wanglab/gogpt-training-data huggingface dataset:
Protein: Inactive metacaspase-4 (TbMCA4) (Q8T8E5)
Organism: Trypanosoma brucei brucei
Function: Inactive metacaspase which plays a role in parasite bloodstream form growth and in parasite virulence within the mammalian host.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:21949125}; Lipid-anchor {ECO:0000269|PubMed:21949125}; Cytoplasmic side {ECO:0000269|PubMed:21949125}. Secreted {ECO:0000269|PubMed:21949125}. Note=Secreted by the parasite bloodstream form (PubMed:21949125). Membrane localization is required for MCA4 processing but is dispensable for MCA4 secretion, and parasite growth and virulence in the mammalian host (PubMed:21949125). {ECO:0000269|PubMed:21949125}.
Interaction partners:
Sequence:
MGGCVSTALKVGAETVAEGHIDLISFAINYFKNAVPYIVKYLGRQQRPKEVDMEATLTEAKESKGFQPWKISCQPKGAVRGLFIGVNYGNTEAQLSGCCHDIMMMIGALQKRNFPLTEVVILADEEDVPGRTGEPTRANILRYLAWLAQDAQPNDVLFFHYSGHGTRANARDDDCEEYDQCIVPMDYVENGCIVDNEIHEILVSQLPKGVRLTAVFDCSHSGSMLDLPYAYVCDSSKDGSGSCGMKRVREDNDVQADVLMISACADDEAALGVDNTQDFYESGKDSGGAATFCLTAMMMREEPLTFLDLLVHTREMLKSRGFTQVPHLSASKPINLMQRFSLEGLFPQERTLL
Protein: leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (Q9VQR8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Lysine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Tyrosine--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
- AaRS-interacting multifunctional protein 3
- Tyrosine--tRNA ligase, mitochondrial
Sequence:
MATTERKGTFKVEYLQKIEREVQQRWEAERVHESDAPTAPKKRQAEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMPIKACADKLTRELEQFGFPPQFPETEEVVPVAAEAASEVPKDKSKGKKSKAVAKTGAAKYQWQIMQSLGLKDEEIKDFANAEHWLNYFPPLAVQDLKRIGVHVDWRRTFITTDANPYFDSFVRWQFNHLKERGKIMYGKRYTIYSPKDGQPCMDHDRSSGEGVGPQEYTLIKMKVLEVPKALSSIKQPIFMVAATLRPETMYGQTNCWLHPDIKYIAWQANKNNEVWVSTRRAARNMTYQGFTAVEGEIKVLAEVTGQDLLGVPLSAPLTKHKVVYSLPMLSIKEDKGTGVVTSVPSDSPDDYAALVDLQKKEAFRQKYGLKDEMVLPYEPIPIIEVPTLGKLSAVHAYETLKIQSQNDKDKLAEAKEMCYLKSFYDGVMLVGAFAGRKIQDVKKDLQKRLVDANEADVYYEPEKTIMSRSADECVVALCNQWYLNYGEPEWQAQATKILHGMETFHEEARNNFEACLNWLHEYACSRTYGLGTKLPWDDKWLIESLSDSTIYMAFYTVVHLLQGGTFRGEKPGPFGIKPSDMTGEIWDYIFFKETPLPKKTAIKQEHLAVLRREFEYWYPMDLRVSGKDLIQNHLTFCLYNHAAIWPNDENKWPKGMRVNGHLLLNSAKMSKSDGNFLTLTEAVDKFSADGMRLCLADAGDSVEDANFVESTADAGILRLYTFIEWVKEMLENRSSLRKGTDKTFNDQVFLSELNLKTQQTDENYRKMLFKEALRSGFYELQLARDKYRELCGANGMHEDLVLEFIRRQALLVSPICPHMAEHVWGLLGNKESIVHARWPEVGAINEVDILCSEYLMEAAHSFRLNLKNLLQIKGKAGKDKSVNVQAAKPNRGLVWVAKTYPPWQCCVLDTMKELFNKSQALPDNKVIAATLQQKAELKKFMKRVMPFAQMIREKVESGKGVAALAVTLEFDERQVLISNLEYLKNTLDLDVLEIKYTDDPSAPEKTREEVRPGSPFISFSVAPNVSVELTNPIERSSLFQVNTVISEGDTVQSLREKLSKIIGLKTDAATLKIWRYEDPVLGPRKIPNFEDYKAGKSVLGEGNFVLDVENKKVSLEQAGKLTEVGRNLIYVVD
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (oxoG:A-specific adenine glycosylase) (P83847)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product. 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs. May also be able to remove adenine from A:G mispairs, although this activity may not be physiologically relevant.
