wanglab/gogpt-training-data huggingface dataset:
Protein: Tryptophan--tRNA ligase, mitochondrial (EC 6.1.1.2) ((Mt)TrpRS) (Tryptophanyl-tRNA synthetase) (TrpRS) (Q9UGM6)
Organism: Homo sapiens (Human)
Function: Mitochondrial aminoacyl-tRNA synthetase that activate and transfer the amino acids to their corresponding tRNAs during the translation of mitochondrial genes and protein synthesis.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:28236339}. Mitochondrion {ECO:0000269|PubMed:10828066}.
Interaction partners:
- Tryptophan--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, mitochondrial
- Valine--tRNA ligase, mitochondrial
- Valine--tRNA ligase
- Probable proline--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Alanine--tRNA ligase, cytoplasmic
Sequence:
MALHSMRKARERWSFIRALHKGSAAAPALQKDSKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGFL
Protein: Metaxin-3 (Q5HYI7)
Organism: Homo sapiens (Human)
Function: Could function in transport of proteins into the mitochondrion.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:26477565}. Mitochondrion outer membrane {ECO:0000305}.
Interaction partners:
- Sorting and assembly machinery component 50 homolog
- Metaxin-2
- Mitochondrial import receptor subunit TOM40 homolog
- Mitochondrial import receptor subunit TOM22 homolog
- MICOS complex subunit MIC19
- Mitochondrial import receptor subunit TOM40B
- MICOS complex subunit MIC27
- Mitochondrial import receptor subunit TOM7 homolog
- DnaJ homolog subfamily C member 11
- MICOS complex subunit MIC25
Sequence:
MAAPLELSCWGGGWGLPSVHSESLVVMAYAKFSGAPLKVNVIDNTWRGSRGDVPILTTEDDMVSQPAKILNFLRKQKYNADYELSAKQGADTLAYIALLEEKLLPAVLHTFWVESDNYFTVTKPWFASQIPFPLSLILPGRMSKGALNRILLTRGQPPLYHLREVEAQIYRDAKECLNLLSNRLGTSQFFFGDTPSTLDAYVFGFLAPLYKVRFPKVQLQEHLKQLSNLCRFCDDILSSYFRLSLGGISPAGQETVDANLQKLTQLVNKESNLIEKMDDNLRQSPQLPPRKLPTLKLTPAEEENNSFQRLSP
Protein: Merozoite surface protein 7 (Q8IDX8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKSNIIFYFSFFFVYLYYVSCNQSTHSTPVNNEEDQEELYIKNKKLEKLKNIVSGDFVGNYKNNEELLNKKIEELQNSKEKNVHVLINGNSIIDEIEKNEENDDNEENNDDDNTYELDMNDDTFLGQNNDSHFENVDDDAVENEQEDENKEKSESFPLFQNLGLFGKNVLSKVKAQSETDTQSKNEQEISTQGQEVQKPAQGGESTFQKDLDKKLYNLGDVFNHVVDISNKKNKINLDEYGKKYTDFKKEYEDFVLNSKEYDIIKNLIIMFGQEDNKSKNGKTDIVSEAKHMTEIFIKLFKDKEYHEQFKNYIYGVYSYAKQNSHLSEKKIKPEEEYKKFLEYSFNLLNTM
Protein: LD07278p (Q9W4G1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Mitosis initiation protein fs
- CG5272 protein
- Chorion peroxidase
- Deubiquitinase otu
- Maternal effect protein oskar
- Female sterile
- Tubulin alpha-4 chain
- LD24340p
- EG:8D8.1 protein
- Protein swallow
Sequence:
MEWSLIISILLNCLYASASALDEDCPTLDDGDSLSQTQLLDRLTHGCRYDRLERPITYSETGQRLPVDVYMRAYIYFMQNLEAHDLQFKIYALLQMRYLDPRLNFRNVSPKRRQPILGEEHLRNSLWMPHIFLANERDSSILGLTEKDILTSISPDGTVIVSNRIKATLYCWLNLKKFPFDEQHCSTVLESWMYNTSELVLHWEQKRPITYDGALHLTEFVLQRSWSNETVINADLSDLRHGAFAGNYSSLSFTVHLTRVVGFYLMDYFLPSMLIVAISWVSFWLQADQAPPRITLGTSTLLTFITLASAQGKTLPKVSYIKVSEVWFLGCTIFIFGSMVEFAFVNTIWRRKKSVPVKKLNSKHILKSTLSPNLLRRRSHARSRSFSGTALHKTADTGSLGGAGFNNYLTVNLPITTIKEGQVLDQQRTSRVVQKMDVNFVESAFGSMGSAQSTGAISAASSSQTLTNNNRTESAGHQEEIDLSGWTTLTPQEIAMWIDSRARFVFPLSFLVFNLFFWTFVYCI
Protein: Glycoprotein Ib platelet subunit alpha (D3ZQU7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- von Willebrand factor
- Glycoprotein 9
- Platelet glycoprotein Ib beta chain
- Prothrombin
- Filamin, alpha
- Platelet glycoprotein V
- P-selectin
- Tyrosine-protein kinase Lyn
- SCO-spondin
- 14-3-3 protein zeta/delta
Sequence:
MALLILLFLLPSPLHSQPTCDVSKVTSLLEVNCEDKKLKKLPTDLPADTGILHLSKNQLGTFSTSYLVHFTHLTHLYLSRCELTSLQAHEKLLKLETLDLSHNHLQSLPSLGRALPALTTLDVSFNKLGSLSPGALEGLGQLEELYLQNNDLKSLPPGLLMPTTKLLKLSLANNKLRELPPGLLDGLEDLDTLYLQGNWLSTIPKGFFGSLLLPFVFLHANTWYCDCEILYFRNWLQENPNRVYLWKEGVDVKAMTANVASVRCANLGNAPVYSYPGKGCPTNEGDIDYDDYADTPTTRTEVKFSTNTKAHTTYWGLFYSESSTSPDSQMTSLPPIHEPTKKQPTFAHTEIPGFTTLPDTMESNTAFYSLNNTVPTTTPEPTSTQATPEPSSTPMLTTPVPTPEPSSIPMLTVPVSTPEPSSTPMLTTPVSTPEPSSIPMPTIPVPTPEPSSIPMPTIPVPTPEPSSTPMPTIPVPTPEPSSTPMFTTPVPTPEPSSTPMLTTPTLTTPESSSTPSILVSTIPPVLTTTLAPPESIPKTVLEQFYTLEPTLPRTLESTIIIPEQNSLNSQAVPQASSDTPKSNPFLNSDFCCLLPLGFYVLGLLWLLFASVVLIVLLTWIWHVTPHNLDMDQSAALATSTHTTSLEMQRARQVTMPWAWLLSLQGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGHGQDLLGRVGIRYSGHSL
Protein: Hemocyanin subunit D (Q95P07)
Organism: Scutigera coleoptrata (House centipede)
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:12823556}.
Interaction partners:
Sequence:
MDTRVLRLTLALVALSGVLADSESCSSAIVNDYKLKQKEIQHLVDTINKPVYPDFKDTRGIIDESKLKGLGTLPRREVFSLFDERNWAEAAKVVELLLEPKTFREFIHLADIIHHRVNEDLFLYALSVAIAHRPDCQGVQVPRVLDIYPDKFLRKEVIHKIKEVSNEGAYLDKVPVIDATEVSDNHLDPNQELLYFLEDLGMNSHHHHWHVIHPAIWLPKHGGVKDRKGELFFYMHKQMVARYDTERLSNDLPRVRPFENWNDPIDEGYSPHLIIDKTGYKYAYRPQGVIVHDLPNLPKTKMFEWKNRIMVGIRKGSLISANKTQVPLNNDHGIDLLGDVVESSLLSVNRVFYGNLHCYAHVIAGKVTDPQSTYGEKNGAMYDVATSARDPLFYSWHKFIDNIFQEHKETLQPYNKDELNFPDVQVDSLRINVANGTYENIVRTYWQNSLFKIAKGFTFTTEGSVLVKVKHLNHETFYYNLEVTNNALEEKHGVVRIFGAVINDERGHPYILNDQRHLVIELDKFTVNLKPGKNSVRQPCYNSAVTAKYDVFYGDVESQKPQEGCNCGWPDYMLLPKGKYEGLRFRVFAIVTNHDEDKVSDQETCLCGDAVAYCGAHNQKYPDKKPMGFPFDRRIDERTFEHFHTPNMIATDVIIKFTGEFLPPKGDI
Protein: GRASP65 homolog protein 1 (Q04410)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the spindle assembly checkpoint. Involved in ER to Golgi vesicle-mediated transport by either facilitating USO1-dependent and -independent tethering or increasing target accuracy of fusion events of COPII-coated vesicles.
