wanglab/gogpt-training-data huggingface dataset:
Protein: Ecotropic viral integration site 5 protein homolog (EVI-5) (Neuroblastoma stage 4S gene protein) (O60447)
Organism: Homo sapiens (Human)
Function: Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Associates with the mitotic spindle through anaphase and remains within the midzone and midbody until completion of cytokinesis.
Interaction partners:
- Ras-related protein Rab-11A
- F-box only protein 5
- Outer dense fiber protein 2
- Serine/threonine-protein kinase PLK1
Sequence:
MVTNKMTAAFRNPSGKQVATDKVAEKLSSTLSWVKNTVSHTVSQMASQVASPSTSLHTTSSSTTLSTPALSPSSPSQLSPDDLELLAKLEEQNRLLETDSKSLRSVNGSRRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVNEWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLCSAQSMPIKDQYSELLKMTSPCEKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEEAFCVFVKLMQDYRLRELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELMQLDMEGMLQHFQKVIPHQFDGVPDKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELRCLKGQRGFSGQPPFDGIHIVNHLIGDDESFHSSDEDFIDNSLQETGVGFPLHGKSGSMSLDPAVADGSESETEDSVLETRESNQVVQKERPPRRRESYSTTV
Protein: UPF0056 membrane protein YhcE (P25743)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YhcF
Sequence:
MIQTFFDFPVYFKFFIGLFALVNPVGIIPVFISMTSYQTAAARNKTNLTANLSVAIILWISLFLGDTILQLFGISIDSFRIAGGILVVTIAMSMISGKLGEDKQNKQEKSETAVRESIGVVPLALPLMAGPGAISSTIVWGTRYHSISYLFGFFVAIALFALCCWGLFRMAPWLVRVLRQTGINVITRIMGLLLMALGIEFIVTGIKGIFPGLLN
Protein: Aldehyde dehydrogenase family protein (P96405)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MSDSATEYDKLFIGGKWTKPSTSDVIEVRCPATGEYVGKVPMAAAADVDAAVAAARAAFDNGPWPSTPPHERAAVIAAAVKMLAERKDLFTKLLAAETGQPPTIIETMHWMGSMGAMNYFAGAADKVTWTETRTGSYGQSIVSREPVGVVGAIVAWNVPLFLAVNKIAPALLAGCTIVLKPAAETPLTANALAEVFAEVGLPEGVLSVVPGGIETGQALTSNPDIDMFTFTGSSAVGREVGRRAAEMLKPCTLELGGKSAAIILEDVDLAAAIPMMVFSGVMNAGQGCVNQTRILAPRSRYDEIVAAVTNFVTALPVGPPSDPAAQIGPLISEKQRTRVEGYIAKGIEEGARLVCGGGRPEGLDNGFFIQPTVFADVDNKMTIAQEEIFGPVLAIIPYDTEEDAIAIANDSVYGLAGSVWTTDVPKGIKISQQIRTGTYGINWYAFDPGSPFGGYKNSGIGRENGPEGVEHFTQQKSVLLPMGYTVA
Protein: cDNA FLJ60222, highly similar to Homo sapiens sarcolemma associated protein (SLMAP), mRNA (cDNA, FLJ79335, highly similar to Homo sapiens sarcolemma associated protein (SLMAP), mRNA) (B7Z964)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNKPWPWMPMLAALVAVTAIVLYVPGLARASP
Protein: Polypeptide N-acetylgalactosaminyltransferase 5 (pp-GaNTase 5) (EC 2.4.1.41) (Protein-UDP acetylgalactosaminyltransferase 5) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5) (Q95ZJ1)
Organism: Caenorhabditis elegans
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
- GLY-16
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Bromo domain-containing protein
- Putative tyrosinase-like protein tyr-1
Sequence:
MIIFKKKAILKVLLLVPVFWICSLIFFAATSNDSSQIGSNNDLANKIAEANFHPKAAKQDVIQGFGPPIEPEPVVENNKVEEEEQPGGNLAKPKFMVDPNDPIYKKGDAAQAGELGKAVVVDKTKLSTEEKAKYDKGMLNNAFNQYASDMISVHRTLPTNIDAECKTEKYNENLPRTSVIICFHNEAWSVLLRTVHSVLERTPDHLLEEVVLVDDFSDMDHTKRPLEEYMSQFGGKVKILRMEKREGLIRARLRGAAVATGEVLTYLDSHCECMEGWMEPLLDRIKRDPTTVVCPVIDVIDDNTFEYHHSKAYFTSVGGFDWGLQFNWHSIPERDRKNRTRPIDPVRSPTMAGGLFSIDKKYFEKLGTYDPGFDIWGGENLELSFKIWMCGGTLEIVPCSHVGHVFRKRSPYKWRTGVNVLKRNSIRLAEVWLDDYKTYYYERINNQLGDFGDISSRKKLREDLGCKSFKWYLDNIYPELFVPGESVAKGEVRNSAVQPARCLDCMVGRHEKNRPVGTYQCHGQGGNQYWMLSKDGEIRRDESCVDYAGSDVMVFPCHGMKGNQEWRYNHDTGRLQHAVSQKCLGMTKDGAKLEMVACQYDDPYQHWKFKEYNEAKAIEHGAKPPS
