wanglab/gogpt-training-data huggingface dataset:
Protein: Female gametocyte surface protein P47 (Q8IDN0)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Mediates evasion of the mosquito innate immune response by suppressing midgut nitration responses that are critical to activate the mosquito complement system. It is unclear whether the protein has a role in passive evasion by making the parasite invisible to the mosquito immune system, acts as a decoy to prevent recognition of another surface protein or anchors the decoy protein. Not required for female fertility.
Subcellular location: Cell surface {ECO:0000269|PubMed:16824624}. Cell membrane {ECO:0000305|PubMed:16824624}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:16824624}. Note=Specifically present on the surface of female gametocytes. {ECO:0000269|PubMed:16824624}.
Interaction partners:
- Gametocyte surface protein P230
Sequence:
MCMGRMISIINIILFYFFLWVKKSISELLSSTQYVCDFYFNPLTNVKPTVVGSSEIYEEVGCTINNPTLGDHIVLICPKKNNGDFSNIEIVPTNCFESHLYSAYKNDSSAYHLEKLDIDKKYAINSSFSDFYLKILVIPNEYKSHKTIYCRCDNSKTEKNIPGQDKILKGKLGLVKIILRNQYNNIIELEKTKPIIHNKKDTYKYDIKLKESDILMFYMKEETIVESGNCEEILNTKINLLSNNNVVIKMPSIFINNINCMLSSQDQNNEKNYINLKADKTKHIDGCDFTKPKGKGIYKNGFIINDIPNEEERICTVHLWNKKNQTIAGIKCPYKLIPPYCFKHVLYEKEIDSQKTYKTFLLSDVLDTPNIEYYGNNKEGMYMLALPTKPEKTNKIRCICEQGGKKAVMELHIASTSTKYISMFLIFFLIVIFYMYVSI
Protein: phosphatidylinositol-4,5-bisphosphate 3-kinase (EC 2.7.1.153) (Q6NTI2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEQQASDDEPPVVRREENKRRRRRMKAFTSASAVSMEHIAVEFVLPTTNKNSKTLDTLQLDVTGNWTVEQVKVQLWHRAVTSKLCPEFYQKYSPDYCILLYQKKGNWYEIYDKQQVFQTLDCIRYWKALRKDVGKIHLVVRQQPAEDSLQYQRFLNHLIGYDVTDVSNVHDDELEFTRRKLLTPRKIELSDRDPNLYSMDPWMTTTPMPEYLLSKISNNHILMVIHKETTSQTIKVSIDDTPVQVLQSFFAKITNKRALLGISEDVSESDFVLRVCGREEYLYGNNAIKDFHWIRQCLKNGEEIHLVLEHPPNPEQDVVQKEDWSQVDDCTGVAGTHEQLTITEKDHEKVFTISLWDCNRKFRVKILGIDIPVLPRNSELIVFVEASIFHGQQLLAQERTSSKPFTEEVIWNTWLEFNIKIKDLPKGARLSLQVSCGKAQTQTSKETECKNKSRLLYYVNLLLVDHRSLLRQGEFILHMWKMPEKSEDNSSVNADKLTSATNPDKNNSMAVAILLDKYCYPVALPKSKDSPDIEGERGQREMPNHLRKQFEQIIATDPLHPLTSEDKELLWHFRQECMRDPKAYPKFLSSVKWGKQEAVAITHHLLERSTIWDRSVLDVGLVLQLLDCHFSDENVRTIAVRKLETLGDDDVLRYLLQLVQAVKFEPYHDSALARFLLKRALRSKRIGHFLFWFLRSEIAQSMHYQQRYAVILEAYLRGCGEEMLQDFRKQVEITEALQKVAREIKQISAEKYDISAQVVFQLRQKLEGLQVLGLPDSFKVPYDPGLRAGALVIEQCKVMASKKKPLWLQFKRADPTTLSSDTIGIIFKDGDDLRQDMLILQILLIMESIWELESLDLSLLPYGCISTGNKIGMIEIVKDATTIANIQQSTVGNTGAFKDEILSQWLREKCVNEDKHQQAVDRFVFSCGGYCVATYVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGISKERVPFVLTPDFLYLMGTTGKKSSPNFLQFQNVCLKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIREALTVGRSEDEAKQHFLDQIEICRDKGWTVQFNWFLHLVLGIKQGVEKRSA
Protein: Arpin (Arp2/3 inhibition protein) (Q9D0A3)
Organism: Mus musculus (Mouse)
Function: Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence (By similarity).
