wanglab/gogpt-training-data huggingface dataset:
Protein: Phenylalanine--tRNA ligase alpha subunit, cytoplasmic (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) (Q9T034)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277, ECO:0000305|PubMed:16297076}.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit, cytoplasmic
- Phenylalanine--tRNA ligase, chloroplastic/mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase 2, cytoplasmic
- Arginine--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, chloroplastic/mitochondrial
- Methionine--tRNA ligase, chloroplastic/mitochondrial
- Serine--tRNA ligase, cytoplasmic
Sequence:
MAEEAILGFLQNNEQITDSGQFSAEFNIDHNELVNVIKSLHGFRYIDVQDIKKETWILTDEGKKYAAEGSPEVQLFLAVPEEGSISKDELQKKLAPAVFKIGCSQAGKNKWVEMGKQVSRKVKDVEDKVKGQLLQIQQGKEFDKESINSLKARKLIVPQIWKGYSVKKGPNYAPERKKVATDLTRENLQNWKELEFKEYNFKAKGAPVDAGHLHALLKVRKQFKDIFVQMGFEEMPTNNYVESSFWNFDALFQPQQHPARDSHDTFFLKVPSTTRTLPEDYVERVKRVHESGGYGSRGYNYDWKREEANKNLLRTHTTAVSSRMLYALAQKPFVPKKYFSIDRVFRNEAVDRTHLAEFHQIEGLICDRGLTLGDLIGVLEDFFSRLGMSKLRFKPAYNPYTEPSMEIFSYHEGLGKWVEIGNSGMFRPEMLLPMGLPEDVRVIAWGLSLERPTMILYGIDNIRDLFGHKVDLDLIKRNPICRIGI
Protein: Rhomboid-like protease (EC 3.4.21.105) (Q8IIM2)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362115}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362115}.
Interaction partners:
Sequence:
MSNIHTLAEYRDDYAENTPFNRTPDYYQSQSSFVQRSKPIDLLNLIFPHFTWKSFMVVISIIQLIVFIISVSIKPADFLTPSDSLLVTLGANVASRIKQGEIHRLILPIFLHANIFHAIFNIFFQLRMGFTLEKNYGIMKIIILYFVTGMYGNILSSSITYCPIKVGASTSGMGLVGIVTSELILLWHIIRHRERVVFNIIFFSLISFFYYFTFNGSNIDHVGHLGGLISGISLGILYNEHMDNKPRWYNHLKIGSYISLVLLAIIPTVVLFTIPRTC
Protein: Synemin (Desmuslin) (Q70IV5)
Organism: Mus musculus (Mouse)
Function: Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteromeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteromeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17356066}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O15061}. Note=There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere. {ECO:0000250|UniProtKB:O15061, ECO:0000269|PubMed:17356066}.
Interaction partners:
- Vinculin
- Nestin
- Talin-1
- Talin-2
- Syncoilin
- Plectin
- Dystrobrevin alpha
- Zyxin
Sequence:
MLSWRLQTGSEKAELQELNARLYDYVCRVRELERENLLLEEELRSRLSREDRWAEDQALYAEEARSLRQQLDELNWSTALAEGERDALRRELLELQREGVEAGTARSRLDAELGAQRRELEEALGARAALEALLGRLETERRDLDAAHERQVRDLRARAASLTMHFRARATSPAAPPPRLRDVHDSYALLVAESWRESVQLYEDEVRELEQALRRGQESRLQAEDEARLCAQEADALRNQALELEQLRARLEDELLRMREEYGMQAEERQRVIDSLEDEKEALTLAMADRLRDYQELLQVKTGLSLEVATYRALLEGESNPEILIWTENIENVPQEPRNTSYRYTNSVLQRKNEKNLFPRRKTPWAAVNHSSASYSNWPGHLDSQTTTAVGSAARRGLLTSRHSSSATTSGQQKPLEKTISSRANLRPVTPTHGFLRNTDAQMKTLPHRSKVEGTGDTHARRATESVITRESYRGHQGHVAAGAVSSTPSNERTVILGKKLEAQATKEQERDRSGVIRIKPEEKMFDSKEKASEERNLRWEELTKLDRDARKRESRHLRDEAREKEALKERSVKEREVPISLEVSRGSRAEVSTIHLQSPGRKDVSHSGGREAETKETRFRLDTQDTASSLQSDSTTETIAESIVTTILKQFTQSPGAEEEATSFPDTKVTYVDRKEFPGDGKTKTEIVVESKLTDVVDVSDEAGLDYLLSKDVKEVGLKGKSTETMIGEMINLGLKGREGRAKVVNVEIVEEPMSYIGGGKIDFSTPFQVEEVDDVSPSPKGFVEEEDGEGETHMAFSMRPHQTKQPQGTIPHVEEVTEAGDSEGEQSYFVSTPDEYPGGHDREDDGSVYGQIHIEEESTIRYSWQDEIAQGTWRRKMRGDVGGEKPVKVLEVPALSLGGAIGSAHLKEEASGELRAEPTVIEKEIKIPHEFHTSIKGVFSSEPRHQLVEVIGQLEETLPERMKEELSALTRQSQGESGSVSVDVKKVQSAAGGSVTLMAEVNLSQTVDADQLDLEQLSRDEAGEIERAVESVVRESLAKRSSPVPRSPDREDGEEVPAGGILFKRWATRELYSPSGERDDAGQVSPSSDQRVTQGPVSATVEVTSPTGFVQSHVLEDVSQSVRHVKLGPTEMWRTEQVTFGGPTAQVVEVSGDFSEAVSSEGASRSVRHITLGPHQSQVSTEVIFRGSVPTWQETGDTEKPGPVVLSVGADISGSGRMPGSERSHTEKEIRFQGPVSGTAQVGGNFATEESVGSQTFVRSLQLGPKEGFREEIQFIAPIPDKVGWGEEDSEHTKVSLERATSIQRIDIVPQRYLASKQMAPQTLEFRDSEDMVMVEGSAGTIQATHNFTSDREILQNKENTFQRVISGSPPDSVGDTGAEVTANVSRSFRHIQIGPTEEEPSEYFVTGRPVSKTFVLDGSVASPGLVGGADGGSTPCRIALGPKETSFTFQMDLSDTRAIRSWTRDTGSEVEAHGVSHRGGWRIAHSRDERVASTGSGASPGDAHQAPGEKGTEQAGFDKTVQLQRMVDQRSVASDEKKVALLYLDNEEEEEEEGEGWF
Protein: Transcription factor EB (A0A1B0GXL9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASRIGLRMQLMREQAQQEEQRERMQQQAVMHYMQQQQQQQQQQLGGPPTPAINTPVHFQSPPPVPGEVLKVQSYLENPTSYHLQQSQHQKVREYLSETYGNKFAAHISPAQGSPKPPPAASPGVRAGHVLSSSAGNSAPNSPMAMLHIGSNPERELDDVIDNIMRLDDVLGYINPEMQMPNTLPLSSSHLNVYSSDPQVTASLVGVTSSSCPADLTQKRELTDAESRALAKERQKKDNHNLIERRRRFNINDRIKELGMLIPKAND
Protein: Zinc finger protein 467 (Q3USQ2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRETLEALNSLGFSVGQPEMAPQSEPRDGFSNAQEKMSSRGESTLHSCSGHETPGQKEGIHTEQAEAPCMGSQASTPQKAEPAGSVPGDHMKFHCSLRRKHLMSPDACSSVSV
Protein: Phenolic glucoside malonyltransferase 1 (NtMaT1) (EC 2.3.1.-) (EC 2.3.1.116) (Flavonol/naphthol glucoside malonyltransferase 1) (Phenolic glucoside-6'-O-malonyltransferase 1) (Q589Y0)
Organism: Nicotiana tabacum (Common tobacco)
Function: Malonyltransferase with broad substrate specificity acting on phenolic glucosides including xenobiotic naphthols. Has activity against flavonoid 7-O-glucosides, flavonoid 3-O-glucosides and naphthol glucosides, and to a lesser extent against coumarin glucosides in vitro. Prefers malonyl-CoA as an acyl donor, but also active with succinyl-CoA and methylmalonyl-CoA, but not with acetyl-CoA.