Protein: Germ cell nuclear acidic protein (Germ cell nuclear acidic peptidase) (Q7KW09)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in DNA-protein cross-links (DPCs) clearance, ensuring the genomic stability by protecting germ cells and early embryos from various sources of damage. Limits replication stress and DNA double-strand breaks.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31839537}. Chromosome {ECO:0000269|PubMed:31839537}. Note=During mitosis, associated with dividing chromosomes. {ECO:0000269|PubMed:31839537}.
Interaction partners:
Sequence:
MADHKYRLFNAVDPSKVSHAPKDHPEKRNDQKTRKLPAAPMRANVGAPAPSCGANTEDTELDNSDYMEALQLSADGCSQDVANVGDVELLSAGISNLKVQPINEEHSAKPEISICISSTTEENVSGDDDAASCITISDSSEDEQEPLPPDSMAVSEREIVANPGQEDIPQPMLTTEKVQRIEAFLRDVSIERREMEWNGPLTPPPLSSSQRQSRLADADTESMSPTDEDWQPPTTRPIYNSTQLANNDTQVNTICSADATRLDSSKRLADDETEANTLGSEELEPTYSSKRLADNDTEPNTLCSDSSETHNSTIHNNEPVPDESIEIPETSSEGELTPQKASSGSSTSGGDEHGSIQVSSINISAKINIKISIPTMESSSAEDDDEHYSSPRATKSLPSSEEVQHQEHQQQDPQSHQKSMLSVDDASEDEQFLTHAEKLLNQLYGKSWQTPDVIRTLKRSSGSGGKQAPLRPRNIQATAVTTAKKKKPKPDESVLGDFSIFTKPLRTNQTPLNSTRLPPMRAVQTERRPRTQKPLTRPRTNHIDEDRWRKLIDSDSGTDASDDEDADATFSESGSDSDSDKDKENKQKRGDLTYLDLSKDEVEVISNPDQDSPSPKCHRRLDDILRSCRASVKAKLPATPVQQPNIRRQLFTPNAGFENDNQAKEIVNRALDLDMLDELESDYLPGTPVHRRVQEVKKKLGIGQQGQTTPHESPILKLLTPKTAPPKGTAPPKTSAPPKVSTPPKSTKQIPKPRKQKDLSPVASGGKCGFLKSLEGQVSRDRADNEAFFYRENFARNKDQLAQHLYKMYNAQVFNNELDVPITWSKLLRNTAGRCMNKRKLNQRSSVVELSVKVLTTADRLRCTLIHELCHAAAWVFNGEGGHGRVWKMWAQRANDKFPDLPQIKVCHNYSIEFKYTYKCLSCDKASHAHSRSRKVEDLRCRICRGPITLFLNKKDKQGNTVSTPAGEAKGFAKFVKDNFQRHKRDNMTAAQVMRILSVEYAKQKGQPAEETAASIASRVETLTLDESSN
Protein: 5-hydroxytryptamine receptor 2B (5-HT-2B) (5-HT2B) (5-HT-2F) (Serotonin receptor 2B) (Stomach fundus serotonin receptor) (P30994)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various ergot alkaloid derivatives and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores (By similarity). Plays a role in the regulation of dopamine and 5-hydroxytryptamine release, 5-hydroxytryptamine uptake and in the regulation of extracellular dopamine and 5-hydroxytryptamine levels, and thereby affects neural activity. Plays a role in the regulation of behavior, including impulsive behavior. Required for normal proliferation of embryonic cardiac myocytes and normal heart development. Protects cardiomyocytes against apoptosis. Plays a role in the adaptation of pulmonary arteries to chronic hypoxia. Plays a role in vasoconstriction. Required for normal osteoblast function and proliferation, and for maintaining normal bone density. Required for normal proliferation of the interstitial cells of Cajal in the intestine (By similarity). May play a role in the perception of pain.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1331748, ECO:0000269|PubMed:1505525, ECO:0000269|PubMed:22525520}; Multi-pass membrane protein {ECO:0000269|PubMed:1505525}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q02152}.