Interaction partners:
Sequence:
MTRETERFPAREFQRDLLDWFARERRDLPWRKDRDPYKVWVSEVMLQQTRVETVIPYFEQFIDRFPTLEALADADEDEVLKAWEGLGYYSRVRNLHAAVKEVKTRYGGKVPDDPDEFSRLKGVGPYTVGAVLSLAYGVPEPAVDGNVMRVLSRLFLVTDDIAKPSTRKRFEQIVREIMAYENPGAFNEALIELGALVCTPRRPSCLLCPVQAYCQAFAEGVAEELPVKMKKTAVKQVPLAVAVLADDEGRVLIRKRDSTGLLANLWEFPSCETDGADGKEKLEQMVGEQYGLQVELTEPIVSFEHAFSHLVWQLTVFPGRLVHGGPVEEPYRLAPEDELKAYAFPVSHQRVWREYKEWASGVRRPD
Protein: Cyclin-T (O96433)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cyclin-dependent kinase 9
- Cyclin-dependent kinase 12
- Transcription elongation factor SPT5
- Cyclin-H
- Cyclin-dependent kinase 7
- Transcription elongation factor SPT4
- AF4/FMR2 family member lilli
- Hexamethylene bisacetamide inducible, isoform B
- RNA polymerase II elongation factor Ell
- Hyrax
Sequence:
MSLLATPMPQAATASSSSSASAAASASGIPITANNNLPFEKDKIWYFSNDQLANSPSRRCGIKGDDELQYRQMTAYLIQEMGQRLQVSQLCINTAIVYMHRFYAFHSFTHFHRNSMASASLFLAAKVEEQPRKLEHVIRAANKCLPPTTEQNYAELAQELVFNENVLLQTLGFDVAIDHPHTHVVRTCQLVKACKDLAQTSYFLASNSLHLTSMCLQYRPTVVACFCIYLACKWSRWEIPQSTEGKHWFYYVDKTVSLDLLKQLTDEFIAIYEKSPARLKSKLNSIKAIAQGASNRTANSKDKPKEDWKITEMMKGYHSNITTPPELLNGNDSRDRDRDRERERERERDPSSLLPPPAMVPQQRRQDGGHQRSSSVSGVPGSSSSSSSSSHKMPNYPGGMPPDAHTDHKSKQPGYNNRMPSSHQRSSSSGLGSSGSGSQRSSSSSSSSSQQPGRPSMPVDYHKSSRGMPPVGVGMPPHGSHKMTSGSKPQQPQQQPVPHPSASNSSASGMSSKDKSQSNKMYPNAPPPYSNSAPQNPLMSRGGYPGASNGSQPPPPAGYGGHRSKSGSTVHGMPPFEQQLPYSQSQSYGHMQQQPVPQSQQQQMPPEASQHSLQSKNSLFSPEWPDIKKEPMSQSQPQPFNGLLPPPAPPGHDYKLNSHPRDKESPKKERLTPTKKDKHRPVMPPVGSGNSSSGSGSSKPMLPPHKKQIPHGGDLLTNPGESGSLKRPNEISGSQYGLNKLDEIDNSNMPREKLRKLDTTTGLPTYPNYEEKHTPLNMSNGIETTPDLVRSLLKESLCPSNASLLKPDALTMPGLKPPAELLEPMPAPATIKKEQGITPMTSLASGPAPMDLEVPTKQAGEIKEESSSKSEKKKKKDKHKHKEKDKSKDKTEKEERKKHKKDKQKDRSGSGGSKDSSLPNEPLKMVIKNPNGSLQAGASAPIKLKISKNKVEPNNYSAAAGLPGAIGYGLPPTTATTTSASIGAAAPVLPPYGAGGGGYSSSGGSSSGGSSKKKHSDRDRDKESKKNKSQDYAKYNGAGGGIFNPLGGAGAAPNMSGGMGAPMSTAVPPSMLLAPTGAVPPSAAGLAPPPMPVYNKK
Protein: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC 2.4.1.255) (O-GlcNAc transferase subunit p110) (O-linked N-acetylglucosamine transferase 110 kDa subunit) (Q5GA11)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASSVGNVADSTEPTKRVLSFQGLAELAHREYQSGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPMLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAGYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGNVSEAEECYNTALRLCPTHADSLNNLANIKREQGNIEEAVQLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINALHKPAYEHPKDLKASSGRLRVGYISSDFGNHPTSHLMQSIPGMHNSEKFEVFCYALSPDDGTNFRVKVMAEAHHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLAYPGTSGAPFMDYIVSDKATSPIEVAEQYSEKLAYMPNTFFIGDHANMFPHLKKKAVIDFKSNGHIFDNRIVLNGIDLKAFLESLPDVKVVKMECDGQEVADSNGALSMPIIPMNTAAEAIINMINQGQIQVTINGFTVSNGLATTQINNKAATGEEVPRTIVVTTRSQYGLPEDSIVYCNFNQLYKIDPPTLQMWANILKRVPNSVIWLLRFPAVGEPNIQQYAQNLGLPASRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCPELIAQSRQEYEDVAVKLGTDMEFLKKVRARVWKQRICSPLFNTKQYTMDLEKLYLQMWENHASGGKPDHLVKMQSLETSEST
