wanglab/gogpt-training-data huggingface dataset:
Protein: Spermatogenesis-defective protein 39 homolog (hSPE-39) (VPS33B-interacting protein in apical-basolateral polarity regulator) (VPS33B-interacting protein in polarity and apical restriction) (Q5TYV4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Proposed to be involved in endosomal maturation implicating in part vps33b. In epithelial cells, the vps33b:vipas39 complex may play a role in the apical rab11a-dependent recycling pathway and in the maintenance of the apical-basolateral polarity. May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be independent of vps33b. May play a role in vesicular trafficking during spermatogenesis (By similarity). May be involved in direct or indirect transcriptional regulation of E-cadherin.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000250|UniProtKB:Q9H9C1}. Recycling endosome {ECO:0000250|UniProtKB:Q9H9C1}. Late endosome {ECO:0000250|UniProtKB:Q9H9C1}.
Interaction partners:
- Vacuolar protein sorting-associated protein 33B
- Vacuolar protein sorting-associated protein 33A
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 45
Sequence:
MTRAKPEDDEYWNSSKFKAFTFDDEDDEFSRLKESKRAVNSILVDDDDDEDDVEKVSWSGEPVGSISWSVRETASSIRSGSEQNFPKIDTAPSLSKQGSGYSLSSLFKAKSKPTAFQSFSESFSETSARTYAPELRKPKSDGKDFVSDLSPEETIRRMQKGRAFSMEKFRSLQDKLLLLDEAVSVYDGNVITAVLIYLKKSLSKEILFRELMPREVALRHYIHYLKEMGEQKLLVELLKALGRTEDMALMQYKEHLNIKDEGRRRDFLKSCLSLPFSQDDSTHVQDHYTLLERQIIIEASDKKADTDIFKKFPRKASILNMPIITTLYYSCFYHYGEPEGTFSSPSNIRKTFRISEKQYITTALGARAKLKSWFDVDSLFNTKNWLGYTKKRSPIAFHRVVDILQKNSAPVQVLQEYVNLIDDPELKLSVALKYKCHDIIINTYRDLKDRQQLIVYREKLERDSPEYRKIQELLNNGQIRWKN
Protein: Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit) (Q6FXX4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU365061}. Chromosome, telomere {ECO:0000256|RuleBase:RU365061}.
Interaction partners:
- Telomere replication protein EST3
- H/ACA ribonucleoprotein complex subunit NOP10
- H/ACA ribonucleoprotein complex subunit CBF5
- ATP-dependent DNA helicase II subunit 2
- ATP-dependent DNA helicase II subunit 1
- Nonsense-mediated mRNA decay factor
- H/ACA ribonucleoprotein complex subunit 2
- H/ACA ribonucleoprotein complex subunit GAR1
- Candida glabrata strain CBS138 chromosome G complete sequence
- Replication protein A subunit
Sequence:
MKVLREVVTTNENSLRQLGVLLDSTFVIENEVQIDIDKDFFDSSAGHRKLIDQCIVFLLQKRLLNNVLVAGYKLAKNNTVRSILHCENSNSAVKTLKSSSWELLHTNIGSPKFVNLILNHSIFTFNGEFTQQVAGNSLNKPHLPPSWIIDNDYEQETDINCFSINNRPYLYHNTRGFCIKSIILDRDMLNETLDIQVKYLMREIFENDIKLNKKALRTTVIETVLKQVLENQQRIPIIPILDKICPKTYSNYHLDRATPVKCVNKFIVVILEKLKILQLIGSRKNSFVLFSKISQLLKLPLNGKINVKEFFTKLNVNAVRRYLSIDPIGQQKQSMRLYLTCVVNYLLSKLIPSLLKSFFYCTEVSSYSKILYFRNDEWNSISTPFLKEYLDKYLVQNTHCNSHFSYMESQFNHCNFRLIPKKGNNEFRVIGIPYKGNNAEELLQYKQNHTKVIVPTKLILDYLRKSRQTTQKLLFSAMQISDHICQYKCHLHSKYGYIPKLFYLKFDIHNCYDSIPIAKAKSVLNSLINNCGYEEFYVRSVTILNTKNNEVRYDTIVNGHINIRDFEIMVDNSTTTFLTKEDIMDLIEFEMEMTSIRLFDKCYLRKDGLFQGLSLSATIVDILYDDMLEKNRVFKDILNNDGLVLRHADDFLLISPSKEIISYARLKINEGFTEYNAQVNHRKIVFSESDNIANTAIPFCGVEIIPRTLEVIKRFSAMNETDISDHEGNIYSKCAVLFKMRLNYGTMNANLNSISTMLKQVENATINIVRIILNSNHIATSVSSFSSFVNELYNICLLSSRNLNLLNHRDLQRFLTSIKKTILTVLLKNLKRKYSIYNGISRNMNSKRTSK
