWQRKYKLLESEFSDTKENLQKSIALNNELQKALPLIVNTPFQQQPENPPDNPISILEMVENFKPIGAVSLKKGKLKAHC
Protein: Transmembrane protein 190 (Q9D2E9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000269|PubMed:21273369}; Single-pass type I membrane protein {ECO:0000269|PubMed:21273369}. Note=Localizes in the intracellular space in testicular germ cells and sperm. Detected also on the cell surface in post-meiotic round spermatids. In cauda epididymal sperm relocates during the acrosome reaction from the inner-acrosomal membrane onto the equatorial segment surface, on which sperm-oocyte fusion occurs. Colocalizes with IZUMO1 at the inner-acrosomal membrane.
Interaction partners:
- Sperm acrosome membrane-associated protein 3
- Fibrous sheath CABYR-binding protein
- Histone H1.9
Sequence:
MVGSGISALGLLLLMQGSVDANGIQGFFYPWSCEGDVWDRESCGGQAAIENPNLCLRLRCCYRDGVCYHQRPDENMRRKHMWALGWTCGSLLFLITSICLFWWARRQDMLHLPRFLHRKCSKLSKTVSSLSKDRRSANKSTTVLQSPGGEVETAAAVSGEDTGGEE
Protein: Salivary glue protein Sgs-8 (P02842)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Salivary glue protein Sgs-5
- Ecdysone-induced gene 71Ee
- Salivary glue protein Sgs-4
- Sgs5bis
- Salivary glue protein Sgs-3
- Salivary glue protein Sgs-7
- Salivary gland secretion 1
Sequence:
MKLLVVAVIACIMLIGFADPASGCKDCSCVICGPGGEPCPGCSARVPVCKDLINIMEGLERQVRQCACGEQVWLF
Protein: Sulfate adenylyltransferase subunit 2 (EC 2.7.7.4) (ATP-sulfurylase small subunit) (Sulfate adenylate transferase) (SAT) (Q87WW0)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Function: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Interaction partners:
- Sulfate adenylyltransferase subunit 1
- Adenylyl-sulfate kinase
- Sulfate transport system permease protein CysW
- Sulfate/thiosulfate import ATP-binding protein CysA
- Sulfate-binding protein
- Sulfate ABC transporter, periplasmic sulfate-binding protein
- Sulfate transport system permease protein CysT
- 3'
- Adenosine 5'-phosphosulfate reductase
- Sulphite reductase
Sequence:
MVDKLTHLKQLEAESIHIIREVAAEFDNPVMLYSIGKDSAVMLHLARKAFFPGKLPFPVMHVDTRWKFQEMYRFRDQMVEEMGLDLITHINPDGVAQGINPFTHGSAKHTDIMKTEGLKQALDKHGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDPKNQRPELWNVYNGNVNKGESIRVFPLSNWTELDIWQYIYLEGIPIVPLYFAAERDVIEKNGTLIMIDDERILEHLTDEEKSRIVKKKVRFRTLGCYPLTGAVESEATSLTDIIQEMLLTRTSERQGRVIDHDGAGSMEEKKRQGYF
Protein: PDZ and LIM domain protein Zasp (G5EEL1)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MERVTVRMARSDRRTPWGFGVTEAPDGAVLIVNVIGGSLADRAGLRNGDVVDRLEDLDNLDINAVDRLLVTAHEKIELIVTRQPSGAATRIWRPEVTENTGPGQDQTPYRVNLQHSSDTRPPQGFNNSALPFETDQRVKHMQYNSPLGIYSDKSAAEQYVQQTQGLGDNSGARAAAQRQDEPAYLRSETLRLLKEQEHGSAGGAGTTLSNHPNPSGLPVCFMCTRPILGVMARAAGKNLHGDCLSCATCGNSLRNVGHHFIEDKFYCDIHGTQRKHGGRPGMDPNIFVKSSPTAAQPVHIQDSPRAAYHPQVNTARPVSVSPAPSAGSKTVTTHYHTPKTQGILSPGQRGVPTAAFGADLSKSVTYGGGVGPGGTHYDSNRLSPAPSQYSTQSRNQSQQHYQQHVVQAPPPVPSNPPPSNGSSYTKTSFERTTTETRPQQNTGAPRAGDFRGTGHLTTTTTTQQNGGRAPFCESCKQQIRGAFVLATGKSWCPEHFVCANSSCRRRLLECGFVEEDGQKFCESCFEQHIAPRCNKCSKPIISDCLNALQKKWHPTCFTCAHCQKPFGNSAFYLEQGLPYCEQDWNALFTTKCVSCRYPIEAGDRWVEALGNAFHSNCFTCARCNHNLEGESFFAKNGQPFCRLHA
Protein: Lactoylglutathione lyase (EC 4.4.1.5) (Aldoketomutase) (Glyoxalase I) (Glx I) (Ketone-aldehyde mutase) (Methylglyoxalase) (S-D-lactoylglutathione methylglyoxal lyase) (Q9CPU0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (By similarity). Required for normal osteoclastogenesis.