Protein: ABC transporter B family member 24, mitochondrial (ABC transporter ABCB.24) (AtABCB24) (ABC transporter of the mitochondrion 2) (AtATM2) (Iron-sulfur clusters transporter ATM2) (Protein STARIK 3) (Q9M0G9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (By similarity). Not involved in the export of cyclic pyranopterin monophosphate (cPMP) from mitochondria to the cytosol.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17517886}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17517886}.
Interaction partners:
- ABC transporter E family member 2
- Protein AE7-like 2
- Protein AE7-like 1
- ABC transporter E family member 1
- ABC transporter B family member 29, chloroplastic
- ABC transporter B family member 26, chloroplastic
- ABC transporter B family member 27
Sequence:
MMRVSQLQLCRTSLSYRLRSGYHHHHHLHHSFFKLIKRNSILESPPTNASHQSPSPITPMVNARVMFFSTSTSAPHPEKINRTSSENILRMISSYLWMKDNPKLCFRVISAFACLVGAKFLNVQVPFLFKVAIDWLSSSSFVDSNPYLVAAFATPSSVLIGYGIARSGSSAFNELRTSVFSKVALRTIRTISRKVLSRLHDLDLRYHLNRDTGALNRIIDRGSRAINTILSAMVFNIMPTILEISMVSCILAYKFGAVYALITCLSVGSYIAFTLAMTQWRIKIRKAMNEAENDASTRAIDSLINYETVKYFNNEDYEARKYDQLHENYEDAALQSRKSFALLNFGQSFIFSTALSTAMVLCSQGIMNGQMTVGDLVMVNGLLFQLSLPLYFLGVVYSDTVQGLVDMKSMFKFLEERSDIGDKDIDRKLPPLVLKGGSISFENVHFSYLPERKILDGISFEVPAGKSVAIVGSSGSGKSTILRMIFRFFDVDSGNVKIDGQDIKEVRLESLRSSIGVVPQDTVLFNDTIFHNIHYGNLSATEEEVYNAARRAAIHDTIMKFPDKYSTAVGERGLMLSGGEKQRVALARAFLKSPAILLCDEATSALDSKTEAEIMKTLRSLASNRTCIFIAHRLTTAMQCDEILVMEKGKVVEKGTHEVLLGKSGRYAKLWTQQNSKLEV
Protein: ESX-5 secretion system protein EccD5 (ESX conserved component D5) (Type VII secretion system protein EccD5) (T7SS protein EccD5) (P9WNP9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ESX-5 specialized secretion system, which is responsible for the secretion of EsxN and a number of PE_PGRS and PPE proteins, including PPE41.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:B2HSU6}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ESX-5 secretion system protein EccE5
- ESX-5 secretion system protein EccC5
- ESX-5 secretion system ATPase EccB5
- Mycosin-5
- ESX conserved component EccC2. ESX-2 type VII secretion system protein. Possible membrane protein
- ESX-3 secretion system ATPase EccB3
- ESX-5 secretion system protein EccA5
- ESX-3 secretion system protein EccC3
- ESX-5 secretion-associated protein EspG5
- ESX-4 secretion system protein EccC4
Sequence:
MTAVADAPQADIEGVASPQAVVVGVMAGEGVQIGVLLDANAPVSVMTDPLLKVVNSRLRELGEAPLEATGRGRWALCLVDGAPLRATQSLTEQDVYDGDRLWIRFIADTERRSQVIEHISTAVASDLSKRFARIDPIVAVQVGASMVATGVVLATGVLGWWRWHHNTWLTTIYTAVIGVLVLAVAMLLLMRAKTDADRRVADIMLMSAIMPVTVAAAAAPPGPVGSPQAVLGFGVLTVAAALALRFTGRRLGIYTTIVIIGALTMLAALARMVAATSAVTLLSSLLLICVVAYHAAPALSRRLAGIRLPVFPSATSRWVFEARPDLPTTVVVSGGSAPVLEGPSSVRDVLLQAERARSFLSGLLTGLGVMVVVCMTSLCDPHTGQRWLPLILAGFTSGFLLLRGRSYVDRWQSITLAGTAVIIAAAVCVRYALELSSPLAVSIVAAILVLLPAAGMAAAAHVPHTIYSPLFRKFVEWIEYLCLMPIFPLALWLMNVYAAIRYR
Protein: ADP-sugar pyrophosphatase (EC 3.6.1.13) (8-oxo-dGDP phosphatase) (EC 3.6.1.58) (Nuclear ATP-synthesis protein NUDIX5) (EC 2.7.7.96) (Nucleoside diphosphate-linked moiety X motif 5) (Nudix motif 5) (Q9JKX6)
Organism: Mus musculus (Mouse)
Function: Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (By similarity). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze other nucleotide sugars with low activity. In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate (By similarity). Nuclear ATP synthesis takes place when dephosphorylated at Thr-44 (By similarity). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity). Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UKK9}.
Interaction partners:
- ADP-ribose pyrophosphatase, mitochondrial
- Ribose-phosphate pyrophosphokinase 1
- Phosphoglucomutase-1
- Ribose-phosphate pyrophosphokinase 2
- ribose-phosphate diphosphokinase
- Ribose-phosphate pyrophosphokinase 1
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
- Phosphopentomutase
- Nucleotide triphosphate diphosphatase NUDT15
- 8-oxo-dGDP phosphatase NUDT18
Sequence:
METRESTESSPGKHLVTSEELISEGKWVKFEKTTYMDPTGKTRTWETVKLTTRKGKSADAVSVIPVLQRTLHHECVILVKQFRPPMGSYCLEFPAGFIEDGESPEAAALRELEEETGYKGEVAECSPAVCMDPGLSNCTTHVVTVTINGDDAGNVRPKPKPGDGEFMEVISLPKNDLLTRLDALGAEQHLTVDAKVYAYGLALKHANSKPFEVPFLKF
Protein: Corticoliberin (Corticotropin-releasing factor) (Corticotropin-releasing hormone) (M3VX86)
Organism: Felis catus (Cat) (Felis silvestris catus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Corticotropin-releasing factor receptor 1
- Corticotropin releasing hormone receptor 2
- Corticotropin-releasing factor-binding protein
- Urocortin
- Urocortin 3
- Neuropeptide Y
- Pro-opiomelanocortin
- Thyrotropin releasing hormone
- Oxytocin-neurophysin 1
- Cholecystokinin
Sequence:
MRLPLLLSAGVLLVAFLPCPPCRALLSRGPIPRARQAPQQPQPLDFSQLPPQPQQPQQPQARPILLRMGEEYFLRLGNLNKSPAAPLLPASSPVSGGSGSHLSPDEAAANFFRALLQQLPLPRRPLPLDSPAGPAEHGAENALGSRQETLERQRRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEIIGK
Protein: AT-rich interactive domain-containing protein arid-1 (A0A0K3AXH1)
Organism: Caenorhabditis elegans
Function: DNA-binding protein which modulates activity of several transcription factors (By similarity). Plays a role in the modulation of endoplasmic reticulum (ER) homeostasis during chemical and pathogen stress, including exposure to the Gram-negative bacterium P.aeruginosa.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000305}.
