wanglab/gogpt-training-data huggingface dataset:
Protein: Hexokinase-1 (EC 2.7.1.1) (Brain form hexokinase) (Hexokinase type I) (HK I) (Hexokinase-A) (P19367)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively). Does not phosphorylate N-acetyl-D-glucosamine. Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (By similarity). Involved in innate immunity and inflammation by acting as a pattern recognition receptor for bacterial peptidoglycan. When released in the cytosol, N-acetyl-D-glucosamine component of bacterial peptidoglycan inhibits the hexokinase activity of HK1 and causes its dissociation from mitochondrial outer membrane, thereby activating the NLRP3 inflammasome.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:1985912, ECO:0000269|PubMed:27374331}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:27374331}. Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane (Probable). Dissociates from the mitochondrial outer membrane following inhibition by N-acetyl-D-glucosamine, leading to relocation to the cytosol (PubMed:27374331). {ECO:0000269|PubMed:27374331, ECO:0000305|PubMed:1985912}.
Interaction partners:
- Non-selective voltage-gated ion channel VDAC1
- ATP-dependent 6-phosphofructokinase, platelet type
- ATP-dependent 6-phosphofructokinase, muscle type
- Glucose-6-phosphate isomerase
- Hexokinase-2
- Hexokinase-3
- ATP-dependent 6-phosphofructokinase, liver type
- Hexokinase HKDC1
- Mannose-6-phosphate isomerase
- Fructose-1,6-bisphosphatase 1
Sequence:
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRLRTEASS
Protein: Cuticular protein 67Fb (GEO12069p1) (Q9VTC8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIKTALIISLFLVAAIRAADESQAETTKYRNEIKPDGSYSWEYGTSNGIDAQESGVGGVQAAGSVSYAAPDGTPIQLEYTADENGYRPTGAHLPTPPPIPDYILKALAYIEAHPFQRIQLKK
Protein: Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23) (OMP decarboxylase) (OMPDCase) (OMPdecase) (Uridine 5'-monophosphate synthase) (UMP synthase) (P33283)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- orotate phosphoribosyltransferase
- Dihydroorotate dehydrogenase
- Uridylate kinase
- Candida glabrata strain CBS138 chromosome M complete sequence
- uracil phosphoribosyltransferase
- Uridine kinase
- Phosphoribosylaminoimidazole carboxylase
- Candida glabrata strain CBS138 chromosome M complete sequence
- 3-isopropylmalate dehydrogenase
- Candida glabrata strain CBS138 chromosome H complete sequence
Sequence:
MSSASYLQRAEAHPSPVASKLLKLMHEKKTNLCASLDVTTTSELLKLVDTLGPYICLLKTHVDILSDFSFENTVKPLKEMAAKHNFLIFEDRKFADIGNTVKLQYTSGVYKIAEWADITNAHGVTGQGIVTGLKQGAEETTNEPRGLLMLAELSSKGSLAHGEYTKGTVDIAKSDKDFVIGFIAQKDMGGRDEGFDWLIMTPGVGLDDKGDALGQQYRTVDEVFSTGTDIIIVGRGLFAKGRDPKTEGERYRKAGWDAYLKRIGN
Protein: Facilitated trehalose transporter Tret1 (AgTRET1) (Q7PIR5)
Organism: Anopheles gambiae (African malaria mosquito)
Function: High-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20035867}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:20035867}.
