wanglab/gogpt-training-data huggingface dataset:
Protein: Ski-like protein (Ski-related oncogene) (Ski-related protein) (P12757)
Organism: Homo sapiens (Human)
Function: May have regulatory role in cell division or differentiation in response to extracellular signals.
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 3
- E3 ubiquitin-protein ligase Arkadia
- Nuclear receptor corepressor 1
- Ski oncogene
- Mothers against decapentaplegic homolog 7
- E3 ubiquitin-protein ligase SMURF2
- Mothers against decapentaplegic homolog 5
- Mothers against decapentaplegic homolog 6
Sequence:
MENLQTNFSLVQGSTKKLNGMGDDGSPPAKKMITDIHANGKTINKVPTVKKEHLDDYGEAPVETDGEHVKRTCTSVPETLHLNPSLKHTLAQFHLSSQSSLGGPAAFSARHSQESMSPTVFLPLPSPQVLPGPLLIPSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQRLCNALLRPRTFPQNGSVLPAKSSLAQLKETGSAFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYLGTPEEKKLKIILEEMKEKFSMRSGKRNQSKTDAPSGMELQSWYPVIKQEGDHVSQTHSFLHPSYYLYMCDKVVAPNVSLTSAVSQSKELTKTEASKSISRQSEKAHSSGKLQKTVSYPDVSLEEQEKMDLKTSRELCSRLDASISNNSTSKRKSESATCNLVRDINKVGIGLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE
Protein: Twinfilin-2 (A6-related protein) (hA6RP) (Protein tyrosine kinase 9-like) (Twinfilin-1-like protein) (Q6IBS0)
Organism: Homo sapiens (Human)
Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10406962}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10406962}. Cell projection, stereocilium {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization.
Interaction partners:
- Gelsolin
- Epidermal growth factor receptor kinase substrate 8-like protein 2
- Unconventional myosin-XV
- Espin
- Epidermal growth factor receptor kinase substrate 8
- Adenylyl cyclase-associated protein 1
- Whirlin
- Adenylyl cyclase-associated protein 2
- WD repeat-containing protein 82
- Myosin-IIIa
Sequence:
MAHQTGIHATEELKEFFAKARAGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNAQGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCAAPAPLTSAERELQQIRINEVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDVAQLPSRVPRDAARYHFFLYKHTHEGDPLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFKQAFAKPKGPGGKRGHKRLIRGPGENGDDS
Protein: Mitochondrial glycine transporter YMC1 (Yeast mitochondrial carrier protein 1) (P32331)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Secondary mitochondrial glycine transporter required for the biosynthesis of heme at high glycine concentrations. Imports the precursor glycine into the mitochondrial matrix, where it is condensed with succinyl-CoA to produce 5-aminolevulinate (ALA), the first step of heme biosynthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823961, ECO:0000305|PubMed:10930523}; Multi-pass membrane protein {ECO:0000269|PubMed:16823961, ECO:0000305|PubMed:10930523}.
Interaction partners:
Sequence:
MSEEFPSPQLIDDLEEHPQHDNARVVKDLLAGTAGGIAQVLVGQPFDTTKVRLQTSSTPTTAMEVVRKLLANEGPRGFYKGTLTPLIGVGACVSLQFGVNEAMKRFFHHRNADMSSTLSLPQYYACGVTGGIVNSFLASPIEHVRIRLQTQTGSGTNAEFKGPLECIKKLRHNKALLRGLTPTILREGHGCGTYFLVYEALIANQMNKRRGLERKDIPAWKLCIFGALSGTALWLMVYPLDVIKSVMQTDNLQKPKFGNSISSVAKTLYANGGIGAFFKGFGPTMLRAAPANGATFATFELAMRLLG
Protein: Anthocyanidin reductase (AtANR) (EC 1.3.1.77) (Anthocyanin spotted testa) (ast) (Protein BANYULS) (Q9SEV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of condensed tannins. Converts cyanidin into (-)-epicatechin as the major product.