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (Q6IQ43)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPELTPEEEQATKQFLEEINKWTVQYNVSPLSWNVAVKFLMARKFDVLRAIELFHSYRETRRKEGIVKLKPHEEPLRSEILSGKFTILNVRDPTGASIALFTARLHHPHKSVQHVVLQALFYLLDRAVDSFETQRNGLVFIYDMCGSNYADFELDLGKKVLNLLKGAFPARLKKVLIVGAPIWFRVPYSIISLLLKDKVRERIQILKTSEVTQHLPRECLPENLGGYVKIDLATWNFQFLPQVNGHPDRFDEIILFSLPPALDWDSVHVPGPHAMTIQELVDYVNARQKQGIYEEYEDIRRENPVGTFHCSMSPGNLEKNRYGDVPCLDQTRVKLTKRSGHTQTDYINASFMDGYKQKNAYIGTQGPLENTYRDFWLMVWEQKVLVIVMTTRFEEGGRRKCGQYWPLEKDSRIRFGFLTVTNLGVENMNHYKKTTLEIHNTEERQKRQVTHFQFLSWPDYGVPSSAASLIDFLRVVRNQQSLAVSNMGARSKGQCPEPPIVVHCSAGIGRTGTFCSLDICLAQLEELGTLNVFQTVSRMRTQRAFSIQTPEQYYFCYKAILEFAEKEGMVSSGQNLLAVESQ
Protein: Phospholipase A2 (EC 3.1.1.4) (Group IB phospholipase A2) (Phosphatidylcholine 2-acylhydrolase 1B) (P04054)
Organism: Homo sapiens (Human)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner. Upon binding to the PLA2R1 receptor can regulate podocyte survival and glomerular homeostasis. Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:19297324}. Note=Secreted from pancreatic acinar cells in its inactive form.
Interaction partners:
- Secretory phospholipase A2 receptor
- Platelet-activating factor acetylhydrolase
- Cytochrome P450 4A11
- Cytosolic phospholipase A2
- Bile salt-activated lipase
- Cytochrome P450 2E1
- P2X purinoceptor 4
- Phospholipase B1, membrane-associated
- Group 10 secretory phospholipase A2
- Pancreatic triacylglycerol lipase
Sequence:
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPVDELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNCDRNAAICFSKAPYNKAHKNLDTKKYCQS
Protein: RELT-like protein 1 (Q8IUW5)
Organism: Homo sapiens (Human)
Function: Induces activation of MAPK14/p38 cascade, when overexpressed. Induces apoptosis, when overexpressed.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16389068}; Single-pass type I membrane protein {ECO:0000269|PubMed:16389068}.
Interaction partners:
- Serine/threonine-protein kinase OSR1
Sequence:
MAPRALPGSAVLAAAVFVGGAVSSPLVAPDNGSSRTLHSRTETTPSPSNDTGNGHPEYIAYALVPVFFIMGLFGVLICHLLKKKGYRCTTEAEQDIEEEKVEKIELNDSVNENSDTVGQIVHYIMKNEANADVLKAMVADNSLYDPESPVTPSTPGSPPVSPGPLSPGGTPGKHVCGHHLHTVGGVVERDVCHRCRHKRWHFIKPTNKSRESRPRRQGEVTVLSVGRFRVTKVEHKSNQKERRSLMSVSGAETVNGEVPATPVKRERSGTE
Protein: Trans-enoyl reductase iliB (EC 1.-.-.-) (Ilicicolin H biosynthesis cluster protein B) (P0DO31)
Organism: Neonectria sp. (strain DH2)
Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IliB collaborates with the hybrid PKS-NRPS synthetase iliA to assemble the backbone of ilicicolin H. The PKS portion of iliA and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain of iliA during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the iliA C domain, and the resulting PKS-NRPS hybrid is offloaded by the iliA RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).