Interaction partners:
- Glucan endo-1,3-beta-glucosidase
- Glucan endo-1,3-beta-glucosidase
- Glucan endo-1,3-beta-glucosidase
- Glucan endo-1,3-beta-glucosidase
Sequence:
MASVIEQCQVVPSPGSATELTLPLTYFDHVWLAFHRMRRILFYKLPISRPDFVQTIIPTLKDSLSLTLKYYLPLAGNVACPQDWSGYPELRYVTGNSVSVIFSESDMDFNYLIGYHPRNTKDFYHFVPQLAEPKDAPGVQLAPVLAIQVTLFPNHGISIGFTNHHVAGDGATIVKFVRAWALLNKFGGDEQFLANEFIPFYDRSVIKDPNGVGMSIWNEMKKYKHMMKMSDVVTPPDKVRGTFIITRHDIGKLKNLVLTRRPKLTHVTSFTVTCAYVWTCIIKSEAATGEEIDENGMEFFGCAADCRAQFNPPLPPSYFGNALVGYVARTRQVDLAGKEGFTIAVELIGEAIRKRMKDEEWILSGSWFKEYDKVDAKRSLSVAGSPKLDLYAADFGWGRPEKLEFVSIDNDDGISMSLSKSKDSDGDLEIGLSLSKTRMNAFAAMFTHGISFL
Protein: Agouti-signaling protein (ASP) (Agouti switch protein) (P42127)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). In higher primates, agouti may affect the quality of hair pigmentation rather than its pattern of deposition. Could well play a role in neuroendocrine aspects of melanocortin action. May have some functional role in regulating the lipid metabolism with adipocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:36536132}.
Interaction partners:
- Melanocyte-stimulating hormone receptor
- Pro-opiomelanocortin
- Attractin
- Agouti-related protein
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- P protein
- RNA-binding protein Raly
- Beta-defensin 103
- Tyrosinase
- Membrane-associated transporter protein
Sequence:
MDVTRLLLATLLVFLCFFTANSHLPPEEKLRDDRSLRSNSSVNLLDVPSVSIVALNKKSKQIGRKAAEKKRSSKKEASMKKVVRPRTPLSAPCVATRNSCKPPAPACCDPCASCQCRFFRSACSCRVLSLNC
Protein: Transportin-1 (Importin beta-2) (Karyopherin beta-2) (Q3SYU7)
Organism: Bos taurus (Bovine)
Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. May mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. Mediates nuclear import of ADAR/ADAR1 in a RanGTP-dependent manner (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- RNA-binding protein FUS
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein A1
- GTP-binding nuclear protein Ran
- Importin 7
- mRNA decay activator protein ZFP36
- Importin 8
- Transportin-3
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran
Sequence:
MVWDRQTKMEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSEDEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASKGELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFLQFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALVMLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLIRHLPKLIPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEEDDDDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV
Protein: Dimethylaniline monooxygenase [N-oxide-forming] 2 (EC 1.14.13.-) (Dimethylaniline oxidase 2) (Pulmonary flavin-containing monooxygenase 2) (FMO 2) (Q8K2I3)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidative metabolism of numerous xenobiotics, including mainly therapeutic drugs and insecticides that contain a soft nucleophile, most commonly nitrogen and sulfur and participates to their bioactivation. Catalyzes the S-oxygenation of the prodrug ethionamide (ETA) to the S-oxide (ETASO), the first step in its bioactivation following by the second oxygenation to the sulfinic acid but to a lesser extend.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein {ECO:0000250|UniProtKB:P17635}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein {ECO:0000250|UniProtKB:P17635}.