Interaction partners:
- SWI/SNF Subunit INI1 DNA binding domain-containing protein
- SWI/SNF complex subunit SMARCC2
- SWI/SNF chromatin remodeling complex core catalytic subunit swsn-4
- SWI/SNF chromatin-remodeling accessory subunit 2
- Bromo domain-containing protein
- Retinoblastoma-like protein homolog lin-35
- Lysine-specific demethylase 7 homolog
- Paired box protein 1 homolog
- JmjC domain-containing protein
- LITAF domain-containing protein
Sequence:
MSDDPAFLALGTEVSAKFKGAYCEAKIQKVDRSLKVKVSLKESPFGQMIVQDNDLPNAKFEINELTDVVFQRKFIRCQIQSIKDQSKYHVVFNDGDEKELRRTQLVLKGGKHFAADGNLDSMPLTNPESFSTPVIRGAAKRGAQKIRNAISEASGSRGGAVLLHNDDDENDEEDQEDGENEEDADDDDDDTEEQQQPRERRRAAAISAIGVLKKAIEDTQSEESSADSSEERERARSRRKRKDEASSAVTSDEEDQEDLATTDSENPVINGASSAAALSKTLQRKLEKQAMKREKQRLKEEEREEKLRLKEENREKKRREKARIMELKRLEKVYRTSNARIQENHEKSMTQIISHRSVRYFARFSDLKHRRKKKKLYLHEHRQKVNSRIRNVKLYFAWRFVAHKARLSYFARYALQWWRTSEDQAYSLIRTEKLLRSQRRRDWVGSWLEGLEREKIRFVVIHESYTQARRILKYIERGTEKRTFAERCDIEYEDIESSTVSSHFRDQEWFPAVLFPQVFSDENGSEGRQRIVRHMGNGQLVQVWEDDLVPFDWLPEYSFADVTAMTEKKPVEMRRKFKLAWRFATDYAQNRLDARSIRSILEWKFIRPSSRRLKITPIPVQAPSPNRCGEDHDDLVSTPNESDYDSDATIKNVDAETKDLFVAMLVQFHDAHNSVIDTNPTIQGHEVDLYYLYELAKKTGGPKKVYAANLWSDYAKKLVPAATDAEEELKTIFKNFLESYLAINTKLSWPMESLQPRTERKVVLPGQYSESRKKRTQAIMSQVQTPPTAPGSSKKGRVGSGGTRGRKRKVSSESVQLKKRNRKSSSRATTASPGPSEDRFSFQRPQDSDDVTDVPDDMTDHEDLLPEAATRKKYERKSQTPGRRSLSSRRDDTTPVSSMAAAPPKKGRPRKNTTVTTPVLSVPKSEGRGPRKEDTTTKFVRANVLSHILSGQKLRAFYGDEWFRANAIEDATDCTDEIMDIMLAHQDFFTPDTPRLSPSAIQDLDKVLKKIRAKTHYTGWNQRYDEFMKLEKLMVTVEDQMIARGRFRHLPRGRELKAETLALVEKHFRADDEDDGVPKTLAFYLKIAQEALSLSEKRAVADDDESSDSDTDFEQKPDTSAAAAVNGGKSESEEEEEEKTVVMGGDEEAEEEVKSEDVLVESVDQESPPTTSQGTTTPETAATGGLESESDEPEYPPVPEELVPPPPVLLENFPSTDRFSSGGSSNYPTLSRQGSINSMASPMFSPNSDLSLSGPLTLPRSGPLTMANIRQSPTPDEVVGSLRKRLSQTSESSESSELPPPPSAASKSKRIRRASERSIDSASEHHRMMRSPRILTTQHSSGALIFDISTTQPTDTSGPIEALSVRKPGRRKTVFAASPTLLTSGPLTLSSSAPPPPPASPAPPQHAQKTLGRPRKTPSTSSRKPEEEDEAEQIPTTVVGVTEEASVADSSAKEDLTSEDGSATPQDEKDDSESTTTTDTITPKSIRGGKRRRGGGRFGGSYPVKPAKPGRKPKDPHAEEGADEKDPEDQTPTTMTTSTPTRADSFQTQKNRMAKLMEGKPHDYSFLDLPDFDKIIEEAPKEDINILMEERTYELREIFAQCKADLSALEKRYRQQNEAKRKAEFAAKTASSAAAAQASSSTCSTPRP
Protein: Kinesin-associated protein 3 (KAP-3) (KAP3) (Smg GDS-associated protein) (Q92845)
Organism: Homo sapiens (Human)
Function: Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex (By similarity).