Interaction partners:
Sequence:
MALATPLPATQAAVKVTGPSTVDVSAATTLPVLEAFEVLVRVACVSINHVDGKSADMSPTPGATSGVDFSGLIVALGSKVDSDEFRANNNMRALSIGDRVFGGVFGNNPLRHDNGAFAEYVAVPARLIWHMPAAMDFSTAATIGATLATVGLALFQYLQVPMPSTQTISDSKTIPDPQQKTRMALVYGGGTATGAMAIQVLKLAGFRPITTCSPGSAARAMHLGAAATFDYRSPTCGADLREHTANGLELALDCITDTASMSICYEALGSAGGRYVALDAFPLRGHTRRSVAAEWVCTYTQFGHAVAWVPPYNLDARPRDREIAEAWYVVAQQLVDEGLIEPYPKEDRTGGLAAVGEGMRAVWKGEISGRKLAYPIAEECY
Protein: Polycomb group RING finger protein 6 (Mel18 and Bmi1-like RING finger) (RING finger protein 134) (Q99NA9)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. May modulate the levels of histone H3K4Me3 by activating KDM5D histone demethylase. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BYE7}.
Interaction partners:
- E3 ubiquitin-protein ligase RING2
- E3 ubiquitin-protein ligase RING1
- YY1-associated factor 2
- Lethal
- RING1 and YY1-binding protein
- Transcription factor E2F6
- Chromobox protein homolog 3
- Chromobox protein homolog 2
- Chromobox protein homolog 7
- Polyhomeotic-like protein 3
Sequence:
MDEAETDATENKRASEAKRASAMPPPPPPPPPISPPALIPAPAAGEEGPASLGQAGAAGCSRSRPPALEPERSLGRLRGRFEDYDEELEEEEEMEEEEEEEEEMSHFSLRLESGRADSEDEEERLINLVELTPYILCSICKGYLIDATTITECLHTFCKSCIVRHFYYSNRCPKCNIVVHQTQPLYNIRLDRQLQDIVYKLVINLEEREKKQMHDFYKERGLEVPKPAAPQPVPSSKGKTKKVLESVFRIPPELDMSLLLEFIGANEDTGHFKPLEKKFVRVSGEATIGHVEKFLRRKMGLDPACQVDIICGDHLLERYQTLREIRRAIGDTAMQDGLLVLHYGLVVSPLKIT
Protein: Protein NRT1/ PTR FAMILY 2.11 (AtNPF2.11) (Nitrate transporter 1.10) (Protein GLUCOSINOLATE TRANSPORTER-2) (Q9LV10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-affinity, proton-dependent glucosinolate-specific transporter. Involved in apoplasmic phloem-loading of glucosinolates and in bidirectional long-distance transport of aliphatic but not indole glucosinolates. May be involved in removal of glucosinolates from the xylem in roots.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22864417}; Multi-pass membrane protein {ECO:0000269|PubMed:22864417}.
