wanglab/gogpt-training-data huggingface dataset:
Protein: PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component (EIIBC-Asc) (EII-Asc) [Includes: Arbutin-, cellobiose-, and salicin-specific phosphotransferase enzyme IIB component (EC 2.7.1.-) (PTS system arbutin-, cellobiose-, and salicin-specific EIIB component); Arbutin, cellobiose, and salicin permease IIC component (PTS system arbutin-, cellobiose-, and salicin-specific EIIC component)] (P24241)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in arbutin, cellobiose, and salicin transport.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00426, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00426, ECO:0000269|PubMed:15919996}.
Interaction partners:
- 6-phospho-beta-glucosidase AscB
- PTS system glucose-specific EIIA component
- 6-phospho-beta-glucosidase BglB
- 6-phospho-beta-glucosidase
- 6-phospho-beta-glucosidase BglA
- HTH-type transcriptional regulator AscG
- Phosphocarrier protein HPr
- Cryptic beta-glucoside bgl operon antiterminator
- PTS system N,N'-diacetylchitobiose-specific EIIA component
- PTS system N,N'-diacetylchitobiose-specific EIIB component
Sequence:
MAKNYAALARSVIAALGGVDNISAVTHCMTRLRFVIKDDALIDSPTLKTIPGVLGVVRSDNQCQVIIGNTVSQAFQEVVSLLPGDMQPAQPVGKPKLTLRRIGAGILDALIGTMSPLIPAIIGGSMVKLLAMILEMSGVLTKGSPTLTILNVIGDGAFFFLPLMVAASAAIKFKTNMSLAIAIAGVLVHPSFIELMAKAAQGEHVEFALIPVTAVKYTYTVIPALVMTWCLSYIERWVDSITPAVTKNFLKPMLIVLIAAPLAILLIGPIGIWIGSAISALVYTIHGYLGWLSVAIMGALWPLLVMTGMHRVFTPTIIQTIAETGKEGMVMPSEIGANLSLGGSSLAVAWKTKNPELRQTALAAAASAIMAGISEPALYGVAIRLKRPLIASLISGFICGAVAGMAGLASHSMAAPGLFTSVQFFDPANPMSIVWVFAVMALAVVLSFILTLLLGFEDIPVEEAAAQARKYQSVQPTVAKEVSLN
Protein: 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 (EC 2.5.1.108) (Diphthamide biosynthesis protein 1) (Diphtheria toxin resistance protein 1) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1) (I3L1H5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAALVVSGAAEQGGRDGPGRGRAPRGRVANQIPPEILKNPQLQAAIRVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGADFLVHYGHSCLIPMDTSAQDFRVLYVFVDIRIDTTHLLDSLRLTFPPATALALAAAQELKAEYRVSVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNVPAYRYDPYSKVLSREHYDHQRMQAARQEAIATARSAKSWGLILGTLGRQGSPKILEHLESRLRALGLSFVRLLLSEIFPSKLSLLPEVDVWVQVACPRLSIDWGTAFPKPLLTPYEAAVALRDISWQQPYPMDFYAGSSLGPWTVNHGQDRRPHAPGRPARGKVQEGSARPPSAVACEDCSCRDEKVAPLAP
Protein: 3-ketoacyl-CoA synthase 6 (KCS-6) (EC 2.3.1.199) (Cuticular protein 1) (Eceriferum 6) (Very long-chain fatty acid condensing enzyme 6) (VLCFA condensing enzyme 6) (Q9XF43)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to cuticular wax and suberin biosynthesis. Involved in both decarbonylation and acyl-reduction wax synthesis pathways. Required for elongation of C24 fatty acids, an essential step of the cuticular wax production. Major condensing enzyme for stem wax and pollen coat lipid biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12467640, ECO:0000269|PubMed:18465198}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Very-long-chain
- Very-long-chain enoyl-CoA reductase
- Protein ECERIFERUM 2
- Protein ECERIFERUM 26-like
- 3-ketoacyl-CoA synthase 9
- 3-ketoacyl-CoA synthase 2
- ABC transporter G family member 12
- Very-long-chain aldehyde decarbonylase CER1
- Very-long-chain aldehyde decarbonylase CER3
