wanglab/gogpt-training-data huggingface dataset:
Protein: Slit-2 (Q90XG2)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
NEFSVLEATGIFKKLXQLRKINLSNNKITDIEEGAFDGASGVNELLLTSNRLETVRDKMFKGLESLKTLMLRSNRVSCVGNDSFTGLSSVRLLSLYDNQITTVAPGSFDTLHSLSTLNLLANPFNCNCHLAWLGDWLRKKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTCDDGNDDNSCSPLSRCPAECTCLDTVVRCSNKGLKALPKGIPKDVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPARTFDGLKSLRLLSLHGNDISVVPEGAFNDLSALSHLAIGANPLYCDCNMQWLSDWVKSEYKEPGIARCAGPGEMADKLLLTTPSKKFTCQGPVDVNILAKCNPCLSNPCKNDGTCNNDPVDFYRCTCPYGFKGQDCDIPIHACISNPCNHGGTCHLKEGEKDGFWCTCADGFEGENCEINVDDCEDNDCENNSTCVDGINNYTCLCPPEYTGELCEEKLDFCAQNLNPCQHDSKCILTPKGYKCDCTPGYVGEHCDIDFDDCQDNKCKNGAQCTDAVNGYTCICPEGYSGLFCEFSPPMVLPRTSPCDNYECQNGAQCIVKESEPICQCLSGYQGEKCEKLISINFVNKESYLQIPSAKIHSQTNITLQIATDEDSGILLYKGDKDHIAVELYRGRVRVSYDTGSYPASAIYSVETINDGNFHIVELLAMDQILSLSIDGGSPKIITNLSKQSTLNFDSPLYVGGMPVKNNIAALRQSPGQNGTSFHGCIRNLYINSELQDFQKWPL
Protein: Cytochrome b6/f complex 12.6 kDa peptide (P83688)
Organism: Euglena gracilis
Function: May be a component of the cytochrome b6/f complex which is part of the photosynthetic respiratory chain.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12837550}.
Interaction partners:
Sequence:
SGSGVRSAKKGGKAQGGQAGVGYKGSTEPG
Protein: U1-type domain-containing protein (Q8BKW5)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMASFQRSNSHDKVRRIVAEEGRTARNLIAWSVPLESKDDDGKPKCQTGGKSKRTIQGTHKTTKQNTAVECKITSTTGEKHFDKSPTKTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDYYVRDFKALIDWIQLQEKLEKTDAQSRPTSLAWEVKKMSPGRHVIQSPSTDRMNVTSTARRSLNFGSLPGAVTAPCLAPTGVSWADKVKAHHTGSAPPEATPAQSCAPMTVQKTSRKNERKDAEGWETVQRGRPVRSRSTAVIPKVSLVTETLRSKDDSDKENICLLPEESIQKGKLEDRCSTVESLSKDSLLHSSDHPLSERTQFTVCILDDVKNSGSSQDSSVHTSEIPAIDSDAVCVAPQNTTALPTDRVPAETTGMVTEMTDPSDISNVSAADWSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGSGSLSFCGVSLDWNDVLADYEARESWRQNTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKKQCSLCNVLIASGVYLFSHIKGKKHQQAVRENSSIQGRELSDEEVEHLSLKKYVVDIVIESAAPPEPVKDGEER
Protein: B3 domain-containing protein At5g60142 (Q9LST3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326}.
Interaction partners:
- Transcription factor STKL1
- Transcription factor
- Probable transcription factor At3g04930
- Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 6
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Sequence-specific DNA binding transcription factor
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS21y
Sequence:
MMNRGISVDDCLPKFFKVYLPDDSGDDLELPISFNSFLPKSLPKNVIVRSIYGNIWKVAFRKFCGDSERFVMVNGWKKIVKDEDLKGGEFLEFEFDGSWCFNFCIYGRATCKRLRSSVQITVLDDNDDGFNDDQDYGEEVKSSENFIVLDDDDISDVQDYNEEDTSSEDITALDDADNDDINDVQDYVEEDTSSEDIIVIDDDDDDDDQDYGDDDHADVEKERWRGVKTEKKKKGSSGEHDRQYLDNHMNPFFTVNQHRQIKYNMLRIPTKVITKYGLHFPEFINLIDPLEKNFGKLKRKVKGQTIKGFRSIIRRNNVKLNDKVICELEKEMDGLVREIKVHVIRG
Protein: Achaete-scute homolog 2 (Mash2) (P19360)
Organism: Rattus norvegicus (Rat)
Function: AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:12196582}. Cytoplasm {ECO:0000269|PubMed:12196582}.