Interaction partners:
- Leucoanthocyanidin dioxygenase
- 2-oxoglutarate
- Naringenin,2-oxoglutarate 3-dioxygenase
- Chalcone synthase
- Flavonoid 3'-monooxygenase
- Flavonol synthase/flavanone 3-hydroxylase
- Trans-cinnamate 4-monooxygenase
- Jasmonate-induced oxygenase 4
- Anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase
- Probable flavonol synthase 5
Sequence:
MDQTLTHTGSKKACVIGGTGNLASILIKHLLQSGYKVNTTVRDPENEKKIAHLRKLQELGDLKIFKADLTDEDSFESSFSGCEYIFHVATPINFKSEDPEKDMIKPAIQGVINVLKSCLKSKSVKRVIYTSSAAAVSINNLSGTGIVMNEENWTDVEFLTEEKPFNWGYPISKVLAEKTAWEFAKENKINLVTVIPALIAGNSLLSDPPSSLSLSMSFITGKEMHVTGLKEMQKLSGSISFVHVDDLARAHLFLAEKETASGRYICCAYNTSVPEIADFLIQRYPKYNVLSEFEEGLSIPKLTLSSQKLINEGFRFEYGINEMYDQMIEYFESKGLIKAK
Protein: Cellular retinoic acid-binding protein 2 (Cellular retinoic acid-binding protein II) (CRABP-II) (P29373)
Organism: Homo sapiens (Human)
Function: Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.
Subcellular location: Cytoplasm. Endoplasmic reticulum. Nucleus. Note=Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus.
Interaction partners:
- Retinoic acid receptor beta
- Retinoic acid receptor gamma
- Retinoic acid receptor alpha
- Retinoic acid receptor RXR-alpha
- Protein S100-A13
- Phospholipase A and acyltransferase 4
- Phospholipase A and acyltransferase 3
- Protein polybromo-1
- G1/S-specific cyclin-D3
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MPNFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCKSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE
Protein: Malolactic enzyme (MLE) (EC 4.1.1.101) (Q48796)
Organism: Oenococcus oeni (Leuconostoc oenos)
Function: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate. It can also use pyruvate as substrate.
Interaction partners:
Sequence:
MTDPVSILNDPFINKGTAFTEAEREELGLNGLLPAKVQALQEQVDQTYAQFQSKVSNLEKRLFLMEIFNTNHVLFYKLFSQHVVEFMPIVYDPTIADTIENYSELFVEPQGAAFLDINHPENIQSTLKNAANGRDIKLLVVSDAEGILGIGDWGVQGVDIAVGKLMVYTVAAGIDPSTVLAVVIDAGTNNEKLLKDPMYLGNKFNRVRGDKYYDFIDKFVNHAESLFPNLYLHWEDFGRSNASNILNSYKDKIATFNDDIQGTGIVVLAGVLGALKISGQKLTDQTYMSFGAGTAGMGIVKQLHEEMVEQGLSDEEAKKHFFLVDKQGLLFDDDPDLTPEQKPFAAKRSDFKNANQLTNLQAAVEAVHPTILVGTSTHPNSFTEEIVKDMSGYTERPIIFPISNPTKLAEAKAEDVLKWSNGKALIGTGVPVDDIEYEGNAYQIGQANNALIYPGLGFGAIAAQSKLLTPEMISAAAHSLGGIVDTTKVGAAVLPPVSKLADFSRTVAVAVAKKAVEQGLNRQPIDDVEKAVDDLKWDPKY
Protein: Uncharacterized HTH-type transcriptional regulator Rv0681 (O53789)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Putative mycofactocin biosynthesis transcriptional regulator MftR
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS7
- Probable conserved transmembrane protein
Sequence:
MAAQPQAPSAGGRPRAGKAVKSVARPAKLSRESIVEGALTFLDREGWDSLTINALATQLGTKGPSLYNHVDSLEDLRRAVRIRVIDDIITMLNRVGAGRARDDAVLVMAGAYRSYAHHHPGRYSAFTRMPLGGDDPEYTAATRGAAAPVIAVLSSYGLDGEQAFYAALEFWSALHGFVLLEMTGVMDDIDTDAVFTDMVLRLAAGMERRTTHGGTAST
Protein: Hydroxyacid-oxoacid transhydrogenase, mitochondrial (HOT) (EC 1.1.99.24) (Alcohol dehydrogenase iron-containing protein 1) (ADHFe1) (Fe-containing alcohol dehydrogenase) (Q8IWW8)
Organism: Homo sapiens (Human)
Function: Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). D,L-3-hydroxyisobutyrate and L-3-hydroxybutyrate (L-3-OHB) are also substrates for HOT with 10-fold lower activities.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Myocardin-related transcription factor A
- Hydroxysteroid dehydrogenase-like protein 2
- Sorbitol dehydrogenase
- Carboxymethylenebutenolidase homolog
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Alanine--glyoxylate aminotransferase
- Vasopressin-neurophysin 2-copeptin
- Deoxyribose-phosphate aldolase
- Pseudouridine-5'-phosphatase
- Monoglyceride lipase
Sequence:
MAAAARARVAYLLRQLQRAACQCPTHSHTYSQAPGLSPSGKTTDYAFEMAVSNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPYHLRSPCPSNPITRPAYQGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASMKLY
Protein: AP-1 accessory protein LAA1 (Large AP-1 accessory protein 1) (P39526)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the trans-Golgi network (TGN)-endosome transport. Important for the correct localization of the adapter protein complex AP-1.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16687571, ECO:0000269|PubMed:16702403}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:30523155}. Note=Colocalizes with AP-1 adapter complex, with clathrin-coated vesicles to the late-Golgi apparatus and with ribosomes (PubMed:30523155). Localization depends on ADP-ribosylation factor (ARF) (PubMed:16702403). {ECO:0000269|PubMed:16702403, ECO:0000269|PubMed:30523155}.