Sequence:
MPQAPMPEFSSSVKLKYVKLGYQYLVNHFLSFLLIPIMAIVAVELLRMGPEEILNVWNSLQFDLVQVLCSSFFVIFISTVYFMSKPRTIYLVDYSCYKPPVTCRVPFATFMEHSRLILKDKPKSVEFQMRILERSGLGEETCLPPAIHYIPPTPTMDAARSEAQMVIFEAMDDLFKKTGLKPKDVDILIVNCSLFSPTPSLSAMVINKYKLRSNIKSFNLSGMGCSAGLISVDLARDLLQVHPNSNAIIVSTEIITPNYYQGNERAMLLPNCLFRMGAAAIHMSNRRSDRWRAKYKLSHLVRTHRGADDKSFYCVYEQEDKEGHVGINLSKDLMAIAGEALKANITTIGPLVLPASEQLLFLTSLIGRKIFNPKWKPYIPDFKLAFEHFCIHAGGRAVIDELQKNLQLSGEHVEASRMTLHRFGNTSSSSLWYELSYIESKGRMRRGDRVWQIAFGSGFKCNSAVWKCNRTIKTPKDGPWSDCIDRYPVFIPEVVKL
Protein: Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (EC 3.1.3.36) (Inositol polyphosphate 5-phosphatase J) (Phosphatidylinositol 1,3,4,5-tetrakisphosphate 5-phosphatase) (EC 3.1.3.56) (Phosphatidylinositol 1,4,5-trisphosphate 5-phosphatase) (EC 3.1.3.56) (P59644)
Organism: Mus musculus (Mouse)
Function: Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12536145}. Note=Predominantly localized to membrane ruffles.
Interaction partners:
- Inositol polyphosphate-5-phosphatase A.
- Inositol polyphosphate 1-phosphatase
- Inositol-tetrakisphosphate 1-kinase
- Inositol polyphosphate multikinase
- Kinase
- Inositol-trisphosphate 3-kinase A
- Inositol-trisphosphate 3-kinase C
- Inositol polyphosphate 5-phosphatase K
- Multiple inositol polyphosphate phosphatase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
Sequence:
MEGQTRSGSARPGTRTGLGPLPGTHGVLQAEIPSKKVNSSFQLPAKNSGPASSEPRLTLAPVGPRAAVSPPSERPRLVLSSPRPVLAPLSIAGEQKRPPPPHSSNRAAKSVGQLVVSAAAASKPPPVASVSILAPKSLGQLVISASAMPRPSPAPLGSVLTPTSRDQKQLSPTSVGPKPALATSGLSLALASQEQPPQSPSSPSPVPSPVLSPSQEGHLAAASVTSTPASERQLPARQKDTAVPRPTPPADKCLYTPERAAGPATSPPRAQAFSDPRLSPSFRARPEAPRHSPEDPVLPPPPQTLPLDVSPGLPESGTRSPGLLSPTFRPGIPSSQTVPPPLPKPPRSPSRSPSRSPNRSPCLPPAPEVALPKPVTQAAGSGRCPSPNLQAQESPAAATTTTSPTSSWSAQPTCKSDPGFRITVVTWNVGTAMPPDDVTSLLHLGSGHDNDGADMIAIGLQEVNSMINKRLKDALFTDQWSELFMDALGPFNFVLVSTVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAHGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSNQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPSGGPSPSGRESHRLQVTQHSYRSHMEYTVSDHKPVAAQFILQFAFRDDVPLVRLEVADEWARPEQAVVRYRVETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEEVDGNIYQVTFSEESLPKGHGDFILGYYSHHHSILIGVTEPFQISLPTSESASSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPSLALHPSSRERRGGSRSPSPQSRQLPRVAPDRGHSSSSRGSSEEGPSGLPGPWAFPPSVPRSLGLLPALRLETVDPGGGGSWGADQEAPDPNSLSPSPQGRLGLEEGGLGP
Protein: Protein vreteno (Q9VCU7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gonad-specific protein essential for germline development to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process in both germline and somatic gonadal tissues by mediating the repression of transposable elements during meiosis. Required for primary piRNA biogenesis in both germline and somatic gonadal tissues.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21831924, ECO:0000269|PubMed:21863019}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:21863019}. Note=Component of the perinuclear meiotic nuage (also known as germline granule or P granule), a germline-specific membraneless ribonucleoprotein biocondensate involved in post-transcriptional regulation of transposons and mRNAs (PubMed:21863019). Localizes to Yb bodies in follicle cells (PubMed:21863019). {ECO:0000269|PubMed:21863019}.