Interaction partners:
Sequence:
MNRKVGPVLEYSRRFSRVLCALRDEIRDPLQYGYQRVNTAEGSLSTSTTATSLDTIVLDTNAEDLASVPPRTLQHHQPQRTFSPILETDDTNPFLEPVEKAKSKSSLKSSRVSFDQEDDRFDEDENSFRKQREHFQKHKSHSTSEHKSQLIKELRHLLATDNRRQFQGKKHVSLDVKSAKVLEQLLKASSSSDDFEGQRKEFQERKHKSLDARHISFKFDKEPSPSSSDEDFEPSTSLLRIDADITKPVIIDLKDLDSSDEEDYISSRKHFQQSKSMSTDSRKSIRFLEMEMGTKEENMRTAVPFVRQITEEGKPKLEVYRPTTNPIYIWTQVLAALSVSLGSMVVGFSSAYTSPALVSMKDRNITSFEVTDQSGSWVGGIMPLAGLAGGILGGPMIEYLGRKNTILATATPFIISWLLIGCATHVAMVLVGRALSGLCVGIASLSLPVYLGETVQPEVRGTLGLLPTAFGNIGILLCFVAGKYLDWSGLAFLGAALPIPFLLLMFLIPETPRWYVSRNREDRARKALQWLRGRKADVEPELKGISKSHQDAERHASSSAMLDLLNKANLKPLLISLGLMFFQQLSGINAVIFYTVQIFQSAGSTIDEKLCTIIVGVVNFIATFIATVLIDRLGRKILLYISDVAMIITLMTLGTFFYMKNNGDDVSEIGWLPLAAFVVFVVGFSLGFGPIPWLMMGEILPGKIRGSAASVATAFNWSCTFVVTKTFADITASIGNHGAFWMFGSICIVGLLFVIVYVPETQGKSLEDIERKMMGRVRRMSSVANIKPLSFNM
Protein: Fgl2 protein (Q6IN12)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
SAVLAACRAAEKHNLTEGLEDASAQAACPARLEGSGRCEGSQCPFQLTLPTLTLQLPQQFGSMEEVLKEVRTLQEAVDSLKKSCQDCKLQADEHPDPGGNGAETAEDNRVQELESQVNKLSSELKNAKEEIQGLQGRLESLQLVNMNNIENYVDNKVANLTSVVNSLDSKCFKCPSQEHNQPNPVQHLIYKDCSDYYVLGKRSSGTYRVTPDHRNSSFEVYCDMETTGGGWTVLQARLDGSTNFTRGWKDYKAGFGNLEREFWLGNDKIHLLTKSKEMILRIDLEDFNGLTLYAVYDQFYVANEFLKYRLHLGNYNGTAGDALRFSRHYNHDLRFFTTPDRDNDRYPSGNCGLYYSSGWWFDACLSANLNGKYYHQRYKGVRNGIFWGTWPGVSQAHPGGYKFSFKKAKMMIRPKSFKP
Protein: WD repeat-containing protein 18 (A0A0A0MQU0)
Organism: Homo sapiens (Human)
Subcellular location: Dynein axonemal particle {ECO:0000256|ARBA:ARBA00024190, ECO:0000256|RuleBase:RU369067}. Nucleus, nucleolus {ECO:0000256|RuleBase:RU369067}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642, ECO:0000256|RuleBase:RU369067}. Cytoplasm {ECO:0000256|RuleBase:RU369067}. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions. {ECO:0000256|RuleBase:RU369067}.
Interaction partners:
Sequence:
XAPMEVAVCTDSAAPMWSCIVWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSVLQADPSRIPAPRHVWSHHALPITDLHCGFGGPLARVATSSLDQTVKLWEVSSGELLLSVLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERSFHPEQDAGKVFKGNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTVALKGPVTNAAILLAPVSMLSSDFRPSLPLPHFNKHLLGAEHGDEPRHGGLTLRLGLHQQGSEPSYLDRTEQLQAVLCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRDLFDFSTRFITRPAK
Protein: Probable HTH-type transcriptional regulator LrhA (P36771)
Organism: Escherichia coli (strain K12)
Function: Not known, does not seem to act on the proton translocating NADH dehydrogenase genes (nuoA-N) which are part of the lrhA operon.
Interaction partners:
- HTH-type transcriptional activator AaeR
- Uncharacterized HTH-type transcriptional regulator YfiE
- Transcriptional activator protein LysR
- Hca operon transcriptional activator HcaR
- HTH-type transcriptional regulator CynR
- Uncharacterized HTH-type transcriptional regulator YafC
- HTH-type transcriptional regulator AbgR
Sequence:
MISANRPIINLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEACSSLMFSNLQGVLTIGASDESADTILPFLLNRVSSVYPKLALDVRVKRNAYMAEMLESQEVDLMVTTHRPSAFKALNLRTSPTHWYCAAEYILQKGEPIPLVLLDDPSPFRDMVLATLNKADIPWRLAYVASTLPAVRAAVKAGLGVTARPVEMMSPDLRVLSGVDGLPPLPDTEYLLCYDPSSNNELAQVIYQAMESYHNPWQYSPMSAPEGDDSLLIERDIE
Protein: Hepatoma-derived growth factor (HDGF) (High mobility group protein 1-like 2) (HMG-1L2) (P51858)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. Has mitogenic activity for fibroblasts. Heparin-binding protein.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:11751870, ECO:0000269|PubMed:26845719}. Cytoplasm {ECO:0000269|PubMed:11751870}. Secreted, extracellular exosome {ECO:0000269|PubMed:27926477}. Note=Secreted by exosomes and is located inside the exosome (PubMed:27926477). May also be secreted as free protein via an as yet unknown pathway (PubMed:27926477). {ECO:0000269|PubMed:27926477}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:26845719}. Cytoplasm {ECO:0000269|PubMed:26845719}. Secreted, extracellular exosome {ECO:0000269|PubMed:27926477}. Note=Secreted by exosomes and is located on the outer exosome surface. {ECO:0000269|PubMed:27926477}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:26845719}. Cytoplasm {ECO:0000269|PubMed:26845719}. Secreted, extracellular exosome {ECO:0000269|PubMed:27926477}. Note=Secreted by exosomes and is located on the outer exosome surface. {ECO:0000269|PubMed:27926477}.