Interaction partners:
- Hydroxyacylglutathione hydrolase, mitochondrial
- Glyoxylate reductase/hydroxypyruvate reductase
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Amine oxidase [copper-containing] 3
- Serine dehydratase-like
- L-serine dehydratase/L-threonine deaminase
- Amine oxidase [copper-containing] 2
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
Sequence:
MAEPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKIATII
Protein: Aspartic proteinase PCS1 (EC 3.4.23.-) (Aspartic protease 38) (AtASP38) (Protein EMBRYO DEFECTIVE 24) (Protein PROMOTION OF CELL SURVIVAL 1) (Q9LZL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Embryo-specific aspartic protease that limits programmed cell death during reproductive development. Possesses peptidase activity toward casein in vitro.
Subcellular location: Endoplasmic reticulum.
Interaction partners:
- Embryo defective 2737
- Eukaryotic aspartyl protease family protein
- Alanine--tRNA ligase, chloroplastic/mitochondrial
- Phosphatidylinositol/phosphatidylcholine transfer protein SFH11
- FAD/NAD
- Pentatricopeptide repeat-containing protein At1g30610, chloroplastic
- Aspartic proteinase A3
- U4/U6 small nuclear ribonucleoprotein PRP4-like protein
- Ankyrin repeat domain-containing protein EMB506, chloroplastic
- Myb family transcription factor EFM
Sequence:
MFSRFHALFLLLVLSVRTYKCVSSSSSSSSSFSFSSFSSSSSSQTLVLPLKTRITPTDHRPTDKLHFHHNVTLTVTLTVGTPPQNISMVIDTGSELSWLRCNRSSNPNPVNNFDPTRSSSYSPIPCSSPTCRTRTRDFLIPASCDSDKLCHATLSYADASSSEGNLAAEIFHFGNSTNDSNLIFGCMGSVSGSDPEEDTKTTGLLGMNRGSLSFISQMGFPKFSYCISGTDDFPGFLLLGDSNFTWLTPLNYTPLIRISTPLPYFDRVAYTVQLTGIKVNGKLLPIPKSVLVPDHTGAGQTMVDSGTQFTFLLGPVYTALRSHFLNRTNGILTVYEDPDFVFQGTMDLCYRISPVRIRSGILHRLPTVSLVFEGAEIAVSGQPLLYRVPHLTVGNDSVYCFTFGNSDLMGMEAYVIGHHHQQNMWIEFDLQRSRIGLAPVECDVSGQRLGIGS
Protein: Cytochrome c oxidase subunit 6A2, mitochondrial (Cytochrome c oxidase polypeptide VIa-heart) (COXVIAH) (P43023)
Organism: Mus musculus (Mouse)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Plays a role in the assembly and stabilization of complex IV.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 9
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 3
Sequence:
MALPLKVLSRSMASAAKGDHGGAGANTWRLLTFVLALPGVALCSLNCWMHAGHHERPEFIPYHHLRIRTKPFAWGDGNHTLFHNPHVNPLPTGYEHP