Interaction partners:
- Kinesin-like protein KIF3B
- Kinesin-like protein KIF3C
- Kinesin-like protein KIF3A
- Kinesin-like protein KIF15
- Kinesin light chain 1
- Kinesin-like protein KIF17
- Choline O-acetyltransferase
- Neutrophil cytosol factor 2
- Intraflagellar transport protein 88 homolog
- Kinesin-like protein KIFC3
Sequence:
MQGEDARYLKRKVKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQLLYYLQNRRDSLSGKEKKEKSSKPKDPPPFEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELLLNETALGALARVLREDWKQSVELATNIIYIFFCFSSFSQFHGLITHYKIGALCMNIIDHELKRHELWQEELSKKKKAVDEDPENQTLRKDYEKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMRNKNIVHMLVKALDRDNFELLILVVSFLKKLSIFMENKNDMVEMDIVEKLVKMIPCEHEDLLNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNDNYKQIAMCVLYHISMDDRFKSMFAYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLLMKMIRNISQHDGPTKNLFIDYVGDLAAQISNDEEEEFVIECLGTLANLTIPDLDWELVLKEYKLVPYLKDKLKPGAAEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNNEIRKVCDNTLDIIAEYDEEWAKKIQSEKFRWHNSQWLEMVESRQMDESEQYLYGDDRIEPYIHEGDILERPDLFYNSDGLIASEGAISPDFFNDYHLQNGDVVGQHSFPGSLGMDGFGQPVGILGRPATAYGFRPDEPYYYGYGS
Protein: Probable arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) (Q558Z0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P54136}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
Interaction partners:
- Probable glutamate--tRNA ligase, cytoplasmic
- Probable isoleucine--tRNA ligase, cytoplasmic
- Probable isoleucine--tRNA ligase, mitochondrial
- Probable asparagine--tRNA ligase, mitochondrial
- arginine--tRNA ligase
- Probable methionine--tRNA ligase, cytoplasmic
- proline--tRNA ligase
- glutamate--tRNA ligase
- Probable glutamine--tRNA ligase
- Tryptophan--tRNA ligase, cytoplasmic
Sequence:
MFQEEIAKQLSVLTEIEANKILECIESTKNKDMADFAVPIPKLNKFKKLVGKPDQLAIDFASKIQLNDCIQGASATGNYLNFKVNRLLQVQEILKEVINQKEKYGMTEQGKGKKVIVEFSSPNIAKPFHAGHLRSTIIGNFMVNLFNELAYETVSMNYLGDWGKQYGLLAVGFEKYGSEEELLADPIKHLYNVYVQINGEAEKEEEAKKKYAEEIAAGVEPTAPLQTTPTIHDTARAYFKRMEDGDAEALAIWKRFRDLSIVKYKDIYNRLNVKFDIYAGESLVTEGMTIEFKKLQDKNLLEDSQGAKVIDLSKPNKLGKVLVQKTDGTTLYITRDIAAAVDRKNNIGFDKMYYVVASQQDFHFRQLFDILGKMDYQWQKDLTHINYGMVKGMSTRKGTVVFLEDILNKTQKKMLKIMKQNEQKFAEIEDPEKVADIVGLSAVVIQDFNAKRNKDYDFNWDRMLKSDGDTGPYLQYAHARLCSLERKSGFEFNPNANLSLLSEPEAFNLAITIGRYPEIIQLTHNQLEPSTLVGYLFELAHAVSSAHQVLWIKDREKDVAEARFVLYWAAKVILGSGLRILGLVPLERM
Protein: Sterile alpha motif domain-containing protein 9 (SAM domain-containing protein 9) (Q5K651)
Organism: Homo sapiens (Human)
Function: Double-stranded nucleic acid binding that acts as a an antiviral factor by playing an essential role in the formation of cytoplasmic antiviral granules. May play a role in the inflammatory response to tissue injury and the control of extra-osseous calcification, acting as a downstream target of TNF-alpha signaling. Involved in the regulation of EGR1, in coordination with RGL2. May be involved in endosome fusion.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16960814, ECO:0000269|PubMed:17407603, ECO:0000269|PubMed:25428864, ECO:0000269|PubMed:28157624}.