Interaction partners:
- Midkine
- Pleiotrophin
- X-box-binding protein 1
- Fibroblast growth factor 4
- Fibroblast growth factor 17
- Fibroblast growth factor 2
- Probable ATP-dependent RNA helicase DDX5
- Nucleoside diphosphate-linked moiety X motif 6
- Nucleolin
- Azurocidin
Sequence:
MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEAAEGDGDKKGNAEGSSDEEGKLVIDEPAKEKNEKGALKRRAGDLLEDSPKRPKEAENPEGEEKEAATLEVERPLPMEVEKNSTPSEPGSGRGPPQEEEEEEDEEEEATKEDAEAPGIRDHESL
Protein: Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic (CPS) (CPSase) (EC 6.3.4.16) (EC 6.3.5.5) (Ammonium-dependent carbamoyl phosphate synthetase) (Arginine-specific carbamoyl phosphate synthetase, ammonia chain) (Glutamine-dependent carbamoyl phosphate synthetase) (Protein VENOSA 3) (Q42601)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the carbamoyl-phosphate synthetase (CPS) composed of a small chain CARA/VEN6 and a large chain CARB/VEN3. Involved in arginine biosynthesis. Required for mesophyll development.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Argininosuccinate synthase, chloroplastic
- Carbamoyl phosphate synthase small chain, chloroplastic
- Ornithine transcarbamylase, chloroplastic
- Aspartate carbamoyltransferase, chloroplastic
- Amidophosphoribosyltransferase 2, chloroplastic
- Dihydroorotate dehydrogenase
- Amidophosphoribosyltransferase 3, chloroplastic
- Uridine 5'-monophosphate synthase
- Amidophosphoribosyltransferase 1, chloroplastic
- Glutamine synthetase cytosolic isozyme 1-1
Sequence:
MRNHCLELSSNCSSIFASSKSNPRFSPSKLSYSTFFSRSAIYYRSKPKQASSSSSFSTFPPCLNRKSSLTHVLKPVSELADTTTKPFSPEIVGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALREEGYEVILINSNPATIMTDPETANRTYIAPMTPELVEQVIEKERPDALLPTMGGQTALNLAVALAESGALEKYGVELIGAKLGAIKKAEDRELFKDAMKNIGLKTPPSGIGTTLDECFDIAEKIGEFPLIIRPAFTLGGTGGGIAYNKEEFESICKSGLAASATSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDREYQRLRDYSIAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDITRKTPASFEPSIDYVVTKIPRFAFEKFPGSQPLLTTQMKSVGESMALGRTFQESFQKALRSLECGFSGWGCAKIKELDWDWDQLKYSLRVPNPDRIHAIYAAMKKGMKIDEIYELSMVDKWFLTQLKELVDVEQYLMSGTLSEITKEDLYEVKKRGFSDKQIAFATKTTEEEVRTKRISLGVVPSYKRVDTCAAEFEAHTPYMYSSYDVECESAPNNKKKVLILGGGPNRIGQGIEFDYCCCHTSFALQDAGYETIMLNSNPETVSTDYDTSDRLYFEPLTIEDVLNVIDLEKPDGIIVQFGGQTPLKLALPIKHYLDKHMPMSLSGAGPVRIWGTSPDSIDAAEDRERFNAILDELKIEQPKGGIAKSEADALAIAKEVGYPVVVRPSYVLGGRAMEIVYDDSRLITYLENAVQVDPERPVLVDKYLSDAIEIDVDTLTDSYGNVVIGGIMEHIEQAGVHSGDSACMLPTQTIPASCLQTIRTWTTKLAKKLNVCGLMNCQYAITTSGDVFLLEANPRASRTVPFVSKAIGHPLAKYAALVMSGKSLKDLNFEKEVIPKHVSVKEAVFPFEKFQGCDVILGPEMRSTGEVMSISSEFSSAFAMAQIAAGQKLPLSGTVFLSLNDMTKPHLEKIAVSFLELGFKIVATSGTAHFLELKGIPVERVLKLHEGRPHAADMVANGQIHLMLITSSGDALDQKDGRQLRQMALAYKVPVITTVAGALATAEGIKSLKSSAIKMTALQDFFEVKNVSSLLV
Protein: Eukaryotic translation initiation factor 4G (eIF-4G) (eIF4G) (Protein synthesis initiation factor 4G) (A0A1S3C4H6)
Organism: Cucumis melo (Muskmelon)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome.