Interaction partners:
- AP-1 complex subunit gamma-1
- Putative transcriptional regulatory protein YJL206C
Sequence:
MANRSLKKVIETSSNNGHDLLTWITTNLEKLICLKEVNDNEIQEVKEIHTQLDEFVRYISVLENTDDLELHSVFISLSQLYTISIWRLKDEYPGVVFDSAAFLTNVLCEEDVSIDDGDTDPNQKKKKKKSSTKKKKYIYSPAKDIACTILVQLFENFGSSISSLIPLLFNAIFKNLKKIMEKSKYYHATFMTTLLQLFNAILRNSNNDDKILDPATYAKFSKLSKTVFDSISTDEKDFSVTFVSVLIECWTAHFKQTNFIREHSHDIIETIYSRFTEGEIGVYGFANDETRIFTAKSLAEILFDYYFSKNILTLQEVWSIYVKIFLNCDTRDVESGCFESIIHLINLNLLADNTFLSNSKYLDIVLSLSGVFSSYEVNNRSMNTLSRYLRYFQHMHEVILPHLNDSAKTQMLYYILGCSDTYQSSSKSDSASNFKYSIDAKPETQWLTLLQLDFTYVLISDLGSTFTTEENTVKEIRDKLVDLATCEIFTIRVHTVEILKVFLNNCPEYLSETIENSLRALSTDFKSTGKFIFHKNHGHAFIIANLIKGAESDYISYELIMRITVFSTSFIKNNTTSTSSNLYFKGLLCWILLIGLMNYKDEQYLKLQIPQLFLFWKVLLTHTYTYHDEDELYKNLEIRNHALTCLLTYLSNTTIDKEMAKQVSYLLTKCSNFNHSIDLKSKNIDNALLHNENRILQVYLKLEKYINSDFNSSLLILIVKNFSDPNLYTESSSSVLGSLKDIGNRKVSNKDDMESNIVLESSINTLLRQNNGFAFGLSSKITGDRIVNLSMSSAYKYDESISGSWPSKDYNWYNIFEVEVSKPISPILSLDSLILLYGSGSYSQIDRYAPQVTTSLIDSSMELFSSVFPFLNSKIQYSIMETLNLSMFSKMTTPLRSVAVAANVCSALHNALRIMQENNLELDYSVGQLIIESIKKIQFFNDIFLTKIKADCVGLLTAAIARTLGDEERQKFLTEQSRIFIKNVADMDEPYLRMFHVLSLATIFKYNSQYANFEEYFDVIFALMRDPHPVVHSWSLKAMHILLEKHLVIDLKTAALLLSSMEELLVQDKYGIYGRSTLRCNYNRDFNSHVAIGEISRTLTETVGPNFLELNTKVLDSFRNITLSMLISNNILNSITSIKMFENIATFKMKNILNYEIFILASKSIIKSSIVTGIGSSYFDTTFTGSNELISRTSSLKGAFENFDLLTLLYKLQMEEFFMKEMENLSWRYLALFPNSGSVKNYFTEWILHTFKRDNHWFDKLYSIFNMSLGRLFQSYNRDVSALLEVNGLKKSSEKEIKGEEEESIANVNQLTDTDAGGLDSENLQWKSRQIILNLILMLCLESEKYENLLLALSNKIADLIKISFRGSTVRNEGMKLTGLHILNFVLKNYSTMRDPQVPGSSILEQQEAQITSALMPAFSKGSSPTVMSFAITVAAEVLASNIMPPDKLGRISQLLIDLLGNFKDPNSGIRIGEAIIVTPKAKRKIELAVLDAWAEVVQRSITSSNDALFSFTRKYWSILVPLWIISLREYMMIKYNDNDSTVQVKNDSKENSLIEPRSTKIELYEPVWLNFVEALGCTLDSDVQVILASLNDEELEYFLFILFSQCLEAIVKNIDDHSVKMQVLPALHNVLKSNLCIKSIFEDDIITEVVEIMDRLISTGDSKEEFLLVDIISDLIIGYSKCNATPETFLQDIDKLYELLRLLMTIISERLPFIKYNVLTSEEDDNEIKISPTDISLLKKTFIAFESNISNFDNMFKVDLYSCLLFIIGKIYECSHREVIIPIILPLFKALVKALTESEDEKNIVLLEIFYGSIKDVIYHKLDSKNKVATILILLSNGYSKLSFQELNQCANILSEALNNPATQPIALQGFKRIISNIFKYPLLQYFMKLVIKRFFQDIQTNDSLSQASIKTKLIIQFSEEVIKQDHQKASLSIALCLSFFAAYHSAYTEKIDNEVASGIVALAKLDKNSFKEAISSTISPQQKAIIGSVMEAYVKSQSLGSVEEAFQLKSFD