Subcellular location: Cell projection, lamellipodium {ECO:0000269|PubMed:24132237}. Note=Colocalized with the WAVE complex at lamellipodium tip.
Interaction partners:
- AP-3 complex subunit sigma-2
- AP-3 complex subunit delta-1
Sequence:
MSRIYQDSALRNKAVQSARLPGTWDPATHQGGNGILLEGELVDVSRHSILDAHGRKERYYVLYIQPSCIHRRKFDPKGNEIEPNFSATRKVNTGFLMSSYKVEAKGDTDRLTLEALKSLVNKPQLLELTESLTPDQAVAFWMPESEMEVMELELGTGVRLKTRGDGPFIDSLAKLELGTVTKCNFAGDGKTGASWTDNIMAQKSSERNTAEIREQGDGAEDEEWDD
Protein: Testis-specific protein 10-interacting protein (Tsga10-interacting protein) (Q3SY00)
Organism: Homo sapiens (Human)
Interaction partners:
- Huntingtin-interacting protein K
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
Sequence:
MGQDTDMLNTYQQLVRTPSVRPGQDVRLQAPGTRTGLLKLLSTVSQDKQGCLGSGDGVPNQDLQQRSQSSRQTAKKDRKPRGQSKKGQGSEESEDHFPLLPRKPSFPFQWAWESIATDVRAVLQPSSPTPGHQALPMPSSFSQRQSRRKSTANLPEAHGCCWKTEAQNLKARQQLGAWGGVSIPTGKGELGSEPPSGLQLPGRRPGSGSASDKQVQLQSLGAEEAERGLSSGVLPQRPRRGSISEEEQFSEATEEAEEGEHRTPCRRRAGCQRKGQISGEEASDEGEVQGQSQGSSPSFNNLRRRQWRKTRAKELQGPWDLEKLHRQLQRDLDCGPQKLPWKTLRAAFQASKRNGKAYASGYDETFVSANLPNRTFHKRQEATRSLLQAWERQRQEERQQAELRRARTQHVQRQVAHCLAAYAPRGSRGPGAAQRKLEELRRQERQRFAEYQAELQGIQHRVQARPFLFQQAMQANARLTVTRRFSQVLSALGLDEEQLLSEAGKVDREGTPRKPRSHRSMGVRMEHSPQRPPRTEPTGSQPDRHYNPSLDPECSP
Protein: RNA-binding protein with serine-rich domain 1 (SR-related protein LDC2) (Q15287)
Organism: Homo sapiens (Human)
Function: Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54 and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions.
Subcellular location: Nucleus. Nucleus speckle. Cytoplasm. Note=Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.
Interaction partners:
- Serine/arginine repetitive matrix protein 1
- Regulator of nonsense transcripts 2
- Regulator of nonsense transcripts 3B
- Regulator of nonsense transcripts 1
- Histone deacetylase complex subunit SAP18
- Apoptotic chromatin condensation inducer in the nucleus
- Pinin
- RNA-binding protein 8A
- Regulator of nonsense transcripts 3A
- Eukaryotic initiation factor 4A-III
Sequence:
MDLSGVKKKSLLGVKENNKKSSTRAPSPTKRKDRSDEKSKDRSKDKGATKESSEKDRGRDKTRKRRSASSGSSSTRSRSSSTSSSGSSTSTGSSSGSSSSSASSRSGSSSTSRSSSSSSSSGSPSPSRRRHDNRRRSRSKSKPPKRDEKERKRRSPSPKPTKVHIGRLTRNVTKDHIMEIFSTYGKIKMIDMPVERMHPHLSKGYAYVEFENPDEAEKALKHMDGGQIDGQEITATAVLAPWPRPPPRRFSPPRRMLPPPPMWRRSPPRMRRRSRSPRRRSPVRRRSRSPGRRRHRSRSSSNSSR
Protein: Alpha-1A adrenergic receptor (Alpha-1A adrenoreceptor) (Alpha-1A adrenoceptor) (Alpha-1C adrenergic receptor) (P97718)
Organism: Mus musculus (Mouse)
Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity).