Interaction partners:
- Probable sodium/metabolite cotransporter BASS5, chloroplastic
- Transcription factor MYB28
- Cytochrome P450 83A1
- Myrosinase 4
- Methylthioalkylmalate synthase 1, chloroplastic
Sequence:
MERKPLELESTDNHQNPSSAVYGGSVTAVDSVEEDVQNQKKVVYRGWKVMPFIIGNETFEKLGIIGTLSNLLVYLTAVFNLKSITAATIINAFSGTINFGTFVAAFLCDTYFGRYKTLSVAVIACFLGSFVILLTAAVPQLHPAACGTAADSICNGPSGGQIAFLLMGLGFLVVGAGGIRPCNLAFGADQFNPKSESGKRGIDSFFNWYFFTFTFAQILSLTLVVYVQSNVSWTIGLTIPAVLMFLACLIFFAGDKLYVKIKASGSPLAGIAQVIAVAIKKRGLKPAKQPWLNLYNYYPPKYANSKLKYTDQFRFLDKAAILTPEDKLQPDGKPADPWKLCTMQQVEEVKCIVRVLPIWFASSIYYLTITQQMTYPVFQALQSDRRLGSGGFVIPAATYVVFLMTGMTVFIVVYDRVLVPTMRRITGLDTGITLLQRIGTGIFFATASLVVAGFVEERRRTFALTKPTLGMAPRKGEISSMSAMWLIPQLSLAGVAEAFAAIGQMEFYYKQFPENMRSFAGSIFYVGGGVSSYLGSFLIATVHRTTQNSSGGNWLAEDLNKGRLDLFYFMIAGILAVNFAYFLVMSRWYRYKGSDDEVTTYETNENIIKQQDKNVA
Protein: Odorant receptor (Q2PRE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEDKTFNISYQEFYLIGFTDLQDYRRYLFIPFFLIFAFTLFTNSIIILVIVKESKLHAPMYILIGFVAALGFLQPIFAIPRILISFLFGRNMIYKSECLVQMFCLHMAGCFQSTVLVAMAVDRFFAITFPLQYHYYVNLKTSLIFGLALFLRNLVVVVSMVGLIAPLQFCKTNVIYHCVCEHTSVVSIACGDVSKNYAAGTVAFSIVTGDCVFIMCSYIVIFVIIFRSPPGDSRQKAINTCSTHLMVMVVAYCSCVVAYVGYRVSSIPRDIRVLCTMSYLLFTNFFNPVIYGIRTKEIKAQIVKYLSKNKVGSY
Protein: Adenosine receptor A2 (Q29ST6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU201114}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU201114}.
Interaction partners:
- Adenosine A2a receptor b.
- Adenosine A2b receptor
- Lymphocyte antigen 75.
- Guanine nucleotide-binding protein G
- Uncharacterized protein.
- Adenosine kinase b.
Sequence:
MLNNVFDVLYMILELLIALLSVLGNVLVCWAVGLNSNLQSITNFFVVSLAVADIAVGVLAIPFSIVISTGFCANFYGCLFIACFVLVLTQSSIFSLLAIAIDRYIAIKIPLRYNSLVTGQRARGIIAICWVLSVIIGLTPMLGWHKARLQEGHNGTCPPGMMECLFEEVVVMDYMVYFNFFACVLVPLLLMLAIYLRIFMAARHQLKCIESKAIPCELKSRSTLQKEVHAAKSLAIIVGLFAVCWLPLHIINCFTLFCPECERPPALIMYLAIILSHANSVVNPFIYAYRIREFRHTFRKIVRYHILGRREPLSCNGSTRTSTRTSVADSLRIKVNGLVRELYAEQSSTTSSCESAEPGHTHRPVSTENSILDNQPIEISNSHRHTALRHPESPLTGNNEGLACRKHAGLDITDGKDLSSPLHIKSALYVQTAHCVELTEVS
Protein: Peptide encoded by miPEP164a (P0DKJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory peptide encoded by the primary transcript (pri-miR164a) of the microRNA miR164a that enhances the accumulation of its corresponding mature miRNA. Acts probably as a transcriptional activator of its corresponding pri-miRNA.
Interaction partners:
Sequence:
MPSWHGMVLLPYVKHTHASTHTHTHNIYGCACELVFH
Protein: Rho guanine nucleotide exchange factor 3 (Q1MT42)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- RING finger protein 145
- Cilia- and flagella-associated protein 251
- GTP:AMP phosphotransferase AK3, mitochondrial
- Rho-related GTP-binding protein Rho6
Sequence:
MVAKDYPIYLLIKLANCSVDESSSCGRGVGRELEEPSTKRVKPLSRVTSLASLIPPVKAAPLKRIGQTLQRSISFRSDCRPEIMAPRPWSRQVVPTITKRRDSKLWSETFDVGLGHMLSSKEIKRQEAIFELSQGEQDLIEDLKLAKKAYHDPMLKLCIMTEHELNQIFGTLDSLIPLHEDLLSRLRDVRNPDGSTDHMGHILVHWLPCLETYNSYCSNQVAAKALLDHKKQDHRVHDFLQRCLESPFSRKLDLWNFLDIPRSRLVKYPLLLREILKHTPNEHPDRQHLDEAINMIQSIVAGINTQTGESECRYYKERLLYLESGQRDLLIESSRILICHGELKNNRGVKLHVFLFQDVLVITRAISHNEQLWYQLYRQPIPVRDLEWEDLQDGEMRVGGSIRGAFSNNERTKNFFRVMFRCGGQTQMHCFQASDTFNKQQWLNCIRQAKEAVGSAESEPPRSPQMDRERQHNDCSDSNMMDTMEDSSSEYPQMELADIPVSPVRE
Protein: Tau-tubulin kinase 1 (EC 2.7.11.1) (Brain-derived tau kinase) (Q5TCY1)
Organism: Homo sapiens (Human)
Function: Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16923168}.