Protein: 11S globulin seed storage protein 2 (11S globulin Ses i 6) (11S globulin seed storage protein II) (Allergen Ses i 6) (Alpha-globulin) (allergen Ses i 6.0101) [Cleaved into: 11S globulin seed storage protein 2 acidic chain (11S globulin seed storage protein II acidic chain); 11S globulin seed storage protein 2 basic chain (11S globulin seed storage protein II basic chain)] (Q9XHP0)
Organism: Sesamum indicum (Oriental sesame) (Sesamum orientale)
Function: Seed storage protein.
Interaction partners:
Sequence:
MVAFKFLLALSLSLLVSAAIAQTREPRLTQGQQCRFQRISGAQPSLRIQSEGGTTELWDERQEQFQCAGIVAMRSTIRPNGLSLPNYHPSPRLVYIERGQGLISIMVPGCAETYQVHRSQRTMERTEASEQQDRGSVRDLHQKVHRLRQGDIVAIPSGAAHWCYNDGSEDLVAVSINDVNHLSNQLDQKFRAFYLAGGVPRSGEQEQQARQTFHNIFRAFDAELLSEAFNVPQETIRRMQSEEEERGLIVMARERMTFVRPDEEEGEQEHRGRQLDNGLEETFCTMKFRTNVESRREADIFSRQAGRVHVVDRNKLPILKYMDLSAEKGNLYSNALVSPDWSMTGHTIVYVTRGDAQVQVVDHNGQALMNDRVNQGEMFVVPQYYTSTARAGNNGFEWVAFKTTGSPMRSPLAGYTSVIRAMPLQVITNSYQISPNQAQALKMNRGSQSFLLSPGGRRS
Protein: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 (E-NPP 3) (NPP3) (Alkaline phosphodiesterase I) (EC 3.1.4.1) (Dinucleoside polyphosphatase) (EC 3.6.1.-) (Nucleotide diphosphatase) (Nucleotide pyrophosphatase) (NPPase) (EC 3.6.1.9) (Phosphodiesterase I beta) (PD-Ibeta) (Phosphodiesterase I/nucleotide pyrophosphatase 3) (CD antigen CD203c) (O14638)
Organism: Homo sapiens (Human)
Function: Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP. Limits mast cell and basophil responses during inflammation and during the chronic phases of allergic responses by eliminating the extracellular ATP that functions as signaling molecule and activates basophils and mast cells and induces the release of inflammatory cytokines. Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic cells (By similarity). Has also alkaline phosphodiesterase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11342463, ECO:0000269|PubMed:12846830}; Single-pass type II membrane protein {ECO:0000305|PubMed:29717535}. Apical cell membrane {ECO:0000269|PubMed:15072822}; Single-pass type II membrane protein {ECO:0000305|PubMed:29717535}. Secreted {ECO:0000269|PubMed:15072822}. Note=Detected at the cell surface of basophils (PubMed:11342463). Detected at the apical plasma membrane of bile duct cells (PubMed:15072822). Located to the apical surface in intestinal and kidney epithelial cells. Secreted in serum, and in lumen of epithelial cells. {ECO:0000269|PubMed:11342463, ECO:0000269|PubMed:15072822}.