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:22120526}; Multi-pass membrane protein {ECO:0000269|PubMed:22120526}. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-13
- Alpha-1B adrenergic receptor
- Alpha-1D adrenergic receptor
- Guanine nucleotide-binding protein subunit alpha-11
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Guanine nucleotide-binding protein subunit alpha-14
- Guanine nucleotide-binding protein G
Sequence:
MVLLSENASEGSNCTHPPAQVNISKAILLGVILGGLIIFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGVRALLCVWALSLVISIGPLFGWRQQAPEDETICQINEEPGYVLFSALGSFYVPLTIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNVPAEGSGVSSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPNFKPPETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLRRRQSSKHALGYTLHPPSQAVEGQHRGMVRIPVGSGETFYKISKTDGVREWKFFSSMPQGSARITMPKDQSACTTARVRSKSFLQVCCCVGSSTPRPEENHQVPTIKIHTISLGENGEEV
Protein: Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform (IMYPNO1) (PP2A subunit B isoform B55-gamma) (PP2A subunit B isoform PR55-gamma) (PP2A subunit B isoform R2-gamma) (PP2A subunit B isoform gamma) (Q9Y2T4)
Organism: Homo sapiens (Human)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit alpha
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit delta
Sequence:
MGEDTDTRKINHSFLRDHSYVTEADIISTVEFNHTGELLATGDKGGRVVIFQREPESKNAPHSQGEYDVYSTFQSHEPEFDYLKSLEIEEKINKIKWLPQQNAAHSLLSTNDKTIKLWKITERDKRPEGYNLKDEEGKLKDLSTVTSLQVPVLKPMDLMVEVSPRRIFANGHTYHINSISVNSDCETYMSADDLRINLWHLAITDRSFNIVDIKPANMEDLTEVITASEFHPHHCNLFVYSSSKGSLRLCDMRAAALCDKHSKLFEEPEDPSNRSFFSEIISSVSDVKFSHSGRYMLTRDYLTVKVWDLNMEARPIETYQVHDYLRSKLCSLYENDCIFDKFECAWNGSDSVIMTGAYNNFFRMFDRNTKRDVTLEASRESSKPRAVLKPRRVCVGGKRRRDDISVDSLDFTKKILHTAWHPAENIIAIAATNNLYIFQDKVNSDMH
Protein: DNA repair protein SWI5 homolog (Protein SAE3 homolog) (Q8K3D3)
Organism: Mus musculus (Mouse)
Function: Component of the SWI5-SFR1 complex, a complex required for double-strand break repair via homologous recombination.
Subcellular location: Nucleus {ECO:0000269|PubMed:20976249}.
Interaction partners:
- Swi5-dependent recombination DNA repair protein 1 homolog
- Transmembrane protein 208
- DNA repair protein XRCC3
- DNA repair protein RAD51 homolog 2
- DNA repair protein RAD51 homolog 3
- DNA repair protein RAD51 homolog 4
- Meiotic recombination protein DMC1/LIM15 homolog
- DNA repair protein RAD51 homolog 1
- DNA repair protein XRCC2
- Meiotic nuclear division protein 1 homolog
Sequence:
MIDENNDVSEEALSSDIKKLKEKHDMLDKEISQLIAEGYRVIELEKHISLLHEYNDIKDVSQMLLGKLAVTRGVTTKELYPDFDLNLND
Protein: Protein wech (Protein dappled) (Q9V4M2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Vital for larval development. Plays a role in tumor formation. A crucial component for the physical link between integrins and the cytoskeleton in the epidermal muscle attachment sites.