Interaction partners:
- WD repeat-containing protein 5
- Transcription factor E2-alpha
- Leucine-rich repeat-containing G-protein coupled receptor 5
- Retinoblastoma-binding protein 5
- Olfactomedin 4
Sequence:
MESHFNWYGVPRLQKASDACPRESCSSALPEAREGANVHFPPHPVPREHFSCGAPKPVAGAPALNASLMDGGALPRLVPTSSGVAGACTARRRPPSPELLRCSRRRRSGATEASSSSAAVARRNERERNRVKLVNLGFQALRQHVPHGGANKKLSKVETLRSAVEYIRALQRLLAEHDAVRAALSGGLLTPATRPSDVCTQPSASPASASLSCTSTSPDRLGCSEPASPRSAYSSEDSSCEGETYPMGQMFDFSNWLGGY
Protein: Cytochrome b translation regulator cbp8 (Q10302)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:34634819}.
Interaction partners:
- Mitochondrial translation ATP-dependent RNA helicase mrh5
- Mitochondrial translation factor sls1
- Cytochrome b translation regulator cbp7
- Small ribosomal subunit protein L51-b
- Pentatricopeptide repeat-containing protein 7
- CBP3-like protein
- Mitochondrial cox1 translation regulator ppr4
- Cytochrome B pre-mRNA-processing protein 6
Sequence:
MLKTLSKVSKNLSNTSAFLVKSKPLYISFCTCKAYFEDNTSLSRRFFSAKKSLQFKSLIRKYSEDSTLAWRDYENYNDDDLLYQRELSEIYNKCLKALHPFYPVFEVNSNLYYQLLMFTNYSNPKDNGFSKLLFSQYSDEKKVLVNFVYNVLRLDPDLQRQKRILESIISAALNICVSTVNLSRTDLKSSLKIILQTIDLFKYDSSFSSIYFRKDGPYHKVEKLLKSANIRSSLNSKTFNDFRTLFLLLIRDYSLFHGNSSHCMLANSMLPPSIAFSKMEKAEIFLRLRAFFQLMEHIDNERITPSEQFLDKVFISLLSAKNSCSLKMWLIHSFNKGWPVKIEFFVSFFKNFSNIVEGSMEVYSAYLHIIRDHYNLSDLADVQAIFLSRFILLRKKEDCKKLLEHVLPIRQLFLLNCYSLLNVLANYVVVFKDRLIFQEINQNWEEHKGQIPENFIFSLLKMFGEMQENQGFLNACIYYINKKKNLNEVSRYKINLLLLQGVNSFEVKDFYRKRGIEIMPKNLPRFFCYCLKKNKLSYALKYIRLSGLQFDYIVDCFRNSSDWTRTLISILSKKMGTEFAIRFLKIISFPLLSNDKVLREIEFFAIHEVNFRSLKWVADQQLRILPGWSSRPQKATFPLCTVHLKK
Protein: Histone deacetylase complex subunit SAP18 (18 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p18) (O55128)
Organism: Mus musculus (Mouse)
Function: Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. 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 mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O00422}. Cytoplasm {ECO:0000250|UniProtKB:O00422}. Nucleus speckle {ECO:0000250|UniProtKB:O00422}. Note=Shuttles between the nucleus and the cytoplasm (By similarity). Colocalizes with ACIN1 and SRSF2 in nuclear speckles (By similarity). {ECO:0000250|UniProtKB:O00422}.