Interaction partners:
- Probable ATP-dependent RNA helicase DDX60
- Antiviral innate immune response receptor RIG-I
- Interferon-induced protein 44
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- 2'-5'-oligoadenylate synthase 2
- Interferon-induced helicase C domain-containing protein 1
- Probable ATP-dependent RNA helicase DDX60-like
- Protein mono-ADP-ribosyltransferase PARP9
- Ral guanine nucleotide dissociation stimulator-like 2
- Sterile alpha motif domain-containing protein 9-like
Sequence:
MAKQLNLPENTDDWTKEDVNQWLESHKIDQKHREILTEQDVNGAVLKWLKKEHLVDMGITHGPAIQIEELFKELRKTAIEDSIQTSKMGKPSKNAPKDQTVSQKERRETSKQKQKGKENPDMANPSAMSTTAKGSKSLKVELIEDKIDYTKERQPSIDLTCVSYPFDEFSNPYRYKLDFSLQPETGPGNLIDPIHEFKAFTNTATATEEDVKMKFSNEVFRFASACMNSRTNGTIHFGVKDKPHGKIVGIKVTNDTKEALINHFNLMINKYFEDHQVQQAKKCIREPRFVEVLLPNSTLSDRFVIEVDIIPQFSECQYDYFQIKMQNYNNKIWEQSKKFSLFVRDGTSSKDITKNKVDFRAFKADFKTLAESRKAAEEKFRAKTNKKEREGPKLVKLLTGNQDLLDNSYYEQYILVTNKCHPDQTKHLDFLKEIKWFAVLEFDPESNINGVVKAYKESRVANLHFPSVYVEQKTTPNETISTLNLYHQPSWIFCNGRLDLDSEKYKPFDPSSWQRERASDVRKLISFLTHEDIMPRGKFLVVFLLLSSVDDPRDPLIETFCAFYQDLKGMENILCICVHPHIFQGWKDLLEARLIKHQDEISSQCISALSLEEINGTILKLKSVTQSSKRLLPSIGLSTVLLKKEEDIMTALEIICENECEGTLLEKDKNKFLEFKASKEEDFYRGGKVSWWNFYFSSESYSSPFVKRDKYERLEAMIQNCADSSKPTSTKIIHLYHHPGCGGTTLAMHILWELRKKFRCAVLKNKTVDFSEIGEQVTSLITYGAMNRQEYVPVLLLVDDFEEQDNVYLLQYSIQTAIAKKYIRYEKPLVIILNCMRSQNPEKSARIPDSIAVIQQLSPKEQRAFELKLKEIKEQHKNFEDFYSFMIMKTNFNKEYIENVVRNILKGQNIFTKEAKLFSFLALLNSYVPDTTISLSQCEKFLGIGNKKAFWGTEKFEDKMGTYSTILIKTEVIECGNYCGVRIIHSLIAEFSLEELKKSYHLNKSQIMLDMLTENLFFDTGMGKSKFLQDMHTLLLTRHRDEHEGETGNWFSPFIEALHKDEGNEAVEAVLLESIHRFNPNAFICQALARHFYIKKKDFGNALNWAKQAKIIEPDNSYISDTLGQVYKSKIRWWIEENGGNGNISVDDLIALLDLAEHASSAFKESQQQSEDREYEVKERLYPKSKRRYDTYNIAGYQGEIEVGLYTIQILQLIPFFDNKNELSKRYMVNFVSGSSDIPGDPNNEYKLALKNYIPYLTKLKFSLKKSFDFFDEYFVLLKPRNNIKQNEEAKTRRKVAGYFKKYVDIFCLLEESQNNTGLGSKFSEPLQVERCRRNLVALKADKFSGLLEYLIKSQEDAISTMKCIVNEYTFLLEQCTVKIQSKEKLNFILANIILSCIQPTSRLVKPVEKLKDQLREVLQPIGLTYQFSEPYFLASLLFWPENQQLDQHSEQMKEYAQALKNSFKGQYKHMHRTKQPIAYFFLGKGKRLERLVHKGKIDQCFKKTPDINSLWQSGDVWKEEKVQELLLRLQGRAENNCLYIEYGINEKITIPITPAFLGQLRSGRSIEKVSFYLGFSIGGPLAYDIEIV
Protein: Disulfide bond formation protein B 1 (Disulfide oxidoreductase 1) (P21482)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein (By similarity).