Interaction partners:
- Putative ATP-dependent RNA helicase SoYb
- Probable RNA helicase armi
- Inactive peptidyl-prolyl cis-trans isomerase shutdown
- Putative ATP-dependent RNA helicase BoYb
- RNA helicase
- Mitochondrial cardiolipin hydrolase
- Protein aubergine
- Protein piwi
- Probable ATP-dependent RNA helicase spindle-E
- Tudor domain-containing protein krimp
Sequence:
MESESSQDDWSAFDPMSREYYDQVGNRYTNESGQKLIMEAPLPPKDEKEQRATRQAKYPYLVVPKSSPYVTEKMLINFFGRALIKEMEFRRLSRVYFVYFENIASLETAQQRVQRYPNLIKCITGRPQKEREITSDPVTSTEPMPTPGPAISATERTPVNHNREVPISTGGQNHPEFFRPPLVTKDDYKRGSLLATNDPIQRYLNVKYEFALERHDIYKLKDETRIPQVVLHFRSGRTIPLSTVAVTEEDKTKSLLEDGVSKCVVCQNWTDTFCKLCKMPFCNASCFADVAEQHKQACGKGEILNLDEKVGRKYPKPGLPPSGSKVRITAFEQTNVVYVRSADIQIDIAYYTVLTEVMMLGKDASKLQSTPVCGQIVLYKFEGHMSRAMVLNVDNIKEIYVVFIDFGSVEVTQLERLYECSSYLAGLTCYPVAVKLRGVPRRFVGPNIREVMYELDQSLVFNIKYSSREYDTSKGMQVVVMTEIDINRSLNRLFKTILTPVEPSVSDLGYKEDCLPYIPLHCGKNINVVVMDNTFIQCGFIYCTSIDLAYEVTKMQRDIQEYGEKIAKCATYAPPINELCIAKYEGKWRRGLSVELVGDGYPSILFIDYGNIVPTHVTDIRPYPPQFIFPIMTTQLDLIGVPEKPTDEQIKWLDKNYPIGSVITCSEITFDEETNSYSTRIEKLQEFLSLD
Protein: Cysteine-rich secretory protein 3 (CRISP-3) (Specific granule protein of 28 kDa) (SGP28) (P54108)
Organism: Homo sapiens (Human)
Subcellular location: Secreted. Note=In neutrophils, localized in specific granules.
Interaction partners:
- Alpha-1B-glycoprotein
- Trifunctional purine biosynthetic protein adenosine-3
- Protein LYRIC
- Beta-microseminoprotein
Sequence:
MTLFPVLLFLVAGLLPSFPANEDKDPAFTALLTTQTQVQREIVNKHNELRRAVSPPARNMLKMEWNKEAAANAQKWANQCNYRHSNPKDRMTSLKCGENLYMSSASSSWSQAIQSWFDEYNDFDFGVGPKTPNAVVGHYTQVVWYSSYLVGCGNAYCPNQKVLKYYYVCQYCPAGNWANRLYVPYEQGAPCASCPDNCDDGLCTNGCKYEDLYSNCKSLKLTLTCKHQLVRDSCKASCNCSNSIY
Protein: Calsequestrin-2 (Laminin-binding protein) (P19204)
Organism: Gallus gallus (Chicken)
Function: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:2302244}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000269|PubMed:2302244}.