Interaction partners:
- Histone deacetylase complex subunit SAP30
- RNA-binding protein with serine-rich domain 1
- Paired amphipathic helix protein Sin3a
- Sin3 histone deacetylase corepressor complex component SDS3
- Histone-binding protein RBBP4
- Apoptotic chromatin condensation inducer in the nucleus
- Histone deacetylase 1
- Histone-binding protein RBBP7
- Histone deacetylase 2
- Pinin
Sequence:
MAVESRVTQEEIKKEPEKPIDREKTCPLLLRVFTTNNGRHHRMDEFSRGNVPSSELQIYTWMDATLKELTSLVKEVYPEARKKGTHFNFAIVFMDLKRPGYRVKEIGSTMSGRKGTDDSMTLQSQKFQIGDYLDIAITPPNRAPPSSGRMRPY
Protein: Solute carrier family 7 (Cationic amino acid transporter, y+ system), member 5, isoform CRA_b (Solute carrier family 7 member 5) (A0A0C4DGL4)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET
Protein: Uncharacterized hydrolase C22A12.06c (EC 3.1.-.-) (O13897)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum and cell tip.
Interaction partners:
Sequence:
MKSATKSKILCIHGYAESGELFSVKLRALRERMADSVDFYFPTGPIELDKAKDELNGSGFDALSTVFSSSPASHRRGWWRINEYADTKQLEPTKAFEYLASYIKEHGPFDGILGFSQGTNLAANLAALVTIPKYQEYFSQPPFRFALFFSGYFRPLLMDGAVHATKLDLPTLHLLGKYDTVLSTETSTTLVRACKDAQVLFHPAAHQIPAPHAYVEPAADFIDFFSREDWPIISKHISLIVPTKKVNTTSAQTSLNNVEHDLISKIMSRSFKGGINVVVSDLQMFNEYKRIFGPKVLSLVVTDGQEPDTYSENVHYTPNFKGALAYLEAYQNSIGRIYVIGDKKLLTLGMLCRCTKRIIAITDAEDKFISQSSAQQVSGSLPFLEHSKEWLKAKSSQIRQWTGQSRLKHMSQDNSGEPVTMKLQMWERL
Protein: Threonylcarbamoyl-AMP synthase (TC-AMP synthase) (EC 2.7.7.87) (L-threonylcarbamoyladenylate synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein Sua5) (tRNA threonylcarbamoyladenosine biosynthesis protein Sua5) (Q970S6)
Organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (By similarity). Probably catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Shows ATP hydrolysis activity in vitro, producing AMP.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Biotin protein ligase
- tRNA N6-adenosine threonylcarbamoyltransferase
- Serine hydroxymethyltransferase
- Glutamine--fructose-6-phosphate aminotransferase
- Methyltransferase
- Molybdopterin converting factor
- 2-isopropylmalate synthase
- rRNA methyltransferase
Sequence:
MTQIIKIDPLNPEIDKIKIAADVIRNGGTVAFPTETVYGLGANAFDGNACLKIFQAKNRPVDNPLIVHIADFNQLFEVAKDIPDKVLEIAQIVWPGPLTFVLKKTERVPKEVTAGLDTVAVRMPAHPIALQLIRESGVPIAAPSANLATRPSPTKAEDVIVDLNGRVDVIIDGGHTFFGVESTIINVTVEPPVLLRPGPFTIEELKKLFGEIVIPEFAQGKKEAEIALAPGMKYKHYAPNTRLLLVENRNIFKDVVSLLSKKYKVALLIPKELSKEFEGLQQIILGSDENLYEVARNLFDSFRELDKLNVDLGIMIGFPERGIGFAIMNRARKASGFSIIKAISDVYKYVNI