Subcellular location: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Thiol:disulfide interchange protein DsbA
- Disulfide bond formation protein B 2
- HemY N-terminal domain-containing protein
- Thiol:disulfide interchange protein
Sequence:
MPLASPRQLFLLAFLACVAIMGGALYLEHVVGLEACPLCVVQRIFFILIGLTCLAGAIQGPGLRGRRIYSVLVFLLALGGGATAARQVWLQTVPLDQLPACLPSLDYMMQALPFQEVIRLVLHGTADCAQVSWTLFTLSIPEWSLLAFVAYLGFSIVQFLRRA
Protein: Bombesin (P84213)
Organism: Bombina variegata (Yellow-bellied toad)
Function: Stimulates smooth muscle contraction. Role in induction of hypothermia, stimulation of DNA replication and release of many gastrointestinal hormones. Possesses insulin-releasing activity.
Subcellular location: Secreted {ECO:0000269|PubMed:15134346, ECO:0000269|PubMed:2335218, ECO:0000269|PubMed:4537042}.
Interaction partners:
Sequence:
MSAIPLNRILPLGFLLIFSFISLSSCMEFVEDPNNQGGLNLQQRLGNQWAVGHLMGKKSLQDTDFEEMESFAKRNVENMKAESERELRHAQLVVRNILEQYLKNMQN
Protein: Sphingolipid delta(4)-desaturase (EC 1.14.19.17) (Delta 4-(E)-sphingolipid desaturase) (Dihydroceramide desaturase) (O59715)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Delta(4)-fatty-acid desaturase which introduces a double bond at the 4-position in the long-chain base (LCB) of ceramides. Required for sphingosine biosynthesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sphingosine N-acyltransferase lac1
- Inositol phosphosphingolipids phospholipase C
- PIGF/3-ketodihydrosphingosine reductase fusion protein
- Sphingoid long chain base kinase 4
- Sphingosine N-acyltransferase lag1
- Serine palmitoyltransferase 2
- Dihydrosphingosine 1-phosphate phosphatase C823.11
- Sphingolipid C4-hydroxylase sur2
- Methionine aminopeptidase 2
- Serine palmitoyltransferase 1
Sequence:
MAESTATTTAVPPPAEESWNADSEDVHQFYWTYTEEPHKSRRAAILKAHPEIASLNGYEPLTKWIVLGVVSLQFTCAYLLSQSSLLSWKFFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYNRAYCLFANLPVGAPFAASFRPYHMEHHAYQGVDGMDTDLPTRAELILFDNVLGKAFFCTFQLLFYAFRPLVVRRLPFTLMHFWNIIVQFSFDYLVVRYVGWRALAYFFMSSFLAGSLHPTAGHFLSEHYNMTRTRLIASGPGKETPLETFSYYGPLNFFVYNAGYHIEHHDFPYVAWTRIGKVRELAPEFYDNIPDCKSWCGIIYQFITDSNVGMWCRVKRKQKHADIPTKSMHLHVS