Interaction partners:
Sequence:
MSFNQSRSDKNEGYTQYRKSGRSNNFNPQRGSSGTHSKPGGAGGSAPTSSIASNRSFKKTNNAQGGQSRGGLPAVNSTDSSNAPNPRGVQNGAVAKPPEGPHSQRSTRDVPKAPTSQSAPLSSDGPAPTTPAKGTGDQPKEFAFQFGSISPGFMNGMQLPVRTSSAPPNLDEQKRDQARHESFRPVPPMPIPLAPKPQTQRKDTGAGDQPNVGQQLQQKDTGIINQPNTGDAHTVQKAKKDMQASPNHPTNQTQKPTTPMSGISMTMPYHPPQVPVPFGGPNQQMQSQGLTPTSLHMSIPVPLQIGSSPQVQQPMFVPGLHPHPMQPQGIIHQGQGLGFATQIGSQLPPQLSNLGMNVTSQYPQQQGGKFGGPRKSAVRITDPKTHEELIFDNKQSNAYADTGTSGPRPPYNLPSQTQPLPYAPSHAMNYYPNSYNPNPLYFASPSSLPLPSGQSAPNSQPHRFNYPVSQGSQNVPYIDMHVKKPSGGPMHGISDPPNREHTRDTHTFQPPAPSGTVHVTIKMPTDPTGGKGSDTLPNKLPTTEEGKSQKPSSPSVDLIPPSQRAVDTTSESSLHDSKLGREPSGIKSSPVISKQFTDGPPMVSLESQDSSSVQSSLTASSEESELAVAHSEVRRENLLGSDLHKDHQKKTSKKGYAQSLQHQISGQASSALGVPCQVQDTTSPLVSEAVEAKSLIIPAVVGGKSVSVSAVTSDPLESKDAGLVSVAHSSSPENPGLGNVKNLDLISDDNQDTSSKEKNSEPVVLKIEEQGQATFSEPPVDLKNSENVLDHDVSKSVEVAEKTERNLIVSSATVSNEVLTSETAQRAVDEPVSCNAEADVSASVSSSSTVPENSQDDKLVVDSSGRYDNMSSNEVLKNVVKSDQPSEPALNPGLSEGKNDGEVLDTVGTCANSSQGVSGTKDKSVVETSRVKGTTGKAKKRLKAILQMADAAGTTSDLYNAYKRPEEKKETVAHSESIERTESRSSSVDTEQESNEAIKEDAGALSKAEPDDWEDAADIATPDLESANGDGVGTSMLDSGDRTGDMAKKYSRDFLLKFAEQFLDLPHNFEVTSDIESLMSTHTNVSHHHDRDPYPSPGRVDRPSSGGSRLDRRGSNLVDDDRWSKLPGPFAPGQDPRLDLAYGATAGFRPGQGPNFGVLRNPRAQAPVQYAGGILAGPMQSMGPQGGLQRNNSDADRWQRATNFQKGLIPSPLTPLQTMHKAKKKYEVGKVSDEEETKQRQLKAILNKLTPQNFEKLFEQVKAVNIDNGRTLTGVISQIFDKALMEPTFCEMYANFCFHLAGELPDLSEDNEKITFKRLLLNKCQEEFERGEREQEEANKVEEEGEVKQSEEEREEKRIKARRRMLGNIRLIGELYKKKMLTERIMHECIKKLLGEYQNPDEEDVEALCKLMSTIGEMIDHPRAKDYMDSYFEIMTMLSNNMKLSSRVRFMLKDAIDLRKNKWQQRRKVEGPKKIEEVHRDAAQERQAQTGRFGRGPSINSSARRGGPPMDYGPRGSVVSSPGNQMGGFRAFLHQPRGYGGNQDARQDERQSYEARTLSVTSQRAGGDESITLGPQGGLARGMSIRGPQPSSAAPADMSPLPGDLRSAPIASLNGYSSASERATLTSKEDLISRHMPERFAGPTSMDHISSPERYSNYGNKDLRHSGRSFDRSRPISPATPPGPALTPSLPSEKVLSEDRLQQLSLTAIKEFYSARDEKEVALCIKELNSPAFHPTMISLWVTDVFERTNLERDLLAKLVVNLSRPNNGTLNQAHLVKGFEAVLGNLEDSVNDAPRAPEYLGQILGKVITESMVSLREVADLICQGGEVPGNLLQSGLGADVLGNILKTIKTEKGEGFLTDLRTNSNLRLETFLPPDPVKSRVLEEFI
Protein: Putative respiratory burst oxidase homolog protein G (EC 1.11.1.-) (EC 1.6.3.-) (NADPH oxidase RBOHG) (AtRBOHG) (Q9SW17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-dependent NADPH oxidase that generates superoxide.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- AICARFT/IMPCHase bienzyme family protein