Interaction partners:
- Integrin linked kinase, isoform A
- Ubiquitin-ribosomal protein eS31 fusion protein
- Rhea, isoform B
- GH17761p
- Polyubiquitin
- Ubiquitin-conjugating enzyme E2-17 kDa
Sequence:
MMELLSNNSVPQQMASSNAPSANNVAHSSTANGSGGGSVSSNASNSSERLLAGILESFPAWDLNVGLLPNVGQSSPPRADFFINNFLGGLDTHGDFSIGPIGSGARSNPKMSPESSNNSSISCGWCEVSASIRCLECNEFMCNDCLREHRNSPLSSNHSIVSLPTPIGASPTGGSSVNAQTPPSGNFICDIHNEMLRYVCDYCRKLVCQCCTLHEHKEHSYASIQSFMVGSKEKLEGAIESSQVGTRCIKSSIDKALAFIRLIERNCSELSDNIRKAFRQFIIAIEDRERFLLDFVEKLRQRRLAILHDQMAGLKSALAGLSETSDMLSKVADNACNMDQIEIAMKLTNGQRQMEQFAGIYKDLQPKQEVFAFAPPDYSLLQDIRNQGGVILVDDKNLPIVSSSNGIVPSVSSVNAVAAASVGVVGGVAGVVGGVGVSNGLDLAFGMNMPNNPLSVASSSVRRPLLRDNSFRIPSPIMQPRGGSACGMSSGMSSAALDWELNGLRSSPGLHFSAPRTTQAIPGCMDLVKVRNSNALSLSFATEGHEDGQVSRPWGLCVDKMGHVLVSDRRNNRVQVFNPDGSLKFKFGRKGVGNGEFDLPAGICVDVDNRIIVVDKDNHRVQIFTASGVFLLKFGSYGKEYGQFQYPWDVAVNSRRQIVVTDSRNHRIQQFDSEGRFIRQIVFDNHGQTKGIASPRGVCYTPTGNIIVSDFDNHCLYLIDPDINDILSVKGHEGSGFHEFNRPSGLCCDDEGRIIVADSKNQRILVFNQNLDFMWDIEVRPSINPLMPPTLDEKDRTCDVAIMPDGRIVFLIELSPDSKEGSNPYKRFVHVF
Protein: Carbonic anhydrase 4 (EC 4.2.1.1) (Carbonate dehydratase IV) (Carbonic anhydrase IV) (CA-IV) (Q64444)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible hydration of carbon dioxide into bicarbonate and protons and thus is essential to maintaining intracellular and extracellular pH. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P22748}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P22748}.
Interaction partners:
- Electrogenic sodium bicarbonate cotransporter 1
Sequence:
MQLLLALLALAYVAPSTEDSGWCYEIQTKDPRSSCLGPEKWPGACKENQQSPINIVTARTKVNPRLTPFILVGYDQKQQWPIKNNQHTVEMTLGGGACIIGGDLPARYEAVQLHLHWSNGNDNGSEHSIDGRHFAMEMHIVHKKLTSSKEDSKDKFAVLAFMIEVGDKVNKGFQPLVEALPSISKPHSTSTVRESSLQDMLPPSTKMYTYFRYNGSLTTPNCDETVIWTVYKQPIKIHKNQFLEFSKNLYYDEDQKLNMKDNVRPLQPLGKRQVFKSHAPGQLLSLPLPTLLVPTLTCLVANFLQ
Protein: Pantothenate transporter liz1 (O43000)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transports pantothenate into the cell.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15075270, ECO:0000269|PubMed:9950674}; Multi-pass membrane protein {ECO:0000269|PubMed:15075270, ECO:0000269|PubMed:9950674}.