Subcellular location: Cytoplasm. Golgi apparatus, cis-Golgi network membrane; Peripheral membrane protein. Note=Localizes to cytoplasm in a punctate pattern. Association with the cis-Golgi requires N-terminal acetylation and is probably mediated via an N-terminal amphipathic helix. The localization to the Golgi is MAK3-dependent and SYS1-independent. Localizes to the Golgi together with BUG1.
Interaction partners:
- Binder of USO1 and GRH1 protein 1
- Intracellular protein transport protein USO1
- GTP-binding protein YPT1
- Acyl-CoA-binding protein
- Protein transport protein SEC24
- Protein transport protein SEC23
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- GRIP domain-containing protein RUD3
- Integral membrane protein SED5
- SED5-binding protein 2
Sequence:
MFRIAKNLVRTFEQSVQDTLALSQDSSNLDAFFQSIPPNLLSAQLESPVDAVSEGVKHTNVNETLSGLRIVWVDEMQFQLQSFFDYIVGFNDDPVPVVSNQHGFSYPDYRRITSIFNEHCGRTLKVNIWSAKGGTFRDEYISIISKESDDLDDVSLNHDERRPSSGEAHQFQALGFKVQWTPLIASTFTYHILNVNIPDGPAQSAGLIPDEDYIIGCQDGLLATGGETLLQDIVRSRANYDLVLYVYNKVSDCVRPITVHIGPDGRLGCNVGYGFLHRIPTVKHCPQQAQQQGQDDNPVPVPVPVESETAFVPSAFTAPPVPTKKKSKNKKGTQPLAMDDYFNEGRDKSSTAAKSAESDILAPPPQKQSSSD
Protein: Chitin synthase B (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase B) (Class-III chitin synthase B) (Q00757)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19411617, ECO:0000269|PubMed:25955346, ECO:0000269|PubMed:29387789, ECO:0000269|PubMed:29608571}; Multi-pass membrane protein {ECO:0000255}. Cell tip {ECO:0000269|PubMed:19411617, ECO:0000269|PubMed:25955346, ECO:0000269|PubMed:29387789, ECO:0000269|PubMed:29608571, ECO:0000269|PubMed:31974757, ECO:0000269|PubMed:34537176, ECO:0000269|PubMed:37071151}. Cell septum {ECO:0000269|PubMed:19411617, ECO:0000269|PubMed:25955346}. Note=Mainly localizes at the tips of germ tubes, hyphal tips, and forming septa during hyphal growth (PubMed:19411617). Accumulates at the Spitzenkoerper near the hyphal tips (PubMed:29387789, PubMed:31974757). Localization to the hyphal tips depends on conventional kinesin kinA (PubMed:25955346, PubMed:31974757). Polarization occurs by indirect endocytic recycling, involving delivery/exocytosis to apices followed by internalization by the sub-apical endocytic collar of actin patches and subsequent trafficking to TGN cisternae, where it accumulates for about 1 min before being re-delivered to the apex by a RAB11/TRAPPII-dependent pathway (PubMed:29608571). Predominantly localizes at polarized growth sites and between vesicles and metulae, between metulae and phialides, and between phalides and conidia in asexual development (PubMed:19411617). {ECO:0000269|PubMed:19411617, ECO:0000269|PubMed:25955346, ECO:0000269|PubMed:29387789, ECO:0000269|PubMed:29608571, ECO:0000269|PubMed:31974757}.