Interaction partners:
- Ryanodine receptor 2.
- Uncharacterized protein.
- Asp-B-Hydro_N domain-containing protein.
- Myosin regulatory light chain 2A, cardiac muscle isoform
- Myosin regulatory light chain 2B, cardiac muscle isoform
- Troponin I, fast skeletal muscle
- Troponin T, fast skeletal muscle isoforms
- Sarcalumenin
Sequence:
MKATCWILAGFCLLFCCKAEEGLNFPTYDGKDRVIDLNEKNYKHALKKYDMLCLLFHEPVSSDRVSQKQFQMTEMVLELAAQVLEPRSIGFGMVDSKKDAKLAKKLGLVEEGSLYVFKEERLIEFDGELATDVLVEFLLDLLEDPVEVINSKLELQAFDQIDDEIKLIGYFKGEDSEHYKAFEEAAEHFQPYVKFFATFDKGVAKKLGLKMNEVDFYEPFMDEPVHIPDKPYTEEELVEFVKEHKRATLRKLRPEDMFETWEDDMEGIHIVAFAEEDDPDGFEFLEILKQVARDNTDNPDLSIVWIDPDDFPLLITYWEKTFKIDLFRPQIGIVNVTDADSVWMEIRDDDDLPTAEELEDWIEDVLSGKINTEDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDD
Protein: Group IIF secretory phospholipase A2 (GIIF sPLA2) (sPLA2-IIF) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 2F) (Q9QZT4)
Organism: Mus musculus (Mouse)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at the sn-2 position of phospholipids (phospholipase A2 activity), the catalytic efficiency decreasing in the following order: phosphatidylglycerols > phosphatidylethanolamines > phosphatidylcholines > phosphatidylserines. May play a role in lipid mediator production in inflammatory conditions, by providing arachidonic acid to downstream cyclooxygenases and lipoxygenases.
Subcellular location: Secreted {ECO:0000269|PubMed:11877435}. Cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:11877435}.
Interaction partners:
- Group 3 secretory phospholipase A2
- Group XIIA secretory phospholipase A2
- Group XIIB secretory phospholipase A2-like protein
- Cytochrome P450 2E1
- Phospholipase A and acyltransferase 3
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Phospholipase A2
- Group 10 secretory phospholipase A2
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Group IIE secretory phospholipase A2
Sequence:
MKKFFAIAVLAGSVVTTAHSSLLNLKSMVEAITHRNSILSFVGYGCYCGLGGRGHPMDEVDWCCHAHDCCYEKLFEQGCRPYVDHYDHRIENGTMIVCTELNETECDKQTCECDKSLTLCLKDHPYRNKYRGYFNVYCQGPTPNCSIYDPYPEEVTCGHGLPATPVST
Protein: Nuclear factor 1 (A0A8J8YK50)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPNSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSTSPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQPNSSGQVVGKVPGHFTPVLAPSPHPSAVRPVTLTMTDTKPITTSTEGEAASPTATTYTASGTSQANRYVGLSPRDPSFLHQQQSWYLG
Protein: Type IV pilus ATPase PilU (G3XCX3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. Functions as a PilT-dependent retraction ATPase, providing a functional coupling between PilT and PilU and an optimal mechanism for pilus retraction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15659660}. Note=Localizes only to the piliated pole. {ECO:0000269|PubMed:15659660}.