Interaction partners:
Sequence:
MALLNRLAKTFSPYYGLNKVEQKLLIKIDWFILSYCCVSYFINYLDRSSINNAYLSGMQEDLKMHGNELQDINVVFTCGYIIGQLPGSYALQRVPARLWFSVMNILWGLMTIFSFAVHSVRALMILRFFMAVAEASTFAGTHYILGAWYKESELCKRAGIFSASGLVGTMFAGYLQTAVHSSLNGKGGLSGWRWLFIIDGILTIPLSLYGLFLFPDVPETTKAPYFTEQEKELSFKRLPARPKKKPLTLKAIKDIVRSWRIYGLCILWIFSGETQAIAVNVLMGQWMKWSNKFSVAQINNYPTVITAVGVVSTLGASVISDKLAGNPRWPFGLFLCVITTVSATILLAWNVPDGAKFFAYFASGCTYAGQAVWFSWANDICRDNDQERGVVVFLMNMCQNIWHIWWAPIMYPNTDTPRFIKGLIGLLVVGGIVFVSSCIVSYMQIRDKRIKRSIQDAKDFDDVFTEHESLELKKIGKNDEESLNTTNAVKEISSPGLVITRQRISMPKETNAQD
Protein: Lipoxygenase (EC 1.13.11.-) (Q96573)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Interaction partners:
Sequence:
MLKPQFQQSTKTLIPSWNTNTLFLASFPINILNKNFILKKKNNFRVHHNYNGANTIKAVLNSTQKSIGVKAVVTVQKQVNLNLLRGLDGIGDLLGKSLILWIVAAELDHKTGLEKPSIRSYAHRGLDVDGDTYYEADFEIPEDFGEVGAILVENEHHKEMYVKNIVIDGFVHAKVEITCNSWVHSKFANPDKRIFFTNKSYLPSQTPSGVIRLREGRTRTLRGDGVGERKVFERIYDYDVYNDLGEVVSNNDDAKRPILGGKKLPYPRRCRTGRQRSKKDPLYETRSTFVYVPRDEAFSAVKSLTFSGNTVYSALHAVVPALESVVSDPDLGFPHFPAIDSLFNVGVDLSGLSDKKSSLFNIVPRLIKSISETGKDVLLFESPQLVQRDKFSWFRDVEFARQTLAGLNPYSIRLVTEWPLRSNLDPKVSGPPESEITKELIENEIGNNMTVEQAVQQKKLFILDYHDLLLPYVNKVNELKGSVLYGSRTIFFLTPHGTLKPLAIELTRPPIDDKPQWKEVYSPNNWNATGAWLWKLAKAHVLSHDSGYHQLVSHWLRTHCCTEPYIIATNRQLSAMHPIYRLLHPHFRYTMEINALAREALINANGIIESSFFPGKYSVELSSIAYGAEWRFDQEALPQNLISRGLAEEDPNEPHGLKLAIEDYPFANDGLVLWDILKQWVTNYVNHYYPQTNLIESDKELQAWWSEIKNVGHGDKKDEPWWPELKTPNDLIGIITTIVWVTSGHHAAVNFGQYSYGGYFPNRPTTARSKMPTEDPTAEEWEWFLNKPEEALLRCFPSQIQATKVMTILDVLSNHSPDEEYIGEKIEPYWAEDPVINAAFEVFSGKLKELEGIIDARNNDSKLNNRNGAGVMPYELLKPYSEPGVTGKGVPYSISI
Protein: Dodeca-satellite-binding protein 1, isoform A (Dodeca-satellite-binding protein 1, isoform B) (Dodeca-satellite-binding protein 1, isoform D) (Dodeca-satellite-binding protein 1, isoform E) (Dodeca-satellite-binding protein 1, isoform F) (Dodeca-satellite-binding protein 1, isoform G) (Dodeca-satellite-binding protein 1, isoform H) (Q7KN75)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein RACK1
- Polyadenylate-binding protein
- Uncharacterized protein, isoform O
Sequence:
MQAAAVMEETNNATTIEQQPIALINGQEQVANEQQPSSPTSVATPTSTTSGGTGNATPAFSYDDLFPALPANTSAQSQSGASGSTLARVTSSQKTHIVHVPCKERKSTESEKFGEGESKRICQQITKETGAQIEIVSGKNQSLTFLIKGKQSELLDARRKILMGFSTQASRQVTVPREHFRVILGKGGQRLREIERVTATRINIPSQSDESEFITIAGTKEGIAQAEQEIRQLSAEQYKKSSDRITVPKVYHPFIVGPYSENLNKLQEETGARINVPPQQVQKDEIVISGEKDAVAAAKAKVEAIYKDMEKKCSTVSVEVAKPKHRYVIGPKGSTIAEILQLTGVSVEMPPNDSPSETITLRGPQVALGNALTVVYQKSNSVKSVEINAAHWIHKYVIGRKGANMKQLEEDCPNVNVNCLEDKIKLEGDPENVDRAVAYLSEIIKNYEENFTFEVMTVNPSYYKHIIGKAGANVNRLKDELKVNINIEEREGQNNIRIEGPKEGVRQAQLELQEKIDKLENEKSKDVIIDRRLHRSIIGAKGEKIREVKDRYRQVTITIPTPQENTDIVKLRGPKEDVDKCHKDLLKLVKEIQESSHIIEVPIFKQFHKFVIGKGGANIKKIRDETQTKIDLPAEGDTNEVIVITGKKENVLEAKERIQKIQNELSDIVTEEVQIPPKYYNSIIGTGGKLISSIMEECGGVSIKFPNSDSKSDKVTIRGPKDDVEKAKVQLLELANERQLASFTAEVRAKQQHHKFLIGKNGASIRKIRDATGARIIFPSNEDTDKEVITIIGKEESVKKAREQLEAIIKECDEVTEGEVSVDPKHHKHFVAKRGFILHRISEECGGVMISFPRVGINSDKVTIKGAKDCIEAARQRIEEIVADLEAQTTIEVVIPQRHHRTIMGARGFKVQQVTFEFDVQIKFPDRDATEPVEGLTNGGSGENGGENEGQEGEQEVEKEAEQEPVRQCDVIRITGRIEKCEAAKQALLDLIPIEEELSVPFDLHRTIIGPRGANVRQFMSKHDVHVELPPSELKSDVIKVCGTPARVAEAREALVKMIEDYEADRADRELRSFVLQVDVDTEFHSKLIGRHGAVINKLRADHDVIISLPKRDEPNDRIISITGYQANAEAARDAILEIVGDPETLHREVIEIDKRIHPHLIGQRRRTIRKIIEDNKVNIKFSADDDNPNSIFISGKIEDVENVKELLFGMAEDYERDYLDNVAIAPPTIGAFLTGQGSGSDAAGASENGFVIKDAPWEKQKQAKNLTAPNTQSQEDFPHFAAGGAPVASTPITSVWGPKN
Protein: Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (CAD ATPase) (Katanin-1) (AtKTN1) (Katanin-like microtubule-severing protein) (AtKSS) (Protein BOTERO 1) (Protein ECTOPIC ROOT HAIR 3) (Protein FAT ROOT) (Protein FRAGILE FIBER 2) (AtAAA1) (p60 katanin) (Atp60) (Q9SEX2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Severs microtubules in vitro in an ATP-dependent manner. Required for oligomerization of functional KTN80-KTN1 complexes that catalyze microtubule severing. This activity may promote rapid reorganization of cellular microtubule arrays. May be required for reorientation of cortical microtubule arrays during cellular elongation. Failure to correctly orient these arrays drastically compromises fiber length, cell wall thickness and mechanical strength. May also be required for the spatial organization of developmental cues within the root.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:12571277, ECO:0000269|PubMed:28978669}. Note=Present in dynamic discrete particles specifically localized to microtubule (MT) crossovers and branching nucleation sites, in a KTN80s-dependent manner. {ECO:0000269|PubMed:28978669}.