Interaction partners:
Sequence:
MAKKVVVIGAGVSGLISLKCCVDEGLEPTCFERTEDIGGLWRFKENVEDGRASIYRSVITNTSKEMSCFSDFPMPEDFPNFLHNSKLLEYFRIFAKKFDLLKYIQFQTTVISVKKRPDFASSGQWEVYTQSNGKEQRTVFDAVMVCSGHHIQPHLPLKSFPGIERFRGQYFHSREYKHPVGFEGKRILVVGIGNSAADIASELSKTAAQVFVSTRHGSWVMSRISEDGYPWDMVFHTRFSSMLRNVLPRTVVKWMMEQQMNRWFNHENYGLVPQNKYLMKEPVLNDDLPSRLLYGAIKVKTRVKELTETAVVFEDGTVEEDVDIIVFATGYTFSFSFLEDSLVKVEDNRVSLYKAMFPPHLEKPTLACIGLIQPLGSIFPTVELQARWATRVFKGLCSLPSETTMMADIVERNEKRVNLFGKSQSQILQTNYVDYLDELALEIGAKPDFVSLFFKDPKLAVKLYFGPCNSYQYRLVGPGQWEGARNAILTQKQRILKPLKTRTLQSSDSAPVSFLLKILGLLAVVLAFFFQLQGF
Protein: Magnesium-transporting ATPase, P-type 1 (EC 7.2.2.14) (Mg(2+) transport ATPase, P-type 1) (P0ABB8)
Organism: Escherichia coli (strain K12)
Function: Mediates magnesium influx to the cytosol.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- mgtA leader peptide
- Sensor protein PhoQ
- Transcriptional regulatory protein PhoP
- Putative magnesium transporter YhiD
- PhoP/PhoQ regulator MgrB
- Small protein MgtS
- Transcription termination factor Rho
- Sulfite reductase flavoprotein alpha-component
- Divalent metal cation transporter MntH
Sequence:
MFKEIFTRLIRHLPSRLVHRDPLPGAQQTVNTVVPPSLSAHCLKMAVMPEEELWKTFDTHPEGLNQAEVESAREQHGENKLPAQQPSPWWVHLWVCYRNPFNILLTILGAISYATEDLFAAGVIALMVAISTLLNFIQEARSTKAADALKAMVSNTATVLRVINDKGENGWLEIPIDQLVPGDIIKLAAGDMIPADLRILQARDLFVAQASLTGESLPVEKAATTRQPEHSNPLECDTLCFMGTTVVSGTAQAMVIATGANTWFGQLAGRVSEQESEPNAFQQGISRVSMLLIRFMLVMAPVVLLINGYTKGDWWEAALFALSVAVGLTPEMLPMIVTSTLARGAVKLSKQKVIVKHLDAIQNFGAMDILCTDKTGTLTQDKIVLENHTDISGKTSERVLHSAWLNSHYQTGLKNLLDTAVLEGTDEESARSLASRWQKIDEIPFDFERRRMSVVVAENTEHHQLVCKGALQEILNVCSQVRHNGEIVPLDDIMLRKIKRVTDTLNRQGLRVVAVATKYLPAREGDYQRADESDLILEGYIAFLDPPKETTAPALKALKASGITVKILTGDSELVAAKVCHEVGLDAGEVVIGSDIETLSDDELANLAQRTTLFARLTPMHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLEKSLMVLEEGVIEGRRTFANMLKYIKMTASSNFGNVFSVLVASAFLPFLPMLPLHLLIQNLLYDVSQVAIPFDNVDDEQIQKPQRWNPADLGRFMIFFGPISSIFDILTFCLMWWVFHANTPETQTLFQSGWFVVGLLSQTLIVHMIRTRRVPFIQSCASWPLMIMTVIVMIVGIALPFSPLASYLQLQALPLSYFPWLVAILAGYMTLTQLVKGFYSRRYGWQ
Protein: Arabino-1,4-lactone oxidase (C8CCV9)
Organism: Leishmania donovani
Interaction partners:
Sequence:
MSAQSAASRWTNLAGIGSCHPRHHHYPTSTKEVQDAFELVRSQNGKCRVSGAGKSPNTATFTNEHLIHMERMNRILSIDTVAHTITCEAGAVMEEVMRSVDKVGLMVRCVPSYVRTTVGGCIATATHSSGIQCHCLSDYVRGLKIVDGCAQIRTLVAGKDDAELRLAACHLGVMGIITEVTLEVQPRIQWKLVSQPLLMKDATNAALVAENVRSTEYYRWWWVPHTDGCYESYGRVESKTGISALHPLPDAHTAQDDTTVQPSPAALPEKAAPAKSAERAGDRSTSRIVKSALKYTATDFVRHQVVEWSLWAACLYQAIQPYVNKAYRRVFFSALQVQRGSALECFTFDCLFKQWANEWAIDASRAVEAFNRMRDMIDREGMLLHFPVEFRFTAPDVSDMSPAVGRPTCWIGVVMYRPYGQEARDTRRCYDGFCRVMEEMGGRPHWAKYYDWGHREITATYGNHWERFRAVRRRMDPDDIFVNGWFRNLMSPDRVNSTACTP
Protein: Fad2 (EC 1.14.19.1) (Q9VTD4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Very long chain fatty acid elongase F
Sequence:
MPRNTKDTTGVLYESDVETVDGGLSTELSNRKTTDGSKLELVWVNIVLFVILHISSLYGVWLLFTSATWTTVVLFWPTVVVTILGVSGGAHRLWAHRTFKANTPLKLIFLFLNTLAFQDAVYYWARDHRVHHKYTETDADPYNSQRGWFFAHIGWLCCRKHPEVVEKGKQIDLSDLEADPLIMFQKKYYLLLMPIICFVLPTVLPMYLWGESLNVSWHVMALLRWCLSLNLIWTVNSSAHMHGMRPYDKNICPVDQGFLIFFRVGEGYHNYHHVFPWDYKSAELGKYSQDVTTKFIEFMAYLGWAYDLKSVSLDLVKQRVQRSGDGSHPVWGWGDKDQLKEDVGVTTITHQRNEK
Protein: Large ribosomal subunit protein mL59 (54S ribosomal protein L25, mitochondrial) (Q9UUJ5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL22m
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein uL14m
- Large ribosomal subunit protein mL38
- Small ribosomal subunit protein mS45
Sequence:
MPVFTKEALERLPIQLGNFFKKFPPENPNAWTTNPNRQNPFLATRNPQNGLVINPYYSNRRQAEIYKEARLQNLDNLLPQQMSWQKDSTRHILKGLLNPKGKISERKRDEILENRRLKLSESLKKTSKFKNERQKASKIAKPSPF
Protein: Tubby protein homolog 1 (Q09306)
Organism: Caenorhabditis elegans
Function: Has a role in fat regulation independent of daf-16. Implicated in ciliar sensory function which is required for normal sensory behavior such as chemotaxis. Required for extension and growth of sensory neuronal cilia during postembryonic development, potentially via mediating signaling protein transport and localization of PI(4,5)P2 to the ciliary base. Functions in life span control via the insulin/IGF-1 pathway. Thought to be involved in neuronal trafficking.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15790967, ECO:0000269|PubMed:16054097, ECO:0000269|PubMed:31259686}. Cell projection, axon {ECO:0000269|PubMed:16462744}. Cell projection, dendrite {ECO:0000269|PubMed:16462744}. Cell projection, cilium {ECO:0000269|PubMed:16462744, ECO:0000269|PubMed:31259686}. Note=Expressed in the periciliary membrane compartment in AWB and ASK sensory neurons. {ECO:0000269|PubMed:31259686}.
Interaction partners:
- Rab-GAP TBC domain-containing protein
- Cationic amino acid transporter C-terminal domain-containing protein
- Bridge-like lipid transfer protein family member 1 C-terminal domain-containing protein
- Trafficking protein particle complex subunit 11 domain-containing protein
- LiPid Depleted
- WD_REPEATS_REGION domain-containing protein
- Intraflagellar transport protein 122 homolog
- WD repeat-containing protein dyf-2
- Tetratricopeptide repeat protein 21 homolog
- Vacuolar protein sorting-associated protein 51 homolog
Sequence:
MTDTNSQWIEMNLQRQRKMLEDKQKQKRHQSAGSVRTTSTAMSMNSMKDYPTFDNSLPFSISDNSSVSVSMNTPLIPTQDPIAQPRMQSMPRQQPQQVQESLISIGDYPDNDINAKLSKVNLTSCVVSDDEDEDKRSYADSPWNTDVVADRIPSEVLPDYNFIKNNLAKFVEDPAVEHCLYKCSITRQKSGVDKGMFPTYFLHLEEFDTDKRQKIFLLAARKRKKSTTANYLLSTDPTNLSREGEGYCAKVRSNALGTQFTVYDSGQNPKKTTNHAAIRQELAAVIYETNVLGFKGPRKMTIVMPGIEPPTENRPAVRCPVRPIQDKHTLLERYRLNDLDSLKILSNKSPQWNDETQSYVLNFHGRVTQASVKNFQIIHQSSPEYIVMQFGRISDDEFTMDFRYPLSAVQAFGIAMTSFHGKLACE
Protein: Antitoxin VapB28 (P9WJ39)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin VapC28.