Interaction partners:
- Type IV pilus inner membrane component PilM
- Prepilin leader peptidase/N-methyltransferase
- Fimbrial assembly protein PilQ
- Type IV pilus inner membrane component PilO
- Type IV pilus inner membrane component PilN
- Type IV pilus inner membrane component PilP
- Type IV pilus assembly protein PilF
- Type 4 fimbrial biogenesis protein PilZ
- Protein PilH
- Protein PilJ
Sequence:
MEFEKLLRLMVEKGGSDLFITAGVPPSMKVNGRVMPVTKTPLSPEQTRETVLGVMNEQQRRDFAENHECNFAISARGIGRFRVSAFYQRNLVGMVLRRIETNIPTLEELKLPEILKKLALTKRGLVIFVGATGTGKSTSLAAMIGYRNKNSTGHIISIEDPIEYIHQHQGCIVTQREVGLDTDSFEVALKNTLRQAPDVIMIGEVRSRETMDHAVAFAETGHLCLATLHANNANQALERIIHFFPADRHGQVWMDLSLNLKAIVAQQLVPTPDGKGRRAVIEVLLNTPLAADLIRKGEVHELKPLMKRSTEQGMQTFDQALYQLYTQGEITYEDALAHADSANDLRLMIKLGSESDADHLSSLTQGLSLEITDDDPAGRRFR
Protein: At1g77350/F2P24_6 (Keratinocyte-associated-like protein) (Q9FVX3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit-like protein
- Binding protein
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- At4g29870
Sequence:
MAGAVGTSMLGSLIVFTVILSLQEIYRGKLASSELFTILGGFTSSLLFLFSLTFIGNFQESSGIKSGWGAVILAEIIALIAAGTVHRVCITTCFLFSAGLLYEVNKISGYMLSKTESKSKRH
Protein: tRNA-specific adenosine deaminase 1 (EC 3.5.4.34) (tRNA-specific adenosine-37 deaminase) (Q389P9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHVDVPHDCFPGCATPLEAFAIALRSQPRGFGWDCSAISALDGRGEVVAGFVLGLPRASPCDKISGPSFVCVSLGSGTRCVGYKPVEFTVEADLMLRDGHAEVMARRGLVAFLLDAAAYLSRGDDRLHFAVERHHCFPQFSGGDASCDAVGECFRLRPGVSVHLVCTEYPCGAMSTPFGGAHVLLSTPSGRSLFDGGLDSNPLLVGEEHVSRCDGKTLPEFVDARVFDGPGSFTVCYGHRVAAHRCWPVDDMPFVARVKPGKGRQNLCMSCSDKLLRWHCLGIQGRRRTRLFPEPIRLAAVWLPRKVSIVSDNCVAVNAFSPLEKAREGLNSRLHCFCPRLRPGELGAPSEGTNEPVRGGSPFPQVDVCDFESSALRLILVGMSGDDTPLGNGGAPKRKDESCWSRAAWATVEDGNQVVPCSAGAKRRRGELEGLVVRCVLRWNEESTAALNTKAGVPRGVTKQSMNRTVQQLLQLQSDVYSGAKPPDPDTAALLEGIASRFPLSRLWMALRQREIARTVSGRYHQSCRRLQAFPPTEGEADHETRRVGNYSLYIPQRVVSVGDMAEIGRNIASGDSVHCWLQGSQRAGESVLDEVWKEGLGRKLPLLWVEKREQRVA
Protein: Crp1p (A0A1D8PEI4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Copper metallochaperone
- Superoxide dismutase 1 copper chaperone
- RRN6 beta-propeller domain-containing protein
Sequence:
MQKFIINFANIHCDKCEGIIRNVVSRYYKISDETDLNANIKPSEVIFKLENNEVTLYGNDLIDFHGDIKSIIKSLGKSGFDILSWDLHNGDETVSSSQIVNTNIQGANEPDGFIDIVGMYHKFINSRNKKKHMKYCKVCQESEQHKKKSTDSDFSSSSEDTVVEIPHQEFRASFLVTGMTCASCAQSITDNLRSILGESKKEDEPNFSVNVIQQSVVVIIPNKQIINKIVDAINDMGFDCKLIEVLPVQRSVNTKVTALIGGMTCAACANSIDSAVKELPFILESGINVVTKAAQFVLEDDGGSNIAKLKETIEDCGFDFELLSTEKVNYTSGKQKPRSINLKVNGMFCNHCPDIITQYLTNYGDAVVINDPISLDHPVIKFTYVPSQTLKTRKILFDLNHLKDDGNGGYTITPDEKGAFECEIIKPVTVDEHVRKLAHREVLGLAIRLAIATLFAIPTFIFGIVAMSLLPKHHPFRVWVEDPLWVGNVSRNSWILFILATPVYFFAADTFHRKAIKEIKSLWFHKNSFKSRLLKFGSMNLLMSLGTTVAYFASIVLIGLSATQKPMTHHGLHTTYFDSVVFLSFFLLIGKLLQSYSKSKTADAISELSKLKQTEATLIEDDKDTRVDIQLLEIGDQIRIGTGESPPVDCVLVEGSTEFDESALTGESTPVKHQEGHQIFSGTVNIGNSSVVGKVTSLEGDSLLNQIVNTVRDGQMRKAPMERTADLITGYFVPLIIACAVITWVIWLALGYSGALPQSYLDIDVGGWTVWSLEFAIAVFVVACPCGIGLAAPTALFVGSGLAAKNGILAKGGGVAFQDGANVNIVCFDKTGTLTKGELTITDFHFPDKSSIAKTFALQAARDLEVPSHHPLGKAVKSFVTSYDGKSLTANKIPQVETVPGKGLRGQIIYDEGDDIWNEYKPTQAILGNEKLMEENDIEFTEKERQWLKKWKGECKSVILVGLQCESYFKDSKFHLALIMAARDQLRPETKKVIEFLKHKDIECWMITGDNKLTADAIAKEIGIENVVSEVLPDEKEAQIKKIRQLNSGGKKEPVIAMIGDGINDAPALASADVGIALSSGADLAVTSSDFILLNKIHPLVSLATLLDICSKVFQRVKLNFGWSLVYNLIALPIAAGVIYPYKNSRLDPVWASAAMALSSVSVVLSSLALKLYKPSLKAEDFGVDDSTESELSPNEV
Protein: C-type lectin domain family 6 member A (C-type lectin superfamily member 10) (Dendritic cell-associated C-type lectin 2) (DC-associated C-type lectin 2) (Dectin-2) (Q9JKF4)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: specifically recognizes and binds alpha-mannans on C.albicans hypheas. Binding of C.albicans alpha-mannans to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. Recognizes also, in a mannose-dependent manner, allergens from house dust mite and fungi, by promoting cysteinyl leukotriene production. Recognizes soluble elements from the eggs of Shistosoma mansoni altering adaptive immune responses.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6EIG7}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit gamma
- Tyrosine-protein kinase SYK
- Caspase recruitment domain-containing protein 9
- Antigen presenting cell lectin-like receptor A2
- E3 ubiquitin-protein ligase CBL-B
- Antigen presenting cell lectin-like receptor A1
- TYRO protein tyrosine kinase-binding protein
- C-type lectin domain family 4 member D
- C-type lectin domain family 4 member E
- Toll-like receptor 2
Sequence:
MVQERQSQGKGVCWTLRLWSAAVISMLLLSTCFIASCVVTYQFIMDQPSRRLYELHTYHSSLTCFSEGTMVSEKMWGCCPNHWKSFGSSCYLISTKENFWSTSEQNCVQMGAHLVVINTEAEQNFITQQLNESLSYFLGLSDPQGNGKWQWIDDTPFSQNVRFWHPHEPNLPEERCVSIVYWNPSKWGWNDVFCDSKHNSICEMKKIYL