Protein: Ac2-120 (Coagulation factor V) (Q7TPK2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MQSSEGQVQEKQAEIRRSDKNHVGAFLYVPLYVFHDLEYKQFQTYPSLGLLGPTLYAEVGDTIKVHFRNKADKPLSIHPQGIRYSKFSEAQLFAEEEMDFAAPFILLRCLFDPPSLSQQALVLLPKRKTGFYVTPLLLEGVPGVHRLSMGLYTMKRGIFTLGQTGFMCPRSRLHAGAGCGDRRGGEEPERASASPFLHTGEWWKTLDVFVAVTSPGASYLDHTSPAERKDDAVAAGEEYTYEWFIGEDSGPTPDDPPCLTHIYYSYENLTQDFNSGLIGPLLICKEGTLTEDGTQKMFDKQHVLLFAVFDESKSWSQSPALMYTVNGFVNRTMPDVTVCAYDHVSWHLIGMSSGPELFSIHFNGQVLEQNQHKVSTVTLLQTVGIFIRPIALNTVQGYIASRGEDLLVPWATRAAGMQAYIDIKNCPKKTRSSKTLTREQRRHMKRWEYFIAAEEVIWNYAPVIPANMDKHSYPLSPMGMWPDDSNRNNGSRMLATVNPCSRCLLRLSHQFYKLGAILVFLYLREGARKSEALVVRHMPFLRVADMEQEVVFAMFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMNTINGYVPESISTLGFCFDDAVQWHFCSVGTHDDILTVHFTGHSFIYGRRHEDTLTLFPMSGESVTVVMDNIGTWMLTTMSSNPRRRNLRLRFRDVKCNRNDDDDEDSYEIYQPLEPTSMTTRKIHDSVENDFGIENEDDDYQYELASTLGIRSFRKSLLNPKEDEFNLTALALENSSEFISLSTDGVVDSKSSRNLSKITNNNLNDSQRTLSGSGATIAGILLGNLTGLGKNSVLNPSTEYHSSSYYENDMEDPQSNITVVYLLPLGAKGSGSREQTKPKTIKTGRPHRMKHRFSWMKAPAGKTGRHSNPKNTSSRMKSEEDIPSDLLLLKQKVASKLLNRQWHMASEKGSYEIIPANGENTDIDKLTNSPQNQNISTPWGASTSRINTTGKPSNLPTFSRFRHKSPHVRQEEESGDFKKRQLFIRTRKKKKNRKRLLNHSLLLHKSNETALSTDLNQTSPPVSTDRSLPDYNQNPSNDTEQMSSSLDLFQSVPPEEHSPTFPTQDPNQTHSTTDPSYRSSPPEPSQGIDYDLSHEFYSDDISQTSFFPDQSQKSPLTSDDGQAIPSSDLNLFTISPELDQTIIYPDLDQLFLSPDDIQKTSSQDLGQVTLSPDENQETSSQDLGQVTLSPNENQETSSQDLGQVTLSPDDIQETSSQDLGQVTLSPDENQETSSPDLGQVPLTPDDNQKTSPDLGQVLLSLDDKQKTYFLDPGQVPISSDQSWETSSTDLSLLTLSPKFGQTVISPDLDKMPLSSDNSQVTLSPDLSLLTLSPDFNEIILSPDIDQVTLSPDLIQTSPALNHRHKTSSADPGQASYPPDSGQSSPLPELNQTLPHPDLIHMQPPLLSPTPNDTSLSKTFNPLVVVGLSRVDGDDVEMIPSEELESIDEDYPEDDYVTYNDPYKTDTRANVNSSRNPDTIAAWYLRSFGGNKKFYYIAAEEISWDYSKFAPSEMDNEETDNTPKDTTYKKVVFRKYLDSTFTSRDPQGEYEEHLGILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKNYEDDSPKWFQEDDAVQPNSSYTYVWHATERAGPENPGSACRAWVYYSAVDVERDIHSGLIGPLLICRKGTLDRASNLPLDMREFVLLFMVFDEKKSWYYEKSKGSWRIESPEAKNSHEFYAINGMIYNLPGLRMYEQEWVRLYLLNMGGPQDIHVVHFHGQILLDNRTKQHHLGVWPLLPECKMPMGLSTGAISDSQIKASEYLSCLGGHARGLTDPVWYSMSPDKIPRSFLIPRLLPKEKYSNAESLSVIIVQTTLSLFLLVLYSFAGNSDASTIKENRFDPPIVARYIRIHPTKSYNRPTLRLELLGCEVNGCSTPLGLEDGRIQNKQITASSFKKSWWGSYWEPSLARLNAQGRVNAWQAKANNNKQWLQIDLLKIKKVTAIVTQGCKSLSSEMYVKSYSILYSDQGVSWKPYRQKSSMVDKIFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWNQSIALRLELFGCDIY
Protein: Developmentally-regulated GTP-binding protein 1 (DRG-1) (Neural precursor cell expressed developmentally down-regulated protein 3) (NEDD-3) (Translation factor GTPase DRG1) (TRAFAC GTPase DRG1) (EC 3.6.5.-) (P32233)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. Appears to have an intrinsic GTPase activity that is stimulated by ZC3H15/DFRP1 binding likely by increasing the affinity for the potassium ions. When hydroxylated at C-3 of 'Lys-22' by JMJD7, may bind to RNA and play a role in translation. Binds to microtubules and promotes microtubule polymerization and bundling that are required for mitotic spindle assembly during prophase to anaphase transition. GTPase activity is not necessary for these microtubule-related functions.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y295}. Cytoplasm {ECO:0000269|PubMed:1280421}. Note=The DRG1-DFRP2/ZC3H15 complex associates with polysomes. {ECO:0000250|UniProtKB:Q9Y295}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 15