Interaction partners:
Sequence:
MQCLAAALKDETNMSGGGEQADILPANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFENSMKERGIAENEAFDWEKAGTDALLSTSTSTPPQQNTRQTAAMFGVVNVTPVPGDLLRENTEDVLQGEHLSDQENAPPILPGRPSEGLGPSPHLVPHPGGPEAEVWEETDVNRNKLRINIGKSPCVEEEQSRGMGVPSSPVRAPPDSPTTPVRSLRYRRVNSPESERLSTADGRVELPERRSRMDLPGSPSRQACSSQPAQMLSVDTGHADRQASGRMDVSASVEQEALSNAFRSVPLAEEEDFDSKEWVIIDKETELKDFPPGAEPSTSGTTDEEPEELRPLPEEGEERRRLGAEPTVRPRGRSMQALAEEDLQHLPPQPLPPQLSQGDGRSETSQPPTPGSPSHSPLHSGPRPRRRESDPTGPQRQVFSVAPPFEVNGLPRAVPLSLPYQDFKRDLSDYRERARLLNRVRRVGFSHMLLTTPQVPLAPVQPQANGKEEEEEEEEDEEEEEEDEEEEEEEEEEEEEEEEEEEEEEEAAAAVALGEVLGPRSGSSSEGSERSTDRSQEGAPSTLLADDQKESRGRASMADGDLEPEEGSKTLVLVSPGDMKKSPVTAELAPDPDLGTLAALTPQHERPQPTGSQLDVSEPGTLSSVLKSEPKPPGPGAGLGAGTVTTGVGGVAVTSSPFTKVERTFVHIAEKTHLNVMSSGGQALRSEEFSAGGELGLELASDGGAVEEGARAPLENGLALSGLNGAEIEGSALSGAPRETPSEMATNSLPNGPALADGPAPVSPLEPSPEKVATISPRRHAMPGSRPRSRIPVLLSEEDTGSEPSGSLSAKERWSKRARPQQDLARLVMEKRQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKSGRAAATRSRIPRPIGLRMPMPVAAQQPASRSHGAAPALDTAITSRLQLQTPPGSATAADLRPKQPPGRGLGPGRAQAGARPPAPRSPRLPASTSAARNASASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAQPDGTPSPGGSKKGPRGKLQAQRATTKGRAGGAEGRAGAR
Protein: ORF9b protein (Accessory protein 9b) (ORF-9b) (Protein 9b) (P59636)
Organism: Severe acute respiratory syndrome coronavirus (SARS-CoV)
Function: Plays a role in the inhibition of host innate immune response by targeting the mitochondrial-associated adapter MAVS. Mechanistically, usurps the E3 ligase ITCH to trigger the degradation of MAVS, TRAF3, and TRAF6. In addition, causes mitochondrial elongation by triggering ubiquitination and proteasomal degradation of dynamin-like protein 1/DNM1L.
Subcellular location: Virion {ECO:0000269|PubMed:19394665}. Host cytoplasmic vesicle membrane {ECO:0000269|PubMed:16843897}; Peripheral membrane protein {ECO:0000269|PubMed:16843897}. Host cytoplasm {ECO:0000269|PubMed:16843897, ECO:0000269|PubMed:21637748, ECO:0000269|PubMed:22820404}. Host endoplasmic reticulum {ECO:0000269|PubMed:17448558}. Host nucleus {ECO:0000269|PubMed:21637748}. Host mitochondrion {ECO:0000269|PubMed:25135833}. Note=Binds non-covalently to intracellular lipid bilayers.