Protein: Voltage-dependent T-type calcium channel subunit alpha (G5EBS2)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
Sequence:
MLRQPVPELRSFQSLSKYAGGPRSVLGRRTSAITVNRRQSQSTRRHEDVEALGSIEGSKETLQLSEHGRLASSSEASPSRWEGRQIEWGNEEQIEEESELPYPGFAEPALRCFYQARPPRKWALQMVMSPWFDRITMAVIMINCVTLGMYRPCEDGPDCDTYRCQILDIIDNCIFVYFAFEMVIKIMALGFYGPAAYMSDTWNRLDFFIVMAGIAEFVLHEYLGGNINLTAIRTVRVLRPLRAVNRIPSMRILVNLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCVINLPKTISENQSALFNNVKLTRFYIPEDTSLEYICSQPDANGLHTCSNLPPYTVDGVKCNLTLDEYDKVTNDSCINWNIYYNECQVMQRNPFQGSVSFDNIGFAWVAIFLVISLEGWTDIMYYVQDAHSFWNWIYFVLLIVIGAFFMINLCLVVIATQFAETKRRETERMLQERKMLLNRDSISCTGSEIGGASSKEEGDTVYAAFVRFIGHTFRRTKRAAKKKYTAYMEERAERKSSERQQRRKSKLDDMATLSRIEEKAEDEEDETTITRENGDDQIEQNGDGVRIKRVKIEEEPKIKIGNGNSNGPHYKHSSSDEESDEDGEEDQVYDGEEAKKKSTPSKLWWFREKIQKFVICDHFTRGILVAILVNTLSMGVEYHQQPEILTVILEYSNLFFTALFALEMLLKIIASGLFGYLADGFNLFDGGIVALSVLELFQEGKGGLSVLRTFRLLRILKLVRFMPALRYQLVVMLRTMDNVTVFFGLLVLFIFIFSILGMNLFGCKFCKVEEKFLGGLAKKCERKNFDTLLWALITVFQILTQEDWNMVLFNGMAQTNPWAALYFVALMTFGNYVLFNLLVAILVEGFQESKEEEKRQLEEDARKQAVEEEDERKRELELIIAKTTSPAFNNGVAPAECTCQRPSSPEESPSPRLLSANYHPSPERKHSANLDAIIDKRLVLRNSAPFDRSPVSEGRDDSRLNRHASLVLPVANGVPYRRQRVHSWSGLCHHFNPNCPVHGRRALIETYAREKFLEASQELKQALAEEEKRNEAKQNTFVRKLLKKTCLHNRTEFSLFLMGPKNPLRIKCLQTTQKKWFDYTVLFFIGINCITLAMERPSIPPDSFERQFLHISGYIFTVIFTGEMMMKVIANGCFIGQAAYFKDGWNILDGILVVISLINIAFELLATGDSPKIFGVIRVLRLLRALRPLRVINRAPGVKLVVMTLISSLKPIGNIVLICCTFFIIFGILGVQLFKGMMYHCIGPEVGNVTTKADCIEDYRNKWVNHRYNFDNLGQALMSLFVLSSKDGWVSIMYQGIDAVGVDVQPIENYNEWRMIYFISFLLLVGFFVLNMFVGVVVENFHKCKEALEKEMREKEKEKRLKRKLKRQKFEESMAGKRKKMERNYPYYHDYGHTRLFLHGIVTSKYFDLAIAAVIGINVISMAMEFYMMPMGLKYVLKALNYFFTAVFTLEAAMKLIALGFKRFFIEKWNRLDMFIVILSIAGIIFEEFEALELPINPTIIRVMRVLRIARVLKLLKMAKGIRSLLDTVGEALPQVGNLGSLFFLLFFIFAALGVELFGKLECSEDHPCDGLGEHAHFKNFGMAFLTLFRIATGDNWNGIMKDALRDDCDSSDHCETNCCVDPILAPCFFVIFVLISQFVLVNVVVAVLMKHLEESNKRDAEGPAEPTGENIENEITKSDDDEIVEEHEPLAIEHVKEGELDEEEETEEGPTTQIPDGHGGIKRLSMQVLEQELIEVERHLEERYRRASECLGGELQPLNPGEIEDLDDPEFRPRSRSHRPRARTNSALSNKSRGSHKSAL