- RWD domain-containing protein 1
- COP9 signalosome complex subunit 3
- 26S proteasome regulatory subunit 8
- 26S proteasome regulatory subunit 6B
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS3
- DNA polymerase epsilon subunit 2
Sequence:
MSGTLAKIAEIEAEMARTQKNKATAHHLGLLKARLAKLRRELITPKGGGGGGPGEGFDVAKTGDARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLILIVLDVLKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKGGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNRVYIPCIYVLNKIDQISIEELDIIYKVPHCVPISAHHRWNFDDLLEKIWDYLKLVRIYTKPKGQLPDYTSPVVLPYSRTTVEDFCMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVKK
Protein: Neurochondrin (Q9UBB6)
Organism: Homo sapiens (Human)
Function: Probably involved in signal transduction in the nervous system, via increasing cell surface localization of GRM5/mGluR5 and positively regulating its signaling. Required for the spatial learning process. Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play a role in modulating melanin-concentrating hormone-mediated functions via its interaction with MCHR1 that interferes with G protein-coupled signal transduction. May be involved in bone metabolism. May also be involved in neurite outgrowth (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23687301}. Endosome membrane {ECO:0000250|UniProtKB:O35095}; Lipid-anchor {ECO:0000305|PubMed:23687301}. Cell projection, dendrite {ECO:0000250|UniProtKB:O35095}. Postsynapse {ECO:0000250|UniProtKB:O35095}. Note=Localizes to somatic regions of neurons. Localization to endosome membrane requires palmitoylation. {ECO:0000250|UniProtKB:O35095}.
Interaction partners:
- Protein AAR2 homolog
- Glutamate receptor ionotropic, kainate 1
- Metabotropic glutamate receptor 5
- Protein TAMALIN
- Glutamate receptor 4
- Tetratricopeptide repeat protein 27
- E2F-associated phosphoprotein
- Zinc finger HIT domain-containing protein 2
Sequence:
MSCCDLAAAGQLGKASIMASDCEPALNQAEGRNPTLERYLGALREAKNDSEQFAALLLVTKAVKAGDIDAKTRRRIFDAVGFTFPNRLLTTKEAPDGCPDHVLRALGVALLACFCSDPELAAHPQVLNKIPILSTFLTARGDPDDAARRSMIDDTYQCLTAVAGTPRGPRHLIAGGTVSALCQAYLGHGYGFDQALALLVGLLAAAETQCWKEAEPDLLAVLRGLSEDFQKAEDASKFELCQLLPLFLPPTTVPPECYRDLQAGLARILGSKLSSWQRNPALKLAARLAHACGSDWIPAGSSGSKFLALLVNLACVEVRLALEETGTEVKEDVVTACYALMELGIQECTRCEQSLLKEPQKVQLVSVMKEAIGAVIHYLLQVGSEKQKEPFVFASVRILGAWLAEETSSLRKEVCQLLPFLVRYAKTLYEEAEEANDLSQQVANLAISPTTPGPTWPGDALRLLLPGWCHLTVEDGPREILIKEGAPSLLCKYFLQQWELTSPGHDTSVLPDSVEIGLQTCCHIFLNLVVTAPGLIKRDACFTSLMNTLMTSLPALVQQQGRLLLAANVATLGLLMARLLSTSPALQGTPASRGFFAAAILFLSQSHVARATPGSDQAVLALSPEYEGIWADLQELWFLGMQAFTGCVPLLPWLAPAALRSRWPQELLQLLGSVSPNSVKPEMVAAYQGVLVELARANRLCREAMRLQAGEETASHYRMAALEQCLSEP
Protein: Pantothenate kinase 2 (EC 2.7.1.33) (B8A4W8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Phosphopantothenoylcysteine decarboxylase.