Interaction partners:
- Ribonuclease VapC28
- PE family protein PE12
- Uncharacterized protein
- Putative antitoxin VapB23
Sequence:
MALNIKDPSVHQAVKQIAKITGESQARAVATAVNERLARLRSDDLAARLLAIGHKTASRMSPEAKRLDHDALLYDERGLPA
Protein: Sperm-associated antigen 8 (E1BNS6)
Organism: Bos taurus (Bovine)
Function: Plays a role in spermatogenesis by enhancing the binding of CREM isoform tau to its coactivator FHL5 and increasing the FHL5-regulated transcriptional activation of CREM isoform tau (By similarity). Involved in the acrosome reaction and in binding of sperm to the zona pellucida (By similarity). Plays a role in regulation of the cell cycle by controlling progression through the G2/M phase, possibly by delaying the activation of CDK1 which is required for entry into mitosis. May play a role in fertility and microtubule formation through interaction with RANBP9 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3V0Q6}. Nucleus {ECO:0000250|UniProtKB:Q3V0Q6}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q99932}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q99932}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q99932}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37327785}. Note=In mature sperm cells, detected in the acrosomal region of the head and in the middle piece of the tail (By similarity). Localized to the nucleus and cytoplasm of spermatocytes and round spermatids while, in elongating spermatids, expressed in the cytoplasm but not in the nucleus (By similarity). During the cell cycle, localized on the microtubule-organizing center (MTOC) during prophase. In metaphase, extends along spindle microtubules. In anaphase, detected on the astral microtubules and mid-zone. In telophase, remains at the mid-zone. After cytokinesis, returns to the MTOC (By similarity). Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme (PubMed:34715025). {ECO:0000250|UniProtKB:Q3V0Q6, ECO:0000250|UniProtKB:Q99932, ECO:0000269|PubMed:34715025}.
Interaction partners:
- Protein Flattop
- Cilia- and flagella-associated protein 95
- EF-hand domain-containing family member C2
- Tektin-4
- EF-hand domain-containing protein 1
- Cilia- and flagella-associated protein 52
- Tektin-3
- Cilia- and flagella-associated protein 276
- Parkin coregulated gene protein
- Outer dynein arm-docking complex subunit 2
Sequence:
METSESTDRSQSRCLDLQPSSDGLGSSSDPFSSWDGRHRSALVAATAAASAAATAASTARAAALWTKSPAPYSHGNLLTEPSSDSLTERYTGPRFTHKISHGRLGFQPAYFSHIAWNPYTTNDLSSSRGPIPGSSSGPVPGSSSSPGPDSSSDPGPSSSSGPGGSPGGSGRGPGHGPGPGGGSGQGPGGGSGQGTDLGPAIDSRHSPGHGHGPRFNFSAPVGFRNPRGDLIPNYTGCKHHCHWEPQKQSWKFLKVSEPGARGLWKPPEVEGKSTVLSETLPRGQCLLYNWEEERATNYLDQVPVMQDGSESFFFRHGHRGLLTLQPQSPTSSCTTQKDSYQPPKSHCQPIRGKREAILEMLLRQQICKEVQAEQEPTRKDSEVESVTHHDYKKELVQAGPPAPTKIHDYHTEQPETFWLERAPQLPGVSNIRTLDTPFRKNCSFSTPVPLSLEQPLPFEPESYSQHGEISSLACQGGGQGGGGG
Protein: NTPase, isoform F (EC 3.6.1.42, EC 3.6.1.6, EC 3.6.1.64) (M9PBV2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- UMP-CMP kinase
- Adenylosuccinate synthetase
- GMP synthase
- Inosine triphosphate pyrophosphatase
- Uridine kinase
- Nucleoside diphosphate kinase
- AMP deaminase
- Inosine-5'-monophosphate dehydrogenase
- Adenine phosphoribosyltransferase
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11
Sequence:
MTNTDVRKRKLATDEKPPRRKSSGSPNASSGGNRGPSGLKISFLCLIISVILLLFVFGVYHLYYVKDEVPKVVLTKTSDFPTVTVPYAHVEPHFAPPVRRVITKKPIANKPTTDNDAGFVSENASPYLARLASKFGYSKVQYAAIIDAGSTGSRVLAYKFNRSFIDNKLVLYEELFKERKPGLSSFADNPAEGAHSIKLLLDEARAFIPKEHWSSTPLVLKATAGLRLLPASKAENILNAVRDLFAKSEFSVDMDAVEIMDGTDEGIFSWFTVNFLLGRLSKTNQAAALDLGGGSTQVTFSPTDPDQVPVYDKYMHEVVTSSKKINVFTHSYLGLGLMAARHAVFTHGYKKEDTVLESVCVNPIIANRTWTYGNVQYKVSGKENGKSSAEQPIVDFDACLELVKSKVMPLVKPKPFTLKQHAVAAFSYYFERAIESGLVDPLAGGETTVEAYRKKAQEICAIPNDEQPFMCFDLTFISTLLREGFGLNDGKKIKLYKKIDGHEISWALGCAYNVLTSDEKFSNS
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 13 (ADAM-TS 13) (ADAM-TS13) (ADAMTS-13) (EC 3.4.24.87) (von Willebrand factor-cleaving protease) (vWF-CP) (vWF-cleaving protease) (Q769J6)
Organism: Mus musculus (Mouse)
Function: Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation.