Interaction partners:
- UDP-N-acetylglucosamine diphosphorylase
- rRNA-processing protein cgrA
- Chitin synthase export chaperone
Sequence:
MAYHGSGPQSPGEHTYDDGHQLRDLSHSNTSYEEEASHGLLSSQQSPFAGPFDDPHQQRGLTASPVQRPTSGYSLTESYAPDAAYHDPYSANQSVYSGHSENPAAAFGVPGRVASPYARSETSSTEAWRQRQAGAAGGGNGLRRYATRKVKLVQGSVLSVDYPVPSAIQNAIQAKYRNDLEGGSEEFTHMRYTAATCDPNEFTLHNGYNLRPAMYNRHTELLIAITYYNEDKTLTARTLHGVMQNIRDIVNLKKSEFWNKGGPAWQKIVVCLVFDGIDPCDKDTLDVLATVGIYQDGVMKRDVDGKETVAHIFEYTTQLSVTPNQQLIRPTDDGPSTLPPVQMMFCLKQKNSKKINSHRWLFNAFGRILNPEVCILLDAGTKPGPKSLLYLWEAFYNDKDLGGACGEIHAMLGKGWKKLLNPLVAAQNFEYKISNILDKPLESSFGYVSVLPGAFSAYRFRAIMGRPLEQYFHGDHTLSKQLGKKGIEGMNIFKKNMFLAEDRILCFELVAKAGSKWHLSYVKASKGETDVPEGAPEFISQRRRWLNGSFAAGIYSLMHFGRMYKSGHNIVRMFFLHLQMLYNWFSTFLTWFSLASYWLTTSVIMDLVGTPSSSNGYTAFPFGKTATPIINTLVKYIYLAFLLLQFILALGNRPKGSKLSYLASFVAFGIIQLYVVVDALYLVVRAFTGGAPMDFNTDDGIGAFLSSFFGSSGAGIIIIALAATFGLYFVASFMYLDPWHMFTSFPAYMAVQSSYINILNVYAFSNWHDVSWGTKGSDKADALPSAKTTGGKGEEAVIEEIDKPQADIDSQFEATVKRALTPYVPPEEKEEKSLDDSYKSFRTRLVTLWLFSNGLLAVCITSEGLDKFGFTNTSTERTSRFFQALLWSNAVVALIRFIGATWFLGKTGLLCCFARR
Protein: Probable transcriptional regulator (Q9I0P6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Putrescine/agmatine-binding protein
- HTH-type quorum-sensing regulator RhlR
- histidine kinase
Sequence:
MDIALHGGAWHESLGKLLEALDRPFFWRILAQTLGQFAPVDNWAALIFSDSSPLILSFMEEEREEVEPDPLISRYITGLYLQDPFYQVSRNCRRGGLFHLADIVSEDFETTEYYNTYFAHYVVTDEVQYNVPLDGERTLCLSLGSESRFGAEQIALFELLRPWVIALMKKRIHFEDAVREEAKPIAAAEVEVQPWRGLISPLTARESDVIRLMLDGYSNKEIADRLTLSIATIKVHRRHIYAKLNVKSHSEIFALLINPPAPRLADAR
Protein: Small ribosomal subunit protein mS26 (28S ribosomal protein S26, mitochondrial) (H6UQ70)
Organism: Gallus gallus (Chicken)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAPGGCPLLALLLLAGTAQGQHWSHGWYPGGKRDLSAPQAIPAWSPWLVPSRGRKSRYDPPAKSKASRLKVPPPVDPAELYVVTERYRQHRLVLSALRSIFRSEVVQRKREAQRDAEDSAALSEEHRLLMAWNDAENARQRARR
Protein: Phosphatidylinositol glycan anchor biosynthesis class T (RE52151p) (Q9W3G0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Putative GPI-anchor transamidase
- Glycosylphosphatidylinositol anchor attachment 1
- LD37974p
- Phosphatidylinositol glycan anchor biosynthesis class S
- GPI inositol-deacylase
- GPI ethanolamine phosphate transferase 3
- Phosphatidylinositol glycan anchor biosynthesis class F
- Prolyl 3-hydroxylase sudestada1
- GPI mannosyltransferase 1
- GPI mannosyltransferase 3