- Bifunctional coenzyme A synthase
- Phosphopantothenoylcysteine synthetase.
- Pantothenate kinase 1b.
- pantothenate kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase 1
- WD repeat domain phosphoinositide-interacting protein 4
- DDB1- and CUL4-associated factor 17
- RALBP1-associated Eps domain-containing 1
- Phospholipase A2, group VI.
Sequence:
MELNGFHCEGEGCTEKQEEESTALKLPRSKTDASCSMIATAAPDGEAAGGSALRERRVSESMPAMLRLDSLKKNRPPFPWFGMDIGGTLVKLVYFEPKDITAEEEQEEVESLKSIRRFLTSHTAYGKTGIRDVHLELLDLTLWGRKGSLHFIRFSTHELPAFLQMGRNKHFSSLHTALCATGGGAFKYEEDFRTMANLKLFKLDELECLIKGVLYIDSVVSSGLSECYYFEHPTDPELCEQKAYNLENPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCSTFEEALAMATEGESTRVDKLVREIYGGDYERFGLPGWAVASSFGNMMCKEKRESVSKEDLARATLVTITNNIGSITRMCALNENIKRVVFVGNFLRVNTLSMKLLAYALDYWSKGQLKALFLRHEGYFGAVGALLELPNPS
Protein: Probable peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (Rotamase B) (P9WHW1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Interaction partners:
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Phthioceranic/hydroxyphthioceranic acid synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Mycoketide-CoA synthase
- Mycocerosic acid synthase-like polyketide synthase
- Chaperone protein HtpG
- RNA helicase
- ATP-dependent RNA helicase DeaD
- Probable polyketide synthase Pks17
- Chaperone protein DnaJ 2
Sequence:
MGHLTPVAAPRLACAFVPTNAQRRATAKRKLERQLERRAKQAKRRRILTIVGGSLAAVAVIVAVVVTVVVNKDDHQSTTSATPTDSASTSPPQAATAPPLPPFKPSANLGANCQYPPSPDKAVKPVKLPRTGKVPTDPAQVSVSMVTNQGNIGLMLANNESPCTVNSFVSLAQQGFFKGTTCHRLTTSPMLAVLQCGDPKGDGTGGPGYQFANEYPTDQYSANDPKLNEPVIYPRGTLAMANAGPNTNSSQFFMVYRDSKLPPQYTVFGTIQADGLTTLDKIAKAGVAGGGEDGKPATEVTITSVLLD
Protein: Tumor necrosis factor ligand superfamily member 6 (Apoptosis antigen ligand) (APTL) (CD95 ligand) (CD95-L) (Fas antigen ligand) (Fas ligand) (FasL) (CD antigen CD178) [Cleaved into: Tumor necrosis factor ligand superfamily member 6, membrane form; Tumor necrosis factor ligand superfamily member 6, soluble form (Receptor-binding FasL ectodomain) (Soluble Fas ligand) (sFasL); ADAM10-processed FasL form (APL); FasL intracellular domain (FasL ICD) (SPPL2A-processed FasL form) (SPA)] (P48023)
Organism: Homo sapiens (Human)
Function: Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development. Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses (By similarity). TNFRSF6/FAS-mediated apoptosis has also a role in the induction of peripheral tolerance (By similarity). Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:9427603}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:17164290}. Lysosome lumen {ECO:0000269|PubMed:17164290}. Note=Is internalized into multivesicular bodies of secretory lysosomes after phosphorylation by FGR and monoubiquitination (PubMed:17164290). Colocalizes with the SPPL2A protease at the cell membrane (PubMed:17557115). {ECO:0000269|PubMed:17164290, ECO:0000269|PubMed:17557115}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 6, soluble form]: Secreted {ECO:0000269|PubMed:9427603}. Note=May be released into the extracellular fluid by cleavage from the cell surface. {ECO:0000269|PubMed:9427603}.; SUBCELLULAR LOCATION: [FasL intracellular domain]: Nucleus {ECO:0000269|PubMed:17557115}. Note=The FasL ICD cytoplasmic form is translocated into the nucleus. {ECO:0000269|PubMed:17557115}.