Interaction partners:
- Ectonucleoside triphosphate diphosphohydrolase 3
- Ectonucleoside triphosphate diphosphohydrolase 8
- Nucleoside diphosphate phosphatase ENTPD5
- Ectonucleoside triphosphate diphosphohydrolase 1
- cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
- Ectonucleoside triphosphate diphosphohydrolase 6
- Cytosolic 5'-nucleotidase 3A
- 5'-nucleotidase
- Guanylyl cyclase C
Sequence:
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFDASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCLQRKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTLMPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLSSKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERISTLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRNLHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNSEEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGGGNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLNHLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEITATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPTVPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEEFRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHYFVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVRDVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
Protein: At2g31490 (Expressed protein) (Neuronal acetylcholine receptor subunit alpha-5) (Uncharacterized protein At2g31490) (Q9SIQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 8
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 beta subcomplex subunit 10-B
- Gamma carbonic anhydrase-like 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- NADH dehydrogenase 1 beta subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 3-A
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- Transmembrane protein
- Gamma carbonic anhydrase 2, mitochondrial
Sequence:
MGGGMETNKNKFIEDWGSARENLEHNFRWTRRNFALIGIFGIALPIIVYKGIVKDFHMQDEDAGRPHRKFL
Protein: Serine protease inhibitor Kazal-type 13 (Hepatitis B virus DNA polymerase transactivated serine protease inhibitor) (Hespintor) (Serine protease inhibitor Kazal-type 5-like 3) (Q1W4C9)
Organism: Homo sapiens (Human)
Function: May be a serine protease inhibitor (By similarity). Essential for sperm maturation and fertility. Inhibits sperm acrosome reaction, protecting sperm from premature reaction (By similarity).
Subcellular location: Secreted {ECO:0000250}. Note=Secreted into the lumen of the initial segment of the epididymis and binds to sperm. In the initial segment of epididymis, localizes on the dorsal surface of the acrosomal region of sperm, gradually becomes more restricted to the acrosomal region in spermatozoa during epididymal transit (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MAAFPHKIIFFLVCSTLTHVAFSGIFNKRDFTRWPKPRCKMYIPLDPDYNADCPNVTAPVCASNGHTFQNECFFCVEQREFHYRIKFEKYGKCD
Protein: DNA-directed RNA polymerase subunit Rpo7 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit E) (B8YB57)
Organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (Probable). The highly mobile Rpo4/Rpo7 heterodimer is conditionally required for transcription initiation (Probable).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00865}.