Interaction partners:
Sequence:
MDPNQTNVVPPALHLVDPQIQLTITRMEDAMGQGQNSADPKVYPIILRLGSQLSLSMARRNLDSLEARAFQSTPIVVQMTKLATTEELPDEFVVVTAK
Protein: Endoplasmic reticulum chaperone BIP (EC 3.6.4.10) (78 kDa glucose-regulated protein homolog) (GRP-78 homolog) (Binding-immunoglobulin protein homolog) (BiP) (Heat shock protein 70-2) (Pbhsp70-2) (A0A509AJG0)
Organism: Plasmodium berghei (strain Anka)
Function: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins (By similarity). Acts as a key repressor of the unfolded protein response (UPR) (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:29241041}.
Interaction partners:
- Heat shock protein 110, putative
- non-specific serine/threonine protein kinase
- Ran-specific GTPase-activating protein 1, putative
- Endoplasmin, putative
- Hsp70 nucleotide exchange factor FES1
- Translocation protein SEC63, putative
- Heat shock 70 kDa protein
- DNA-binding chaperone, putative
- GrpE protein homolog
- Merozoite organizing protein, putative
Sequence:
MGNSKAFVLVLFVSLLKFISAVDPAIEGPIIGIDLGTTYSCVGVFKNGRVEILNNDLGNRITPSYVSFVDGERKVGEAAKLEATLHPTQTVFDVKRLIGRKFDDKEVAKDRTLLPYEIVNNEGKPNIRVQIKDKPTTFAPEQISAMVLEKMKEIAQSFLGKPVKNAVVTVPAYFNDAQRQATKDAGAIAGLNIVRIINEPTAAALAYGLDKKEETSILVYDLGGGTFDVSILVIDNGVFEVYATAGNTHLGGEDFDQRVMDYFIKMFKKKNNIDLRSDKRAIQKLRKEVEIAKRNLSVVHSTQIEIEDIIEGHNFSETLTRAKFEELNDDLFRETLEPVKKVLDDAKYEKSKIDEIVLVGGSTRIPKIQQIIKDFFNGKEPNRGINPDEAVAYGAAIQAGIILGEELQDVVLLDVTPLTLGIETVGGIMTQLIKRNTVIPTKKSQTFSTYQDNQPAVLIQVFEGERALTKDNHLLGKFELSGIPPAQRGVPKIEVTFTVDKNGILHVEAEDKGTGKSKGITITNDKGRLSKEQIEKMINDAEKFADEDKNLREKVESKNNLDNYIQSMKATVEDKDKLADKIEKEDKDTILNTIKEAEDWLNNNSNADSEALKQKLKEVEAICQPIIVKLYGQPGANTPPPGDEDVDSDEL
Protein: Ribosomal RNA processing protein 1 homolog A (Novel nuclear protein 1) (NNP-1) (Nucleolar protein Nop52) (RRP1-like protein) (P56182)
Organism: Homo sapiens (Human)
Function: Plays a critical role in the generation of 28S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:9192856}.