Interaction partners:
- FAS-associated death domain protein
- Tumor necrosis factor receptor superfamily member 6
- Tumor necrosis factor receptor superfamily member 10B
- Tumor necrosis factor receptor superfamily member 6B
- Caspase-8
- Tumor necrosis factor receptor superfamily member 10A
- Tumor necrosis factor receptor superfamily member 1A
- Perforin-1
- Tumor necrosis factor receptor superfamily member 25
- Tumor necrosis factor
Sequence:
MQQPFNYPYPQIYWVDSSASSPWAPPGTVLPCPTSVPRRPGQRRPPPPPPPPPLPPPPPPPPLPPLPLPPLKKRGNHSTGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELAELRESTSQMHTASSLEKQIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKMMSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLYKL
Protein: At5g18910 (Protein kinase superfamily protein) (Q8GXZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ras-related protein RABH1d
- CRIB domain-containing protein RIC1
- Type I inositol polyphosphate 5-phosphatase 5
- Adenine nucleotide alpha hydrolases-like superfamily protein
- Serine protease inhibitor
- Rop guanine nucleotide exchange factor 4
- Serine protease inhibitor
- Probable non-inhibitory serpin-Z5
- Serine protease inhibitor
- Serine protease inhibitor
Sequence:
MEGLRDSSSQTISSTTSSSSSPSCDVDVDNRGKQLTPSTRRSRAGFSDSFSSHDLSSFCRDEEVKTFCPIKSESDDELLRSIEAETSSSVVSTSDSSETHHHHHHHHSSGGPNNGHWRRGFFRLLKKGSSAMPFNTFTPLKGVPKLTRRKSKRIRDNMVPVIPALDTDHLFYFKPSWRNFSLRDIQTATNDYSRENLIGEGGYAEVYKGQMADGQIVAIKKLTRGSAEEMTMDYLSELGIIVHVDHPNIAKLIGYCVEGGMHLVLELSPNGSLASLLYEAKEKLNWSMRYKVAMGTAEGLYYLHEGCQRRIIHKDIKASNILLTQNFEAQISDFGLAKWLPDQWTHHTVSKVEGTFGYLPPEFFMHGIVDEKTDVYAYGVLLLELITGRQALDSSQHSIVMWAKPLIKENKIKQLVDPILEDDYDVEELDRLVFIASLCIHQTSMNRPQMSQVVEILRGDKCSLDKLRERENSKLQRTYSEELLDNEEYNSTRYLNDINRHMETVLGTSKD
Protein: Dehydrodolichyl diphosphate synthase 2 (Dedol-PP synthase 2) (EC 2.5.1.-) (Q56Y11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for the biosynthesis of several classes of glycoprotein.
Interaction partners:
- Geranylgeranyl pyrophosphate synthase 12, chloroplastic
- Geranylgeranyl pyrophosphate synthase 10, mitochondrial
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
- Geranylgeranyl pyrophosphate synthase 3, chloroplastic
- Farnesyl pyrophosphate synthase 2
- Farnesyl pyrophosphate synthase 1, mitochondrial
- Geranylgeranyl pyrophosphate synthase 4
- Putative geranylgeranyl pyrophosphate synthase 8, chloroplastic
- Geranylgeranyl pyrophosphate synthase 7, chloroplastic
Sequence:
MLSLRVPTPTSFDFRRYQAGDLERRWRLSRDSFLSFSPKFEENRGFRFGVKSSKSDVSFTAAEEEETLPEELHAELMPKHVAIIMDGNGRWAKNRGLQPWDGHRAGVEALKEIVELCGKWGIQVLTVFAFSTDNWIRPRIEIDFLFSLFERSLKTEFQNLAKNNVRISIIGDSSKLPKSLLRVINEVEEVTKNNTRLQLIVAVGYSGKYDVLQACRGIARRVKDGEIEVEEIDERLIEEELETNCTEFPYPDLLIRTSGELRVSNFLLWQLAYTELFFAQELWPDFGRSGFIEALMSFQQRQRRFGGRKS