Protein: ABC1 family protein MCP2 homolog (O60111)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mitochondrial lipid homeostasis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q06567}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MFSRFSWPRITRCFRSYPKKKSSCISFTHHAREHTNFKKPAVVGASITLMASVALVDFDPVKHAGVSSKRAYRVVLAGFLCFSDYKKVLGSSYASEEERQLALSECHLRCAERSLKVFEENGGIYIKIGQHLSAMGYVIPKEWTNTMVKLQDRCPSTSLKDIDHLFRVDTGKGLDETFDEFDPIALGVASLAQVHKARLKDSDVWVAVKVQHPSVSLNSPLDLSMTRWVFKAIKTFFPDFKLMWLADEIERSLPQELDFTREAKNSIETKEHFAHLSTSLYVPEVMWSKPRILVMEYVAGARIDNLSFMDEHSISRDLVSVDICHIFNEMIFGKGGHLHCDPHGGNVLIRSKPKNSKSPRNYEIVLLDHGLYRDIPHELQVDYANMWLNIINFNEKNLKFYAKKVANVSDENFPIFATAITGRPYKSLKSLPIGGPNHEEEQKKFISALQKGGMLQSIIRLLSTMPRLTLLLMKTNDLVRSLDENLKTKSGPEKLYLIMARYCLRCVYDDKMDSLWNSRSFWVSKVFKGTYYRLSYLFSSLKYTLAENYFYYKHMYL
Protein: Spindle pole body component 110 (Extragenic suppressor of CMD1-1 mutant protein 1) (Nuclear filament-related protein 1) (Spindle pole body spacer protein SPC110) (P32380)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Potential role in cross-linking filaments or anchoring other molecules. It is essential for growth.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Tightly associated with the nucleus. It is present in a granular pattern that excludes the nucleolus.
Interaction partners:
- Spindle pole body component SPC98
- Calmodulin
- Tubulin gamma chain
- Spindle pole body component SPC97
- Protein STU2
- S-phase entry cyclin-5
- G2/mitotic-specific cyclin-2
- Mitosis inhibitor protein kinase SWE1
- Sporulation-specific protein 12
- Gamma tubulin complex adapter SPC72
Sequence:
MDEASHLPNGSLKNMEFTPVGFIKSKRNTTQTQVVSPTKVPNANNGDENEGPVKKRQRRSIDDTIDSTRLFSEASQFDDSFPEIKANIPPSPRSGNVDKSRKRNLIDDLKKDVPMSQPLKEQEVREHQMKKERFDRALESKLLGKRHITYANSDISNKELYINEIKSLKHEIKELRKEKNDTLNNYDTLEEETDDLKNRLQALEKELDAKNKIVNSRKVDDHSGCIEEREQMERKLAELERKLKTVKDQVLELENNSDVQSLKLRSKEDELKNLMNELNELKSNAEEKDTQLEFKKNELRKRTNELNELKIKSDEMDLQLKQKQNESKRLKDELNELETKFSENGSQSSAKENELKMLKNKIAELEEEISTKNSQLIAKEGKLASLMAQLTQLESKLNQRDSQLGSREEELKKTNDKLQKDIRIAREETVSKDERIIDLQKKVKQLENDLFVIKKTHSESKTITDNELESKDKLIKILENDLKVAQEKYSKMEKELKEREFNYKISESKLEDEKTTLNEKISNLAAENSQLKNKIEDNSTATHHMKENYEKQLESLRKDIEEYKESAKDSEDKIEELKIRIAENSAKVSEKRSKDIKQKDEQISDLTQNLKLQEDEISSLKSIIDRYKKDFNQLKSEQSNIQHDLNLQILNLENKLIESEDELKSLRDSQKIEIENWKRKYNNLSLENDRLLTEKESASDKEREISILNRKLDEMDKEKWNLQESKEKYKRELQKVITANDRLRREKEELNENSNNIRIMEDKMTRIKKNYLSEITSLQEENRRLEERLILNERRKDNDSTMQLNDIISYYKLKYHSEVRHNNDLKVINDYLNKVLALGTRRLRLDTRKGEHSLNISLPDDDELDRDYYNSHVYTRYHDYEYPLRFNLNRRGPYFERRLSFKTVALLVLACVRMKRIAFYRRSDDNRLRILRDRIESSSGRISW