Subcellular location: Secreted {ECO:0000269|PubMed:15136581}. Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats. {ECO:0000250}.
Interaction partners:
- von Willebrand factor
- Coagulation factor VIII
- Platelet glycoprotein Ib alpha chain
- Inactive rhomboid protein 2
- Prothrombin
Sequence:
MSQLCLWLTCQPCYAVSVRGILTGAIFILGCWGLSDFQKSLLQDLEPKDVSSYFGHHAAPFTGHPPSHLQRLRRRRTLEDILHLELLVAVGPDVSRAHQEDTERYVLTNLNIGSELLRNPSLGVQFQVHLVKLITLSDSESTPNITANITSSLMSVCEWSQTINPHDDRDPSHADLILYITRFDLELPDGNQQVRGVTQLGGACSLSWSCLITEDTGFDLGVTIAHEIGHSFGLDHDGAPGSGSTCKASGHVMAADGATPTGGTLEWSACSQRQLQHLLSTGQMHCFQDPPGLQSGLTRHQLMAQPGLYYSADDQCRVAFGSGAVACTFSREGLDVCQALSCHTDPLDQSSCSRLLVPLLDGTECGVEKWCSKARCRSLAELAPVAAVHGHWSSWGPHSPCSRSCGGGVITRRRWCNNPRPAFGGRACVGEDLQAKMCNTQACEKTQLEFMSEQCAQTDRQPLQLSQGTASFYHWDAAVQYSQGDTLCRHMCWAVGESFIVSRGDRFLDGTRCVPSGPQDDGTLSLCLLGSCRTFGCDGRMDSQKVWDACQVCGGDNSTCSSRNGSFTAGRAREYVTFLIVTPNMTNAHIVNRRPLFTHLAVRIQGHYIVAGKTSISPNTTYPSLLEDYRVEYRVTLTEDQLPHLEEIHIRGPVRDDIEIQVYRRYGGEYGDLTHPDITFSYFQLKQQAAWVWTAKRGPCSVSCGAGLRWVTYSCQDQAQDKWVKNAQCQGSPQPPAWQEPCVSAPCSPYWVAGDFSPCSVSCGGGLRERSLRCVETQDGFLKTLPPARCRAVAQQPAAEVENCNSQPCPTRWEVSDPGPCMSSACEAGLDSRNVTCVSRAGDPEKPETAGPCRTDEMSAMLEPCSRSLCSPGLGQVDNTMSLGEEAPSPVGSDKPGAQAEHVWTPLVGLCSISCGRGLKELYFLCMDSVLKMPVQEELCGLASKPPSRWEVCRARPCPARWETQVLAPCPVTCGGGRVPLSVRCVQLDRGHPISVPHSKCSPVPKPGSFEDCSPEPCPARWKVLSLGPCSASCGLGTATQMVACMQLDQGHDNEVNETFCKALVRPQASVPCLIADCAFRWHISAWTECSVSCGDGIQRRHDTCLGPQAQVPVPANFCQHLPKPMTVRGCWAGPCAGQETSSSLPHKEATLPSQTQAAATVASLQWSQPRARTPTLFSASQSLGLQENLEEHGACGRQYLEPTGTIHMRDQGRLDCVVAIGRPLGEVVTLQILESSLKCSAGEQLLLWGRFTWRKTCRKMPGMTFSTKTNTVVVKQHRVLPGGGVLLRYWSQPAPGTFYKECDRQLFGPRGEIVSPSLSPDGRKAGTCRVFISVAPQARIAIRALASDMGTASEGTNANYVSIRDIHSLRTTTFWGQQVLYWESEGSEAELEFSPGFLEAHASLQGEYWTISPRTSEQDDSLALS