Interaction partners:
Sequence:
MYKLIKARSIVRIPPNEFGKPLNEIALNELRQQYQEKILKDLGLVLAILNVKTSEEGMLVFGDGATYHEVEFDMITYVPVVQEVVEGEVLQVDNYGVFVNLGPMDGLVHISQITDDTLKYDNVRGIIFGEKSKKVIQKGDKVRARVISVASTVTGRLPRIALTMRQPYLGKLEWITQAKK
Protein: Bnm1 like protein (Plant invertase/pectin methylesterase inhibitor superfamily protein) (Q9SB59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Invertase/pectin methylesterase inhibitor family protein
- Beta-D-glucan exohydrolase-like protein
- At5g46950
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- AT3g16670/MGL6_12
- At4g00080
- Uncharacterized protein
- Exocyst subunit Exo70 family protein
Sequence:
MATSSVLSTFAAAAITLQLLLSPASASPHMKYIDAICDRSHDQAFCVKTLTTNPPTAAPIGLLPLSEAVINLAISHAEKTAIFVDETAKKDPTVKVAFTECHKAYLAVAADLKSANVKLKASPDTANYDVRASSDSMRRVNELVGKNTDKASTTLKEMTVQMEKLLDLAAGAADAVDDDDENMRLRV
Protein: 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component beta chain) (BCKDE1B) (BCKDH E1-beta) (P35738)
Organism: Rattus norvegicus (Rat)
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P21953}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyl dehydrogenase, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Branched-chain-amino-acid aminotransferase, cytosolic
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Ac1164
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Sequence:
MAAVAARAGGLLRLGAAGAERRRRGLRCAALVQGFLQPAVDDASQKRRVAHFTFQPDPESLQYGQTQKMNLFQSITSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVFNTPLCEQGIVGFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSLTIRAPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQAKGLLLSCIEDKNPCIFFEPKILYRAAVEQVPVEPYKIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASMAQEKLGVSCEVIDLRTIVPWDVDTVCKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRVCGYDTPFPHIFEPFYIPDKWKCYDALRKMINY
Protein: TNF receptor associated factor 2 (B1AMX8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAASVTPPGSLELLQPGFSKTLLGTKLEAKYLCSACRNVLRRPFQAQCGHRYCSFCLASILSSGPQNCAACVHEGIYEEGISILESSSAFPDNAARREVESLPAVCPSDGCTWKGTLKEYESCHEGRCPLMLTECPACKGLVRLGEKERHLEHECPERSLSCRHCRAPCCGADVKAHHEVCPKFPLTCDGCG
Protein: Histone chaperone ASF1B (Anti-silencing function protein 1 homolog B) (CCG1-interacting factor A-II) (CIA-II) (mCIA-II) (Q9DAP7)
Organism: Mus musculus (Mouse)
Function: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly (By similarity). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' (H3K9me1) and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5ac and H4K12ac) marks in the cytosol (By similarity). Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA (By similarity). Required for gonad development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NVP2}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NVP2}.
Interaction partners:
- Nuclear autoantigenic sperm protein
- Chromatin assembly factor 1 subunit B
- DNA replication licensing factor MCM2
- Protein HIRA
- Importin-4
- Chromatin assembly factor 1 subunit A
- Histone acetyltransferase type B catalytic subunit
- Cell division control protein 45 homolog
- Histone H3.2
- Histone H3.3
Sequence:
MAKVSVLNVAVLENPSPFHSPFRFEISFECSEALSDDLEWKIIYVGSAESEEFDQILDSVLVGPVPAGRHMFVFQADAPNPSLIPETDAVGVTVVLITCTYHGQEFIRVGYYVNNEYPDPELRENPPPKPDFSQLQRNILASNPRVTRFHINWDNNPDSLEAIENQDPNVDFSLSLSCTPVKSLGLPSCIPGLLPENSMDCI
Protein: Keratin-associated protein 5-10 (Keratin-associated protein 5.10) (Ultrahigh sulfur keratin-associated protein 5.10) (Q6L8G5)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 5-7
Sequence:
MGCCGCSGGCGSGCGGCGSGCGGCGSGCGGYGSGCGGCGSSCCVPVCCCKPVCCCVPACSCSSCGSCGGSKGDCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGCSQCNCCKPCCCSSGCGSCCQSSCCNPCCCQSSCCVPVCCQSSCCKPCCCQSSCCVPVCCQCKI
Protein: Ribonuclease 1 (EC 4.6.1.19) (P42813)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May remobilize phosphate, particularly when cells senesce or when phosphate becomes limiting.
Interaction partners:
- SPX domain-containing protein 1
- Protein PHOSPHATE STARVATION RESPONSE 1
- Inositol-3-phosphate synthase isozyme 1
- Inorganic phosphate transporter 1-4
- Inorganic phosphate transporter 1-1
- SPX domain-containing protein 3
- AT2G24420 protein
- Phosphate transporter PHO1
- Protein PHR1-LIKE 1
Sequence:
MKILLASLCLISLLVILPSVFSASSSSEDFDFFYFVQQWPGSYCDTQKKCCYPNSGKPAADFGIHGLWPNYKDGTYPSNCDASKPFDSSTISDLLTSMKKSWPTLACPSGSGEAFWEHEWEKHGTCSESVIDQHEYFQTALNLKQKTNLLGALTKAGINPDGKSYSLESIRDSIKESIGFTPWVECNRDGSGNSQLYQVYLCVDRSGSGLIECPVFPHGKCGAEIEFPSF