Interaction partners:
- Peroxidase 60
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.4
- Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.2
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
- 26S proteasome regulatory subunit RPN13
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
Sequence:
MVGSSNSLAGLQDHLKLAREYALEGSYDTSVIFFDGAIAQINKHLNTLDDPLARTKWMNVKKAIMEETEVVKQLDAERRAFKEAPTGRRAASPPINTKSSFVFQPLDEYPTSSGGGPMDDPDVWRPPTRDVTSRRPARAGQTGTRKSPQDGAWARGPTTRTGPASRGGRGGATSKSTAGARSSTAGKKGAASKSNKAESMNGDAEDGKSKRGLYEGPDEDLAAMLERDVLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSNTATNEDGSRKIVMVLAATNFPWDIDEALRRRLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASMNGMRRKIAGKTRDEIKNMSKDDISNDPVAMCDFEEAIRKVQPSVSSSDIEKHEKWLSEFGSA
Protein: GH11843p (Q9W0C3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD36772p
- Translational regulator orb2
- Uncharacterized protein, isoform A
- DnaJ homolog subfamily C member 21
- FI08257p
- RH40246p
- RH61816p
- FI17904p1
Sequence:
MADNNNCPKCKKSIAAKEATSIGCSGEDCRRRYHRTCVNIDDAVFEAIQKNSMISFHCDECKNQSPRAFAAKLHTIEEKVNKVCNGVNQIQGRMYQQYFQFGNQPLQALGASAAGVGGGGLGGGLDGKKHPQQNNLIVVGNNCNSDRLQVVCDYGRWVQVGKFATNTSEEDVIDHLAEELKINKNLVKCTKLVKNDANLSQLSYCKFKISIPDYRFNELFNEAIWPSGVMVSPFTPRSQLNQNRL
Protein: Excitatory amino acid transporter 1 (Sodium-dependent glutamate/aspartate transporter 1) (GLAST-1) (Solute carrier family 1 member 3) (P43003)
Organism: Homo sapiens (Human)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:20477940, ECO:0000269|PubMed:26690923, ECO:0000269|PubMed:28032905, ECO:0000269|PubMed:7521911, ECO:0000269|PubMed:8123008}; Multi-pass membrane protein {ECO:0000269|PubMed:28424515}.
Interaction partners:
- Excitatory amino acid transporter 2
- Glutamine synthetase
- Glial fibrillary acidic protein
- Cytosolic 10-formyltetrahydrofolate dehydrogenase
- Sodium-coupled neutral amino acid transporter 3
- Glutamate receptor ionotropic, NMDA 2B
- Nuclear factor 1 A-type
- Voltage-dependent L-type calcium channel subunit beta-4
- Nestin
- Fatty acid-binding protein, brain
Sequence:
MTKSNGEEPKMGGRMERFQQGVRKRTLLAKKKVQNITKEDVKSYLFRNAFVLLTVTAVIVGTILGFTLRPYRMSYREVKYFSFPGELLMRMLQMLVLPLIISSLVTGMAALDSKASGKMGMRAVVYYMTTTIIAVVIGIIIVIIIHPGKGTKENMHREGKIVRVTAADAFLDLIRNMFPPNLVEACFKQFKTNYEKRSFKVPIQANETLVGAVINNVSEAMETLTRITEELVPVPGSVNGVNALGLVVFSMCFGFVIGNMKEQGQALREFFDSLNEAIMRLVAVIMWYAPVGILFLIAGKIVEMEDMGVIGGQLAMYTVTVIVGLLIHAVIVLPLLYFLVTRKNPWVFIGGLLQALITALGTSSSSATLPITFKCLEENNGVDKRVTRFVLPVGATINMDGTALYEALAAIFIAQVNNFELNFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWFLDRLRTTTNVLGDSLGAGIVEHLSRHELKNRDVEMGNSVIEENEMKKPYQLIAQDNETEKPIDSETKM
Protein: Ribonuclease J (RNase J) (EC 3.1.-.-) (Q72JJ7)
Organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
Function: An RNase that has endonuclease and possibly 5'-3' exonuclease activity. Probably involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
Interaction partners:
Sequence:
MENQERKPRRRRRRRPQEGSQGGPQDHVEIIPLGGMGEIGKNITVFRFRDEIFVLDGGLAFPEEGMPGVDLLIPRVDYLIEHRHKIKAWVLTHGHEDHIGGLPFLLPMIFGKESPVPIYGARLTLGLLRGKLEEFGLRPGAFNLKEISPDDRIQVGRYFTLDLFRMTHSIPDNSGVVIRTPIGTIVHTGDFKLDPTPIDGKVSHLAKVAQAGAEGVLLLIADATNAERPGYTPSEMEIAKELDRVIGRAPGRVFVTTFASHIHRIQSVIWAAEKYGRKVAMEGRSMLKFSRIALELGYLKVKDRLYTLEEVKDLPDHQVLILATGSQGQPMSVLHRLAFEGHAKMAIKPGDTVILSSSPIPGNEEAVNRVINRLYALGAYVLYPPTYKVHASGHASQEELKLILNLTTPRFFLPWHGEVRHQMNFKWLAESMSRPPEKTLIGENGAVYRLTRETFEKVGEVPHGVLYVDGLGVGDITEEILADRRHMAEEGLVVITALAGEDPVVEVVSRGFVKAGERLLGEVRRMALEALKNGVREKKPLERIRDDIYYPVKKFLKKATGRDPMILPVVIEG
Protein: Aminoadipic semialdehyde synthase (Q54P64)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Putative aldehyde dehydrogenase family 7 member A1 homolog
- Probable saccharopine dehydrogenase [NADP
- Spermidine synthase
Sequence:
MTKVYSLGIRREDKNRWERRAPLAPSHVEELVKKGIKVIVQPSTLRNYPNVLYEKAGAIIQEDLKECDVIVAVKEVPSEYLYNDKTYIFFSHTIKAQPYNMAMLDEINKKRIRLIDYERITDDQNRRLVRFGSFAGYAGMIDMLHALGDRLLAKGFSTPFLHVGYSYVYSKLESAMEAVKAIGEEISQVGLPDDLLPFTFAFTSDGAVSQGALKIFKLLPHKMVTPDEMVELVKNKKGERGILYGTIITSEHMAAPIDPEKKFNKAEYYADPSKYKPIFCEKYAPYISCIINCMYWDAKYPRLITIRQMEELVETNNSRLIGVADISADVNGSLEFLMTTTSIDSPLYIYDPRTQEVHDPTTDQQYMYRDGILFLAVDNLPTEFPKEATQWFGDHLLKFMEQVVKSDPKLPYEKMTDIAPEMKRAIITCHGSLTPPFEYITELRKKREELTTRILILGAGSVSYPTISYLARNPSHKLTVGDVSIEQSKKAASYDPECQTVVIDVNDQEKLDEIVKRHRVVVSLLPDELTILVAKSCIRQKKHMVSPGYMSSEMEALDKDAKEAGITLLNEMGLDPGIDHLEACRVINDATNKGGKVRTFVSWCGGLPAPESSDNPLGYKFTWSPKEIISGVTNDSKFRRDGQDIYIPGSEVYKRVQPVDIFPALSLEGVPNRDCLHLTKTYGIESVNTLFRGTIRYKGFCQVMEAAVEIGLLDTTSKSHLAPSAPPMSWNLAMRHILPIPQSEGIPTQELLRRKLRTRRGYPSKGYDDDKITYILYVFEWLDIFSEKNNVAQCGNYFEAFTELLKTKLNLLPSERDLIILHNVVGIEWDGGKHETKTSTLVYYGSKDQSAVSTVVGLPVAIAAELLVENQIKEVGAIRPITKEFYKPMLKSLHNEGISFIHRSEFDKI