- Tetratricopeptide repeat
- At5g47635
- Calcium-dependent protein kinase 10
- Putative L-type lectin-domain containing receptor kinase I.1
Sequence:
MQRVSFEVKDTEAEKSSSEILSGSLPSTYRNPAMENVGNAVDDGSSVKNNPKLDMQKQNGLVKWFKKCLTMVSGESKAPRLDRSKSTAGQALKGLKIISKTDGNAAWTVVEKRYLKITANTDGLLLRSKFGECIGMNSKEFALELFDALARKSHLKGDVITETELKKFWEQINDKSFDSRLITFFDLMDKDSDGRLTEDEVREIIKLSSSANHLSCIQNKADEYAAMIMEELDPDHMGYIMMESLKKLLLQAETKSVSTDINSEERKELSDMLTESLKPTRDPNHLRRWYCQLRFFVLDSWQRVWVIALWLTIMAILFAYKYIQYKNRAVYEVLGPCVCLAKGAAETLKLNMALILLPVCRNTITWLRNKTRLGVFVPFDDNLNFHKVIAVGIAIGVAIHSVSHLACDFPLLIAATPAEYMPLGKFFGEEQPKRYLHFVKSTEGITGLVMVFLMVIAFTLAMPWFRRGKLEKKLPGPLKKLASFNAFWYTHHLFVIVYILLVLHGYYIYLNKEWYKKTTWMYLAVPVALYAYERLIRAFRSSIRTVKVLKMAAYPGKVLTLQMSKPTNFKYMSGQYMFVNCPAVSPFEWHPFSITSTPQDDYLSVHIKALGDWTEAIQGVFSEVSKPPPVGDMLNGANSPRFPKIMIDGPYGAPAQDYKKYEVVLLIGLGIGATPMISIIKDIINNTETKEQLSQMEKGSPQEQQGNKETFKTRRAYFYWVTKEQGTFDWFKNIMNEIAERDKSKVIELHNHCTSVYEEGDVRSALIRMLQSLNYAKNGLDIVAGTRVMSHFARPNWKNVYKQIAMDHPGANVGVFYCGAPVLTKELRQLALEFTHKTSTRFSFHKENF
Protein: Uncharacterized protein C212.03 (Q9HGP9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSIEFDDSSRHNMNMTQLMQLGAFDRRSGDDFMVQDFKNGIRDCSGIPVNNRNLAFKAYDAVKQKCDSSIKVFNIQDITIKGATWQHHNCQSTGKWYSQLYDYQNTFIGKQEYNILFDCYSYLKYNLNG
Protein: Lysophosphatidic acid receptor 2a (Zgc:101053) (Q6DC27)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
Sequence:
MVFNSCEAFDNPVSYFYNRTGKPISPNWRTHDFVVVGLGLPICVFIILANMLVIAAIIVNRKFHFPIYYLLGNMAAADLFAGISYSYLVFHTGPWTINLTIKEWFVRGALINMSLTASVVNLLAVAVERHQTIFTMQLHTTMTRWRVVMLIVTIWVVAVVMGLVPTMGWNCVCDQLGCSTVAPLYSRSFLVFWAILNLMAFFIMVAVYTHIFIYVRRRSQVMSPHTDQPSNNQTVISLMKTMSMILGAFVICWTPGLVILLLDGLKCIECHVLKYEKYCLVLAECNSLVNPIIYSFRDEDMRTTYKRILCFPWRRMRPHEGPSGIRFEPVKTGAPPEKNSQNSSSPEAAPPQSPLS
Protein: Interleukin-1 alpha (IL-1 alpha) (P01582)
Organism: Mus musculus (Mouse)
Function: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P01583}. Cytoplasm {ECO:0000250|UniProtKB:P01583}. Secreted {ECO:0000250|UniProtKB:P01583}. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. Recruited to DNA damage sites and secreted after genotoxic stress. {ECO:0000250|UniProtKB:P01583}.