Interaction partners:
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 2C
- 5-hydroxytryptamine receptor 2A
- Guanine nucleotide-binding protein subunit alpha-11
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Basigin
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent L-type calcium channel subunit alpha
- Sodium-dependent serotonin transporter
Sequence:
MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI
Protein: Probable vacuolar protein sorting-associated protein 16 homolog (Q9UT38)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for vacuolar protein sorting. Required for vacuole biogenesis, stability and to maintain vacuole morphology (By similarity).
Interaction partners:
- Vacuolar membrane protein pep3
- Vacuolar protein sorting-associated protein 33
- Vacuolar morphogenesis protein 6
- Vacuolar protein sorting-associated protein 8
- Vacuolar protein sorting-associated protein 41
- Vacuolar protein sorting-associated protein 3
- E3 ubiquitin-protein ligase pep5
- Syntaxin pep12
- Vesicle transport v-SNARE protein vti1
- Ypt/Rab-type GTPase ypt7
Sequence:
MEPSIKYPIYEWELLQDTYYQKSAIGKAEWEYIDPVDFMFAVAPCGGAIAITRSESNLQSNYKYDQVPMYSICVFCLSGQLLQTLTWDKTSLVGMGWNENEELIVVSKQGQVRVYNLLGEFHQFSLGKGVENIGIRECQFSEGGVFALLQNDTFISITGFEEPWRKTYASIPFNTLEYYNIDSWALIPNPFSPDLGMDIVVTVGPHILQIDEQDSQLHSISSLQHVSHISISPNARYLALYESVGKVRVISSDFSKELLDLRLPETVAEASLKQMAWCGNDAVVLVHENLLTLVGPFGGSVPYLYNHTPIVSTEVDGVRILTKDSSEFLRKVPAPLENIFHIGSKTPGAKLVEAFQKMKLKSVFAEKMLLELKDELHDAVDTCVQASLNEFSIEWQKVLLEAASLGKNSLRMYNHQEYVDVCRELRVLNAARDPNVGIYITHEEYLHLGLERLIQRFSCRQLYGLAVQASMWMQIPCDWVYIQWAQTYIKQSSEPEEVVLDNIVKRLSSRKYISYEKIARTAYQEGRLILSTKLLDFEPLAKHQVMLLLNMEAYEQALKKVIETMDNNLIIYVVLQIKQQMAIASFFQILNEYPDAVKVYVEFAKKNDRKTLHDFFYQDDNKQGIAVLAVEDTLKTATVNQRITSLKSAAKVCSESKELSLEEKCLGDEIKLLQLQQTYEDQFTGNFVGLTVNEVVVKLIQINQTQRANKLRSDFQIPEKRFAWLKLRALVAIRDWVQIEQWAGSMRRSPIGFEPFVTEILSAGNKKEAAKYIPRCTQLTTQEKVDMWVQVGDVKSASEEAAKSKSGSVLGDLLERVQTMPESRFVQNALDQLRR
Protein: Glutathione S-transferase T1 (AtGSTT1) (EC 2.5.1.18) (GST class-theta member 1) (Glutathione S-transferase 10) (Q9ZRT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrobenzyl chloride (pNBC), and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Nucleus {ECO:0000269|PubMed:19174456}. Peroxisome {ECO:0000269|PubMed:17951448}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Probable glutathione peroxidase 2
- Probable glutathione peroxidase 3, mitochondrial
- Glutathione S-transferase DHAR2
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Glutathione S-transferase L3
- Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic
- Putative glutathione peroxidase 7, chloroplastic
- Probable glutathione peroxidase 4
- Probable glutathione peroxidase 5
Sequence:
MMKLKVYADRMSQPSRAVIIFCKVNGIQFDEVLISLAKRQQLSPEFKDINPLGKVPAIVDGRLKLFESHAILIYLSSAFPSVADHWYPNDLSKRAKIHSVLDWHHTNLRRGAAGYVLNSVLGPALGLPLNPKAAAEAEQLLTKSLSTLETFWLKGNAKFLLGSNQPSIADLSLVCELMQLQVLDDKDRLRLLSTHKKVEQWIENTKKATMPHFDETHEILFKVKEGFQKRREMGTLSKPGLQSKI
Protein: Hemocyanin subunit 1 (P84461)
Organism: Liocarcinus depurator (Harbour crab) (Portunus depurator)
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular location: Secreted, extracellular space {ECO:0000250|UniProtKB:P84293}.