Sequence:
MYPVAFVLLLLVAPNADANLGRDDERFHEELVVRPLSGDHVNTYFQFTTRWHYGEKDNLYHTQLTPRVIAELLQQFAVKELHIGLTQGLWRYETWGYPIVEATSGAEMWAWFSGANLTNRDVDRQWKELANVFSGVLCASLNFVDNTNSIAPRHLIRPQFMPANGQRFVRYATLPREIVCTENLTPWKKLLPCGSASGFASLLNSGHVHNTKYHSLGLKVRVLCEDHDEDNCIVELTQTANLVYDLRLFELSNNDFSLRRLFGMGLNGYCELAESSKIYVQRNELGERYQLVPEPVHEVKTTRGGHSVVYSVYDMHEQFKEAGERLFNVAWLAPKSANRRRNLAKPSLPPVTVHRYLLGHGQERGRIVTEVTNSHYDALPIMLQEVIPWYVHAYLHTLSIRRKPQRVNEYGGQRLTFKLLHYTPGKQRELPSHLEIGFMLPGQTSALISIDVDYLLLKWLEYPPDANHGHYIGSAIVSSQLPMGRNYTALPPEGHLFEHSFNATRPSYVLSLHTEALIVSLPTPDFSMPYNVICLACTVVALAFGPIHSVATKMIIVGRQTSAPKNFVKKIFNQLFRRGKATDETAAEGEGLPAAGAAATGVASGRAAISPGSPSGDQPLLEDLDEEEEEEQD
Protein: Ent-kaurene synthase 1, chloroplastic (SrKS1) (EC 4.2.3.19) (Q9XEH9)
Organism: Stevia rebaudiana (Stevia) (Eupatorium rebaudianum)
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities, and in the production of gibberellins phytohormones. Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-kaurene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MNLSLCIASPLLTKSSRPTALSAIHTASTSHGGQTNPTNLIIDTTKERIQKLFKNVEISVSSYDTAWVAMVPSPNSPKSPCFPECLNWLINNQLNDGSWGLVNHTHNHNHPLLKDSLSSTLACIVALKRWNVGEDQINKGLSFIESNLASATDKSQPSPIGFDIIFPGLLEYAKNLDINLLSKQTDFSLMLHKRELEQKRCHSNEIDGYLAYISEGLGNLYDWNMVKKYQMKNGSVFNSPSATAAAFINHQNPGCLNYLNSLLDKFGNAVPTVYPLDLYIRLSMVDTIERLGISHHFRVEIKNVLDETYRCWVERDEQIFMDVVTCALAFRLLRIHGYKVSPDQLAEITNELAFKDEYAALETYHASQILYQEDLSSGKQILKSADFLKGILSTDSNRLSKLIHKEVENALKFPINTGLERINTRRNIQLYNVDNTRILKTTYHSSNISNTYYLRLAVEDFYTCQSIYREELKGLERWVVQNKLDQLKFARQKTAYCYFSVAATLSSPELSDARISWAKNGILTTVVDDFFDIGGTIDELTNLIQCVEKWNVDVDKDCCSEHVRILFLALKDAICWIGDEAFKWQARDVTSHVIQTWLELMNSMLREAIWTRDAYVPTLNEYMENAYVSFALGPIVKPAIYFVGPKLSEEIVESSEYHNLFKLMSTQGRLLNDIHSFKREFKEGKLNAVALHLSNGESGKVEEEVVEEMMMMIKNKRKELMKLIFEENGSIVPRACKDAFWNMCHVLNFFYANDDGFTGNTILDTVKDIIYNPLVLVNENEEQR
Protein: Paraflagellar rod component (Q389K9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSHYLLVTFTFNCPEIRILGPIKEQTIEKLNDVIPNATTTSRSNRTALPKFEYLPNPNHWYIKLDRQFCDEDGKSHLMVLLLDALSEEGSWRLVSSFVTKEPSGTGSKEGTETHTLFLNKLLAEDS
Protein: L-carnitine dehydrogenase (CDH) (L-CDH) (EC 1.1.1.108) (Q9HTH8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-dehydrocarnitine. Is specific for L-carnitine and NAD(+) as substrates. D,L-3-hydroxybutyrate, L-lactate, ethanol, L-malate and D,L-isocitrate are not substrates. Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02129}.