Interaction partners:
- Interleukin-1 receptor type 1
- Interleukin-1 beta
- Interleukin-1 receptor type 2
- Interleukin-2
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-3
- Granulocyte colony-stimulating factor
- Interleukin-4
- Interleukin-1 receptor accessory protein
- Interferon gamma
Sequence:
MAKVPDLFEDLKNCYSENEDYSSAIDHLSLNQKSFYDASYGSLHETCTDQFVSLRTSETSKMSNFTFKESRVTVSATSSNGKILKKRRLSFSETFTEDDLQSITHDLEETIQPRSAPYTYQSDLRYKLMKLVRQKFVMNDSLNQTIYQDVDKHYLSTTWLNDLQQEVKFDMYAYSSGGDDSKYPVTLKISDSQLFVSAQGEDQPVLLKELPETPKLITGSETDLIFFWKSINSKNYFTSAAYPELFIATKEQSRVHLARGLPSMTDFQIS
Protein: Peroxisomal membrane protein PMP34 (34 kDa peroxisomal membrane protein) (Solute carrier family 25 member 17) (O43808)
Organism: Homo sapiens (Human)
Function: Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extent for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal matrix by a counter-exchange mechanism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14709540}. Peroxisome membrane {ECO:0000269|PubMed:11121399, ECO:0000269|PubMed:11402059, ECO:0000269|PubMed:14709540, ECO:0000269|PubMed:9874197}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisomal biogenesis factor 19
- Mitochondrial carrier homolog 1
- Mitochondrial carrier homolog 2
- Peroxisomal membrane protein PEX16
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein 11B
- Peroxisomal biogenesis factor 3
- ATP-binding cassette sub-family D member 3
- ATP-binding cassette sub-family D member 1
Sequence:
MASVLSYESLVHAVAGAVGSVTAMTVFFPLDTARLRLQVDEKRKSKTTHMVLLEIIKEEGLLAPYRGWFPVISSLCCSNFVYFYTFNSLKALWVKGQHSTTGKDLVVGFVAGVVNVLLTTPLWVVNTRLKLQGAKFRNEDIVPTNYKGIIDAFHQIIRDEGISALWNGTFPSLLLVFNPAIQFMFYEGLKRQLLKKRMKLSSLDVFIIGAVAKAIATTVTYPLQTVQSILRFGRHRLNPENRTLGSLRNILYLLHQRVRRFGIMGLYKGLEAKLLQTVLTAALMFLVYEKLTAATFTVMGLKRAHQH
Protein: Target of early activation tagged (EAT) 2 (F4JXG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLDLNLDVDSTESTQNERDSITVKGVSLNQMDESVTSNSSVVNAEASSCIDGEDELCSTRTVKFQFEILKGGGEEEEEDDDERSAVMMTKEFFPVAKGMNFMDSSAQSSRSTVDISFQRGKQGGDFIGSGSGGGDASRVMQPPSQPVKKSRRGPRSKSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAVKFRGLEADINFVIGDYEEDLKQMANLSKEEVVQVLRRQSSGFSRNNSRYQGVALQKIGGWGAQMEQLHGNMGCDKAAVQWKGREAASLIEPHASRMIPEAANVKLDLNLGISLSLGDGPKQKDRALRLHHVPNNSVCGRNTMVQFFLQCTKYDLLYFHMRFAATMENHMAAAACDTPFNFLKRGSDHLNNRHALPSAFFSPMERTPEKGLMLRSHQSFPARTWQGHDQSSGGTAVAATAPPLFSNAASSGFSLSATRPPSSTAIHHPSQPFVNLNQPGLYVIHPSDYISQHQHNLMNRPQPPP