Interaction partners:
Sequence:
DSPGGASDAQKQ
Protein: Astrotactin-1 (O14525)
Organism: Homo sapiens (Human)
Function: Neuronal adhesion molecule that is required for normal migration of young postmitotic neuroblasts along glial fibers, especially in the cerebellum. Required for normal rate of migration of granule cells during brain development and for normal cerebellum development.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q61137}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q61137}. Perikaryon {ECO:0000250|UniProtKB:Q61137}. Endosome {ECO:0000250|UniProtKB:Q61137}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q61137}. Note=Detected close to the anterior pole and at the base of the leading process in migrating neurons. Is internalized from the membrane via clathrin-coated vesicles and endosomes, and recycled to the anterior pole of the migrating cell. {ECO:0000250|UniProtKB:Q61137}.
Interaction partners:
Sequence:
MALAGLCALLACCWGPAAVLATAAGDVDPSKELECKLKSITVSALPFLRENDLSIMHSPSASEPKLLFSVRNDFPGEMVVVDDLENTELPYFVLEISGNTEDIPLVRWRQQWLENGTLLFHIHHQDGAPSLPGQDPTEEPQHESAEEELRILHISVMGGMIALLLSILCLVMILYTRRRWCKRRRVPQPQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDLRHHLQRECMNGGEDFASQVTRTLDSLQGCNEKSGMDLTPGSDNAKLSLMNKYKDNIIATSPVDSNHQQATLLSHTSSSQRKRINNKARAGSAFLNPEGDSGTEAENDPQLTFYTDPSRSRRRSRVGSPRSPVNKTTLTLISITSCVIGLVCSSHVNCPLVVKITLHVPEHLIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWAMDLCARRLLDPCEHQCDPETGRREHRAAGECLCYEGYMKDPVHKHLCIRNEWGTNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELAINPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSKDNGGCSKNFRCISDRKLDSTGCVCPSGLSPMKDSSGCYDRHIGVDCSDGFNGGCEQLCLQQMAPFPDDPTLYNILMFCGCIEDYKLGVDGRSCQLITETCPEGSDCGESRELPMNQTLFGEMFFGYNNHSKEVAAGQVLKGTFRQNNFARGLDQQLPDGLVVATVPLENQCLEEISEPTPDPDFLTGMVNFSEVSGYPVLQHWKVRSVMYHIKLNQVAISQALSNALHSLDGATSRADFVALLDQFGNHYIQEAIYGFEESCSIWYPNKQVQRRLWLEYEDISKGNSPSDESEERERDPKVLTFPEYITSLSDSGTKHMAAGVRMECHSKGRCPSSCPLCHVTSSPDTPAEPVLLEVTKAAPIYELVTNNQTQRLLQEATMSSLWCSGTGDVIEDWCRCDSTAFGADGLPTCAPLPQPVLRLSTVHEPSSTLVVLEWEHSEPPIGVQIVDYLLRQEKVTDRMDHSKVETETVLSFVDDIISGAKSPCAMPSQVPDKQLTTISLIIRCLEPDTIYMFTLWGVDNTGRRSRPSDVIVKTPCPVVDDVKAQEIADKIYNLFNGYTSGKEQQTAYNTLLDLGSPTLHRVLYHYNQHYESFGEFTWRCEDELGPRKAGLILSQLGDLSSWCNGLLQEPKISLRRSSLKYLGCRYSEIKPYGLDWAELSRDLRKTCEEQTLSIPYNDYGDSKEI
Protein: S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) (5'-methylthioadenosine phosphorylase) (MTA phosphorylase) (MTAP) (MTAPase) (A0A8I5ZXI1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03155}.