Interaction partners:
- Ribosome biogenesis protein BOP1
- Probable rRNA-processing protein EBP2
- Protein MAK16 homolog
- WD repeat-containing protein 74
- Ribosome biogenesis protein BRX1 homolog
- mRNA turnover protein 4 homolog
- Ribosome production factor 1
- Pescadillo homolog
- Ribosomal L1 domain-containing protein 1
- MKI67 FHA domain-interacting nucleolar phosphoprotein
Sequence:
MVSRVQLPPEIQLAQRLAGNEQVTRDRAVRKLRKYIVARTQRAAGGFTHDELLKVWKGLFYCMWMQDKPLLQEELGRTISQLVHAFQTTEAQHLFLQAFWQTMNREWTGIDRLRLDKFYMLMRMVLNESLKVLKMQGWEERQIEELLELLMTEILHPSSQAPNGVKSHFIEIFLEELTKVGAEELTADQNLKFIDPFCRIAARTKDSLVLNNITRGIFETIVEQAPLAIEDLLNELDTQDEEVASDSDESSEGGERGDALSQKRSEKPPAGSICRAEPEAGEEQAGDDRDSGGPVLQFDYEAVANRLFEMASRQSTPSQNRKRLYKVIRKLQDLAGGIFPEDEIPEKACRRLLEGRRQKKTKKQKRLLRLQQERGKGEKEPPSPGMERKRSRRRGVGADPEARAEAGEQPGTAERALLRDQPRGRGQRGARQRRRTPRPLTSARAKAANVQEPEKKKKRRE
Protein: Odorant receptor coreceptor (AgOr7) (Gustatory and odorant receptor 7) (Q7QCC7)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Orco is a universal and integral part of the functional odorant receptor, involved in the dendritic localization of other olfactory receptors. Can form functional ion channels in the absence of an odor-binding OR. Plays a key role in preferred attraction of females for humans over non-human hosts for blood feeding. Human attraction plays a crucial role in the transmission of Plasmodium protozoans by the mosquito leading to infection diseases like malaria. Also required for the response to N,N-Diethyl-meta-toluamide (DEET), the most widely used insect repellent worldwide.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor Or2
- Odorant receptor Or1
- AGAP011978-PA
Sequence:
MQVQPTKYVGLVADLMPNIRLMQASGHFLFRYVTGPILIRKVYSWWTLAMVLIQFFAILGNLATNADDVNELTANTITTLFFTHSVTKFIYFAVNSENFYRTLAIWNQTNTHPLFAESDARYHSIALAKMRKLLVLVMATTVLSVVAWVTITFFGESVKTVLDKATNETYTVDIPRLPIKSWYPWNAMSGPAYIFSFIYQIYFLLFSMVQSNLADVMFCSWLLLACEQLQHLKGIMRSLMELSASLDTYRPNSSQLFRAISAGSKSELIINEEKDPDVKDFDLSGIYSSKADWGAQFRAPSTLQTFDENGRNGNPNGLTRKQEMMVRSAIKYWVERHKHVVRLVSAIGDTYGPALLLHMLTSTIKLTLLAYQATKIDGVNVYGLTVIGYLCYALAQVFLFCIFGNRLIEESSSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMTISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK
Protein: Galactocerebrosidase (GALCERase) (EC 3.2.1.46) (Galactosylceramidase) (Q5SNX7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Hydrolyzes the galactose ester bonds of glycolipids such as galactosylceramide and galactosylsphingosine.
Subcellular location: Lysosome {ECO:0000250}.
Interaction partners:
- Non-lysosomal glucosylceramidase
- Arylsulfatase A.
- N-acylsphingosine amidohydrolase
- Acid ceramidase
- UDP glycosyltransferase 8
- UDP-glucose ceramide glucosyltransferase.
- Ceramide kinase family protein
- Sphingomyelin phosphodiesterase
- Alpha-galactosidase
- Ceramide kinase
Sequence:
MQTHNFLCIISVILGCSAQFYVIDDRIGLGREFDGIGGLSGGGATSRLLVNYEEPYRSQILDYLFKPNFGASLHILKVEIGGDAQTTDGTEPSHMHSKDEGNFFRGYEWWLMKEAKKRNPNIKLIGLPWAFPGWVGYGTQWPYFFPNVTANYVITWVMGAKQHHNLDIDYIGIWNEKAFDPTYIKVLRDALDRAGFTNIGIIAADGDWSIASAMLDDPYLNDAVEVIGVHYPGTNTVKEALLTERKLWSSEDYSTYNDDIGAGCWARILNQNYVNGKMTSTISWNVIASYYENLSFGRDGLMTAEEPWSGHYIVESPIWMTAHTTQFTQPGWFYLQTVGKLNHGGSYVALTDRKGNLTIIIETMTHEHSQCIRPPLPHFDVSPQIATFELKGSFAHLADLQVWYSKLDFKSGNGTLFKQLRPIRAHNGLLSLKLDVDEVFTITTVTTAQRGFYPEPPKSCPFPKNYTDDFTIDNPPFSEAPYFADQTGVFEYFRNTTDNSSHAFTLRQVVTERPVAWAKDADQTISIIGDYSWSDVNVSCDVFIETPKTGGVFLAARVDQGGESVRQAKGVFYWIYANGTYRVTNDIGGKRVLAEGLSGTKAGVWYTLTLSVKGYFATGSLNGFPLWKNAAVLEPKSGWAALGTLSFEYAQFDNFNVIAG