Interaction partners:
- Betainyl-CoA thioesterase
- 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase
- ABC-type glycine betaine transport system substrate-binding domain-containing protein
- Probable lipolytic enzyme
- Glutathione-independent formaldehyde dehydrogenase
- HTH-type transcriptional regulator CdhR
- 3-ketoacyl-CoA thiolase
Sequence:
MSFVTEIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLAPGAAQERLRFVASIEECVGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTAAEAVRAAMRVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGNAGMRHFMAQFGPALQLPWTYLPAPELTEALIDRVVEGTAEQQGARSIAELERYRDDCLLAVLGAIRETKARHGFAFAE
Protein: Protein CASPARIAN STRIP INTEGRITY FACTOR 1 (Q84MD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Peptide hormone required for contiguous Casparian strip diffusion barrier formation in roots via the regulation of CASPs protein expression and distribution in a GSO1-GSO2 signaling pathway. The Casparian strip is required for ion homeostasis (e.g. iron and potassium ions).
Interaction partners:
- Transmembrane protein
- At4g37295
- Precursor of CEP16
- PAMP-induced secreted peptide 2
- At2g23270
- F28L1.2 protein
- Precursor of CEP9
- Precursor of CEP12
Sequence:
MGMSPLTVKKLGFIFMIVSASALSVSFAGRPSIFVHKKINLREEMVERSMHEHERLLRMNTKDYGNNSPSPRLERPPFKLIPN
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 20 (ADAM-TS 20) (ADAM-TS20) (ADAMTS-20) (EC 3.4.24.-) (P59510)
Organism: Homo sapiens (Human)
Function: May play a role in tissue-remodeling process occurring in both normal and pathological conditions. May have a protease-independent function in the transport from the endoplasmic reticulum to the Golgi apparatus of secretory cargos, mediated by the GON domain.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
Sequence:
MWVAKWLTGLLYHLSLFITRSWEVDFHPRQEALVRTLTSYEVVIPERVNEFGEVFPQSHHFSRQKRSSEALEPMPFRTHYRFTAYGQLFQLNLTADASFLAAGYTEVHLGTPERGAWESDAGPSDLRHCFYRGQVNSQEDYKAVVSLCGGLTGTFKGQNGEYFLEPIMKADGNEYEDGHNKPHLIYRQDLNNSFLQTLKYCSVSESQIKETSLPFHTYSNMNEDLNVMKERVLGHTSKNVPLKDERRHSRKKRLISYPRYIEIMVTADAKVVSAHGSNLQNYILTLMSIVATIYKDPSIGNLIHIVVVKLVMIHREEEGPVINFDGATTLKNFCSWQQTQNDLDDVHPSHHDTAVLITREDICSSKEKCNMLGLSYLGTICDPLQSCFINEEKGLISAFTIAHELGHTLGVQHDDNPRCKEMKVTKYHVMAPALSFHMSPWSWSNCSRKYVTEFLDTGYGECLLDKPDEEIYNLPSELPGSRYDGNKQCELAFGPGSQMCPHINICMHLWCTSTEKLHKGCFTQHVPPADGTDCGPGMHCRHGLCVNKETETRPVNGEWGPWEPYSSCSRTCGGGIESATRRCNRPEPRNGGNYCVGRRMKFRSCNTDSCPKGTQDFREKQCSDFNGKHLDISGIPSNVRWLPRYSGIGTKDRCKLYCQVAGTNYFYLLKDMVEDGTPCGTETHDICVQGQCMAAGCDHVLNSSAKIDKCGVCGGDNSSCKTITGVFNSSHYGYNVVVKIPAGATNVDIRQYSYSGQPDDSYLALSDAEGNFLFNGNFLLSTSKKEINVQGTRTVIEYSGSNNAVERINSTNRQEKEILIEVLCVGNLYNPDVHYSFNIPLEERSDMFTWDPYGPWEGCTKMCQGLQRRNITCIHKSDHSVVSDKECDHLPLPSFVTQSCNTDCELRWHVIGKSECSSQCGQGYRTLDIHCMKYSIHEGQTVQVDDHYCGDQLKPPTQELCHGNCVFTRWHYSEWSQCSRSCGGGERSRESYCMNNFGHRLADNECQELSRVTRENCNEFSCPSWAASEWSECLVTCGKGTKQRQVWCQLNVDHLSDGFCNSSTKPESLSPCELHTCASWQVGPWGPCTTTCGHGYQMRDVKCVNELASAVLEDTECHEASRPSDRQSCVLTPCSFISKLETALLPTVLIKKMAQWRHGSWTPCSVSCGRGTQARYVSCRDALDRIADESYCAHLPRPAEIWDCFTPCGEWQAGDWSPCSASCGHGKTTRQVLCMNYHQPIDENYCDPEVRPLMEQECSLAACPPAHSHFPSSPVQPSYYLSTNLPLTQKLEDNENQVVHPSVRGNQWRTGPWGSCSSSCSGGLQHRAVVCQDENGQSASYCDAASKPPELQQCGPGPCPQWNYGNWGECSQTCGGGIKSRLVICQFPNGQILEDHNCEIVNKPPSVIQCHMHACPADVSWHQEPWTSCSASCGKGRKYREVFCIDQFQRKLEDTNCSQVQKPPTHKACRSVRCPSWKANSWNECSVTCGSGVQQRDVYCRLKGVGQVVEEMCDQSTRPCSQRRCWSQDCVQHKGMERGRLNCSTSCERKDSHQRMECTDNQIRQVNEIVYNSSTISLTSKNCRNPPCNYIVVTADSSQCANNCGFSYRQRITYCTEIPSTKKHKLHRLRPIVYQECPVVPSSQVYQCINSCLHLATWKVGKWSKCSVTCGIGIMKRQVKCITKHGLSSDLCLNHLKPGAQKKCYANDCKSFTTCKEIQVKNHIRKDGDYYLNIKGRIIKIYCADMYLENPKEYLTLVQGEENFSEVYGFRLKNPYQCPFNGSRREDCECDNGHLAAGYTVFSKIRIDLTSMQIKTTDLLFSKTIFGNAVPFATAGDCYSAFRCPQGQFSINLSGTGMKISSTAKWLTQGSYTSVSIRRSEDGTRFFGKCGGYCGKCLPHMTTGLPIQVI
Protein: Active breakpoint cluster region-related protein (Q12979)
Organism: Homo sapiens (Human)
Function: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form. The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form. Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF-1 directed motility and phagocytosis through the modulation of RAC1 activity (By similarity).
Subcellular location: Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q5SSL4}. Cell projection, axon {ECO:0000250|UniProtKB:Q5SSL4}. Synapse {ECO:0000250|UniProtKB:A0A0G2JTR4}.
Interaction partners:
- Transforming protein RhoA
Sequence:
MEPLSHRGLPRLSWIDTLYSNFSYGTDEYDGEGNEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGDGVSPTPPEGLAPGVEAGKGLEMRKLVLSGFLASEEIYINQLEALLLPMKPLKATATTSQPVLTIQQIETIFYKIQDIYEIHKEFYDNLCPKVQQWDSQVTMGHLFQKLASQLGVYKAFVDNYKVALETAEKCSQSNNQFQKISEELKVKGPKDSKDSHTSVTMEALLYKPIDRVTRSTLVLHDLLKHTPVDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEVSESSRKLRHVFLFTDVLLCAKLKKTSAGKHQQYDCKWYIPLADLVFPSPEESEASPQVHPFPDHELEDMKMKISALKSEIQKEKANKGQSRAIERLKKKMFENEFLLLLNSPTIPFRIHNRNGKSYLFLLSSDYERSEWREAIQKLQKKDLQAFVLSSVELQVLTGSCFKLRTVHNIPVTSNKDDDESPGLYGFLHVIVHSAKGFKQSANLYCTLEVDSFGYFVSKAKTRVFRDTAEPKWDEEFEIELEGSQSLRILCYEKCYDKTKVNKDNNEIVDKIMGKGQIQLDPQTVETKNWHTDVIEMNGIKVEFSMKFTSRDMSLKRTPSKKQTGVFGVKISVVTKRERSKVPYIVRQCVEEVEKRGIEEVGIYRISGVATDIQALKAVFDANNKDILLMLSDMDINAIAGTLKLYFRELPEPLLTDRLYPAFMEGIALSDPAAKENCMMHLLRSLPDPNLITFLFLLEHLKRVAEKEPINKMSLHNLATVFGPTLLRPSEVESKAHLTSAADIWSHDVMAQVQVLLYYLQHPPISFAELKRNTLYFSTDV
Protein: Glutamate--tRNA ligase, mitochondrial (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS) (P48525)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Methionine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- tRNA-aminoacylation cofactor ARC1