Interaction partners:
Sequence:
WEPTGPCTAHSRAVPAPQSPLGPALRPAVDFPGADMASGSACTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLASMYVLDRMCEFLLLPFCVQLNSLHEIPPGSSCHTSYLFAFVARWERRVRWLARVLCERAFVPSSASTSVQWKETKHSKEITQRSKASRFSTTVQQQAIREECQTSLRPQTFYDGSHCSARGVCHIPMAEPFCPKTREVLIEMAKKLGLRCHSKGTIVTIEGPRFSSRAESFIFRTWGADVINMTTVPEVVLAKEAGLCYASIAMATDYDCWKEHEEAVSVDGVLKTMKENANKAKSLLLTTIPQIGSMEWSETLRNLKVSVLMSKISIYQTLN
Protein: ATP-dependent Clp protease adapter protein ClpS (P0A8Q6)
Organism: Escherichia coli (strain K12)
Function: Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
Interaction partners:
- ATP-dependent Clp protease ATP-binding subunit ClpA
- ATP-dependent Clp protease proteolytic subunit
- DNA protection during starvation protein
- Leucyl/phenylalanyl-tRNA--protein transferase
- ATP-dependent Clp protease ATP-binding subunit ClpX
- Putrescine aminotransferase
- Stringent starvation protein B
- Chaperone protein ClpB
Sequence:
MGKTNDWLDFDQLAEEKVRDALKPPSMYKVILVNDDYTPMEFVIDVLQKFFSYDVERATQLMLAVHYQGKAICGVFTAEVAETKVAMVNKYARENEHPLLCTLEKA
Protein: Ethylene-responsive transcription factor ERF038 (Q9ZQP3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MERDDCRRFQDSPAQTTERRVKYKPKKKRAKDDDDEKVVSKHPNFRGVRMRQWGKWVSEIREPKKKSRIWLGTFSTAEMAARAHDVAALAIKGGSAHLNFPELAYHLPRPASADPKDIQAAAAAAAAAVAIDMDVETSSPSPSPTVTETSSPAMIALSDDAFSDLPDLLLNVNHNIDGFWDSFPYEEPFLSQSY
Protein: Transmembrane protein (Q38DW4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRTAFHSITSRLTLFYTNAALHVPVVASSQRWQATCAREEGDFETSGENKTFGGKQQQQKEEQQWNSNALGKTQEVPKRRNITVLCNTTKAVYIHPTNHIASWYWFITDFHKWFVGFVFLFVGTQVIARYRVAKLQTVIQAQLGENLLDQRTRDLLTDIEVLRQKDPIRLEQEANIYHEQFWKRRALAVAESRNEVRRVELQRGILQGQARGTDMTEWLGAKAKDDEERKVAQRTQDYIQGFHQHLKSKRLI
Protein: Penicillin-binding protein H (EC 3.4.16.4) (Q796K8)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the polymerization of peptidoglycan. Plays a redundant role with PBP-2A (pbpA) in determining the rod shape of the cell during vegetative growth and spore outgrowth.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Peptidoglycan glycosyltransferase RodA
- Cell shape-determining protein MreC
- Cell shape-determining protein MreB
- Rod shape-determining protein MreD
- Cell shape-determining protein Mbl
- Penicillin-binding protein 1A/1B
- Cell shape-determining protein MreBH
- UDP-N-acetylmuramate--L-alanine ligase
- Septation ring formation regulator EzrA
- Probable peptidoglycan glycosyltransferase FtsW
Sequence:
MTEIGREPKKKSKGNRAIRMNLFFLAVFVLFTALIFKLGVVQIVEGEQHEEDAEKSNAKTAYYPAPRGKMYDRNQKVAVDNQSVPEIVYVSTSSTKTEDKIKTAKRLASFIHIDTEFLKERDLRDYWIAAHPKKAAALLKESESNLKGDQAYKLQIERVPDQELKAIQQDDEEMETAAIYTRFSSGNAYEPQIVKAMNPNKSNSNGKNGALLDEKKNSSQRPKNDLTYDEISIVSEHLEELPGIDIVNDWTRKYPYDKTLYSVFGGVTTPDQGLLSDRKDFYLTRGYANNDRVGKSYLEYQYEEYLNSHKEKVEYVEDNKGNVVSQKTIDKGSRGYDLQLSFDMELQAKVEKIIEEEVRNSRARGNYMLDRAFAVMMDPNNGDILSMAGKKIDLKTNKIEDYAIGAFTTQYEMGSAVKGATVLAGYQDGIPHYKYYIDAPMLLGTNLIKKSYTNMGTINELTALQKSSNVYMFNVAMHIAGVTYKPHGSLPADQNDLLKMRNYYSQFGLGVKTGIDLPQESAGMQTTPKTVGGLILDLAIGQYDTYTPLQMAQYISVIANGGYRVQPRIVTSIHKPGKKDQLGKAIEHRKPKVLNKINNSESDLKQVQTGMKLVTSSGTAKNTFTEDVSGKTGTAETFYYGTNRNWWGKKTYNLTFVGYYPSKKPKVAFSVVVPSVDDDDKINKIIAKRAIHAYAELEKKHSKK
Protein: Fructose-1,6-bisphosphatase 1 (FBPase 1) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) (Liver FBPase) (P19112)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain.
Interaction partners:
- Fructose-bisphosphate aldolase B
- Glucose-6-phosphate isomerase
- Transaldolase
- ATP-dependent 6-phosphofructokinase, platelet type
- ATP-dependent 6-phosphofructokinase, liver type
- ATP-dependent 6-phosphofructokinase, muscle type
- transketolase
- transketolase
- Transketolase
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
Sequence:
MVDHAPFETDISTLTRFVLEEGRKAGGTGEMTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSANEPSEKDALQPGRNLVAAGYALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGSTEDVQEFLEIYNKDKAKSRPSLPLPQSRARESPVHSICDELF
Protein: Homeobox protein notochord (Xnot) (Q06615)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional repressor. Plays a fundamental role in notochord formation, acting within the mesodermal region.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MLHSPVFPAFGHHLAQHPAMPLAMELPRTPKASFNIDSILSRTDRPASKLSMEMPSWQPPSPPSMPYRYSYGMMPYPPVWLIKPTVGYPNMAQQQPMRMPRGECLCPDPTCKERVLPFSHCPNGAMNPLSWRTGPCKMKRIRTVFTPEQLEKLEKEFLKQQYMVGTERVDLASTLNLTETQVKVWFQNRRIKWRKQSLEQKKAKLSQFGVIPADSSDHTDDSRETEEDEDDLDVEL
Protein: Large ribosomal subunit protein uL2 (50S ribosomal protein L2) (P60422)
Organism: Escherichia coli (strain K12)
Function: One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.
Interaction partners:
- Protein translocase subunit SecY
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein bL12
Sequence:
MAVVKCKPTSPGRRHVVKVVNPELHKGKPFAPLLEKNSKSGGRNNNGRITTRHIGGGHKQAYRIVDFKRNKDGIPAVVERLEYDPNRSANIALVLYKDGERRYILAPKGLKAGDQIQSGVDAAIKPGNTLPMRNIPVGSTVHNVEMKPGKGGQLARSAGTYVQIVARDGAYVTLRLRSGEMRKVEADCRATLGEVGNAEHMLRVLGKAGAARWRGVRPTVRGTAMNPVDHPHGGGEGRNFGKHPVTPWGVQTKGKKTRSNKRTDKFIVRRRSK
Protein: ADP-ribosylation factor (Q6FNU1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555, ECO:0000256|RuleBase:RU369003}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome H complete sequence
- Coatomer subunit gamma
- AP-1 complex subunit gamma
- ADP-ribosylation factor
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MGLFASKLFSNLFGSKEMRILMVGLDGAGKTTVLYKLKLGEVITTIPTIGFNVETVQYKNISFTVWDVGGQDRIRSLWRHYYRNTEGVIFVVDSNDRSRIGEAREVMQRMLNEDELRNAVWLVFANKQDLPEAMSAAEITEKLGLHSIRNRPWFIQATCATSGEGLYEGLEWLSNNLSNQS