Protein: Scytovirin (SVN) (P86041)
Organism: Scytonema varium
Function: Has strong anti-HIV activity against T-tropic strains of HIV-1 and weaker activity against M-tropic strains of HIV-1. Inhibits HIV-1 fusion and infection of CD4 LTR beta-gal cells in vitro. Inhibits fusion of HIV infected CEM-SS cells with uninfected CEM-SS cells, and fusion of HIV-1 Env expressing HL2/3 cells with CD4 LTR beta-gal cells. Binds to HIV gp120, HIV gp160 and to a lesser extent HIV gp41. Binding to HIV gp120 is glycosylation dependent. Binds with high specificity to the tetrasaccharide Man-alpha-1,2-Man-alpha-1,6-Man-alpha-1,6-Man and also binds the higher-order oligosaccharides oligomannose 8 and oligomannose 9. Does not bind to monosaccharides, complex or hybrid N-linked oligosaccharides or chitin.
Interaction partners:
Sequence:
GSGPTYCWNEANNPGGPNRCSNNKQCDGARTCSSSGFCQGTSRKPDPGPKGPTYCWDEAKNPGGPNRCSNSKQCDGARTCSSSGFCQGTAGHAAA
Protein: Auxilin-related protein 2 (Q0WQ57)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes probably uncoating of clathrin-coated vesicles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18433157}.
Interaction partners:
- Clathrin heavy chain 1
- Clathrin heavy chain 2
- AP-2 complex subunit alpha-2
- AP-5 complex subunit mu
- AP-2 complex subunit alpha-1
- Coatomer subunit beta'-1
- Coatomer subunit beta'-2
- Beta-adaptin-like protein B
- Exocyst subunit Exo70 family protein
- Calcium-binding EF hand family protein
Sequence:
MDDFTGLLARDFGLKPQGKSAPMASQSNSSAADFNTFASSYSFASAAGKKSDSLPVFDDLGRDGDDLLFRDVFSGPPPKYGSSGDSRSPSAPAFDYDVMFKEPKSKSASSMPVYDKPVYDDEDVFESIPELKIPSTSSQSARFENVFSSISSSPTKHRKQNSSPFDDLMGNNLGKKESDREEKGSSIFDDLIPGFGRTSSPPAKRTTSETTSQSQKPPYRTAETSSNVKEDPFVVLEESTSTLREPSTGGFTDPLEEIGKFNSRKTDHSSVHGGVFVDTDPLDSLGKSGPDMNSRGKSHLRPPGNISGSQSPVESSGLYHSKNVSFDDVVEPQNTSTPPPTNSDGSFESSDDVWLTVSEIPLFTQPTSAPPPTRPPPPRPTRPIKKKVNEPSIPTSAYHSHVPSSGRASVNSPTASQMDELDDFSIGRNQTAANGYPDPSSGEDSDVFSTAAASAAAMKDAMDKAEAKFRHAKERREKESLKASRSREGDHTENYDSRERELREKQVRLDRERAEREAEMEKTQAREREEREREQKRIERERERLLARQAVERATREARERAATEAHAKVQRAAVGKVTDARERAERAAVQRAHAEARERAAAGAREKAEKAAAEARERANAEVREKEAKVRAERAAVERAAAEARGRAAAQAKAKQQQENNNDLDSFFNSVSRPSSVPRQRTNPPDPFQDSWNKGGSFESSRPSSRVPSGPTENLRKASSATNIVDDLSSIFGAPASQSGGFQDVDGETEERRRARLERHQRTQERAAKALAEKNERDLQVQREQAEKDRIGGTLDVEIRRWGAGKEGNLRALLSTLQYVLWPECGWQPVSLTDLITGASVKKVYRKATLCIHPDKVQQKGANLQQKYIAEKVFDMLKEAWNKFNSEELF