- Isoleucine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, mitochondrial
- Probable proline--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, cytoplasmic
- Asparagine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
Sequence:
MIMLRIPTRSYCSPSKLIKGVGLSPLKKSLLSKKIKEDIHPSLPVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLIYDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSMASYDRCCAHLGEEEIKSKLAQGIPFTVRFKSPERYPTFTDLLHGQINLQPQVNFNDKRYDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIPLLTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDLASKKHECFSMEELETIFNLNGLTKGNAKVDDKKLWFFNKHFLQKRILNPSTLRELVDDIMPSLESIYNTSTISREKVAKILLNCGGSLSRINDFHDEFYYFFEKPKYNDNDAVTKFLSKNESRHIAHLLKKLGQFQEGTDAQEVESMVETMYYENGFSRKVTYQAMRFALAGCHPGAKIAAMIDILGIKESNKRLSEGLQFLQREKK
Protein: Heat shock protein homolog SSE1 (Q6FJI3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Nucleoporin NSP1
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Hsp70 nucleotide exchange factor FES1
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- CCT-theta
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
Sequence:
MSTPFGLDFGNDNSVLAVARNRGIDIVVNEVSNRSTPSMVGFGQKNRFLGESAKTKQTSNIKNTVGNLKRILGLDYDHPDFQEESKFFTSKLVKLEDGKIGTQVRFAGESTTFSATQLNAMFINKVKQTVETETKANITDVCIAVPTWYTEEQRYAAADAARIAGLNPVRIVNDITAAGVSYGVFKTDLPEGEEKPRIVAFIDIGHSSYTCSIMAFKKGELKVLGTAWDKNFGGRNFDRAITEHFADEFKTKYKIDIRENPKAYNRVMTSAERLKKVLSANTAAPFSVENVMNDVDASSQLSREELEELVKPMLERVTEPVTKALAQAGLTKDDVDFVEIIGGTTRIPTLKNSISEAFGKPLSTTLNQDEAIAKGAAFICAIHSPTLRVRPFKFEDIHQFSVSYKWDKQVEDEDHLEVFPANSNFPSTKLITLHRSGDFSMEANYTNKEELPPHLDANIAKWDITGVQIPEGETSVPVKLKLRCDPSGLHIIEEAYSLEDIVVKEEVPLPEDAPEDAVPEVKEVTKTVKKDTLEITAHTFTLADDKLNTLIEKENDMTAQDRLVAETEDRKNNLEEYIYTLRGKLDEEYSDFASDAEKTKLKDMLAKAEEWLYEDGFDTIKAKYIAKYEELAAIGNVIRGRYLAKEEEKKQALRAKQEAANLAALSEKLAAQRSADSEAKKDATPEGDAQMDLD
Protein: NAC transcription factor 47 (NAC domain-containing protein 47) (ANAC047) (Protein SPEEDY HYPONASTIC GROWTH) (Q84TD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds to the promoter of ACO5, an ACC oxidase involved in ethylene biosynthesis. Mediates waterlogging-induced hyponastic leaf movement, and cell expansion in abaxial cells of the basal petiole region, by directly regulating the expression of ACO5. Required for normal seed development and morphology.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:24363315}.
Interaction partners:
Sequence:
MISKDPRSSLPPGFRFHPTDEELILHYLRKKVSSSPVPLSIIADVDIYKSDPWDLPAKAPFGEKEWYFFSPRDRKYPNGARPNRAAASGYWKATGTDKLIAVPNGEGFHENIGIKKALVFYRGKPPKGVKTNWIMHEYRLADSLSPKRINSSRSGGSEVNNNFGDRNSKEYSMRLDDWVLCRIYKKSHASLSSPDVALVTSNQEHEENDNEPFVDRGTFLPNLQNDQPLKRQKSSCSFSNLLDATDLTFLANFLNETPENRSESDFSFMIGNFSNPDIYGNHYLDQKLPQLSSPTSETSGIGSKRERVDFAEETINASKKMMNTYSYNNSIDQMDHSMMQQPSFLNQELMMSSHLQYQG